data_8WEC
# 
_entry.id   8WEC 
# 
_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   8WEC         pdb_00008wec 10.2210/pdb8wec/pdb 
WWPDB D_1300040306 ?            ?                   
# 
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                        8WEC 
_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 'SERINE-RICH ENDOGENOUS PEPTIDE (SCOOP)' 1318.399  2 ?                 ?                 ? ? 
4  branched    syn '2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose' 424.401   9 ? ? ? ? 
5  branched    syn 
;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 ?                 ?                 ? ? 
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   2 
?                 ?                 ? ? 
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    syn 'alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose' 342.297   1 ?                 ?                 ? ? 
9  branched    syn '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   8 ?                 ?                 ? ? 
11 non-polymer syn beta-D-mannopyranose 180.156   1 ?                 ?                 ? ? 
# 
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 PVRSSQSSQAGGR PVRSSQSSQAGGR C,F ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
10 2-acetamido-2-deoxy-beta-D-glucopyranose NAG 
11 beta-D-mannopyranose                     BMA 
# 
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   PRO n 
3 2   VAL n 
3 3   ARG n 
3 4   SER n 
3 5   SER n 
3 6   GLN n 
3 7   SER n 
3 8   SER n 
3 9   GLN 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    'Arabidopsis thaliana' 
_pdbx_entity_src_syn.organism_common_name   'Mouse-ear cress' 
_pdbx_entity_src_syn.ncbi_taxonomy_id       3702 
_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 DGlcpNAcb1-4DGlcpNAcb1-ROH                                                            'Glycam Condensed Sequence' GMML       
1.0   
2  4 'WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1'                                 WURCS                       PDB2Glycan 
1.1.0 
3  4 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-4-deoxy-GlcpNAc]{}}'                               LINUCS                      PDB-CARE   
?     
4  5 'LFucpa1-3[DGlcpNAcb1-4][LFucpa1-6]DGlcpNAcb1-ROH'                                    'Glycam Condensed Sequence' GMML       
1.0   
5  5 '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 
6  5 '[][D-1-deoxy-GlcpNAc]{[(3+1)][a-L-Fucp]{}[(4+1)][b-D-GlcpNAc]{}[(6+1)][a-L-Fucp]{}}' 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 DManpa1-3DManpb1-ROH                                                                  'Glycam Condensed Sequence' GMML       
1.0   
14 8 'WURCS=2.0/2,2,1/[a1122h-1b_1-5][a1122h-1a_1-5]/1-2/a3-b1'                            WURCS                       PDB2Glycan 
1.1.0 
15 8 '[][b-D-Manp]{[(3+1)][a-D-Manp]{}}'                                                   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 NAG C1 O1 1 NAG O4 HO4 sing ? 
2  5 2 FUC C1 O1 1 NAG O3 HO3 sing ? 
3  5 3 NAG C1 O1 1 NAG O4 HO4 sing ? 
4  5 4 FUC C1 O1 1 NAG O6 HO6 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 MAN C1 O1 1 BMA O3 HO3 sing ? 
10 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 
MAN 'D-saccharide, alpha linking' . alpha-D-mannopyranose                    'alpha-D-mannose; D-mannose; mannose' 'C6 H12 O6' 
180.156 
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                            
MAN 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DManpa                         
MAN 'COMMON NAME'                         GMML     1.0 a-D-mannopyranose              
MAN 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 a-D-Manp                       
MAN 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Man                            
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   PRO 1   1   1   PRO PRO C . n 
C 3 2   VAL 2   2   2   VAL VAL C . n 
C 3 3   ARG 3   3   3   ARG ARG 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   GLN 6   6   6   GLN GLN C . n 
C 3 7   SER 7   7   7   SER SER C . n 
C 3 8   SER 8   8   8   SER SER C . n 
C 3 9   GLN 9   9   9   GLN GLN 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   PRO 1   1   1   PRO PRO F . n 
F 3 2   VAL 2   2   2   VAL VAL F . n 
F 3 3   ARG 3   3   3   ARG ARG 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   GLN 6   6   6   GLN GLN F . n 
F 3 7   SER 7   7   7   SER SER F . n 
F 3 8   SER 8   8   8   SER SER F . n 
F 3 9   GLN 9   9   9   GLN GLN 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 A NAG 1001 n 
G 4 NAG 2 G NAG 2 A NAG 1002 n 
H 5 NAG 1 H NAG 1 A NAG 1101 n 
H 5 FUC 2 H FUC 2 A FUC 1103 n 
H 5 NAG 3 H NAG 3 A NAG 1102 n 
H 5 FUC 4 H FUC 4 A FUC 1100 n 
I 4 NAG 1 I NAG 1 A NAG 1201 n 
I 4 NAG 2 I NAG 2 A NAG 1202 n 
J 4 NAG 1 J NAG 1 A NAG 1301 n 
J 4 NAG 2 J NAG 2 A NAG 1302 n 
K 4 NAG 1 K NAG 1 A NAG 1401 n 
K 4 NAG 2 K NAG 2 A NAG 1402 n 
L 4 NAG 1 L NAG 1 A NAG 1501 n 
L 4 NAG 2 L NAG 2 A NAG 1502 n 
M 6 NAG 1 M NAG 1 A NAG 1901 n 
M 6 NAG 2 M NAG 2 A NAG 1902 n 
M 6 FUC 3 M FUC 3 A FUC 1900 n 
N 7 NAG 1 N NAG 1 D NAG 1001 n 
N 7 NAG 2 N NAG 2 D NAG 1002 n 
N 7 BMA 3 N BMA 3 D BMA 1003 n 
O 6 NAG 1 O NAG 1 D NAG 1101 n 
O 6 NAG 2 O NAG 2 D NAG 1102 n 
O 6 FUC 3 O FUC 3 D FUC 1100 n 
P 8 BMA 1 P BMA 1 D BMA 1103 n 
P 8 MAN 2 P MAN 2 D MAN 1104 n 
Q 4 NAG 1 Q NAG 1 D NAG 1201 n 
Q 4 NAG 2 Q NAG 2 D NAG 1202 n 
R 4 NAG 1 R NAG 1 D NAG 1301 n 
R 4 NAG 2 R NAG 2 D NAG 1302 n 
S 4 NAG 1 S NAG 1 D NAG 1701 n 
S 4 NAG 2 S NAG 2 D NAG 1702 n 
T 7 NAG 1 T NAG 1 D NAG 1801 n 
T 7 NAG 2 T NAG 2 D NAG 1802 n 
T 7 BMA 3 T BMA 3 D BMA 1803 n 
U 9 NAG 1 U NAG 1 D NAG 1901 n 
U 9 FUC 2 U FUC 2 D FUC 1902 n 
V 9 NAG 1 V NAG 1 D NAG 2201 n 
V 9 FUC 2 V FUC 2 D FUC 2202 n 
W 4 NAG 1 W NAG 1 D NAG 2301 n 
W 4 NAG 2 W NAG 2 D NAG 2302 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 FUC ? ? FUC ? ? 'SUBJECT OF INVESTIGATION' ? 
3 MAN ? ? MAN ? ? 'SUBJECT OF INVESTIGATION' ? 
4 NAG ? ? NAG ? ? '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 
X  10 NAG 1 1601 1601 NAG NAG A . 
Y  10 NAG 1 1602 1701 NAG NAG A . 
Z  10 NAG 1 1603 1801 NAG NAG A . 
AA 11 BMA 1 301  1003 BMA BMA B . 
BA 10 NAG 1 1401 1401 NAG NAG D . 
CA 10 NAG 1 1402 1501 NAG NAG D . 
DA 10 NAG 1 1403 1601 NAG NAG D . 
EA 10 NAG 1 1404 2001 NAG NAG D . 
FA 10 NAG 1 1405 2101 NAG NAG D . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 N 1 G NAG 2 ? O4 ? G NAG 2 O4 
2 1 N 1 O NAG 2 ? O4 ? O NAG 2 O4 
# 
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' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? '(1.20.1_4487: ???)' 4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.79 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8WEC 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     73.004 
_cell.length_a_esd                 ? 
_cell.length_b                     178.690 
_cell.length_b_esd                 ? 
_cell.length_c                     144.161 
_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                         8WEC 
_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                   8WEC 
_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             4.93 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          75.07 
_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         2022-09-09 
_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                        'NFPSS 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       NFPSS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8WEC 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              3.1 
_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                                     66926 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.99 
_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                                    3.1 
_reflns_shell.d_res_low                                     3.17 
_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                             6711 
_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                                  0.68 
_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                                 8WEC 
_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                            3.10 
_refine.ls_d_res_low                             46.15 
_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                     66822 
_refine.ls_number_reflns_R_free                  3307 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.79 
_refine.ls_percent_reflns_R_free                 4.95 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2455 
_refine.ls_R_factor_R_free                       0.2558 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2450 
_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                          1.48 
_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                 28.43 
_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                            0.49 
_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                       3.10 
_refine_hist.d_res_low                        46.15 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               13386 
_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        13386 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_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' ? 0.005  ? ?    ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.794  ? ?    ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 18.056 ? 5152 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.055  ? 2311 ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.009  ? 2355 ? 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' 3.10 3.17  . . 244 4262 100.00 . . . . 0.3794 . . . . . . . . . . . 0.3842 
'X-RAY DIFFRACTION' 3.17 3.25  . . 238 4165 100.00 . . . . 0.3569 . . . . . . . . . . . 0.3593 
'X-RAY DIFFRACTION' 3.25 3.34  . . 221 4249 100.00 . . . . 0.3356 . . . . . . . . . . . 0.3577 
'X-RAY DIFFRACTION' 3.34 3.44  . . 202 4238 100.00 . . . . 0.3327 . . . . . . . . . . . 0.3235 
'X-RAY DIFFRACTION' 3.44 3.55  . . 206 4207 100.00 . . . . 0.3036 . . . . . . . . . . . 0.3064 
'X-RAY DIFFRACTION' 3.55 3.68  . . 216 4246 100.00 . . . . 0.2926 . . . . . . . . . . . 0.2942 
'X-RAY DIFFRACTION' 3.68 3.82  . . 217 4230 100.00 . . . . 0.2649 . . . . . . . . . . . 0.2815 
'X-RAY DIFFRACTION' 3.82 4.00  . . 197 4250 100.00 . . . . 0.2410 . . . . . . . . . . . 0.2487 
'X-RAY DIFFRACTION' 4.00 4.21  . . 195 4247 100.00 . . . . 0.2287 . . . . . . . . . . . 0.2251 
'X-RAY DIFFRACTION' 4.21 4.47  . . 216 4258 100.00 . . . . 0.2076 . . . . . . . . . . . 0.2093 
'X-RAY DIFFRACTION' 4.47 4.81  . . 234 4231 100.00 . . . . 0.2039 . . . . . . . . . . . 0.2003 
'X-RAY DIFFRACTION' 4.81 5.30  . . 221 4232 100.00 . . . . 0.2010 . . . . . . . . . . . 0.2024 
'X-RAY DIFFRACTION' 5.30 6.06  . . 247 4253 100.00 . . . . 0.2388 . . . . . . . . . . . 0.2573 
'X-RAY DIFFRACTION' 6.06 7.63  . . 203 4251 100.00 . . . . 0.2144 . . . . . . . . . . . 0.2242 
'X-RAY DIFFRACTION' 7.64 46.15 . . 250 4196 98.00  . . . . 0.2216 . . . . . . . . . . . 0.2625 
# 
_struct.entry_id                     8WEC 
_struct.title                        
'Crystal structure of Arabidopsis thaliana MIK2 ectodomain in complex with BAK1 ectodomain and SCOOP12' 
_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        8WEC 
_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 4  ? 
J  N N 4  ? 
K  N N 4  ? 
L  N N 4  ? 
M  N N 6  ? 
N  N N 7  ? 
O  N N 6  ? 
P  N N 8  ? 
Q  N N 4  ? 
R  N N 4  ? 
S  N N 4  ? 
T  N N 7  ? 
U  N N 9  ? 
V  N N 9  ? 
W  N N 4  ? 
X  N N 10 ? 
Y  N N 10 ? 
Z  N N 10 ? 
AA N N 11 ? 
BA N N 10 ? 
CA N N 10 ? 
DA N N 10 ? 
EA N N 10 ? 
FA 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 8WEC       8WEC   ? 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 8WEC A 1 ? 683 ? Q8VZG8 1 ? 683 ? 1 683 
2 2 8WEC B 1 ? 220 ? Q94F62 1 ? 220 ? 1 220 
3 3 8WEC C 1 ? 13  ? 8WEC   1 ? 13  ? 1 13  
4 1 8WEC D 1 ? 683 ? Q8VZG8 1 ? 683 ? 1 683 
5 2 8WEC E 1 ? 220 ? Q94F62 1 ? 220 ? 1 220 
6 3 8WEC F 1 ? 13  ? 8WEC   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 8WEC GLU A 137 ? UNP Q8VZG8 LEU 137 'engineered mutation' 137 1  
1 8WEC LYS A 164 ? UNP Q8VZG8 ASP 164 'engineered mutation' 164 2  
1 8WEC PHE A 564 ? UNP Q8VZG8 SER 564 'engineered mutation' 564 3  
2 8WEC HIS B 221 ? UNP Q94F62 ?   ?   'expression tag'      221 4  
2 8WEC HIS B 222 ? UNP Q94F62 ?   ?   'expression tag'      222 5  
2 8WEC HIS B 223 ? UNP Q94F62 ?   ?   'expression tag'      223 6  
2 8WEC HIS B 224 ? UNP Q94F62 ?   ?   'expression tag'      224 7  
2 8WEC HIS B 225 ? UNP Q94F62 ?   ?   'expression tag'      225 8  
2 8WEC HIS B 226 ? UNP Q94F62 ?   ?   'expression tag'      226 9  
2 8WEC HIS B 227 ? UNP Q94F62 ?   ?   'expression tag'      227 10 
2 8WEC HIS B 228 ? UNP Q94F62 ?   ?   'expression tag'      228 11 
2 8WEC HIS B 229 ? UNP Q94F62 ?   ?   'expression tag'      229 12 
2 8WEC HIS B 230 ? UNP Q94F62 ?   ?   'expression tag'      230 13 
4 8WEC GLU D 137 ? UNP Q8VZG8 LEU 137 'engineered mutation' 137 14 
4 8WEC LYS D 164 ? UNP Q8VZG8 ASP 164 'engineered mutation' 164 15 
4 8WEC PHE D 564 ? UNP Q8VZG8 SER 564 'engineered mutation' 564 16 
5 8WEC HIS E 221 ? UNP Q94F62 ?   ?   'expression tag'      221 17 
5 8WEC HIS E 222 ? UNP Q94F62 ?   ?   'expression tag'      222 18 
5 8WEC HIS E 223 ? UNP Q94F62 ?   ?   'expression tag'      223 19 
5 8WEC HIS E 224 ? UNP Q94F62 ?   ?   'expression tag'      224 20 
5 8WEC HIS E 225 ? UNP Q94F62 ?   ?   'expression tag'      225 21 
5 8WEC HIS E 226 ? UNP Q94F62 ?   ?   'expression tag'      226 22 
5 8WEC HIS E 227 ? UNP Q94F62 ?   ?   'expression tag'      227 23 
5 8WEC HIS E 228 ? UNP Q94F62 ?   ?   'expression tag'      228 24 
5 8WEC HIS E 229 ? UNP Q94F62 ?   ?   'expression tag'      229 25 
5 8WEC 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,P,X,Y,Z,AA         
2 1 D,E,F,N,O,Q,R,S,T,U,V,W,BA,CA,DA,EA,FA 
# 
_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  ? SER A 59  ? THR A 47  SER A 59  1 ? 13 
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  ? CYS A 82  ? ASN A 77  CYS A 82  1 ? 6  
HELX_P HELX_P4  AA4 PRO A 113 ? LEU A 117 ? PRO A 113 LEU A 117 5 ? 5  
HELX_P HELX_P5  AA5 SER A 135 ? PHE A 141 ? SER A 135 PHE A 141 5 ? 7  
HELX_P HELX_P6  AA6 PRO A 159 ? LEU A 165 ? PRO A 159 LEU A 165 5 ? 7  
HELX_P HELX_P7  AA7 PRO A 183 ? LEU A 189 ? PRO A 183 LEU A 189 5 ? 7  
HELX_P HELX_P8  AA8 PRO A 207 ? LEU A 213 ? PRO A 207 LEU A 213 5 ? 7  
HELX_P HELX_P9  AA9 PRO A 231 ? LEU A 237 ? PRO A 231 LEU A 237 5 ? 7  
HELX_P HELX_P10 AB1 PRO A 255 ? LEU A 261 ? PRO A 255 LEU A 261 5 ? 7  
HELX_P HELX_P11 AB2 PRO A 279 ? MET A 285 ? PRO A 279 MET A 285 5 ? 7  
HELX_P HELX_P12 AB3 PRO A 303 ? ILE A 309 ? PRO A 303 ILE A 309 5 ? 7  
HELX_P HELX_P13 AB4 PRO A 327 ? MET A 333 ? PRO A 327 MET A 333 5 ? 7  
HELX_P HELX_P14 AB5 PRO A 351 ? LEU A 357 ? PRO A 351 LEU A 357 5 ? 7  
HELX_P HELX_P15 AB6 GLY A 377 ? SER A 381 ? GLY A 377 SER A 381 5 ? 5  
HELX_P HELX_P16 AB7 PRO A 423 ? ASP A 428 ? PRO A 423 ASP A 428 1 ? 6  
HELX_P HELX_P17 AB8 ILE A 446 ? PHE A 450 ? ILE A 446 PHE A 450 1 ? 5  
HELX_P HELX_P18 AB9 SER A 471 ? SER A 477 ? SER A 471 SER A 477 5 ? 7  
HELX_P HELX_P19 AC1 PRO A 495 ? MET A 501 ? PRO A 495 MET A 501 5 ? 7  
HELX_P HELX_P20 AC2 PRO A 519 ? ASN A 526 ? PRO A 519 ASN A 526 5 ? 8  
HELX_P HELX_P21 AC3 PRO A 543 ? LEU A 549 ? PRO A 543 LEU A 549 5 ? 7  
HELX_P HELX_P22 AC4 PRO A 591 ? LEU A 597 ? PRO A 591 LEU A 597 5 ? 7  
HELX_P HELX_P23 AC5 SER A 615 ? LEU A 621 ? SER A 615 LEU A 621 5 ? 7  
HELX_P HELX_P24 AC6 PRO A 639 ? MET A 645 ? PRO A 639 MET A 645 5 ? 7  
HELX_P HELX_P25 AC7 ASN A 665 ? ASN A 670 ? ASN A 665 ASN A 670 1 ? 6  
HELX_P HELX_P26 AC8 PRO A 672 ? GLU A 677 ? PRO A 672 GLU A 677 5 ? 6  
HELX_P HELX_P27 AC9 ALA B 27  ? SER B 38  ? ALA B 27  SER B 38  1 ? 12 
HELX_P HELX_P28 AD1 LYS B 44  ? TRP B 49  ? LYS B 44  TRP B 49  5 ? 6  
HELX_P HELX_P29 AD2 THR B 55  ? TRP B 59  ? THR B 55  TRP B 59  5 ? 5  
HELX_P HELX_P30 AD3 VAL B 85  ? LEU B 91  ? VAL B 85  LEU B 91  5 ? 7  
HELX_P HELX_P31 AD4 PRO B 109 ? LEU B 115 ? PRO B 109 LEU B 115 5 ? 7  
HELX_P HELX_P32 AD5 PRO B 133 ? LEU B 139 ? PRO B 133 LEU B 139 5 ? 7  
HELX_P HELX_P33 AD6 PRO B 157 ? VAL B 163 ? PRO B 157 VAL B 163 5 ? 7  
HELX_P HELX_P34 AD7 SER B 185 ? PHE B 189 ? SER B 185 PHE B 189 5 ? 5  
HELX_P HELX_P35 AD8 THR B 190 ? ALA B 195 ? THR B 190 ALA B 195 5 ? 6  
HELX_P HELX_P36 AD9 VAL D 48  ? SER D 59  ? VAL D 48  SER D 59  1 ? 12 
HELX_P HELX_P37 AE1 SER D 68  ? TRP D 73  ? SER D 68  TRP D 73  5 ? 6  
HELX_P HELX_P38 AE2 SER D 80  ? TRP D 85  ? SER D 80  TRP D 85  1 ? 6  
HELX_P HELX_P39 AE3 SER D 135 ? PHE D 141 ? SER D 135 PHE D 141 5 ? 7  
HELX_P HELX_P40 AE4 PRO D 159 ? LEU D 165 ? PRO D 159 LEU D 165 5 ? 7  
HELX_P HELX_P41 AE5 PRO D 183 ? LEU D 189 ? PRO D 183 LEU D 189 5 ? 7  
HELX_P HELX_P42 AE6 PRO D 207 ? LEU D 213 ? PRO D 207 LEU D 213 5 ? 7  
HELX_P HELX_P43 AE7 PRO D 231 ? LEU D 237 ? PRO D 231 LEU D 237 5 ? 7  
HELX_P HELX_P44 AE8 PRO D 255 ? LEU D 261 ? PRO D 255 LEU D 261 5 ? 7  
HELX_P HELX_P45 AE9 PRO D 279 ? MET D 285 ? PRO D 279 MET D 285 5 ? 7  
HELX_P HELX_P46 AF1 PRO D 303 ? ILE D 309 ? PRO D 303 ILE D 309 5 ? 7  
HELX_P HELX_P47 AF2 PRO D 327 ? MET D 333 ? PRO D 327 MET D 333 5 ? 7  
HELX_P HELX_P48 AF3 PRO D 351 ? LEU D 357 ? PRO D 351 LEU D 357 5 ? 7  
HELX_P HELX_P49 AF4 GLY D 377 ? SER D 381 ? GLY D 377 SER D 381 5 ? 5  
HELX_P HELX_P50 AF5 PRO D 423 ? ASP D 428 ? PRO D 423 ASP D 428 1 ? 6  
HELX_P HELX_P51 AF6 ILE D 446 ? PHE D 450 ? ILE D 446 PHE D 450 1 ? 5  
HELX_P HELX_P52 AF7 SER D 471 ? SER D 477 ? SER D 471 SER D 477 5 ? 7  
HELX_P HELX_P53 AF8 PRO D 495 ? MET D 501 ? PRO D 495 MET D 501 5 ? 7  
HELX_P HELX_P54 AF9 PRO D 519 ? ILE D 525 ? PRO D 519 ILE D 525 5 ? 7  
HELX_P HELX_P55 AG1 PRO D 543 ? LEU D 549 ? PRO D 543 LEU D 549 5 ? 7  
HELX_P HELX_P56 AG2 PRO D 591 ? LEU D 597 ? PRO D 591 LEU D 597 5 ? 7  
HELX_P HELX_P57 AG3 SER D 615 ? LEU D 621 ? SER D 615 LEU D 621 5 ? 7  
HELX_P HELX_P58 AG4 PRO D 639 ? MET D 645 ? PRO D 639 MET D 645 5 ? 7  
HELX_P HELX_P59 AG5 ASN D 665 ? ASN D 670 ? ASN D 665 ASN D 670 1 ? 6  
HELX_P HELX_P60 AG6 PRO D 672 ? GLU D 677 ? PRO D 672 GLU D 677 5 ? 6  
HELX_P HELX_P61 AG7 ALA E 27  ? SER E 38  ? ALA E 27  SER E 38  1 ? 12 
HELX_P HELX_P62 AG8 LYS E 44  ? TRP E 49  ? LYS E 44  TRP E 49  5 ? 6  
HELX_P HELX_P63 AG9 THR E 55  ? TRP E 59  ? THR E 55  TRP E 59  5 ? 5  
HELX_P HELX_P64 AH1 VAL E 85  ? LEU E 91  ? VAL E 85  LEU E 91  5 ? 7  
HELX_P HELX_P65 AH2 PRO E 109 ? LEU E 115 ? PRO E 109 LEU E 115 5 ? 7  
HELX_P HELX_P66 AH3 PRO E 133 ? LEU E 139 ? PRO E 133 LEU E 139 5 ? 7  
HELX_P HELX_P67 AH4 PRO E 157 ? ALA E 162 ? PRO E 157 ALA E 162 5 ? 6  
HELX_P HELX_P68 AH5 SER E 185 ? PHE E 189 ? SER E 185 PHE E 189 5 ? 5  
HELX_P HELX_P69 AH6 THR E 190 ? ALA E 195 ? THR E 190 ALA E 195 5 ? 6  
# 
_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 ? ? ? ? ? ? ? 2.038 ? ? 
disulf2  disulf ?    ? A CYS 403 SG  ? ? ? 1_555 A  CYS 429 SG ? ? A CYS 403 A CYS 429  1_555 ? ? ? ? ? ? ? 2.042 ? ? 
disulf3  disulf ?    ? B CYS 57  SG  ? ? ? 1_555 B  CYS 64  SG ? ? B CYS 57  B CYS 64   1_555 ? ? ? ? ? ? ? 2.047 ? ? 
disulf4  disulf ?    ? D CYS 82  SG  ? ? ? 1_555 D  CYS 90  SG ? ? D CYS 82  D CYS 90   1_555 ? ? ? ? ? ? ? 2.041 ? ? 
disulf5  disulf ?    ? D CYS 403 SG  ? ? ? 1_555 D  CYS 429 SG ? ? D CYS 403 D CYS 429  1_555 ? ? ? ? ? ? ? 2.043 ? ? 
disulf6  disulf ?    ? E CYS 57  SG  ? ? ? 1_555 E  CYS 64  SG ? ? E CYS 57  E CYS 64   1_555 ? ? ? ? ? ? ? 2.053 ? ? 
covale1  covale one  ? A ASN 99  ND2 ? ? ? 1_555 K  NAG .   C1 ? ? A ASN 99  K NAG 1    1_555 ? ? ? ? ? ? ? 1.438 ? 
N-Glycosylation 
covale2  covale one  ? A ASN 119 ND2 ? ? ? 1_555 J  NAG .   C1 ? ? A ASN 119 J NAG 1    1_555 ? ? ? ? ? ? ? 1.439 ? 
N-Glycosylation 
covale3  covale one  ? A ASN 179 ND2 ? ? ? 1_555 H  NAG .   C1 ? ? A ASN 179 H NAG 1    1_555 ? ? ? ? ? ? ? 1.445 ? 
N-Glycosylation 
covale4  covale one  ? A ASN 263 ND2 ? ? ? 1_555 Y  NAG .   C1 ? ? A ASN 263 A NAG 1602 1_555 ? ? ? ? ? ? ? 1.441 ? 
N-Glycosylation 
covale5  covale one  ? A ASN 284 ND2 ? ? ? 1_555 Z  NAG .   C1 ? ? A ASN 284 A NAG 1603 1_555 ? ? ? ? ? ? ? 1.460 ? 
N-Glycosylation 
covale6  covale one  ? A ASN 380 ND2 ? ? ? 1_555 L  NAG .   C1 ? ? A ASN 380 L NAG 1    1_555 ? ? ? ? ? ? ? 1.442 ? 
N-Glycosylation 
covale7  covale one  ? A ASN 410 ND2 ? ? ? 1_555 G  NAG .   C1 ? ? A ASN 410 G NAG 1    1_555 ? ? ? ? ? ? ? 1.446 ? 
N-Glycosylation 
covale8  covale one  ? A ASN 487 ND2 ? ? ? 1_555 X  NAG .   C1 ? ? A ASN 487 A NAG 1601 1_555 ? ? ? ? ? ? ? 1.454 ? 
N-Glycosylation 
covale9  covale one  ? A ASN 500 ND2 ? ? ? 1_555 M  NAG .   C1 ? ? A ASN 500 M NAG 1    1_555 ? ? ? ? ? ? ? 1.449 ? 
N-Glycosylation 
covale10 covale one  ? A ASN 580 ND2 ? ? ? 1_555 I  NAG .   C1 ? ? A ASN 580 I NAG 1    1_555 ? ? ? ? ? ? ? 1.439 ? 
N-Glycosylation 
covale11 covale one  ? D ASN 63  ND2 ? ? ? 1_555 DA NAG .   C1 ? ? D ASN 63  D NAG 1403 1_555 ? ? ? ? ? ? ? 1.454 ? 
N-Glycosylation 
covale12 covale one  ? D ASN 99  ND2 ? ? ? 1_555 R  NAG .   C1 ? ? D ASN 99  R NAG 1    1_555 ? ? ? ? ? ? ? 1.442 ? 
N-Glycosylation 
covale13 covale one  ? D ASN 119 ND2 ? ? ? 1_555 BA 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 ? ? ? ? ? ? ? 1.444 ? 
N-Glycosylation 
covale15 covale one  ? D ASN 249 ND2 ? ? ? 1_555 W  NAG .   C1 ? ? D ASN 249 W NAG 1    1_555 ? ? ? ? ? ? ? 1.446 ? 
N-Glycosylation 
covale16 covale one  ? D ASN 263 ND2 ? ? ? 1_555 CA NAG .   C1 ? ? D ASN 263 D NAG 1402 1_555 ? ? ? ? ? ? ? 1.442 ? 
N-Glycosylation 
covale17 covale one  ? D ASN 284 ND2 ? ? ? 1_555 U  NAG .   C1 ? ? D ASN 284 U NAG 1    1_555 ? ? ? ? ? ? ? 1.443 ? 
N-Glycosylation 
covale18 covale one  ? D ASN 323 ND2 ? ? ? 1_555 EA NAG .   C1 ? ? D ASN 323 D NAG 1404 1_555 ? ? ? ? ? ? ? 1.442 ? 
N-Glycosylation 
covale19 covale one  ? D ASN 380 ND2 ? ? ? 1_555 T  NAG .   C1 ? ? D ASN 380 T NAG 1    1_555 ? ? ? ? ? ? ? 1.444 ? 
N-Glycosylation 
covale20 covale one  ? D ASN 410 ND2 ? ? ? 1_555 N  NAG .   C1 ? ? D ASN 410 N NAG 1    1_555 ? ? ? ? ? ? ? 1.444 ? 
N-Glycosylation 
covale21 covale one  ? D ASN 487 ND2 ? ? ? 1_555 FA NAG .   C1 ? ? D ASN 487 D NAG 1405 1_555 ? ? ? ? ? ? ? 1.444 ? 
N-Glycosylation 
covale22 covale one  ? D ASN 500 ND2 ? ? ? 1_555 V  NAG .   C1 ? ? D ASN 500 V NAG 1    1_555 ? ? ? ? ? ? ? 1.447 ? 
N-Glycosylation 
covale23 covale one  ? D ASN 580 ND2 ? ? ? 1_555 Q  NAG .   C1 ? ? D ASN 580 Q NAG 1    1_555 ? ? ? ? ? ? ? 1.462 ? 
N-Glycosylation 
covale24 covale one  ? D ASN 633 ND2 ? ? ? 1_555 S  NAG .   C1 ? ? D ASN 633 S NAG 1    1_555 ? ? ? ? ? ? ? 1.454 ? 
N-Glycosylation 
covale25 covale both ? G NAG .   O4  ? ? ? 1_555 G  NAG .   C1 ? ? G NAG 1   G NAG 2    1_555 ? ? ? ? ? ? ? 1.433 ? ? 
covale26 covale both ? H NAG .   O3  ? ? ? 1_555 H  FUC .   C1 ? ? H NAG 1   H FUC 2    1_555 ? ? ? ? ? ? ? 1.435 ? ? 
covale27 covale both ? H NAG .   O4  ? ? ? 1_555 H  NAG .   C1 ? ? H NAG 1   H NAG 3    1_555 ? ? ? ? ? ? ? 1.455 ? ? 
covale28 covale both ? H NAG .   O6  ? ? ? 1_555 H  FUC .   C1 ? ? H NAG 1   H FUC 4    1_555 ? ? ? ? ? ? ? 1.445 ? ? 
covale29 covale both ? I NAG .   O4  ? ? ? 1_555 I  NAG .   C1 ? ? I NAG 1   I NAG 2    1_555 ? ? ? ? ? ? ? 1.440 ? ? 
covale30 covale both ? J NAG .   O4  ? ? ? 1_555 J  NAG .   C1 ? ? J NAG 1   J NAG 2    1_555 ? ? ? ? ? ? ? 1.445 ? ? 
covale31 covale both ? K NAG .   O4  ? ? ? 1_555 K  NAG .   C1 ? ? K NAG 1   K NAG 2    1_555 ? ? ? ? ? ? ? 1.445 ? ? 
covale32 covale both ? L NAG .   O4  ? ? ? 1_555 L  NAG .   C1 ? ? L NAG 1   L NAG 2    1_555 ? ? ? ? ? ? ? 1.459 ? ? 
covale33 covale both ? M NAG .   O4  ? ? ? 1_555 M  NAG .   C1 ? ? M NAG 1   M NAG 2    1_555 ? ? ? ? ? ? ? 1.454 ? ? 
covale34 covale both ? M NAG .   O6  ? ? ? 1_555 M  FUC .   C1 ? ? M NAG 1   M FUC 3    1_555 ? ? ? ? ? ? ? 1.451 ? ? 
covale35 covale both ? N NAG .   O4  ? ? ? 1_555 N  NAG .   C1 ? ? N NAG 1   N NAG 2    1_555 ? ? ? ? ? ? ? 1.438 ? ? 
covale36 covale both ? N NAG .   O4  ? ? ? 1_555 N  BMA .   C1 ? ? N NAG 2   N BMA 3    1_555 ? ? ? ? ? ? ? 1.432 ? ? 
covale37 covale both ? O NAG .   O4  ? ? ? 1_555 O  NAG .   C1 ? ? O NAG 1   O NAG 2    1_555 ? ? ? ? ? ? ? 1.449 ? ? 
covale38 covale both ? O NAG .   O6  ? ? ? 1_555 O  FUC .   C1 ? ? O NAG 1   O FUC 3    1_555 ? ? ? ? ? ? ? 1.452 ? ? 
covale39 covale both ? P BMA .   O3  ? ? ? 1_555 P  MAN .   C1 ? ? P BMA 1   P MAN 2    1_555 ? ? ? ? ? ? ? 1.454 ? ? 
covale40 covale both ? Q NAG .   O4  ? ? ? 1_555 Q  NAG .   C1 ? ? Q NAG 1   Q NAG 2    1_555 ? ? ? ? ? ? ? 1.446 ? ? 
covale41 covale both ? R NAG .   O4  ? ? ? 1_555 R  NAG .   C1 ? ? R NAG 1   R NAG 2    1_555 ? ? ? ? ? ? ? 1.440 ? ? 
covale42 covale both ? S NAG .   O4  ? ? ? 1_555 S  NAG .   C1 ? ? S NAG 1   S NAG 2    1_555 ? ? ? ? ? ? ? 1.449 ? ? 
covale43 covale both ? T NAG .   O4  ? ? ? 1_555 T  NAG .   C1 ? ? T NAG 1   T NAG 2    1_555 ? ? ? ? ? ? ? 1.438 ? ? 
covale44 covale both ? T NAG .   O4  ? ? ? 1_555 T  BMA .   C1 ? ? T NAG 2   T BMA 3    1_555 ? ? ? ? ? ? ? 1.430 ? ? 
covale45 covale both ? U NAG .   O6  ? ? ? 1_555 U  FUC .   C1 ? ? U NAG 1   U FUC 2    1_555 ? ? ? ? ? ? ? 1.444 ? ? 
covale46 covale both ? V NAG .   O6  ? ? ? 1_555 V  FUC .   C1 ? ? V NAG 1   V FUC 2    1_555 ? ? ? ? ? ? ? 1.448 ? ? 
covale47 covale both ? W NAG .   O4  ? ? ? 1_555 W  NAG .   C1 ? ? W NAG 1   W NAG 2    1_555 ? ? ? ? ? ? ? 1.447 ? ? 
# 
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 BA .   ? ASN D 119 ? NAG D 1401 ? 1_555 ASN D 119 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
2  NAG CA .   ? ASN D 263 ? NAG D 1402 ? 1_555 ASN D 263 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
3  NAG DA .   ? ASN D 63  ? NAG D 1403 ? 1_555 ASN D 63  ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
4  NAG EA .   ? ASN D 323 ? NAG D 1404 ? 1_555 ASN D 323 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
5  NAG FA .   ? ASN D 487 ? NAG D 1405 ? 1_555 ASN D 487 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
6  NAG G  .   ? ASN A 410 ? NAG G 1    ? 1_555 ASN A 410 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
7  NAG H  .   ? ASN A 179 ? NAG H 1    ? 1_555 ASN A 179 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
8  NAG I  .   ? ASN A 580 ? NAG I 1    ? 1_555 ASN A 580 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
9  NAG J  .   ? ASN A 119 ? NAG J 1    ? 1_555 ASN A 119 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
10 NAG K  .   ? ASN A 99  ? NAG K 1    ? 1_555 ASN A 99  ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
11 NAG L  .   ? ASN A 380 ? NAG L 1    ? 1_555 ASN A 380 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
12 NAG M  .   ? ASN A 500 ? NAG M 1    ? 1_555 ASN A 500 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
13 NAG N  .   ? ASN D 410 ? NAG N 1    ? 1_555 ASN D 410 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
14 NAG O  .   ? ASN D 179 ? NAG O 1    ? 1_555 ASN D 179 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
15 NAG Q  .   ? ASN D 580 ? NAG Q 1    ? 1_555 ASN D 580 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
16 NAG R  .   ? ASN D 99  ? NAG R 1    ? 1_555 ASN D 99  ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
17 NAG S  .   ? ASN D 633 ? NAG S 1    ? 1_555 ASN D 633 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
18 NAG T  .   ? ASN D 380 ? NAG T 1    ? 1_555 ASN D 380 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
19 NAG U  .   ? ASN D 284 ? NAG U 1    ? 1_555 ASN D 284 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
20 NAG V  .   ? ASN D 500 ? NAG V 1    ? 1_555 ASN D 500 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
21 NAG W  .   ? ASN D 249 ? NAG W 1    ? 1_555 ASN D 249 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
22 NAG X  .   ? ASN A 487 ? NAG A 1601 ? 1_555 ASN A 487 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
23 NAG Y  .   ? ASN A 263 ? NAG A 1602 ? 1_555 ASN A 263 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
24 NAG Z  .   ? ASN A 284 ? NAG A 1603 ? 1_555 ASN A 284 ? 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 ? 7  ? 
AA3 ? 2  ? 
AA4 ? 6  ? 
AA5 ? 2  ? 
AA6 ? 3  ? 
AA7 ? 3  ? 
AA8 ? 6  ? 
AA9 ? 2  ? 
AB1 ? 25 ? 
AB2 ? 3  ? 
AB3 ? 4  ? 
AB4 ? 2  ? 
AB5 ? 4  ? 
AB6 ? 3  ? 
AB7 ? 2  ? 
AB8 ? 5  ? 
AB9 ? 4  ? 
AC1 ? 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      
AA2 5  6  ? parallel      
AA2 6  7  ? 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      
AA5 1  2  ? parallel      
AA6 1  2  ? parallel      
AA6 2  3  ? parallel      
AA7 1  2  ? anti-parallel 
AA7 2  3  ? parallel      
AA8 1  2  ? anti-parallel 
AA8 2  3  ? parallel      
AA8 3  4  ? parallel      
AA8 4  5  ? parallel      
AA8 5  6  ? parallel      
AA9 1  2  ? parallel      
AB1 1  2  ? anti-parallel 
AB1 2  3  ? parallel      
AB1 3  4  ? parallel      
AB1 4  5  ? parallel      
AB1 5  6  ? parallel      
AB1 6  7  ? parallel      
AB1 7  8  ? parallel      
AB1 8  9  ? parallel      
AB1 9  10 ? parallel      
AB1 10 11 ? parallel      
AB1 11 12 ? parallel      
AB1 12 13 ? parallel      
AB1 13 14 ? parallel      
AB1 14 15 ? parallel      
AB1 15 16 ? parallel      
AB1 16 17 ? parallel      
AB1 17 18 ? parallel      
AB1 18 19 ? parallel      
AB1 19 20 ? parallel      
AB1 20 21 ? parallel      
AB1 21 22 ? parallel      
AB1 22 23 ? parallel      
AB1 23 24 ? parallel      
AB1 24 25 ? parallel      
AB2 1  2  ? parallel      
AB2 2  3  ? parallel      
AB3 1  2  ? parallel      
AB3 2  3  ? parallel      
AB3 3  4  ? parallel      
AB4 1  2  ? parallel      
AB5 1  2  ? parallel      
AB5 2  3  ? parallel      
AB5 3  4  ? parallel      
AB6 1  2  ? parallel      
AB6 2  3  ? parallel      
AB7 1  2  ? parallel      
AB8 1  2  ? parallel      
AB8 2  3  ? parallel      
AB8 3  4  ? parallel      
AB8 4  5  ? parallel      
AB9 1  2  ? anti-parallel 
AB9 2  3  ? parallel      
AB9 3  4  ? parallel      
AC1 1  2  ? anti-parallel 
AC1 2  3  ? parallel      
AC1 3  4  ? parallel      
AC1 4  5  ? parallel      
AC1 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 ? THR A 108 ? GLU A 106 THR A 108 
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 ? GLY A 204 ? LEU A 201 GLY A 204 
AA2 6  SER A 225 ? GLY A 228 ? SER A 225 GLY A 228 
AA2 7  ASN A 249 ? LEU A 250 ? ASN A 249 LEU A 250 
AA3 1  THR A 299 ? GLY A 300 ? THR A 299 GLY A 300 
AA3 2  GLN A 321 ? LEU A 322 ? GLN A 321 LEU A 322 
AA4 1  THR A 347 ? GLY A 348 ? THR A 347 GLY A 348 
AA4 2  GLN A 369 ? GLY A 372 ? GLN A 369 GLY A 372 
AA4 3  ASN A 393 ? GLY A 396 ? ASN A 393 GLY A 396 
AA4 4  HIS A 417 ? GLY A 420 ? HIS A 417 GLY A 420 
AA4 5  SER A 441 ? ASP A 445 ? SER A 441 ASP A 445 
AA4 6  ASN A 465 ? HIS A 467 ? ASN A 465 HIS A 467 
AA5 1  THR A 491 ? ALA A 493 ? THR A 491 ALA A 493 
AA5 2  ARG A 513 ? THR A 515 ? ARG A 513 THR A 515 
AA6 1  ASP A 611 ? GLU A 613 ? ASP A 611 GLU A 613 
AA6 2  ASN A 633 ? GLY A 636 ? ASN A 633 GLY A 636 
AA6 3  ASN A 657 ? LEU A 658 ? ASN A 657 LEU A 658 
AA7 1  LEU B 39  ? ALA B 40  ? LEU B 39  ALA B 40  
AA7 2  SER B 81  ? GLN B 83  ? SER B 81  GLN B 83  
AA7 3  ASN B 103 ? THR B 105 ? ASN B 103 THR B 105 
AA8 1  VAL B 62  ? CYS B 64  ? VAL B 62  CYS B 64  
AA8 2  VAL B 70  ? ASP B 74  ? VAL B 70  ASP B 74  
AA8 3  TYR B 96  ? GLU B 98  ? TYR B 96  GLU B 98  
AA8 4  SER B 120 ? ASP B 122 ? SER B 120 ASP B 122 
AA8 5  PHE B 144 ? ARG B 146 ? PHE B 144 ARG B 146 
AA8 6  VAL B 168 ? ASP B 170 ? VAL B 168 ASP B 170 
AA9 1  SER B 129 ? GLY B 130 ? SER B 129 GLY B 130 
AA9 2  SER B 151 ? LEU B 152 ? SER B 151 LEU B 152 
AB1 1  VAL D 88  ? SER D 91  ? VAL D 88  SER D 91  
AB1 2  SER D 94  ? ASN D 99  ? SER D 94  ASN D 99  
AB1 3  PHE D 122 ? ASP D 124 ? PHE D 122 ASP D 124 
AB1 4  TYR D 146 ? ASP D 148 ? TYR D 146 ASP D 148 
AB1 5  THR D 170 ? HIS D 172 ? THR D 170 HIS D 172 
AB1 6  GLU D 194 ? ALA D 196 ? GLU D 194 ALA D 196 
AB1 7  ASN D 218 ? TYR D 220 ? ASN D 218 TYR D 220 
AB1 8  GLU D 242 ? CYS D 244 ? GLU D 242 CYS D 244 
AB1 9  LEU D 266 ? ASN D 268 ? LEU D 266 ASN D 268 
AB1 10 THR D 290 ? SER D 292 ? THR D 290 SER D 292 
AB1 11 VAL D 314 ? HIS D 316 ? VAL D 314 HIS D 316 
AB1 12 ASP D 338 ? GLU D 340 ? ASP D 338 GLU D 340 
AB1 13 TRP D 362 ? PHE D 364 ? TRP D 362 PHE D 364 
AB1 14 VAL D 386 ? GLN D 388 ? VAL D 386 GLN D 388 
AB1 15 ASN D 410 ? THR D 412 ? ASN D 410 THR D 412 
AB1 16 ARG D 434 ? ARG D 436 ? ARG D 434 ARG D 436 
AB1 17 PHE D 458 ? ASP D 460 ? PHE D 458 ASP D 460 
AB1 18 ALA D 482 ? ILE D 484 ? ALA D 482 ILE D 484 
AB1 19 GLN D 506 ? ASP D 508 ? GLN D 506 ASP D 508 
AB1 20 LYS D 530 ? GLN D 532 ? LYS D 530 GLN D 532 
AB1 21 TYR D 554 ? ASP D 556 ? TYR D 554 ASP D 556 
AB1 22 TYR D 578 ? ASN D 580 ? TYR D 578 ASN D 580 
AB1 23 MET D 602 ? ASP D 604 ? MET D 602 ASP D 604 
AB1 24 ARG D 626 ? ASP D 628 ? ARG D 626 ASP D 628 
AB1 25 HIS D 650 ? ASP D 652 ? HIS D 650 ASP D 652 
AB2 1  GLU D 106 ? THR D 108 ? GLU D 106 THR D 108 
AB2 2  ARG D 129 ? GLY D 132 ? ARG D 129 GLY D 132 
AB2 3  GLN D 153 ? LEU D 154 ? GLN D 153 LEU D 154 
AB3 1  ASN D 179 ? SER D 181 ? ASN D 179 SER D 181 
AB3 2  LEU D 201 ? GLY D 204 ? LEU D 201 GLY D 204 
AB3 3  SER D 225 ? GLY D 228 ? SER D 225 GLY D 228 
AB3 4  ASN D 249 ? LEU D 250 ? ASN D 249 LEU D 250 
AB4 1  THR D 299 ? GLY D 300 ? THR D 299 GLY D 300 
AB4 2  GLN D 321 ? LEU D 322 ? GLN D 321 LEU D 322 
AB5 1  THR D 347 ? GLY D 348 ? THR D 347 GLY D 348 
AB5 2  GLN D 369 ? PRO D 373 ? GLN D 369 PRO D 373 
AB5 3  ASN D 393 ? GLY D 396 ? ASN D 393 GLY D 396 
AB5 4  HIS D 417 ? PHE D 418 ? HIS D 417 PHE D 418 
AB6 1  SER D 443 ? ASP D 445 ? SER D 443 ASP D 445 
AB6 2  ASN D 465 ? GLY D 468 ? ASN D 465 GLY D 468 
AB6 3  SER D 489 ? ILE D 490 ? SER D 489 ILE D 490 
AB7 1  SER D 539 ? GLY D 540 ? SER D 539 GLY D 540 
AB7 2  ARG D 561 ? PHE D 562 ? ARG D 561 PHE D 562 
AB8 1  ASP D 587 ? GLN D 588 ? ASP D 587 GLN D 588 
AB8 2  GLN D 609 ? GLU D 613 ? GLN D 609 GLU D 613 
AB8 3  ASN D 633 ? GLN D 637 ? ASN D 633 GLN D 637 
AB8 4  ASN D 657 ? GLY D 660 ? ASN D 657 GLY D 660 
AB8 5  ASP D 681 ? LEU D 682 ? ASP D 681 LEU D 682 
AB9 1  LEU E 39  ? ALA E 40  ? LEU E 39  ALA E 40  
AB9 2  SER E 81  ? GLN E 83  ? SER E 81  GLN E 83  
AB9 3  ASN E 103 ? GLY E 106 ? ASN E 103 GLY E 106 
AB9 4  ASN E 127 ? LEU E 128 ? ASN E 127 LEU E 128 
AC1 1  VAL E 62  ? CYS E 64  ? VAL E 62  CYS E 64  
AC1 2  VAL E 70  ? ASP E 74  ? VAL E 70  ASP E 74  
AC1 3  TYR E 96  ? GLU E 98  ? TYR E 96  GLU E 98  
AC1 4  SER E 120 ? ASP E 122 ? SER E 120 ASP E 122 
AC1 5  PHE E 144 ? ARG E 146 ? PHE E 144 ARG E 146 
AC1 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 ALA A 89  ? N ALA A 89  O ILE A 96  ? O ILE A 96  
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 CYS A 244 ? O CYS A 244 
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 SER A 292 ? O SER A 292 
AA1 10 11 N LEU A 291 ? N LEU A 291 O HIS A 316 ? O HIS A 316 
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 GLN A 388 ? O GLN A 388 
AA1 14 15 N LEU A 387 ? N LEU A 387 O THR A 412 ? O THR A 412 
AA1 15 16 N LEU A 411 ? N LEU A 411 O ARG A 436 ? O ARG A 436 
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 ILE A 484 ? O ILE A 484 
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 TYR A 578 ? O TYR A 578 
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 
AA2 5  6  N GLY A 204 ? N GLY A 204 O SER A 227 ? O SER A 227 
AA2 6  7  N LEU A 226 ? N LEU A 226 O ASN A 249 ? O ASN A 249 
AA3 1  2  N GLY A 300 ? N GLY A 300 O GLN A 321 ? O GLN A 321 
AA4 1  2  N GLY A 348 ? N GLY A 348 O SER A 371 ? O SER A 371 
AA4 2  3  N GLY A 372 ? N GLY A 372 O THR A 395 ? O THR A 395 
AA4 3  4  N GLY A 396 ? N GLY A 396 O GLU A 419 ? O GLU A 419 
AA4 4  5  N PHE A 418 ? N PHE A 418 O SER A 441 ? O SER A 441 
AA4 5  6  N GLY A 444 ? N GLY A 444 O HIS A 467 ? O HIS A 467 
AA5 1  2  N GLY A 492 ? N GLY A 492 O THR A 515 ? O THR A 515 
AA6 1  2  N GLY A 612 ? N GLY A 612 O SER A 635 ? O SER A 635 
AA6 2  3  N LEU A 634 ? N LEU A 634 O ASN A 657 ? O ASN A 657 
AA7 1  2  N ALA B 40  ? N ALA B 40  O SER B 81  ? O SER B 81  
AA7 2  3  N GLY B 82  ? N GLY B 82  O THR B 105 ? O THR B 105 
AA8 1  2  N THR B 63  ? N THR B 63  O THR B 71  ? O THR B 71  
AA8 2  3  N VAL B 73  ? N VAL B 73  O GLU B 98  ? O GLU B 98  
AA8 3  4  N LEU B 97  ? N LEU B 97  O ASP B 122 ? O ASP B 122 
AA8 4  5  N LEU B 121 ? N LEU B 121 O PHE B 144 ? O PHE B 144 
AA8 5  6  N LEU B 145 ? N LEU B 145 O VAL B 168 ? O VAL B 168 
AA9 1  2  N GLY B 130 ? N GLY B 130 O SER B 151 ? O SER B 151 
AB1 1  2  N SER D 91  ? N SER D 91  O SER D 94  ? O SER D 94  
AB1 2  3  N LEU D 98  ? N LEU D 98  O PHE D 122 ? O PHE D 122 
AB1 3  4  N VAL D 123 ? N VAL D 123 O TYR D 146 ? O TYR D 146 
AB1 4  5  N PHE D 147 ? N PHE D 147 O HIS D 172 ? O HIS D 172 
AB1 5  6  N LEU D 171 ? N LEU D 171 O ALA D 196 ? O ALA D 196 
AB1 6  7  N ILE D 195 ? N ILE D 195 O TYR D 220 ? O TYR D 220 
AB1 7  8  N LEU D 219 ? N LEU D 219 O CYS D 244 ? O CYS D 244 
AB1 8  9  N LEU D 243 ? N LEU D 243 O LEU D 266 ? O LEU D 266 
AB1 9  10 N LEU D 267 ? N LEU D 267 O SER D 292 ? O SER D 292 
AB1 10 11 N LEU D 291 ? N LEU D 291 O HIS D 316 ? O HIS D 316 
AB1 11 12 N LEU D 315 ? N LEU D 315 O ASP D 338 ? O ASP D 338 
AB1 12 13 N LEU D 339 ? N LEU D 339 O PHE D 364 ? O PHE D 364 
AB1 13 14 N LEU D 363 ? N LEU D 363 O GLN D 388 ? O GLN D 388 
AB1 14 15 N LEU D 387 ? N LEU D 387 O ASN D 410 ? O ASN D 410 
AB1 15 16 N LEU D 411 ? N LEU D 411 O ARG D 436 ? O ARG D 436 
AB1 16 17 N VAL D 435 ? N VAL D 435 O PHE D 458 ? O PHE D 458 
AB1 17 18 N ILE D 459 ? N ILE D 459 O ILE D 484 ? O ILE D 484 
AB1 18 19 N PHE D 483 ? N PHE D 483 O ASP D 508 ? O ASP D 508 
AB1 19 20 N LEU D 507 ? N LEU D 507 O GLN D 532 ? O GLN D 532 
AB1 20 21 N LEU D 531 ? N LEU D 531 O TYR D 554 ? O TYR D 554 
AB1 21 22 N LEU D 555 ? N LEU D 555 O ASN D 580 ? O ASN D 580 
AB1 22 23 N MET D 579 ? N MET D 579 O ASP D 604 ? O ASP D 604 
AB1 23 24 N LEU D 603 ? N LEU D 603 O ARG D 626 ? O ARG D 626 
AB1 24 25 N LEU D 627 ? N LEU D 627 O HIS D 650 ? O HIS D 650 
AB2 1  2  N GLY D 107 ? N GLY D 107 O SER D 131 ? O SER D 131 
AB2 2  3  N PHE D 130 ? N PHE D 130 O GLN D 153 ? O GLN D 153 
AB3 1  2  N GLY D 180 ? N GLY D 180 O THR D 203 ? O THR D 203 
AB3 2  3  N GLY D 204 ? N GLY D 204 O SER D 227 ? O SER D 227 
AB3 3  4  N LEU D 226 ? N LEU D 226 O ASN D 249 ? O ASN D 249 
AB4 1  2  N GLY D 300 ? N GLY D 300 O GLN D 321 ? O GLN D 321 
AB5 1  2  N GLY D 348 ? N GLY D 348 O SER D 371 ? O SER D 371 
AB5 2  3  N GLY D 372 ? N GLY D 372 O THR D 395 ? O THR D 395 
AB5 3  4  N PHE D 394 ? N PHE D 394 O HIS D 417 ? O HIS D 417 
AB6 1  2  N GLY D 444 ? N GLY D 444 O HIS D 467 ? O HIS D 467 
AB6 2  3  N PHE D 466 ? N PHE D 466 O SER D 489 ? O SER D 489 
AB7 1  2  N GLY D 540 ? N GLY D 540 O ARG D 561 ? O ARG D 561 
AB8 1  2  N GLN D 588 ? N GLN D 588 O ASP D 611 ? O ASP D 611 
AB8 2  3  N LEU D 610 ? N LEU D 610 O ASN D 633 ? O ASN D 633 
AB8 3  4  N LEU D 634 ? N LEU D 634 O ASN D 657 ? O ASN D 657 
AB8 4  5  N GLY D 660 ? N GLY D 660 O ASP D 681 ? O ASP D 681 
AB9 1  2  N ALA E 40  ? N ALA E 40  O SER E 81  ? O SER E 81  
AB9 2  3  N GLY E 82  ? N GLY E 82  O THR E 105 ? O THR E 105 
AB9 3  4  N ILE E 104 ? N ILE E 104 O ASN E 127 ? O ASN E 127 
AC1 1  2  N THR E 63  ? N THR E 63  O THR E 71  ? O THR E 71  
AC1 2  3  N VAL E 73  ? N VAL E 73  O GLU E 98  ? O GLU E 98  
AC1 3  4  N LEU E 97  ? N LEU E 97  O ASP E 122 ? O ASP E 122 
AC1 4  5  N LEU E 121 ? N LEU E 121 O PHE E 144 ? O PHE E 144 
AC1 5  6  N LEU E 145 ? N LEU E 145 O VAL E 168 ? O VAL E 168 
# 
_pdbx_entry_details.entry_id                   8WEC 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 C4  G NAG 2  ? ? O1  B BMA 301 ? ? 1.56 
2 1 C4  O NAG 2  ? ? O1  P BMA 1   ? ? 1.66 
3 1 OG1 A THR 62 ? ? OE1 A GLU 106 ? ? 1.87 
4 1 C3  G NAG 2  ? ? O1  B BMA 301 ? ? 2.00 
5 1 OG  E SER 38 ? ? O   E GLN 83  ? ? 2.15 
# 
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 VAL A 74  ? ? -121.52 -60.92  
2  1 ASN A 128 ? ? -129.18 -169.65 
3  1 ILE A 151 ? ? 47.68   73.34   
4  1 ILE A 433 ? ? -121.15 -58.75  
5  1 LYS A 680 ? ? -94.09  -61.47  
6  1 LEU B 164 ? ? 68.99   -3.85   
7  1 SER B 185 ? ? 126.89  -44.95  
8  1 SER D 79  ? ? 74.60   -5.78   
9  1 ILE D 151 ? ? 48.99   74.13   
10 1 ILE D 223 ? ? 55.98   71.80   
11 1 ILE D 433 ? ? -121.30 -59.27  
12 1 GLN D 588 ? ? 65.15   -172.32 
13 1 LEU E 164 ? ? 67.47   -0.22   
14 1 LYS E 198 ? ? 58.58   -143.77 
# 
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 -47.4351 31.7193  112.4332 0.6146 ? 0.1115  ? 0.0267  ? 0.2855 ? 0.0683  ? 0.6180 ? 3.5328 ? 
1.9912  ? 1.6603  ? 1.8970 ? 2.0837  ? 3.6122 ? 0.0556  ? -0.1996 ? -0.2355 ? 0.1711  ? -0.0432 ? -0.2220 ? 0.2252  ? 0.0893  ? 
-0.0054 ? 
2  'X-RAY DIFFRACTION' ? refined -58.7276 20.5292  73.6016  0.5752 ? 0.1865  ? -0.1200 ? 0.6413 ? -0.0718 ? 0.6219 ? 2.1588 ? 
-1.0969 ? -1.9826 ? 1.5764 ? 1.8347  ? 4.8512 ? 0.2934  ? 0.7292  ? -0.0940 ? -0.3647 ? -0.4993 ? 0.4479  ? -0.4150 ? -1.0960 ? 
0.1989  ? 
3  'X-RAY DIFFRACTION' ? refined -35.8383 6.9615   54.1371  0.5992 ? 0.0533  ? -0.1091 ? 0.5059 ? -0.0420 ? 0.4624 ? 3.6226 ? 
-3.1396 ? -3.3112 ? 5.5359 ? 1.3083  ? 3.9337 ? 0.0051  ? 0.7531  ? 0.0377  ? -0.7218 ? -0.2605 ? 0.2429  ? -0.6242 ? -0.7251 ? 
0.2466  ? 
4  'X-RAY DIFFRACTION' ? refined -26.6068 -8.2105  60.1206  0.6428 ? 0.0479  ? -0.0248 ? 0.3801 ? 0.0033  ? 0.3597 ? 6.3622 ? 
-2.0789 ? -1.2970 ? 8.0048 ? -1.1153 ? 5.0762 ? -0.3753 ? -0.1419 ? -0.1540 ? 0.3534  ? 0.0301  ? -0.0559 ? 0.7246  ? 0.2512  ? 
0.3287  ? 
5  'X-RAY DIFFRACTION' ? refined -29.4096 -27.9064 69.1010  2.0769 ? 0.1011  ? 0.3470  ? 0.7194 ? 0.2001  ? 1.0766 ? 0.9423 ? 
-1.2452 ? 0.1434  ? 3.2670 ? -1.6667 ? 1.5217 ? -0.8178 ? -0.3820 ? -0.9794 ? 1.2586  ? 0.0964  ? 0.4133  ? 1.8182  ? -0.0493 ? 
0.6004  ? 
6  'X-RAY DIFFRACTION' ? refined -37.7276 6.6759   84.6290  1.2747 ? 0.1612  ? 0.1142  ? 0.8614 ? 0.0094  ? 0.6915 ? 6.2903 ? 
2.3740  ? -2.2371 ? 7.2401 ? -0.5890 ? 1.9979 ? 0.3529  ? -1.0845 ? 0.0171  ? 1.6942  ? -0.1891 ? 0.3348  ? 0.0163  ? 0.3824  ? 
-0.1569 ? 
7  'X-RAY DIFFRACTION' ? refined -36.0226 6.6794   76.1058  0.9577 ? 0.0170  ? -0.1006 ? 0.6078 ? -0.1398 ? 0.5486 ? 2.7910 ? 
-1.9017 ? 0.0193  ? 5.9654 ? 0.7662  ? 1.8635 ? 0.2495  ? 0.0192  ? 0.0349  ? 0.5459  ? -0.2696 ? 0.2777  ? 0.4434  ? 0.4790  ? 
0.0580  ? 
8  'X-RAY DIFFRACTION' ? refined -37.8963 -2.1266  82.7069  1.2296 ? 0.1948  ? 0.1439  ? 0.7602 ? 0.2185  ? 0.6631 ? 5.0441 ? 
-1.2379 ? 3.6388  ? 3.7228 ? 2.6854  ? 6.3925 ? -0.2960 ? -0.2704 ? -0.1642 ? 1.3031  ? 0.0853  ? 0.6077  ? 1.1706  ? 0.2100  ? 
0.1808  ? 
9  'X-RAY DIFFRACTION' ? refined -32.4576 -3.7849  90.1866  1.9999 ? 0.5724  ? -0.2005 ? 1.1328 ? 0.0971  ? 0.8552 ? 2.3986 ? 
0.3412  ? 0.3396  ? 5.5190 ? 2.3397  ? 8.5185 ? -0.5405 ? -0.3617 ? -0.0391 ? 1.7361  ? 0.2152  ? 0.2583  ? 0.9168  ? 1.7862  ? 
0.2996  ? 
10 'X-RAY DIFFRACTION' ? refined -34.7635 -10.9778 91.2462  1.8913 ? 0.3910  ? 0.3402  ? 1.2841 ? 0.2339  ? 0.8038 ? 3.7717 ? 
0.4464  ? 2.8865  ? 3.5419 ? -0.3677 ? 2.9488 ? -0.2106 ? -0.7295 ? -0.1608 ? 1.4004  ? 0.0824  ? 0.3709  ? 1.2936  ? 0.5712  ? 
0.1071  ? 
11 'X-RAY DIFFRACTION' ? refined -29.8926 -16.8412 97.9531  2.8093 ? 0.4095  ? 0.0629  ? 1.4155 ? 0.2932  ? 1.0052 ? 3.2888 ? 
0.6142  ? -0.2962 ? 0.2422 ? -0.7267 ? 3.3122 ? -0.4661 ? -2.0267 ? -1.2533 ? 1.8500  ? -0.3222 ? -0.5502 ? 1.1300  ? 0.3966  ? 
0.8058  ? 
12 'X-RAY DIFFRACTION' ? refined -24.3850 -21.6687 97.6885  2.7671 ? 0.8940  ? 0.1327  ? 1.8365 ? 0.5549  ? 1.2465 ? 4.1769 ? 
-0.0407 ? 1.8047  ? 1.7405 ? -1.8431 ? 2.6839 ? -0.7436 ? -0.8510 ? -0.3447 ? 0.4445  ? -0.2764 ? -0.5362 ? 0.3512  ? 0.6910  ? 
0.9899  ? 
13 'X-RAY DIFFRACTION' ? refined -48.7396 21.1930  83.5812  0.9745 ? 0.0807  ? 0.0416  ? 0.4669 ? 0.1139  ? 0.9042 ? 2.7604 ? 
-2.3194 ? -1.6922 ? 2.1875 ? 1.9173  ? 2.0964 ? -0.9133 ? 0.1575  ? 0.5483  ? 1.4302  ? -0.3062 ? 0.9857  ? 1.7106  ? 0.6367  ? 
1.2015  ? 
14 'X-RAY DIFFRACTION' ? refined -4.9119  -12.7624 23.8049  0.4053 ? 0.0897  ? -0.1755 ? 0.3201 ? 0.0624  ? 0.5301 ? 2.2695 ? 
0.8472  ? -1.1750 ? 1.1890 ? -0.6589 ? 1.3273 ? -0.0699 ? -0.2429 ? -0.0779 ? 0.1012  ? -0.0682 ? -0.1649 ? 0.0181  ? 0.2181  ? 
0.1283  ? 
15 'X-RAY DIFFRACTION' ? refined 4.2645   24.7588  -11.6938 0.5713 ? 0.0121  ? 0.0515  ? 0.3684 ? 0.0454  ? 0.5734 ? 2.6822 ? 
-0.5196 ? -0.6046 ? 6.0883 ? -1.0735 ? 3.4885 ? 0.2141  ? -0.0156 ? 0.4837  ? 0.0308  ? 0.0876  ? 0.1638  ? -0.7958 ? -0.1789 ? 
-0.2314 ? 
16 'X-RAY DIFFRACTION' ? refined -9.7146  6.2853   7.7711   0.5103 ? -0.0266 ? 0.1026  ? 0.6052 ? 0.1065  ? 0.8031 ? 9.4886 ? 
-1.1180 ? 1.0087  ? 5.9212 ? 0.7355  ? 7.0673 ? 0.0004  ? -0.0876 ? -1.1967 ? 0.6365  ? 0.3764  ? 1.1123  ? 0.1077  ? -1.2490 ? 
-0.3533 ? 
17 'X-RAY DIFFRACTION' ? refined -3.7935  10.6450  2.4784   0.4288 ? 0.0442  ? 0.0112  ? 0.4880 ? 0.0931  ? 0.6113 ? 8.5695 ? 
-1.2087 ? -0.6557 ? 6.2694 ? 0.3805  ? 5.3910 ? 0.1974  ? 0.0009  ? -0.2816 ? 0.1171  ? 0.1103  ? 0.1443  ? -0.4774 ? -0.9868 ? 
-0.3107 ? 
18 'X-RAY DIFFRACTION' ? refined -14.8012 15.4272  8.5227   0.6742 ? 0.2837  ? 0.1254  ? 1.0260 ? 0.2652  ? 0.9221 ? 7.3872 ? 
-0.9160 ? 0.1901  ? 6.7448 ? 0.6718  ? 3.9639 ? -0.1588 ? -0.3927 ? 0.7620  ? 0.8522  ? 0.3172  ? 1.5574  ? -0.3437 ? -1.3843 ? 
-0.1235 ? 
19 'X-RAY DIFFRACTION' ? refined -16.3629 23.9151  9.3695   0.9721 ? 0.3873  ? 0.2299  ? 1.0020 ? 0.1960  ? 0.8755 ? 4.5965 ? 
-1.5968 ? -0.4886 ? 9.3271 ? 2.3292  ? 4.6776 ? -0.1329 ? -0.2895 ? 0.6485  ? 0.8096  ? 0.4914  ? 0.9542  ? -0.8755 ? -1.3075 ? 
-0.3331 ? 
20 'X-RAY DIFFRACTION' ? refined -27.3000 24.0859  7.0234   1.1282 ? 0.6340  ? 0.5537  ? 1.8079 ? 0.4303  ? 1.9031 ? 6.2605 ? 
-2.4679 ? -1.4920 ? 7.7385 ? 3.6972  ? 2.8355 ? 0.5192  ? 0.3276  ? 0.0386  ? 0.6754  ? -0.2695 ? 1.5408  ? -1.0826 ? -2.2338 ? 
-0.1667 ? 
21 'X-RAY DIFFRACTION' ? refined -17.6981 33.2788  11.8549  1.6464 ? 0.3718  ? 0.4418  ? 0.9675 ? 0.0174  ? 1.0929 ? 6.5999 ? 
-3.4290 ? -0.3227 ? 6.1699 ? 4.2822  ? 4.4194 ? -0.0595 ? -1.0245 ? 0.7337  ? 1.1803  ? 0.2629  ? 1.1031  ? -0.7652 ? -0.8368 ? 
-0.2545 ? 
22 'X-RAY DIFFRACTION' ? refined -27.6758 33.7018  6.9141   0.8703 ? 0.3335  ? 0.2786  ? 1.3162 ? 0.1895  ? 1.4613 ? 7.8395 ? 
-3.7029 ? -0.8266 ? 7.6261 ? 3.9075  ? 3.3472 ? 0.3505  ? -0.0368 ? -0.1061 ? 0.3157  ? -0.7100 ? 1.9340  ? -0.5976 ? -1.4605 ? 
0.2864  ? 
23 'X-RAY DIFFRACTION' ? refined -2.6790  -8.7051  15.8693  0.6458 ? 0.1069  ? 0.1128  ? 0.6032 ? 0.1227  ? 1.1919 ? 3.9696 ? 
3.5622  ? -2.8545 ? 3.6283 ? -1.7214 ? 3.5447 ? 0.3719  ? 0.3757  ? -1.1919 ? 0.1372  ? -0.1926 ? -0.5617 ? -0.2133 ? -0.1676 ? 
-0.2108 ? 
# 
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 212 )
;
2  'X-RAY DIFFRACTION' 2  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 213 through 442 )
;
3  'X-RAY DIFFRACTION' 3  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 443 through 500 )
;
4  'X-RAY DIFFRACTION' 4  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 501 through 591 )
;
5  'X-RAY DIFFRACTION' 5  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 592 through 683 )
;
6  'X-RAY DIFFRACTION' 6  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 26 through 41 )
;
7  'X-RAY DIFFRACTION' 7  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 42 through 61 )
;
8  'X-RAY DIFFRACTION' 8  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 62 through 95 )
;
9  'X-RAY DIFFRACTION' 9  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 96 through 114 )
;
10 'X-RAY DIFFRACTION' 10 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 115 through 146 )
;
11 'X-RAY DIFFRACTION' 11 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 147 through 185 )
;
12 'X-RAY DIFFRACTION' 12 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 186 through 200 )
;
13 'X-RAY DIFFRACTION' 13 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 1 through 13 )
;
14 'X-RAY DIFFRACTION' 14 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 47 through 442 )
;
15 'X-RAY DIFFRACTION' 15 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 443 through 683 )
;
16 'X-RAY DIFFRACTION' 16 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'E' and (resid 26 through 41 )
;
17 'X-RAY DIFFRACTION' 17 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'E' and (resid 42 through 79 )
;
18 'X-RAY DIFFRACTION' 18 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'E' and (resid 80 through 114 )
;
19 'X-RAY DIFFRACTION' 19 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'E' and (resid 115 through 146 )
;
20 'X-RAY DIFFRACTION' 20 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'E' and (resid 147 through 157 )
;
21 'X-RAY DIFFRACTION' 21 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'E' and (resid 158 through 170 )
;
22 'X-RAY DIFFRACTION' 22 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'E' and (resid 171 through 199 )
;
23 'X-RAY DIFFRACTION' 23 ? ? ? ? ? ? ? ? ? ? ? 
;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 
MAN C1   C N S 274 
MAN C2   C N S 275 
MAN C3   C N S 276 
MAN C4   C N S 277 
MAN C5   C N R 278 
MAN C6   C N N 279 
MAN O1   O N N 280 
MAN O2   O N N 281 
MAN O3   O N N 282 
MAN O4   O N N 283 
MAN O5   O N N 284 
MAN O6   O N N 285 
MAN H1   H N N 286 
MAN H2   H N N 287 
MAN H3   H N N 288 
MAN H4   H N N 289 
MAN H5   H N N 290 
MAN H61  H N N 291 
MAN H62  H N N 292 
MAN HO1  H N N 293 
MAN HO2  H N N 294 
MAN HO3  H N N 295 
MAN HO4  H N N 296 
MAN HO6  H N N 297 
MET N    N N N 298 
MET CA   C N S 299 
MET C    C N N 300 
MET O    O N N 301 
MET CB   C N N 302 
MET CG   C N N 303 
MET SD   S N N 304 
MET CE   C N N 305 
MET OXT  O N N 306 
MET H    H N N 307 
MET H2   H N N 308 
MET HA   H N N 309 
MET HB2  H N N 310 
MET HB3  H N N 311 
MET HG2  H N N 312 
MET HG3  H N N 313 
MET HE1  H N N 314 
MET HE2  H N N 315 
MET HE3  H N N 316 
MET HXT  H N N 317 
NAG C1   C N R 318 
NAG C2   C N R 319 
NAG C3   C N R 320 
NAG C4   C N S 321 
NAG C5   C N R 322 
NAG C6   C N N 323 
NAG C7   C N N 324 
NAG C8   C N N 325 
NAG N2   N N N 326 
NAG O1   O N N 327 
NAG O3   O N N 328 
NAG O4   O N N 329 
NAG O5   O N N 330 
NAG O6   O N N 331 
NAG O7   O N N 332 
NAG H1   H N N 333 
NAG H2   H N N 334 
NAG H3   H N N 335 
NAG H4   H N N 336 
NAG H5   H N N 337 
NAG H61  H N N 338 
NAG H62  H N N 339 
NAG H81  H N N 340 
NAG H82  H N N 341 
NAG H83  H N N 342 
NAG HN2  H N N 343 
NAG HO1  H N N 344 
NAG HO3  H N N 345 
NAG HO4  H N N 346 
NAG HO6  H N N 347 
PHE N    N N N 348 
PHE CA   C N S 349 
PHE C    C N N 350 
PHE O    O N N 351 
PHE CB   C N N 352 
PHE CG   C Y N 353 
PHE CD1  C Y N 354 
PHE CD2  C Y N 355 
PHE CE1  C Y N 356 
PHE CE2  C Y N 357 
PHE CZ   C Y N 358 
PHE OXT  O N N 359 
PHE H    H N N 360 
PHE H2   H N N 361 
PHE HA   H N N 362 
PHE HB2  H N N 363 
PHE HB3  H N N 364 
PHE HD1  H N N 365 
PHE HD2  H N N 366 
PHE HE1  H N N 367 
PHE HE2  H N N 368 
PHE HZ   H N N 369 
PHE HXT  H N N 370 
PRO N    N N N 371 
PRO CA   C N S 372 
PRO C    C N N 373 
PRO O    O N N 374 
PRO CB   C N N 375 
PRO CG   C N N 376 
PRO CD   C N N 377 
PRO OXT  O N N 378 
PRO H    H N N 379 
PRO HA   H N N 380 
PRO HB2  H N N 381 
PRO HB3  H N N 382 
PRO HG2  H N N 383 
PRO HG3  H N N 384 
PRO HD2  H N N 385 
PRO HD3  H N N 386 
PRO HXT  H N N 387 
SER N    N N N 388 
SER CA   C N S 389 
SER C    C N N 390 
SER O    O N N 391 
SER CB   C N N 392 
SER OG   O N N 393 
SER OXT  O N N 394 
SER H    H N N 395 
SER H2   H N N 396 
SER HA   H N N 397 
SER HB2  H N N 398 
SER HB3  H N N 399 
SER HG   H N N 400 
SER HXT  H N N 401 
THR N    N N N 402 
THR CA   C N S 403 
THR C    C N N 404 
THR O    O N N 405 
THR CB   C N R 406 
THR OG1  O N N 407 
THR CG2  C N N 408 
THR OXT  O N N 409 
THR H    H N N 410 
THR H2   H N N 411 
THR HA   H N N 412 
THR HB   H N N 413 
THR HG1  H N N 414 
THR HG21 H N N 415 
THR HG22 H N N 416 
THR HG23 H N N 417 
THR HXT  H N N 418 
TRP N    N N N 419 
TRP CA   C N S 420 
TRP C    C N N 421 
TRP O    O N N 422 
TRP CB   C N N 423 
TRP CG   C Y N 424 
TRP CD1  C Y N 425 
TRP CD2  C Y N 426 
TRP NE1  N Y N 427 
TRP CE2  C Y N 428 
TRP CE3  C Y N 429 
TRP CZ2  C Y N 430 
TRP CZ3  C Y N 431 
TRP CH2  C Y N 432 
TRP OXT  O N N 433 
TRP H    H N N 434 
TRP H2   H N N 435 
TRP HA   H N N 436 
TRP HB2  H N N 437 
TRP HB3  H N N 438 
TRP HD1  H N N 439 
TRP HE1  H N N 440 
TRP HE3  H N N 441 
TRP HZ2  H N N 442 
TRP HZ3  H N N 443 
TRP HH2  H N N 444 
TRP HXT  H N N 445 
TYR N    N N N 446 
TYR CA   C N S 447 
TYR C    C N N 448 
TYR O    O N N 449 
TYR CB   C N N 450 
TYR CG   C Y N 451 
TYR CD1  C Y N 452 
TYR CD2  C Y N 453 
TYR CE1  C Y N 454 
TYR CE2  C Y N 455 
TYR CZ   C Y N 456 
TYR OH   O N N 457 
TYR OXT  O N N 458 
TYR H    H N N 459 
TYR H2   H N N 460 
TYR HA   H N N 461 
TYR HB2  H N N 462 
TYR HB3  H N N 463 
TYR HD1  H N N 464 
TYR HD2  H N N 465 
TYR HE1  H N N 466 
TYR HE2  H N N 467 
TYR HH   H N N 468 
TYR HXT  H N N 469 
VAL N    N N N 470 
VAL CA   C N S 471 
VAL C    C N N 472 
VAL O    O N N 473 
VAL CB   C N N 474 
VAL CG1  C N N 475 
VAL CG2  C N N 476 
VAL OXT  O N N 477 
VAL H    H N N 478 
VAL H2   H N N 479 
VAL HA   H N N 480 
VAL HB   H N N 481 
VAL HG11 H N N 482 
VAL HG12 H N N 483 
VAL HG13 H N N 484 
VAL HG21 H N N 485 
VAL HG22 H N N 486 
VAL HG23 H N N 487 
VAL HXT  H N N 488 
# 
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 
MAN C1  C2   sing N N 263 
MAN C1  O1   sing N N 264 
MAN C1  O5   sing N N 265 
MAN C1  H1   sing N N 266 
MAN C2  C3   sing N N 267 
MAN C2  O2   sing N N 268 
MAN C2  H2   sing N N 269 
MAN C3  C4   sing N N 270 
MAN C3  O3   sing N N 271 
MAN C3  H3   sing N N 272 
MAN C4  C5   sing N N 273 
MAN C4  O4   sing N N 274 
MAN C4  H4   sing N N 275 
MAN C5  C6   sing N N 276 
MAN C5  O5   sing N N 277 
MAN C5  H5   sing N N 278 
MAN C6  O6   sing N N 279 
MAN C6  H61  sing N N 280 
MAN C6  H62  sing N N 281 
MAN O1  HO1  sing N N 282 
MAN O2  HO2  sing N N 283 
MAN O3  HO3  sing N N 284 
MAN O4  HO4  sing N N 285 
MAN O6  HO6  sing N N 286 
MET N   CA   sing N N 287 
MET N   H    sing N N 288 
MET N   H2   sing N N 289 
MET CA  C    sing N N 290 
MET CA  CB   sing N N 291 
MET CA  HA   sing N N 292 
MET C   O    doub N N 293 
MET C   OXT  sing N N 294 
MET CB  CG   sing N N 295 
MET CB  HB2  sing N N 296 
MET CB  HB3  sing N N 297 
MET CG  SD   sing N N 298 
MET CG  HG2  sing N N 299 
MET CG  HG3  sing N N 300 
MET SD  CE   sing N N 301 
MET CE  HE1  sing N N 302 
MET CE  HE2  sing N N 303 
MET CE  HE3  sing N N 304 
MET OXT HXT  sing N N 305 
NAG C1  C2   sing N N 306 
NAG C1  O1   sing N N 307 
NAG C1  O5   sing N N 308 
NAG C1  H1   sing N N 309 
NAG C2  C3   sing N N 310 
NAG C2  N2   sing N N 311 
NAG C2  H2   sing N N 312 
NAG C3  C4   sing N N 313 
NAG C3  O3   sing N N 314 
NAG C3  H3   sing N N 315 
NAG C4  C5   sing N N 316 
NAG C4  O4   sing N N 317 
NAG C4  H4   sing N N 318 
NAG C5  C6   sing N N 319 
NAG C5  O5   sing N N 320 
NAG C5  H5   sing N N 321 
NAG C6  O6   sing N N 322 
NAG C6  H61  sing N N 323 
NAG C6  H62  sing N N 324 
NAG C7  C8   sing N N 325 
NAG C7  N2   sing N N 326 
NAG C7  O7   doub N N 327 
NAG C8  H81  sing N N 328 
NAG C8  H82  sing N N 329 
NAG C8  H83  sing N N 330 
NAG N2  HN2  sing N N 331 
NAG O1  HO1  sing N N 332 
NAG O3  HO3  sing N N 333 
NAG O4  HO4  sing N N 334 
NAG O6  HO6  sing N N 335 
PHE N   CA   sing N N 336 
PHE N   H    sing N N 337 
PHE N   H2   sing N N 338 
PHE CA  C    sing N N 339 
PHE CA  CB   sing N N 340 
PHE CA  HA   sing N N 341 
PHE C   O    doub N N 342 
PHE C   OXT  sing N N 343 
PHE CB  CG   sing N N 344 
PHE CB  HB2  sing N N 345 
PHE CB  HB3  sing N N 346 
PHE CG  CD1  doub Y N 347 
PHE CG  CD2  sing Y N 348 
PHE CD1 CE1  sing Y N 349 
PHE CD1 HD1  sing N N 350 
PHE CD2 CE2  doub Y N 351 
PHE CD2 HD2  sing N N 352 
PHE CE1 CZ   doub Y N 353 
PHE CE1 HE1  sing N N 354 
PHE CE2 CZ   sing Y N 355 
PHE CE2 HE2  sing N N 356 
PHE CZ  HZ   sing N N 357 
PHE OXT HXT  sing N N 358 
PRO N   CA   sing N N 359 
PRO N   CD   sing N N 360 
PRO N   H    sing N N 361 
PRO CA  C    sing N N 362 
PRO CA  CB   sing N N 363 
PRO CA  HA   sing N N 364 
PRO C   O    doub N N 365 
PRO C   OXT  sing N N 366 
PRO CB  CG   sing N N 367 
PRO CB  HB2  sing N N 368 
PRO CB  HB3  sing N N 369 
PRO CG  CD   sing N N 370 
PRO CG  HG2  sing N N 371 
PRO CG  HG3  sing N N 372 
PRO CD  HD2  sing N N 373 
PRO CD  HD3  sing N N 374 
PRO OXT HXT  sing N N 375 
SER N   CA   sing N N 376 
SER N   H    sing N N 377 
SER N   H2   sing N N 378 
SER CA  C    sing N N 379 
SER CA  CB   sing N N 380 
SER CA  HA   sing N N 381 
SER C   O    doub N N 382 
SER C   OXT  sing N N 383 
SER CB  OG   sing N N 384 
SER CB  HB2  sing N N 385 
SER CB  HB3  sing N N 386 
SER OG  HG   sing N N 387 
SER OXT HXT  sing N N 388 
THR N   CA   sing N N 389 
THR N   H    sing N N 390 
THR N   H2   sing N N 391 
THR CA  C    sing N N 392 
THR CA  CB   sing N N 393 
THR CA  HA   sing N N 394 
THR C   O    doub N N 395 
THR C   OXT  sing N N 396 
THR CB  OG1  sing N N 397 
THR CB  CG2  sing N N 398 
THR CB  HB   sing N N 399 
THR OG1 HG1  sing N N 400 
THR CG2 HG21 sing N N 401 
THR CG2 HG22 sing N N 402 
THR CG2 HG23 sing N N 403 
THR OXT HXT  sing N N 404 
TRP N   CA   sing N N 405 
TRP N   H    sing N N 406 
TRP N   H2   sing N N 407 
TRP CA  C    sing N N 408 
TRP CA  CB   sing N N 409 
TRP CA  HA   sing N N 410 
TRP C   O    doub N N 411 
TRP C   OXT  sing N N 412 
TRP CB  CG   sing N N 413 
TRP CB  HB2  sing N N 414 
TRP CB  HB3  sing N N 415 
TRP CG  CD1  doub Y N 416 
TRP CG  CD2  sing Y N 417 
TRP CD1 NE1  sing Y N 418 
TRP CD1 HD1  sing N N 419 
TRP CD2 CE2  doub Y N 420 
TRP CD2 CE3  sing Y N 421 
TRP NE1 CE2  sing Y N 422 
TRP NE1 HE1  sing N N 423 
TRP CE2 CZ2  sing Y N 424 
TRP CE3 CZ3  doub Y N 425 
TRP CE3 HE3  sing N N 426 
TRP CZ2 CH2  doub Y N 427 
TRP CZ2 HZ2  sing N N 428 
TRP CZ3 CH2  sing Y N 429 
TRP CZ3 HZ3  sing N N 430 
TRP CH2 HH2  sing N N 431 
TRP OXT HXT  sing N N 432 
TYR N   CA   sing N N 433 
TYR N   H    sing N N 434 
TYR N   H2   sing N N 435 
TYR CA  C    sing N N 436 
TYR CA  CB   sing N N 437 
TYR CA  HA   sing N N 438 
TYR C   O    doub N N 439 
TYR C   OXT  sing N N 440 
TYR CB  CG   sing N N 441 
TYR CB  HB2  sing N N 442 
TYR CB  HB3  sing N N 443 
TYR CG  CD1  doub Y N 444 
TYR CG  CD2  sing Y N 445 
TYR CD1 CE1  sing Y N 446 
TYR CD1 HD1  sing N N 447 
TYR CD2 CE2  doub Y N 448 
TYR CD2 HD2  sing N N 449 
TYR CE1 CZ   doub Y N 450 
TYR CE1 HE1  sing N N 451 
TYR CE2 CZ   sing Y N 452 
TYR CE2 HE2  sing N N 453 
TYR CZ  OH   sing N N 454 
TYR OH  HH   sing N N 455 
TYR OXT HXT  sing N N 456 
VAL N   CA   sing N N 457 
VAL N   H    sing N N 458 
VAL N   H2   sing N N 459 
VAL CA  C    sing N N 460 
VAL CA  CB   sing N N 461 
VAL CA  HA   sing N N 462 
VAL C   O    doub N N 463 
VAL C   OXT  sing N N 464 
VAL CB  CG1  sing N N 465 
VAL CB  CG2  sing N N 466 
VAL CB  HB   sing N N 467 
VAL CG1 HG11 sing N N 468 
VAL CG1 HG12 sing N N 469 
VAL CG1 HG13 sing N N 470 
VAL CG2 HG21 sing N N 471 
VAL CG2 HG22 sing N N 472 
VAL CG2 HG23 sing N N 473 
VAL OXT HXT  sing N N 474 
# 
_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 NAG 2 n 
5 NAG 1 n 
5 FUC 2 n 
5 NAG 3 n 
5 FUC 4 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 BMA 1 n 
8 MAN 2 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                    8WEC 
_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]   0.013698 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000189 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.005596 
_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]   0.006937 
_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  ? -42.925 45.156  124.761 1.00 74.17  ?  47   THR A N   1 
ATOM   2     C CA  . THR A  1  47  ? -41.754 44.538  124.140 1.00 73.86  ?  47   THR A CA  1 
ATOM   3     C C   . THR A  1  47  ? -41.047 43.586  125.082 1.00 79.04  ?  47   THR A C   1 
ATOM   4     O O   . THR A  1  47  ? -40.848 42.418  124.757 1.00 78.41  ?  47   THR A O   1 
ATOM   5     C CB  . THR A  1  47  ? -40.694 45.568  123.684 1.00 73.27  ?  47   THR A CB  1 
ATOM   6     O OG1 . THR A  1  47  ? -39.809 45.860  124.775 1.00 77.97  ?  47   THR A OG1 1 
ATOM   7     C CG2 . THR A  1  47  ? -41.339 46.842  123.225 1.00 70.09  ?  47   THR A CG2 1 
ATOM   8     N N   . VAL A  1  48  ? -40.634 44.106  126.242 1.00 69.62  ?  48   VAL A N   1 
ATOM   9     C CA  . VAL A  1  48  ? -39.820 43.314  127.157 1.00 75.23  ?  48   VAL A CA  1 
ATOM   10    C C   . VAL A  1  48  ? -40.545 42.033  127.539 1.00 77.50  ?  48   VAL A C   1 
ATOM   11    O O   . VAL A  1  48  ? -39.918 40.979  127.705 1.00 79.00  ?  48   VAL A O   1 
ATOM   12    C CB  . VAL A  1  48  ? -39.431 44.161  128.384 1.00 78.55  ?  48   VAL A CB  1 
ATOM   13    C CG1 . VAL A  1  48  ? -39.017 43.280  129.544 1.00 82.69  ?  48   VAL A CG1 1 
ATOM   14    C CG2 . VAL A  1  48  ? -38.304 45.107  128.019 1.00 77.64  ?  48   VAL A CG2 1 
ATOM   15    N N   . GLU A  1  49  ? -41.875 42.081  127.631 1.00 81.51  ?  49   GLU A N   1 
ATOM   16    C CA  . GLU A  1  49  ? -42.632 40.846  127.790 1.00 83.50  ?  49   GLU A CA  1 
ATOM   17    C C   . GLU A  1  49  ? -42.692 40.069  126.481 1.00 77.11  ?  49   GLU A C   1 
ATOM   18    O O   . GLU A  1  49  ? -42.518 38.845  126.472 1.00 75.97  ?  49   GLU A O   1 
ATOM   19    C CB  . GLU A  1  49  ? -44.038 41.156  128.303 1.00 83.67  ?  49   GLU A CB  1 
ATOM   20    C CG  . GLU A  1  49  ? -44.054 41.755  129.704 1.00 85.34  ?  49   GLU A CG  1 
ATOM   21    C CD  . GLU A  1  49  ? -44.072 43.278  129.694 1.00 82.17  ?  49   GLU A CD  1 
ATOM   22    O OE1 . GLU A  1  49  ? -44.840 43.862  128.896 1.00 78.49  ?  49   GLU A OE1 1 
ATOM   23    O OE2 . GLU A  1  49  ? -43.313 43.890  130.480 1.00 82.83  -1 49   GLU A OE2 1 
ATOM   24    N N   . GLU A  1  50  ? -42.927 40.761  125.363 1.00 79.44  ?  50   GLU A N   1 
ATOM   25    C CA  . GLU A  1  50  ? -42.917 40.098  124.062 1.00 72.83  ?  50   GLU A CA  1 
ATOM   26    C C   . GLU A  1  50  ? -41.549 39.492  123.767 1.00 71.56  ?  50   GLU A C   1 
ATOM   27    O O   . GLU A  1  50  ? -41.445 38.323  123.381 1.00 68.92  ?  50   GLU A O   1 
ATOM   28    C CB  . GLU A  1  50  ? -43.307 41.089  122.962 1.00 67.76  ?  50   GLU A CB  1 
ATOM   29    C CG  . GLU A  1  50  ? -44.691 41.718  123.103 1.00 67.82  ?  50   GLU A CG  1 
ATOM   30    C CD  . GLU A  1  50  ? -44.975 42.752  122.015 1.00 62.81  ?  50   GLU A CD  1 
ATOM   31    O OE1 . GLU A  1  50  ? -44.034 43.475  121.612 1.00 61.71  ?  50   GLU A OE1 1 
ATOM   32    O OE2 . GLU A  1  50  ? -46.137 42.833  121.553 1.00 60.55  -1 50   GLU A OE2 1 
ATOM   33    N N   . ALA A  1  51  ? -40.482 40.277  123.952 1.00 69.13  ?  51   ALA A N   1 
ATOM   34    C CA  . ALA A  1  51  ? -39.138 39.803  123.630 1.00 68.90  ?  51   ALA A CA  1 
ATOM   35    C C   . ALA A  1  51  ? -38.742 38.614  124.495 1.00 71.08  ?  51   ALA A C   1 
ATOM   36    O O   . ALA A  1  51  ? -38.124 37.661  124.005 1.00 68.65  ?  51   ALA A O   1 
ATOM   37    C CB  . ALA A  1  51  ? -38.124 40.935  123.790 1.00 72.18  ?  51   ALA A CB  1 
ATOM   38    N N   . ASN A  1  52  ? -39.074 38.656  125.788 1.00 70.47  ?  52   ASN A N   1 
ATOM   39    C CA  . ASN A  1  52  ? -38.745 37.538  126.667 1.00 71.74  ?  52   ASN A CA  1 
ATOM   40    C C   . ASN A  1  52  ? -39.603 36.316  126.366 1.00 68.14  ?  52   ASN A C   1 
ATOM   41    O O   . ASN A  1  52  ? -39.149 35.180  126.548 1.00 66.60  ?  52   ASN A O   1 
ATOM   42    C CB  . ASN A  1  52  ? -38.898 37.951  128.130 1.00 77.40  ?  52   ASN A CB  1 
ATOM   43    C CG  . ASN A  1  52  ? -37.739 38.800  128.617 1.00 80.62  ?  52   ASN A CG  1 
ATOM   44    O OD1 . ASN A  1  52  ? -36.579 38.515  128.320 1.00 79.39  ?  52   ASN A OD1 1 
ATOM   45    N ND2 . ASN A  1  52  ? -38.048 39.850  129.370 1.00 84.54  ?  52   ASN A ND2 1 
ATOM   46    N N   . ALA A  1  53  ? -40.838 36.526  125.911 1.00 73.19  ?  53   ALA A N   1 
ATOM   47    C CA  . ALA A  1  53  ? -41.683 35.399  125.535 1.00 69.99  ?  53   ALA A CA  1 
ATOM   48    C C   . ALA A  1  53  ? -41.183 34.741  124.255 1.00 64.24  ?  53   ALA A C   1 
ATOM   49    O O   . ALA A  1  53  ? -41.188 33.509  124.143 1.00 62.14  ?  53   ALA A O   1 
ATOM   50    C CB  . ALA A  1  53  ? -43.130 35.859  125.381 1.00 70.99  ?  53   ALA A CB  1 
ATOM   51    N N   . LEU A  1  54  ? -40.758 35.545  123.273 1.00 68.33  ?  54   LEU A N   1 
ATOM   52    C CA  . LEU A  1  54  ? -40.129 34.983  122.082 1.00 64.33  ?  54   LEU A CA  1 
ATOM   53    C C   . LEU A  1  54  ? -38.857 34.231  122.443 1.00 65.74  ?  54   LEU A C   1 
ATOM   54    O O   . LEU A  1  54  ? -38.608 33.133  121.931 1.00 63.43  ?  54   LEU A O   1 
ATOM   55    C CB  . LEU A  1  54  ? -39.813 36.086  121.071 1.00 62.98  ?  54   LEU A CB  1 
ATOM   56    C CG  . LEU A  1  54  ? -40.825 36.407  119.969 1.00 58.88  ?  54   LEU A CG  1 
ATOM   57    C CD1 . LEU A  1  54  ? -41.114 35.200  119.102 1.00 55.36  ?  54   LEU A CD1 1 
ATOM   58    C CD2 . LEU A  1  54  ? -42.084 36.906  120.572 1.00 59.59  ?  54   LEU A CD2 1 
ATOM   59    N N   . LEU A  1  55  ? -38.041 34.809  123.329 1.00 64.51  ?  55   LEU A N   1 
ATOM   60    C CA  . LEU A  1  55  ? -36.792 34.170  123.731 1.00 66.07  ?  55   LEU A CA  1 
ATOM   61    C C   . LEU A  1  55  ? -37.045 32.821  124.397 1.00 65.34  ?  55   LEU A C   1 
ATOM   62    O O   . LEU A  1  55  ? -36.254 31.883  124.235 1.00 64.41  ?  55   LEU A O   1 
ATOM   63    C CB  . LEU A  1  55  ? -36.018 35.096  124.666 1.00 70.80  ?  55   LEU A CB  1 
ATOM   64    C CG  . LEU A  1  55  ? -34.873 35.894  124.049 1.00 72.29  ?  55   LEU A CG  1 
ATOM   65    C CD1 . LEU A  1  55  ? -34.521 37.078  124.938 1.00 76.79  ?  55   LEU A CD1 1 
ATOM   66    C CD2 . LEU A  1  55  ? -33.665 35.000  123.824 1.00 72.49  ?  55   LEU A CD2 1 
ATOM   67    N N   . LYS A  1  56  ? -38.138 32.706  125.158 1.00 69.58  ?  56   LYS A N   1 
ATOM   68    C CA  . LYS A  1  56  ? -38.489 31.422  125.757 1.00 68.93  ?  56   LYS A CA  1 
ATOM   69    C C   . LYS A  1  56  ? -38.885 30.405  124.691 1.00 64.64  ?  56   LYS A C   1 
ATOM   70    O O   . LYS A  1  56  ? -38.563 29.216  124.807 1.00 63.51  ?  56   LYS A O   1 
ATOM   71    C CB  . LYS A  1  56  ? -39.614 31.608  126.774 1.00 71.50  ?  56   LYS A CB  1 
ATOM   72    C CG  . LYS A  1  56  ? -40.439 30.356  127.028 1.00 70.02  ?  56   LYS A CG  1 
ATOM   73    C CD  . LYS A  1  56  ? -40.836 30.239  128.490 1.00 73.47  ?  56   LYS A CD  1 
ATOM   74    C CE  . LYS A  1  56  ? -41.988 29.260  128.671 1.00 72.36  ?  56   LYS A CE  1 
ATOM   75    N NZ  . LYS A  1  56  ? -41.862 28.460  129.926 1.00 73.52  ?  56   LYS A NZ  1 
ATOM   76    N N   . TRP A  1  57  ? -39.575 30.857  123.641 1.00 72.64  ?  57   TRP A N   1 
ATOM   77    C CA  . TRP A  1  57  ? -39.948 29.956  122.554 1.00 68.78  ?  57   TRP A CA  1 
ATOM   78    C C   . TRP A  1  57  ? -38.725 29.495  121.770 1.00 67.54  ?  57   TRP A C   1 
ATOM   79    O O   . TRP A  1  57  ? -38.653 28.332  121.351 1.00 65.71  ?  57   TRP A O   1 
ATOM   80    C CB  . TRP A  1  57  ? -40.944 30.642  121.622 1.00 66.70  ?  57   TRP A CB  1 
ATOM   81    C CG  . TRP A  1  57  ? -41.299 29.820  120.425 1.00 63.05  ?  57   TRP A CG  1 
ATOM   82    C CD1 . TRP A  1  57  ? -41.678 28.511  120.416 1.00 61.88  ?  57   TRP A CD1 1 
ATOM   83    C CD2 . TRP A  1  57  ? -41.316 30.252  119.060 1.00 60.52  ?  57   TRP A CD2 1 
ATOM   84    N NE1 . TRP A  1  57  ? -41.930 28.098  119.129 1.00 58.96  ?  57   TRP A NE1 1 
ATOM   85    C CE2 . TRP A  1  57  ? -41.715 29.149  118.279 1.00 58.15  ?  57   TRP A CE2 1 
ATOM   86    C CE3 . TRP A  1  57  ? -41.033 31.463  118.423 1.00 60.36  ?  57   TRP A CE3 1 
ATOM   87    C CZ2 . TRP A  1  57  ? -41.839 29.222  116.897 1.00 55.94  ?  57   TRP A CZ2 1 
ATOM   88    C CZ3 . TRP A  1  57  ? -41.157 31.533  117.051 1.00 57.86  ?  57   TRP A CZ3 1 
ATOM   89    C CH2 . TRP A  1  57  ? -41.556 30.420  116.302 1.00 55.77  ?  57   TRP A CH2 1 
ATOM   90    N N   . LYS A  1  58  ? -37.758 30.396  121.553 1.00 65.42  ?  58   LYS A N   1 
ATOM   91    C CA  . LYS A  1  58  ? -36.529 30.023  120.858 1.00 65.48  ?  58   LYS A CA  1 
ATOM   92    C C   . LYS A  1  58  ? -35.791 28.906  121.583 1.00 66.38  ?  58   LYS A C   1 
ATOM   93    O O   . LYS A  1  58  ? -35.082 28.118  120.947 1.00 65.63  ?  58   LYS A O   1 
ATOM   94    C CB  . LYS A  1  58  ? -35.625 31.248  120.704 1.00 68.16  ?  58   LYS A CB  1 
ATOM   95    C CG  . LYS A  1  58  ? -34.301 30.975  120.000 1.00 69.34  ?  58   LYS A CG  1 
ATOM   96    C CD  . LYS A  1  58  ? -33.364 32.168  120.094 1.00 73.03  ?  58   LYS A CD  1 
ATOM   97    C CE  . LYS A  1  58  ? -31.906 31.740  120.032 1.00 75.27  ?  58   LYS A CE  1 
ATOM   98    N NZ  . LYS A  1  58  ? -30.987 32.857  120.392 1.00 79.32  ?  58   LYS A NZ  1 
ATOM   99    N N   . SER A  1  59  ? -35.968 28.804  122.904 1.00 68.11  ?  59   SER A N   1 
ATOM   100   C CA  . SER A  1  59  ? -35.285 27.770  123.677 1.00 68.98  ?  59   SER A CA  1 
ATOM   101   C C   . SER A  1  59  ? -35.741 26.368  123.285 1.00 66.25  ?  59   SER A C   1 
ATOM   102   O O   . SER A  1  59  ? -34.976 25.406  123.424 1.00 66.27  ?  59   SER A O   1 
ATOM   103   C CB  . SER A  1  59  ? -35.515 28.009  125.171 1.00 71.64  ?  59   SER A CB  1 
ATOM   104   O OG  . SER A  1  59  ? -35.628 26.784  125.876 1.00 71.31  ?  59   SER A OG  1 
ATOM   105   N N   . THR A  1  60  ? -36.971 26.234  122.783 1.00 71.32  ?  60   THR A N   1 
ATOM   106   C CA  . THR A  1  60  ? -37.503 24.931  122.404 1.00 69.02  ?  60   THR A CA  1 
ATOM   107   C C   . THR A  1  60  ? -36.790 24.350  121.188 1.00 67.44  ?  60   THR A C   1 
ATOM   108   O O   . THR A  1  60  ? -36.769 23.124  121.018 1.00 66.33  ?  60   THR A O   1 
ATOM   109   C CB  . THR A  1  60  ? -39.012 25.079  122.148 1.00 67.54  ?  60   THR A CB  1 
ATOM   110   O OG1 . THR A  1  60  ? -39.704 25.086  123.402 1.00 69.19  ?  60   THR A OG1 1 
ATOM   111   C CG2 . THR A  1  60  ? -39.582 23.972  121.251 1.00 65.10  ?  60   THR A CG2 1 
ATOM   112   N N   . PHE A  1  61  ? -36.121 25.194  120.404 1.00 70.07  ?  61   PHE A N   1 
ATOM   113   C CA  . PHE A  1  61  ? -35.592 24.771  119.115 1.00 69.02  ?  61   PHE A CA  1 
ATOM   114   C C   . PHE A  1  61  ? -34.516 23.708  119.291 1.00 69.78  ?  61   PHE A C   1 
ATOM   115   O O   . PHE A  1  61  ? -33.707 23.759  120.222 1.00 71.77  ?  61   PHE A O   1 
ATOM   116   C CB  . PHE A  1  61  ? -35.025 25.974  118.360 1.00 70.25  ?  61   PHE A CB  1 
ATOM   117   C CG  . PHE A  1  61  ? -36.044 27.038  118.054 1.00 69.35  ?  61   PHE A CG  1 
ATOM   118   C CD1 . PHE A  1  61  ? -37.401 26.762  118.113 1.00 67.09  ?  61   PHE A CD1 1 
ATOM   119   C CD2 . PHE A  1  61  ? -35.642 28.315  117.702 1.00 71.00  ?  61   PHE A CD2 1 
ATOM   120   C CE1 . PHE A  1  61  ? -38.338 27.744  117.831 1.00 66.19  ?  61   PHE A CE1 1 
ATOM   121   C CE2 . PHE A  1  61  ? -36.570 29.298  117.418 1.00 70.06  ?  61   PHE A CE2 1 
ATOM   122   C CZ  . PHE A  1  61  ? -37.921 29.013  117.483 1.00 67.48  ?  61   PHE A CZ  1 
ATOM   123   N N   . THR A  1  62  ? -34.525 22.728  118.396 1.00 77.59  ?  62   THR A N   1 
ATOM   124   C CA  . THR A  1  62  ? -33.609 21.601  118.438 1.00 80.63  ?  62   THR A CA  1 
ATOM   125   C C   . THR A  1  62  ? -32.632 21.664  117.268 1.00 81.28  ?  62   THR A C   1 
ATOM   126   O O   . THR A  1  62  ? -32.934 22.233  116.213 1.00 79.11  ?  62   THR A O   1 
ATOM   127   C CB  . THR A  1  62  ? -34.371 20.278  118.401 1.00 82.36  ?  62   THR A CB  1 
ATOM   128   O OG1 . THR A  1  62  ? -34.570 19.899  117.040 1.00 81.77  ?  62   THR A OG1 1 
ATOM   129   C CG2 . THR A  1  62  ? -35.733 20.429  119.069 1.00 80.49  ?  62   THR A CG2 1 
ATOM   130   N N   . ASN A  1  63  ? -31.445 21.086  117.479 1.00 86.75  ?  63   ASN A N   1 
ATOM   131   C CA  . ASN A  1  63  ? -30.408 20.963  116.449 1.00 88.41  ?  63   ASN A CA  1 
ATOM   132   C C   . ASN A  1  63  ? -30.030 22.314  115.842 1.00 85.83  ?  63   ASN A C   1 
ATOM   133   O O   . ASN A  1  63  ? -29.638 22.396  114.675 1.00 86.13  ?  63   ASN A O   1 
ATOM   134   C CB  . ASN A  1  63  ? -30.838 19.987  115.346 1.00 89.21  ?  63   ASN A CB  1 
ATOM   135   C CG  . ASN A  1  63  ? -30.817 18.535  115.803 1.00 93.13  ?  63   ASN A CG  1 
ATOM   136   O OD1 . ASN A  1  63  ? -30.810 18.251  117.001 1.00 94.71  ?  63   ASN A OD1 1 
ATOM   137   N ND2 . ASN A  1  63  ? -30.804 17.609  114.848 1.00 95.00  ?  63   ASN A ND2 1 
ATOM   138   N N   . GLN A  1  64  ? -30.126 23.382  116.631 1.00 84.81  ?  64   GLN A N   1 
ATOM   139   C CA  . GLN A  1  64  ? -29.815 24.725  116.159 1.00 86.80  ?  64   GLN A CA  1 
ATOM   140   C C   . GLN A  1  64  ? -28.327 25.006  116.333 1.00 89.60  ?  64   GLN A C   1 
ATOM   141   O O   . GLN A  1  64  ? -27.770 24.794  117.416 1.00 90.44  ?  64   GLN A O   1 
ATOM   142   C CB  . GLN A  1  64  ? -30.652 25.763  116.910 1.00 86.88  ?  64   GLN A CB  1 
ATOM   143   C CG  . GLN A  1  64  ? -30.979 27.014  116.104 1.00 87.82  ?  64   GLN A CG  1 
ATOM   144   C CD  . GLN A  1  64  ? -31.988 26.749  115.002 1.00 85.53  ?  64   GLN A CD  1 
ATOM   145   O OE1 . GLN A  1  64  ? -33.149 26.443  115.270 1.00 82.97  ?  64   GLN A OE1 1 
ATOM   146   N NE2 . GLN A  1  64  ? -31.549 26.872  113.753 1.00 86.72  ?  64   GLN A NE2 1 
ATOM   147   N N   . THR A  1  65  ? -27.686 25.470  115.262 1.00 87.13  ?  65   THR A N   1 
ATOM   148   C CA  . THR A  1  65  ? -26.266 25.792  115.287 1.00 89.71  ?  65   THR A CA  1 
ATOM   149   C C   . THR A  1  65  ? -26.051 27.256  115.666 1.00 92.32  ?  65   THR A C   1 
ATOM   150   O O   . THR A  1  65  ? -26.958 28.091  115.581 1.00 92.37  ?  65   THR A O   1 
ATOM   151   C CB  . THR A  1  65  ? -25.608 25.503  113.933 1.00 90.21  ?  65   THR A CB  1 
ATOM   152   O OG1 . THR A  1  65  ? -25.699 26.662  113.095 1.00 92.05  ?  65   THR A OG1 1 
ATOM   153   C CG2 . THR A  1  65  ? -26.288 24.328  113.240 1.00 87.62  ?  65   THR A CG2 1 
ATOM   154   N N   . SER A  1  66  ? -24.821 27.558  116.093 1.00 86.94  ?  66   SER A N   1 
ATOM   155   C CA  . SER A  1  66  ? -24.468 28.914  116.499 1.00 89.68  ?  66   SER A CA  1 
ATOM   156   C C   . SER A  1  66  ? -24.438 29.889  115.331 1.00 91.39  ?  66   SER A C   1 
ATOM   157   O O   . SER A  1  66  ? -24.400 31.104  115.560 1.00 93.66  ?  66   SER A O   1 
ATOM   158   C CB  . SER A  1  66  ? -23.112 28.910  117.207 1.00 91.35  ?  66   SER A CB  1 
ATOM   159   O OG  . SER A  1  66  ? -22.118 28.297  116.404 1.00 91.26  ?  66   SER A OG  1 
ATOM   160   N N   . SER A  1  67  ? -24.458 29.391  114.097 1.00 87.33  ?  67   SER A N   1 
ATOM   161   C CA  . SER A  1  67  ? -24.490 30.225  112.905 1.00 89.02  ?  67   SER A CA  1 
ATOM   162   C C   . SER A  1  67  ? -25.909 30.564  112.474 1.00 88.22  ?  67   SER A C   1 
ATOM   163   O O   . SER A  1  67  ? -26.095 31.139  111.397 1.00 89.58  ?  67   SER A O   1 
ATOM   164   C CB  . SER A  1  67  ? -23.743 29.537  111.757 1.00 88.71  ?  67   SER A CB  1 
ATOM   165   O OG  . SER A  1  67  ? -24.378 28.328  111.373 1.00 85.99  ?  67   SER A OG  1 
ATOM   166   N N   . SER A  1  68  ? -26.909 30.209  113.277 1.00 82.46  ?  68   SER A N   1 
ATOM   167   C CA  . SER A  1  68  ? -28.288 30.530  112.942 1.00 81.14  ?  68   SER A CA  1 
ATOM   168   C C   . SER A  1  68  ? -28.509 32.039  112.941 1.00 83.98  ?  68   SER A C   1 
ATOM   169   O O   . SER A  1  68  ? -27.828 32.792  113.643 1.00 86.36  ?  68   SER A O   1 
ATOM   170   C CB  . SER A  1  68  ? -29.246 29.864  113.931 1.00 77.75  ?  68   SER A CB  1 
ATOM   171   O OG  . SER A  1  68  ? -30.580 30.303  113.725 1.00 76.09  ?  68   SER A OG  1 
ATOM   172   N N   . LYS A  1  69  ? -29.479 32.478  112.135 1.00 73.90  ?  69   LYS A N   1 
ATOM   173   C CA  . LYS A  1  69  ? -29.792 33.899  112.055 1.00 76.78  ?  69   LYS A CA  1 
ATOM   174   C C   . LYS A  1  69  ? -30.289 34.449  113.381 1.00 76.05  ?  69   LYS A C   1 
ATOM   175   O O   . LYS A  1  69  ? -30.157 35.651  113.633 1.00 79.16  ?  69   LYS A O   1 
ATOM   176   C CB  . LYS A  1  69  ? -30.838 34.153  110.969 1.00 76.50  ?  69   LYS A CB  1 
ATOM   177   C CG  . LYS A  1  69  ? -30.311 33.996  109.557 1.00 78.58  ?  69   LYS A CG  1 
ATOM   178   C CD  . LYS A  1  69  ? -29.266 35.055  109.235 1.00 83.01  ?  69   LYS A CD  1 
ATOM   179   C CE  . LYS A  1  69  ? -29.232 35.362  107.747 1.00 84.73  ?  69   LYS A CE  1 
ATOM   180   N NZ  . LYS A  1  69  ? -29.915 34.302  106.950 1.00 82.45  ?  69   LYS A NZ  1 
ATOM   181   N N   . LEU A  1  70  ? -30.851 33.596  114.232 1.00 75.57  ?  70   LEU A N   1 
ATOM   182   C CA  . LEU A  1  70  ? -31.464 34.032  115.477 1.00 74.41  ?  70   LEU A CA  1 
ATOM   183   C C   . LEU A  1  70  ? -30.442 34.312  116.570 1.00 77.14  ?  70   LEU A C   1 
ATOM   184   O O   . LEU A  1  70  ? -30.828 34.490  117.732 1.00 76.56  ?  70   LEU A O   1 
ATOM   185   C CB  . LEU A  1  70  ? -32.484 32.990  115.950 1.00 69.57  ?  70   LEU A CB  1 
ATOM   186   C CG  . LEU A  1  70  ? -33.891 33.002  115.328 1.00 66.03  ?  70   LEU A CG  1 
ATOM   187   C CD1 . LEU A  1  70  ? -33.875 33.128  113.818 1.00 66.92  ?  70   LEU A CD1 1 
ATOM   188   C CD2 . LEU A  1  70  ? -34.684 31.771  115.735 1.00 61.97  ?  70   LEU A CD2 1 
ATOM   189   N N   . SER A  1  71  ? -29.152 34.350  116.220 1.00 74.28  ?  71   SER A N   1 
ATOM   190   C CA  . SER A  1  71  ? -28.124 34.806  117.147 1.00 77.02  ?  71   SER A CA  1 
ATOM   191   C C   . SER A  1  71  ? -28.336 36.252  117.569 1.00 79.96  ?  71   SER A C   1 
ATOM   192   O O   . SER A  1  71  ? -27.802 36.671  118.603 1.00 81.73  ?  71   SER A O   1 
ATOM   193   C CB  . SER A  1  71  ? -26.747 34.665  116.508 1.00 78.91  ?  71   SER A CB  1 
ATOM   194   O OG  . SER A  1  71  ? -26.634 33.426  115.839 1.00 76.47  ?  71   SER A OG  1 
ATOM   195   N N   . SER A  1  72  ? -29.087 37.026  116.782 1.00 72.89  ?  72   SER A N   1 
ATOM   196   C CA  . SER A  1  72  ? -29.336 38.429  117.084 1.00 75.94  ?  72   SER A CA  1 
ATOM   197   C C   . SER A  1  72  ? -30.305 38.631  118.241 1.00 73.97  ?  72   SER A C   1 
ATOM   198   O O   . SER A  1  72  ? -30.423 39.761  118.728 1.00 76.56  ?  72   SER A O   1 
ATOM   199   C CB  . SER A  1  72  ? -29.872 39.142  115.839 1.00 77.43  ?  72   SER A CB  1 
ATOM   200   O OG  . SER A  1  72  ? -30.846 38.352  115.179 1.00 73.29  ?  72   SER A OG  1 
ATOM   201   N N   . TRP A  1  73  ? -30.989 37.578  118.693 1.00 77.34  ?  73   TRP A N   1 
ATOM   202   C CA  . TRP A  1  73  ? -31.986 37.688  119.758 1.00 75.27  ?  73   TRP A CA  1 
ATOM   203   C C   . TRP A  1  73  ? -31.261 37.652  121.097 1.00 77.90  ?  73   TRP A C   1 
ATOM   204   O O   . TRP A  1  73  ? -31.108 36.597  121.716 1.00 76.45  ?  73   TRP A O   1 
ATOM   205   C CB  . TRP A  1  73  ? -33.010 36.560  119.661 1.00 70.10  ?  73   TRP A CB  1 
ATOM   206   C CG  . TRP A  1  73  ? -33.909 36.622  118.460 1.00 66.90  ?  73   TRP A CG  1 
ATOM   207   C CD1 . TRP A  1  73  ? -33.679 37.291  117.294 1.00 68.47  ?  73   TRP A CD1 1 
ATOM   208   C CD2 . TRP A  1  73  ? -35.179 35.974  118.304 1.00 62.02  ?  73   TRP A CD2 1 
ATOM   209   N NE1 . TRP A  1  73  ? -34.727 37.106  116.424 1.00 64.51  ?  73   TRP A NE1 1 
ATOM   210   C CE2 . TRP A  1  73  ? -35.661 36.301  117.021 1.00 60.29  ?  73   TRP A CE2 1 
ATOM   211   C CE3 . TRP A  1  73  ? -35.957 35.152  119.125 1.00 59.56  ?  73   TRP A CE3 1 
ATOM   212   C CZ2 . TRP A  1  73  ? -36.884 35.836  116.540 1.00 55.65  ?  73   TRP A CZ2 1 
ATOM   213   C CZ3 . TRP A  1  73  ? -37.175 34.692  118.646 1.00 55.50  ?  73   TRP A CZ3 1 
ATOM   214   C CH2 . TRP A  1  73  ? -37.625 35.036  117.367 1.00 53.35  ?  73   TRP A CH2 1 
ATOM   215   N N   . VAL A  1  74  ? -30.809 38.818  121.562 1.00 75.31  ?  74   VAL A N   1 
ATOM   216   C CA  . VAL A  1  74  ? -30.023 38.867  122.792 1.00 77.87  ?  74   VAL A CA  1 
ATOM   217   C C   . VAL A  1  74  ? -30.674 39.758  123.845 1.00 79.79  ?  74   VAL A C   1 
ATOM   218   O O   . VAL A  1  74  ? -31.040 39.291  124.931 1.00 79.42  ?  74   VAL A O   1 
ATOM   219   C CB  . VAL A  1  74  ? -28.588 39.343  122.497 1.00 80.88  ?  74   VAL A CB  1 
ATOM   220   C CG1 . VAL A  1  74  ? -27.653 38.952  123.627 1.00 81.62  ?  74   VAL A CG1 1 
ATOM   221   C CG2 . VAL A  1  74  ? -28.097 38.776  121.180 1.00 79.73  ?  74   VAL A CG2 1 
ATOM   222   N N   . ASN A  1  75  ? -30.842 41.040  123.534 1.00 81.68  ?  75   ASN A N   1 
ATOM   223   C CA  . ASN A  1  75  ? -31.284 42.001  124.536 1.00 84.19  ?  75   ASN A CA  1 
ATOM   224   C C   . ASN A  1  75  ? -32.795 42.177  124.453 1.00 81.65  ?  75   ASN A C   1 
ATOM   225   O O   . ASN A  1  75  ? -33.305 42.549  123.388 1.00 78.46  ?  75   ASN A O   1 
ATOM   226   C CB  . ASN A  1  75  ? -30.576 43.334  124.338 1.00 86.68  ?  75   ASN A CB  1 
ATOM   227   C CG  . ASN A  1  75  ? -31.147 44.447  125.206 1.00 86.99  ?  75   ASN A CG  1 
ATOM   228   O OD1 . ASN A  1  75  ? -31.694 44.203  126.282 1.00 87.19  ?  75   ASN A OD1 1 
ATOM   229   N ND2 . ASN A  1  75  ? -31.021 45.684  124.731 1.00 85.75  ?  75   ASN A ND2 1 
ATOM   230   N N   . PRO A  1  76  ? -33.542 41.930  125.532 1.00 82.61  ?  76   PRO A N   1 
ATOM   231   C CA  . PRO A  1  76  ? -35.001 42.086  125.482 1.00 79.76  ?  76   PRO A CA  1 
ATOM   232   C C   . PRO A  1  76  ? -35.480 43.530  125.503 1.00 79.61  ?  76   PRO A C   1 
ATOM   233   O O   . PRO A  1  76  ? -36.689 43.764  125.392 1.00 76.52  ?  76   PRO A O   1 
ATOM   234   C CB  . PRO A  1  76  ? -35.459 41.342  126.745 1.00 81.92  ?  76   PRO A CB  1 
ATOM   235   C CG  . PRO A  1  76  ? -34.316 41.510  127.691 1.00 85.19  ?  76   PRO A CG  1 
ATOM   236   C CD  . PRO A  1  76  ? -33.085 41.410  126.833 1.00 84.46  ?  76   PRO A CD  1 
ATOM   237   N N   . ASN A  1  77  ? -34.577 44.498  125.636 1.00 85.46  ?  77   ASN A N   1 
ATOM   238   C CA  . ASN A  1  77  ? -34.971 45.899  125.655 1.00 83.29  ?  77   ASN A CA  1 
ATOM   239   C C   . ASN A  1  77  ? -35.378 46.368  124.261 1.00 78.61  ?  77   ASN A C   1 
ATOM   240   O O   . ASN A  1  77  ? -34.867 45.890  123.244 1.00 78.03  ?  77   ASN A O   1 
ATOM   241   C CB  . ASN A  1  77  ? -33.832 46.763  126.194 1.00 85.59  ?  77   ASN A CB  1 
ATOM   242   C CG  . ASN A  1  77  ? -33.654 46.609  127.688 1.00 88.19  ?  77   ASN A CG  1 
ATOM   243   O OD1 . ASN A  1  77  ? -34.539 46.097  128.377 1.00 88.65  ?  77   ASN A OD1 1 
ATOM   244   N ND2 . ASN A  1  77  ? -32.508 47.048  128.199 1.00 89.31  ?  77   ASN A ND2 1 
ATOM   245   N N   . THR A  1  78  ? -36.311 47.326  124.230 1.00 82.54  ?  78   THR A N   1 
ATOM   246   C CA  . THR A  1  78  ? -36.852 47.821  122.965 1.00 78.06  ?  78   THR A CA  1 
ATOM   247   C C   . THR A  1  78  ? -35.774 48.440  122.083 1.00 78.79  ?  78   THR A C   1 
ATOM   248   O O   . THR A  1  78  ? -35.931 48.486  120.857 1.00 76.25  ?  78   THR A O   1 
ATOM   249   C CB  . THR A  1  78  ? -37.949 48.852  123.233 1.00 75.39  ?  78   THR A CB  1 
ATOM   250   O OG1 . THR A  1  78  ? -38.789 48.395  124.299 1.00 76.34  ?  78   THR A OG1 1 
ATOM   251   C CG2 . THR A  1  78  ? -38.794 49.076  121.987 1.00 70.63  ?  78   THR A CG2 1 
ATOM   252   N N   . SER A  1  79  ? -34.682 48.925  122.681 1.00 75.45  ?  79   SER A N   1 
ATOM   253   C CA  . SER A  1  79  ? -33.622 49.556  121.902 1.00 76.51  ?  79   SER A CA  1 
ATOM   254   C C   . SER A  1  79  ? -32.920 48.583  120.964 1.00 77.98  ?  79   SER A C   1 
ATOM   255   O O   . SER A  1  79  ? -32.216 49.021  120.055 1.00 78.38  ?  79   SER A O   1 
ATOM   256   C CB  . SER A  1  79  ? -32.597 50.203  122.833 1.00 79.39  ?  79   SER A CB  1 
ATOM   257   O OG  . SER A  1  79  ? -32.135 49.274  123.798 1.00 82.42  ?  79   SER A OG  1 
ATOM   258   N N   . SER A  1  80  ? -33.085 47.279  121.150 1.00 75.67  ?  80   SER A N   1 
ATOM   259   C CA  . SER A  1  80  ? -32.488 46.340  120.211 1.00 77.06  ?  80   SER A CA  1 
ATOM   260   C C   . SER A  1  80  ? -33.536 45.367  119.689 1.00 73.47  ?  80   SER A C   1 
ATOM   261   O O   . SER A  1  80  ? -33.422 44.875  118.562 1.00 72.82  ?  80   SER A O   1 
ATOM   262   C CB  . SER A  1  80  ? -31.330 45.591  120.866 1.00 81.95  ?  80   SER A CB  1 
ATOM   263   O OG  . SER A  1  80  ? -31.715 45.122  122.139 1.00 82.91  ?  80   SER A OG  1 
ATOM   264   N N   . PHE A  1  81  ? -34.560 45.092  120.503 1.00 79.35  ?  81   PHE A N   1 
ATOM   265   C CA  . PHE A  1  81  ? -35.628 44.189  120.083 1.00 74.79  ?  81   PHE A CA  1 
ATOM   266   C C   . PHE A  1  81  ? -36.285 44.675  118.799 1.00 70.71  ?  81   PHE A C   1 
ATOM   267   O O   . PHE A  1  81  ? -36.491 43.899  117.860 1.00 68.55  ?  81   PHE A O   1 
ATOM   268   C CB  . PHE A  1  81  ? -36.670 44.056  121.191 1.00 73.46  ?  81   PHE A CB  1 
ATOM   269   C CG  . PHE A  1  81  ? -37.881 43.255  120.793 1.00 68.72  ?  81   PHE A CG  1 
ATOM   270   C CD1 . PHE A  1  81  ? -37.762 41.920  120.445 1.00 67.42  ?  81   PHE A CD1 1 
ATOM   271   C CD2 . PHE A  1  81  ? -39.141 43.833  120.780 1.00 65.69  ?  81   PHE A CD2 1 
ATOM   272   C CE1 . PHE A  1  81  ? -38.876 41.175  120.089 1.00 63.19  ?  81   PHE A CE1 1 
ATOM   273   C CE2 . PHE A  1  81  ? -40.259 43.093  120.423 1.00 62.02  ?  81   PHE A CE2 1 
ATOM   274   C CZ  . PHE A  1  81  ? -40.124 41.764  120.078 1.00 60.77  ?  81   PHE A CZ  1 
ATOM   275   N N   . CYS A  1  82  ? -36.612 45.959  118.733 1.00 73.02  ?  82   CYS A N   1 
ATOM   276   C CA  . CYS A  1  82  ? -37.351 46.496  117.601 1.00 69.13  ?  82   CYS A CA  1 
ATOM   277   C C   . CYS A  1  82  ? -36.463 46.974  116.461 1.00 70.95  ?  82   CYS A C   1 
ATOM   278   O O   . CYS A  1  82  ? -36.991 47.490  115.471 1.00 68.09  ?  82   CYS A O   1 
ATOM   279   C CB  . CYS A  1  82  ? -38.249 47.643  118.063 1.00 66.87  ?  82   CYS A CB  1 
ATOM   280   S SG  . CYS A  1  82  ? -39.709 47.075  118.953 1.00 64.25  ?  82   CYS A SG  1 
ATOM   281   N N   . THR A  1  83  ? -35.137 46.851  116.580 1.00 66.45  ?  83   THR A N   1 
ATOM   282   C CA  . THR A  1  83  ? -34.269 47.294  115.489 1.00 68.31  ?  83   THR A CA  1 
ATOM   283   C C   . THR A  1  83  ? -33.297 46.230  114.998 1.00 72.17  ?  83   THR A C   1 
ATOM   284   O O   . THR A  1  83  ? -33.023 46.170  113.797 1.00 72.39  ?  83   THR A O   1 
ATOM   285   C CB  . THR A  1  83  ? -33.472 48.547  115.913 1.00 70.09  ?  83   THR A CB  1 
ATOM   286   O OG1 . THR A  1  83  ? -32.251 48.153  116.553 1.00 74.63  ?  83   THR A OG1 1 
ATOM   287   C CG2 . THR A  1  83  ? -34.280 49.398  116.868 1.00 67.76  ?  83   THR A CG2 1 
ATOM   288   N N   . SER A  1  84  ? -32.769 45.388  115.889 1.00 65.12  ?  84   SER A N   1 
ATOM   289   C CA  . SER A  1  84  ? -31.679 44.491  115.534 1.00 69.60  ?  84   SER A CA  1 
ATOM   290   C C   . SER A  1  84  ? -32.031 43.011  115.598 1.00 69.58  ?  84   SER A C   1 
ATOM   291   O O   . SER A  1  84  ? -31.229 42.190  115.136 1.00 73.14  ?  84   SER A O   1 
ATOM   292   C CB  . SER A  1  84  ? -30.456 44.752  116.429 1.00 73.50  ?  84   SER A CB  1 
ATOM   293   O OG  . SER A  1  84  ? -30.672 44.294  117.748 1.00 74.47  ?  84   SER A OG  1 
ATOM   294   N N   . TRP A  1  85  ? -33.180 42.640  116.162 1.00 73.27  ?  85   TRP A N   1 
ATOM   295   C CA  . TRP A  1  85  ? -33.580 41.238  116.173 1.00 70.45  ?  85   TRP A CA  1 
ATOM   296   C C   . TRP A  1  85  ? -34.021 40.813  114.778 1.00 68.42  ?  85   TRP A C   1 
ATOM   297   O O   . TRP A  1  85  ? -34.906 41.434  114.181 1.00 64.98  ?  85   TRP A O   1 
ATOM   298   C CB  . TRP A  1  85  ? -34.711 41.008  117.176 1.00 65.32  ?  85   TRP A CB  1 
ATOM   299   C CG  . TRP A  1  85  ? -34.266 40.950  118.605 1.00 67.84  ?  85   TRP A CG  1 
ATOM   300   C CD1 . TRP A  1  85  ? -33.246 41.651  119.175 1.00 73.25  ?  85   TRP A CD1 1 
ATOM   301   C CD2 . TRP A  1  85  ? -34.835 40.149  119.651 1.00 65.61  ?  85   TRP A CD2 1 
ATOM   302   N NE1 . TRP A  1  85  ? -33.140 41.336  120.509 1.00 74.39  ?  85   TRP A NE1 1 
ATOM   303   C CE2 . TRP A  1  85  ? -34.104 40.416  120.825 1.00 69.99  ?  85   TRP A CE2 1 
ATOM   304   C CE3 . TRP A  1  85  ? -35.887 39.230  119.706 1.00 60.99  ?  85   TRP A CE3 1 
ATOM   305   C CZ2 . TRP A  1  85  ? -34.392 39.798  122.039 1.00 70.08  ?  85   TRP A CZ2 1 
ATOM   306   C CZ3 . TRP A  1  85  ? -36.172 38.622  120.913 1.00 61.36  ?  85   TRP A CZ3 1 
ATOM   307   C CH2 . TRP A  1  85  ? -35.427 38.908  122.061 1.00 65.96  ?  85   TRP A CH2 1 
ATOM   308   N N   . TYR A  1  86  ? -33.402 39.756  114.257 1.00 69.29  ?  86   TYR A N   1 
ATOM   309   C CA  . TYR A  1  86  ? -33.731 39.291  112.915 1.00 68.55  ?  86   TYR A CA  1 
ATOM   310   C C   . TYR A  1  86  ? -35.180 38.825  112.847 1.00 61.15  ?  86   TYR A C   1 
ATOM   311   O O   . TYR A  1  86  ? -35.636 38.037  113.682 1.00 57.17  ?  86   TYR A O   1 
ATOM   312   C CB  . TYR A  1  86  ? -32.789 38.161  112.497 1.00 70.89  ?  86   TYR A CB  1 
ATOM   313   C CG  . TYR A  1  86  ? -33.079 37.576  111.128 1.00 70.67  ?  86   TYR A CG  1 
ATOM   314   C CD1 . TYR A  1  86  ? -32.550 38.148  109.979 1.00 76.23  ?  86   TYR A CD1 1 
ATOM   315   C CD2 . TYR A  1  86  ? -33.871 36.443  110.988 1.00 65.20  ?  86   TYR A CD2 1 
ATOM   316   C CE1 . TYR A  1  86  ? -32.808 37.613  108.725 1.00 76.42  ?  86   TYR A CE1 1 
ATOM   317   C CE2 . TYR A  1  86  ? -34.136 35.902  109.741 1.00 65.34  ?  86   TYR A CE2 1 
ATOM   318   C CZ  . TYR A  1  86  ? -33.601 36.491  108.612 1.00 71.09  ?  86   TYR A CZ  1 
ATOM   319   O OH  . TYR A  1  86  ? -33.861 35.957  107.369 1.00 71.54  ?  86   TYR A OH  1 
ATOM   320   N N   . GLY A  1  87  ? -35.908 39.333  111.858 1.00 66.59  ?  87   GLY A N   1 
ATOM   321   C CA  . GLY A  1  87  ? -37.238 38.855  111.556 1.00 60.28  ?  87   GLY A CA  1 
ATOM   322   C C   . GLY A  1  87  ? -38.372 39.557  112.268 1.00 55.25  ?  87   GLY A C   1 
ATOM   323   O O   . GLY A  1  87  ? -39.536 39.233  112.006 1.00 50.57  ?  87   GLY A O   1 
ATOM   324   N N   . VAL A  1  88  ? -38.086 40.497  113.160 1.00 59.06  ?  88   VAL A N   1 
ATOM   325   C CA  . VAL A  1  88  ? -39.141 41.196  113.881 1.00 55.48  ?  88   VAL A CA  1 
ATOM   326   C C   . VAL A  1  88  ? -39.186 42.650  113.427 1.00 56.23  ?  88   VAL A C   1 
ATOM   327   O O   . VAL A  1  88  ? -38.165 43.252  113.074 1.00 60.29  ?  88   VAL A O   1 
ATOM   328   C CB  . VAL A  1  88  ? -38.969 41.095  115.414 1.00 56.62  ?  88   VAL A CB  1 
ATOM   329   C CG1 . VAL A  1  88  ? -38.593 39.680  115.817 1.00 56.91  ?  88   VAL A CG1 1 
ATOM   330   C CG2 . VAL A  1  88  ? -37.934 42.064  115.901 1.00 61.29  ?  88   VAL A CG2 1 
ATOM   331   N N   . ALA A  1  89  ? -40.396 43.205  113.417 1.00 58.09  ?  89   ALA A N   1 
ATOM   332   C CA  . ALA A  1  89  ? -40.625 44.608  113.104 1.00 57.78  ?  89   ALA A CA  1 
ATOM   333   C C   . ALA A  1  89  ? -41.714 45.138  114.023 1.00 55.29  ?  89   ALA A C   1 
ATOM   334   O O   . ALA A  1  89  ? -42.688 44.437  114.307 1.00 52.93  ?  89   ALA A O   1 
ATOM   335   C CB  . ALA A  1  89  ? -41.028 44.807  111.640 1.00 56.16  ?  89   ALA A CB  1 
ATOM   336   N N   . CYS A  1  90  ? -41.553 46.372  114.484 1.00 54.65  ?  90   CYS A N   1 
ATOM   337   C CA  . CYS A  1  90  ? -42.446 46.931  115.483 1.00 53.70  ?  90   CYS A CA  1 
ATOM   338   C C   . CYS A  1  90  ? -43.206 48.137  114.947 1.00 51.62  ?  90   CYS A C   1 
ATOM   339   O O   . CYS A  1  90  ? -42.754 48.827  114.025 1.00 51.67  ?  90   CYS A O   1 
ATOM   340   C CB  . CYS A  1  90  ? -41.677 47.353  116.729 1.00 57.22  ?  90   CYS A CB  1 
ATOM   341   S SG  . CYS A  1  90  ? -40.776 46.042  117.557 1.00 60.42  ?  90   CYS A SG  1 
ATOM   342   N N   . SER A  1  91  ? -44.370 48.383  115.548 1.00 49.78  ?  91   SER A N   1 
ATOM   343   C CA  . SER A  1  91  ? -45.084 49.646  115.422 1.00 50.28  ?  91   SER A CA  1 
ATOM   344   C C   . SER A  1  91  ? -45.374 50.150  116.825 1.00 51.07  ?  91   SER A C   1 
ATOM   345   O O   . SER A  1  91  ? -45.872 49.394  117.664 1.00 51.34  ?  91   SER A O   1 
ATOM   346   C CB  . SER A  1  91  ? -46.384 49.497  114.625 1.00 50.38  ?  91   SER A CB  1 
ATOM   347   O OG  . SER A  1  91  ? -47.067 50.739  114.537 1.00 52.57  ?  91   SER A OG  1 
ATOM   348   N N   . LEU A  1  92  ? -45.029 51.411  117.084 1.00 52.43  ?  92   LEU A N   1 
ATOM   349   C CA  . LEU A  1  92  ? -45.210 52.021  118.404 1.00 53.57  ?  92   LEU A CA  1 
ATOM   350   C C   . LEU A  1  92  ? -44.611 51.147  119.505 1.00 52.22  ?  92   LEU A C   1 
ATOM   351   O O   . LEU A  1  92  ? -45.149 51.034  120.607 1.00 52.54  ?  92   LEU A O   1 
ATOM   352   C CB  . LEU A  1  92  ? -46.686 52.318  118.673 1.00 54.69  ?  92   LEU A CB  1 
ATOM   353   C CG  . LEU A  1  92  ? -47.369 53.196  117.628 1.00 56.47  ?  92   LEU A CG  1 
ATOM   354   C CD1 . LEU A  1  92  ? -48.798 53.476  118.026 1.00 57.90  ?  92   LEU A CD1 1 
ATOM   355   C CD2 . LEU A  1  92  ? -46.612 54.494  117.437 1.00 58.57  ?  92   LEU A CD2 1 
ATOM   356   N N   . GLY A  1  93  ? -43.480 50.522  119.201 1.00 52.61  ?  93   GLY A N   1 
ATOM   357   C CA  . GLY A  1  93  ? -42.791 49.676  120.160 1.00 55.86  ?  93   GLY A CA  1 
ATOM   358   C C   . GLY A  1  93  ? -43.495 48.385  120.514 1.00 55.78  ?  93   GLY A C   1 
ATOM   359   O O   . GLY A  1  93  ? -43.487 47.985  121.678 1.00 58.89  ?  93   GLY A O   1 
ATOM   360   N N   . SER A  1  94  ? -44.114 47.724  119.543 1.00 58.89  ?  94   SER A N   1 
ATOM   361   C CA  . SER A  1  94  ? -44.705 46.416  119.786 1.00 58.92  ?  94   SER A CA  1 
ATOM   362   C C   . SER A  1  94  ? -44.574 45.602  118.512 1.00 55.96  ?  94   SER A C   1 
ATOM   363   O O   . SER A  1  94  ? -44.784 46.129  117.416 1.00 53.29  ?  94   SER A O   1 
ATOM   364   C CB  . SER A  1  94  ? -46.179 46.514  120.199 1.00 58.47  ?  94   SER A CB  1 
ATOM   365   O OG  . SER A  1  94  ? -46.821 45.250  120.117 1.00 58.27  ?  94   SER A OG  1 
ATOM   366   N N   . ILE A  1  95  ? -44.235 44.322  118.656 1.00 58.25  ?  95   ILE A N   1 
ATOM   367   C CA  . ILE A  1  95  ? -43.994 43.498  117.478 1.00 55.65  ?  95   ILE A CA  1 
ATOM   368   C C   . ILE A  1  95  ? -45.296 43.358  116.698 1.00 52.34  ?  95   ILE A C   1 
ATOM   369   O O   . ILE A  1  95  ? -46.324 42.927  117.230 1.00 52.56  ?  95   ILE A O   1 
ATOM   370   C CB  . ILE A  1  95  ? -43.396 42.133  117.860 1.00 56.82  ?  95   ILE A CB  1 
ATOM   371   C CG1 . ILE A  1  95  ? -43.118 41.299  116.604 1.00 54.11  ?  95   ILE A CG1 1 
ATOM   372   C CG2 . ILE A  1  95  ? -44.284 41.369  118.850 1.00 58.00  ?  95   ILE A CG2 1 
ATOM   373   C CD1 . ILE A  1  95  ? -42.321 40.036  116.868 1.00 55.07  ?  95   ILE A CD1 1 
ATOM   374   N N   . ILE A  1  96  ? -45.265 43.763  115.433 1.00 55.29  ?  96   ILE A N   1 
ATOM   375   C CA  . ILE A  1  96  ? -46.401 43.606  114.535 1.00 52.48  ?  96   ILE A CA  1 
ATOM   376   C C   . ILE A  1  96  ? -46.102 42.659  113.388 1.00 51.03  ?  96   ILE A C   1 
ATOM   377   O O   . ILE A  1  96  ? -47.033 42.276  112.662 1.00 49.04  ?  96   ILE A O   1 
ATOM   378   C CB  . ILE A  1  96  ? -46.870 44.969  113.983 1.00 51.43  ?  96   ILE A CB  1 
ATOM   379   C CG1 . ILE A  1  96  ? -45.804 45.558  113.059 1.00 51.88  ?  96   ILE A CG1 1 
ATOM   380   C CG2 . ILE A  1  96  ? -47.135 45.929  115.111 1.00 52.97  ?  96   ILE A CG2 1 
ATOM   381   C CD1 . ILE A  1  96  ? -46.298 46.702  112.209 1.00 50.62  ?  96   ILE A CD1 1 
ATOM   382   N N   . ARG A  1  97  ? -44.847 42.243  113.226 1.00 55.73  ?  97   ARG A N   1 
ATOM   383   C CA  . ARG A  1  97  ? -44.374 41.546  112.037 1.00 55.38  ?  97   ARG A CA  1 
ATOM   384   C C   . ARG A  1  97  ? -43.341 40.515  112.465 1.00 56.98  ?  97   ARG A C   1 
ATOM   385   O O   . ARG A  1  97  ? -42.365 40.858  113.137 1.00 59.81  ?  97   ARG A O   1 
ATOM   386   C CB  . ARG A  1  97  ? -43.767 42.544  111.049 1.00 57.04  ?  97   ARG A CB  1 
ATOM   387   C CG  . ARG A  1  97  ? -43.994 42.217  109.596 1.00 56.71  ?  97   ARG A CG  1 
ATOM   388   C CD  . ARG A  1  97  ? -43.622 43.383  108.688 1.00 58.28  ?  97   ARG A CD  1 
ATOM   389   N NE  . ARG A  1  97  ? -44.801 44.049  108.144 1.00 55.60  ?  97   ARG A NE  1 
ATOM   390   C CZ  . ARG A  1  97  ? -44.762 45.095  107.329 1.00 55.97  ?  97   ARG A CZ  1 
ATOM   391   N NH1 . ARG A  1  97  ? -43.613 45.620  106.931 1.00 58.85  ?  97   ARG A NH1 1 
ATOM   392   N NH2 . ARG A  1  97  ? -45.904 45.634  106.906 1.00 53.66  ?  97   ARG A NH2 1 
ATOM   393   N N   . LEU A  1  98  ? -43.563 39.255  112.093 1.00 52.65  ?  98   LEU A N   1 
ATOM   394   C CA  . LEU A  1  98  ? -42.648 38.163  112.412 1.00 54.10  ?  98   LEU A CA  1 
ATOM   395   C C   . LEU A  1  98  ? -42.387 37.381  111.134 1.00 54.46  ?  98   LEU A C   1 
ATOM   396   O O   . LEU A  1  98  ? -43.283 36.702  110.620 1.00 51.86  ?  98   LEU A O   1 
ATOM   397   C CB  . LEU A  1  98  ? -43.210 37.252  113.502 1.00 52.68  ?  98   LEU A CB  1 
ATOM   398   C CG  . LEU A  1  98  ? -42.273 36.110  113.909 1.00 54.24  ?  98   LEU A CG  1 
ATOM   399   C CD1 . LEU A  1  98  ? -41.021 36.662  114.572 1.00 58.06  ?  98   LEU A CD1 1 
ATOM   400   C CD2 . LEU A  1  98  ? -42.966 35.107  114.825 1.00 53.18  ?  98   LEU A CD2 1 
ATOM   401   N N   . ASN A  1  99  ? -41.161 37.475  110.630 1.00 52.63  ?  99   ASN A N   1 
ATOM   402   C CA  . ASN A  1  99  ? -40.780 36.923  109.335 1.00 54.31  ?  99   ASN A CA  1 
ATOM   403   C C   . ASN A  1  99  ? -39.583 36.004  109.554 1.00 57.87  ?  99   ASN A C   1 
ATOM   404   O O   . ASN A  1  99  ? -38.459 36.479  109.734 1.00 62.65  ?  99   ASN A O   1 
ATOM   405   C CB  . ASN A  1  99  ? -40.454 38.049  108.365 1.00 57.81  ?  99   ASN A CB  1 
ATOM   406   C CG  . ASN A  1  99  ? -40.300 37.573  106.950 1.00 61.02  ?  99   ASN A CG  1 
ATOM   407   O OD1 . ASN A  1  99  ? -40.444 36.387  106.663 1.00 60.57  ?  99   ASN A OD1 1 
ATOM   408   N ND2 . ASN A  1  99  ? -40.000 38.503  106.048 1.00 64.35  ?  99   ASN A ND2 1 
ATOM   409   N N   . LEU A  1  100 ? -39.820 34.694  109.551 1.00 54.55  ?  100  LEU A N   1 
ATOM   410   C CA  . LEU A  1  100 ? -38.765 33.711  109.767 1.00 57.07  ?  100  LEU A CA  1 
ATOM   411   C C   . LEU A  1  100 ? -38.783 32.657  108.671 1.00 57.66  ?  100  LEU A C   1 
ATOM   412   O O   . LEU A  1  100 ? -38.528 31.472  108.912 1.00 56.67  ?  100  LEU A O   1 
ATOM   413   C CB  . LEU A  1  100 ? -38.894 33.064  111.142 1.00 54.20  ?  100  LEU A CB  1 
ATOM   414   C CG  . LEU A  1  100 ? -38.599 33.977  112.331 1.00 55.11  ?  100  LEU A CG  1 
ATOM   415   C CD1 . LEU A  1  100 ? -38.686 33.209  113.638 1.00 53.72  ?  100  LEU A CD1 1 
ATOM   416   C CD2 . LEU A  1  100 ? -37.236 34.619  112.178 1.00 60.69  ?  100  LEU A CD2 1 
ATOM   417   N N   . THR A  1  101 ? -39.087 33.082  107.447 1.00 57.09  ?  101  THR A N   1 
ATOM   418   C CA  . THR A  1  101 ? -39.008 32.197  106.295 1.00 58.96  ?  101  THR A CA  1 
ATOM   419   C C   . THR A  1  101 ? -37.599 31.659  106.131 1.00 63.18  ?  101  THR A C   1 
ATOM   420   O O   . THR A  1  101 ? -36.620 32.401  106.247 1.00 67.47  ?  101  THR A O   1 
ATOM   421   C CB  . THR A  1  101 ? -39.411 32.939  105.024 1.00 62.23  ?  101  THR A CB  1 
ATOM   422   O OG1 . THR A  1  101 ? -40.651 33.614  105.248 1.00 57.61  ?  101  THR A OG1 1 
ATOM   423   C CG2 . THR A  1  101 ? -39.561 31.975  103.861 1.00 63.69  ?  101  THR A CG2 1 
ATOM   424   N N   . ASN A  1  102 ? -37.505 30.354  105.871 1.00 60.22  ?  102  ASN A N   1 
ATOM   425   C CA  . ASN A  1  102 ? -36.272 29.725  105.398 1.00 63.18  ?  102  ASN A CA  1 
ATOM   426   C C   . ASN A  1  102 ? -35.105 29.962  106.355 1.00 64.52  ?  102  ASN A C   1 
ATOM   427   O O   . ASN A  1  102 ? -33.980 30.242  105.935 1.00 68.25  ?  102  ASN A O   1 
ATOM   428   C CB  . ASN A  1  102 ? -35.927 30.213  103.991 1.00 67.94  ?  102  ASN A CB  1 
ATOM   429   C CG  . ASN A  1  102 ? -35.000 29.277  103.267 1.00 68.81  ?  102  ASN A CG  1 
ATOM   430   O OD1 . ASN A  1  102 ? -34.930 28.088  103.576 1.00 65.72  ?  102  ASN A OD1 1 
ATOM   431   N ND2 . ASN A  1  102 ? -34.275 29.807  102.296 1.00 72.67  ?  102  ASN A ND2 1 
ATOM   432   N N   . THR A  1  103 ? -35.374 29.838  107.653 1.00 63.63  ?  103  THR A N   1 
ATOM   433   C CA  . THR A  1  103 ? -34.377 30.076  108.686 1.00 64.88  ?  103  THR A CA  1 
ATOM   434   C C   . THR A  1  103 ? -33.751 28.790  109.214 1.00 63.17  ?  103  THR A C   1 
ATOM   435   O O   . THR A  1  103 ? -32.753 28.854  109.942 1.00 64.59  ?  103  THR A O   1 
ATOM   436   C CB  . THR A  1  103 ? -35.014 30.859  109.841 1.00 63.10  ?  103  THR A CB  1 
ATOM   437   O OG1 . THR A  1  103 ? -35.741 31.970  109.305 1.00 63.93  ?  103  THR A OG1 1 
ATOM   438   C CG2 . THR A  1  103 ? -33.959 31.399  110.782 1.00 65.63  ?  103  THR A CG2 1 
ATOM   439   N N   . GLY A  1  104 ? -34.304 27.631  108.867 1.00 66.95  ?  104  GLY A N   1 
ATOM   440   C CA  . GLY A  1  104 ? -33.762 26.382  109.360 1.00 65.54  ?  104  GLY A CA  1 
ATOM   441   C C   . GLY A  1  104 ? -34.119 26.083  110.797 1.00 63.20  ?  104  GLY A C   1 
ATOM   442   O O   . GLY A  1  104 ? -33.340 25.435  111.501 1.00 63.39  ?  104  GLY A O   1 
ATOM   443   N N   . ILE A  1  105 ? -35.277 26.541  111.253 1.00 68.45  ?  105  ILE A N   1 
ATOM   444   C CA  . ILE A  1  105 ? -35.722 26.302  112.619 1.00 66.57  ?  105  ILE A CA  1 
ATOM   445   C C   . ILE A  1  105 ? -36.368 24.926  112.698 1.00 64.05  ?  105  ILE A C   1 
ATOM   446   O O   . ILE A  1  105 ? -37.159 24.543  111.828 1.00 62.59  ?  105  ILE A O   1 
ATOM   447   C CB  . ILE A  1  105 ? -36.693 27.410  113.067 1.00 65.58  ?  105  ILE A CB  1 
ATOM   448   C CG1 . ILE A  1  105 ? -35.957 28.750  113.159 1.00 68.58  ?  105  ILE A CG1 1 
ATOM   449   C CG2 . ILE A  1  105 ? -37.323 27.063  114.400 1.00 63.95  ?  105  ILE A CG2 1 
ATOM   450   C CD1 . ILE A  1  105 ? -36.861 29.970  113.136 1.00 67.83  ?  105  ILE A CD1 1 
ATOM   451   N N   . GLU A  1  106 ? -36.022 24.168  113.738 1.00 72.94  ?  106  GLU A N   1 
ATOM   452   C CA  . GLU A  1  106 ? -36.604 22.854  113.984 1.00 71.11  ?  106  GLU A CA  1 
ATOM   453   C C   . GLU A  1  106 ? -37.236 22.863  115.369 1.00 70.56  ?  106  GLU A C   1 
ATOM   454   O O   . GLU A  1  106 ? -36.544 23.095  116.366 1.00 72.12  ?  106  GLU A O   1 
ATOM   455   C CB  . GLU A  1  106 ? -35.536 21.765  113.877 1.00 72.75  ?  106  GLU A CB  1 
ATOM   456   C CG  . GLU A  1  106 ? -36.082 20.366  113.681 1.00 74.41  ?  106  GLU A CG  1 
ATOM   457   C CD  . GLU A  1  106 ? -35.163 19.303  114.244 1.00 78.61  ?  106  GLU A CD  1 
ATOM   458   O OE1 . GLU A  1  106 ? -35.196 19.095  115.474 1.00 79.83  ?  106  GLU A OE1 1 
ATOM   459   O OE2 . GLU A  1  106 ? -34.410 18.675  113.467 1.00 80.98  -1 106  GLU A OE2 1 
ATOM   460   N N   . GLY A  1  107 ? -38.540 22.609  115.432 1.00 67.27  ?  107  GLY A N   1 
ATOM   461   C CA  . GLY A  1  107 ? -39.234 22.641  116.708 1.00 67.36  ?  107  GLY A CA  1 
ATOM   462   C C   . GLY A  1  107 ? -40.736 22.546  116.519 1.00 65.83  ?  107  GLY A C   1 
ATOM   463   O O   . GLY A  1  107 ? -41.216 22.015  115.516 1.00 64.53  ?  107  GLY A O   1 
ATOM   464   N N   . THR A  1  108 ? -41.467 23.062  117.510 1.00 64.63  ?  108  THR A N   1 
ATOM   465   C CA  . THR A  1  108 ? -42.924 23.030  117.524 1.00 63.99  ?  108  THR A CA  1 
ATOM   466   C C   . THR A  1  108 ? -43.481 24.399  117.896 1.00 64.73  ?  108  THR A C   1 
ATOM   467   O O   . THR A  1  108 ? -42.775 25.260  118.426 1.00 66.01  ?  108  THR A O   1 
ATOM   468   C CB  . THR A  1  108 ? -43.467 21.992  118.517 1.00 64.95  ?  108  THR A CB  1 
ATOM   469   O OG1 . THR A  1  108 ? -43.378 22.516  119.847 1.00 67.13  ?  108  THR A OG1 1 
ATOM   470   C CG2 . THR A  1  108 ? -42.683 20.694  118.435 1.00 65.93  ?  108  THR A CG2 1 
ATOM   471   N N   . PHE A  1  109 ? -44.767 24.590  117.610 1.00 62.77  ?  109  PHE A N   1 
ATOM   472   C CA  . PHE A  1  109 ? -45.498 25.766  118.061 1.00 63.95  ?  109  PHE A CA  1 
ATOM   473   C C   . PHE A  1  109 ? -46.170 25.552  119.414 1.00 66.91  ?  109  PHE A C   1 
ATOM   474   O O   . PHE A  1  109 ? -47.054 26.331  119.785 1.00 68.76  ?  109  PHE A O   1 
ATOM   475   C CB  . PHE A  1  109 ? -46.557 26.171  117.032 1.00 62.25  ?  109  PHE A CB  1 
ATOM   476   C CG  . PHE A  1  109 ? -46.006 26.461  115.670 1.00 59.59  ?  109  PHE A CG  1 
ATOM   477   C CD1 . PHE A  1  109 ? -44.904 27.285  115.514 1.00 59.53  ?  109  PHE A CD1 1 
ATOM   478   C CD2 . PHE A  1  109 ? -46.602 25.922  114.540 1.00 57.78  ?  109  PHE A CD2 1 
ATOM   479   C CE1 . PHE A  1  109 ? -44.400 27.557  114.255 1.00 58.01  ?  109  PHE A CE1 1 
ATOM   480   C CE2 . PHE A  1  109 ? -46.105 26.189  113.281 1.00 56.07  ?  109  PHE A CE2 1 
ATOM   481   C CZ  . PHE A  1  109 ? -45.003 27.009  113.138 1.00 56.35  ?  109  PHE A CZ  1 
ATOM   482   N N   . GLU A  1  110 ? -45.787 24.505  120.147 1.00 71.00  ?  110  GLU A N   1 
ATOM   483   C CA  . GLU A  1  110 ? -46.450 24.220  121.414 1.00 73.92  ?  110  GLU A CA  1 
ATOM   484   C C   . GLU A  1  110 ? -46.168 25.302  122.447 1.00 76.85  ?  110  GLU A C   1 
ATOM   485   O O   . GLU A  1  110 ? -47.057 25.677  123.218 1.00 79.84  ?  110  GLU A O   1 
ATOM   486   C CB  . GLU A  1  110 ? -46.020 22.854  121.942 1.00 73.74  ?  110  GLU A CB  1 
ATOM   487   C CG  . GLU A  1  110 ? -46.799 22.421  123.167 1.00 76.37  ?  110  GLU A CG  1 
ATOM   488   C CD  . GLU A  1  110 ? -46.606 20.956  123.492 1.00 75.67  ?  110  GLU A CD  1 
ATOM   489   O OE1 . GLU A  1  110 ? -45.516 20.590  123.990 1.00 75.59  ?  110  GLU A OE1 1 
ATOM   490   O OE2 . GLU A  1  110 ? -47.549 20.171  123.252 1.00 75.41  -1 110  GLU A OE2 1 
ATOM   491   N N   . ASP A  1  111 ? -44.937 25.812  122.484 1.00 68.19  ?  111  ASP A N   1 
ATOM   492   C CA  . ASP A  1  111 ? -44.574 26.895  123.388 1.00 71.17  ?  111  ASP A CA  1 
ATOM   493   C C   . ASP A  1  111 ? -44.481 28.236  122.669 1.00 70.67  ?  111  ASP A C   1 
ATOM   494   O O   . ASP A  1  111 ? -43.717 29.115  123.083 1.00 72.33  ?  111  ASP A O   1 
ATOM   495   C CB  . ASP A  1  111 ? -43.263 26.567  124.101 1.00 71.95  ?  111  ASP A CB  1 
ATOM   496   C CG  . ASP A  1  111 ? -43.481 25.748  125.360 1.00 73.99  ?  111  ASP A CG  1 
ATOM   497   O OD1 . ASP A  1  111 ? -44.589 25.822  125.930 1.00 75.89  ?  111  ASP A OD1 1 
ATOM   498   O OD2 . ASP A  1  111 ? -42.554 25.021  125.774 1.00 73.78  -1 111  ASP A OD2 1 
ATOM   499   N N   . PHE A  1  112 ? -45.243 28.404  121.595 1.00 64.09  ?  112  PHE A N   1 
ATOM   500   C CA  . PHE A  1  112 ? -45.375 29.710  120.966 1.00 63.36  ?  112  PHE A CA  1 
ATOM   501   C C   . PHE A  1  112 ? -46.118 30.650  121.909 1.00 67.70  ?  112  PHE A C   1 
ATOM   502   O O   . PHE A  1  112 ? -47.135 30.257  122.492 1.00 70.48  ?  112  PHE A O   1 
ATOM   503   C CB  . PHE A  1  112 ? -46.120 29.587  119.641 1.00 59.81  ?  112  PHE A CB  1 
ATOM   504   C CG  . PHE A  1  112 ? -46.062 30.825  118.792 1.00 57.69  ?  112  PHE A CG  1 
ATOM   505   C CD1 . PHE A  1  112 ? -44.919 31.134  118.070 1.00 55.56  ?  112  PHE A CD1 1 
ATOM   506   C CD2 . PHE A  1  112 ? -47.154 31.673  118.705 1.00 58.40  ?  112  PHE A CD2 1 
ATOM   507   C CE1 . PHE A  1  112 ? -44.863 32.269  117.281 1.00 53.81  ?  112  PHE A CE1 1 
ATOM   508   C CE2 . PHE A  1  112 ? -47.103 32.809  117.917 1.00 56.12  ?  112  PHE A CE2 1 
ATOM   509   C CZ  . PHE A  1  112 ? -45.957 33.107  117.206 1.00 53.66  ?  112  PHE A CZ  1 
ATOM   510   N N   . PRO A  1  113 ? -45.652 31.885  122.088 1.00 62.02  ?  113  PRO A N   1 
ATOM   511   C CA  . PRO A  1  113 ? -46.269 32.801  123.069 1.00 67.42  ?  113  PRO A CA  1 
ATOM   512   C C   . PRO A  1  113 ? -47.524 33.481  122.533 1.00 68.03  ?  113  PRO A C   1 
ATOM   513   O O   . PRO A  1  113 ? -47.559 34.681  122.249 1.00 68.05  ?  113  PRO A O   1 
ATOM   514   C CB  . PRO A  1  113 ? -45.132 33.788  123.346 1.00 68.38  ?  113  PRO A CB  1 
ATOM   515   C CG  . PRO A  1  113 ? -44.401 33.865  122.054 1.00 62.79  ?  113  PRO A CG  1 
ATOM   516   C CD  . PRO A  1  113 ? -44.466 32.483  121.449 1.00 59.47  ?  113  PRO A CD  1 
ATOM   517   N N   . PHE A  1  114 ? -48.595 32.696  122.396 1.00 67.09  ?  114  PHE A N   1 
ATOM   518   C CA  . PHE A  1  114 ? -49.849 33.232  121.873 1.00 68.38  ?  114  PHE A CA  1 
ATOM   519   C C   . PHE A  1  114 ? -50.371 34.376  122.735 1.00 75.42  ?  114  PHE A C   1 
ATOM   520   O O   . PHE A  1  114 ? -50.831 35.398  122.213 1.00 74.41  ?  114  PHE A O   1 
ATOM   521   C CB  . PHE A  1  114 ? -50.899 32.125  121.783 1.00 69.38  ?  114  PHE A CB  1 
ATOM   522   C CG  . PHE A  1  114 ? -50.542 31.023  120.832 1.00 63.16  ?  114  PHE A CG  1 
ATOM   523   C CD1 . PHE A  1  114 ? -50.762 31.165  119.473 1.00 58.40  ?  114  PHE A CD1 1 
ATOM   524   C CD2 . PHE A  1  114 ? -49.996 29.837  121.299 1.00 62.31  ?  114  PHE A CD2 1 
ATOM   525   C CE1 . PHE A  1  114 ? -50.440 30.148  118.594 1.00 53.74  ?  114  PHE A CE1 1 
ATOM   526   C CE2 . PHE A  1  114 ? -49.668 28.816  120.426 1.00 57.68  ?  114  PHE A CE2 1 
ATOM   527   C CZ  . PHE A  1  114 ? -49.892 28.972  119.073 1.00 53.72  ?  114  PHE A CZ  1 
ATOM   528   N N   . SER A  1  115 ? -50.310 34.224  124.057 1.00 67.45  ?  115  SER A N   1 
ATOM   529   C CA  . SER A  1  115 ? -50.864 35.219  124.968 1.00 74.49  ?  115  SER A CA  1 
ATOM   530   C C   . SER A  1  115 ? -50.008 36.473  125.084 1.00 74.60  ?  115  SER A C   1 
ATOM   531   O O   . SER A  1  115 ? -50.423 37.413  125.768 1.00 75.34  ?  115  SER A O   1 
ATOM   532   C CB  . SER A  1  115 ? -51.061 34.601  126.351 1.00 75.63  ?  115  SER A CB  1 
ATOM   533   O OG  . SER A  1  115 ? -50.024 33.681  126.635 1.00 72.74  ?  115  SER A OG  1 
ATOM   534   N N   . SER A  1  116 ? -48.837 36.518  124.451 1.00 69.14  ?  116  SER A N   1 
ATOM   535   C CA  . SER A  1  116 ? -47.898 37.608  124.657 1.00 68.45  ?  116  SER A CA  1 
ATOM   536   C C   . SER A  1  116 ? -47.735 38.530  123.454 1.00 60.82  ?  116  SER A C   1 
ATOM   537   O O   . SER A  1  116 ? -47.112 39.588  123.594 1.00 60.28  ?  116  SER A O   1 
ATOM   538   C CB  . SER A  1  116 ? -46.527 37.043  125.049 1.00 67.97  ?  116  SER A CB  1 
ATOM   539   O OG  . SER A  1  116 ? -46.674 35.949  125.936 1.00 70.64  ?  116  SER A OG  1 
ATOM   540   N N   . LEU A  1  117 ? -48.270 38.171  122.283 1.00 69.36  ?  117  LEU A N   1 
ATOM   541   C CA  . LEU A  1  117 ? -48.067 38.926  121.045 1.00 62.79  ?  117  LEU A CA  1 
ATOM   542   C C   . LEU A  1  117 ? -49.408 39.340  120.453 1.00 61.26  ?  117  LEU A C   1 
ATOM   543   O O   . LEU A  1  117 ? -49.802 38.854  119.385 1.00 57.25  ?  117  LEU A O   1 
ATOM   544   C CB  . LEU A  1  117 ? -47.286 38.106  120.023 1.00 57.68  ?  117  LEU A CB  1 
ATOM   545   C CG  . LEU A  1  117 ? -46.077 37.358  120.556 1.00 58.96  ?  117  LEU A CG  1 
ATOM   546   C CD1 . LEU A  1  117 ? -45.394 36.640  119.409 1.00 54.00  ?  117  LEU A CD1 1 
ATOM   547   C CD2 . LEU A  1  117 ? -45.151 38.345  121.249 1.00 61.85  ?  117  LEU A CD2 1 
ATOM   548   N N   . PRO A  1  118 ? -50.124 40.258  121.105 1.00 61.10  ?  118  PRO A N   1 
ATOM   549   C CA  . PRO A  1  118 ? -51.470 40.599  120.626 1.00 59.76  ?  118  PRO A CA  1 
ATOM   550   C C   . PRO A  1  118 ? -51.488 41.335  119.296 1.00 53.69  ?  118  PRO A C   1 
ATOM   551   O O   . PRO A  1  118 ? -52.542 41.369  118.647 1.00 51.96  ?  118  PRO A O   1 
ATOM   552   C CB  . PRO A  1  118 ? -52.024 41.476  121.755 1.00 62.92  ?  118  PRO A CB  1 
ATOM   553   C CG  . PRO A  1  118 ? -50.814 42.095  122.361 1.00 63.90  ?  118  PRO A CG  1 
ATOM   554   C CD  . PRO A  1  118 ? -49.735 41.055  122.281 1.00 65.07  ?  118  PRO A CD  1 
ATOM   555   N N   . ASN A  1  119 ? -50.366 41.907  118.856 1.00 63.08  ?  119  ASN A N   1 
ATOM   556   C CA  . ASN A  1  119 ? -50.360 42.812  117.713 1.00 58.76  ?  119  ASN A CA  1 
ATOM   557   C C   . ASN A  1  119 ? -49.787 42.182  116.447 1.00 55.38  ?  119  ASN A C   1 
ATOM   558   O O   . ASN A  1  119 ? -49.458 42.905  115.502 1.00 52.89  ?  119  ASN A O   1 
ATOM   559   C CB  . ASN A  1  119 ? -49.596 44.089  118.054 1.00 58.99  ?  119  ASN A CB  1 
ATOM   560   C CG  . ASN A  1  119 ? -50.277 44.903  119.132 1.00 61.48  ?  119  ASN A CG  1 
ATOM   561   O OD1 . ASN A  1  119 ? -51.504 44.891  119.262 1.00 61.75  ?  119  ASN A OD1 1 
ATOM   562   N ND2 . ASN A  1  119 ? -49.477 45.621  119.915 1.00 63.41  ?  119  ASN A ND2 1 
ATOM   563   N N   . LEU A  1  120 ? -49.656 40.860  116.400 1.00 56.36  ?  120  LEU A N   1 
ATOM   564   C CA  . LEU A  1  120 ? -49.139 40.219  115.199 1.00 53.01  ?  120  LEU A CA  1 
ATOM   565   C C   . LEU A  1  120 ? -50.108 40.435  114.042 1.00 50.77  ?  120  LEU A C   1 
ATOM   566   O O   . LEU A  1  120 ? -51.289 40.083  114.137 1.00 51.49  ?  120  LEU A O   1 
ATOM   567   C CB  . LEU A  1  120 ? -48.920 38.728  115.441 1.00 53.11  ?  120  LEU A CB  1 
ATOM   568   C CG  . LEU A  1  120 ? -47.782 38.334  116.385 1.00 55.20  ?  120  LEU A CG  1 
ATOM   569   C CD1 . LEU A  1  120 ? -47.671 36.816  116.488 1.00 55.03  ?  120  LEU A CD1 1 
ATOM   570   C CD2 . LEU A  1  120 ? -46.461 38.955  115.940 1.00 54.47  ?  120  LEU A CD2 1 
ATOM   571   N N   . THR A  1  121 ? -49.615 41.032  112.953 1.00 53.63  ?  121  THR A N   1 
ATOM   572   C CA  . THR A  1  121 ? -50.402 41.175  111.738 1.00 51.91  ?  121  THR A CA  1 
ATOM   573   C C   . THR A  1  121 ? -49.769 40.518  110.520 1.00 50.73  ?  121  THR A C   1 
ATOM   574   O O   . THR A  1  121 ? -50.484 40.263  109.545 1.00 49.86  ?  121  THR A O   1 
ATOM   575   C CB  . THR A  1  121 ? -50.673 42.659  111.423 1.00 51.55  ?  121  THR A CB  1 
ATOM   576   O OG1 . THR A  1  121 ? -49.618 43.186  110.618 1.00 51.35  ?  121  THR A OG1 1 
ATOM   577   C CG2 . THR A  1  121 ? -50.767 43.483  112.693 1.00 53.08  ?  121  THR A CG2 1 
ATOM   578   N N   . PHE A  1  122 ? -48.466 40.231  110.547 1.00 53.60  ?  122  PHE A N   1 
ATOM   579   C CA  . PHE A  1  122 ? -47.777 39.521  109.472 1.00 53.58  ?  122  PHE A CA  1 
ATOM   580   C C   . PHE A  1  122 ? -46.960 38.395  110.084 1.00 53.92  ?  122  PHE A C   1 
ATOM   581   O O   . PHE A  1  122 ? -46.018 38.653  110.839 1.00 55.46  ?  122  PHE A O   1 
ATOM   582   C CB  . PHE A  1  122 ? -46.862 40.460  108.682 1.00 55.43  ?  122  PHE A CB  1 
ATOM   583   C CG  . PHE A  1  122 ? -46.047 39.770  107.611 1.00 57.24  ?  122  PHE A CG  1 
ATOM   584   C CD1 . PHE A  1  122 ? -46.618 39.416  106.397 1.00 57.20  ?  122  PHE A CD1 1 
ATOM   585   C CD2 . PHE A  1  122 ? -44.691 39.522  107.799 1.00 60.01  ?  122  PHE A CD2 1 
ATOM   586   C CE1 . PHE A  1  122 ? -45.855 38.800  105.402 1.00 60.10  ?  122  PHE A CE1 1 
ATOM   587   C CE2 . PHE A  1  122 ? -43.929 38.901  106.814 1.00 63.09  ?  122  PHE A CE2 1 
ATOM   588   C CZ  . PHE A  1  122 ? -44.512 38.542  105.615 1.00 63.25  ?  122  PHE A CZ  1 
ATOM   589   N N   . VAL A  1  123 ? -47.299 37.155  109.745 1.00 52.30  ?  123  VAL A N   1 
ATOM   590   C CA  . VAL A  1  123 ? -46.599 35.986  110.262 1.00 52.64  ?  123  VAL A CA  1 
ATOM   591   C C   . VAL A  1  123 ? -46.251 35.085  109.086 1.00 53.04  ?  123  VAL A C   1 
ATOM   592   O O   . VAL A  1  123 ? -47.150 34.537  108.432 1.00 51.81  ?  123  VAL A O   1 
ATOM   593   C CB  . VAL A  1  123 ? -47.432 35.225  111.299 1.00 51.86  ?  123  VAL A CB  1 
ATOM   594   C CG1 . VAL A  1  123 ? -46.838 33.860  111.553 1.00 52.12  ?  123  VAL A CG1 1 
ATOM   595   C CG2 . VAL A  1  123 ? -47.501 36.011  112.585 1.00 53.29  ?  123  VAL A CG2 1 
ATOM   596   N N   . ASP A  1  124 ? -44.952 34.925  108.819 1.00 51.08  ?  124  ASP A N   1 
ATOM   597   C CA  . ASP A  1  124 ? -44.450 33.976  107.827 1.00 52.97  ?  124  ASP A CA  1 
ATOM   598   C C   . ASP A  1  124 ? -43.394 33.099  108.489 1.00 54.46  ?  124  ASP A C   1 
ATOM   599   O O   . ASP A  1  124 ? -42.309 33.577  108.832 1.00 57.35  ?  124  ASP A O   1 
ATOM   600   C CB  . ASP A  1  124 ? -43.878 34.691  106.603 1.00 56.89  ?  124  ASP A CB  1 
ATOM   601   C CG  . ASP A  1  124 ? -43.612 33.740  105.450 1.00 59.81  ?  124  ASP A CG  1 
ATOM   602   O OD1 . ASP A  1  124 ? -43.646 32.511  105.673 1.00 58.51  ?  124  ASP A OD1 1 
ATOM   603   O OD2 . ASP A  1  124 ? -43.381 34.216  104.317 1.00 63.80  -1 124  ASP A OD2 1 
ATOM   604   N N   . LEU A  1  125 ? -43.714 31.822  108.670 1.00 51.87  ?  125  LEU A N   1 
ATOM   605   C CA  . LEU A  1  125 ? -42.794 30.850  109.246 1.00 53.17  ?  125  LEU A CA  1 
ATOM   606   C C   . LEU A  1  125 ? -42.541 29.699  108.280 1.00 54.40  ?  125  LEU A C   1 
ATOM   607   O O   . LEU A  1  125 ? -42.255 28.573  108.698 1.00 54.22  ?  125  LEU A O   1 
ATOM   608   C CB  . LEU A  1  125 ? -43.321 30.328  110.580 1.00 51.00  ?  125  LEU A CB  1 
ATOM   609   C CG  . LEU A  1  125 ? -43.667 31.387  111.619 1.00 50.46  ?  125  LEU A CG  1 
ATOM   610   C CD1 . LEU A  1  125 ? -44.309 30.730  112.814 1.00 49.84  ?  125  LEU A CD1 1 
ATOM   611   C CD2 . LEU A  1  125 ? -42.425 32.150  112.029 1.00 53.25  ?  125  LEU A CD2 1 
ATOM   612   N N   . SER A  1  126 ? -42.664 29.971  106.984 1.00 54.43  ?  126  SER A N   1 
ATOM   613   C CA  . SER A  1  126 ? -42.564 28.935  105.969 1.00 55.97  ?  126  SER A CA  1 
ATOM   614   C C   . SER A  1  126 ? -41.122 28.469  105.792 1.00 59.83  ?  126  SER A C   1 
ATOM   615   O O   . SER A  1  126 ? -40.167 29.129  106.213 1.00 62.25  ?  126  SER A O   1 
ATOM   616   C CB  . SER A  1  126 ? -43.120 29.441  104.636 1.00 57.78  ?  126  SER A CB  1 
ATOM   617   O OG  . SER A  1  126 ? -42.342 30.514  104.130 1.00 62.38  ?  126  SER A OG  1 
ATOM   618   N N   . MET A  1  127 ? -40.982 27.301  105.161 1.00 54.27  ?  127  MET A N   1 
ATOM   619   C CA  . MET A  1  127 ? -39.682 26.741  104.782 1.00 57.50  ?  127  MET A CA  1 
ATOM   620   C C   . MET A  1  127 ? -38.791 26.493  106.001 1.00 56.95  ?  127  MET A C   1 
ATOM   621   O O   . MET A  1  127 ? -37.599 26.814  106.014 1.00 59.95  ?  127  MET A O   1 
ATOM   622   C CB  . MET A  1  127 ? -38.986 27.636  103.755 1.00 62.53  ?  127  MET A CB  1 
ATOM   623   C CG  . MET A  1  127 ? -39.856 27.953  102.550 1.00 63.94  ?  127  MET A CG  1 
ATOM   624   S SD  . MET A  1  127 ? -38.915 28.646  101.180 1.00 70.82  ?  127  MET A SD  1 
ATOM   625   C CE  . MET A  1  127 ? -37.679 27.370  100.925 1.00 70.79  ?  127  MET A CE  1 
ATOM   626   N N   . ASN A  1  128 ? -39.383 25.881  107.021 1.00 60.08  ?  128  ASN A N   1 
ATOM   627   C CA  . ASN A  1  128 ? -38.690 25.506  108.247 1.00 59.63  ?  128  ASN A CA  1 
ATOM   628   C C   . ASN A  1  128 ? -38.977 24.041  108.541 1.00 57.62  ?  128  ASN A C   1 
ATOM   629   O O   . ASN A  1  128 ? -39.489 23.324  107.676 1.00 57.09  ?  128  ASN A O   1 
ATOM   630   C CB  . ASN A  1  128 ? -39.100 26.418  109.399 1.00 58.38  ?  128  ASN A CB  1 
ATOM   631   C CG  . ASN A  1  128 ? -38.506 27.807  109.268 1.00 61.02  ?  128  ASN A CG  1 
ATOM   632   O OD1 . ASN A  1  128 ? -37.320 28.010  109.524 1.00 63.76  ?  128  ASN A OD1 1 
ATOM   633   N ND2 . ASN A  1  128 ? -39.321 28.768  108.843 1.00 60.36  ?  128  ASN A ND2 1 
ATOM   634   N N   . ARG A  1  129 ? -38.609 23.565  109.724 1.00 67.06  ?  129  ARG A N   1 
ATOM   635   C CA  . ARG A  1  129 ? -38.847 22.178  110.107 1.00 65.66  ?  129  ARG A CA  1 
ATOM   636   C C   . ARG A  1  129 ? -39.747 22.100  111.339 1.00 63.96  ?  129  ARG A C   1 
ATOM   637   O O   . ARG A  1  129 ? -39.503 21.320  112.266 1.00 64.44  ?  129  ARG A O   1 
ATOM   638   C CB  . ARG A  1  129 ? -37.528 21.450  110.345 1.00 67.08  ?  129  ARG A CB  1 
ATOM   639   C CG  . ARG A  1  129 ? -36.649 21.389  109.111 1.00 69.00  ?  129  ARG A CG  1 
ATOM   640   C CD  . ARG A  1  129 ? -35.503 20.404  109.283 1.00 71.27  ?  129  ARG A CD  1 
ATOM   641   N NE  . ARG A  1  129 ? -35.843 19.317  110.194 1.00 73.08  ?  129  ARG A NE  1 
ATOM   642   C CZ  . ARG A  1  129 ? -36.203 18.098  109.811 1.00 75.02  ?  129  ARG A CZ  1 
ATOM   643   N NH1 . ARG A  1  129 ? -36.276 17.769  108.530 1.00 75.35  ?  129  ARG A NH1 1 
ATOM   644   N NH2 . ARG A  1  129 ? -36.499 17.188  110.737 1.00 76.90  ?  129  ARG A NH2 1 
ATOM   645   N N   . PHE A  1  130 ? -40.806 22.917  111.351 1.00 59.04  ?  130  PHE A N   1 
ATOM   646   C CA  . PHE A  1  130 ? -41.805 22.865  112.412 1.00 58.45  ?  130  PHE A CA  1 
ATOM   647   C C   . PHE A  1  130 ? -42.667 21.618  112.274 1.00 59.56  ?  130  PHE A C   1 
ATOM   648   O O   . PHE A  1  130 ? -43.118 21.271  111.180 1.00 59.14  ?  130  PHE A O   1 
ATOM   649   C CB  . PHE A  1  130 ? -42.696 24.109  112.377 1.00 56.25  ?  130  PHE A CB  1 
ATOM   650   C CG  . PHE A  1  130 ? -42.009 25.359  112.837 1.00 57.30  ?  130  PHE A CG  1 
ATOM   651   C CD1 . PHE A  1  130 ? -41.601 25.494  114.152 1.00 58.35  ?  130  PHE A CD1 1 
ATOM   652   C CD2 . PHE A  1  130 ? -41.770 26.401  111.955 1.00 57.60  ?  130  PHE A CD2 1 
ATOM   653   C CE1 . PHE A  1  130 ? -40.960 26.640  114.576 1.00 59.73  ?  130  PHE A CE1 1 
ATOM   654   C CE2 . PHE A  1  130 ? -41.131 27.550  112.376 1.00 58.94  ?  130  PHE A CE2 1 
ATOM   655   C CZ  . PHE A  1  130 ? -40.727 27.670  113.687 1.00 60.02  ?  130  PHE A CZ  1 
ATOM   656   N N   . SER A  1  131 ? -42.898 20.944  113.395 1.00 61.70  ?  131  SER A N   1 
ATOM   657   C CA  . SER A  1  131 ? -43.726 19.749  113.443 1.00 63.06  ?  131  SER A CA  1 
ATOM   658   C C   . SER A  1  131 ? -44.768 19.898  114.546 1.00 62.70  ?  131  SER A C   1 
ATOM   659   O O   . SER A  1  131 ? -44.667 20.766  115.417 1.00 62.18  ?  131  SER A O   1 
ATOM   660   C CB  . SER A  1  131 ? -42.875 18.494  113.669 1.00 66.63  ?  131  SER A CB  1 
ATOM   661   O OG  . SER A  1  131 ? -42.160 18.592  114.885 1.00 68.19  ?  131  SER A OG  1 
ATOM   662   N N   . GLY A  1  132 ? -45.779 19.036  114.507 1.00 62.41  ?  132  GLY A N   1 
ATOM   663   C CA  . GLY A  1  132 ? -46.877 19.146  115.447 1.00 62.30  ?  132  GLY A CA  1 
ATOM   664   C C   . GLY A  1  132 ? -48.176 19.520  114.767 1.00 61.15  ?  132  GLY A C   1 
ATOM   665   O O   . GLY A  1  132 ? -48.375 19.186  113.595 1.00 60.29  ?  132  GLY A O   1 
ATOM   666   N N   . THR A  1  133 ? -49.064 20.211  115.476 1.00 57.67  ?  133  THR A N   1 
ATOM   667   C CA  . THR A  1  133 ? -50.367 20.576  114.940 1.00 56.20  ?  133  THR A CA  1 
ATOM   668   C C   . THR A  1  133 ? -50.535 22.091  114.944 1.00 56.02  ?  133  THR A C   1 
ATOM   669   O O   . THR A  1  133 ? -49.724 22.833  115.503 1.00 55.99  ?  133  THR A O   1 
ATOM   670   C CB  . THR A  1  133 ? -51.495 19.914  115.742 1.00 58.61  ?  133  THR A CB  1 
ATOM   671   O OG1 . THR A  1  133 ? -51.341 20.225  117.131 1.00 60.46  ?  133  THR A OG1 1 
ATOM   672   C CG2 . THR A  1  133 ? -51.460 18.409  115.566 1.00 60.27  ?  133  THR A CG2 1 
ATOM   673   N N   . ILE A  1  134 ? -51.606 22.547  114.302 1.00 55.99  ?  134  ILE A N   1 
ATOM   674   C CA  . ILE A  1  134 ? -51.967 23.960  114.296 1.00 56.06  ?  134  ILE A CA  1 
ATOM   675   C C   . ILE A  1  134 ? -52.904 24.208  115.472 1.00 60.21  ?  134  ILE A C   1 
ATOM   676   O O   . ILE A  1  134 ? -54.003 23.643  115.533 1.00 62.56  ?  134  ILE A O   1 
ATOM   677   C CB  . ILE A  1  134 ? -52.625 24.365  112.969 1.00 54.34  ?  134  ILE A CB  1 
ATOM   678   C CG1 . ILE A  1  134 ? -51.623 24.256  111.821 1.00 51.03  ?  134  ILE A CG1 1 
ATOM   679   C CG2 . ILE A  1  134 ? -53.158 25.784  113.056 1.00 55.00  ?  134  ILE A CG2 1 
ATOM   680   C CD1 . ILE A  1  134 ? -52.269 24.265  110.454 1.00 49.89  ?  134  ILE A CD1 1 
ATOM   681   N N   . SER A  1  135 ? -52.470 25.050  116.409 1.00 53.58  ?  135  SER A N   1 
ATOM   682   C CA  . SER A  1  135 ? -53.233 25.272  117.628 1.00 58.43  ?  135  SER A CA  1 
ATOM   683   C C   . SER A  1  135 ? -54.461 26.141  117.356 1.00 61.34  ?  135  SER A C   1 
ATOM   684   O O   . SER A  1  135 ? -54.439 27.007  116.478 1.00 59.27  ?  135  SER A O   1 
ATOM   685   C CB  . SER A  1  135 ? -52.362 25.944  118.688 1.00 59.76  ?  135  SER A CB  1 
ATOM   686   O OG  . SER A  1  135 ? -53.034 26.032  119.934 1.00 64.68  ?  135  SER A OG  1 
ATOM   687   N N   . PRO A  1  136 ? -55.545 25.935  118.106 1.00 55.81  ?  136  PRO A N   1 
ATOM   688   C CA  . PRO A  1  136 ? -56.678 26.865  118.020 1.00 60.26  ?  136  PRO A CA  1 
ATOM   689   C C   . PRO A  1  136 ? -56.318 28.269  118.459 1.00 62.46  ?  136  PRO A C   1 
ATOM   690   O O   . PRO A  1  136 ? -57.024 29.219  118.096 1.00 65.42  ?  136  PRO A O   1 
ATOM   691   C CB  . PRO A  1  136 ? -57.721 26.238  118.955 1.00 64.56  ?  136  PRO A CB  1 
ATOM   692   C CG  . PRO A  1  136 ? -57.299 24.826  119.121 1.00 61.36  ?  136  PRO A CG  1 
ATOM   693   C CD  . PRO A  1  136 ? -55.811 24.839  119.048 1.00 57.42  ?  136  PRO A CD  1 
ATOM   694   N N   . GLU A  1  137 ? -55.244 28.427  119.239 1.00 62.15  ?  137  GLU A N   1 
ATOM   695   C CA  . GLU A  1  137 ? -54.813 29.744  119.691 1.00 64.31  ?  137  GLU A CA  1 
ATOM   696   C C   . GLU A  1  137 ? -54.414 30.647  118.534 1.00 59.50  ?  137  GLU A C   1 
ATOM   697   O O   . GLU A  1  137 ? -54.422 31.872  118.693 1.00 60.98  ?  137  GLU A O   1 
ATOM   698   C CB  . GLU A  1  137 ? -53.645 29.605  120.666 1.00 63.63  ?  137  GLU A CB  1 
ATOM   699   C CG  . GLU A  1  137 ? -53.893 28.623  121.786 1.00 65.84  ?  137  GLU A CG  1 
ATOM   700   C CD  . GLU A  1  137 ? -54.266 29.304  123.084 1.00 71.18  ?  137  GLU A CD  1 
ATOM   701   O OE1 . GLU A  1  137 ? -55.289 30.024  123.105 1.00 74.83  ?  137  GLU A OE1 1 
ATOM   702   O OE2 . GLU A  1  137 ? -53.538 29.114  124.082 1.00 71.35  -1 137  GLU A OE2 1 
ATOM   703   N N   . TRP A  1  138 ? -54.056 30.075  117.380 1.00 67.91  ?  138  TRP A N   1 
ATOM   704   C CA  . TRP A  1  138 ? -53.723 30.892  116.220 1.00 62.51  ?  138  TRP A CA  1 
ATOM   705   C C   . TRP A  1  138 ? -54.865 31.820  115.825 1.00 64.30  ?  138  TRP A C   1 
ATOM   706   O O   . TRP A  1  138 ? -54.620 32.859  115.206 1.00 60.67  ?  138  TRP A O   1 
ATOM   707   C CB  . TRP A  1  138 ? -53.344 29.999  115.035 1.00 57.21  ?  138  TRP A CB  1 
ATOM   708   C CG  . TRP A  1  138 ? -51.949 29.435  115.111 1.00 54.23  ?  138  TRP A CG  1 
ATOM   709   C CD1 . TRP A  1  138 ? -51.604 28.138  115.349 1.00 54.26  ?  138  TRP A CD1 1 
ATOM   710   C CD2 . TRP A  1  138 ? -50.716 30.149  114.936 1.00 51.51  ?  138  TRP A CD2 1 
ATOM   711   N NE1 . TRP A  1  138 ? -50.239 27.998  115.343 1.00 52.07  ?  138  TRP A NE1 1 
ATOM   712   C CE2 . TRP A  1  138 ? -49.669 29.218  115.092 1.00 50.62  ?  138  TRP A CE2 1 
ATOM   713   C CE3 . TRP A  1  138 ? -50.396 31.486  114.672 1.00 50.26  ?  138  TRP A CE3 1 
ATOM   714   C CZ2 . TRP A  1  138 ? -48.325 29.578  114.989 1.00 49.23  ?  138  TRP A CZ2 1 
ATOM   715   C CZ3 . TRP A  1  138 ? -49.058 31.840  114.568 1.00 48.63  ?  138  TRP A CZ3 1 
ATOM   716   C CH2 . TRP A  1  138 ? -48.041 30.889  114.726 1.00 48.44  ?  138  TRP A CH2 1 
ATOM   717   N N   . GLY A  1  139 ? -56.100 31.484  116.188 1.00 57.94  ?  139  GLY A N   1 
ATOM   718   C CA  . GLY A  1  139 ? -57.244 32.331  115.930 1.00 59.82  ?  139  GLY A CA  1 
ATOM   719   C C   . GLY A  1  139 ? -57.427 33.489  116.883 1.00 62.77  ?  139  GLY A C   1 
ATOM   720   O O   . GLY A  1  139 ? -58.433 34.199  116.794 1.00 63.27  ?  139  GLY A O   1 
ATOM   721   N N   . ARG A  1  140 ? -56.485 33.700  117.803 1.00 58.77  ?  140  ARG A N   1 
ATOM   722   C CA  . ARG A  1  140 ? -56.581 34.786  118.768 1.00 61.37  ?  140  ARG A CA  1 
ATOM   723   C C   . ARG A  1  140 ? -55.974 36.088  118.271 1.00 55.94  ?  140  ARG A C   1 
ATOM   724   O O   . ARG A  1  140 ? -56.264 37.145  118.840 1.00 56.99  ?  140  ARG A O   1 
ATOM   725   C CB  . ARG A  1  140 ? -55.898 34.388  120.080 1.00 66.87  ?  140  ARG A CB  1 
ATOM   726   C CG  . ARG A  1  140 ? -56.770 33.566  121.016 1.00 73.14  ?  140  ARG A CG  1 
ATOM   727   C CD  . ARG A  1  140 ? -56.002 33.149  122.264 1.00 77.08  ?  140  ARG A CD  1 
ATOM   728   N NE  . ARG A  1  140 ? -55.802 34.266  123.182 1.00 77.14  ?  140  ARG A NE  1 
ATOM   729   C CZ  . ARG A  1  140 ? -54.994 34.242  124.234 1.00 79.06  ?  140  ARG A CZ  1 
ATOM   730   N NH1 . ARG A  1  140 ? -54.271 33.171  124.526 1.00 78.93  ?  140  ARG A NH1 1 
ATOM   731   N NH2 . ARG A  1  140 ? -54.909 35.319  125.013 1.00 78.90  ?  140  ARG A NH2 1 
ATOM   732   N N   . PHE A  1  141 ? -55.148 36.046  117.229 1.00 63.12  ?  141  PHE A N   1 
ATOM   733   C CA  . PHE A  1  141 ? -54.428 37.231  116.760 1.00 58.70  ?  141  PHE A CA  1 
ATOM   734   C C   . PHE A  1  141 ? -55.403 38.112  115.984 1.00 56.97  ?  141  PHE A C   1 
ATOM   735   O O   . PHE A  1  141 ? -55.566 37.988  114.769 1.00 53.45  ?  141  PHE A O   1 
ATOM   736   C CB  . PHE A  1  141 ? -53.219 36.822  115.928 1.00 53.64  ?  141  PHE A CB  1 
ATOM   737   C CG  . PHE A  1  141 ? -52.183 36.072  116.713 1.00 54.95  ?  141  PHE A CG  1 
ATOM   738   C CD1 . PHE A  1  141 ? -51.477 36.694  117.725 1.00 57.48  ?  141  PHE A CD1 1 
ATOM   739   C CD2 . PHE A  1  141 ? -51.934 34.736  116.457 1.00 53.89  ?  141  PHE A CD2 1 
ATOM   740   C CE1 . PHE A  1  141 ? -50.527 36.003  118.455 1.00 59.13  ?  141  PHE A CE1 1 
ATOM   741   C CE2 . PHE A  1  141 ? -50.986 34.041  117.184 1.00 54.95  ?  141  PHE A CE2 1 
ATOM   742   C CZ  . PHE A  1  141 ? -50.283 34.678  118.184 1.00 57.66  ?  141  PHE A CZ  1 
ATOM   743   N N   . SER A  1  142 ? -56.037 39.039  116.707 1.00 57.85  ?  142  SER A N   1 
ATOM   744   C CA  . SER A  1  142 ? -57.185 39.766  116.173 1.00 56.13  ?  142  SER A CA  1 
ATOM   745   C C   . SER A  1  142 ? -56.817 40.675  115.005 1.00 51.23  ?  142  SER A C   1 
ATOM   746   O O   . SER A  1  142 ? -57.675 40.976  114.166 1.00 50.18  ?  142  SER A O   1 
ATOM   747   C CB  . SER A  1  142 ? -57.838 40.579  117.287 1.00 58.41  ?  142  SER A CB  1 
ATOM   748   O OG  . SER A  1  142 ? -56.890 41.424  117.916 1.00 58.10  ?  142  SER A OG  1 
ATOM   749   N N   . LYS A  1  143 ? -55.571 41.138  114.935 1.00 59.25  ?  143  LYS A N   1 
ATOM   750   C CA  . LYS A  1  143 ? -55.172 42.076  113.897 1.00 55.59  ?  143  LYS A CA  1 
ATOM   751   C C   . LYS A  1  143 ? -54.421 41.405  112.754 1.00 53.17  ?  143  LYS A C   1 
ATOM   752   O O   . LYS A  1  143 ? -53.988 42.095  111.825 1.00 50.96  ?  143  LYS A O   1 
ATOM   753   C CB  . LYS A  1  143 ? -54.333 43.205  114.504 1.00 55.51  ?  143  LYS A CB  1 
ATOM   754   C CG  . LYS A  1  143 ? -55.124 44.071  115.477 1.00 57.37  ?  143  LYS A CG  1 
ATOM   755   C CD  . LYS A  1  143 ? -54.555 45.476  115.632 1.00 56.43  ?  143  LYS A CD  1 
ATOM   756   C CE  . LYS A  1  143 ? -53.253 45.466  116.410 1.00 57.88  ?  143  LYS A CE  1 
ATOM   757   N NZ  . LYS A  1  143 ? -53.413 44.893  117.771 1.00 61.69  ?  143  LYS A NZ  1 
ATOM   758   N N   . LEU A  1  144 ? -54.304 40.077  112.779 1.00 56.62  ?  144  LEU A N   1 
ATOM   759   C CA  . LEU A  1  144 ? -53.506 39.355  111.792 1.00 54.27  ?  144  LEU A CA  1 
ATOM   760   C C   . LEU A  1  144 ? -54.091 39.494  110.388 1.00 52.66  ?  144  LEU A C   1 
ATOM   761   O O   . LEU A  1  144 ? -55.295 39.318  110.182 1.00 53.58  ?  144  LEU A O   1 
ATOM   762   C CB  . LEU A  1  144 ? -53.421 37.881  112.185 1.00 55.00  ?  144  LEU A CB  1 
ATOM   763   C CG  . LEU A  1  144 ? -52.402 37.008  111.455 1.00 52.47  ?  144  LEU A CG  1 
ATOM   764   C CD1 . LEU A  1  144 ? -50.988 37.335  111.909 1.00 52.15  ?  144  LEU A CD1 1 
ATOM   765   C CD2 . LEU A  1  144 ? -52.717 35.533  111.671 1.00 53.07  ?  144  LEU A CD2 1 
ATOM   766   N N   . GLU A  1  145 ? -53.227 39.802  109.416 1.00 53.60  ?  145  GLU A N   1 
ATOM   767   C CA  . GLU A  1  145 ? -53.631 39.932  108.023 1.00 52.90  ?  145  GLU A CA  1 
ATOM   768   C C   . GLU A  1  145 ? -52.977 38.922  107.091 1.00 52.55  ?  145  GLU A C   1 
ATOM   769   O O   . GLU A  1  145 ? -53.547 38.631  106.033 1.00 52.86  ?  145  GLU A O   1 
ATOM   770   C CB  . GLU A  1  145 ? -53.317 41.343  107.500 1.00 52.45  ?  145  GLU A CB  1 
ATOM   771   C CG  . GLU A  1  145 ? -54.034 42.455  108.245 1.00 52.62  ?  145  GLU A CG  1 
ATOM   772   C CD  . GLU A  1  145 ? -53.512 43.840  107.890 1.00 52.17  ?  145  GLU A CD  1 
ATOM   773   O OE1 . GLU A  1  145 ? -53.278 44.098  106.691 1.00 52.08  ?  145  GLU A OE1 1 
ATOM   774   O OE2 . GLU A  1  145 ? -53.349 44.677  108.806 1.00 52.45  -1 145  GLU A OE2 1 
ATOM   775   N N   . TYR A  1  146 ? -51.804 38.393  107.443 1.00 49.52  ?  146  TYR A N   1 
ATOM   776   C CA  . TYR A  1  146 ? -51.041 37.474  106.604 1.00 49.59  ?  146  TYR A CA  1 
ATOM   777   C C   . TYR A  1  146 ? -50.598 36.302  107.466 1.00 48.92  ?  146  TYR A C   1 
ATOM   778   O O   . TYR A  1  146 ? -49.887 36.494  108.459 1.00 49.04  ?  146  TYR A O   1 
ATOM   779   C CB  . TYR A  1  146 ? -49.827 38.181  105.995 1.00 51.00  ?  146  TYR A CB  1 
ATOM   780   C CG  . TYR A  1  146 ? -49.133 37.435  104.875 1.00 52.82  ?  146  TYR A CG  1 
ATOM   781   C CD1 . TYR A  1  146 ? -48.117 36.527  105.146 1.00 53.65  ?  146  TYR A CD1 1 
ATOM   782   C CD2 . TYR A  1  146 ? -49.489 37.638  103.546 1.00 54.49  ?  146  TYR A CD2 1 
ATOM   783   C CE1 . TYR A  1  146 ? -47.471 35.845  104.128 1.00 56.52  ?  146  TYR A CE1 1 
ATOM   784   C CE2 . TYR A  1  146 ? -48.848 36.959  102.521 1.00 57.42  ?  146  TYR A CE2 1 
ATOM   785   C CZ  . TYR A  1  146 ? -47.841 36.061  102.820 1.00 58.64  ?  146  TYR A CZ  1 
ATOM   786   O OH  . TYR A  1  146 ? -47.197 35.373  101.817 1.00 62.69  ?  146  TYR A OH  1 
ATOM   787   N N   . PHE A  1  147 ? -51.012 35.094  107.088 1.00 49.96  ?  147  PHE A N   1 
ATOM   788   C CA  . PHE A  1  147 ? -50.737 33.885  107.861 1.00 49.55  ?  147  PHE A CA  1 
ATOM   789   C C   . PHE A  1  147 ? -50.147 32.849  106.915 1.00 49.88  ?  147  PHE A C   1 
ATOM   790   O O   . PHE A  1  147 ? -50.843 32.360  106.019 1.00 50.18  ?  147  PHE A O   1 
ATOM   791   C CB  . PHE A  1  147 ? -52.013 33.364  108.536 1.00 49.94  ?  147  PHE A CB  1 
ATOM   792   C CG  . PHE A  1  147 ? -51.772 32.311  109.588 1.00 50.50  ?  147  PHE A CG  1 
ATOM   793   C CD1 . PHE A  1  147 ? -50.609 32.315  110.342 1.00 50.51  ?  147  PHE A CD1 1 
ATOM   794   C CD2 . PHE A  1  147 ? -52.718 31.322  109.828 1.00 51.80  ?  147  PHE A CD2 1 
ATOM   795   C CE1 . PHE A  1  147 ? -50.387 31.345  111.311 1.00 51.60  ?  147  PHE A CE1 1 
ATOM   796   C CE2 . PHE A  1  147 ? -52.502 30.350  110.798 1.00 53.10  ?  147  PHE A CE2 1 
ATOM   797   C CZ  . PHE A  1  147 ? -51.336 30.363  111.541 1.00 52.89  ?  147  PHE A CZ  1 
ATOM   798   N N   . ASP A  1  148 ? -48.873 32.508  107.111 1.00 49.68  ?  148  ASP A N   1 
ATOM   799   C CA  . ASP A  1  148 ? -48.178 31.566  106.240 1.00 51.18  ?  148  ASP A CA  1 
ATOM   800   C C   . ASP A  1  148 ? -47.394 30.571  107.082 1.00 51.21  ?  148  ASP A C   1 
ATOM   801   O O   . ASP A  1  148 ? -46.469 30.958  107.803 1.00 51.97  ?  148  ASP A O   1 
ATOM   802   C CB  . ASP A  1  148 ? -47.247 32.299  105.272 1.00 54.28  ?  148  ASP A CB  1 
ATOM   803   C CG  . ASP A  1  148 ? -46.823 31.428  104.100 1.00 57.36  ?  148  ASP A CG  1 
ATOM   804   O OD1 . ASP A  1  148 ? -46.944 30.187  104.208 1.00 56.53  ?  148  ASP A OD1 1 
ATOM   805   O OD2 . ASP A  1  148 ? -46.360 31.979  103.073 1.00 61.29  -1 148  ASP A OD2 1 
ATOM   806   N N   . LEU A  1  149 ? -47.762 29.288  106.978 1.00 51.19  ?  149  LEU A N   1 
ATOM   807   C CA  . LEU A  1  149 ? -47.044 28.184  107.607 1.00 51.67  ?  149  LEU A CA  1 
ATOM   808   C C   . LEU A  1  149 ? -46.738 27.095  106.587 1.00 53.10  ?  149  LEU A C   1 
ATOM   809   O O   . LEU A  1  149 ? -46.727 25.906  106.918 1.00 53.04  ?  149  LEU A O   1 
ATOM   810   C CB  . LEU A  1  149 ? -47.835 27.600  108.780 1.00 50.58  ?  149  LEU A CB  1 
ATOM   811   C CG  . LEU A  1  149 ? -48.102 28.504  109.987 1.00 50.35  ?  149  LEU A CG  1 
ATOM   812   C CD1 . LEU A  1  149 ? -48.957 27.788  111.025 1.00 51.12  ?  149  LEU A CD1 1 
ATOM   813   C CD2 . LEU A  1  149 ? -46.793 29.006  110.604 1.00 51.33  ?  149  LEU A CD2 1 
ATOM   814   N N   . SER A  1  150 ? -46.470 27.489  105.346 1.00 54.17  ?  150  SER A N   1 
ATOM   815   C CA  . SER A  1  150 ? -46.273 26.543  104.261 1.00 56.30  ?  150  SER A CA  1 
ATOM   816   C C   . SER A  1  150 ? -44.904 25.870  104.363 1.00 58.49  ?  150  SER A C   1 
ATOM   817   O O   . SER A  1  150 ? -44.019 26.307  105.102 1.00 59.01  ?  150  SER A O   1 
ATOM   818   C CB  . SER A  1  150 ? -46.418 27.248  102.914 1.00 59.10  ?  150  SER A CB  1 
ATOM   819   O OG  . SER A  1  150 ? -47.641 27.958  102.857 1.00 57.19  ?  150  SER A OG  1 
ATOM   820   N N   . ILE A  1  151 ? -44.742 24.793  103.588 1.00 54.17  ?  151  ILE A N   1 
ATOM   821   C CA  . ILE A  1  151 ? -43.498 24.029  103.486 1.00 56.30  ?  151  ILE A CA  1 
ATOM   822   C C   . ILE A  1  151 ? -42.945 23.728  104.878 1.00 54.80  ?  151  ILE A C   1 
ATOM   823   O O   . ILE A  1  151 ? -41.968 24.337  105.333 1.00 56.15  ?  151  ILE A O   1 
ATOM   824   C CB  . ILE A  1  151 ? -42.470 24.763  102.607 1.00 60.51  ?  151  ILE A CB  1 
ATOM   825   C CG1 . ILE A  1  151 ? -43.048 24.988  101.215 1.00 62.84  ?  151  ILE A CG1 1 
ATOM   826   C CG2 . ILE A  1  151 ? -41.210 23.946  102.460 1.00 62.33  ?  151  ILE A CG2 1 
ATOM   827   C CD1 . ILE A  1  151 ? -42.988 26.416  100.767 1.00 65.86  ?  151  ILE A CD1 1 
ATOM   828   N N   . ASN A  1  152 ? -43.598 22.804  105.571 1.00 58.34  ?  152  ASN A N   1 
ATOM   829   C CA  . ASN A  1  152 ? -43.244 22.415  106.926 1.00 57.41  ?  152  ASN A CA  1 
ATOM   830   C C   . ASN A  1  152 ? -43.624 20.951  107.096 1.00 56.79  ?  152  ASN A C   1 
ATOM   831   O O   . ASN A  1  152 ? -43.890 20.245  106.118 1.00 57.36  ?  152  ASN A O   1 
ATOM   832   C CB  . ASN A  1  152 ? -43.933 23.330  107.943 1.00 55.73  ?  152  ASN A CB  1 
ATOM   833   C CG  . ASN A  1  152 ? -43.088 24.529  108.308 1.00 56.66  ?  152  ASN A CG  1 
ATOM   834   O OD1 . ASN A  1  152 ? -41.903 24.395  108.590 1.00 58.40  ?  152  ASN A OD1 1 
ATOM   835   N ND2 . ASN A  1  152 ? -43.691 25.716  108.282 1.00 55.61  ?  152  ASN A ND2 1 
ATOM   836   N N   . GLN A  1  153 ? -43.648 20.490  108.341 1.00 62.28  ?  153  GLN A N   1 
ATOM   837   C CA  . GLN A  1  153 ? -43.968 19.103  108.660 1.00 63.12  ?  153  GLN A CA  1 
ATOM   838   C C   . GLN A  1  153 ? -45.130 19.025  109.644 1.00 62.45  ?  153  GLN A C   1 
ATOM   839   O O   . GLN A  1  153 ? -45.132 18.212  110.571 1.00 64.48  ?  153  GLN A O   1 
ATOM   840   C CB  . GLN A  1  153 ? -42.742 18.388  109.212 1.00 66.10  ?  153  GLN A CB  1 
ATOM   841   C CG  . GLN A  1  153 ? -41.447 19.063  108.827 1.00 66.28  ?  153  GLN A CG  1 
ATOM   842   C CD  . GLN A  1  153 ? -40.255 18.415  109.477 1.00 69.40  ?  153  GLN A CD  1 
ATOM   843   O OE1 . GLN A  1  153 ? -40.335 17.920  110.603 1.00 70.78  ?  153  GLN A OE1 1 
ATOM   844   N NE2 . GLN A  1  153 ? -39.136 18.406  108.769 1.00 70.88  ?  153  GLN A NE2 1 
ATOM   845   N N   . LEU A  1  154 ? -46.138 19.871  109.437 1.00 60.50  ?  154  LEU A N   1 
ATOM   846   C CA  . LEU A  1  154 ? -47.301 19.926  110.312 1.00 60.54  ?  154  LEU A CA  1 
ATOM   847   C C   . LEU A  1  154 ? -48.260 18.782  110.000 1.00 61.11  ?  154  LEU A C   1 
ATOM   848   O O   . LEU A  1  154 ? -48.292 18.257  108.882 1.00 61.18  ?  154  LEU A O   1 
ATOM   849   C CB  . LEU A  1  154 ? -48.026 21.263  110.147 1.00 59.55  ?  154  LEU A CB  1 
ATOM   850   C CG  . LEU A  1  154 ? -47.567 22.493  110.930 1.00 59.17  ?  154  LEU A CG  1 
ATOM   851   C CD1 . LEU A  1  154 ? -46.061 22.642  110.928 1.00 59.77  ?  154  LEU A CD1 1 
ATOM   852   C CD2 . LEU A  1  154 ? -48.209 23.737  110.347 1.00 57.65  ?  154  LEU A CD2 1 
ATOM   853   N N   . VAL A  1  155 ? -49.049 18.396  111.007 1.00 58.87  ?  155  VAL A N   1 
ATOM   854   C CA  . VAL A  1  155 ? -50.037 17.327  110.893 1.00 59.87  ?  155  VAL A CA  1 
ATOM   855   C C   . VAL A  1  155 ? -51.284 17.720  111.674 1.00 60.95  ?  155  VAL A C   1 
ATOM   856   O O   . VAL A  1  155 ? -51.296 18.695  112.427 1.00 61.08  ?  155  VAL A O   1 
ATOM   857   C CB  . VAL A  1  155 ? -49.506 15.972  111.406 1.00 62.84  ?  155  VAL A CB  1 
ATOM   858   C CG1 . VAL A  1  155 ? -48.530 15.368  110.414 1.00 64.05  ?  155  VAL A CG1 1 
ATOM   859   C CG2 . VAL A  1  155 ? -48.858 16.146  112.765 1.00 64.07  ?  155  VAL A CG2 1 
ATOM   860   N N   . GLY A  1  156 ? -52.337 16.928  111.507 1.00 59.87  ?  156  GLY A N   1 
ATOM   861   C CA  . GLY A  1  156 ? -53.581 17.193  112.198 1.00 61.67  ?  156  GLY A CA  1 
ATOM   862   C C   . GLY A  1  156 ? -54.541 18.028  111.378 1.00 61.86  ?  156  GLY A C   1 
ATOM   863   O O   . GLY A  1  156 ? -54.318 18.338  110.204 1.00 60.24  ?  156  GLY A O   1 
ATOM   864   N N   . GLU A  1  157 ? -55.650 18.384  112.019 1.00 57.07  ?  157  GLU A N   1 
ATOM   865   C CA  . GLU A  1  157 ? -56.704 19.155  111.379 1.00 58.09  ?  157  GLU A CA  1 
ATOM   866   C C   . GLU A  1  157 ? -56.440 20.650  111.497 1.00 57.34  ?  157  GLU A C   1 
ATOM   867   O O   . GLU A  1  157 ? -55.660 21.108  112.333 1.00 56.85  ?  157  GLU A O   1 
ATOM   868   C CB  . GLU A  1  157 ? -58.063 18.822  111.990 1.00 61.84  ?  157  GLU A CB  1 
ATOM   869   C CG  . GLU A  1  157 ? -58.304 17.342  112.203 1.00 62.49  ?  157  GLU A CG  1 
ATOM   870   C CD  . GLU A  1  157 ? -59.747 16.949  111.957 1.00 65.23  ?  157  GLU A CD  1 
ATOM   871   O OE1 . GLU A  1  157 ? -60.522 17.809  111.482 1.00 66.78  ?  157  GLU A OE1 1 
ATOM   872   O OE2 . GLU A  1  157 ? -60.109 15.788  112.247 1.00 65.91  -1 157  GLU A OE2 1 
ATOM   873   N N   . ILE A  1  158 ? -57.107 21.408  110.634 1.00 53.82  ?  158  ILE A N   1 
ATOM   874   C CA  . ILE A  1  158 ? -57.092 22.864  110.702 1.00 52.19  ?  158  ILE A CA  1 
ATOM   875   C C   . ILE A  1  158 ? -58.163 23.272  111.708 1.00 52.89  ?  158  ILE A C   1 
ATOM   876   O O   . ILE A  1  158 ? -59.328 22.884  111.553 1.00 53.64  ?  158  ILE A O   1 
ATOM   877   C CB  . ILE A  1  158 ? -57.347 23.488  109.320 1.00 50.69  ?  158  ILE A CB  1 
ATOM   878   C CG1 . ILE A  1  158 ? -56.214 23.139  108.355 1.00 50.29  ?  158  ILE A CG1 1 
ATOM   879   C CG2 . ILE A  1  158 ? -57.528 24.999  109.431 1.00 49.51  ?  158  ILE A CG2 1 
ATOM   880   C CD1 . ILE A  1  158 ? -56.574 23.341  106.900 1.00 49.49  ?  158  ILE A CD1 1 
ATOM   881   N N   . PRO A  1  159 ? -57.827 24.038  112.747 1.00 52.72  ?  159  PRO A N   1 
ATOM   882   C CA  . PRO A  1  159 ? -58.828 24.359  113.767 1.00 58.58  ?  159  PRO A CA  1 
ATOM   883   C C   . PRO A  1  159 ? -59.920 25.244  113.196 1.00 62.02  ?  159  PRO A C   1 
ATOM   884   O O   . PRO A  1  159 ? -59.673 26.044  112.278 1.00 59.13  ?  159  PRO A O   1 
ATOM   885   C CB  . PRO A  1  159 ? -58.014 25.096  114.846 1.00 58.96  ?  159  PRO A CB  1 
ATOM   886   C CG  . PRO A  1  159 ? -56.811 25.613  114.138 1.00 53.40  ?  159  PRO A CG  1 
ATOM   887   C CD  . PRO A  1  159 ? -56.523 24.671  113.006 1.00 49.41  ?  159  PRO A CD  1 
ATOM   888   N N   . PRO A  1  160 ? -61.154 25.129  113.702 1.00 58.59  ?  160  PRO A N   1 
ATOM   889   C CA  . PRO A  1  160 ? -62.204 26.071  113.286 1.00 63.10  ?  160  PRO A CA  1 
ATOM   890   C C   . PRO A  1  160 ? -61.944 27.489  113.754 1.00 64.41  ?  160  PRO A C   1 
ATOM   891   O O   . PRO A  1  160 ? -62.484 28.428  113.158 1.00 62.16  ?  160  PRO A O   1 
ATOM   892   C CB  . PRO A  1  160 ? -63.476 25.502  113.933 1.00 67.28  ?  160  PRO A CB  1 
ATOM   893   C CG  . PRO A  1  160 ? -63.101 24.149  114.459 1.00 64.25  ?  160  PRO A CG  1 
ATOM   894   C CD  . PRO A  1  160 ? -61.636 24.205  114.738 1.00 60.54  ?  160  PRO A CD  1 
ATOM   895   N N   . GLU A  1  161 ? -61.145 27.667  114.809 1.00 65.65  ?  161  GLU A N   1 
ATOM   896   C CA  . GLU A  1  161 ? -60.845 28.995  115.332 1.00 65.99  ?  161  GLU A CA  1 
ATOM   897   C C   . GLU A  1  161 ? -60.179 29.898  114.301 1.00 58.46  ?  161  GLU A C   1 
ATOM   898   O O   . GLU A  1  161 ? -60.271 31.123  114.423 1.00 57.00  ?  161  GLU A O   1 
ATOM   899   C CB  . GLU A  1  161 ? -59.957 28.868  116.570 1.00 67.68  ?  161  GLU A CB  1 
ATOM   900   C CG  . GLU A  1  161 ? -60.716 28.520  117.835 1.00 71.34  ?  161  GLU A CG  1 
ATOM   901   C CD  . GLU A  1  161 ? -60.925 27.022  118.022 1.00 69.03  ?  161  GLU A CD  1 
ATOM   902   O OE1 . GLU A  1  161 ? -60.689 26.245  117.069 1.00 65.83  ?  161  GLU A OE1 1 
ATOM   903   O OE2 . GLU A  1  161 ? -61.323 26.619  119.137 1.00 69.74  -1 161  GLU A OE2 1 
ATOM   904   N N   . LEU A  1  162 ? -59.521 29.330  113.285 1.00 64.88  ?  162  LEU A N   1 
ATOM   905   C CA  . LEU A  1  162 ? -58.951 30.150  112.222 1.00 58.20  ?  162  LEU A CA  1 
ATOM   906   C C   . LEU A  1  162 ? -60.004 31.011  111.542 1.00 58.45  ?  162  LEU A C   1 
ATOM   907   O O   . LEU A  1  162 ? -59.670 32.068  110.997 1.00 54.67  ?  162  LEU A O   1 
ATOM   908   C CB  . LEU A  1  162 ? -58.252 29.269  111.186 1.00 53.23  ?  162  LEU A CB  1 
ATOM   909   C CG  . LEU A  1  162 ? -56.939 28.604  111.606 1.00 50.40  ?  162  LEU A CG  1 
ATOM   910   C CD1 . LEU A  1  162 ? -56.114 28.241  110.378 1.00 45.11  ?  162  LEU A CD1 1 
ATOM   911   C CD2 . LEU A  1  162 ? -56.145 29.497  112.554 1.00 50.27  ?  162  LEU A CD2 1 
ATOM   912   N N   . GLY A  1  163 ? -61.268 30.593  111.582 1.00 58.83  ?  163  GLY A N   1 
ATOM   913   C CA  . GLY A  1  163 ? -62.345 31.345  110.971 1.00 58.78  ?  163  GLY A CA  1 
ATOM   914   C C   . GLY A  1  163 ? -62.634 32.681  111.622 1.00 58.89  ?  163  GLY A C   1 
ATOM   915   O O   . GLY A  1  163 ? -63.333 33.501  111.017 1.00 57.28  ?  163  GLY A O   1 
ATOM   916   N N   . LYS A  1  164 ? -62.117 32.927  112.825 1.00 56.75  ?  164  LYS A N   1 
ATOM   917   C CA  . LYS A  1  164 ? -62.376 34.177  113.525 1.00 56.44  ?  164  LYS A CA  1 
ATOM   918   C C   . LYS A  1  164 ? -61.244 35.187  113.375 1.00 52.55  ?  164  LYS A C   1 
ATOM   919   O O   . LYS A  1  164 ? -61.214 36.181  114.107 1.00 52.30  ?  164  LYS A O   1 
ATOM   920   C CB  . LYS A  1  164 ? -62.673 33.909  115.003 1.00 60.82  ?  164  LYS A CB  1 
ATOM   921   C CG  . LYS A  1  164 ? -61.499 33.493  115.860 1.00 62.99  ?  164  LYS A CG  1 
ATOM   922   C CD  . LYS A  1  164 ? -61.999 32.667  117.037 1.00 68.00  ?  164  LYS A CD  1 
ATOM   923   C CE  . LYS A  1  164 ? -61.030 32.719  118.199 1.00 70.45  ?  164  LYS A CE  1 
ATOM   924   N NZ  . LYS A  1  164 ? -61.630 32.180  119.449 1.00 73.65  ?  164  LYS A NZ  1 
ATOM   925   N N   . LEU A  1  165 ? -60.317 34.956  112.441 1.00 62.56  ?  165  LEU A N   1 
ATOM   926   C CA  . LEU A  1  165 ? -59.304 35.943  112.061 1.00 58.23  ?  165  LEU A CA  1 
ATOM   927   C C   . LEU A  1  165 ? -59.923 36.910  111.052 1.00 55.65  ?  165  LEU A C   1 
ATOM   928   O O   . LEU A  1  165 ? -59.649 36.883  109.850 1.00 53.00  ?  165  LEU A O   1 
ATOM   929   C CB  . LEU A  1  165 ? -58.074 35.261  111.485 1.00 54.68  ?  165  LEU A CB  1 
ATOM   930   C CG  . LEU A  1  165 ? -57.207 34.429  112.424 1.00 55.55  ?  165  LEU A CG  1 
ATOM   931   C CD1 . LEU A  1  165 ? -56.258 33.568  111.608 1.00 51.55  ?  165  LEU A CD1 1 
ATOM   932   C CD2 . LEU A  1  165 ? -56.442 35.332  113.364 1.00 55.81  ?  165  LEU A CD2 1 
ATOM   933   N N   . SER A  1  166 ? -60.789 37.782  111.571 1.00 63.18  ?  166  SER A N   1 
ATOM   934   C CA  . SER A  1  166 ? -61.636 38.609  110.720 1.00 61.56  ?  166  SER A CA  1 
ATOM   935   C C   . SER A  1  166 ? -60.852 39.600  109.875 1.00 57.92  ?  166  SER A C   1 
ATOM   936   O O   . SER A  1  166 ? -61.427 40.183  108.951 1.00 56.90  ?  166  SER A O   1 
ATOM   937   C CB  . SER A  1  166 ? -62.646 39.366  111.576 1.00 63.06  ?  166  SER A CB  1 
ATOM   938   O OG  . SER A  1  166 ? -61.972 40.194  112.509 1.00 62.58  ?  166  SER A OG  1 
ATOM   939   N N   . ASN A  1  167 ? -59.573 39.816  110.164 1.00 60.01  ?  167  ASN A N   1 
ATOM   940   C CA  . ASN A  1  167 ? -58.769 40.747  109.392 1.00 57.13  ?  167  ASN A CA  1 
ATOM   941   C C   . ASN A  1  167 ? -57.869 40.060  108.376 1.00 55.62  ?  167  ASN A C   1 
ATOM   942   O O   . ASN A  1  167 ? -57.133 40.746  107.661 1.00 53.92  ?  167  ASN A O   1 
ATOM   943   C CB  . ASN A  1  167 ? -57.918 41.604  110.330 1.00 56.64  ?  167  ASN A CB  1 
ATOM   944   C CG  . ASN A  1  167 ? -58.638 42.852  110.784 1.00 56.92  ?  167  ASN A CG  1 
ATOM   945   O OD1 . ASN A  1  167 ? -59.148 43.620  109.966 1.00 55.85  ?  167  ASN A OD1 1 
ATOM   946   N ND2 . ASN A  1  167 ? -58.690 43.063  112.096 1.00 58.67  ?  167  ASN A ND2 1 
ATOM   947   N N   . LEU A  1  168 ? -57.913 38.733  108.288 1.00 55.48  ?  168  LEU A N   1 
ATOM   948   C CA  . LEU A  1  168 ? -56.983 38.009  107.434 1.00 54.10  ?  168  LEU A CA  1 
ATOM   949   C C   . LEU A  1  168 ? -57.212 38.339  105.964 1.00 53.60  ?  168  LEU A C   1 
ATOM   950   O O   . LEU A  1  168 ? -58.349 38.405  105.487 1.00 54.81  ?  168  LEU A O   1 
ATOM   951   C CB  . LEU A  1  168 ? -57.119 36.505  107.662 1.00 55.15  ?  168  LEU A CB  1 
ATOM   952   C CG  . LEU A  1  168 ? -55.899 35.659  107.294 1.00 53.08  ?  168  LEU A CG  1 
ATOM   953   C CD1 . LEU A  1  168 ? -54.802 35.821  108.341 1.00 52.18  ?  168  LEU A CD1 1 
ATOM   954   C CD2 . LEU A  1  168 ? -56.284 34.194  107.112 1.00 53.69  ?  168  LEU A CD2 1 
ATOM   955   N N   . ASP A  1  169 ? -56.112 38.549  105.247 1.00 55.31  ?  169  ASP A N   1 
ATOM   956   C CA  . ASP A  1  169 ? -56.127 38.794  103.813 1.00 55.84  ?  169  ASP A CA  1 
ATOM   957   C C   . ASP A  1  169 ? -55.559 37.633  103.002 1.00 56.60  ?  169  ASP A C   1 
ATOM   958   O O   . ASP A  1  169 ? -56.051 37.355  101.905 1.00 58.20  ?  169  ASP A O   1 
ATOM   959   C CB  . ASP A  1  169 ? -55.350 40.086  103.515 1.00 55.24  ?  169  ASP A CB  1 
ATOM   960   C CG  . ASP A  1  169 ? -54.768 40.119  102.127 1.00 56.50  ?  169  ASP A CG  1 
ATOM   961   O OD1 . ASP A  1  169 ? -55.499 39.776  101.173 1.00 57.95  -1 169  ASP A OD1 1 
ATOM   962   O OD2 . ASP A  1  169 ? -53.588 40.522  101.990 1.00 56.67  ?  169  ASP A OD2 1 
ATOM   963   N N   . THR A  1  170 ? -54.571 36.919  103.535 1.00 52.19  ?  170  THR A N   1 
ATOM   964   C CA  . THR A  1  170 ? -53.941 35.815  102.828 1.00 52.85  ?  170  THR A CA  1 
ATOM   965   C C   . THR A  1  170 ? -53.699 34.666  103.798 1.00 51.38  ?  170  THR A C   1 
ATOM   966   O O   . THR A  1  170 ? -53.156 34.877  104.887 1.00 50.14  ?  170  THR A O   1 
ATOM   967   C CB  . THR A  1  170 ? -52.623 36.272  102.189 1.00 54.08  ?  170  THR A CB  1 
ATOM   968   O OG1 . THR A  1  170 ? -52.903 37.193  101.128 1.00 55.89  ?  170  THR A OG1 1 
ATOM   969   C CG2 . THR A  1  170 ? -51.853 35.089  101.637 1.00 55.54  ?  170  THR A CG2 1 
ATOM   970   N N   . LEU A  1  171 ? -54.095 33.454  103.406 1.00 49.49  ?  171  LEU A N   1 
ATOM   971   C CA  . LEU A  1  171 ? -53.906 32.261  104.224 1.00 48.42  ?  171  LEU A CA  1 
ATOM   972   C C   . LEU A  1  171 ? -53.144 31.221  103.415 1.00 49.12  ?  171  LEU A C   1 
ATOM   973   O O   . LEU A  1  171 ? -53.627 30.768  102.371 1.00 50.85  ?  171  LEU A O   1 
ATOM   974   C CB  . LEU A  1  171 ? -55.246 31.693  104.695 1.00 49.20  ?  171  LEU A CB  1 
ATOM   975   C CG  . LEU A  1  171 ? -55.185 30.382  105.482 1.00 49.07  ?  171  LEU A CG  1 
ATOM   976   C CD1 . LEU A  1  171 ? -54.403 30.565  106.773 1.00 48.11  ?  171  LEU A CD1 1 
ATOM   977   C CD2 . LEU A  1  171 ? -56.582 29.859  105.762 1.00 51.48  ?  171  LEU A CD2 1 
ATOM   978   N N   . HIS A  1  172 ? -51.963 30.839  103.902 1.00 50.59  ?  172  HIS A N   1 
ATOM   979   C CA  . HIS A  1  172 ? -51.099 29.874  103.229 1.00 52.08  ?  172  HIS A CA  1 
ATOM   980   C C   . HIS A  1  172 ? -50.767 28.741  104.190 1.00 50.77  ?  172  HIS A C   1 
ATOM   981   O O   . HIS A  1  172 ? -50.124 28.971  105.221 1.00 49.79  ?  172  HIS A O   1 
ATOM   982   C CB  . HIS A  1  172 ? -49.813 30.541  102.731 1.00 54.41  ?  172  HIS A CB  1 
ATOM   983   C CG  . HIS A  1  172 ? -50.016 31.453  101.561 1.00 57.19  ?  172  HIS A CG  1 
ATOM   984   N ND1 . HIS A  1  172 ? -49.017 32.265  101.068 1.00 60.41  ?  172  HIS A ND1 1 
ATOM   985   C CD2 . HIS A  1  172 ? -51.103 31.681  100.786 1.00 57.91  ?  172  HIS A CD2 1 
ATOM   986   C CE1 . HIS A  1  172 ? -49.479 32.951  100.037 1.00 62.74  ?  172  HIS A CE1 1 
ATOM   987   N NE2 . HIS A  1  172 ? -50.742 32.615  99.845  1.00 61.19  ?  172  HIS A NE2 1 
ATOM   988   N N   . LEU A  1  173 ? -51.194 27.523  103.852 1.00 51.88  ?  173  LEU A N   1 
ATOM   989   C CA  . LEU A  1  173 ? -50.931 26.316  104.639 1.00 51.30  ?  173  LEU A CA  1 
ATOM   990   C C   . LEU A  1  173 ? -50.455 25.199  103.727 1.00 52.97  ?  173  LEU A C   1 
ATOM   991   O O   . LEU A  1  173 ? -50.887 24.047  103.819 1.00 53.08  ?  173  LEU A O   1 
ATOM   992   C CB  . LEU A  1  173 ? -52.162 25.875  105.428 1.00 50.86  ?  173  LEU A CB  1 
ATOM   993   C CG  . LEU A  1  173 ? -52.652 26.819  106.530 1.00 50.35  ?  173  LEU A CG  1 
ATOM   994   C CD1 . LEU A  1  173 ? -54.099 26.525  106.885 1.00 51.95  ?  173  LEU A CD1 1 
ATOM   995   C CD2 . LEU A  1  173 ? -51.764 26.720  107.758 1.00 50.00  ?  173  LEU A CD2 1 
ATOM   996   N N   . VAL A  1  174 ? -49.535 25.544  102.839 1.00 53.74  ?  174  VAL A N   1 
ATOM   997   C CA  . VAL A  1  174 ? -49.180 24.739  101.677 1.00 56.47  ?  174  VAL A CA  1 
ATOM   998   C C   . VAL A  1  174 ? -48.112 23.716  102.025 1.00 56.95  ?  174  VAL A C   1 
ATOM   999   O O   . VAL A  1  174 ? -47.252 23.940  102.882 1.00 56.41  ?  174  VAL A O   1 
ATOM   1000  C CB  . VAL A  1  174 ? -48.706 25.652  100.531 1.00 60.07  ?  174  VAL A CB  1 
ATOM   1001  C CG1 . VAL A  1  174 ? -48.763 24.908  99.255  1.00 63.26  ?  174  VAL A CG1 1 
ATOM   1002  C CG2 . VAL A  1  174 ? -49.576 26.891  100.454 1.00 59.47  ?  174  VAL A CG2 1 
ATOM   1003  N N   . GLU A  1  175 ? -48.168 22.578  101.328 1.00 56.31  ?  175  GLU A N   1 
ATOM   1004  C CA  . GLU A  1  175 ? -47.114 21.564  101.361 1.00 57.38  ?  175  GLU A CA  1 
ATOM   1005  C C   . GLU A  1  175 ? -46.849 21.081  102.785 1.00 55.33  ?  175  GLU A C   1 
ATOM   1006  O O   . GLU A  1  175 ? -45.711 21.048  103.259 1.00 55.90  ?  175  GLU A O   1 
ATOM   1007  C CB  . GLU A  1  175 ? -45.838 22.084  100.702 1.00 60.39  ?  175  GLU A CB  1 
ATOM   1008  C CG  . GLU A  1  175 ? -45.930 22.125  99.196  1.00 63.61  ?  175  GLU A CG  1 
ATOM   1009  C CD  . GLU A  1  175 ? -44.596 22.380  98.557  1.00 67.09  ?  175  GLU A CD  1 
ATOM   1010  O OE1 . GLU A  1  175 ? -43.567 22.100  99.208  1.00 66.70  ?  175  GLU A OE1 1 
ATOM   1011  O OE2 . GLU A  1  175 ? -44.573 22.856  97.405  1.00 70.45  -1 175  GLU A OE2 1 
ATOM   1012  N N   . ASN A  1  176 ? -47.929 20.733  103.474 1.00 59.61  ?  176  ASN A N   1 
ATOM   1013  C CA  . ASN A  1  176 ? -47.928 20.120  104.795 1.00 58.62  ?  176  ASN A CA  1 
ATOM   1014  C C   . ASN A  1  176 ? -48.645 18.771  104.703 1.00 59.14  ?  176  ASN A C   1 
ATOM   1015  O O   . ASN A  1  176 ? -48.982 18.298  103.613 1.00 60.08  ?  176  ASN A O   1 
ATOM   1016  C CB  . ASN A  1  176 ? -48.573 21.048  105.824 1.00 57.00  ?  176  ASN A CB  1 
ATOM   1017  C CG  . ASN A  1  176 ? -47.593 22.050  106.388 1.00 56.68  ?  176  ASN A CG  1 
ATOM   1018  O OD1 . ASN A  1  176 ? -46.792 21.720  107.262 1.00 57.11  ?  176  ASN A OD1 1 
ATOM   1019  N ND2 . ASN A  1  176 ? -47.653 23.286  105.895 1.00 56.31  ?  176  ASN A ND2 1 
ATOM   1020  N N   . LYS A  1  177 ? -48.866 18.139  105.851 1.00 59.67  ?  177  LYS A N   1 
ATOM   1021  C CA  . LYS A  1  177 ? -49.589 16.873  105.900 1.00 60.65  ?  177  LYS A CA  1 
ATOM   1022  C C   . LYS A  1  177 ? -50.824 16.984  106.790 1.00 60.86  ?  177  LYS A C   1 
ATOM   1023  O O   . LYS A  1  177 ? -51.159 16.069  107.550 1.00 62.10  ?  177  LYS A O   1 
ATOM   1024  C CB  . LYS A  1  177 ? -48.676 15.740  106.366 1.00 62.18  ?  177  LYS A CB  1 
ATOM   1025  C CG  . LYS A  1  177 ? -47.543 15.446  105.397 1.00 63.50  ?  177  LYS A CG  1 
ATOM   1026  C CD  . LYS A  1  177 ? -48.057 14.879  104.074 1.00 63.84  ?  177  LYS A CD  1 
ATOM   1027  C CE  . LYS A  1  177 ? -47.131 15.233  102.895 1.00 64.08  ?  177  LYS A CE  1 
ATOM   1028  N NZ  . LYS A  1  177 ? -46.886 16.713  102.719 1.00 63.04  ?  177  LYS A NZ  1 
ATOM   1029  N N   . LEU A  1  178 ? -51.529 18.110  106.678 1.00 57.60  ?  178  LEU A N   1 
ATOM   1030  C CA  . LEU A  1  178 ? -52.767 18.314  107.419 1.00 58.17  ?  178  LEU A CA  1 
ATOM   1031  C C   . LEU A  1  178 ? -53.879 17.426  106.865 1.00 59.74  ?  178  LEU A C   1 
ATOM   1032  O O   . LEU A  1  178 ? -54.040 17.296  105.649 1.00 59.73  ?  178  LEU A O   1 
ATOM   1033  C CB  . LEU A  1  178 ? -53.189 19.785  107.353 1.00 57.08  ?  178  LEU A CB  1 
ATOM   1034  C CG  . LEU A  1  178 ? -52.147 20.860  107.677 1.00 55.46  ?  178  LEU A CG  1 
ATOM   1035  C CD1 . LEU A  1  178 ? -52.683 22.243  107.346 1.00 54.59  ?  178  LEU A CD1 1 
ATOM   1036  C CD2 . LEU A  1  178 ? -51.713 20.790  109.133 1.00 56.02  ?  178  LEU A CD2 1 
ATOM   1037  N N   . ASN A  1  179 ? -54.655 16.819  107.768 1.00 64.25  ?  179  ASN A N   1 
ATOM   1038  C CA  . ASN A  1  179 ? -55.730 15.906  107.399 1.00 66.15  ?  179  ASN A CA  1 
ATOM   1039  C C   . ASN A  1  179 ? -57.021 16.319  108.092 1.00 68.05  ?  179  ASN A C   1 
ATOM   1040  O O   . ASN A  1  179 ? -57.026 17.123  109.025 1.00 68.25  ?  179  ASN A O   1 
ATOM   1041  C CB  . ASN A  1  179 ? -55.394 14.444  107.750 1.00 67.17  ?  179  ASN A CB  1 
ATOM   1042  C CG  . ASN A  1  179 ? -55.085 14.239  109.229 1.00 67.40  ?  179  ASN A CG  1 
ATOM   1043  O OD1 . ASN A  1  179 ? -54.836 15.197  109.963 1.00 66.82  ?  179  ASN A OD1 1 
ATOM   1044  N ND2 . ASN A  1  179 ? -55.090 12.978  109.671 1.00 68.22  ?  179  ASN A ND2 1 
ATOM   1045  N N   . GLY A  1  180 ? -58.119 15.744  107.631 1.00 60.68  ?  180  GLY A N   1 
ATOM   1046  C CA  . GLY A  1  180 ? -59.442 16.103  108.091 1.00 63.31  ?  180  GLY A CA  1 
ATOM   1047  C C   . GLY A  1  180 ? -60.186 16.900  107.035 1.00 63.96  ?  180  GLY A C   1 
ATOM   1048  O O   . GLY A  1  180 ? -59.720 17.091  105.910 1.00 62.19  ?  180  GLY A O   1 
ATOM   1049  N N   . SER A  1  181 ? -61.373 17.365  107.418 1.00 64.09  ?  181  SER A N   1 
ATOM   1050  C CA  . SER A  1  181 ? -62.195 18.200  106.553 1.00 65.69  ?  181  SER A CA  1 
ATOM   1051  C C   . SER A  1  181 ? -61.954 19.673  106.853 1.00 65.48  ?  181  SER A C   1 
ATOM   1052  O O   . SER A  1  181 ? -61.657 20.056  107.987 1.00 65.82  ?  181  SER A O   1 
ATOM   1053  C CB  . SER A  1  181 ? -63.680 17.877  106.732 1.00 69.88  ?  181  SER A CB  1 
ATOM   1054  O OG  . SER A  1  181 ? -63.995 16.595  106.214 1.00 69.86  ?  181  SER A OG  1 
ATOM   1055  N N   . ILE A  1  182 ? -62.080 20.500  105.820 1.00 59.83  ?  182  ILE A N   1 
ATOM   1056  C CA  . ILE A  1  182 ? -61.954 21.946  105.988 1.00 59.61  ?  182  ILE A CA  1 
ATOM   1057  C C   . ILE A  1  182 ? -63.113 22.416  106.857 1.00 64.98  ?  182  ILE A C   1 
ATOM   1058  O O   . ILE A  1  182 ? -64.277 22.163  106.515 1.00 68.80  ?  182  ILE A O   1 
ATOM   1059  C CB  . ILE A  1  182 ? -61.937 22.676  104.635 1.00 58.02  ?  182  ILE A CB  1 
ATOM   1060  C CG1 . ILE A  1  182 ? -60.719 22.261  103.813 1.00 53.78  ?  182  ILE A CG1 1 
ATOM   1061  C CG2 . ILE A  1  182 ? -61.947 24.181  104.836 1.00 57.68  ?  182  ILE A CG2 1 
ATOM   1062  C CD1 . ILE A  1  182 ? -60.686 22.889  102.447 1.00 53.09  ?  182  ILE A CD1 1 
ATOM   1063  N N   . PRO A  1  183 ? -62.851 23.080  107.982 1.00 58.99  ?  183  PRO A N   1 
ATOM   1064  C CA  . PRO A  1  183 ? -63.955 23.542  108.832 1.00 65.11  ?  183  PRO A CA  1 
ATOM   1065  C C   . PRO A  1  183 ? -64.853 24.512  108.084 1.00 66.81  ?  183  PRO A C   1 
ATOM   1066  O O   . PRO A  1  183 ? -64.391 25.327  107.285 1.00 62.61  ?  183  PRO A O   1 
ATOM   1067  C CB  . PRO A  1  183 ? -63.244 24.228  110.005 1.00 65.05  ?  183  PRO A CB  1 
ATOM   1068  C CG  . PRO A  1  183 ? -61.846 23.730  109.962 1.00 59.01  ?  183  PRO A CG  1 
ATOM   1069  C CD  . PRO A  1  183 ? -61.537 23.453  108.527 1.00 54.96  ?  183  PRO A CD  1 
ATOM   1070  N N   . SER A  1  184 ? -66.155 24.416  108.352 1.00 72.30  ?  184  SER A N   1 
ATOM   1071  C CA  . SER A  1  184 ? -67.101 25.340  107.737 1.00 70.72  ?  184  SER A CA  1 
ATOM   1072  C C   . SER A  1  184 ? -66.839 26.779  108.165 1.00 68.65  ?  184  SER A C   1 
ATOM   1073  O O   . SER A  1  184 ? -67.150 27.714  107.416 1.00 66.47  ?  184  SER A O   1 
ATOM   1074  C CB  . SER A  1  184 ? -68.528 24.932  108.093 1.00 72.91  ?  184  SER A CB  1 
ATOM   1075  O OG  . SER A  1  184 ? -68.655 23.519  108.107 1.00 75.11  ?  184  SER A OG  1 
ATOM   1076  N N   . GLU A  1  185 ? -66.258 26.974  109.355 1.00 69.97  ?  185  GLU A N   1 
ATOM   1077  C CA  . GLU A  1  185 ? -66.015 28.310  109.892 1.00 68.25  ?  185  GLU A CA  1 
ATOM   1078  C C   . GLU A  1  185 ? -65.011 29.105  109.065 1.00 63.85  ?  185  GLU A C   1 
ATOM   1079  O O   . GLU A  1  185 ? -64.923 30.327  109.233 1.00 62.03  ?  185  GLU A O   1 
ATOM   1080  C CB  . GLU A  1  185 ? -65.529 28.211  111.340 1.00 70.63  ?  185  GLU A CB  1 
ATOM   1081  C CG  . GLU A  1  185 ? -66.577 27.708  112.322 1.00 73.56  ?  185  GLU A CG  1 
ATOM   1082  C CD  . GLU A  1  185 ? -66.776 26.201  112.257 1.00 75.97  ?  185  GLU A CD  1 
ATOM   1083  O OE1 . GLU A  1  185 ? -66.007 25.523  111.541 1.00 76.22  ?  185  GLU A OE1 1 
ATOM   1084  O OE2 . GLU A  1  185 ? -67.705 25.695  112.922 1.00 76.92  -1 185  GLU A OE2 1 
ATOM   1085  N N   . ILE A  1  186 ? -64.256 28.451  108.178 1.00 69.41  ?  186  ILE A N   1 
ATOM   1086  C CA  . ILE A  1  186 ? -63.350 29.189  107.303 1.00 64.34  ?  186  ILE A CA  1 
ATOM   1087  C C   . ILE A  1  186 ? -64.137 30.160  106.432 1.00 64.11  ?  186  ILE A C   1 
ATOM   1088  O O   . ILE A  1  186 ? -63.619 31.210  106.028 1.00 61.30  ?  186  ILE A O   1 
ATOM   1089  C CB  . ILE A  1  186 ? -62.500 28.208  106.465 1.00 61.44  ?  186  ILE A CB  1 
ATOM   1090  C CG1 . ILE A  1  186 ? -61.775 27.221  107.386 1.00 61.64  ?  186  ILE A CG1 1 
ATOM   1091  C CG2 . ILE A  1  186 ? -61.499 28.949  105.584 1.00 56.53  ?  186  ILE A CG2 1 
ATOM   1092  C CD1 . ILE A  1  186 ? -60.929 27.877  108.463 1.00 60.37  ?  186  ILE A CD1 1 
ATOM   1093  N N   . GLY A  1  187 ? -65.407 29.851  106.160 1.00 64.29  ?  187  GLY A N   1 
ATOM   1094  C CA  . GLY A  1  187 ? -66.278 30.736  105.409 1.00 64.20  ?  187  GLY A CA  1 
ATOM   1095  C C   . GLY A  1  187 ? -66.596 32.056  106.080 1.00 63.11  ?  187  GLY A C   1 
ATOM   1096  O O   . GLY A  1  187 ? -67.335 32.862  105.504 1.00 62.58  ?  187  GLY A O   1 
ATOM   1097  N N   . ARG A  1  188 ? -66.080 32.290  107.287 1.00 64.51  ?  188  ARG A N   1 
ATOM   1098  C CA  . ARG A  1  188 ? -66.266 33.556  107.985 1.00 63.23  ?  188  ARG A CA  1 
ATOM   1099  C C   . ARG A  1  188 ? -65.242 34.611  107.588 1.00 59.51  ?  188  ARG A C   1 
ATOM   1100  O O   . ARG A  1  188 ? -65.369 35.764  108.019 1.00 58.16  ?  188  ARG A O   1 
ATOM   1101  C CB  . ARG A  1  188 ? -66.201 33.333  109.495 1.00 65.28  ?  188  ARG A CB  1 
ATOM   1102  C CG  . ARG A  1  188 ? -67.382 32.580  110.072 1.00 68.50  ?  188  ARG A CG  1 
ATOM   1103  C CD  . ARG A  1  188 ? -67.306 32.550  111.591 1.00 70.34  ?  188  ARG A CD  1 
ATOM   1104  N NE  . ARG A  1  188 ? -68.462 31.882  112.173 1.00 72.61  ?  188  ARG A NE  1 
ATOM   1105  C CZ  . ARG A  1  188 ? -69.021 32.224  113.324 1.00 73.18  ?  188  ARG A CZ  1 
ATOM   1106  N NH1 . ARG A  1  188 ? -68.545 33.220  114.055 1.00 72.17  ?  188  ARG A NH1 1 
ATOM   1107  N NH2 . ARG A  1  188 ? -70.088 31.554  113.749 1.00 74.51  ?  188  ARG A NH2 1 
ATOM   1108  N N   . LEU A  1  189 ? -64.236 34.247  106.789 1.00 63.87  ?  189  LEU A N   1 
ATOM   1109  C CA  . LEU A  1  189 ? -63.130 35.142  106.443 1.00 60.21  ?  189  LEU A CA  1 
ATOM   1110  C C   . LEU A  1  189 ? -63.562 36.045  105.289 1.00 59.07  ?  189  LEU A C   1 
ATOM   1111  O O   . LEU A  1  189 ? -63.158 35.886  104.135 1.00 58.34  ?  189  LEU A O   1 
ATOM   1112  C CB  . LEU A  1  189 ? -61.885 34.339  106.092 1.00 58.69  ?  189  LEU A CB  1 
ATOM   1113  C CG  . LEU A  1  189 ? -61.377 33.384  107.169 1.00 59.64  ?  189  LEU A CG  1 
ATOM   1114  C CD1 . LEU A  1  189 ? -60.077 32.770  106.736 1.00 56.03  ?  189  LEU A CD1 1 
ATOM   1115  C CD2 . LEU A  1  189 ? -61.193 34.107  108.484 1.00 60.23  ?  189  LEU A CD2 1 
ATOM   1116  N N   . THR A  1  190 ? -64.398 37.031  105.621 1.00 62.76  ?  190  THR A N   1 
ATOM   1117  C CA  . THR A  1  190 ? -64.990 37.879  104.593 1.00 62.42  ?  190  THR A CA  1 
ATOM   1118  C C   . THR A  1  190 ? -63.977 38.794  103.915 1.00 59.77  ?  190  THR A C   1 
ATOM   1119  O O   . THR A  1  190 ? -64.273 39.327  102.840 1.00 59.98  ?  190  THR A O   1 
ATOM   1120  C CB  . THR A  1  190 ? -66.115 38.721  105.190 1.00 63.09  ?  190  THR A CB  1 
ATOM   1121  O OG1 . THR A  1  190 ? -65.605 39.477  106.295 1.00 61.56  ?  190  THR A OG1 1 
ATOM   1122  C CG2 . THR A  1  190 ? -67.245 37.822  105.668 1.00 66.06  ?  190  THR A CG2 1 
ATOM   1123  N N   . LYS A  1  191 ? -62.802 38.998  104.509 1.00 61.92  ?  191  LYS A N   1 
ATOM   1124  C CA  . LYS A  1  191 ? -61.795 39.892  103.948 1.00 59.68  ?  191  LYS A CA  1 
ATOM   1125  C C   . LYS A  1  191 ? -60.676 39.160  103.213 1.00 59.09  ?  191  LYS A C   1 
ATOM   1126  O O   . LYS A  1  191 ? -59.795 39.816  102.647 1.00 57.86  ?  191  LYS A O   1 
ATOM   1127  C CB  . LYS A  1  191 ? -61.195 40.763  105.055 1.00 58.00  ?  191  LYS A CB  1 
ATOM   1128  C CG  . LYS A  1  191 ? -62.081 41.913  105.478 1.00 58.15  ?  191  LYS A CG  1 
ATOM   1129  C CD  . LYS A  1  191 ? -61.350 42.848  106.427 1.00 56.77  ?  191  LYS A CD  1 
ATOM   1130  C CE  . LYS A  1  191 ? -62.316 43.796  107.130 1.00 57.91  ?  191  LYS A CE  1 
ATOM   1131  N NZ  . LYS A  1  191 ? -61.645 44.613  108.184 1.00 58.27  ?  191  LYS A NZ  1 
ATOM   1132  N N   . VAL A  1  192 ? -60.687 37.824  103.209 1.00 55.60  ?  192  VAL A N   1 
ATOM   1133  C CA  . VAL A  1  192 ? -59.626 37.066  102.557 1.00 55.13  ?  192  VAL A CA  1 
ATOM   1134  C C   . VAL A  1  192 ? -59.718 37.240  101.044 1.00 56.54  ?  192  VAL A C   1 
ATOM   1135  O O   . VAL A  1  192 ? -60.807 37.420  100.476 1.00 58.43  ?  192  VAL A O   1 
ATOM   1136  C CB  . VAL A  1  192 ? -59.697 35.581  102.963 1.00 56.07  ?  192  VAL A CB  1 
ATOM   1137  C CG1 . VAL A  1  192 ? -60.704 34.816  102.108 1.00 58.84  ?  192  VAL A CG1 1 
ATOM   1138  C CG2 . VAL A  1  192 ? -58.334 34.946  102.879 1.00 54.36  ?  192  VAL A CG2 1 
ATOM   1139  N N   . THR A  1  193 ? -58.555 37.222  100.383 1.00 51.90  ?  193  THR A N   1 
ATOM   1140  C CA  . THR A  1  193 ? -58.482 37.276  98.928  1.00 54.21  ?  193  THR A CA  1 
ATOM   1141  C C   . THR A  1  193 ? -57.778 36.081  98.301  1.00 55.84  ?  193  THR A C   1 
ATOM   1142  O O   . THR A  1  193 ? -58.025 35.797  97.122  1.00 58.91  ?  193  THR A O   1 
ATOM   1143  C CB  . THR A  1  193 ? -57.769 38.558  98.466  1.00 53.64  ?  193  THR A CB  1 
ATOM   1144  O OG1 . THR A  1  193 ? -56.531 38.698  99.171  1.00 51.88  ?  193  THR A OG1 1 
ATOM   1145  C CG2 . THR A  1  193 ? -58.624 39.774  98.725  1.00 54.58  ?  193  THR A CG2 1 
ATOM   1146  N N   . GLU A  1  194 ? -56.916 35.382  99.042  1.00 51.82  ?  194  GLU A N   1 
ATOM   1147  C CA  . GLU A  1  194 ? -56.237 34.190  98.549  1.00 53.11  ?  194  GLU A CA  1 
ATOM   1148  C C   . GLU A  1  194 ? -56.230 33.116  99.625  1.00 50.72  ?  194  GLU A C   1 
ATOM   1149  O O   . GLU A  1  194 ? -55.869 33.388  100.774 1.00 48.04  ?  194  GLU A O   1 
ATOM   1150  C CB  . GLU A  1  194 ? -54.798 34.498  98.119  1.00 53.99  ?  194  GLU A CB  1 
ATOM   1151  C CG  . GLU A  1  194 ? -54.014 33.261  97.684  1.00 55.89  ?  194  GLU A CG  1 
ATOM   1152  C CD  . GLU A  1  194 ? -52.700 33.600  97.008  1.00 58.94  ?  194  GLU A CD  1 
ATOM   1153  O OE1 . GLU A  1  194 ? -52.723 34.068  95.849  1.00 62.45  ?  194  GLU A OE1 1 
ATOM   1154  O OE2 . GLU A  1  194 ? -51.641 33.399  97.638  1.00 58.20  -1 194  GLU A OE2 1 
ATOM   1155  N N   . ILE A  1  195 ? -56.614 31.900  99.249  1.00 52.15  ?  195  ILE A N   1 
ATOM   1156  C CA  . ILE A  1  195 ? -56.497 30.728  100.107 1.00 50.15  ?  195  ILE A CA  1 
ATOM   1157  C C   . ILE A  1  195 ? -55.687 29.684  99.352  1.00 51.44  ?  195  ILE A C   1 
ATOM   1158  O O   . ILE A  1  195 ? -55.986 29.381  98.190  1.00 54.73  ?  195  ILE A O   1 
ATOM   1159  C CB  . ILE A  1  195 ? -57.873 30.166  100.509 1.00 50.92  ?  195  ILE A CB  1 
ATOM   1160  C CG1 . ILE A  1  195 ? -58.617 31.156  101.405 1.00 50.62  ?  195  ILE A CG1 1 
ATOM   1161  C CG2 . ILE A  1  195 ? -57.718 28.830  101.217 1.00 49.76  ?  195  ILE A CG2 1 
ATOM   1162  C CD1 . ILE A  1  195 ? -60.041 30.751  101.721 1.00 53.14  ?  195  ILE A CD1 1 
ATOM   1163  N N   . ALA A  1  196 ? -54.652 29.154  100.000 1.00 53.20  ?  196  ALA A N   1 
ATOM   1164  C CA  . ALA A  1  196 ? -53.809 28.123  99.401  1.00 54.79  ?  196  ALA A CA  1 
ATOM   1165  C C   . ALA A  1  196 ? -53.535 27.062  100.458 1.00 52.13  ?  196  ALA A C   1 
ATOM   1166  O O   . ALA A  1  196 ? -52.809 27.324  101.424 1.00 50.12  ?  196  ALA A O   1 
ATOM   1167  C CB  . ALA A  1  196 ? -52.509 28.719  98.864  1.00 57.15  ?  196  ALA A CB  1 
ATOM   1168  N N   . ILE A  1  197 ? -54.146 25.883  100.297 1.00 54.96  ?  197  ILE A N   1 
ATOM   1169  C CA  . ILE A  1  197 ? -53.907 24.745  101.183 1.00 53.39  ?  197  ILE A CA  1 
ATOM   1170  C C   . ILE A  1  197 ? -53.519 23.500  100.389 1.00 55.04  ?  197  ILE A C   1 
ATOM   1171  O O   . ILE A  1  197 ? -53.768 22.373  100.832 1.00 54.61  ?  197  ILE A O   1 
ATOM   1172  C CB  . ILE A  1  197 ? -55.134 24.455  102.069 1.00 52.86  ?  197  ILE A CB  1 
ATOM   1173  C CG1 . ILE A  1  197 ? -55.929 25.725  102.339 1.00 52.85  ?  197  ILE A CG1 1 
ATOM   1174  C CG2 . ILE A  1  197 ? -54.708 23.868  103.406 1.00 51.50  ?  197  ILE A CG2 1 
ATOM   1175  C CD1 . ILE A  1  197 ? -57.205 25.458  103.078 1.00 54.24  ?  197  ILE A CD1 1 
ATOM   1176  N N   . TYR A  1  198 ? -52.916 23.677  99.216  1.00 52.16  ?  198  TYR A N   1 
ATOM   1177  C CA  . TYR A  1  198 ? -52.661 22.522  98.364  1.00 54.20  ?  198  TYR A CA  1 
ATOM   1178  C C   . TYR A  1  198 ? -51.470 21.706  98.868  1.00 53.44  ?  198  TYR A C   1 
ATOM   1179  O O   . TYR A  1  198 ? -50.687 22.143  99.719  1.00 52.04  ?  198  TYR A O   1 
ATOM   1180  C CB  . TYR A  1  198 ? -52.435 22.949  96.912  1.00 58.27  ?  198  TYR A CB  1 
ATOM   1181  C CG  . TYR A  1  198 ? -51.274 23.895  96.655  1.00 60.42  ?  198  TYR A CG  1 
ATOM   1182  C CD1 . TYR A  1  198 ? -51.451 25.271  96.696  1.00 61.04  ?  198  TYR A CD1 1 
ATOM   1183  C CD2 . TYR A  1  198 ? -50.015 23.410  96.336  1.00 62.30  ?  198  TYR A CD2 1 
ATOM   1184  C CE1 . TYR A  1  198 ? -50.403 26.137  96.436  1.00 63.98  ?  198  TYR A CE1 1 
ATOM   1185  C CE2 . TYR A  1  198 ? -48.964 24.267  96.065  1.00 65.26  ?  198  TYR A CE2 1 
ATOM   1186  C CZ  . TYR A  1  198 ? -49.162 25.630  96.122  1.00 66.44  ?  198  TYR A CZ  1 
ATOM   1187  O OH  . TYR A  1  198 ? -48.117 26.485  95.874  1.00 70.18  ?  198  TYR A OH  1 
ATOM   1188  N N   . ASP A  1  199 ? -51.342 20.499  98.309  1.00 60.39  ?  199  ASP A N   1 
ATOM   1189  C CA  . ASP A  1  199 ? -50.326 19.518  98.699  1.00 60.05  ?  199  ASP A CA  1 
ATOM   1190  C C   . ASP A  1  199 ? -50.428 19.169  100.186 1.00 57.45  ?  199  ASP A C   1 
ATOM   1191  O O   . ASP A  1  199 ? -49.500 19.372  100.974 1.00 56.64  ?  199  ASP A O   1 
ATOM   1192  C CB  . ASP A  1  199 ? -48.921 20.004  98.339  1.00 61.74  ?  199  ASP A CB  1 
ATOM   1193  C CG  . ASP A  1  199 ? -47.938 18.875  98.239  1.00 62.34  ?  199  ASP A CG  1 
ATOM   1194  O OD1 . ASP A  1  199 ? -48.234 17.801  98.804  1.00 60.94  ?  199  ASP A OD1 1 
ATOM   1195  O OD2 . ASP A  1  199 ? -46.875 19.061  97.608  1.00 64.44  -1 199  ASP A OD2 1 
ATOM   1196  N N   . ASN A  1  200 ? -51.583 18.615  100.550 1.00 60.58  ?  200  ASN A N   1 
ATOM   1197  C CA  . ASN A  1  200 ? -51.892 18.231  101.922 1.00 59.19  ?  200  ASN A CA  1 
ATOM   1198  C C   . ASN A  1  200 ? -52.660 16.911  101.888 1.00 60.28  ?  200  ASN A C   1 
ATOM   1199  O O   . ASN A  1  200 ? -52.725 16.231  100.858 1.00 61.65  ?  200  ASN A O   1 
ATOM   1200  C CB  . ASN A  1  200 ? -52.667 19.348  102.629 1.00 57.88  ?  200  ASN A CB  1 
ATOM   1201  C CG  . ASN A  1  200 ? -51.756 20.317  103.345 1.00 56.47  ?  200  ASN A CG  1 
ATOM   1202  O OD1 . ASN A  1  200 ? -51.271 20.034  104.437 1.00 55.89  ?  200  ASN A OD1 1 
ATOM   1203  N ND2 . ASN A  1  200 ? -51.513 21.467  102.730 1.00 56.40  ?  200  ASN A ND2 1 
ATOM   1204  N N   . LEU A  1  201 ? -53.240 16.538  103.026 1.00 55.67  ?  201  LEU A N   1 
ATOM   1205  C CA  . LEU A  1  201 ? -54.011 15.308  103.165 1.00 57.44  ?  201  LEU A CA  1 
ATOM   1206  C C   . LEU A  1  201 ? -55.456 15.615  103.539 1.00 56.43  ?  201  LEU A C   1 
ATOM   1207  O O   . LEU A  1  201 ? -56.091 14.884  104.301 1.00 57.81  ?  201  LEU A O   1 
ATOM   1208  C CB  . LEU A  1  201 ? -53.370 14.381  104.194 1.00 59.81  ?  201  LEU A CB  1 
ATOM   1209  C CG  . LEU A  1  201 ? -51.899 14.043  103.945 1.00 61.29  ?  201  LEU A CG  1 
ATOM   1210  C CD1 . LEU A  1  201 ? -51.298 13.293  105.122 1.00 63.72  ?  201  LEU A CD1 1 
ATOM   1211  C CD2 . LEU A  1  201 ? -51.773 13.234  102.676 1.00 62.70  ?  201  LEU A CD2 1 
ATOM   1212  N N   . LEU A  1  202 ? -55.987 16.714  103.008 1.00 56.24  ?  202  LEU A N   1 
ATOM   1213  C CA  . LEU A  1  202 ? -57.345 17.132  103.325 1.00 57.58  ?  202  LEU A CA  1 
ATOM   1214  C C   . LEU A  1  202 ? -58.362 16.158  102.734 1.00 59.88  ?  202  LEU A C   1 
ATOM   1215  O O   . LEU A  1  202 ? -58.159 15.582  101.660 1.00 60.20  ?  202  LEU A O   1 
ATOM   1216  C CB  . LEU A  1  202 ? -57.603 18.549  102.807 1.00 57.08  ?  202  LEU A CB  1 
ATOM   1217  C CG  . LEU A  1  202 ? -56.667 19.634  103.347 1.00 54.81  ?  202  LEU A CG  1 
ATOM   1218  C CD1 . LEU A  1  202 ? -57.099 21.020  102.892 1.00 54.71  ?  202  LEU A CD1 1 
ATOM   1219  C CD2 . LEU A  1  202 ? -56.595 19.565  104.856 1.00 54.70  ?  202  LEU A CD2 1 
ATOM   1220  N N   . THR A  1  203 ? -59.460 15.964  103.464 1.00 58.53  ?  203  THR A N   1 
ATOM   1221  C CA  . THR A  1  203 ? -60.523 15.039  103.096 1.00 60.96  ?  203  THR A CA  1 
ATOM   1222  C C   . THR A  1  203 ? -61.864 15.765  103.152 1.00 63.47  ?  203  THR A C   1 
ATOM   1223  O O   . THR A  1  203 ? -61.955 16.927  103.565 1.00 63.53  ?  203  THR A O   1 
ATOM   1224  C CB  . THR A  1  203 ? -60.546 13.810  104.020 1.00 61.73  ?  203  THR A CB  1 
ATOM   1225  O OG1 . THR A  1  203 ? -60.884 14.219  105.352 1.00 62.50  ?  203  THR A OG1 1 
ATOM   1226  C CG2 . THR A  1  203 ? -59.198 13.113  104.043 1.00 60.01  ?  203  THR A CG2 1 
ATOM   1227  N N   . GLY A  1  204 ? -62.915 15.064  102.735 1.00 63.17  ?  204  GLY A N   1 
ATOM   1228  C CA  . GLY A  1  204 ? -64.260 15.579  102.822 1.00 66.31  ?  204  GLY A CA  1 
ATOM   1229  C C   . GLY A  1  204 ? -64.579 16.629  101.778 1.00 67.08  ?  204  GLY A C   1 
ATOM   1230  O O   . GLY A  1  204 ? -63.781 16.921  100.881 1.00 65.00  ?  204  GLY A O   1 
ATOM   1231  N N   . PRO A  1  205 ? -65.769 17.214  101.876 1.00 63.67  ?  205  PRO A N   1 
ATOM   1232  C CA  . PRO A  1  205 ? -66.218 18.167  100.858 1.00 64.97  ?  205  PRO A CA  1 
ATOM   1233  C C   . PRO A  1  205 ? -65.605 19.549  101.031 1.00 63.56  ?  205  PRO A C   1 
ATOM   1234  O O   . PRO A  1  205 ? -65.058 19.900  102.078 1.00 62.42  ?  205  PRO A O   1 
ATOM   1235  C CB  . PRO A  1  205 ? -67.735 18.212  101.071 1.00 69.23  ?  205  PRO A CB  1 
ATOM   1236  C CG  . PRO A  1  205 ? -67.906 17.906  102.510 1.00 70.11  ?  205  PRO A CG  1 
ATOM   1237  C CD  . PRO A  1  205 ? -66.809 16.947  102.885 1.00 66.61  ?  205  PRO A CD  1 
ATOM   1238  N N   . ILE A  1  206 ? -65.698 20.330  99.962  1.00 64.96  ?  206  ILE A N   1 
ATOM   1239  C CA  . ILE A  1  206 ? -65.422 21.766  100.072 1.00 63.95  ?  206  ILE A CA  1 
ATOM   1240  C C   . ILE A  1  206 ? -66.599 22.432  100.773 1.00 67.07  ?  206  ILE A C   1 
ATOM   1241  O O   . ILE A  1  206 ? -67.753 22.232  100.355 1.00 69.66  ?  206  ILE A O   1 
ATOM   1242  C CB  . ILE A  1  206 ? -65.190 22.378  98.690  1.00 63.35  ?  206  ILE A CB  1 
ATOM   1243  C CG1 . ILE A  1  206 ? -63.951 21.770  98.031  1.00 60.69  ?  206  ILE A CG1 1 
ATOM   1244  C CG2 . ILE A  1  206 ? -65.049 23.887  98.801  1.00 62.76  ?  206  ILE A CG2 1 
ATOM   1245  C CD1 . ILE A  1  206 ? -63.850 22.041  96.543  1.00 61.94  ?  206  ILE A CD1 1 
ATOM   1246  N N   . PRO A  1  207 ? -66.379 23.198  101.838 1.00 66.84  ?  207  PRO A N   1 
ATOM   1247  C CA  . PRO A  1  207 ? -67.515 23.776  102.567 1.00 69.59  ?  207  PRO A CA  1 
ATOM   1248  C C   . PRO A  1  207 ? -68.314 24.724  101.682 1.00 69.76  ?  207  PRO A C   1 
ATOM   1249  O O   . PRO A  1  207 ? -67.758 25.612  101.031 1.00 68.08  ?  207  PRO A O   1 
ATOM   1250  C CB  . PRO A  1  207 ? -66.849 24.513  103.736 1.00 68.56  ?  207  PRO A CB  1 
ATOM   1251  C CG  . PRO A  1  207 ? -65.496 23.870  103.874 1.00 65.89  ?  207  PRO A CG  1 
ATOM   1252  C CD  . PRO A  1  207 ? -65.090 23.510  102.479 1.00 63.51  ?  207  PRO A CD  1 
ATOM   1253  N N   . SER A  1  208 ? -69.635 24.531  101.669 1.00 69.68  ?  208  SER A N   1 
ATOM   1254  C CA  . SER A  1  208 ? -70.503 25.409  100.896 1.00 70.18  ?  208  SER A CA  1 
ATOM   1255  C C   . SER A  1  208 ? -70.532 26.827  101.454 1.00 69.24  ?  208  SER A C   1 
ATOM   1256  O O   . SER A  1  208 ? -70.960 27.747  100.749 1.00 69.44  ?  208  SER A O   1 
ATOM   1257  C CB  . SER A  1  208 ? -71.915 24.837  100.839 1.00 71.87  ?  208  SER A CB  1 
ATOM   1258  O OG  . SER A  1  208 ? -72.431 24.679  102.143 1.00 72.19  ?  208  SER A OG  1 
ATOM   1259  N N   . SER A  1  209 ? -70.080 27.024  102.698 1.00 68.13  ?  209  SER A N   1 
ATOM   1260  C CA  . SER A  1  209 ? -69.977 28.359  103.279 1.00 66.76  ?  209  SER A CA  1 
ATOM   1261  C C   . SER A  1  209 ? -68.958 29.232  102.564 1.00 64.67  ?  209  SER A C   1 
ATOM   1262  O O   . SER A  1  209 ? -68.915 30.441  102.823 1.00 63.14  ?  209  SER A O   1 
ATOM   1263  C CB  . SER A  1  209 ? -69.616 28.269  104.764 1.00 66.73  ?  209  SER A CB  1 
ATOM   1264  O OG  . SER A  1  209 ? -68.369 27.626  104.961 1.00 66.21  ?  209  SER A OG  1 
ATOM   1265  N N   . PHE A  1  210 ? -68.138 28.648  101.683 1.00 69.58  ?  210  PHE A N   1 
ATOM   1266  C CA  . PHE A  1  210 ? -67.171 29.422  100.917 1.00 67.59  ?  210  PHE A CA  1 
ATOM   1267  C C   . PHE A  1  210 ? -67.844 30.424  99.991  1.00 68.50  ?  210  PHE A C   1 
ATOM   1268  O O   . PHE A  1  210 ? -67.170 31.326  99.480  1.00 66.89  ?  210  PHE A O   1 
ATOM   1269  C CB  . PHE A  1  210 ? -66.265 28.488  100.113 1.00 66.99  ?  210  PHE A CB  1 
ATOM   1270  C CG  . PHE A  1  210 ? -65.039 28.034  100.863 1.00 63.56  ?  210  PHE A CG  1 
ATOM   1271  C CD1 . PHE A  1  210 ? -65.066 27.893  102.243 1.00 63.33  ?  210  PHE A CD1 1 
ATOM   1272  C CD2 . PHE A  1  210 ? -63.861 27.739  100.186 1.00 60.94  ?  210  PHE A CD2 1 
ATOM   1273  C CE1 . PHE A  1  210 ? -63.939 27.474  102.938 1.00 60.57  ?  210  PHE A CE1 1 
ATOM   1274  C CE2 . PHE A  1  210 ? -62.733 27.319  100.874 1.00 57.51  ?  210  PHE A CE2 1 
ATOM   1275  C CZ  . PHE A  1  210 ? -62.772 27.186  102.250 1.00 57.24  ?  210  PHE A CZ  1 
ATOM   1276  N N   . GLY A  1  211 ? -69.152 30.280  99.751  1.00 65.84  ?  211  GLY A N   1 
ATOM   1277  C CA  . GLY A  1  211 ? -69.889 31.294  99.019  1.00 66.92  ?  211  GLY A CA  1 
ATOM   1278  C C   . GLY A  1  211 ? -69.920 32.634  99.725  1.00 64.54  ?  211  GLY A C   1 
ATOM   1279  O O   . GLY A  1  211 ? -70.197 33.660  99.092  1.00 64.58  ?  211  GLY A O   1 
ATOM   1280  N N   . ASN A  1  212 ? -69.643 32.646  101.027 1.00 69.28  ?  212  ASN A N   1 
ATOM   1281  C CA  . ASN A  1  212 ? -69.598 33.881  101.793 1.00 66.96  ?  212  ASN A CA  1 
ATOM   1282  C C   . ASN A  1  212 ? -68.279 34.630  101.635 1.00 63.97  ?  212  ASN A C   1 
ATOM   1283  O O   . ASN A  1  212 ? -68.189 35.784  102.065 1.00 61.92  ?  212  ASN A O   1 
ATOM   1284  C CB  . ASN A  1  212 ? -69.858 33.582  103.277 1.00 66.90  ?  212  ASN A CB  1 
ATOM   1285  C CG  . ASN A  1  212 ? -71.307 33.161  103.555 1.00 69.18  ?  212  ASN A CG  1 
ATOM   1286  O OD1 . ASN A  1  212 ? -72.124 33.051  102.638 1.00 70.76  ?  212  ASN A OD1 1 
ATOM   1287  N ND2 . ASN A  1  212 ? -71.625 32.932  104.827 1.00 69.42  ?  212  ASN A ND2 1 
ATOM   1288  N N   . LEU A  1  213 ? -67.261 34.016  101.032 1.00 65.17  ?  213  LEU A N   1 
ATOM   1289  C CA  . LEU A  1  213 ? -65.950 34.650  100.873 1.00 63.17  ?  213  LEU A CA  1 
ATOM   1290  C C   . LEU A  1  213 ? -65.924 35.524  99.619  1.00 62.13  ?  213  LEU A C   1 
ATOM   1291  O O   . LEU A  1  213 ? -65.162 35.289  98.686  1.00 60.94  ?  213  LEU A O   1 
ATOM   1292  C CB  . LEU A  1  213 ? -64.855 33.591  100.819 1.00 62.31  ?  213  LEU A CB  1 
ATOM   1293  C CG  . LEU A  1  213 ? -64.804 32.512  101.899 1.00 63.09  ?  213  LEU A CG  1 
ATOM   1294  C CD1 . LEU A  1  213 ? -63.764 31.471  101.529 1.00 62.08  ?  213  LEU A CD1 1 
ATOM   1295  C CD2 . LEU A  1  213 ? -64.496 33.116  103.256 1.00 63.12  ?  213  LEU A CD2 1 
ATOM   1296  N N   . THR A  1  214 ? -66.766 36.562  99.623  1.00 65.66  ?  214  THR A N   1 
ATOM   1297  C CA  . THR A  1  214 ? -67.007 37.344  98.409  1.00 64.76  ?  214  THR A CA  1 
ATOM   1298  C C   . THR A  1  214 ? -65.734 37.976  97.849  1.00 62.89  ?  214  THR A C   1 
ATOM   1299  O O   . THR A  1  214 ? -65.640 38.207  96.638  1.00 62.02  ?  214  THR A O   1 
ATOM   1300  C CB  . THR A  1  214 ? -68.059 38.424  98.675  1.00 65.27  ?  214  THR A CB  1 
ATOM   1301  O OG1 . THR A  1  214 ? -67.637 39.257  99.762  1.00 65.06  ?  214  THR A OG1 1 
ATOM   1302  C CG2 . THR A  1  214 ? -69.393 37.785  99.018  1.00 67.05  ?  214  THR A CG2 1 
ATOM   1303  N N   . LYS A  1  215 ? -64.755 38.270  98.696  1.00 65.61  ?  215  LYS A N   1 
ATOM   1304  C CA  . LYS A  1  215 ? -63.549 38.958  98.254  1.00 64.08  ?  215  LYS A CA  1 
ATOM   1305  C C   . LYS A  1  215 ? -62.481 38.026  97.687  1.00 63.19  ?  215  LYS A C   1 
ATOM   1306  O O   . LYS A  1  215 ? -61.405 38.502  97.311  1.00 62.03  ?  215  LYS A O   1 
ATOM   1307  C CB  . LYS A  1  215 ? -62.964 39.763  99.411  1.00 64.08  ?  215  LYS A CB  1 
ATOM   1308  C CG  . LYS A  1  215 ? -63.862 40.885  99.890  1.00 64.70  ?  215  LYS A CG  1 
ATOM   1309  C CD  . LYS A  1  215 ? -64.048 41.949  98.819  1.00 63.90  ?  215  LYS A CD  1 
ATOM   1310  C CE  . LYS A  1  215 ? -65.451 42.544  98.862  1.00 64.85  ?  215  LYS A CE  1 
ATOM   1311  N NZ  . LYS A  1  215 ? -65.435 44.038  98.835  1.00 66.31  ?  215  LYS A NZ  1 
ATOM   1312  N N   . LEU A  1  216 ? -62.738 36.722  97.625  1.00 60.75  ?  216  LEU A N   1 
ATOM   1313  C CA  . LEU A  1  216 ? -61.723 35.771  97.186  1.00 59.92  ?  216  LEU A CA  1 
ATOM   1314  C C   . LEU A  1  216 ? -61.392 35.978  95.711  1.00 58.83  ?  216  LEU A C   1 
ATOM   1315  O O   . LEU A  1  216 ? -62.295 36.145  94.885  1.00 59.19  ?  216  LEU A O   1 
ATOM   1316  C CB  . LEU A  1  216 ? -62.215 34.343  97.428  1.00 61.00  ?  216  LEU A CB  1 
ATOM   1317  C CG  . LEU A  1  216 ? -61.200 33.199  97.422  1.00 60.29  ?  216  LEU A CG  1 
ATOM   1318  C CD1 . LEU A  1  216 ? -60.266 33.288  98.617  1.00 59.99  ?  216  LEU A CD1 1 
ATOM   1319  C CD2 . LEU A  1  216 ? -61.920 31.860  97.414  1.00 61.44  ?  216  LEU A CD2 1 
ATOM   1320  N N   . VAL A  1  217 ? -60.095 35.985  95.377  1.00 61.44  ?  217  VAL A N   1 
ATOM   1321  C CA  . VAL A  1  217 ? -59.681 36.044  93.975  1.00 60.44  ?  217  VAL A CA  1 
ATOM   1322  C C   . VAL A  1  217 ? -58.931 34.780  93.569  1.00 60.01  ?  217  VAL A C   1 
ATOM   1323  O O   . VAL A  1  217 ? -58.956 34.393  92.397  1.00 59.64  ?  217  VAL A O   1 
ATOM   1324  C CB  . VAL A  1  217 ? -58.828 37.296  93.683  1.00 59.49  ?  217  VAL A CB  1 
ATOM   1325  C CG1 . VAL A  1  217 ? -59.497 38.539  94.236  1.00 59.91  ?  217  VAL A CG1 1 
ATOM   1326  C CG2 . VAL A  1  217 ? -57.421 37.150  94.236  1.00 59.07  ?  217  VAL A CG2 1 
ATOM   1327  N N   . ASN A  1  218 ? -58.270 34.121  94.524  1.00 56.74  ?  218  ASN A N   1 
ATOM   1328  C CA  . ASN A  1  218 ? -57.421 32.968  94.241  1.00 56.22  ?  218  ASN A CA  1 
ATOM   1329  C C   . ASN A  1  218 ? -57.726 31.841  95.218  1.00 56.95  ?  218  ASN A C   1 
ATOM   1330  O O   . ASN A  1  218 ? -57.638 32.032  96.434  1.00 57.55  ?  218  ASN A O   1 
ATOM   1331  C CB  . ASN A  1  218 ? -55.931 33.336  94.330  1.00 55.55  ?  218  ASN A CB  1 
ATOM   1332  C CG  . ASN A  1  218 ? -55.460 34.198  93.167  1.00 54.74  ?  218  ASN A CG  1 
ATOM   1333  O OD1 . ASN A  1  218 ? -56.108 34.269  92.124  1.00 54.46  ?  218  ASN A OD1 1 
ATOM   1334  N ND2 . ASN A  1  218 ? -54.313 34.846  93.340  1.00 54.57  ?  218  ASN A ND2 1 
ATOM   1335  N N   . LEU A  1  219 ? -58.049 30.661  94.688  1.00 51.31  ?  219  LEU A N   1 
ATOM   1336  C CA  . LEU A  1  219 ? -58.362 29.491  95.506  1.00 51.01  ?  219  LEU A CA  1 
ATOM   1337  C C   . LEU A  1  219 ? -57.521 28.317  95.025  1.00 50.06  ?  219  LEU A C   1 
ATOM   1338  O O   . LEU A  1  219 ? -57.755 27.791  93.931  1.00 49.71  ?  219  LEU A O   1 
ATOM   1339  C CB  . LEU A  1  219 ? -59.854 29.156  95.438  1.00 51.91  ?  219  LEU A CB  1 
ATOM   1340  C CG  . LEU A  1  219 ? -60.355 28.114  96.445  1.00 52.58  ?  219  LEU A CG  1 
ATOM   1341  C CD1 . LEU A  1  219 ? -59.871 28.435  97.847  1.00 52.73  ?  219  LEU A CD1 1 
ATOM   1342  C CD2 . LEU A  1  219 ? -61.861 28.013  96.419  1.00 54.46  ?  219  LEU A CD2 1 
ATOM   1343  N N   . TYR A  1  220 ? -56.557 27.890  95.842  1.00 55.32  ?  220  TYR A N   1 
ATOM   1344  C CA  . TYR A  1  220 ? -55.643 26.808  95.484  1.00 54.74  ?  220  TYR A CA  1 
ATOM   1345  C C   . TYR A  1  220 ? -55.809 25.668  96.479  1.00 55.93  ?  220  TYR A C   1 
ATOM   1346  O O   . TYR A  1  220 ? -55.430 25.800  97.648  1.00 57.09  ?  220  TYR A O   1 
ATOM   1347  C CB  . TYR A  1  220 ? -54.195 27.300  95.453  1.00 54.53  ?  220  TYR A CB  1 
ATOM   1348  C CG  . TYR A  1  220 ? -53.987 28.499  94.559  1.00 53.80  ?  220  TYR A CG  1 
ATOM   1349  C CD1 . TYR A  1  220 ? -54.533 28.534  93.283  1.00 52.92  ?  220  TYR A CD1 1 
ATOM   1350  C CD2 . TYR A  1  220 ? -53.261 29.601  94.994  1.00 54.36  ?  220  TYR A CD2 1 
ATOM   1351  C CE1 . TYR A  1  220 ? -54.361 29.628  92.464  1.00 52.61  ?  220  TYR A CE1 1 
ATOM   1352  C CE2 . TYR A  1  220 ? -53.081 30.701  94.180  1.00 53.80  ?  220  TYR A CE2 1 
ATOM   1353  C CZ  . TYR A  1  220 ? -53.635 30.708  92.917  1.00 52.92  ?  220  TYR A CZ  1 
ATOM   1354  O OH  . TYR A  1  220 ? -53.458 31.802  92.106  1.00 52.53  ?  220  TYR A OH  1 
ATOM   1355  N N   . LEU A  1  221 ? -56.368 24.546  96.016  1.00 54.05  ?  221  LEU A N   1 
ATOM   1356  C CA  . LEU A  1  221 ? -56.549 23.386  96.882  1.00 55.49  ?  221  LEU A CA  1 
ATOM   1357  C C   . LEU A  1  221 ? -56.207 22.068  96.179  1.00 55.10  ?  221  LEU A C   1 
ATOM   1358  O O   . LEU A  1  221 ? -56.810 21.036  96.494  1.00 56.41  ?  221  LEU A O   1 
ATOM   1359  C CB  . LEU A  1  221 ? -57.990 23.321  97.410  1.00 57.32  ?  221  LEU A CB  1 
ATOM   1360  C CG  . LEU A  1  221 ? -58.579 24.546  98.124  1.00 57.93  ?  221  LEU A CG  1 
ATOM   1361  C CD1 . LEU A  1  221 ? -60.095 24.503  98.105  1.00 59.90  ?  221  LEU A CD1 1 
ATOM   1362  C CD2 . LEU A  1  221 ? -58.078 24.659  99.559  1.00 58.83  ?  221  LEU A CD2 1 
ATOM   1363  N N   . PHE A  1  222 ? -55.259 22.058  95.230  1.00 60.05  ?  222  PHE A N   1 
ATOM   1364  C CA  . PHE A  1  222 ? -55.292 20.970  94.251  1.00 59.55  ?  222  PHE A CA  1 
ATOM   1365  C C   . PHE A  1  222 ? -54.828 19.629  94.829  1.00 60.33  ?  222  PHE A C   1 
ATOM   1366  O O   . PHE A  1  222 ? -55.603 18.666  94.860  1.00 61.29  ?  222  PHE A O   1 
ATOM   1367  C CB  . PHE A  1  222 ? -54.520 21.304  92.956  1.00 57.72  ?  222  PHE A CB  1 
ATOM   1368  C CG  . PHE A  1  222 ? -53.290 22.154  93.116  1.00 57.14  ?  222  PHE A CG  1 
ATOM   1369  C CD1 . PHE A  1  222 ? -53.379 23.526  93.307  1.00 57.12  ?  222  PHE A CD1 1 
ATOM   1370  C CD2 . PHE A  1  222 ? -52.036 21.588  92.969  1.00 57.06  ?  222  PHE A CD2 1 
ATOM   1371  C CE1 . PHE A  1  222 ? -52.238 24.300  93.412  1.00 57.38  ?  222  PHE A CE1 1 
ATOM   1372  C CE2 . PHE A  1  222 ? -50.899 22.357  93.075  1.00 57.53  ?  222  PHE A CE2 1 
ATOM   1373  C CZ  . PHE A  1  222 ? -51.001 23.715  93.290  1.00 57.82  ?  222  PHE A CZ  1 
ATOM   1374  N N   . ILE A  1  223 ? -53.589 19.525  95.306  1.00 56.48  ?  223  ILE A N   1 
ATOM   1375  C CA  . ILE A  1  223 ? -53.088 18.192  95.662  1.00 56.69  ?  223  ILE A CA  1 
ATOM   1376  C C   . ILE A  1  223 ? -53.669 17.828  97.024  1.00 58.27  ?  223  ILE A C   1 
ATOM   1377  O O   . ILE A  1  223 ? -53.147 18.233  98.063  1.00 59.18  ?  223  ILE A O   1 
ATOM   1378  C CB  . ILE A  1  223 ? -51.560 18.129  95.665  1.00 56.29  ?  223  ILE A CB  1 
ATOM   1379  C CG1 . ILE A  1  223 ? -51.013 18.381  94.262  1.00 54.82  ?  223  ILE A CG1 1 
ATOM   1380  C CG2 . ILE A  1  223 ? -51.086 16.804  96.231  1.00 56.63  ?  223  ILE A CG2 1 
ATOM   1381  C CD1 . ILE A  1  223 ? -49.755 19.179  94.282  1.00 55.21  ?  223  ILE A CD1 1 
ATOM   1382  N N   . ASN A  1  224 ? -54.750 17.054  97.021  1.00 55.27  ?  224  ASN A N   1 
ATOM   1383  C CA  . ASN A  1  224 ? -55.500 16.746  98.235  1.00 57.10  ?  224  ASN A CA  1 
ATOM   1384  C C   . ASN A  1  224 ? -56.374 15.525  97.962  1.00 57.81  ?  224  ASN A C   1 
ATOM   1385  O O   . ASN A  1  224 ? -56.231 14.855  96.932  1.00 56.78  ?  224  ASN A O   1 
ATOM   1386  C CB  . ASN A  1  224 ? -56.311 17.963  98.695  1.00 58.15  ?  224  ASN A CB  1 
ATOM   1387  C CG  . ASN A  1  224 ? -55.557 18.817  99.701  1.00 58.48  ?  224  ASN A CG  1 
ATOM   1388  O OD1 . ASN A  1  224 ? -54.982 18.301  100.656 1.00 59.31  ?  224  ASN A OD1 1 
ATOM   1389  N ND2 . ASN A  1  224 ? -55.546 20.129  99.482  1.00 57.99  ?  224  ASN A ND2 1 
ATOM   1390  N N   . SER A  1  225 ? -57.275 15.227  98.896  1.00 57.32  ?  225  SER A N   1 
ATOM   1391  C CA  . SER A  1  225 ? -58.244 14.145  98.759  1.00 58.51  ?  225  SER A CA  1 
ATOM   1392  C C   . SER A  1  225 ? -59.647 14.636  99.095  1.00 61.03  ?  225  SER A C   1 
ATOM   1393  O O   . SER A  1  225 ? -60.423 13.948  99.765  1.00 62.88  ?  225  SER A O   1 
ATOM   1394  C CB  . SER A  1  225 ? -57.863 12.951  99.633  1.00 58.72  ?  225  SER A CB  1 
ATOM   1395  O OG  . SER A  1  225 ? -56.879 12.136  99.011  1.00 56.76  ?  225  SER A OG  1 
ATOM   1396  N N   . LEU A  1  226 ? -59.987 15.844  98.643  1.00 58.43  ?  226  LEU A N   1 
ATOM   1397  C CA  . LEU A  1  226 ? -61.325 16.382  98.847  1.00 61.20  ?  226  LEU A CA  1 
ATOM   1398  C C   . LEU A  1  226 ? -62.350 15.546  98.090  1.00 62.80  ?  226  LEU A C   1 
ATOM   1399  O O   . LEU A  1  226 ? -62.055 14.949  97.052  1.00 61.38  ?  226  LEU A O   1 
ATOM   1400  C CB  . LEU A  1  226 ? -61.397 17.842  98.397  1.00 60.80  ?  226  LEU A CB  1 
ATOM   1401  C CG  . LEU A  1  226 ? -60.474 18.802  99.150  1.00 59.02  ?  226  LEU A CG  1 
ATOM   1402  C CD1 . LEU A  1  226 ? -60.711 20.244  98.736  1.00 58.38  ?  226  LEU A CD1 1 
ATOM   1403  C CD2 . LEU A  1  226 ? -60.651 18.640  100.647 1.00 60.73  ?  226  LEU A CD2 1 
ATOM   1404  N N   . SER A  1  227 ? -63.569 15.509  98.620  1.00 65.67  ?  227  SER A N   1 
ATOM   1405  C CA  . SER A  1  227 ? -64.581 14.569  98.169  1.00 66.91  ?  227  SER A CA  1 
ATOM   1406  C C   . SER A  1  227 ? -65.907 15.286  97.949  1.00 69.86  ?  227  SER A C   1 
ATOM   1407  O O   . SER A  1  227 ? -66.080 16.449  98.315  1.00 71.48  ?  227  SER A O   1 
ATOM   1408  C CB  . SER A  1  227 ? -64.755 13.430  99.175  1.00 66.95  ?  227  SER A CB  1 
ATOM   1409  O OG  . SER A  1  227 ? -65.494 12.383  98.588  1.00 66.82  ?  227  SER A OG  1 
ATOM   1410  N N   . GLY A  1  228 ? -66.846 14.579  97.324  1.00 70.26  ?  228  GLY A N   1 
ATOM   1411  C CA  . GLY A  1  228 ? -68.172 15.119  97.101  1.00 72.08  ?  228  GLY A CA  1 
ATOM   1412  C C   . GLY A  1  228 ? -68.254 16.011  95.876  1.00 72.48  ?  228  GLY A C   1 
ATOM   1413  O O   . GLY A  1  228 ? -67.306 16.177  95.105  1.00 71.64  ?  228  GLY A O   1 
ATOM   1414  N N   . SER A  1  229 ? -69.432 16.603  95.703  1.00 76.06  ?  229  SER A N   1 
ATOM   1415  C CA  . SER A  1  229 ? -69.682 17.492  94.581  1.00 75.88  ?  229  SER A CA  1 
ATOM   1416  C C   . SER A  1  229 ? -69.175 18.900  94.874  1.00 75.61  ?  229  SER A C   1 
ATOM   1417  O O   . SER A  1  229 ? -69.041 19.319  96.026  1.00 75.74  ?  229  SER A O   1 
ATOM   1418  C CB  . SER A  1  229 ? -71.173 17.534  94.248  1.00 75.90  ?  229  SER A CB  1 
ATOM   1419  O OG  . SER A  1  229 ? -71.671 16.231  93.994  1.00 75.69  ?  229  SER A OG  1 
ATOM   1420  N N   . ILE A  1  230 ? -68.880 19.628  93.807  1.00 77.87  ?  230  ILE A N   1 
ATOM   1421  C CA  . ILE A  1  230 ? -68.472 21.029  93.953  1.00 76.41  ?  230  ILE A CA  1 
ATOM   1422  C C   . ILE A  1  230 ? -69.655 21.841  94.469  1.00 76.34  ?  230  ILE A C   1 
ATOM   1423  O O   . ILE A  1  230 ? -70.767 21.726  93.923  1.00 76.71  ?  230  ILE A O   1 
ATOM   1424  C CB  . ILE A  1  230 ? -67.972 21.576  92.618  1.00 74.94  ?  230  ILE A CB  1 
ATOM   1425  C CG1 . ILE A  1  230 ? -66.992 20.588  91.986  1.00 75.32  ?  230  ILE A CG1 1 
ATOM   1426  C CG2 . ILE A  1  230 ? -67.336 22.950  92.811  1.00 72.59  ?  230  ILE A CG2 1 
ATOM   1427  C CD1 . ILE A  1  230 ? -66.235 21.143  90.818  1.00 73.44  ?  230  ILE A CD1 1 
ATOM   1428  N N   . PRO A  1  231 ? -69.482 22.662  95.506  1.00 76.38  ?  231  PRO A N   1 
ATOM   1429  C CA  . PRO A  1  231 ? -70.602 23.486  95.980  1.00 76.38  ?  231  PRO A CA  1 
ATOM   1430  C C   . PRO A  1  231 ? -70.982 24.523  94.934  1.00 75.15  ?  231  PRO A C   1 
ATOM   1431  O O   . PRO A  1  231 ? -70.129 25.247  94.420  1.00 73.58  ?  231  PRO A O   1 
ATOM   1432  C CB  . PRO A  1  231 ? -70.051 24.147  97.251  1.00 75.77  ?  231  PRO A CB  1 
ATOM   1433  C CG  . PRO A  1  231 ? -68.849 23.348  97.627  1.00 75.78  ?  231  PRO A CG  1 
ATOM   1434  C CD  . PRO A  1  231 ? -68.285 22.820  96.347  1.00 75.52  ?  231  PRO A CD  1 
ATOM   1435  N N   . SER A  1  232 ? -72.280 24.601  94.635  1.00 79.66  ?  232  SER A N   1 
ATOM   1436  C CA  . SER A  1  232 ? -72.753 25.522  93.610  1.00 78.58  ?  232  SER A CA  1 
ATOM   1437  C C   . SER A  1  232 ? -72.572 26.982  94.007  1.00 77.33  ?  232  SER A C   1 
ATOM   1438  O O   . SER A  1  232 ? -72.570 27.851  93.130  1.00 76.09  ?  232  SER A O   1 
ATOM   1439  C CB  . SER A  1  232 ? -74.223 25.245  93.297  1.00 79.28  ?  232  SER A CB  1 
ATOM   1440  O OG  . SER A  1  232 ? -74.906 24.798  94.454  1.00 80.41  ?  232  SER A OG  1 
ATOM   1441  N N   . GLU A  1  233 ? -72.435 27.273  95.304  1.00 79.46  ?  233  GLU A N   1 
ATOM   1442  C CA  . GLU A  1  233 ? -72.174 28.642  95.734  1.00 78.24  ?  233  GLU A CA  1 
ATOM   1443  C C   . GLU A  1  233 ? -70.841 29.159  95.215  1.00 76.48  ?  233  GLU A C   1 
ATOM   1444  O O   . GLU A  1  233 ? -70.655 30.377  95.119  1.00 75.18  ?  233  GLU A O   1 
ATOM   1445  C CB  . GLU A  1  233 ? -72.196 28.737  97.263  1.00 78.88  ?  233  GLU A CB  1 
ATOM   1446  C CG  . GLU A  1  233 ? -73.560 28.508  97.889  1.00 80.28  ?  233  GLU A CG  1 
ATOM   1447  C CD  . GLU A  1  233 ? -73.970 27.044  97.902  1.00 81.73  ?  233  GLU A CD  1 
ATOM   1448  O OE1 . GLU A  1  233 ? -73.099 26.178  98.133  1.00 82.06  ?  233  GLU A OE1 1 
ATOM   1449  O OE2 . GLU A  1  233 ? -75.166 26.761  97.671  1.00 82.40  -1 233  GLU A OE2 1 
ATOM   1450  N N   . ILE A  1  234 ? -69.918 28.261  94.861  1.00 76.99  ?  234  ILE A N   1 
ATOM   1451  C CA  . ILE A  1  234 ? -68.614 28.698  94.380  1.00 75.04  ?  234  ILE A CA  1 
ATOM   1452  C C   . ILE A  1  234 ? -68.754 29.448  93.062  1.00 73.93  ?  234  ILE A C   1 
ATOM   1453  O O   . ILE A  1  234 ? -67.943 30.329  92.750  1.00 72.13  ?  234  ILE A O   1 
ATOM   1454  C CB  . ILE A  1  234 ? -67.668 27.486  94.280  1.00 75.08  ?  234  ILE A CB  1 
ATOM   1455  C CG1 . ILE A  1  234 ? -67.053 27.195  95.650  1.00 75.02  ?  234  ILE A CG1 1 
ATOM   1456  C CG2 . ILE A  1  234 ? -66.584 27.692  93.222  1.00 73.11  ?  234  ILE A CG2 1 
ATOM   1457  C CD1 . ILE A  1  234 ? -65.885 26.243  95.603  1.00 74.29  ?  234  ILE A CD1 1 
ATOM   1458  N N   . GLY A  1  235 ? -69.811 29.167  92.300  1.00 80.10  ?  235  GLY A N   1 
ATOM   1459  C CA  . GLY A  1  235 ? -70.058 29.883  91.061  1.00 79.01  ?  235  GLY A CA  1 
ATOM   1460  C C   . GLY A  1  235 ? -70.457 31.334  91.240  1.00 78.06  ?  235  GLY A C   1 
ATOM   1461  O O   . GLY A  1  235 ? -70.499 32.071  90.248  1.00 76.91  ?  235  GLY A O   1 
ATOM   1462  N N   . ASN A  1  236 ? -70.757 31.755  92.470  1.00 77.83  ?  236  ASN A N   1 
ATOM   1463  C CA  . ASN A  1  236 ? -71.259 33.094  92.746  1.00 77.21  ?  236  ASN A CA  1 
ATOM   1464  C C   . ASN A  1  236 ? -70.221 34.013  93.382  1.00 75.92  ?  236  ASN A C   1 
ATOM   1465  O O   . ASN A  1  236 ? -70.571 35.117  93.815  1.00 75.58  ?  236  ASN A O   1 
ATOM   1466  C CB  . ASN A  1  236 ? -72.499 33.008  93.635  1.00 78.71  ?  236  ASN A CB  1 
ATOM   1467  C CG  . ASN A  1  236 ? -73.697 32.428  92.905  1.00 79.61  ?  236  ASN A CG  1 
ATOM   1468  O OD1 . ASN A  1  236 ? -74.141 31.317  93.203  1.00 80.99  ?  236  ASN A OD1 1 
ATOM   1469  N ND2 . ASN A  1  236 ? -74.229 33.179  91.943  1.00 78.76  ?  236  ASN A ND2 1 
ATOM   1470  N N   . LEU A  1  237 ? -68.966 33.594  93.451  1.00 74.38  ?  237  LEU A N   1 
ATOM   1471  C CA  . LEU A  1  237 ? -67.922 34.494  93.925  1.00 72.92  ?  237  LEU A CA  1 
ATOM   1472  C C   . LEU A  1  237 ? -67.645 35.531  92.845  1.00 71.32  ?  237  LEU A C   1 
ATOM   1473  O O   . LEU A  1  237 ? -67.213 35.164  91.746  1.00 70.62  ?  237  LEU A O   1 
ATOM   1474  C CB  . LEU A  1  237 ? -66.650 33.724  94.268  1.00 72.42  ?  237  LEU A CB  1 
ATOM   1475  C CG  . LEU A  1  237 ? -66.609 32.931  95.576  1.00 73.69  ?  237  LEU A CG  1 
ATOM   1476  C CD1 . LEU A  1  237 ? -67.044 33.811  96.725  1.00 74.09  ?  237  LEU A CD1 1 
ATOM   1477  C CD2 . LEU A  1  237 ? -67.458 31.688  95.523  1.00 75.47  ?  237  LEU A CD2 1 
ATOM   1478  N N   . PRO A  1  238 ? -67.843 36.817  93.110  1.00 72.53  ?  238  PRO A N   1 
ATOM   1479  C CA  . PRO A  1  238 ? -67.798 37.817  92.035  1.00 71.48  ?  238  PRO A CA  1 
ATOM   1480  C C   . PRO A  1  238 ? -66.395 38.178  91.576  1.00 70.41  ?  238  PRO A C   1 
ATOM   1481  O O   . PRO A  1  238 ? -66.188 38.492  90.397  1.00 71.51  ?  238  PRO A O   1 
ATOM   1482  C CB  . PRO A  1  238 ? -68.489 39.030  92.669  1.00 73.98  ?  238  PRO A CB  1 
ATOM   1483  C CG  . PRO A  1  238 ? -68.490 38.775  94.167  1.00 72.57  ?  238  PRO A CG  1 
ATOM   1484  C CD  . PRO A  1  238 ? -67.865 37.442  94.437  1.00 72.84  ?  238  PRO A CD  1 
ATOM   1485  N N   . ASN A  1  239 ? -65.428 38.134  92.491  1.00 74.12  ?  239  ASN A N   1 
ATOM   1486  C CA  . ASN A  1  239 ? -64.064 38.568  92.221  1.00 72.62  ?  239  ASN A CA  1 
ATOM   1487  C C   . ASN A  1  239 ? -63.115 37.417  91.920  1.00 72.18  ?  239  ASN A C   1 
ATOM   1488  O O   . ASN A  1  239 ? -61.919 37.657  91.715  1.00 71.00  ?  239  ASN A O   1 
ATOM   1489  C CB  . ASN A  1  239 ? -63.532 39.383  93.407  1.00 72.43  ?  239  ASN A CB  1 
ATOM   1490  C CG  . ASN A  1  239 ? -64.288 40.687  93.604  1.00 72.64  ?  239  ASN A CG  1 
ATOM   1491  O OD1 . ASN A  1  239 ? -64.327 41.532  92.710  1.00 71.93  ?  239  ASN A OD1 1 
ATOM   1492  N ND2 . ASN A  1  239 ? -64.893 40.856  94.778  1.00 73.65  ?  239  ASN A ND2 1 
ATOM   1493  N N   . LEU A  1  240 ? -63.610 36.182  91.872  1.00 67.93  ?  240  LEU A N   1 
ATOM   1494  C CA  . LEU A  1  240 ? -62.727 35.041  91.674  1.00 67.60  ?  240  LEU A CA  1 
ATOM   1495  C C   . LEU A  1  240 ? -62.033 35.123  90.315  1.00 66.34  ?  240  LEU A C   1 
ATOM   1496  O O   . LEU A  1  240 ? -62.663 35.432  89.298  1.00 66.41  ?  240  LEU A O   1 
ATOM   1497  C CB  . LEU A  1  240 ? -63.521 33.739  91.796  1.00 69.23  ?  240  LEU A CB  1 
ATOM   1498  C CG  . LEU A  1  240 ? -62.641 32.501  91.979  1.00 69.13  ?  240  LEU A CG  1 
ATOM   1499  C CD1 . LEU A  1  240 ? -61.925 32.565  93.320  1.00 68.79  ?  240  LEU A CD1 1 
ATOM   1500  C CD2 . LEU A  1  240 ? -63.432 31.207  91.838  1.00 70.89  ?  240  LEU A CD2 1 
ATOM   1501  N N   . ARG A  1  241 ? -60.724 34.865  90.311  1.00 72.31  ?  241  ARG A N   1 
ATOM   1502  C CA  . ARG A  1  241 ? -59.902 34.886  89.105  1.00 71.20  ?  241  ARG A CA  1 
ATOM   1503  C C   . ARG A  1  241 ? -59.292 33.531  88.787  1.00 71.09  ?  241  ARG A C   1 
ATOM   1504  O O   . ARG A  1  241 ? -59.317 33.101  87.629  1.00 70.99  ?  241  ARG A O   1 
ATOM   1505  C CB  . ARG A  1  241 ? -58.785 35.934  89.242  1.00 70.09  ?  241  ARG A CB  1 
ATOM   1506  C CG  . ARG A  1  241 ? -58.875 37.076  88.241  1.00 69.57  ?  241  ARG A CG  1 
ATOM   1507  C CD  . ARG A  1  241 ? -58.068 38.283  88.701  1.00 69.00  ?  241  ARG A CD  1 
ATOM   1508  N NE  . ARG A  1  241 ? -58.934 39.353  89.186  1.00 69.31  ?  241  ARG A NE  1 
ATOM   1509  C CZ  . ARG A  1  241 ? -58.582 40.250  90.101  1.00 69.32  ?  241  ARG A CZ  1 
ATOM   1510  N NH1 . ARG A  1  241 ? -57.371 40.246  90.641  1.00 69.10  ?  241  ARG A NH1 1 
ATOM   1511  N NH2 . ARG A  1  241 ? -59.468 41.168  90.488  1.00 69.64  ?  241  ARG A NH2 1 
ATOM   1512  N N   . GLU A  1  242 ? -58.742 32.844  89.785  1.00 61.55  ?  242  GLU A N   1 
ATOM   1513  C CA  . GLU A  1  242 ? -58.072 31.566  89.597  1.00 61.32  ?  242  GLU A CA  1 
ATOM   1514  C C   . GLU A  1  242 ? -58.699 30.524  90.509  1.00 62.56  ?  242  GLU A C   1 
ATOM   1515  O O   . GLU A  1  242 ? -58.778 30.731  91.724  1.00 62.82  ?  242  GLU A O   1 
ATOM   1516  C CB  . GLU A  1  242 ? -56.577 31.685  89.890  1.00 60.15  ?  242  GLU A CB  1 
ATOM   1517  C CG  . GLU A  1  242 ? -55.900 32.804  89.135  1.00 59.36  ?  242  GLU A CG  1 
ATOM   1518  C CD  . GLU A  1  242 ? -54.435 32.524  88.883  1.00 58.71  ?  242  GLU A CD  1 
ATOM   1519  O OE1 . GLU A  1  242 ? -53.908 31.531  89.430  1.00 58.79  ?  242  GLU A OE1 1 
ATOM   1520  O OE2 . GLU A  1  242 ? -53.812 33.292  88.125  1.00 58.31  -1 242  GLU A OE2 1 
ATOM   1521  N N   . LEU A  1  243 ? -59.138 29.409  89.928  1.00 53.94  ?  243  LEU A N   1 
ATOM   1522  C CA  . LEU A  1  243 ? -59.754 28.316  90.681  1.00 54.83  ?  243  LEU A CA  1 
ATOM   1523  C C   . LEU A  1  243 ? -59.039 27.023  90.297  1.00 54.00  ?  243  LEU A C   1 
ATOM   1524  O O   . LEU A  1  243 ? -59.254 26.494  89.202  1.00 54.51  ?  243  LEU A O   1 
ATOM   1525  C CB  . LEU A  1  243 ? -61.259 28.230  90.408  1.00 57.13  ?  243  LEU A CB  1 
ATOM   1526  C CG  . LEU A  1  243 ? -62.081 27.196  91.199  1.00 59.11  ?  243  LEU A CG  1 
ATOM   1527  C CD1 . LEU A  1  243 ? -61.903 27.366  92.697  1.00 58.86  ?  243  LEU A CD1 1 
ATOM   1528  C CD2 . LEU A  1  243 ? -63.562 27.255  90.843  1.00 61.54  ?  243  LEU A CD2 1 
ATOM   1529  N N   . CYS A  1  244 ? -58.186 26.515  91.193  1.00 56.55  ?  244  CYS A N   1 
ATOM   1530  C CA  . CYS A  1  244 ? -57.431 25.279  90.969  1.00 55.72  ?  244  CYS A CA  1 
ATOM   1531  C C   . CYS A  1  244 ? -57.913 24.202  91.936  1.00 57.06  ?  244  CYS A C   1 
ATOM   1532  O O   . CYS A  1  244 ? -57.509 24.175  93.102  1.00 56.87  ?  244  CYS A O   1 
ATOM   1533  C CB  . CYS A  1  244 ? -55.930 25.511  91.129  1.00 53.92  ?  244  CYS A CB  1 
ATOM   1534  S SG  . CYS A  1  244 ? -55.200 26.686  89.968  1.00 53.08  ?  244  CYS A SG  1 
ATOM   1535  N N   . LEU A  1  245 ? -58.756 23.295  91.438  1.00 53.83  ?  245  LEU A N   1 
ATOM   1536  C CA  . LEU A  1  245 ? -59.269 22.179  92.226  1.00 55.82  ?  245  LEU A CA  1 
ATOM   1537  C C   . LEU A  1  245 ? -58.792 20.834  91.685  1.00 55.62  ?  245  LEU A C   1 
ATOM   1538  O O   . LEU A  1  245 ? -59.370 19.793  92.018  1.00 57.68  ?  245  LEU A O   1 
ATOM   1539  C CB  . LEU A  1  245 ? -60.798 22.214  92.273  1.00 59.43  ?  245  LEU A CB  1 
ATOM   1540  C CG  . LEU A  1  245 ? -61.444 23.472  92.848  1.00 59.75  ?  245  LEU A CG  1 
ATOM   1541  C CD1 . LEU A  1  245 ? -62.940 23.458  92.592  1.00 63.19  ?  245  LEU A CD1 1 
ATOM   1542  C CD2 . LEU A  1  245 ? -61.149 23.573  94.326  1.00 59.21  ?  245  LEU A CD2 1 
ATOM   1543  N N   . ASP A  1  246 ? -57.752 20.839  90.854  1.00 61.78  ?  246  ASP A N   1 
ATOM   1544  C CA  . ASP A  1  246 ? -57.294 19.642  90.164  1.00 61.47  ?  246  ASP A CA  1 
ATOM   1545  C C   . ASP A  1  246 ? -56.722 18.623  91.149  1.00 61.04  ?  246  ASP A C   1 
ATOM   1546  O O   . ASP A  1  246 ? -56.433 18.933  92.302  1.00 60.83  ?  246  ASP A O   1 
ATOM   1547  C CB  . ASP A  1  246 ? -56.241 20.000  89.110  1.00 59.14  ?  246  ASP A CB  1 
ATOM   1548  C CG  . ASP A  1  246 ? -55.129 20.889  89.661  1.00 56.99  ?  246  ASP A CG  1 
ATOM   1549  O OD1 . ASP A  1  246 ? -55.417 22.054  90.007  1.00 57.03  ?  246  ASP A OD1 1 
ATOM   1550  O OD2 . ASP A  1  246 ? -53.966 20.429  89.741  1.00 55.83  -1 246  ASP A OD2 1 
ATOM   1551  N N   . ARG A  1  247 ? -56.589 17.381  90.682  1.00 61.38  ?  247  ARG A N   1 
ATOM   1552  C CA  . ARG A  1  247 ? -55.921 16.313  91.428  1.00 60.95  ?  247  ARG A CA  1 
ATOM   1553  C C   . ARG A  1  247 ? -56.568 16.084  92.795  1.00 62.44  ?  247  ARG A C   1 
ATOM   1554  O O   . ARG A  1  247 ? -55.910 16.102  93.839  1.00 62.03  ?  247  ARG A O   1 
ATOM   1555  C CB  . ARG A  1  247 ? -54.428 16.617  91.578  1.00 59.07  ?  247  ARG A CB  1 
ATOM   1556  C CG  . ARG A  1  247 ? -53.607 16.238  90.367  1.00 57.78  ?  247  ARG A CG  1 
ATOM   1557  C CD  . ARG A  1  247 ? -52.158 16.635  90.539  1.00 56.44  ?  247  ARG A CD  1 
ATOM   1558  N NE  . ARG A  1  247 ? -51.919 18.008  90.115  1.00 55.55  ?  247  ARG A NE  1 
ATOM   1559  C CZ  . ARG A  1  247 ? -50.835 18.707  90.425  1.00 55.28  ?  247  ARG A CZ  1 
ATOM   1560  N NH1 . ARG A  1  247 ? -49.863 18.187  91.154  1.00 55.94  ?  247  ARG A NH1 1 
ATOM   1561  N NH2 . ARG A  1  247 ? -50.719 19.958  89.982  1.00 54.82  ?  247  ARG A NH2 1 
ATOM   1562  N N   . ASN A  1  248 ? -57.880 15.846  92.767  1.00 58.65  ?  248  ASN A N   1 
ATOM   1563  C CA  . ASN A  1  248 ? -58.655 15.553  93.969  1.00 60.45  ?  248  ASN A CA  1 
ATOM   1564  C C   . ASN A  1  248 ? -59.558 14.349  93.724  1.00 62.08  ?  248  ASN A C   1 
ATOM   1565  O O   . ASN A  1  248 ? -59.429 13.667  92.701  1.00 61.54  ?  248  ASN A O   1 
ATOM   1566  C CB  . ASN A  1  248 ? -59.476 16.769  94.406  1.00 62.06  ?  248  ASN A CB  1 
ATOM   1567  C CG  . ASN A  1  248 ? -58.750 17.624  95.430  1.00 60.86  ?  248  ASN A CG  1 
ATOM   1568  O OD1 . ASN A  1  248 ? -58.559 17.214  96.570  1.00 61.32  ?  248  ASN A OD1 1 
ATOM   1569  N ND2 . ASN A  1  248 ? -58.357 18.825  95.029  1.00 59.49  ?  248  ASN A ND2 1 
ATOM   1570  N N   . ASN A  1  249 ? -60.458 14.063  94.660  1.00 63.30  ?  249  ASN A N   1 
ATOM   1571  C CA  . ASN A  1  249 ? -61.412 12.966  94.533  1.00 64.78  ?  249  ASN A CA  1 
ATOM   1572  C C   . ASN A  1  249 ? -62.834 13.508  94.424  1.00 67.78  ?  249  ASN A C   1 
ATOM   1573  O O   . ASN A  1  249 ? -63.781 12.952  94.987  1.00 69.40  ?  249  ASN A O   1 
ATOM   1574  C CB  . ASN A  1  249 ? -61.298 12.004  95.714  1.00 64.61  ?  249  ASN A CB  1 
ATOM   1575  C CG  . ASN A  1  249 ? -60.091 11.092  95.618  1.00 62.21  ?  249  ASN A CG  1 
ATOM   1576  O OD1 . ASN A  1  249 ? -60.136 10.051  94.959  1.00 61.62  ?  249  ASN A OD1 1 
ATOM   1577  N ND2 . ASN A  1  249 ? -59.007 11.471  96.289  1.00 60.99  ?  249  ASN A ND2 1 
ATOM   1578  N N   . LEU A  1  250 ? -62.986 14.614  93.702  1.00 65.14  ?  250  LEU A N   1 
ATOM   1579  C CA  . LEU A  1  250 ? -64.290 15.240  93.543  1.00 68.42  ?  250  LEU A CA  1 
ATOM   1580  C C   . LEU A  1  250 ? -65.187 14.394  92.649  1.00 69.32  ?  250  LEU A C   1 
ATOM   1581  O O   . LEU A  1  250 ? -64.748 13.858  91.629  1.00 67.97  ?  250  LEU A O   1 
ATOM   1582  C CB  . LEU A  1  250 ? -64.127 16.636  92.950  1.00 69.18  ?  250  LEU A CB  1 
ATOM   1583  C CG  . LEU A  1  250 ? -64.274 17.799  93.924  1.00 70.20  ?  250  LEU A CG  1 
ATOM   1584  C CD1 . LEU A  1  250 ? -63.373 17.617  95.139  1.00 67.59  ?  250  LEU A CD1 1 
ATOM   1585  C CD2 . LEU A  1  250 ? -63.960 19.101  93.206  1.00 69.41  ?  250  LEU A CD2 1 
ATOM   1586  N N   . THR A  1  251 ? -66.454 14.285  93.032  1.00 71.14  ?  251  THR A N   1 
ATOM   1587  C CA  . THR A  1  251 ? -67.459 13.552  92.274  1.00 71.47  ?  251  THR A CA  1 
ATOM   1588  C C   . THR A  1  251 ? -68.571 14.508  91.846  1.00 73.26  ?  251  THR A C   1 
ATOM   1589  O O   . THR A  1  251 ? -68.568 15.694  92.185  1.00 74.31  ?  251  THR A O   1 
ATOM   1590  C CB  . THR A  1  251 ? -68.027 12.393  93.100  1.00 71.05  ?  251  THR A CB  1 
ATOM   1591  O OG1 . THR A  1  251 ? -68.892 12.911  94.120  1.00 72.61  ?  251  THR A OG1 1 
ATOM   1592  C CG2 . THR A  1  251 ? -66.908 11.598  93.751  1.00 69.16  ?  251  THR A CG2 1 
ATOM   1593  N N   . GLY A  1  252 ? -69.529 13.984  91.088  1.00 73.77  ?  252  GLY A N   1 
ATOM   1594  C CA  . GLY A  1  252 ? -70.682 14.771  90.706  1.00 74.60  ?  252  GLY A CA  1 
ATOM   1595  C C   . GLY A  1  252 ? -70.457 15.622  89.469  1.00 74.52  ?  252  GLY A C   1 
ATOM   1596  O O   . GLY A  1  252 ? -69.437 15.540  88.781  1.00 74.06  ?  252  GLY A O   1 
ATOM   1597  N N   . LYS A  1  253 ? -71.452 16.460  89.191  1.00 78.17  ?  253  LYS A N   1 
ATOM   1598  C CA  . LYS A  1  253 ? -71.470 17.304  88.006  1.00 77.64  ?  253  LYS A CA  1 
ATOM   1599  C C   . LYS A  1  253 ? -70.746 18.622  88.256  1.00 77.36  ?  253  LYS A C   1 
ATOM   1600  O O   . LYS A  1  253 ? -70.580 19.068  89.395  1.00 77.67  ?  253  LYS A O   1 
ATOM   1601  C CB  . LYS A  1  253 ? -72.908 17.589  87.568  1.00 77.36  ?  253  LYS A CB  1 
ATOM   1602  C CG  . LYS A  1  253 ? -73.676 16.371  87.095  1.00 77.23  ?  253  LYS A CG  1 
ATOM   1603  C CD  . LYS A  1  253 ? -74.764 16.757  86.100  1.00 76.68  ?  253  LYS A CD  1 
ATOM   1604  C CE  . LYS A  1  253 ? -75.708 17.798  86.696  1.00 76.72  ?  253  LYS A CE  1 
ATOM   1605  N NZ  . LYS A  1  253 ? -76.780 18.245  85.751  1.00 77.18  ?  253  LYS A NZ  1 
ATOM   1606  N N   . ILE A  1  254 ? -70.299 19.236  87.168  1.00 79.06  ?  254  ILE A N   1 
ATOM   1607  C CA  . ILE A  1  254 ? -69.811 20.617  87.245  1.00 77.98  ?  254  ILE A CA  1 
ATOM   1608  C C   . ILE A  1  254 ? -71.001 21.543  87.474  1.00 77.58  ?  254  ILE A C   1 
ATOM   1609  O O   . ILE A  1  254 ? -71.989 21.473  86.719  1.00 77.46  ?  254  ILE A O   1 
ATOM   1610  C CB  . ILE A  1  254 ? -69.052 20.993  85.967  1.00 76.72  ?  254  ILE A CB  1 
ATOM   1611  C CG1 . ILE A  1  254 ? -67.811 20.119  85.802  1.00 77.08  ?  254  ILE A CG1 1 
ATOM   1612  C CG2 . ILE A  1  254 ? -68.643 22.455  85.990  1.00 74.95  ?  254  ILE A CG2 1 
ATOM   1613  C CD1 . ILE A  1  254 ? -67.075 20.359  84.502  1.00 75.83  ?  254  ILE A CD1 1 
ATOM   1614  N N   . PRO A  1  255 ? -70.975 22.396  88.497  1.00 80.23  ?  255  PRO A N   1 
ATOM   1615  C CA  . PRO A  1  255 ? -72.135 23.253  88.769  1.00 79.97  ?  255  PRO A CA  1 
ATOM   1616  C C   . PRO A  1  255 ? -72.404 24.210  87.617  1.00 78.56  ?  255  PRO A C   1 
ATOM   1617  O O   . PRO A  1  255 ? -71.501 24.888  87.121  1.00 77.27  ?  255  PRO A O   1 
ATOM   1618  C CB  . PRO A  1  255 ? -71.733 23.999  90.047  1.00 79.77  ?  255  PRO A CB  1 
ATOM   1619  C CG  . PRO A  1  255 ? -70.685 23.141  90.674  1.00 80.47  ?  255  PRO A CG  1 
ATOM   1620  C CD  . PRO A  1  255 ? -69.935 22.532  89.530  1.00 80.20  ?  255  PRO A CD  1 
ATOM   1621  N N   . SER A  1  256 ? -73.669 24.257  87.194  1.00 84.19  ?  256  SER A N   1 
ATOM   1622  C CA  . SER A  1  256 ? -74.079 25.166  86.131  1.00 82.93  ?  256  SER A CA  1 
ATOM   1623  C C   . SER A  1  256 ? -73.934 26.624  86.541  1.00 81.82  ?  256  SER A C   1 
ATOM   1624  O O   . SER A  1  256 ? -73.876 27.500  85.671  1.00 80.51  ?  256  SER A O   1 
ATOM   1625  C CB  . SER A  1  256 ? -75.525 24.876  85.723  1.00 83.28  ?  256  SER A CB  1 
ATOM   1626  O OG  . SER A  1  256 ? -76.388 24.881  86.853  1.00 84.09  ?  256  SER A OG  1 
ATOM   1627  N N   . SER A  1  257 ? -73.880 26.903  87.845  1.00 82.70  ?  257  SER A N   1 
ATOM   1628  C CA  . SER A  1  257 ? -73.686 28.260  88.340  1.00 81.65  ?  257  SER A CA  1 
ATOM   1629  C C   . SER A  1  257 ? -72.326 28.830  87.968  1.00 80.19  ?  257  SER A C   1 
ATOM   1630  O O   . SER A  1  257 ? -72.120 30.040  88.124  1.00 78.99  ?  257  SER A O   1 
ATOM   1631  C CB  . SER A  1  257 ? -73.853 28.296  89.861  1.00 82.55  ?  257  SER A CB  1 
ATOM   1632  O OG  . SER A  1  257 ? -72.842 27.537  90.505  1.00 83.08  ?  257  SER A OG  1 
ATOM   1633  N N   . PHE A  1  258 ? -71.399 27.992  87.494  1.00 76.76  ?  258  PHE A N   1 
ATOM   1634  C CA  . PHE A  1  258 ? -70.074 28.467  87.115  1.00 75.17  ?  258  PHE A CA  1 
ATOM   1635  C C   . PHE A  1  258 ? -70.124 29.485  85.983  1.00 73.62  ?  258  PHE A C   1 
ATOM   1636  O O   . PHE A  1  258 ? -69.137 30.194  85.756  1.00 72.05  ?  258  PHE A O   1 
ATOM   1637  C CB  . PHE A  1  258 ? -69.186 27.283  86.726  1.00 75.55  ?  258  PHE A CB  1 
ATOM   1638  C CG  . PHE A  1  258 ? -68.446 26.672  87.885  1.00 76.16  ?  258  PHE A CG  1 
ATOM   1639  C CD1 . PHE A  1  258 ? -68.958 26.741  89.169  1.00 77.12  ?  258  PHE A CD1 1 
ATOM   1640  C CD2 . PHE A  1  258 ? -67.235 26.031  87.688  1.00 75.67  ?  258  PHE A CD2 1 
ATOM   1641  C CE1 . PHE A  1  258 ? -68.277 26.181  90.234  1.00 77.61  ?  258  PHE A CE1 1 
ATOM   1642  C CE2 . PHE A  1  258 ? -66.549 25.470  88.751  1.00 76.02  ?  258  PHE A CE2 1 
ATOM   1643  C CZ  . PHE A  1  258 ? -67.072 25.547  90.025  1.00 77.01  ?  258  PHE A CZ  1 
ATOM   1644  N N   . GLY A  1  259 ? -71.250 29.583  85.276  1.00 79.42  ?  259  GLY A N   1 
ATOM   1645  C CA  . GLY A  1  259 ? -71.417 30.595  84.252  1.00 78.05  ?  259  GLY A CA  1 
ATOM   1646  C C   . GLY A  1  259 ? -71.426 32.019  84.769  1.00 77.02  ?  259  GLY A C   1 
ATOM   1647  O O   . GLY A  1  259 ? -71.374 32.953  83.961  1.00 78.66  ?  259  GLY A O   1 
ATOM   1648  N N   . ASN A  1  260 ? -71.510 32.210  86.085  1.00 82.16  ?  260  ASN A N   1 
ATOM   1649  C CA  . ASN A  1  260 ? -71.471 33.552  86.651  1.00 81.26  ?  260  ASN A CA  1 
ATOM   1650  C C   . ASN A  1  260 ? -70.055 34.081  86.826  1.00 79.88  ?  260  ASN A C   1 
ATOM   1651  O O   . ASN A  1  260 ? -69.874 35.299  86.942  1.00 78.85  ?  260  ASN A O   1 
ATOM   1652  C CB  . ASN A  1  260 ? -72.196 33.578  87.995  1.00 82.43  ?  260  ASN A CB  1 
ATOM   1653  C CG  . ASN A  1  260 ? -73.658 33.238  87.865  1.00 83.58  ?  260  ASN A CG  1 
ATOM   1654  O OD1 . ASN A  1  260 ? -74.344 33.736  86.972  1.00 83.06  ?  260  ASN A OD1 1 
ATOM   1655  N ND2 . ASN A  1  260 ? -74.149 32.383  88.754  1.00 85.08  ?  260  ASN A ND2 1 
ATOM   1656  N N   . LEU A  1  261 ? -69.048 33.209  86.828  1.00 78.25  ?  261  LEU A N   1 
ATOM   1657  C CA  . LEU A  1  261 ? -67.682 33.622  87.145  1.00 76.89  ?  261  LEU A CA  1 
ATOM   1658  C C   . LEU A  1  261 ? -67.123 34.358  85.932  1.00 75.32  ?  261  LEU A C   1 
ATOM   1659  O O   . LEU A  1  261 ? -66.367 33.821  85.119  1.00 74.75  ?  261  LEU A O   1 
ATOM   1660  C CB  . LEU A  1  261 ? -66.828 32.422  87.531  1.00 77.26  ?  261  LEU A CB  1 
ATOM   1661  C CG  . LEU A  1  261 ? -67.268 31.676  88.791  1.00 78.88  ?  261  LEU A CG  1 
ATOM   1662  C CD1 . LEU A  1  261 ? -67.333 30.191  88.528  1.00 80.23  ?  261  LEU A CD1 1 
ATOM   1663  C CD2 . LEU A  1  261 ? -66.340 31.966  89.947  1.00 78.15  ?  261  LEU A CD2 1 
ATOM   1664  N N   . LYS A  1  262 ? -67.521 35.625  85.815  1.00 82.86  ?  262  LYS A N   1 
ATOM   1665  C CA  . LYS A  1  262 ? -67.140 36.466  84.689  1.00 81.54  ?  262  LYS A CA  1 
ATOM   1666  C C   . LYS A  1  262 ? -65.722 37.012  84.807  1.00 80.16  ?  262  LYS A C   1 
ATOM   1667  O O   . LYS A  1  262 ? -65.226 37.617  83.849  1.00 79.13  ?  262  LYS A O   1 
ATOM   1668  C CB  . LYS A  1  262 ? -68.129 37.627  84.551  1.00 81.48  ?  262  LYS A CB  1 
ATOM   1669  C CG  . LYS A  1  262 ? -68.967 37.580  83.284  1.00 82.72  ?  262  LYS A CG  1 
ATOM   1670  C CD  . LYS A  1  262 ? -70.029 36.494  83.358  1.00 83.62  ?  262  LYS A CD  1 
ATOM   1671  C CE  . LYS A  1  262 ? -70.893 36.488  82.102  1.00 85.19  ?  262  LYS A CE  1 
ATOM   1672  N NZ  . LYS A  1  262 ? -72.073 35.583  82.234  1.00 86.44  ?  262  LYS A NZ  1 
ATOM   1673  N N   . ASN A  1  263 ? -65.069 36.825  85.952  1.00 82.31  ?  263  ASN A N   1 
ATOM   1674  C CA  . ASN A  1  263 ? -63.712 37.296  86.169  1.00 81.05  ?  263  ASN A CA  1 
ATOM   1675  C C   . ASN A  1  263 ? -62.682 36.179  86.168  1.00 80.78  ?  263  ASN A C   1 
ATOM   1676  O O   . ASN A  1  263 ? -61.481 36.470  86.148  1.00 79.68  ?  263  ASN A O   1 
ATOM   1677  C CB  . ASN A  1  263 ? -63.619 38.043  87.507  1.00 81.06  ?  263  ASN A CB  1 
ATOM   1678  C CG  . ASN A  1  263 ? -63.692 39.546  87.346  1.00 80.40  ?  263  ASN A CG  1 
ATOM   1679  O OD1 . ASN A  1  263 ? -63.180 40.106  86.374  1.00 79.51  ?  263  ASN A OD1 1 
ATOM   1680  N ND2 . ASN A  1  263 ? -64.333 40.212  88.311  1.00 80.95  ?  263  ASN A ND2 1 
ATOM   1681  N N   . VAL A  1  264 ? -63.115 34.918  86.203  1.00 72.44  ?  264  VAL A N   1 
ATOM   1682  C CA  . VAL A  1  264 ? -62.184 33.800  86.277  1.00 72.26  ?  264  VAL A CA  1 
ATOM   1683  C C   . VAL A  1  264 ? -61.458 33.652  84.949  1.00 71.35  ?  264  VAL A C   1 
ATOM   1684  O O   . VAL A  1  264 ? -62.085 33.574  83.884  1.00 71.72  ?  264  VAL A O   1 
ATOM   1685  C CB  . VAL A  1  264 ? -62.920 32.507  86.656  1.00 73.89  ?  264  VAL A CB  1 
ATOM   1686  C CG1 . VAL A  1  264 ? -62.085 31.284  86.274  1.00 73.74  ?  264  VAL A CG1 1 
ATOM   1687  C CG2 . VAL A  1  264 ? -63.234 32.500  88.139  1.00 74.69  ?  264  VAL A CG2 1 
ATOM   1688  N N   . THR A  1  265 ? -60.128 33.621  85.005  1.00 65.61  ?  265  THR A N   1 
ATOM   1689  C CA  . THR A  1  265 ? -59.314 33.388  83.824  1.00 64.88  ?  265  THR A CA  1 
ATOM   1690  C C   . THR A  1  265 ? -58.716 31.989  83.773  1.00 64.99  ?  265  THR A C   1 
ATOM   1691  O O   . THR A  1  265 ? -58.414 31.505  82.679  1.00 64.88  ?  265  THR A O   1 
ATOM   1692  C CB  . THR A  1  265 ? -58.183 34.416  83.748  1.00 64.22  ?  265  THR A CB  1 
ATOM   1693  O OG1 . THR A  1  265 ? -57.384 34.335  84.934  1.00 63.35  ?  265  THR A OG1 1 
ATOM   1694  C CG2 . THR A  1  265 ? -58.757 35.811  83.629  1.00 66.86  ?  265  THR A CG2 1 
ATOM   1695  N N   . LEU A  1  266 ? -58.539 31.334  84.918  1.00 59.75  ?  266  LEU A N   1 
ATOM   1696  C CA  . LEU A  1  266 ? -57.930 30.014  84.996  1.00 59.75  ?  266  LEU A CA  1 
ATOM   1697  C C   . LEU A  1  266 ? -58.859 29.084  85.759  1.00 61.20  ?  266  LEU A C   1 
ATOM   1698  O O   . LEU A  1  266 ? -59.309 29.423  86.858  1.00 61.71  ?  266  LEU A O   1 
ATOM   1699  C CB  . LEU A  1  266 ? -56.564 30.084  85.688  1.00 58.59  ?  266  LEU A CB  1 
ATOM   1700  C CG  . LEU A  1  266 ? -55.921 28.761  86.105  1.00 58.41  ?  266  LEU A CG  1 
ATOM   1701  C CD1 . LEU A  1  266 ? -55.620 27.883  84.898  1.00 58.20  ?  266  LEU A CD1 1 
ATOM   1702  C CD2 . LEU A  1  266 ? -54.663 29.028  86.903  1.00 57.60  ?  266  LEU A CD2 1 
ATOM   1703  N N   . LEU A  1  267 ? -59.144 27.916  85.183  1.00 55.80  ?  267  LEU A N   1 
ATOM   1704  C CA  . LEU A  1  267 ? -59.993 26.908  85.822  1.00 55.62  ?  267  LEU A CA  1 
ATOM   1705  C C   . LEU A  1  267 ? -59.333 25.538  85.672  1.00 55.11  ?  267  LEU A C   1 
ATOM   1706  O O   . LEU A  1  267 ? -59.468 24.880  84.636  1.00 55.95  ?  267  LEU A O   1 
ATOM   1707  C CB  . LEU A  1  267 ? -61.404 26.913  85.236  1.00 57.53  ?  267  LEU A CB  1 
ATOM   1708  C CG  . LEU A  1  267 ? -62.361 25.883  85.846  1.00 59.87  ?  267  LEU A CG  1 
ATOM   1709  C CD1 . LEU A  1  267 ? -62.475 26.079  87.349  1.00 60.02  ?  267  LEU A CD1 1 
ATOM   1710  C CD2 . LEU A  1  267 ? -63.726 25.943  85.186  1.00 61.68  ?  267  LEU A CD2 1 
ATOM   1711  N N   . ASN A  1  268 ? -58.616 25.115  86.710  1.00 59.79  ?  268  ASN A N   1 
ATOM   1712  C CA  . ASN A  1  268 ? -57.976 23.806  86.749  1.00 59.35  ?  268  ASN A CA  1 
ATOM   1713  C C   . ASN A  1  268 ? -58.824 22.871  87.605  1.00 61.64  ?  268  ASN A C   1 
ATOM   1714  O O   . ASN A  1  268 ? -58.965 23.080  88.815  1.00 61.57  ?  268  ASN A O   1 
ATOM   1715  C CB  . ASN A  1  268 ? -56.552 23.912  87.297  1.00 56.62  ?  268  ASN A CB  1 
ATOM   1716  C CG  . ASN A  1  268 ? -55.539 24.317  86.233  1.00 55.18  ?  268  ASN A CG  1 
ATOM   1717  O OD1 . ASN A  1  268 ? -55.815 24.243  85.036  1.00 55.86  ?  268  ASN A OD1 1 
ATOM   1718  N ND2 . ASN A  1  268 ? -54.354 24.732  86.670  1.00 53.78  ?  268  ASN A ND2 1 
ATOM   1719  N N   . MET A  1  269 ? -59.389 21.838  86.973  1.00 58.71  ?  269  MET A N   1 
ATOM   1720  C CA  . MET A  1  269 ? -60.121 20.809  87.702  1.00 61.58  ?  269  MET A CA  1 
ATOM   1721  C C   . MET A  1  269 ? -59.787 19.417  87.176  1.00 62.25  ?  269  MET A C   1 
ATOM   1722  O O   . MET A  1  269 ? -60.582 18.487  87.359  1.00 65.15  ?  269  MET A O   1 
ATOM   1723  C CB  . MET A  1  269 ? -61.628 21.062  87.619  1.00 65.32  ?  269  MET A CB  1 
ATOM   1724  C CG  . MET A  1  269 ? -62.109 22.115  88.601  1.00 64.72  ?  269  MET A CG  1 
ATOM   1725  S SD  . MET A  1  269 ? -63.892 22.387  88.603  1.00 67.91  ?  269  MET A SD  1 
ATOM   1726  C CE  . MET A  1  269 ? -64.306 22.068  86.894  1.00 68.68  ?  269  MET A CE  1 
ATOM   1727  N N   . PHE A  1  270 ? -58.634 19.256  86.533  1.00 64.53  ?  270  PHE A N   1 
ATOM   1728  C CA  . PHE A  1  270 ? -58.249 17.992  85.927  1.00 64.55  ?  270  PHE A CA  1 
ATOM   1729  C C   . PHE A  1  270 ? -57.913 16.960  87.001  1.00 63.29  ?  270  PHE A C   1 
ATOM   1730  O O   . PHE A  1  270 ? -57.762 17.278  88.183  1.00 62.30  ?  270  PHE A O   1 
ATOM   1731  C CB  . PHE A  1  270 ? -57.061 18.190  84.986  1.00 61.82  ?  270  PHE A CB  1 
ATOM   1732  C CG  . PHE A  1  270 ? -55.866 18.834  85.636  1.00 58.07  ?  270  PHE A CG  1 
ATOM   1733  C CD1 . PHE A  1  270 ? -54.944 18.072  86.342  1.00 56.26  ?  270  PHE A CD1 1 
ATOM   1734  C CD2 . PHE A  1  270 ? -55.659 20.202  85.530  1.00 56.88  ?  270  PHE A CD2 1 
ATOM   1735  C CE1 . PHE A  1  270 ? -53.848 18.662  86.938  1.00 54.04  ?  270  PHE A CE1 1 
ATOM   1736  C CE2 . PHE A  1  270 ? -54.562 20.800  86.122  1.00 54.40  ?  270  PHE A CE2 1 
ATOM   1737  C CZ  . PHE A  1  270 ? -53.655 20.028  86.826  1.00 53.27  ?  270  PHE A CZ  1 
ATOM   1738  N N   . GLU A  1  271 ? -57.799 15.706  86.568  1.00 65.80  ?  271  GLU A N   1 
ATOM   1739  C CA  . GLU A  1  271 ? -57.473 14.579  87.442  1.00 64.83  ?  271  GLU A CA  1 
ATOM   1740  C C   . GLU A  1  271 ? -58.429 14.513  88.633  1.00 66.46  ?  271  GLU A C   1 
ATOM   1741  O O   . GLU A  1  271 ? -58.037 14.623  89.796  1.00 65.43  ?  271  GLU A O   1 
ATOM   1742  C CB  . GLU A  1  271 ? -56.018 14.647  87.909  1.00 61.89  ?  271  GLU A CB  1 
ATOM   1743  C CG  . GLU A  1  271 ? -55.027 14.018  86.946  1.00 60.59  ?  271  GLU A CG  1 
ATOM   1744  C CD  . GLU A  1  271 ? -53.602 14.067  87.465  1.00 58.53  ?  271  GLU A CD  1 
ATOM   1745  O OE1 . GLU A  1  271 ? -53.283 13.317  88.412  1.00 58.50  ?  271  GLU A OE1 1 
ATOM   1746  O OE2 . GLU A  1  271 ? -52.798 14.860  86.931  1.00 56.94  -1 271  GLU A OE2 1 
ATOM   1747  N N   . ASN A  1  272 ? -59.708 14.340  88.312  1.00 64.64  ?  272  ASN A N   1 
ATOM   1748  C CA  . ASN A  1  272 ? -60.767 14.219  89.305  1.00 66.59  ?  272  ASN A CA  1 
ATOM   1749  C C   . ASN A  1  272 ? -61.690 13.093  88.860  1.00 68.04  ?  272  ASN A C   1 
ATOM   1750  O O   . ASN A  1  272 ? -61.393 12.360  87.912  1.00 67.30  ?  272  ASN A O   1 
ATOM   1751  C CB  . ASN A  1  272 ? -61.519 15.548  89.468  1.00 68.88  ?  272  ASN A CB  1 
ATOM   1752  C CG  . ASN A  1  272 ? -60.977 16.391  90.605  1.00 67.42  ?  272  ASN A CG  1 
ATOM   1753  O OD1 . ASN A  1  272 ? -61.114 16.035  91.773  1.00 67.45  ?  272  ASN A OD1 1 
ATOM   1754  N ND2 . ASN A  1  272 ? -60.361 17.519  90.267  1.00 65.95  ?  272  ASN A ND2 1 
ATOM   1755  N N   . GLN A  1  273 ? -62.821 12.954  89.543  1.00 70.70  ?  273  GLN A N   1 
ATOM   1756  C CA  . GLN A  1  273 ? -63.847 11.994  89.158  1.00 71.76  ?  273  GLN A CA  1 
ATOM   1757  C C   . GLN A  1  273 ? -65.148 12.700  88.788  1.00 74.45  ?  273  GLN A C   1 
ATOM   1758  O O   . GLN A  1  273 ? -66.239 12.170  89.011  1.00 75.32  ?  273  GLN A O   1 
ATOM   1759  C CB  . GLN A  1  273 ? -64.077 10.972  90.269  1.00 71.16  ?  273  GLN A CB  1 
ATOM   1760  C CG  . GLN A  1  273 ? -62.796 10.359  90.811  1.00 68.67  ?  273  GLN A CG  1 
ATOM   1761  C CD  . GLN A  1  273 ? -63.050 9.082   91.583  1.00 68.22  ?  273  GLN A CD  1 
ATOM   1762  O OE1 . GLN A  1  273 ? -63.635 8.130   91.061  1.00 68.37  ?  273  GLN A OE1 1 
ATOM   1763  N NE2 . GLN A  1  273 ? -62.626 9.060   92.843  1.00 67.72  ?  273  GLN A NE2 1 
ATOM   1764  N N   . LEU A  1  274 ? -65.034 13.901  88.222  1.00 70.13  ?  274  LEU A N   1 
ATOM   1765  C CA  . LEU A  1  274 ? -66.197 14.639  87.750  1.00 72.34  ?  274  LEU A CA  1 
ATOM   1766  C C   . LEU A  1  274 ? -66.969 13.809  86.733  1.00 72.15  ?  274  LEU A C   1 
ATOM   1767  O O   . LEU A  1  274 ? -66.383 13.112  85.901  1.00 70.98  ?  274  LEU A O   1 
ATOM   1768  C CB  . LEU A  1  274 ? -65.763 15.966  87.124  1.00 73.17  ?  274  LEU A CB  1 
ATOM   1769  C CG  . LEU A  1  274 ? -65.700 17.225  87.989  1.00 74.19  ?  274  LEU A CG  1 
ATOM   1770  C CD1 . LEU A  1  274 ? -65.078 16.937  89.345  1.00 73.49  ?  274  LEU A CD1 1 
ATOM   1771  C CD2 . LEU A  1  274 ? -64.923 18.314  87.261  1.00 73.35  ?  274  LEU A CD2 1 
ATOM   1772  N N   . SER A  1  275 ? -68.293 13.883  86.805  1.00 74.17  ?  275  SER A N   1 
ATOM   1773  C CA  . SER A  1  275 ? -69.164 13.081  85.960  1.00 73.81  ?  275  SER A CA  1 
ATOM   1774  C C   . SER A  1  275 ? -70.213 13.981  85.319  1.00 74.47  ?  275  SER A C   1 
ATOM   1775  O O   . SER A  1  275 ? -70.223 15.202  85.507  1.00 74.97  ?  275  SER A O   1 
ATOM   1776  C CB  . SER A  1  275 ? -69.819 11.947  86.760  1.00 73.43  ?  275  SER A CB  1 
ATOM   1777  O OG  . SER A  1  275 ? -70.553 12.449  87.865  1.00 74.33  ?  275  SER A OG  1 
ATOM   1778  N N   . GLY A  1  276 ? -71.096 13.365  84.540  1.00 83.09  ?  276  GLY A N   1 
ATOM   1779  C CA  . GLY A  1  276 ? -72.109 14.124  83.835  1.00 83.18  ?  276  GLY A CA  1 
ATOM   1780  C C   . GLY A  1  276 ? -71.575 14.745  82.554  1.00 82.78  ?  276  GLY A C   1 
ATOM   1781  O O   . GLY A  1  276 ? -70.686 14.208  81.892  1.00 82.42  ?  276  GLY A O   1 
ATOM   1782  N N   . GLU A  1  277 ? -72.141 15.895  82.203  1.00 89.61  ?  277  GLU A N   1 
ATOM   1783  C CA  . GLU A  1  277 ? -71.806 16.588  80.971  1.00 88.90  ?  277  GLU A CA  1 
ATOM   1784  C C   . GLU A  1  277 ? -71.289 17.984  81.288  1.00 88.59  ?  277  GLU A C   1 
ATOM   1785  O O   . GLU A  1  277 ? -71.593 18.554  82.340  1.00 88.89  ?  277  GLU A O   1 
ATOM   1786  C CB  . GLU A  1  277 ? -73.017 16.676  80.039  1.00 88.33  ?  277  GLU A CB  1 
ATOM   1787  C CG  . GLU A  1  277 ? -74.004 15.533  80.211  1.00 88.55  ?  277  GLU A CG  1 
ATOM   1788  C CD  . GLU A  1  277 ? -74.880 15.317  78.987  1.00 87.86  ?  277  GLU A CD  1 
ATOM   1789  O OE1 . GLU A  1  277 ? -74.893 16.196  78.097  1.00 87.00  ?  277  GLU A OE1 1 
ATOM   1790  O OE2 . GLU A  1  277 ? -75.558 14.268  78.912  1.00 88.11  -1 277  GLU A OE2 1 
ATOM   1791  N N   . ILE A  1  278 ? -70.492 18.522  80.371  1.00 85.02  ?  278  ILE A N   1 
ATOM   1792  C CA  . ILE A  1  278 ? -69.967 19.874  80.524  1.00 84.11  ?  278  ILE A CA  1 
ATOM   1793  C C   . ILE A  1  278 ? -71.128 20.847  80.376  1.00 83.43  ?  278  ILE A C   1 
ATOM   1794  O O   . ILE A  1  278 ? -71.750 20.909  79.305  1.00 82.87  ?  278  ILE A O   1 
ATOM   1795  C CB  . ILE A  1  278 ? -68.858 20.174  79.505  1.00 83.06  ?  278  ILE A CB  1 
ATOM   1796  C CG1 . ILE A  1  278 ? -67.734 19.144  79.620  1.00 83.78  ?  278  ILE A CG1 1 
ATOM   1797  C CG2 . ILE A  1  278 ? -68.320 21.576  79.713  1.00 81.61  ?  278  ILE A CG2 1 
ATOM   1798  C CD1 . ILE A  1  278 ? -66.773 19.161  78.457  1.00 82.88  ?  278  ILE A CD1 1 
ATOM   1799  N N   . PRO A  1  279 ? -71.452 21.615  81.412  1.00 86.15  ?  279  PRO A N   1 
ATOM   1800  C CA  . PRO A  1  279 ? -72.582 22.547  81.334  1.00 85.54  ?  279  PRO A CA  1 
ATOM   1801  C C   . PRO A  1  279 ? -72.367 23.586  80.248  1.00 83.97  ?  279  PRO A C   1 
ATOM   1802  O O   . PRO A  1  279 ? -71.329 24.264  80.223  1.00 83.01  ?  279  PRO A O   1 
ATOM   1803  C CB  . PRO A  1  279 ? -72.602 23.195  82.727  1.00 85.78  ?  279  PRO A CB  1 
ATOM   1804  C CG  . PRO A  1  279 ? -71.265 22.924  83.318  1.00 85.98  ?  279  PRO A CG  1 
ATOM   1805  C CD  . PRO A  1  279 ? -70.780 21.650  82.722  1.00 86.71  ?  279  PRO A CD  1 
ATOM   1806  N N   . PRO A  1  280 ? -73.344 23.761  79.352  1.00 91.42  ?  280  PRO A N   1 
ATOM   1807  C CA  . PRO A  1  280 ? -73.204 24.768  78.284  1.00 89.92  ?  280  PRO A CA  1 
ATOM   1808  C C   . PRO A  1  280 ? -73.017 26.185  78.791  1.00 88.91  ?  280  PRO A C   1 
ATOM   1809  O O   . PRO A  1  280 ? -72.552 27.042  78.030  1.00 87.58  ?  280  PRO A O   1 
ATOM   1810  C CB  . PRO A  1  280 ? -74.517 24.633  77.499  1.00 89.87  ?  280  PRO A CB  1 
ATOM   1811  C CG  . PRO A  1  280 ? -75.008 23.266  77.810  1.00 91.17  ?  280  PRO A CG  1 
ATOM   1812  C CD  . PRO A  1  280 ? -74.582 22.978  79.216  1.00 92.16  ?  280  PRO A CD  1 
ATOM   1813  N N   . GLU A  1  281 ? -73.378 26.463  80.044  1.00 90.75  ?  281  GLU A N   1 
ATOM   1814  C CA  . GLU A  1  281 ? -73.231 27.792  80.622  1.00 89.83  ?  281  GLU A CA  1 
ATOM   1815  C C   . GLU A  1  281 ? -71.772 28.198  80.789  1.00 88.90  ?  281  GLU A C   1 
ATOM   1816  O O   . GLU A  1  281 ? -71.499 29.387  80.987  1.00 87.75  ?  281  GLU A O   1 
ATOM   1817  C CB  . GLU A  1  281 ? -73.956 27.867  81.978  1.00 90.79  ?  281  GLU A CB  1 
ATOM   1818  C CG  . GLU A  1  281 ? -75.404 27.313  82.034  1.00 91.74  ?  281  GLU A CG  1 
ATOM   1819  C CD  . GLU A  1  281 ? -75.504 25.792  81.923  1.00 92.93  ?  281  GLU A CD  1 
ATOM   1820  O OE1 . GLU A  1  281 ? -74.524 25.161  81.490  1.00 92.80  ?  281  GLU A OE1 1 
ATOM   1821  O OE2 . GLU A  1  281 ? -76.564 25.225  82.270  1.00 93.94  -1 281  GLU A OE2 1 
ATOM   1822  N N   . ILE A  1  282 ? -70.836 27.248  80.702  1.00 85.78  ?  282  ILE A N   1 
ATOM   1823  C CA  . ILE A  1  282 ? -69.414 27.575  80.783  1.00 84.69  ?  282  ILE A CA  1 
ATOM   1824  C C   . ILE A  1  282 ? -69.024 28.549  79.678  1.00 82.98  ?  282  ILE A C   1 
ATOM   1825  O O   . ILE A  1  282 ? -68.104 29.361  79.844  1.00 81.66  ?  282  ILE A O   1 
ATOM   1826  C CB  . ILE A  1  282 ? -68.584 26.274  80.743  1.00 85.51  ?  282  ILE A CB  1 
ATOM   1827  C CG1 . ILE A  1  282 ? -68.444 25.698  82.151  1.00 86.68  ?  282  ILE A CG1 1 
ATOM   1828  C CG2 . ILE A  1  282 ? -67.211 26.501  80.131  1.00 84.10  ?  282  ILE A CG2 1 
ATOM   1829  C CD1 . ILE A  1  282 ? -67.471 24.552  82.245  1.00 87.36  ?  282  ILE A CD1 1 
ATOM   1830  N N   . GLY A  1  283 ? -69.744 28.521  78.555  1.00 89.06  ?  283  GLY A N   1 
ATOM   1831  C CA  . GLY A  1  283 ? -69.508 29.473  77.486  1.00 87.59  ?  283  GLY A CA  1 
ATOM   1832  C C   . GLY A  1  283 ? -69.683 30.924  77.887  1.00 86.57  ?  283  GLY A C   1 
ATOM   1833  O O   . GLY A  1  283 ? -69.190 31.812  77.183  1.00 85.42  ?  283  GLY A O   1 
ATOM   1834  N N   . ASN A  1  284 ? -70.387 31.190  78.991  1.00 90.93  ?  284  ASN A N   1 
ATOM   1835  C CA  . ASN A  1  284 ? -70.513 32.554  79.494  1.00 90.06  ?  284  ASN A CA  1 
ATOM   1836  C C   . ASN A  1  284 ? -69.260 33.033  80.219  1.00 89.21  ?  284  ASN A C   1 
ATOM   1837  O O   . ASN A  1  284 ? -69.171 34.222  80.544  1.00 88.34  ?  284  ASN A O   1 
ATOM   1838  C CB  . ASN A  1  284 ? -71.720 32.677  80.430  1.00 91.33  ?  284  ASN A CB  1 
ATOM   1839  C CG  . ASN A  1  284 ? -73.041 32.825  79.681  1.00 93.45  ?  284  ASN A CG  1 
ATOM   1840  O OD1 . ASN A  1  284 ? -73.264 33.809  78.972  1.00 95.46  ?  284  ASN A OD1 1 
ATOM   1841  N ND2 . ASN A  1  284 ? -73.927 31.834  79.858  1.00 94.50  ?  284  ASN A ND2 1 
ATOM   1842  N N   . MET A  1  285 ? -68.293 32.147  80.472  1.00 78.96  ?  285  MET A N   1 
ATOM   1843  C CA  . MET A  1  285 ? -67.037 32.514  81.130  1.00 77.97  ?  285  MET A CA  1 
ATOM   1844  C C   . MET A  1  285 ? -66.141 33.238  80.124  1.00 76.43  ?  285  MET A C   1 
ATOM   1845  O O   . MET A  1  285 ? -65.120 32.729  79.656  1.00 75.93  ?  285  MET A O   1 
ATOM   1846  C CB  . MET A  1  285 ? -66.347 31.282  81.699  1.00 78.65  ?  285  MET A CB  1 
ATOM   1847  C CG  . MET A  1  285 ? -67.081 30.634  82.857  1.00 80.25  ?  285  MET A CG  1 
ATOM   1848  S SD  . MET A  1  285 ? -66.152 29.279  83.600  1.00 81.00  ?  285  MET A SD  1 
ATOM   1849  C CE  . MET A  1  285 ? -65.403 30.106  85.000  1.00 79.93  ?  285  MET A CE  1 
ATOM   1850  N N   . THR A  1  286 ? -66.544 34.468  79.802  1.00 78.43  ?  286  THR A N   1 
ATOM   1851  C CA  . THR A  1  286 ? -65.945 35.231  78.713  1.00 77.61  ?  286  THR A CA  1 
ATOM   1852  C C   . THR A  1  286 ? -64.564 35.788  79.046  1.00 76.12  ?  286  THR A C   1 
ATOM   1853  O O   . THR A  1  286 ? -63.948 36.414  78.174  1.00 76.20  ?  286  THR A O   1 
ATOM   1854  C CB  . THR A  1  286 ? -66.880 36.370  78.313  1.00 79.50  ?  286  THR A CB  1 
ATOM   1855  O OG1 . THR A  1  286 ? -67.299 37.069  79.491  1.00 79.80  ?  286  THR A OG1 1 
ATOM   1856  C CG2 . THR A  1  286 ? -68.103 35.820  77.589  1.00 81.52  ?  286  THR A CG2 1 
ATOM   1857  N N   . ALA A  1  287 ? -64.071 35.594  80.269  1.00 73.97  ?  287  ALA A N   1 
ATOM   1858  C CA  . ALA A  1  287 ? -62.713 35.969  80.638  1.00 72.90  ?  287  ALA A CA  1 
ATOM   1859  C C   . ALA A  1  287 ? -61.785 34.769  80.742  1.00 72.91  ?  287  ALA A C   1 
ATOM   1860  O O   . ALA A  1  287 ? -60.613 34.934  81.094  1.00 72.06  ?  287  ALA A O   1 
ATOM   1861  C CB  . ALA A  1  287 ? -62.713 36.731  81.965  1.00 72.76  ?  287  ALA A CB  1 
ATOM   1862  N N   . LEU A  1  288 ? -62.279 33.573  80.431  1.00 70.68  ?  288  LEU A N   1 
ATOM   1863  C CA  . LEU A  1  288 ? -61.515 32.353  80.647  1.00 70.85  ?  288  LEU A CA  1 
ATOM   1864  C C   . LEU A  1  288 ? -60.355 32.264  79.662  1.00 69.92  ?  288  LEU A C   1 
ATOM   1865  O O   . LEU A  1  288 ? -60.530 32.435  78.452  1.00 69.91  ?  288  LEU A O   1 
ATOM   1866  C CB  . LEU A  1  288 ? -62.430 31.136  80.513  1.00 72.42  ?  288  LEU A CB  1 
ATOM   1867  C CG  . LEU A  1  288 ? -61.957 29.790  81.065  1.00 73.07  ?  288  LEU A CG  1 
ATOM   1868  C CD1 . LEU A  1  288 ? -61.728 29.875  82.563  1.00 73.02  ?  288  LEU A CD1 1 
ATOM   1869  C CD2 . LEU A  1  288 ? -62.964 28.696  80.737  1.00 74.92  ?  288  LEU A CD2 1 
ATOM   1870  N N   . ASP A  1  289 ? -59.163 32.010  80.193  1.00 71.08  ?  289  ASP A N   1 
ATOM   1871  C CA  . ASP A  1  289 ? -57.940 31.861  79.417  1.00 70.31  ?  289  ASP A CA  1 
ATOM   1872  C C   . ASP A  1  289 ? -57.514 30.405  79.254  1.00 70.68  ?  289  ASP A C   1 
ATOM   1873  O O   . ASP A  1  289 ? -57.091 30.006  78.165  1.00 70.69  ?  289  ASP A O   1 
ATOM   1874  C CB  . ASP A  1  289 ? -56.814 32.656  80.080  1.00 69.32  ?  289  ASP A CB  1 
ATOM   1875  C CG  . ASP A  1  289 ? -55.506 32.522  79.349  1.00 68.83  ?  289  ASP A CG  1 
ATOM   1876  O OD1 . ASP A  1  289 ? -55.525 32.361  78.109  1.00 69.08  ?  289  ASP A OD1 1 
ATOM   1877  O OD2 . ASP A  1  289 ? -54.456 32.564  80.020  1.00 68.36  -1 289  ASP A OD2 1 
ATOM   1878  N N   . THR A  1  290 ? -57.606 29.607  80.319  1.00 63.87  ?  290  THR A N   1 
ATOM   1879  C CA  . THR A  1  290 ? -57.209 28.205  80.313  1.00 64.19  ?  290  THR A CA  1 
ATOM   1880  C C   . THR A  1  290 ? -58.306 27.370  80.953  1.00 65.69  ?  290  THR A C   1 
ATOM   1881  O O   . THR A  1  290 ? -58.755 27.676  82.063  1.00 65.95  ?  290  THR A O   1 
ATOM   1882  C CB  . THR A  1  290 ? -55.904 28.008  81.080  1.00 63.01  ?  290  THR A CB  1 
ATOM   1883  O OG1 . THR A  1  290 ? -54.891 28.840  80.508  1.00 62.16  ?  290  THR A OG1 1 
ATOM   1884  C CG2 . THR A  1  290 ? -55.474 26.555  81.034  1.00 63.06  ?  290  THR A CG2 1 
ATOM   1885  N N   . LEU A  1  291 ? -58.733 26.318  80.257  1.00 60.59  ?  291  LEU A N   1 
ATOM   1886  C CA  . LEU A  1  291 ? -59.770 25.415  80.747  1.00 62.63  ?  291  LEU A CA  1 
ATOM   1887  C C   . LEU A  1  291 ? -59.238 23.992  80.663  1.00 63.26  ?  291  LEU A C   1 
ATOM   1888  O O   . LEU A  1  291 ? -59.034 23.468  79.565  1.00 63.64  ?  291  LEU A O   1 
ATOM   1889  C CB  . LEU A  1  291 ? -61.060 25.573  79.940  1.00 64.13  ?  291  LEU A CB  1 
ATOM   1890  C CG  . LEU A  1  291 ? -62.138 24.502  80.107  1.00 66.66  ?  291  LEU A CG  1 
ATOM   1891  C CD1 . LEU A  1  291 ? -62.483 24.302  81.572  1.00 67.57  ?  291  LEU A CD1 1 
ATOM   1892  C CD2 . LEU A  1  291 ? -63.379 24.876  79.317  1.00 67.42  ?  291  LEU A CD2 1 
ATOM   1893  N N   . SER A  1  292 ? -59.022 23.362  81.813  1.00 60.58  ?  292  SER A N   1 
ATOM   1894  C CA  . SER A  1  292 ? -58.427 22.031  81.870  1.00 60.97  ?  292  SER A CA  1 
ATOM   1895  C C   . SER A  1  292 ? -59.326 21.123  82.697  1.00 63.89  ?  292  SER A C   1 
ATOM   1896  O O   . SER A  1  292 ? -59.420 21.278  83.920  1.00 63.56  ?  292  SER A O   1 
ATOM   1897  C CB  . SER A  1  292 ? -57.016 22.088  82.455  1.00 57.82  ?  292  SER A CB  1 
ATOM   1898  O OG  . SER A  1  292 ? -56.427 20.802  82.503  1.00 57.71  ?  292  SER A OG  1 
ATOM   1899  N N   . LEU A  1  293 ? -59.992 20.182  82.027  1.00 62.83  ?  293  LEU A N   1 
ATOM   1900  C CA  . LEU A  1  293 ? -60.811 19.168  82.680  1.00 66.42  ?  293  LEU A CA  1 
ATOM   1901  C C   . LEU A  1  293 ? -60.350 17.765  82.300  1.00 67.99  ?  293  LEU A C   1 
ATOM   1902  O O   . LEU A  1  293 ? -61.158 16.837  82.241  1.00 69.79  ?  293  LEU A O   1 
ATOM   1903  C CB  . LEU A  1  293 ? -62.290 19.351  82.331  1.00 68.27  ?  293  LEU A CB  1 
ATOM   1904  C CG  . LEU A  1  293 ? -62.873 20.765  82.392  1.00 66.53  ?  293  LEU A CG  1 
ATOM   1905  C CD1 . LEU A  1  293 ? -64.323 20.776  81.950  1.00 67.85  ?  293  LEU A CD1 1 
ATOM   1906  C CD2 . LEU A  1  293 ? -62.749 21.318  83.788  1.00 65.83  ?  293  LEU A CD2 1 
ATOM   1907  N N   . HIS A  1  294 ? -59.058 17.595  82.035  1.00 68.82  ?  294  HIS A N   1 
ATOM   1908  C CA  . HIS A  1  294 ? -58.571 16.312  81.554  1.00 68.01  ?  294  HIS A CA  1 
ATOM   1909  C C   . HIS A  1  294 ? -58.517 15.287  82.686  1.00 66.31  ?  294  HIS A C   1 
ATOM   1910  O O   . HIS A  1  294 ? -58.540 15.628  83.872  1.00 65.36  ?  294  HIS A O   1 
ATOM   1911  C CB  . HIS A  1  294 ? -57.202 16.467  80.881  1.00 64.95  ?  294  HIS A CB  1 
ATOM   1912  C CG  . HIS A  1  294 ? -56.053 16.638  81.830  1.00 60.60  ?  294  HIS A CG  1 
ATOM   1913  N ND1 . HIS A  1  294 ? -55.523 15.596  82.561  1.00 58.84  ?  294  HIS A ND1 1 
ATOM   1914  C CD2 . HIS A  1  294 ? -55.298 17.724  82.127  1.00 57.77  ?  294  HIS A CD2 1 
ATOM   1915  C CE1 . HIS A  1  294 ? -54.510 16.037  83.286  1.00 55.77  ?  294  HIS A CE1 1 
ATOM   1916  N NE2 . HIS A  1  294 ? -54.350 17.325  83.039  1.00 55.01  ?  294  HIS A NE2 1 
ATOM   1917  N N   . THR A  1  295 ? -58.464 14.010  82.297  1.00 68.47  ?  295  THR A N   1 
ATOM   1918  C CA  . THR A  1  295 ? -58.424 12.879  83.228  1.00 67.18  ?  295  THR A CA  1 
ATOM   1919  C C   . THR A  1  295 ? -59.608 12.922  84.202  1.00 68.87  ?  295  THR A C   1 
ATOM   1920  O O   . THR A  1  295 ? -59.454 13.004  85.423  1.00 67.89  ?  295  THR A O   1 
ATOM   1921  C CB  . THR A  1  295 ? -57.084 12.824  83.977  1.00 64.00  ?  295  THR A CB  1 
ATOM   1922  O OG1 . THR A  1  295 ? -56.013 13.105  83.070  1.00 62.43  ?  295  THR A OG1 1 
ATOM   1923  C CG2 . THR A  1  295 ? -56.857 11.445  84.574  1.00 63.15  ?  295  THR A CG2 1 
ATOM   1924  N N   . ASN A  1  296 ? -60.810 12.850  83.630  1.00 67.21  ?  296  ASN A N   1 
ATOM   1925  C CA  . ASN A  1  296 ? -62.046 12.851  84.401  1.00 68.91  ?  296  ASN A CA  1 
ATOM   1926  C C   . ASN A  1  296 ? -62.979 11.796  83.823  1.00 69.58  ?  296  ASN A C   1 
ATOM   1927  O O   . ASN A  1  296 ? -62.616 11.045  82.912  1.00 68.76  ?  296  ASN A O   1 
ATOM   1928  C CB  . ASN A  1  296 ? -62.708 14.234  84.391  1.00 71.31  ?  296  ASN A CB  1 
ATOM   1929  C CG  . ASN A  1  296 ? -62.276 15.094  85.556  1.00 70.85  ?  296  ASN A CG  1 
ATOM   1930  O OD1 . ASN A  1  296 ? -62.766 14.936  86.671  1.00 71.13  ?  296  ASN A OD1 1 
ATOM   1931  N ND2 . ASN A  1  296 ? -61.353 16.014  85.302  1.00 69.81  ?  296  ASN A ND2 1 
ATOM   1932  N N   . LYS A  1  297 ? -64.199 11.743  84.350  1.00 72.19  ?  297  LYS A N   1 
ATOM   1933  C CA  . LYS A  1  297 ? -65.208 10.811  83.863  1.00 72.51  ?  297  LYS A CA  1 
ATOM   1934  C C   . LYS A  1  297 ? -66.414 11.543  83.280  1.00 74.24  ?  297  LYS A C   1 
ATOM   1935  O O   . LYS A  1  297 ? -67.548 11.075  83.391  1.00 74.60  ?  297  LYS A O   1 
ATOM   1936  C CB  . LYS A  1  297 ? -65.628 9.846   84.970  1.00 71.90  ?  297  LYS A CB  1 
ATOM   1937  C CG  . LYS A  1  297 ? -64.526 8.859   85.333  1.00 69.81  ?  297  LYS A CG  1 
ATOM   1938  C CD  . LYS A  1  297 ? -64.934 7.931   86.460  1.00 69.32  ?  297  LYS A CD  1 
ATOM   1939  C CE  . LYS A  1  297 ? -63.766 7.062   86.909  1.00 67.24  ?  297  LYS A CE  1 
ATOM   1940  N NZ  . LYS A  1  297 ? -64.065 6.381   88.204  1.00 66.92  ?  297  LYS A NZ  1 
ATOM   1941  N N   . LEU A  1  298 ? -66.171 12.686  82.643  1.00 76.76  ?  298  LEU A N   1 
ATOM   1942  C CA  . LEU A  1  298 ? -67.225 13.418  81.958  1.00 77.71  ?  298  LEU A CA  1 
ATOM   1943  C C   . LEU A  1  298 ? -67.763 12.608  80.784  1.00 77.22  ?  298  LEU A C   1 
ATOM   1944  O O   . LEU A  1  298 ? -67.077 11.748  80.227  1.00 76.37  ?  298  LEU A O   1 
ATOM   1945  C CB  . LEU A  1  298 ? -66.697 14.765  81.462  1.00 78.05  ?  298  LEU A CB  1 
ATOM   1946  C CG  . LEU A  1  298 ? -66.118 15.694  82.529  1.00 78.50  ?  298  LEU A CG  1 
ATOM   1947  C CD1 . LEU A  1  298 ? -66.059 17.126  82.037  1.00 78.25  ?  298  LEU A CD1 1 
ATOM   1948  C CD2 . LEU A  1  298 ? -66.951 15.615  83.796  1.00 79.07  ?  298  LEU A CD2 1 
ATOM   1949  N N   . THR A  1  299 ? -69.009 12.884  80.413  1.00 83.41  ?  299  THR A N   1 
ATOM   1950  C CA  . THR A  1  299 ? -69.656 12.196  79.306  1.00 82.93  ?  299  THR A CA  1 
ATOM   1951  C C   . THR A  1  299 ? -70.407 13.216  78.462  1.00 82.99  ?  299  THR A C   1 
ATOM   1952  O O   . THR A  1  299 ? -70.517 14.391  78.819  1.00 83.26  ?  299  THR A O   1 
ATOM   1953  C CB  . THR A  1  299 ? -70.606 11.093  79.802  1.00 82.72  ?  299  THR A CB  1 
ATOM   1954  O OG1 . THR A  1  299 ? -71.485 11.620  80.809  1.00 83.33  ?  299  THR A OG1 1 
ATOM   1955  C CG2 . THR A  1  299 ? -69.817 9.915   80.373  1.00 82.03  ?  299  THR A CG2 1 
ATOM   1956  N N   . GLY A  1  300 ? -70.925 12.756  77.326  1.00 86.39  ?  300  GLY A N   1 
ATOM   1957  C CA  . GLY A  1  300 ? -71.704 13.599  76.451  1.00 86.08  ?  300  GLY A CA  1 
ATOM   1958  C C   . GLY A  1  300 ? -70.840 14.405  75.502  1.00 85.66  ?  300  GLY A C   1 
ATOM   1959  O O   . GLY A  1  300 ? -69.611 14.312  75.516  1.00 85.73  ?  300  GLY A O   1 
ATOM   1960  N N   . PRO A  1  301 ? -71.469 15.221  74.662  1.00 88.46  ?  301  PRO A N   1 
ATOM   1961  C CA  . PRO A  1  301 ? -70.728 15.969  73.640  1.00 87.75  ?  301  PRO A CA  1 
ATOM   1962  C C   . PRO A  1  301 ? -70.082 17.233  74.198  1.00 87.50  ?  301  PRO A C   1 
ATOM   1963  O O   . PRO A  1  301 ? -70.362 17.678  75.312  1.00 87.85  ?  301  PRO A O   1 
ATOM   1964  C CB  . PRO A  1  301 ? -71.809 16.311  72.613  1.00 87.01  ?  301  PRO A CB  1 
ATOM   1965  C CG  . PRO A  1  301 ? -73.043 16.441  73.431  1.00 87.29  ?  301  PRO A CG  1 
ATOM   1966  C CD  . PRO A  1  301 ? -72.923 15.429  74.548  1.00 88.21  ?  301  PRO A CD  1 
ATOM   1967  N N   . ILE A  1  302 ? -69.199 17.807  73.389  1.00 87.80  ?  302  ILE A N   1 
ATOM   1968  C CA  . ILE A  1  302 ? -68.601 19.103  73.733  1.00 87.01  ?  302  ILE A CA  1 
ATOM   1969  C C   . ILE A  1  302 ? -69.660 20.187  73.569  1.00 86.21  ?  302  ILE A C   1 
ATOM   1970  O O   . ILE A  1  302 ? -70.347 20.226  72.530  1.00 85.72  ?  302  ILE A O   1 
ATOM   1971  C CB  . ILE A  1  302 ? -67.386 19.400  72.841  1.00 86.11  ?  302  ILE A CB  1 
ATOM   1972  C CG1 . ILE A  1  302 ? -66.081 18.853  73.425  1.00 86.57  ?  302  ILE A CG1 1 
ATOM   1973  C CG2 . ILE A  1  302 ? -67.231 20.897  72.608  1.00 84.66  ?  302  ILE A CG2 1 
ATOM   1974  C CD1 . ILE A  1  302 ? -65.926 17.367  73.277  1.00 87.66  ?  302  ILE A CD1 1 
ATOM   1975  N N   . PRO A  1  303 ? -69.838 21.076  74.545  1.00 88.67  ?  303  PRO A N   1 
ATOM   1976  C CA  . PRO A  1  303 ? -70.820 22.154  74.378  1.00 87.83  ?  303  PRO A CA  1 
ATOM   1977  C C   . PRO A  1  303 ? -70.384 23.107  73.275  1.00 86.34  ?  303  PRO A C   1 
ATOM   1978  O O   . PRO A  1  303 ? -69.264 23.624  73.284  1.00 85.57  ?  303  PRO A O   1 
ATOM   1979  C CB  . PRO A  1  303 ? -70.836 22.840  75.750  1.00 87.96  ?  303  PRO A CB  1 
ATOM   1980  C CG  . PRO A  1  303 ? -69.513 22.509  76.359  1.00 88.22  ?  303  PRO A CG  1 
ATOM   1981  C CD  . PRO A  1  303 ? -69.140 21.149  75.840  1.00 89.13  ?  303  PRO A CD  1 
ATOM   1982  N N   . SER A  1  304 ? -71.287 23.335  72.317  1.00 91.52  ?  304  SER A N   1 
ATOM   1983  C CA  . SER A  1  304 ? -71.004 24.262  71.228  1.00 90.72  ?  304  SER A CA  1 
ATOM   1984  C C   . SER A  1  304 ? -70.748 25.670  71.742  1.00 89.98  ?  304  SER A C   1 
ATOM   1985  O O   . SER A  1  304 ? -70.178 26.494  71.018  1.00 89.57  ?  304  SER A O   1 
ATOM   1986  C CB  . SER A  1  304 ? -72.160 24.272  70.228  1.00 93.70  ?  304  SER A CB  1 
ATOM   1987  O OG  . SER A  1  304 ? -73.334 24.799  70.824  1.00 96.36  ?  304  SER A OG  1 
ATOM   1988  N N   . THR A  1  305 ? -71.168 25.963  72.971  1.00 90.19  ?  305  THR A N   1 
ATOM   1989  C CA  . THR A  1  305 ? -70.924 27.246  73.611  1.00 89.45  ?  305  THR A CA  1 
ATOM   1990  C C   . THR A  1  305 ? -69.467 27.469  74.006  1.00 88.23  ?  305  THR A C   1 
ATOM   1991  O O   . THR A  1  305 ? -69.180 28.485  74.643  1.00 87.38  ?  305  THR A O   1 
ATOM   1992  C CB  . THR A  1  305 ? -71.817 27.406  74.842  1.00 90.11  ?  305  THR A CB  1 
ATOM   1993  O OG1 . THR A  1  305 ? -71.440 26.450  75.840  1.00 90.81  ?  305  THR A OG1 1 
ATOM   1994  C CG2 . THR A  1  305 ? -73.269 27.197  74.467  1.00 92.51  ?  305  THR A CG2 1 
ATOM   1995  N N   . LEU A  1  306 ? -68.542 26.554  73.718  1.00 85.29  ?  306  LEU A N   1 
ATOM   1996  C CA  . LEU A  1  306 ? -67.147 26.885  73.979  1.00 84.35  ?  306  LEU A CA  1 
ATOM   1997  C C   . LEU A  1  306 ? -66.634 27.965  73.035  1.00 82.89  ?  306  LEU A C   1 
ATOM   1998  O O   . LEU A  1  306 ? -65.697 28.687  73.391  1.00 81.83  ?  306  LEU A O   1 
ATOM   1999  C CB  . LEU A  1  306 ? -66.285 25.627  73.901  1.00 85.08  ?  306  LEU A CB  1 
ATOM   2000  C CG  . LEU A  1  306 ? -66.636 24.658  75.031  1.00 86.68  ?  306  LEU A CG  1 
ATOM   2001  C CD1 . LEU A  1  306 ? -65.662 23.498  75.105  1.00 87.39  ?  306  LEU A CD1 1 
ATOM   2002  C CD2 . LEU A  1  306 ? -66.693 25.402  76.359  1.00 86.47  ?  306  LEU A CD2 1 
ATOM   2003  N N   . GLY A  1  307 ? -67.241 28.101  71.853  1.00 88.13  ?  307  GLY A N   1 
ATOM   2004  C CA  . GLY A  1  307 ? -66.832 29.112  70.892  1.00 87.91  ?  307  GLY A CA  1 
ATOM   2005  C C   . GLY A  1  307 ? -67.067 30.550  71.319  1.00 88.19  ?  307  GLY A C   1 
ATOM   2006  O O   . GLY A  1  307 ? -66.487 31.458  70.715  1.00 88.67  ?  307  GLY A O   1 
ATOM   2007  N N   . ASN A  1  308 ? -67.899 30.787  72.340  1.00 90.44  ?  308  ASN A N   1 
ATOM   2008  C CA  . ASN A  1  308 ? -68.096 32.162  72.801  1.00 91.38  ?  308  ASN A CA  1 
ATOM   2009  C C   . ASN A  1  308 ? -66.884 32.722  73.529  1.00 89.02  ?  308  ASN A C   1 
ATOM   2010  O O   . ASN A  1  308 ? -66.710 33.944  73.554  1.00 89.92  ?  308  ASN A O   1 
ATOM   2011  C CB  . ASN A  1  308 ? -69.322 32.295  73.712  1.00 92.72  ?  308  ASN A CB  1 
ATOM   2012  C CG  . ASN A  1  308 ? -70.484 31.442  73.266  1.00 95.01  ?  308  ASN A CG  1 
ATOM   2013  O OD1 . ASN A  1  308 ? -70.445 30.226  73.365  1.00 93.45  ?  308  ASN A OD1 1 
ATOM   2014  N ND2 . ASN A  1  308 ? -71.535 32.086  72.770  1.00 99.38  ?  308  ASN A ND2 1 
ATOM   2015  N N   . ILE A  1  309 ? -66.042 31.877  74.119  1.00 82.37  ?  309  ILE A N   1 
ATOM   2016  C CA  . ILE A  1  309 ? -64.914 32.385  74.895  1.00 81.02  ?  309  ILE A CA  1 
ATOM   2017  C C   . ILE A  1  309 ? -63.823 32.762  73.898  1.00 80.25  ?  309  ILE A C   1 
ATOM   2018  O O   . ILE A  1  309 ? -63.053 31.915  73.439  1.00 80.16  ?  309  ILE A O   1 
ATOM   2019  C CB  . ILE A  1  309 ? -64.417 31.376  75.931  1.00 81.65  ?  309  ILE A CB  1 
ATOM   2020  C CG1 . ILE A  1  309 ? -65.508 31.096  76.959  1.00 82.80  ?  309  ILE A CG1 1 
ATOM   2021  C CG2 . ILE A  1  309 ? -63.200 31.922  76.656  1.00 80.56  ?  309  ILE A CG2 1 
ATOM   2022  C CD1 . ILE A  1  309 ? -65.920 29.653  77.015  1.00 84.39  ?  309  ILE A CD1 1 
ATOM   2023  N N   . LYS A  1  310 ? -63.767 34.046  73.553  1.00 78.34  ?  310  LYS A N   1 
ATOM   2024  C CA  . LYS A  1  310 ? -62.796 34.556  72.597  1.00 78.36  ?  310  LYS A CA  1 
ATOM   2025  C C   . LYS A  1  310 ? -61.404 34.707  73.194  1.00 76.57  ?  310  LYS A C   1 
ATOM   2026  O O   . LYS A  1  310 ? -60.441 34.882  72.442  1.00 76.37  ?  310  LYS A O   1 
ATOM   2027  C CB  . LYS A  1  310 ? -63.277 35.896  72.036  1.00 82.08  ?  310  LYS A CB  1 
ATOM   2028  C CG  . LYS A  1  310 ? -64.703 35.868  71.479  1.00 85.48  ?  310  LYS A CG  1 
ATOM   2029  C CD  . LYS A  1  310 ? -64.986 34.590  70.689  1.00 84.97  ?  310  LYS A CD  1 
ATOM   2030  C CE  . LYS A  1  310 ? -66.136 34.773  69.709  1.00 89.40  ?  310  LYS A CE  1 
ATOM   2031  N NZ  . LYS A  1  310 ? -66.186 33.680  68.695  1.00 89.44  ?  310  LYS A NZ  1 
ATOM   2032  N N   . THR A  1  311 ? -61.280 34.656  74.519  1.00 74.38  ?  311  THR A N   1 
ATOM   2033  C CA  . THR A  1  311 ? -59.993 34.743  75.194  1.00 73.35  ?  311  THR A CA  1 
ATOM   2034  C C   . THR A  1  311 ? -59.363 33.379  75.465  1.00 73.67  ?  311  THR A C   1 
ATOM   2035  O O   . THR A  1  311 ? -58.215 33.326  75.920  1.00 73.14  ?  311  THR A O   1 
ATOM   2036  C CB  . THR A  1  311 ? -60.141 35.506  76.520  1.00 73.04  ?  311  THR A CB  1 
ATOM   2037  O OG1 . THR A  1  311 ? -61.388 35.165  77.139  1.00 73.87  ?  311  THR A OG1 1 
ATOM   2038  C CG2 . THR A  1  311 ? -60.100 37.005  76.284  1.00 73.63  ?  311  THR A CG2 1 
ATOM   2039  N N   . LEU A  1  312 ? -60.074 32.285  75.195  1.00 72.58  ?  312  LEU A N   1 
ATOM   2040  C CA  . LEU A  1  312 ? -59.577 30.956  75.533  1.00 73.03  ?  312  LEU A CA  1 
ATOM   2041  C C   . LEU A  1  312 ? -58.383 30.603  74.658  1.00 72.62  ?  312  LEU A C   1 
ATOM   2042  O O   . LEU A  1  312 ? -58.501 30.545  73.429  1.00 72.89  ?  312  LEU A O   1 
ATOM   2043  C CB  . LEU A  1  312 ? -60.682 29.916  75.363  1.00 74.40  ?  312  LEU A CB  1 
ATOM   2044  C CG  . LEU A  1  312 ? -60.442 28.532  75.967  1.00 75.22  ?  312  LEU A CG  1 
ATOM   2045  C CD1 . LEU A  1  312 ? -60.208 28.627  77.467  1.00 74.96  ?  312  LEU A CD1 1 
ATOM   2046  C CD2 . LEU A  1  312 ? -61.620 27.623  75.669  1.00 76.90  ?  312  LEU A CD2 1 
ATOM   2047  N N   . ALA A  1  313 ? -57.232 30.374  75.290  1.00 67.19  ?  313  ALA A N   1 
ATOM   2048  C CA  . ALA A  1  313 ? -56.014 29.994  74.589  1.00 66.93  ?  313  ALA A CA  1 
ATOM   2049  C C   . ALA A  1  313 ? -55.649 28.526  74.744  1.00 67.32  ?  313  ALA A C   1 
ATOM   2050  O O   . ALA A  1  313 ? -55.057 27.952  73.829  1.00 67.57  ?  313  ALA A O   1 
ATOM   2051  C CB  . ALA A  1  313 ? -54.835 30.851  75.066  1.00 66.10  ?  313  ALA A CB  1 
ATOM   2052  N N   . VAL A  1  314 ? -55.956 27.920  75.887  1.00 63.02  ?  314  VAL A N   1 
ATOM   2053  C CA  . VAL A  1  314 ? -55.619 26.532  76.178  1.00 63.19  ?  314  VAL A CA  1 
ATOM   2054  C C   . VAL A  1  314 ? -56.899 25.785  76.532  1.00 64.61  ?  314  VAL A C   1 
ATOM   2055  O O   . VAL A  1  314 ? -57.701 26.271  77.337  1.00 64.91  ?  314  VAL A O   1 
ATOM   2056  C CB  . VAL A  1  314 ? -54.592 26.437  77.319  1.00 62.10  ?  314  VAL A CB  1 
ATOM   2057  C CG1 . VAL A  1  314 ? -54.256 24.990  77.616  1.00 62.20  ?  314  VAL A CG1 1 
ATOM   2058  C CG2 . VAL A  1  314 ? -53.342 27.232  76.967  1.00 61.32  ?  314  VAL A CG2 1 
ATOM   2059  N N   . LEU A  1  315 ? -57.086 24.605  75.943  1.00 62.21  ?  315  LEU A N   1 
ATOM   2060  C CA  . LEU A  1  315 ? -58.270 23.783  76.194  1.00 64.20  ?  315  LEU A CA  1 
ATOM   2061  C C   . LEU A  1  315 ? -57.845 22.325  76.269  1.00 65.21  ?  315  LEU A C   1 
ATOM   2062  O O   . LEU A  1  315 ? -57.509 21.722  75.245  1.00 65.67  ?  315  LEU A O   1 
ATOM   2063  C CB  . LEU A  1  315 ? -59.325 23.971  75.106  1.00 65.24  ?  315  LEU A CB  1 
ATOM   2064  C CG  . LEU A  1  315 ? -60.694 23.354  75.382  1.00 67.30  ?  315  LEU A CG  1 
ATOM   2065  C CD1 . LEU A  1  315 ? -61.334 24.050  76.551  1.00 67.26  ?  315  LEU A CD1 1 
ATOM   2066  C CD2 . LEU A  1  315 ? -61.579 23.456  74.157  1.00 67.81  ?  315  LEU A CD2 1 
ATOM   2067  N N   . HIS A  1  316 ? -57.858 21.759  77.472  1.00 64.06  ?  316  HIS A N   1 
ATOM   2068  C CA  . HIS A  1  316 ? -57.505 20.361  77.689  1.00 65.32  ?  316  HIS A CA  1 
ATOM   2069  C C   . HIS A  1  316 ? -58.753 19.609  78.132  1.00 68.63  ?  316  HIS A C   1 
ATOM   2070  O O   . HIS A  1  316 ? -59.229 19.791  79.258  1.00 69.08  ?  316  HIS A O   1 
ATOM   2071  C CB  . HIS A  1  316 ? -56.392 20.229  78.726  1.00 63.02  ?  316  HIS A CB  1 
ATOM   2072  C CG  . HIS A  1  316 ? -55.100 20.862  78.314  1.00 60.08  ?  316  HIS A CG  1 
ATOM   2073  N ND1 . HIS A  1  316 ? -54.013 20.944  79.156  1.00 57.59  ?  316  HIS A ND1 1 
ATOM   2074  C CD2 . HIS A  1  316 ? -54.721 21.444  77.152  1.00 59.62  ?  316  HIS A CD2 1 
ATOM   2075  C CE1 . HIS A  1  316 ? -53.020 21.551  78.532  1.00 56.25  ?  316  HIS A CE1 1 
ATOM   2076  N NE2 . HIS A  1  316 ? -53.423 21.862  77.313  1.00 57.45  ?  316  HIS A NE2 1 
ATOM   2077  N N   . LEU A  1  317 ? -59.276 18.764  77.245  1.00 65.79  ?  317  LEU A N   1 
ATOM   2078  C CA  . LEU A  1  317 ? -60.413 17.904  77.546  1.00 68.68  ?  317  LEU A CA  1 
ATOM   2079  C C   . LEU A  1  317 ? -60.063 16.427  77.416  1.00 70.40  ?  317  LEU A C   1 
ATOM   2080  O O   . LEU A  1  317 ? -60.970 15.586  77.396  1.00 71.34  ?  317  LEU A O   1 
ATOM   2081  C CB  . LEU A  1  317 ? -61.599 18.242  76.632  1.00 68.78  ?  317  LEU A CB  1 
ATOM   2082  C CG  . LEU A  1  317 ? -62.344 19.569  76.813  1.00 67.56  ?  317  LEU A CG  1 
ATOM   2083  C CD1 . LEU A  1  317 ? -63.763 19.467  76.268  1.00 68.60  ?  317  LEU A CD1 1 
ATOM   2084  C CD2 . LEU A  1  317 ? -62.364 19.986  78.268  1.00 67.39  ?  317  LEU A CD2 1 
ATOM   2085  N N   . TYR A  1  318 ? -58.779 16.087  77.327  1.00 72.40  ?  318  TYR A N   1 
ATOM   2086  C CA  . TYR A  1  318 ? -58.386 14.729  76.984  1.00 71.68  ?  318  TYR A CA  1 
ATOM   2087  C C   . TYR A  1  318 ? -58.586 13.778  78.167  1.00 70.19  ?  318  TYR A C   1 
ATOM   2088  O O   . TYR A  1  318 ? -58.770 14.192  79.312  1.00 69.90  ?  318  TYR A O   1 
ATOM   2089  C CB  . TYR A  1  318 ? -56.934 14.697  76.496  1.00 69.55  ?  318  TYR A CB  1 
ATOM   2090  C CG  . TYR A  1  318 ? -55.893 15.111  77.514  1.00 66.14  ?  318  TYR A CG  1 
ATOM   2091  C CD1 . TYR A  1  318 ? -55.499 16.439  77.633  1.00 64.38  ?  318  TYR A CD1 1 
ATOM   2092  C CD2 . TYR A  1  318 ? -55.287 14.171  78.340  1.00 63.65  ?  318  TYR A CD2 1 
ATOM   2093  C CE1 . TYR A  1  318 ? -54.541 16.819  78.552  1.00 60.44  ?  318  TYR A CE1 1 
ATOM   2094  C CE2 . TYR A  1  318 ? -54.330 14.541  79.260  1.00 60.20  ?  318  TYR A CE2 1 
ATOM   2095  C CZ  . TYR A  1  318 ? -53.960 15.864  79.362  1.00 58.68  ?  318  TYR A CZ  1 
ATOM   2096  O OH  . TYR A  1  318 ? -53.006 16.228  80.283  1.00 55.37  ?  318  TYR A OH  1 
ATOM   2097  N N   . LEU A  1  319 ? -58.547 12.479  77.862  1.00 70.54  ?  319  LEU A N   1 
ATOM   2098  C CA  . LEU A  1  319 ? -58.714 11.403  78.843  1.00 69.32  ?  319  LEU A CA  1 
ATOM   2099  C C   . LEU A  1  319 ? -60.053 11.513  79.578  1.00 70.82  ?  319  LEU A C   1 
ATOM   2100  O O   . LEU A  1  319 ? -60.122 11.685  80.797  1.00 70.32  ?  319  LEU A O   1 
ATOM   2101  C CB  . LEU A  1  319 ? -57.543 11.377  79.828  1.00 66.72  ?  319  LEU A CB  1 
ATOM   2102  C CG  . LEU A  1  319 ? -56.497 10.316  79.501  1.00 64.95  ?  319  LEU A CG  1 
ATOM   2103  C CD1 . LEU A  1  319 ? -55.467 10.223  80.607  1.00 62.55  ?  319  LEU A CD1 1 
ATOM   2104  C CD2 . LEU A  1  319 ? -57.176 8.979   79.281  1.00 65.67  ?  319  LEU A CD2 1 
ATOM   2105  N N   . ASN A  1  320 ? -61.124 11.423  78.795  1.00 72.32  ?  320  ASN A N   1 
ATOM   2106  C CA  . ASN A  1  320 ? -62.495 11.469  79.287  1.00 73.55  ?  320  ASN A CA  1 
ATOM   2107  C C   . ASN A  1  320 ? -63.326 10.512  78.437  1.00 73.68  ?  320  ASN A C   1 
ATOM   2108  O O   . ASN A  1  320 ? -62.787 9.699   77.678  1.00 72.84  ?  320  ASN A O   1 
ATOM   2109  C CB  . ASN A  1  320 ? -63.032 12.902  79.250  1.00 75.19  ?  320  ASN A CB  1 
ATOM   2110  C CG  . ASN A  1  320 ? -62.831 13.648  80.550  1.00 75.44  ?  320  ASN A CG  1 
ATOM   2111  O OD1 . ASN A  1  320 ? -63.580 13.462  81.506  1.00 75.80  ?  320  ASN A OD1 1 
ATOM   2112  N ND2 . ASN A  1  320 ? -61.823 14.514  80.585  1.00 75.21  ?  320  ASN A ND2 1 
ATOM   2113  N N   . GLN A  1  321 ? -64.651 10.598  78.559  1.00 81.72  ?  321  GLN A N   1 
ATOM   2114  C CA  . GLN A  1  321 ? -65.550 9.759   77.773  1.00 81.66  ?  321  GLN A CA  1 
ATOM   2115  C C   . GLN A  1  321 ? -66.536 10.584  76.945  1.00 82.54  ?  321  GLN A C   1 
ATOM   2116  O O   . GLN A  1  321 ? -67.682 10.172  76.752  1.00 82.61  ?  321  GLN A O   1 
ATOM   2117  C CB  . GLN A  1  321 ? -66.304 8.789   78.680  1.00 81.32  ?  321  GLN A CB  1 
ATOM   2118  C CG  . GLN A  1  321 ? -65.442 8.094   79.720  1.00 80.20  ?  321  GLN A CG  1 
ATOM   2119  C CD  . GLN A  1  321 ? -66.243 7.123   80.567  1.00 79.86  ?  321  GLN A CD  1 
ATOM   2120  O OE1 . GLN A  1  321 ? -66.867 6.196   80.047  1.00 79.62  ?  321  GLN A OE1 1 
ATOM   2121  N NE2 . GLN A  1  321 ? -66.237 7.337   81.880  1.00 79.84  ?  321  GLN A NE2 1 
ATOM   2122  N N   . LEU A  1  322 ? -66.115 11.748  76.449  1.00 81.60  ?  322  LEU A N   1 
ATOM   2123  C CA  . LEU A  1  322 ? -67.001 12.559  75.621  1.00 81.86  ?  322  LEU A CA  1 
ATOM   2124  C C   . LEU A  1  322 ? -67.274 11.874  74.285  1.00 81.34  ?  322  LEU A C   1 
ATOM   2125  O O   . LEU A  1  322 ? -66.425 11.168  73.737  1.00 80.91  ?  322  LEU A O   1 
ATOM   2126  C CB  . LEU A  1  322 ? -66.441 13.970  75.395  1.00 81.90  ?  322  LEU A CB  1 
ATOM   2127  C CG  . LEU A  1  322 ? -66.076 14.782  76.647  1.00 82.31  ?  322  LEU A CG  1 
ATOM   2128  C CD1 . LEU A  1  322 ? -64.674 14.530  77.022  1.00 82.14  ?  322  LEU A CD1 1 
ATOM   2129  C CD2 . LEU A  1  322 ? -66.280 16.265  76.515  1.00 81.82  ?  322  LEU A CD2 1 
ATOM   2130  N N   . ASN A  1  323 ? -68.491 12.072  73.776  1.00 86.70  ?  323  ASN A N   1 
ATOM   2131  C CA  . ASN A  1  323 ? -68.922 11.445  72.531  1.00 86.20  ?  323  ASN A CA  1 
ATOM   2132  C C   . ASN A  1  323 ? -69.488 12.479  71.564  1.00 85.87  ?  323  ASN A C   1 
ATOM   2133  O O   . ASN A  1  323 ? -69.365 13.688  71.793  1.00 85.84  ?  323  ASN A O   1 
ATOM   2134  C CB  . ASN A  1  323 ? -69.938 10.316  72.801  1.00 86.09  ?  323  ASN A CB  1 
ATOM   2135  C CG  . ASN A  1  323 ? -71.304 10.815  73.314  1.00 86.35  ?  323  ASN A CG  1 
ATOM   2136  O OD1 . ASN A  1  323 ? -71.870 11.793  72.821  1.00 86.36  ?  323  ASN A OD1 1 
ATOM   2137  N ND2 . ASN A  1  323 ? -71.842 10.109  74.305  1.00 86.39  ?  323  ASN A ND2 1 
ATOM   2138  N N   . GLY A  1  324 ? -70.076 12.012  70.466  1.00 87.81  ?  324  GLY A N   1 
ATOM   2139  C CA  . GLY A  1  324 ? -70.673 12.901  69.496  1.00 87.27  ?  324  GLY A CA  1 
ATOM   2140  C C   . GLY A  1  324 ? -69.644 13.489  68.552  1.00 86.83  ?  324  GLY A C   1 
ATOM   2141  O O   . GLY A  1  324 ? -68.494 13.046  68.472  1.00 86.98  ?  324  GLY A O   1 
ATOM   2142  N N   . SER A  1  325 ? -70.075 14.511  67.823  1.00 89.90  ?  325  SER A N   1 
ATOM   2143  C CA  . SER A  1  325 ? -69.235 15.135  66.813  1.00 89.24  ?  325  SER A CA  1 
ATOM   2144  C C   . SER A  1  325 ? -68.659 16.452  67.321  1.00 88.86  ?  325  SER A C   1 
ATOM   2145  O O   . SER A  1  325 ? -69.164 17.061  68.267  1.00 88.96  ?  325  SER A O   1 
ATOM   2146  C CB  . SER A  1  325 ? -70.021 15.364  65.519  1.00 89.25  ?  325  SER A CB  1 
ATOM   2147  O OG  . SER A  1  325 ? -70.839 14.247  65.212  1.00 92.56  ?  325  SER A OG  1 
ATOM   2148  N N   . ILE A  1  326 ? -67.570 16.875  66.688  1.00 87.30  ?  326  ILE A N   1 
ATOM   2149  C CA  . ILE A  1  326 ? -66.921 18.134  67.037  1.00 86.59  ?  326  ILE A CA  1 
ATOM   2150  C C   . ILE A  1  326 ? -67.836 19.277  66.617  1.00 85.63  ?  326  ILE A C   1 
ATOM   2151  O O   . ILE A  1  326 ? -68.228 19.356  65.444  1.00 85.10  ?  326  ILE A O   1 
ATOM   2152  C CB  . ILE A  1  326 ? -65.543 18.256  66.372  1.00 86.07  ?  326  ILE A CB  1 
ATOM   2153  C CG1 . ILE A  1  326 ? -64.672 17.052  66.731  1.00 87.04  ?  326  ILE A CG1 1 
ATOM   2154  C CG2 . ILE A  1  326 ? -64.871 19.560  66.783  1.00 85.05  ?  326  ILE A CG2 1 
ATOM   2155  C CD1 . ILE A  1  326 ? -63.458 16.906  65.846  1.00 86.65  ?  326  ILE A CD1 1 
ATOM   2156  N N   . PRO A  1  327 ? -68.222 20.161  67.531  1.00 88.50  ?  327  PRO A N   1 
ATOM   2157  C CA  . PRO A  1  327 ? -69.069 21.298  67.155  1.00 87.85  ?  327  PRO A CA  1 
ATOM   2158  C C   . PRO A  1  327 ? -68.334 22.234  66.214  1.00 87.36  ?  327  PRO A C   1 
ATOM   2159  O O   . PRO A  1  327 ? -67.196 22.642  66.493  1.00 85.90  ?  327  PRO A O   1 
ATOM   2160  C CB  . PRO A  1  327 ? -69.372 21.980  68.499  1.00 87.65  ?  327  PRO A CB  1 
ATOM   2161  C CG  . PRO A  1  327 ? -69.099 20.937  69.534  1.00 88.92  ?  327  PRO A CG  1 
ATOM   2162  C CD  . PRO A  1  327 ? -67.980 20.106  68.981  1.00 89.18  ?  327  PRO A CD  1 
ATOM   2163  N N   . PRO A  1  328 ? -68.947 22.589  65.082  1.00 86.31  ?  328  PRO A N   1 
ATOM   2164  C CA  . PRO A  1  328 ? -68.316 23.562  64.176  1.00 87.02  ?  328  PRO A CA  1 
ATOM   2165  C C   . PRO A  1  328 ? -68.018 24.899  64.833  1.00 86.04  ?  328  PRO A C   1 
ATOM   2166  O O   . PRO A  1  328 ? -67.163 25.642  64.335  1.00 85.55  ?  328  PRO A O   1 
ATOM   2167  C CB  . PRO A  1  328 ? -69.346 23.710  63.048  1.00 92.21  ?  328  PRO A CB  1 
ATOM   2168  C CG  . PRO A  1  328 ? -70.145 22.449  63.100  1.00 93.49  ?  328  PRO A CG  1 
ATOM   2169  C CD  . PRO A  1  328 ? -70.218 22.074  64.546  1.00 90.59  ?  328  PRO A CD  1 
ATOM   2170  N N   . GLU A  1  329 ? -68.696 25.227  65.933  1.00 89.55  ?  329  GLU A N   1 
ATOM   2171  C CA  . GLU A  1  329 ? -68.463 26.490  66.621  1.00 88.81  ?  329  GLU A CA  1 
ATOM   2172  C C   . GLU A  1  329 ? -67.099 26.545  67.299  1.00 84.70  ?  329  GLU A C   1 
ATOM   2173  O O   . GLU A  1  329 ? -66.648 27.635  67.667  1.00 84.09  ?  329  GLU A O   1 
ATOM   2174  C CB  . GLU A  1  329 ? -69.574 26.723  67.647  1.00 89.95  ?  329  GLU A CB  1 
ATOM   2175  C CG  . GLU A  1  329 ? -70.973 26.812  67.038  1.00 94.99  ?  329  GLU A CG  1 
ATOM   2176  C CD  . GLU A  1  329 ? -71.640 25.453  66.864  1.00 96.00  ?  329  GLU A CD  1 
ATOM   2177  O OE1 . GLU A  1  329 ? -70.921 24.450  66.661  1.00 93.56  ?  329  GLU A OE1 1 
ATOM   2178  O OE2 . GLU A  1  329 ? -72.887 25.391  66.921  1.00 99.50  -1 329  GLU A OE2 1 
ATOM   2179  N N   . LEU A  1  330 ? -66.429 25.401  67.469  1.00 84.92  ?  330  LEU A N   1 
ATOM   2180  C CA  . LEU A  1  330 ? -65.087 25.412  68.040  1.00 83.56  ?  330  LEU A CA  1 
ATOM   2181  C C   . LEU A  1  330 ? -64.099 26.166  67.160  1.00 82.44  ?  330  LEU A C   1 
ATOM   2182  O O   . LEU A  1  330 ? -63.048 26.592  67.648  1.00 81.74  ?  330  LEU A O   1 
ATOM   2183  C CB  . LEU A  1  330 ? -64.595 23.983  68.278  1.00 84.69  ?  330  LEU A CB  1 
ATOM   2184  C CG  . LEU A  1  330 ? -65.450 23.127  69.217  1.00 86.06  ?  330  LEU A CG  1 
ATOM   2185  C CD1 . LEU A  1  330 ? -64.684 21.896  69.670  1.00 87.12  ?  330  LEU A CD1 1 
ATOM   2186  C CD2 . LEU A  1  330 ? -65.935 23.932  70.414  1.00 85.87  ?  330  LEU A CD2 1 
ATOM   2187  N N   . GLY A  1  331 ? -64.410 26.335  65.875  1.00 86.97  ?  331  GLY A N   1 
ATOM   2188  C CA  . GLY A  1  331 ? -63.592 27.148  64.995  1.00 86.89  ?  331  GLY A CA  1 
ATOM   2189  C C   . GLY A  1  331 ? -63.636 28.634  65.287  1.00 87.50  ?  331  GLY A C   1 
ATOM   2190  O O   . GLY A  1  331 ? -62.871 29.388  64.676  1.00 88.03  ?  331  GLY A O   1 
ATOM   2191  N N   . GLU A  1  332 ? -64.505 29.072  66.197  1.00 86.77  ?  332  GLU A N   1 
ATOM   2192  C CA  . GLU A  1  332 ? -64.625 30.479  66.552  1.00 88.32  ?  332  GLU A CA  1 
ATOM   2193  C C   . GLU A  1  332 ? -63.877 30.829  67.830  1.00 85.15  ?  332  GLU A C   1 
ATOM   2194  O O   . GLU A  1  332 ? -64.027 31.944  68.338  1.00 86.10  ?  332  GLU A O   1 
ATOM   2195  C CB  . GLU A  1  332 ? -66.098 30.854  66.695  1.00 91.77  ?  332  GLU A CB  1 
ATOM   2196  C CG  . GLU A  1  332 ? -66.990 30.150  65.700  1.00 94.73  ?  332  GLU A CG  1 
ATOM   2197  C CD  . GLU A  1  332 ? -66.954 30.814  64.342  1.00 98.47  ?  332  GLU A CD  1 
ATOM   2198  O OE1 . GLU A  1  332 ? -66.566 32.000  64.280  1.00 99.65  ?  332  GLU A OE1 1 
ATOM   2199  O OE2 . GLU A  1  332 ? -67.308 30.157  63.338  1.00 100.47 -1 332  GLU A OE2 1 
ATOM   2200  N N   . MET A  1  333 ? -63.089 29.900  68.368  1.00 84.04  ?  333  MET A N   1 
ATOM   2201  C CA  . MET A  1  333 ? -62.277 30.159  69.556  1.00 82.46  ?  333  MET A CA  1 
ATOM   2202  C C   . MET A  1  333 ? -60.985 30.824  69.083  1.00 81.71  ?  333  MET A C   1 
ATOM   2203  O O   . MET A  1  333 ? -59.935 30.197  68.923  1.00 81.61  ?  333  MET A O   1 
ATOM   2204  C CB  . MET A  1  333 ? -62.066 28.862  70.330  1.00 83.33  ?  333  MET A CB  1 
ATOM   2205  C CG  . MET A  1  333 ? -63.371 28.048  70.346  1.00 84.60  ?  333  MET A CG  1 
ATOM   2206  S SD  . MET A  1  333 ? -63.480 26.436  71.162  1.00 86.15  ?  333  MET A SD  1 
ATOM   2207  C CE  . MET A  1  333 ? -62.069 26.457  72.213  1.00 85.38  ?  333  MET A CE  1 
ATOM   2208  N N   . GLU A  1  334 ? -61.092 32.138  68.848  1.00 80.91  ?  334  GLU A N   1 
ATOM   2209  C CA  . GLU A  1  334 ? -60.080 32.880  68.098  1.00 81.10  ?  334  GLU A CA  1 
ATOM   2210  C C   . GLU A  1  334 ? -58.712 32.855  68.768  1.00 79.35  ?  334  GLU A C   1 
ATOM   2211  O O   . GLU A  1  334 ? -57.687 32.915  68.082  1.00 79.24  ?  334  GLU A O   1 
ATOM   2212  C CB  . GLU A  1  334 ? -60.535 34.328  67.913  1.00 84.42  ?  334  GLU A CB  1 
ATOM   2213  C CG  . GLU A  1  334 ? -61.745 34.494  67.009  1.00 88.38  ?  334  GLU A CG  1 
ATOM   2214  C CD  . GLU A  1  334 ? -62.603 35.685  67.403  1.00 91.55  ?  334  GLU A CD  1 
ATOM   2215  O OE1 . GLU A  1  334 ? -62.914 35.823  68.605  1.00 90.09  ?  334  GLU A OE1 1 
ATOM   2216  O OE2 . GLU A  1  334 ? -62.974 36.478  66.512  1.00 95.70  -1 334  GLU A OE2 1 
ATOM   2217  N N   . SER A  1  335 ? -58.666 32.793  70.093  1.00 74.95  ?  335  SER A N   1 
ATOM   2218  C CA  . SER A  1  335 ? -57.397 32.836  70.807  1.00 74.45  ?  335  SER A CA  1 
ATOM   2219  C C   . SER A  1  335 ? -56.759 31.463  70.975  1.00 74.87  ?  335  SER A C   1 
ATOM   2220  O O   . SER A  1  335 ? -55.676 31.372  71.563  1.00 74.54  ?  335  SER A O   1 
ATOM   2221  C CB  . SER A  1  335 ? -57.590 33.484  72.184  1.00 73.95  ?  335  SER A CB  1 
ATOM   2222  O OG  . SER A  1  335 ? -57.940 34.852  72.064  1.00 74.07  ?  335  SER A OG  1 
ATOM   2223  N N   . MET A  1  336 ? -57.390 30.408  70.462  1.00 69.81  ?  336  MET A N   1 
ATOM   2224  C CA  . MET A  1  336 ? -56.962 29.048  70.762  1.00 70.29  ?  336  MET A CA  1 
ATOM   2225  C C   . MET A  1  336 ? -55.534 28.797  70.291  1.00 70.13  ?  336  MET A C   1 
ATOM   2226  O O   . MET A  1  336 ? -55.182 29.083  69.144  1.00 70.34  ?  336  MET A O   1 
ATOM   2227  C CB  . MET A  1  336 ? -57.923 28.048  70.120  1.00 71.36  ?  336  MET A CB  1 
ATOM   2228  C CG  . MET A  1  336 ? -57.634 26.598  70.458  1.00 72.09  ?  336  MET A CG  1 
ATOM   2229  S SD  . MET A  1  336 ? -57.231 26.431  72.196  1.00 71.62  ?  336  MET A SD  1 
ATOM   2230  C CE  . MET A  1  336 ? -58.832 26.617  72.937  1.00 72.33  ?  336  MET A CE  1 
ATOM   2231  N N   . ILE A  1  337 ? -54.710 28.269  71.199  1.00 68.26  ?  337  ILE A N   1 
ATOM   2232  C CA  . ILE A  1  337 ? -53.318 27.932  70.926  1.00 68.24  ?  337  ILE A CA  1 
ATOM   2233  C C   . ILE A  1  337 ? -53.063 26.442  71.122  1.00 68.59  ?  337  ILE A C   1 
ATOM   2234  O O   . ILE A  1  337 ? -52.435 25.791  70.280  1.00 69.13  ?  337  ILE A O   1 
ATOM   2235  C CB  . ILE A  1  337 ? -52.355 28.770  71.798  1.00 67.57  ?  337  ILE A CB  1 
ATOM   2236  C CG1 . ILE A  1  337 ? -52.321 30.218  71.315  1.00 67.47  ?  337  ILE A CG1 1 
ATOM   2237  C CG2 . ILE A  1  337 ? -50.955 28.183  71.780  1.00 67.82  ?  337  ILE A CG2 1 
ATOM   2238  C CD1 . ILE A  1  337 ? -51.590 31.146  72.253  1.00 66.97  ?  337  ILE A CD1 1 
ATOM   2239  N N   . ASP A  1  338 ? -53.548 25.884  72.232  1.00 65.30  ?  338  ASP A N   1 
ATOM   2240  C CA  . ASP A  1  338 ? -53.363 24.478  72.584  1.00 65.60  ?  338  ASP A CA  1 
ATOM   2241  C C   . ASP A  1  338 ? -54.737 23.831  72.721  1.00 66.77  ?  338  ASP A C   1 
ATOM   2242  O O   . ASP A  1  338 ? -55.457 24.092  73.692  1.00 66.79  ?  338  ASP A O   1 
ATOM   2243  C CB  . ASP A  1  338 ? -52.558 24.354  73.878  1.00 64.55  ?  338  ASP A CB  1 
ATOM   2244  C CG  . ASP A  1  338 ? -52.278 22.918  74.257  1.00 64.58  ?  338  ASP A CG  1 
ATOM   2245  O OD1 . ASP A  1  338 ? -52.401 22.039  73.381  1.00 65.58  ?  338  ASP A OD1 1 
ATOM   2246  O OD2 . ASP A  1  338 ? -51.927 22.668  75.429  1.00 63.64  -1 338  ASP A OD2 1 
ATOM   2247  N N   . LEU A  1  339 ? -55.089 22.973  71.764  1.00 64.76  ?  339  LEU A N   1 
ATOM   2248  C CA  . LEU A  1  339 ? -56.398 22.325  71.707  1.00 66.43  ?  339  LEU A CA  1 
ATOM   2249  C C   . LEU A  1  339 ? -56.190 20.820  71.805  1.00 67.77  ?  339  LEU A C   1 
ATOM   2250  O O   . LEU A  1  339 ? -55.625 20.211  70.891  1.00 68.12  ?  339  LEU A O   1 
ATOM   2251  C CB  . LEU A  1  339 ? -57.127 22.697  70.415  1.00 66.93  ?  339  LEU A CB  1 
ATOM   2252  C CG  . LEU A  1  339 ? -58.531 22.139  70.194  1.00 68.52  ?  339  LEU A CG  1 
ATOM   2253  C CD1 . LEU A  1  339 ? -59.400 22.418  71.396  1.00 68.85  ?  339  LEU A CD1 1 
ATOM   2254  C CD2 . LEU A  1  339 ? -59.144 22.746  68.947  1.00 68.34  ?  339  LEU A CD2 1 
ATOM   2255  N N   . GLU A  1  340 ? -56.643 20.214  72.906  1.00 65.98  ?  340  GLU A N   1 
ATOM   2256  C CA  . GLU A  1  340 ? -56.396 18.797  73.169  1.00 67.61  ?  340  GLU A CA  1 
ATOM   2257  C C   . GLU A  1  340 ? -57.709 18.099  73.502  1.00 70.30  ?  340  GLU A C   1 
ATOM   2258  O O   . GLU A  1  340 ? -58.338 18.406  74.519  1.00 70.62  ?  340  GLU A O   1 
ATOM   2259  C CB  . GLU A  1  340 ? -55.389 18.622  74.306  1.00 66.13  ?  340  GLU A CB  1 
ATOM   2260  C CG  . GLU A  1  340 ? -54.243 19.615  74.269  1.00 63.02  ?  340  GLU A CG  1 
ATOM   2261  C CD  . GLU A  1  340 ? -53.025 19.140  75.033  1.00 61.10  ?  340  GLU A CD  1 
ATOM   2262  O OE1 . GLU A  1  340 ? -53.135 18.917  76.253  1.00 60.51  ?  340  GLU A OE1 1 
ATOM   2263  O OE2 . GLU A  1  340 ? -51.950 19.002  74.419  1.00 60.11  -1 340  GLU A OE2 1 
ATOM   2264  N N   . ILE A  1  341 ? -58.130 17.176  72.633  1.00 72.54  ?  341  ILE A N   1 
ATOM   2265  C CA  . ILE A  1  341 ? -59.312 16.345  72.856  1.00 74.54  ?  341  ILE A CA  1 
ATOM   2266  C C   . ILE A  1  341 ? -58.960 14.862  72.695  1.00 75.59  ?  341  ILE A C   1 
ATOM   2267  O O   . ILE A  1  341 ? -59.800 14.047  72.294  1.00 76.01  ?  341  ILE A O   1 
ATOM   2268  C CB  . ILE A  1  341 ? -60.461 16.781  71.927  1.00 74.29  ?  341  ILE A CB  1 
ATOM   2269  C CG1 . ILE A  1  341 ? -60.658 18.290  72.035  1.00 72.67  ?  341  ILE A CG1 1 
ATOM   2270  C CG2 . ILE A  1  341 ? -61.773 16.158  72.352  1.00 75.55  ?  341  ILE A CG2 1 
ATOM   2271  C CD1 . ILE A  1  341 ? -60.819 18.981  70.717  1.00 71.59  ?  341  ILE A CD1 1 
ATOM   2272  N N   . SER A  1  342 ? -57.711 14.497  72.979  1.00 74.08  ?  342  SER A N   1 
ATOM   2273  C CA  . SER A  1  342 ? -57.265 13.126  72.766  1.00 73.43  ?  342  SER A CA  1 
ATOM   2274  C C   . SER A  1  342 ? -57.970 12.151  73.707  1.00 72.99  ?  342  SER A C   1 
ATOM   2275  O O   . SER A  1  342 ? -58.585 12.536  74.703  1.00 73.40  ?  342  SER A O   1 
ATOM   2276  C CB  . SER A  1  342 ? -55.759 13.004  72.985  1.00 71.84  ?  342  SER A CB  1 
ATOM   2277  O OG  . SER A  1  342 ? -55.084 14.179  72.595  1.00 72.00  ?  342  SER A OG  1 
ATOM   2278  N N   . GLU A  1  343 ? -57.859 10.865  73.374  1.00 76.96  ?  343  GLU A N   1 
ATOM   2279  C CA  . GLU A  1  343 ? -58.279 9.759   74.240  1.00 76.23  ?  343  GLU A CA  1 
ATOM   2280  C C   . GLU A  1  343 ? -59.726 9.930   74.702  1.00 77.39  ?  343  GLU A C   1 
ATOM   2281  O O   . GLU A  1  343 ? -60.023 10.070  75.890  1.00 77.27  ?  343  GLU A O   1 
ATOM   2282  C CB  . GLU A  1  343 ? -57.331 9.605   75.431  1.00 74.45  ?  343  GLU A CB  1 
ATOM   2283  C CG  . GLU A  1  343 ? -55.891 9.974   75.129  1.00 73.00  ?  343  GLU A CG  1 
ATOM   2284  C CD  . GLU A  1  343 ? -54.919 9.341   76.097  1.00 70.77  ?  343  GLU A CD  1 
ATOM   2285  O OE1 . GLU A  1  343 ? -55.140 8.170   76.469  1.00 70.63  ?  343  GLU A OE1 1 
ATOM   2286  O OE2 . GLU A  1  343 ? -53.936 10.009  76.484  1.00 69.07  -1 343  GLU A OE2 1 
ATOM   2287  N N   . ASN A  1  344 ? -60.628 9.935   73.727  1.00 76.70  ?  344  ASN A N   1 
ATOM   2288  C CA  . ASN A  1  344 ? -62.047 10.123  73.989  1.00 77.56  ?  344  ASN A CA  1 
ATOM   2289  C C   . ASN A  1  344 ? -62.831 9.191   73.077  1.00 77.49  ?  344  ASN A C   1 
ATOM   2290  O O   . ASN A  1  344 ? -62.274 8.276   72.464  1.00 76.84  ?  344  ASN A O   1 
ATOM   2291  C CB  . ASN A  1  344 ? -62.443 11.590  73.803  1.00 78.50  ?  344  ASN A CB  1 
ATOM   2292  C CG  . ASN A  1  344 ? -62.443 12.339  75.101  1.00 78.89  ?  344  ASN A CG  1 
ATOM   2293  O OD1 . ASN A  1  344 ? -63.310 12.120  75.942  1.00 79.19  ?  344  ASN A OD1 1 
ATOM   2294  N ND2 . ASN A  1  344 ? -61.469 13.225  75.285  1.00 78.87  ?  344  ASN A ND2 1 
ATOM   2295  N N   . LYS A  1  345 ? -64.139 9.405   73.010  1.00 78.05  ?  345  LYS A N   1 
ATOM   2296  C CA  . LYS A  1  345 ? -65.013 8.622   72.147  1.00 77.89  ?  345  LYS A CA  1 
ATOM   2297  C C   . LYS A  1  345 ? -65.771 9.524   71.181  1.00 78.26  ?  345  LYS A C   1 
ATOM   2298  O O   . LYS A  1  345 ? -66.958 9.323   70.915  1.00 79.26  ?  345  LYS A O   1 
ATOM   2299  C CB  . LYS A  1  345 ? -65.977 7.777   72.975  1.00 78.05  ?  345  LYS A CB  1 
ATOM   2300  C CG  . LYS A  1  345 ? -65.284 6.741   73.841  1.00 77.18  ?  345  LYS A CG  1 
ATOM   2301  C CD  . LYS A  1  345 ? -66.284 5.869   74.577  1.00 77.91  ?  345  LYS A CD  1 
ATOM   2302  C CE  . LYS A  1  345 ? -65.581 4.859   75.466  1.00 77.02  ?  345  LYS A CE  1 
ATOM   2303  N NZ  . LYS A  1  345 ? -64.704 5.531   76.470  1.00 75.68  ?  345  LYS A NZ  1 
ATOM   2304  N N   . LEU A  1  346 ? -65.087 10.528  70.636  1.00 82.72  ?  346  LEU A N   1 
ATOM   2305  C CA  . LEU A  1  346 ? -65.711 11.422  69.674  1.00 82.62  ?  346  LEU A CA  1 
ATOM   2306  C C   . LEU A  1  346 ? -65.864 10.725  68.324  1.00 82.19  ?  346  LEU A C   1 
ATOM   2307  O O   . LEU A  1  346 ? -65.181 9.743   68.020  1.00 82.01  ?  346  LEU A O   1 
ATOM   2308  C CB  . LEU A  1  346 ? -64.893 12.704  69.511  1.00 82.50  ?  346  LEU A CB  1 
ATOM   2309  C CG  . LEU A  1  346 ? -64.644 13.627  70.707  1.00 82.69  ?  346  LEU A CG  1 
ATOM   2310  C CD1 . LEU A  1  346 ? -64.475 15.053  70.223  1.00 82.16  ?  346  LEU A CD1 1 
ATOM   2311  C CD2 . LEU A  1  346 ? -65.773 13.551  71.717  1.00 83.27  ?  346  LEU A CD2 1 
ATOM   2312  N N   . THR A  1  347 ? -66.782 11.244  67.509  1.00 88.55  ?  347  THR A N   1 
ATOM   2313  C CA  . THR A  1  347 ? -67.091 10.655  66.213  1.00 88.12  ?  347  THR A CA  1 
ATOM   2314  C C   . THR A  1  347 ? -67.274 11.760  65.180  1.00 87.59  ?  347  THR A C   1 
ATOM   2315  O O   . THR A  1  347 ? -67.340 12.948  65.508  1.00 87.43  ?  347  THR A O   1 
ATOM   2316  C CB  . THR A  1  347 ? -68.351 9.774   66.265  1.00 88.07  ?  347  THR A CB  1 
ATOM   2317  O OG1 . THR A  1  347 ? -69.437 10.510  66.846  1.00 88.17  ?  347  THR A OG1 1 
ATOM   2318  C CG2 . THR A  1  347 ? -68.094 8.505   67.075  1.00 88.25  ?  347  THR A CG2 1 
ATOM   2319  N N   . GLY A  1  348 ? -67.342 11.353  63.913  1.00 90.34  ?  348  GLY A N   1 
ATOM   2320  C CA  . GLY A  1  348 ? -67.660 12.263  62.838  1.00 89.78  ?  348  GLY A CA  1 
ATOM   2321  C C   . GLY A  1  348 ? -66.455 12.983  62.267  1.00 89.35  ?  348  GLY A C   1 
ATOM   2322  O O   . GLY A  1  348 ? -65.305 12.711  62.628  1.00 89.65  ?  348  GLY A O   1 
ATOM   2323  N N   . PRO A  1  349 ? -66.702 13.911  61.348  1.00 87.33  ?  349  PRO A N   1 
ATOM   2324  C CA  . PRO A  1  349 ? -65.605 14.645  60.715  1.00 85.40  ?  349  PRO A CA  1 
ATOM   2325  C C   . PRO A  1  349 ? -65.163 15.851  61.534  1.00 82.71  ?  349  PRO A C   1 
ATOM   2326  O O   . PRO A  1  349 ? -65.871 16.345  62.416  1.00 82.96  ?  349  PRO A O   1 
ATOM   2327  C CB  . PRO A  1  349 ? -66.212 15.083  59.379  1.00 89.51  ?  349  PRO A CB  1 
ATOM   2328  C CG  . PRO A  1  349 ? -67.652 15.284  59.701  1.00 92.92  ?  349  PRO A CG  1 
ATOM   2329  C CD  . PRO A  1  349 ? -68.007 14.257  60.755  1.00 92.03  ?  349  PRO A CD  1 
ATOM   2330  N N   . VAL A  1  350 ? -63.958 16.311  61.226  1.00 84.31  ?  350  VAL A N   1 
ATOM   2331  C CA  . VAL A  1  350 ? -63.458 17.569  61.784  1.00 82.33  ?  350  VAL A CA  1 
ATOM   2332  C C   . VAL A  1  350 ? -64.052 18.724  60.982  1.00 85.54  ?  350  VAL A C   1 
ATOM   2333  O O   . VAL A  1  350 ? -64.037 18.674  59.743  1.00 87.86  ?  350  VAL A O   1 
ATOM   2334  C CB  . VAL A  1  350 ? -61.932 17.602  61.752  1.00 78.95  ?  350  VAL A CB  1 
ATOM   2335  C CG1 . VAL A  1  350 ? -61.415 18.939  62.258  1.00 77.42  ?  350  VAL A CG1 1 
ATOM   2336  C CG2 . VAL A  1  350 ? -61.362 16.469  62.589  1.00 77.16  ?  350  VAL A CG2 1 
ATOM   2337  N N   . PRO A  1  351 ? -64.611 19.743  61.629  1.00 84.84  ?  351  PRO A N   1 
ATOM   2338  C CA  . PRO A  1  351 ? -65.207 20.851  60.875  1.00 88.34  ?  351  PRO A CA  1 
ATOM   2339  C C   . PRO A  1  351 ? -64.160 21.645  60.111  1.00 87.83  ?  351  PRO A C   1 
ATOM   2340  O O   . PRO A  1  351 ? -63.032 21.836  60.571  1.00 84.44  ?  351  PRO A O   1 
ATOM   2341  C CB  . PRO A  1  351 ? -65.862 21.712  61.963  1.00 88.35  ?  351  PRO A CB  1 
ATOM   2342  C CG  . PRO A  1  351 ? -65.988 20.810  63.151  1.00 85.87  ?  351  PRO A CG  1 
ATOM   2343  C CD  . PRO A  1  351 ? -64.812 19.893  63.079  1.00 82.71  ?  351  PRO A CD  1 
ATOM   2344  N N   . ASP A  1  352 ? -64.559 22.123  58.928  1.00 93.17  ?  352  ASP A N   1 
ATOM   2345  C CA  . ASP A  1  352 ? -63.708 23.021  58.153  1.00 93.55  ?  352  ASP A CA  1 
ATOM   2346  C C   . ASP A  1  352 ? -63.451 24.333  58.878  1.00 92.70  ?  352  ASP A C   1 
ATOM   2347  O O   . ASP A  1  352 ? -62.500 25.044  58.532  1.00 92.11  ?  352  ASP A O   1 
ATOM   2348  C CB  . ASP A  1  352 ? -64.333 23.312  56.787  1.00 98.38  ?  352  ASP A CB  1 
ATOM   2349  C CG  . ASP A  1  352 ? -64.870 22.069  56.115  1.00 100.10 ?  352  ASP A CG  1 
ATOM   2350  O OD1 . ASP A  1  352 ? -66.020 21.682  56.414  1.00 102.12 ?  352  ASP A OD1 1 
ATOM   2351  O OD2 . ASP A  1  352 ? -64.141 21.479  55.288  1.00 99.63  -1 352  ASP A OD2 1 
ATOM   2352  N N   . SER A  1  353 ? -64.279 24.669  59.872  1.00 90.37  ?  353  SER A N   1 
ATOM   2353  C CA  . SER A  1  353 ? -64.112 25.896  60.639  1.00 89.72  ?  353  SER A CA  1 
ATOM   2354  C C   . SER A  1  353 ? -62.783 25.950  61.379  1.00 85.33  ?  353  SER A C   1 
ATOM   2355  O O   . SER A  1  353 ? -62.392 27.030  61.832  1.00 84.94  ?  353  SER A O   1 
ATOM   2356  C CB  . SER A  1  353 ? -65.271 26.055  61.627  1.00 90.54  ?  353  SER A CB  1 
ATOM   2357  O OG  . SER A  1  353 ? -65.306 24.987  62.557  1.00 87.57  ?  353  SER A OG  1 
ATOM   2358  N N   . PHE A  1  354 ? -62.081 24.820  61.508  1.00 83.87  ?  354  PHE A N   1 
ATOM   2359  C CA  . PHE A  1  354 ? -60.766 24.828  62.138  1.00 81.25  ?  354  PHE A CA  1 
ATOM   2360  C C   . PHE A  1  354 ? -59.768 25.678  61.361  1.00 81.09  ?  354  PHE A C   1 
ATOM   2361  O O   . PHE A  1  354 ? -58.719 26.037  61.906  1.00 80.28  ?  354  PHE A O   1 
ATOM   2362  C CB  . PHE A  1  354 ? -60.238 23.398  62.279  1.00 82.21  ?  354  PHE A CB  1 
ATOM   2363  C CG  . PHE A  1  354 ? -60.742 22.680  63.499  1.00 82.93  ?  354  PHE A CG  1 
ATOM   2364  C CD1 . PHE A  1  354 ? -62.093 22.674  63.810  1.00 83.26  ?  354  PHE A CD1 1 
ATOM   2365  C CD2 . PHE A  1  354 ? -59.865 22.007  64.334  1.00 83.33  ?  354  PHE A CD2 1 
ATOM   2366  C CE1 . PHE A  1  354 ? -62.559 22.012  64.931  1.00 84.12  ?  354  PHE A CE1 1 
ATOM   2367  C CE2 . PHE A  1  354 ? -60.324 21.343  65.455  1.00 84.15  ?  354  PHE A CE2 1 
ATOM   2368  C CZ  . PHE A  1  354 ? -61.672 21.346  65.755  1.00 84.63  ?  354  PHE A CZ  1 
ATOM   2369  N N   . GLY A  1  355 ? -60.069 26.005  60.102  1.00 85.18  ?  355  GLY A N   1 
ATOM   2370  C CA  . GLY A  1  355 ? -59.238 26.929  59.352  1.00 85.96  ?  355  GLY A CA  1 
ATOM   2371  C C   . GLY A  1  355 ? -59.258 28.346  59.885  1.00 86.89  ?  355  GLY A C   1 
ATOM   2372  O O   . GLY A  1  355 ? -58.381 29.141  59.533  1.00 87.39  ?  355  GLY A O   1 
ATOM   2373  N N   . LYS A  1  356 ? -60.247 28.682  60.719  1.00 85.52  ?  356  LYS A N   1 
ATOM   2374  C CA  . LYS A  1  356 ? -60.319 29.999  61.341  1.00 86.51  ?  356  LYS A CA  1 
ATOM   2375  C C   . LYS A  1  356 ? -59.414 30.130  62.560  1.00 82.75  ?  356  LYS A C   1 
ATOM   2376  O O   . LYS A  1  356 ? -59.198 31.251  63.032  1.00 83.38  ?  356  LYS A O   1 
ATOM   2377  C CB  . LYS A  1  356 ? -61.758 30.317  61.744  1.00 88.90  ?  356  LYS A CB  1 
ATOM   2378  C CG  . LYS A  1  356 ? -62.614 30.878  60.630  1.00 93.97  ?  356  LYS A CG  1 
ATOM   2379  C CD  . LYS A  1  356 ? -64.078 30.894  61.031  1.00 96.21  ?  356  LYS A CD  1 
ATOM   2380  C CE  . LYS A  1  356 ? -64.810 29.662  60.522  1.00 96.94  ?  356  LYS A CE  1 
ATOM   2381  N NZ  . LYS A  1  356 ? -66.100 29.441  61.239  1.00 98.03  ?  356  LYS A NZ  1 
ATOM   2382  N N   . LEU A  1  357 ? -58.909 29.020  63.097  1.00 81.40  ?  357  LEU A N   1 
ATOM   2383  C CA  . LEU A  1  357 ? -57.989 29.040  64.235  1.00 79.68  ?  357  LEU A CA  1 
ATOM   2384  C C   . LEU A  1  357 ? -56.611 29.445  63.724  1.00 79.62  ?  357  LEU A C   1 
ATOM   2385  O O   . LEU A  1  357 ? -55.774 28.604  63.395  1.00 80.19  ?  357  LEU A O   1 
ATOM   2386  C CB  . LEU A  1  357 ? -57.954 27.682  64.926  1.00 80.29  ?  357  LEU A CB  1 
ATOM   2387  C CG  . LEU A  1  357 ? -59.304 27.006  65.169  1.00 80.90  ?  357  LEU A CG  1 
ATOM   2388  C CD1 . LEU A  1  357 ? -59.136 25.679  65.902  1.00 81.69  ?  357  LEU A CD1 1 
ATOM   2389  C CD2 . LEU A  1  357 ? -60.214 27.941  65.946  1.00 80.43  ?  357  LEU A CD2 1 
ATOM   2390  N N   . THR A  1  358 ? -56.374 30.757  63.643  1.00 76.41  ?  358  THR A N   1 
ATOM   2391  C CA  . THR A  1  358 ? -55.153 31.270  63.032  1.00 76.75  ?  358  THR A CA  1 
ATOM   2392  C C   . THR A  1  358 ? -53.944 31.230  63.957  1.00 75.73  ?  358  THR A C   1 
ATOM   2393  O O   . THR A  1  358 ? -52.820 31.422  63.484  1.00 76.29  ?  358  THR A O   1 
ATOM   2394  C CB  . THR A  1  358 ? -55.356 32.712  62.551  1.00 79.20  ?  358  THR A CB  1 
ATOM   2395  O OG1 . THR A  1  358 ? -55.091 33.621  63.628  1.00 78.72  ?  358  THR A OG1 1 
ATOM   2396  C CG2 . THR A  1  358 ? -56.768 32.921  62.050  1.00 82.34  ?  358  THR A CG2 1 
ATOM   2397  N N   . ALA A  1  359 ? -54.131 31.001  65.254  1.00 72.63  ?  359  ALA A N   1 
ATOM   2398  C CA  . ALA A  1  359 ? -53.018 31.003  66.192  1.00 71.82  ?  359  ALA A CA  1 
ATOM   2399  C C   . ALA A  1  359 ? -52.746 29.624  66.781  1.00 71.58  ?  359  ALA A C   1 
ATOM   2400  O O   . ALA A  1  359 ? -52.038 29.517  67.789  1.00 71.30  ?  359  ALA A O   1 
ATOM   2401  C CB  . ALA A  1  359 ? -53.268 32.021  67.302  1.00 71.32  ?  359  ALA A CB  1 
ATOM   2402  N N   . LEU A  1  360 ? -53.290 28.568  66.172  1.00 69.58  ?  360  LEU A N   1 
ATOM   2403  C CA  . LEU A  1  360 ? -53.190 27.228  66.740  1.00 69.80  ?  360  LEU A CA  1 
ATOM   2404  C C   . LEU A  1  360 ? -51.774 26.682  66.594  1.00 70.25  ?  360  LEU A C   1 
ATOM   2405  O O   . LEU A  1  360 ? -51.164 26.786  65.525  1.00 71.00  ?  360  LEU A O   1 
ATOM   2406  C CB  . LEU A  1  360 ? -54.189 26.294  66.057  1.00 70.46  ?  360  LEU A CB  1 
ATOM   2407  C CG  . LEU A  1  360 ? -54.272 24.866  66.592  1.00 70.94  ?  360  LEU A CG  1 
ATOM   2408  C CD1 . LEU A  1  360 ? -54.987 24.845  67.926  1.00 70.61  ?  360  LEU A CD1 1 
ATOM   2409  C CD2 . LEU A  1  360 ? -54.977 23.960  65.601  1.00 71.96  ?  360  LEU A CD2 1 
ATOM   2410  N N   . GLU A  1  361 ? -51.253 26.098  67.671  1.00 69.04  ?  361  GLU A N   1 
ATOM   2411  C CA  . GLU A  1  361 ? -49.923 25.499  67.672  1.00 69.50  ?  361  GLU A CA  1 
ATOM   2412  C C   . GLU A  1  361 ? -49.935 24.002  67.942  1.00 69.56  ?  361  GLU A C   1 
ATOM   2413  O O   . GLU A  1  361 ? -49.216 23.257  67.274  1.00 70.32  ?  361  GLU A O   1 
ATOM   2414  C CB  . GLU A  1  361 ? -49.029 26.202  68.703  1.00 69.07  ?  361  GLU A CB  1 
ATOM   2415  C CG  . GLU A  1  361 ? -48.874 27.698  68.478  1.00 69.19  ?  361  GLU A CG  1 
ATOM   2416  C CD  . GLU A  1  361 ? -47.706 28.290  69.249  1.00 69.43  ?  361  GLU A CD  1 
ATOM   2417  O OE1 . GLU A  1  361 ? -46.949 27.516  69.875  1.00 69.65  ?  361  GLU A OE1 1 
ATOM   2418  O OE2 . GLU A  1  361 ? -47.555 29.533  69.239  1.00 69.47  -1 361  GLU A OE2 1 
ATOM   2419  N N   . TRP A  1  362 ? -50.732 23.536  68.903  1.00 67.09  ?  362  TRP A N   1 
ATOM   2420  C CA  . TRP A  1  362 ? -50.889 22.117  69.198  1.00 67.34  ?  362  TRP A CA  1 
ATOM   2421  C C   . TRP A  1  362 ? -52.330 21.713  68.927  1.00 68.25  ?  362  TRP A C   1 
ATOM   2422  O O   . TRP A  1  362 ? -53.261 22.375  69.397  1.00 68.06  ?  362  TRP A O   1 
ATOM   2423  C CB  . TRP A  1  362 ? -50.546 21.792  70.659  1.00 66.28  ?  362  TRP A CB  1 
ATOM   2424  C CG  . TRP A  1  362 ? -49.131 22.051  71.074  1.00 65.61  ?  362  TRP A CG  1 
ATOM   2425  C CD1 . TRP A  1  362 ? -48.124 21.139  71.149  1.00 65.51  ?  362  TRP A CD1 1 
ATOM   2426  C CD2 . TRP A  1  362 ? -48.576 23.297  71.516  1.00 65.36  ?  362  TRP A CD2 1 
ATOM   2427  N NE1 . TRP A  1  362 ? -46.971 21.739  71.590  1.00 65.52  ?  362  TRP A NE1 1 
ATOM   2428  C CE2 . TRP A  1  362 ? -47.222 23.064  71.823  1.00 65.59  ?  362  TRP A CE2 1 
ATOM   2429  C CE3 . TRP A  1  362 ? -49.092 24.588  71.677  1.00 65.20  ?  362  TRP A CE3 1 
ATOM   2430  C CZ2 . TRP A  1  362 ? -46.373 24.075  72.275  1.00 66.11  ?  362  TRP A CZ2 1 
ATOM   2431  C CZ3 . TRP A  1  362 ? -48.246 25.594  72.124  1.00 65.27  ?  362  TRP A CZ3 1 
ATOM   2432  C CH2 . TRP A  1  362 ? -46.903 25.329  72.419  1.00 65.88  ?  362  TRP A CH2 1 
ATOM   2433  N N   . LEU A  1  363 ? -52.516 20.622  68.186  1.00 64.12  ?  363  LEU A N   1 
ATOM   2434  C CA  . LEU A  1  363 ? -53.840 20.051  67.957  1.00 65.50  ?  363  LEU A CA  1 
ATOM   2435  C C   . LEU A  1  363 ? -53.779 18.557  68.242  1.00 66.86  ?  363  LEU A C   1 
ATOM   2436  O O   . LEU A  1  363 ? -53.229 17.789  67.447  1.00 67.57  ?  363  LEU A O   1 
ATOM   2437  C CB  . LEU A  1  363 ? -54.321 20.313  66.532  1.00 66.04  ?  363  LEU A CB  1 
ATOM   2438  C CG  . LEU A  1  363 ? -55.751 19.848  66.259  1.00 67.24  ?  363  LEU A CG  1 
ATOM   2439  C CD1 . LEU A  1  363 ? -56.740 20.700  67.020  1.00 66.86  ?  363  LEU A CD1 1 
ATOM   2440  C CD2 . LEU A  1  363 ? -56.049 19.884  64.775  1.00 67.51  ?  363  LEU A CD2 1 
ATOM   2441  N N   . PHE A  1  364 ? -54.352 18.145  69.365  1.00 65.78  ?  364  PHE A N   1 
ATOM   2442  C CA  . PHE A  1  364 ? -54.353 16.754  69.800  1.00 67.61  ?  364  PHE A CA  1 
ATOM   2443  C C   . PHE A  1  364 ? -55.746 16.173  69.579  1.00 69.71  ?  364  PHE A C   1 
ATOM   2444  O O   . PHE A  1  364 ? -56.679 16.493  70.323  1.00 70.09  ?  364  PHE A O   1 
ATOM   2445  C CB  . PHE A  1  364 ? -53.957 16.660  71.268  1.00 66.95  ?  364  PHE A CB  1 
ATOM   2446  C CG  . PHE A  1  364 ? -52.489 16.492  71.502  1.00 64.93  ?  364  PHE A CG  1 
ATOM   2447  C CD1 . PHE A  1  364 ? -51.614 17.540  71.287  1.00 62.39  ?  364  PHE A CD1 1 
ATOM   2448  C CD2 . PHE A  1  364 ? -51.990 15.295  71.981  1.00 65.48  ?  364  PHE A CD2 1 
ATOM   2449  C CE1 . PHE A  1  364 ? -50.261 17.388  71.524  1.00 60.55  ?  364  PHE A CE1 1 
ATOM   2450  C CE2 . PHE A  1  364 ? -50.641 15.138  72.222  1.00 62.55  ?  364  PHE A CE2 1 
ATOM   2451  C CZ  . PHE A  1  364 ? -49.774 16.186  71.993  1.00 60.38  ?  364  PHE A CZ  1 
ATOM   2452  N N   . LEU A  1  365 ? -55.892 15.330  68.555  1.00 69.35  ?  365  LEU A N   1 
ATOM   2453  C CA  . LEU A  1  365 ? -57.146 14.625  68.305  1.00 70.52  ?  365  LEU A CA  1 
ATOM   2454  C C   . LEU A  1  365 ? -56.971 13.111  68.278  1.00 71.25  ?  365  LEU A C   1 
ATOM   2455  O O   . LEU A  1  365 ? -57.886 12.400  67.842  1.00 71.54  ?  365  LEU A O   1 
ATOM   2456  C CB  . LEU A  1  365 ? -57.780 15.085  66.988  1.00 70.01  ?  365  LEU A CB  1 
ATOM   2457  C CG  . LEU A  1  365 ? -58.190 16.548  66.828  1.00 68.76  ?  365  LEU A CG  1 
ATOM   2458  C CD1 . LEU A  1  365 ? -58.592 16.811  65.390  1.00 68.33  ?  365  LEU A CD1 1 
ATOM   2459  C CD2 . LEU A  1  365 ? -59.325 16.895  67.766  1.00 69.10  ?  365  LEU A CD2 1 
ATOM   2460  N N   . ARG A  1  366 ? -55.828 12.603  68.731  1.00 73.90  ?  366  ARG A N   1 
ATOM   2461  C CA  . ARG A  1  366 ? -55.525 11.185  68.629  1.00 73.39  ?  366  ARG A CA  1 
ATOM   2462  C C   . ARG A  1  366 ? -56.417 10.360  69.553  1.00 73.29  ?  366  ARG A C   1 
ATOM   2463  O O   . ARG A  1  366 ? -57.022 10.869  70.500  1.00 73.63  ?  366  ARG A O   1 
ATOM   2464  C CB  . ARG A  1  366 ? -54.055 10.933  68.958  1.00 72.22  ?  366  ARG A CB  1 
ATOM   2465  C CG  . ARG A  1  366 ? -53.599 11.529  70.275  1.00 71.38  ?  366  ARG A CG  1 
ATOM   2466  C CD  . ARG A  1  366 ? -52.155 11.159  70.567  1.00 69.14  ?  366  ARG A CD  1 
ATOM   2467  N NE  . ARG A  1  366 ? -51.933 9.721   70.483  1.00 68.20  ?  366  ARG A NE  1 
ATOM   2468  C CZ  . ARG A  1  366 ? -52.367 8.842   71.375  1.00 67.56  ?  366  ARG A CZ  1 
ATOM   2469  N NH1 . ARG A  1  366 ? -53.048 9.220   72.445  1.00 67.54  ?  366  ARG A NH1 1 
ATOM   2470  N NH2 . ARG A  1  366 ? -52.113 7.550   71.190  1.00 67.17  ?  366  ARG A NH2 1 
ATOM   2471  N N   . ASP A  1  367 ? -56.492 9.061   69.254  1.00 79.46  ?  367  ASP A N   1 
ATOM   2472  C CA  . ASP A  1  367 ? -57.249 8.091   70.045  1.00 79.23  ?  367  ASP A CA  1 
ATOM   2473  C C   . ASP A  1  367 ? -58.724 8.487   70.155  1.00 80.20  ?  367  ASP A C   1 
ATOM   2474  O O   . ASP A  1  367 ? -59.248 8.772   71.234  1.00 80.33  ?  367  ASP A O   1 
ATOM   2475  C CB  . ASP A  1  367 ? -56.624 7.897   71.428  1.00 78.10  ?  367  ASP A CB  1 
ATOM   2476  C CG  . ASP A  1  367 ? -57.175 6.681   72.139  1.00 77.66  ?  367  ASP A CG  1 
ATOM   2477  O OD1 . ASP A  1  367 ? -58.401 6.452   72.058  1.00 78.57  -1 367  ASP A OD1 1 
ATOM   2478  O OD2 . ASP A  1  367 ? -56.386 5.945   72.767  1.00 76.30  ?  367  ASP A OD2 1 
ATOM   2479  N N   . ASN A  1  368 ? -59.382 8.525   69.003  1.00 81.24  ?  368  ASN A N   1 
ATOM   2480  C CA  . ASN A  1  368 ? -60.811 8.790   68.937  1.00 81.82  ?  368  ASN A CA  1 
ATOM   2481  C C   . ASN A  1  368 ? -61.395 7.920   67.833  1.00 81.71  ?  368  ASN A C   1 
ATOM   2482  O O   . ASN A  1  368 ? -60.742 7.005   67.324  1.00 81.29  ?  368  ASN A O   1 
ATOM   2483  C CB  . ASN A  1  368 ? -61.082 10.284  68.712  1.00 82.30  ?  368  ASN A CB  1 
ATOM   2484  C CG  . ASN A  1  368 ? -61.463 11.006  69.992  1.00 82.71  ?  368  ASN A CG  1 
ATOM   2485  O OD1 . ASN A  1  368 ? -62.573 10.850  70.503  1.00 83.01  ?  368  ASN A OD1 1 
ATOM   2486  N ND2 . ASN A  1  368 ? -60.536 11.794  70.523  1.00 82.69  ?  368  ASN A ND2 1 
ATOM   2487  N N   . GLN A  1  369 ? -62.641 8.197   67.467  1.00 87.88  ?  369  GLN A N   1 
ATOM   2488  C CA  . GLN A  1  369 ? -63.311 7.472   66.397  1.00 87.69  ?  369  GLN A CA  1 
ATOM   2489  C C   . GLN A  1  369 ? -63.785 8.422   65.303  1.00 87.72  ?  369  GLN A C   1 
ATOM   2490  O O   . GLN A  1  369 ? -64.832 8.205   64.689  1.00 87.56  ?  369  GLN A O   1 
ATOM   2491  C CB  . GLN A  1  369 ? -64.481 6.658   66.948  1.00 87.63  ?  369  GLN A CB  1 
ATOM   2492  C CG  . GLN A  1  369 ? -64.233 6.046   68.321  1.00 87.44  ?  369  GLN A CG  1 
ATOM   2493  C CD  . GLN A  1  369 ? -64.827 4.654   68.454  1.00 86.98  ?  369  GLN A CD  1 
ATOM   2494  O OE1 . GLN A  1  369 ? -64.102 3.656   68.457  1.00 86.34  ?  369  GLN A OE1 1 
ATOM   2495  N NE2 . GLN A  1  369 ? -66.152 4.579   68.564  1.00 87.24  ?  369  GLN A NE2 1 
ATOM   2496  N N   . LEU A  1  370 ? -63.017 9.479   65.053  1.00 83.13  ?  370  LEU A N   1 
ATOM   2497  C CA  . LEU A  1  370 ? -63.347 10.416  63.994  1.00 84.71  ?  370  LEU A CA  1 
ATOM   2498  C C   . LEU A  1  370 ? -63.114 9.768   62.631  1.00 86.56  ?  370  LEU A C   1 
ATOM   2499  O O   . LEU A  1  370 ? -62.340 8.817   62.491  1.00 85.60  ?  370  LEU A O   1 
ATOM   2500  C CB  . LEU A  1  370 ? -62.515 11.689  64.131  1.00 81.91  ?  370  LEU A CB  1 
ATOM   2501  C CG  . LEU A  1  370 ? -62.233 12.186  65.548  1.00 82.14  ?  370  LEU A CG  1 
ATOM   2502  C CD1 . LEU A  1  370 ? -61.472 13.500  65.522  1.00 81.73  ?  370  LEU A CD1 1 
ATOM   2503  C CD2 . LEU A  1  370 ? -63.539 12.356  66.286  1.00 82.33  ?  370  LEU A CD2 1 
ATOM   2504  N N   . SER A  1  371 ? -63.794 10.296  61.616  1.00 87.95  ?  371  SER A N   1 
ATOM   2505  C CA  . SER A  1  371 ? -63.826 9.655   60.309  1.00 87.66  ?  371  SER A CA  1 
ATOM   2506  C C   . SER A  1  371 ? -63.905 10.716  59.221  1.00 87.13  ?  371  SER A C   1 
ATOM   2507  O O   . SER A  1  371 ? -64.041 11.911  59.494  1.00 86.83  ?  371  SER A O   1 
ATOM   2508  C CB  . SER A  1  371 ? -65.004 8.684   60.200  1.00 87.85  ?  371  SER A CB  1 
ATOM   2509  O OG  . SER A  1  371 ? -66.233 9.363   60.400  1.00 88.96  ?  371  SER A OG  1 
ATOM   2510  N N   . GLY A  1  372 ? -63.801 10.258  57.973  1.00 89.54  ?  372  GLY A N   1 
ATOM   2511  C CA  . GLY A  1  372 ? -63.892 11.121  56.819  1.00 90.54  ?  372  GLY A CA  1 
ATOM   2512  C C   . GLY A  1  372 ? -62.551 11.697  56.405  1.00 88.69  ?  372  GLY A C   1 
ATOM   2513  O O   . GLY A  1  372 ? -61.496 11.310  56.916  1.00 88.92  ?  372  GLY A O   1 
ATOM   2514  N N   . PRO A  1  373 ? -62.572 12.640  55.467  1.00 90.09  ?  373  PRO A N   1 
ATOM   2515  C CA  . PRO A  1  373 ? -61.339 13.296  55.026  1.00 88.56  ?  373  PRO A CA  1 
ATOM   2516  C C   . PRO A  1  373 ? -60.946 14.466  55.919  1.00 88.05  ?  373  PRO A C   1 
ATOM   2517  O O   . PRO A  1  373 ? -61.766 15.061  56.622  1.00 87.90  ?  373  PRO A O   1 
ATOM   2518  C CB  . PRO A  1  373 ? -61.705 13.794  53.623  1.00 91.65  ?  373  PRO A CB  1 
ATOM   2519  C CG  . PRO A  1  373 ? -63.168 14.088  53.720  1.00 95.19  ?  373  PRO A CG  1 
ATOM   2520  C CD  . PRO A  1  373 ? -63.753 13.135  54.740  1.00 94.58  ?  373  PRO A CD  1 
ATOM   2521  N N   . ILE A  1  374 ? -59.657 14.789  55.876  1.00 88.71  ?  374  ILE A N   1 
ATOM   2522  C CA  . ILE A  1  374 ? -59.117 15.921  56.627  1.00 88.30  ?  374  ILE A CA  1 
ATOM   2523  C C   . ILE A  1  374 ? -59.434 17.210  55.878  1.00 87.41  ?  374  ILE A C   1 
ATOM   2524  O O   . ILE A  1  374 ? -59.075 17.346  54.700  1.00 87.19  ?  374  ILE A O   1 
ATOM   2525  C CB  . ILE A  1  374 ? -57.602 15.771  56.847  1.00 88.53  ?  374  ILE A CB  1 
ATOM   2526  C CG1 . ILE A  1  374 ? -57.313 14.810  57.994  1.00 89.26  ?  374  ILE A CG1 1 
ATOM   2527  C CG2 . ILE A  1  374 ? -56.986 17.113  57.207  1.00 87.85  ?  374  ILE A CG2 1 
ATOM   2528  C CD1 . ILE A  1  374 ? -58.104 15.121  59.225  1.00 89.35  ?  374  ILE A CD1 1 
ATOM   2529  N N   . PRO A  1  375 ? -60.111 18.170  56.500  1.00 88.62  ?  375  PRO A N   1 
ATOM   2530  C CA  . PRO A  1  375 ? -60.323 19.466  55.851  1.00 89.04  ?  375  PRO A CA  1 
ATOM   2531  C C   . PRO A  1  375 ? -59.013 20.221  55.734  1.00 87.96  ?  375  PRO A C   1 
ATOM   2532  O O   . PRO A  1  375 ? -58.195 20.208  56.668  1.00 87.52  ?  375  PRO A O   1 
ATOM   2533  C CB  . PRO A  1  375 ? -61.298 20.189  56.796  1.00 89.28  ?  375  PRO A CB  1 
ATOM   2534  C CG  . PRO A  1  375 ? -61.836 19.133  57.691  1.00 88.84  ?  375  PRO A CG  1 
ATOM   2535  C CD  . PRO A  1  375 ? -60.767 18.101  57.812  1.00 88.87  ?  375  PRO A CD  1 
ATOM   2536  N N   . PRO A  1  376 ? -58.774 20.888  54.602  1.00 88.36  ?  376  PRO A N   1 
ATOM   2537  C CA  . PRO A  1  376 ? -57.523 21.649  54.450  1.00 87.56  ?  376  PRO A CA  1 
ATOM   2538  C C   . PRO A  1  376 ? -57.344 22.732  55.497  1.00 86.58  ?  376  PRO A C   1 
ATOM   2539  O O   . PRO A  1  376 ? -56.213 23.182  55.716  1.00 85.67  ?  376  PRO A O   1 
ATOM   2540  C CB  . PRO A  1  376 ? -57.644 22.247  53.041  1.00 90.60  ?  376  PRO A CB  1 
ATOM   2541  C CG  . PRO A  1  376 ? -58.636 21.376  52.338  1.00 93.26  ?  376  PRO A CG  1 
ATOM   2542  C CD  . PRO A  1  376 ? -59.607 20.941  53.390  1.00 92.49  ?  376  PRO A CD  1 
ATOM   2543  N N   . GLY A  1  377 ? -58.420 23.159  56.158  1.00 88.16  ?  377  GLY A N   1 
ATOM   2544  C CA  . GLY A  1  377 ? -58.302 24.169  57.189  1.00 87.26  ?  377  GLY A CA  1 
ATOM   2545  C C   . GLY A  1  377 ? -57.549 23.720  58.425  1.00 85.82  ?  377  GLY A C   1 
ATOM   2546  O O   . GLY A  1  377 ? -57.134 24.568  59.222  1.00 85.28  ?  377  GLY A O   1 
ATOM   2547  N N   . ILE A  1  378 ? -57.374 22.411  58.616  1.00 83.94  ?  378  ILE A N   1 
ATOM   2548  C CA  . ILE A  1  378 ? -56.714 21.931  59.828  1.00 84.17  ?  378  ILE A CA  1 
ATOM   2549  C C   . ILE A  1  378 ? -55.293 22.469  59.912  1.00 83.89  ?  378  ILE A C   1 
ATOM   2550  O O   . ILE A  1  378 ? -54.864 22.993  60.948  1.00 83.38  ?  378  ILE A O   1 
ATOM   2551  C CB  . ILE A  1  378 ? -56.729 20.396  59.885  1.00 85.18  ?  378  ILE A CB  1 
ATOM   2552  C CG1 . ILE A  1  378 ? -58.154 19.888  60.054  1.00 85.61  ?  378  ILE A CG1 1 
ATOM   2553  C CG2 . ILE A  1  378 ? -55.866 19.908  61.038  1.00 85.38  ?  378  ILE A CG2 1 
ATOM   2554  C CD1 . ILE A  1  378 ? -58.213 18.493  60.610  1.00 86.68  ?  378  ILE A CD1 1 
ATOM   2555  N N   . ALA A  1  379 ? -54.541 22.349  58.819  1.00 84.20  ?  379  ALA A N   1 
ATOM   2556  C CA  . ALA A  1  379 ? -53.144 22.758  58.782  1.00 84.34  ?  379  ALA A CA  1 
ATOM   2557  C C   . ALA A  1  379 ? -52.957 24.190  58.290  1.00 83.97  ?  379  ALA A C   1 
ATOM   2558  O O   . ALA A  1  379 ? -51.887 24.519  57.762  1.00 84.54  ?  379  ALA A O   1 
ATOM   2559  C CB  . ALA A  1  379 ? -52.342 21.784  57.922  1.00 85.26  ?  379  ALA A CB  1 
ATOM   2560  N N   . ASN A  1  380 ? -53.967 25.054  58.453  1.00 86.25  ?  380  ASN A N   1 
ATOM   2561  C CA  . ASN A  1  380 ? -53.871 26.430  57.967  1.00 85.87  ?  380  ASN A CA  1 
ATOM   2562  C C   . ASN A  1  380 ? -52.885 27.261  58.780  1.00 85.75  ?  380  ASN A C   1 
ATOM   2563  O O   . ASN A  1  380 ? -52.230 28.154  58.230  1.00 86.02  ?  380  ASN A O   1 
ATOM   2564  C CB  . ASN A  1  380 ? -55.245 27.101  58.012  1.00 85.85  ?  380  ASN A CB  1 
ATOM   2565  C CG  . ASN A  1  380 ? -55.682 27.645  56.668  1.00 88.37  ?  380  ASN A CG  1 
ATOM   2566  O OD1 . ASN A  1  380 ? -55.084 27.339  55.637  1.00 89.15  ?  380  ASN A OD1 1 
ATOM   2567  N ND2 . ASN A  1  380 ? -56.736 28.462  56.677  1.00 91.22  ?  380  ASN A ND2 1 
ATOM   2568  N N   . SER A  1  381 ? -52.769 26.989  60.078  1.00 82.70  ?  381  SER A N   1 
ATOM   2569  C CA  . SER A  1  381 ? -52.017 27.862  60.971  1.00 82.39  ?  381  SER A CA  1 
ATOM   2570  C C   . SER A  1  381 ? -50.530 27.840  60.643  1.00 83.45  ?  381  SER A C   1 
ATOM   2571  O O   . SER A  1  381 ? -49.925 26.772  60.507  1.00 84.23  ?  381  SER A O   1 
ATOM   2572  C CB  . SER A  1  381 ? -52.238 27.447  62.424  1.00 81.75  ?  381  SER A CB  1 
ATOM   2573  O OG  . SER A  1  381 ? -53.568 27.006  62.624  1.00 81.41  ?  381  SER A OG  1 
ATOM   2574  N N   . THR A  1  382 ? -49.939 29.032  60.529  1.00 80.93  ?  382  THR A N   1 
ATOM   2575  C CA  . THR A  1  382 ? -48.506 29.135  60.286  1.00 82.29  ?  382  THR A CA  1 
ATOM   2576  C C   . THR A  1  382 ? -47.691 28.817  61.534  1.00 82.46  ?  382  THR A C   1 
ATOM   2577  O O   . THR A  1  382 ? -46.500 28.510  61.416  1.00 83.94  ?  382  THR A O   1 
ATOM   2578  C CB  . THR A  1  382 ? -48.157 30.537  59.771  1.00 82.51  ?  382  THR A CB  1 
ATOM   2579  O OG1 . THR A  1  382 ? -48.397 31.508  60.800  1.00 81.36  ?  382  THR A OG1 1 
ATOM   2580  C CG2 . THR A  1  382 ? -49.009 30.886  58.563  1.00 82.35  ?  382  THR A CG2 1 
ATOM   2581  N N   . GLU A  1  383 ? -48.302 28.882  62.718  1.00 77.59  ?  383  GLU A N   1 
ATOM   2582  C CA  . GLU A  1  383 ? -47.638 28.514  63.961  1.00 77.49  ?  383  GLU A CA  1 
ATOM   2583  C C   . GLU A  1  383 ? -47.874 27.065  64.360  1.00 77.21  ?  383  GLU A C   1 
ATOM   2584  O O   . GLU A  1  383 ? -47.407 26.653  65.428  1.00 76.89  ?  383  GLU A O   1 
ATOM   2585  C CB  . GLU A  1  383 ? -48.093 29.430  65.098  1.00 76.16  ?  383  GLU A CB  1 
ATOM   2586  C CG  . GLU A  1  383 ? -47.091 30.514  65.439  1.00 76.63  ?  383  GLU A CG  1 
ATOM   2587  C CD  . GLU A  1  383 ? -47.219 31.723  64.534  1.00 76.80  ?  383  GLU A CD  1 
ATOM   2588  O OE1 . GLU A  1  383 ? -48.360 32.045  64.135  1.00 75.95  ?  383  GLU A OE1 1 
ATOM   2589  O OE2 . GLU A  1  383 ? -46.186 32.356  64.223  1.00 77.85  -1 383  GLU A OE2 1 
ATOM   2590  N N   . LEU A  1  384 ? -48.588 26.293  63.540  1.00 70.62  ?  384  LEU A N   1 
ATOM   2591  C CA  . LEU A  1  384 ? -48.847 24.895  63.859  1.00 70.43  ?  384  LEU A CA  1 
ATOM   2592  C C   . LEU A  1  384 ? -47.537 24.133  64.004  1.00 71.34  ?  384  LEU A C   1 
ATOM   2593  O O   . LEU A  1  384 ? -46.686 24.154  63.111  1.00 72.80  ?  384  LEU A O   1 
ATOM   2594  C CB  . LEU A  1  384 ? -49.719 24.262  62.772  1.00 70.75  ?  384  LEU A CB  1 
ATOM   2595  C CG  . LEU A  1  384 ? -50.250 22.853  63.045  1.00 70.67  ?  384  LEU A CG  1 
ATOM   2596  C CD1 . LEU A  1  384 ? -50.870 22.789  64.421  1.00 69.57  ?  384  LEU A CD1 1 
ATOM   2597  C CD2 . LEU A  1  384 ? -51.259 22.429  61.988  1.00 71.36  ?  384  LEU A CD2 1 
ATOM   2598  N N   . THR A  1  385 ? -47.380 23.459  65.134  1.00 66.73  ?  385  THR A N   1 
ATOM   2599  C CA  . THR A  1  385 ? -46.159 22.737  65.451  1.00 67.41  ?  385  THR A CA  1 
ATOM   2600  C C   . THR A  1  385 ? -46.372 21.255  65.697  1.00 66.85  ?  385  THR A C   1 
ATOM   2601  O O   . THR A  1  385 ? -45.476 20.462  65.407  1.00 67.67  ?  385  THR A O   1 
ATOM   2602  C CB  . THR A  1  385 ? -45.480 23.344  66.683  1.00 67.06  ?  385  THR A CB  1 
ATOM   2603  O OG1 . THR A  1  385 ? -46.479 23.725  67.633  1.00 65.27  ?  385  THR A OG1 1 
ATOM   2604  C CG2 . THR A  1  385 ? -44.682 24.565  66.295  1.00 68.75  ?  385  THR A CG2 1 
ATOM   2605  N N   . VAL A  1  386 ? -47.516 20.858  66.240  1.00 65.65  ?  386  VAL A N   1 
ATOM   2606  C CA  . VAL A  1  386 ? -47.782 19.468  66.576  1.00 65.44  ?  386  VAL A CA  1 
ATOM   2607  C C   . VAL A  1  386 ? -49.157 19.097  66.049  1.00 66.11  ?  386  VAL A C   1 
ATOM   2608  O O   . VAL A  1  386 ? -50.136 19.805  66.309  1.00 65.78  ?  386  VAL A O   1 
ATOM   2609  C CB  . VAL A  1  386 ? -47.701 19.227  68.093  1.00 64.03  ?  386  VAL A CB  1 
ATOM   2610  C CG1 . VAL A  1  386 ? -48.107 17.794  68.426  1.00 64.21  ?  386  VAL A CG1 1 
ATOM   2611  C CG2 . VAL A  1  386 ? -46.299 19.524  68.592  1.00 63.68  ?  386  VAL A CG2 1 
ATOM   2612  N N   . LEU A  1  387 ? -49.233 17.985  65.313  1.00 65.53  ?  387  LEU A N   1 
ATOM   2613  C CA  . LEU A  1  387 ? -50.493 17.526  64.726  1.00 66.64  ?  387  LEU A CA  1 
ATOM   2614  C C   . LEU A  1  387 ? -50.588 16.013  64.977  1.00 67.94  ?  387  LEU A C   1 
ATOM   2615  O O   . LEU A  1  387 ? -50.077 15.212  64.191  1.00 68.83  ?  387  LEU A O   1 
ATOM   2616  C CB  . LEU A  1  387 ? -50.532 17.887  63.242  1.00 67.15  ?  387  LEU A CB  1 
ATOM   2617  C CG  . LEU A  1  387 ? -51.864 18.277  62.605  1.00 67.44  ?  387  LEU A CG  1 
ATOM   2618  C CD1 . LEU A  1  387 ? -51.755 18.496  61.111  1.00 67.93  ?  387  LEU A CD1 1 
ATOM   2619  C CD2 . LEU A  1  387 ? -52.826 17.195  62.888  1.00 68.11  ?  387  LEU A CD2 1 
ATOM   2620  N N   . GLN A  1  388 ? -51.257 15.629  66.071  1.00 70.39  ?  388  GLN A N   1 
ATOM   2621  C CA  . GLN A  1  388 ? -51.391 14.231  66.481  1.00 72.10  ?  388  GLN A CA  1 
ATOM   2622  C C   . GLN A  1  388 ? -52.774 13.703  66.105  1.00 73.45  ?  388  GLN A C   1 
ATOM   2623  O O   . GLN A  1  388 ? -53.778 14.141  66.675  1.00 73.55  ?  388  GLN A O   1 
ATOM   2624  C CB  . GLN A  1  388 ? -51.169 14.090  67.987  1.00 71.69  ?  388  GLN A CB  1 
ATOM   2625  C CG  . GLN A  1  388 ? -49.860 14.664  68.480  1.00 69.02  ?  388  GLN A CG  1 
ATOM   2626  C CD  . GLN A  1  388 ? -48.803 13.603  68.669  1.00 68.40  ?  388  GLN A CD  1 
ATOM   2627  O OE1 . GLN A  1  388 ? -49.080 12.407  68.558  1.00 69.30  ?  388  GLN A OE1 1 
ATOM   2628  N NE2 . GLN A  1  388 ? -47.579 14.032  68.953  1.00 65.78  ?  388  GLN A NE2 1 
ATOM   2629  N N   . LEU A  1  389 ? -52.820 12.719  65.194  1.00 70.84  ?  389  LEU A N   1 
ATOM   2630  C CA  . LEU A  1  389 ? -54.076 12.186  64.665  1.00 71.31  ?  389  LEU A CA  1 
ATOM   2631  C C   . LEU A  1  389 ? -54.162 10.663  64.662  1.00 71.43  ?  389  LEU A C   1 
ATOM   2632  O O   . LEU A  1  389 ? -55.099 10.116  64.069  1.00 71.67  ?  389  LEU A O   1 
ATOM   2633  C CB  . LEU A  1  389 ? -54.332 12.677  63.234  1.00 71.02  ?  389  LEU A CB  1 
ATOM   2634  C CG  . LEU A  1  389 ? -54.374 14.165  62.938  1.00 70.13  ?  389  LEU A CG  1 
ATOM   2635  C CD1 . LEU A  1  389 ? -54.902 14.443  61.544  1.00 69.92  ?  389  LEU A CD1 1 
ATOM   2636  C CD2 . LEU A  1  389 ? -55.291 14.813  63.945  1.00 69.93  ?  389  LEU A CD2 1 
ATOM   2637  N N   . ASP A  1  390 ? -53.227 9.962   65.292  1.00 73.97  ?  390  ASP A N   1 
ATOM   2638  C CA  . ASP A  1  390 ? -53.218 8.510   65.195  1.00 73.54  ?  390  ASP A CA  1 
ATOM   2639  C C   . ASP A  1  390 ? -54.437 7.906   65.883  1.00 73.76  ?  390  ASP A C   1 
ATOM   2640  O O   . ASP A  1  390 ? -55.179 8.578   66.605  1.00 74.12  ?  390  ASP A O   1 
ATOM   2641  C CB  . ASP A  1  390 ? -51.956 7.929   65.817  1.00 72.35  ?  390  ASP A CB  1 
ATOM   2642  C CG  . ASP A  1  390 ? -51.828 8.273   67.280  1.00 71.50  ?  390  ASP A CG  1 
ATOM   2643  O OD1 . ASP A  1  390 ? -51.552 9.451   67.599  1.00 71.58  ?  390  ASP A OD1 1 
ATOM   2644  O OD2 . ASP A  1  390 ? -52.019 7.366   68.114  1.00 70.79  -1 390  ASP A OD2 1 
ATOM   2645  N N   . THR A  1  391 ? -54.637 6.611   65.632  1.00 74.41  ?  391  THR A N   1 
ATOM   2646  C CA  . THR A  1  391 ? -55.668 5.813   66.294  1.00 74.47  ?  391  THR A CA  1 
ATOM   2647  C C   . THR A  1  391 ? -57.057 6.417   66.065  1.00 75.24  ?  391  THR A C   1 
ATOM   2648  O O   . THR A  1  391 ? -57.753 6.843   66.989  1.00 75.43  ?  391  THR A O   1 
ATOM   2649  C CB  . THR A  1  391 ? -55.355 5.650   67.787  1.00 73.72  ?  391  THR A CB  1 
ATOM   2650  O OG1 . THR A  1  391 ? -53.947 5.454   67.963  1.00 72.76  ?  391  THR A OG1 1 
ATOM   2651  C CG2 . THR A  1  391 ? -56.071 4.442   68.344  1.00 73.54  ?  391  THR A CG2 1 
ATOM   2652  N N   . ASN A  1  392 ? -57.438 6.458   64.793  1.00 79.99  ?  392  ASN A N   1 
ATOM   2653  C CA  . ASN A  1  392 ? -58.700 7.034   64.357  1.00 80.43  ?  392  ASN A CA  1 
ATOM   2654  C C   . ASN A  1  392 ? -59.164 6.265   63.125  1.00 80.39  ?  392  ASN A C   1 
ATOM   2655  O O   . ASN A  1  392 ? -58.626 5.202   62.803  1.00 80.16  ?  392  ASN A O   1 
ATOM   2656  C CB  . ASN A  1  392 ? -58.534 8.534   64.095  1.00 80.60  ?  392  ASN A CB  1 
ATOM   2657  C CG  . ASN A  1  392 ? -58.903 9.381   65.296  1.00 80.85  ?  392  ASN A CG  1 
ATOM   2658  O OD1 . ASN A  1  392 ? -60.073 9.478   65.668  1.00 81.10  ?  392  ASN A OD1 1 
ATOM   2659  N ND2 . ASN A  1  392 ? -57.903 9.999   65.912  1.00 80.73  ?  392  ASN A ND2 1 
ATOM   2660  N N   . ASN A  1  393 ? -60.178 6.789   62.439  1.00 87.95  ?  393  ASN A N   1 
ATOM   2661  C CA  . ASN A  1  393 ? -60.770 6.121   61.279  1.00 87.83  ?  393  ASN A CA  1 
ATOM   2662  C C   . ASN A  1  393 ? -60.879 7.083   60.100  1.00 87.70  ?  393  ASN A C   1 
ATOM   2663  O O   . ASN A  1  393 ? -61.895 7.134   59.402  1.00 87.52  ?  393  ASN A O   1 
ATOM   2664  C CB  . ASN A  1  393 ? -62.152 5.543   61.596  1.00 87.80  ?  393  ASN A CB  1 
ATOM   2665  C CG  . ASN A  1  393 ? -62.120 4.467   62.675  1.00 87.76  ?  393  ASN A CG  1 
ATOM   2666  O OD1 . ASN A  1  393 ? -61.426 4.595   63.683  1.00 87.49  ?  393  ASN A OD1 1 
ATOM   2667  N ND2 . ASN A  1  393 ? -62.886 3.397   62.465  1.00 87.90  ?  393  ASN A ND2 1 
ATOM   2668  N N   . PHE A  1  394 ? -59.817 7.845   59.844  1.00 86.40  ?  394  PHE A N   1 
ATOM   2669  C CA  . PHE A  1  394 ? -59.848 8.839   58.782  1.00 86.09  ?  394  PHE A CA  1 
ATOM   2670  C C   . PHE A  1  394 ? -59.601 8.198   57.415  1.00 85.90  ?  394  PHE A C   1 
ATOM   2671  O O   . PHE A  1  394 ? -59.142 7.059   57.300  1.00 86.04  ?  394  PHE A O   1 
ATOM   2672  C CB  . PHE A  1  394 ? -58.825 9.944   59.039  1.00 85.96  ?  394  PHE A CB  1 
ATOM   2673  C CG  . PHE A  1  394 ? -59.221 10.879  60.133  1.00 86.02  ?  394  PHE A CG  1 
ATOM   2674  C CD1 . PHE A  1  394 ? -59.169 10.479  61.453  1.00 86.36  ?  394  PHE A CD1 1 
ATOM   2675  C CD2 . PHE A  1  394 ? -59.635 12.166  59.847  1.00 85.62  ?  394  PHE A CD2 1 
ATOM   2676  C CE1 . PHE A  1  394 ? -59.535 11.339  62.469  1.00 86.45  ?  394  PHE A CE1 1 
ATOM   2677  C CE2 . PHE A  1  394 ? -60.016 13.025  60.862  1.00 85.59  ?  394  PHE A CE2 1 
ATOM   2678  C CZ  . PHE A  1  394 ? -59.955 12.614  62.171  1.00 86.08  ?  394  PHE A CZ  1 
ATOM   2679  N N   . THR A  1  395 ? -59.919 8.959   56.365  1.00 87.84  ?  395  THR A N   1 
ATOM   2680  C CA  . THR A  1  395 ? -59.798 8.516   54.982  1.00 87.64  ?  395  THR A CA  1 
ATOM   2681  C C   . THR A  1  395 ? -59.250 9.651   54.125  1.00 87.19  ?  395  THR A C   1 
ATOM   2682  O O   . THR A  1  395 ? -59.240 10.816  54.532  1.00 86.92  ?  395  THR A O   1 
ATOM   2683  C CB  . THR A  1  395 ? -61.145 8.051   54.406  1.00 87.98  ?  395  THR A CB  1 
ATOM   2684  O OG1 . THR A  1  395 ? -62.090 9.128   54.462  1.00 89.46  ?  395  THR A OG1 1 
ATOM   2685  C CG2 . THR A  1  395 ? -61.686 6.863   55.182  1.00 88.53  ?  395  THR A CG2 1 
ATOM   2686  N N   . GLY A  1  396 ? -58.777 9.293   52.933  1.00 85.69  ?  396  GLY A N   1 
ATOM   2687  C CA  . GLY A  1  396 ? -58.429 10.280  51.924  1.00 85.48  ?  396  GLY A CA  1 
ATOM   2688  C C   . GLY A  1  396 ? -56.981 10.738  51.961  1.00 85.21  ?  396  GLY A C   1 
ATOM   2689  O O   . GLY A  1  396 ? -56.077 10.047  52.441  1.00 85.63  ?  396  GLY A O   1 
ATOM   2690  N N   . PHE A  1  397 ? -56.771 11.948  51.442  1.00 89.13  ?  397  PHE A N   1 
ATOM   2691  C CA  . PHE A  1  397 ? -55.445 12.488  51.173  1.00 89.11  ?  397  PHE A CA  1 
ATOM   2692  C C   . PHE A  1  397 ? -55.056 13.539  52.209  1.00 88.96  ?  397  PHE A C   1 
ATOM   2693  O O   . PHE A  1  397 ? -55.905 14.162  52.853  1.00 88.65  ?  397  PHE A O   1 
ATOM   2694  C CB  . PHE A  1  397 ? -55.380 13.116  49.776  1.00 88.73  ?  397  PHE A CB  1 
ATOM   2695  C CG  . PHE A  1  397 ? -55.523 12.132  48.636  1.00 89.49  ?  397  PHE A CG  1 
ATOM   2696  C CD1 . PHE A  1  397 ? -56.004 10.849  48.838  1.00 89.81  ?  397  PHE A CD1 1 
ATOM   2697  C CD2 . PHE A  1  397 ? -55.179 12.508  47.348  1.00 90.96  ?  397  PHE A CD2 1 
ATOM   2698  C CE1 . PHE A  1  397 ? -56.133 9.971   47.780  1.00 91.76  ?  397  PHE A CE1 1 
ATOM   2699  C CE2 . PHE A  1  397 ? -55.300 11.623  46.289  1.00 93.35  ?  397  PHE A CE2 1 
ATOM   2700  C CZ  . PHE A  1  397 ? -55.780 10.352  46.510  1.00 93.77  ?  397  PHE A CZ  1 
ATOM   2701  N N   . LEU A  1  398 ? -53.743 13.735  52.355  1.00 83.99  ?  398  LEU A N   1 
ATOM   2702  C CA  . LEU A  1  398 ? -53.273 14.839  53.181  1.00 83.30  ?  398  LEU A CA  1 
ATOM   2703  C C   . LEU A  1  398 ? -53.455 16.161  52.432  1.00 83.44  ?  398  LEU A C   1 
ATOM   2704  O O   . LEU A  1  398 ? -53.248 16.218  51.216  1.00 84.14  ?  398  LEU A O   1 
ATOM   2705  C CB  . LEU A  1  398 ? -51.803 14.652  53.553  1.00 83.71  ?  398  LEU A CB  1 
ATOM   2706  C CG  . LEU A  1  398 ? -51.436 13.560  54.559  1.00 84.14  ?  398  LEU A CG  1 
ATOM   2707  C CD1 . LEU A  1  398 ? -50.226 13.978  55.370  1.00 84.08  ?  398  LEU A CD1 1 
ATOM   2708  C CD2 . LEU A  1  398 ? -52.597 13.243  55.474  1.00 84.12  ?  398  LEU A CD2 1 
ATOM   2709  N N   . PRO A  1  399 ? -53.852 17.227  53.123  1.00 88.90  ?  399  PRO A N   1 
ATOM   2710  C CA  . PRO A  1  399 ? -54.016 18.523  52.453  1.00 88.36  ?  399  PRO A CA  1 
ATOM   2711  C C   . PRO A  1  399 ? -52.674 19.147  52.102  1.00 88.69  ?  399  PRO A C   1 
ATOM   2712  O O   . PRO A  1  399 ? -51.644 18.875  52.725  1.00 89.19  ?  399  PRO A O   1 
ATOM   2713  C CB  . PRO A  1  399 ? -54.765 19.384  53.476  1.00 87.74  ?  399  PRO A CB  1 
ATOM   2714  C CG  . PRO A  1  399 ? -54.757 18.636  54.742  1.00 87.94  ?  399  PRO A CG  1 
ATOM   2715  C CD  . PRO A  1  399 ? -54.309 17.235  54.521  1.00 88.79  ?  399  PRO A CD  1 
ATOM   2716  N N   . ASP A  1  400 ? -52.704 20.010  51.082  1.00 91.92  ?  400  ASP A N   1 
ATOM   2717  C CA  . ASP A  1  400 ? -51.495 20.692  50.632  1.00 92.48  ?  400  ASP A CA  1 
ATOM   2718  C C   . ASP A  1  400 ? -51.031 21.782  51.589  1.00 92.41  ?  400  ASP A C   1 
ATOM   2719  O O   . ASP A  1  400 ? -49.930 22.313  51.404  1.00 93.16  ?  400  ASP A O   1 
ATOM   2720  C CB  . ASP A  1  400 ? -51.715 21.296  49.246  1.00 93.17  ?  400  ASP A CB  1 
ATOM   2721  C CG  . ASP A  1  400 ? -51.875 20.242  48.171  1.00 94.04  ?  400  ASP A CG  1 
ATOM   2722  O OD1 . ASP A  1  400 ? -50.852 19.820  47.588  1.00 93.98  -1 400  ASP A OD1 1 
ATOM   2723  O OD2 . ASP A  1  400 ? -53.026 19.831  47.913  1.00 95.03  ?  400  ASP A OD2 1 
ATOM   2724  N N   . THR A  1  401 ? -51.835 22.130  52.593  1.00 86.87  ?  401  THR A N   1 
ATOM   2725  C CA  . THR A  1  401 ? -51.477 23.103  53.618  1.00 86.62  ?  401  THR A CA  1 
ATOM   2726  C C   . THR A  1  401 ? -50.650 22.500  54.751  1.00 87.03  ?  401  THR A C   1 
ATOM   2727  O O   . THR A  1  401 ? -50.460 23.167  55.773  1.00 86.67  ?  401  THR A O   1 
ATOM   2728  C CB  . THR A  1  401 ? -52.745 23.738  54.195  1.00 85.53  ?  401  THR A CB  1 
ATOM   2729  O OG1 . THR A  1  401 ? -53.579 22.714  54.751  1.00 85.31  ?  401  THR A OG1 1 
ATOM   2730  C CG2 . THR A  1  401 ? -53.515 24.459  53.109  1.00 86.38  ?  401  THR A CG2 1 
ATOM   2731  N N   . ILE A  1  402 ? -50.125 21.285  54.570  1.00 84.10  ?  402  ILE A N   1 
ATOM   2732  C CA  . ILE A  1  402 ? -49.687 20.467  55.700  1.00 84.23  ?  402  ILE A CA  1 
ATOM   2733  C C   . ILE A  1  402 ? -48.582 21.157  56.496  1.00 84.58  ?  402  ILE A C   1 
ATOM   2734  O O   . ILE A  1  402 ? -48.542 21.063  57.728  1.00 84.07  ?  402  ILE A O   1 
ATOM   2735  C CB  . ILE A  1  402 ? -49.255 19.073  55.206  1.00 84.95  ?  402  ILE A CB  1 
ATOM   2736  C CG1 . ILE A  1  402 ? -48.815 18.201  56.385  1.00 85.02  ?  402  ILE A CG1 1 
ATOM   2737  C CG2 . ILE A  1  402 ? -48.173 19.186  54.132  1.00 85.98  ?  402  ILE A CG2 1 
ATOM   2738  C CD1 . ILE A  1  402 ? -49.949 17.821  57.298  1.00 84.34  ?  402  ILE A CD1 1 
ATOM   2739  N N   . CYS A  1  403 ? -47.660 21.838  55.820  1.00 79.26  ?  403  CYS A N   1 
ATOM   2740  C CA  . CYS A  1  403 ? -46.569 22.548  56.488  1.00 80.04  ?  403  CYS A CA  1 
ATOM   2741  C C   . CYS A  1  403 ? -46.428 23.951  55.915  1.00 80.36  ?  403  CYS A C   1 
ATOM   2742  O O   . CYS A  1  403 ? -45.336 24.406  55.572  1.00 81.86  ?  403  CYS A O   1 
ATOM   2743  C CB  . CYS A  1  403 ? -45.245 21.790  56.402  1.00 81.71  ?  403  CYS A CB  1 
ATOM   2744  S SG  . CYS A  1  403 ? -43.959 22.444  57.525  1.00 82.98  ?  403  CYS A SG  1 
ATOM   2745  N N   . ARG A  1  404 ? -47.558 24.647  55.789  1.00 82.85  ?  404  ARG A N   1 
ATOM   2746  C CA  . ARG A  1  404 ? -47.569 25.953  55.137  1.00 82.86  ?  404  ARG A CA  1 
ATOM   2747  C C   . ARG A  1  404 ? -46.627 26.941  55.819  1.00 83.49  ?  404  ARG A C   1 
ATOM   2748  O O   . ARG A  1  404 ? -45.883 27.664  55.146  1.00 84.51  ?  404  ARG A O   1 
ATOM   2749  C CB  . ARG A  1  404 ? -48.994 26.500  55.121  1.00 81.24  ?  404  ARG A CB  1 
ATOM   2750  C CG  . ARG A  1  404 ? -49.144 27.796  54.358  1.00 81.16  ?  404  ARG A CG  1 
ATOM   2751  C CD  . ARG A  1  404 ? -50.604 28.152  54.147  1.00 80.80  ?  404  ARG A CD  1 
ATOM   2752  N NE  . ARG A  1  404 ? -51.163 28.888  55.273  1.00 80.10  ?  404  ARG A NE  1 
ATOM   2753  C CZ  . ARG A  1  404 ? -52.364 29.448  55.265  1.00 81.48  ?  404  ARG A CZ  1 
ATOM   2754  N NH1 . ARG A  1  404 ? -53.155 29.368  54.206  1.00 84.64  ?  404  ARG A NH1 1 
ATOM   2755  N NH2 . ARG A  1  404 ? -52.777 30.115  56.340  1.00 80.97  ?  404  ARG A NH2 1 
ATOM   2756  N N   . GLY A  1  405 ? -46.641 26.994  57.150  1.00 79.11  ?  405  GLY A N   1 
ATOM   2757  C CA  . GLY A  1  405 ? -45.808 27.953  57.856  1.00 79.61  ?  405  GLY A CA  1 
ATOM   2758  C C   . GLY A  1  405 ? -44.346 27.580  57.990  1.00 81.70  ?  405  GLY A C   1 
ATOM   2759  O O   . GLY A  1  405 ? -43.533 28.435  58.352  1.00 82.51  ?  405  GLY A O   1 
ATOM   2760  N N   . GLY A  1  406 ? -43.987 26.332  57.706  1.00 75.45  ?  406  GLY A N   1 
ATOM   2761  C CA  . GLY A  1  406 ? -42.609 25.918  57.872  1.00 77.72  ?  406  GLY A CA  1 
ATOM   2762  C C   . GLY A  1  406 ? -42.185 25.762  59.313  1.00 77.77  ?  406  GLY A C   1 
ATOM   2763  O O   . GLY A  1  406 ? -40.997 25.894  59.621  1.00 79.81  ?  406  GLY A O   1 
ATOM   2764  N N   . LYS A  1  407 ? -43.131 25.472  60.208  1.00 77.05  ?  407  LYS A N   1 
ATOM   2765  C CA  . LYS A  1  407 ? -42.834 25.300  61.621  1.00 76.56  ?  407  LYS A CA  1 
ATOM   2766  C C   . LYS A  1  407 ? -43.300 23.962  62.181  1.00 75.20  ?  407  LYS A C   1 
ATOM   2767  O O   . LYS A  1  407 ? -43.174 23.745  63.391  1.00 74.30  ?  407  LYS A O   1 
ATOM   2768  C CB  . LYS A  1  407 ? -43.466 26.434  62.439  1.00 74.76  ?  407  LYS A CB  1 
ATOM   2769  C CG  . LYS A  1  407 ? -43.241 27.812  61.847  1.00 75.35  ?  407  LYS A CG  1 
ATOM   2770  C CD  . LYS A  1  407 ? -43.519 28.902  62.865  1.00 73.90  ?  407  LYS A CD  1 
ATOM   2771  C CE  . LYS A  1  407 ? -43.611 30.271  62.207  1.00 73.78  ?  407  LYS A CE  1 
ATOM   2772  N NZ  . LYS A  1  407 ? -44.101 31.294  63.171  1.00 72.05  ?  407  LYS A NZ  1 
ATOM   2773  N N   . LEU A  1  408 ? -43.819 23.062  61.345  1.00 70.90  ?  408  LEU A N   1 
ATOM   2774  C CA  . LEU A  1  408 ? -44.375 21.806  61.833  1.00 69.45  ?  408  LEU A CA  1 
ATOM   2775  C C   . LEU A  1  408 ? -43.253 20.899  62.319  1.00 70.35  ?  408  LEU A C   1 
ATOM   2776  O O   . LEU A  1  408 ? -42.344 20.557  61.555  1.00 72.44  ?  408  LEU A O   1 
ATOM   2777  C CB  . LEU A  1  408 ? -45.186 21.120  60.735  1.00 69.26  ?  408  LEU A CB  1 
ATOM   2778  C CG  . LEU A  1  408 ? -46.036 19.922  61.174  1.00 67.98  ?  408  LEU A CG  1 
ATOM   2779  C CD1 . LEU A  1  408 ? -47.239 20.381  61.981  1.00 66.44  ?  408  LEU A CD1 1 
ATOM   2780  C CD2 . LEU A  1  408 ? -46.479 19.093  59.976  1.00 68.56  ?  408  LEU A CD2 1 
ATOM   2781  N N   . GLU A  1  409 ? -43.314 20.519  63.594  1.00 64.88  ?  409  GLU A N   1 
ATOM   2782  C CA  . GLU A  1  409 ? -42.311 19.659  64.204  1.00 65.20  ?  409  GLU A CA  1 
ATOM   2783  C C   . GLU A  1  409 ? -42.731 18.196  64.236  1.00 63.77  ?  409  GLU A C   1 
ATOM   2784  O O   . GLU A  1  409 ? -41.990 17.328  63.768  1.00 64.68  ?  409  GLU A O   1 
ATOM   2785  C CB  . GLU A  1  409 ? -42.004 20.133  65.625  1.00 64.32  ?  409  GLU A CB  1 
ATOM   2786  C CG  . GLU A  1  409 ? -41.744 21.612  65.743  1.00 65.59  ?  409  GLU A CG  1 
ATOM   2787  C CD  . GLU A  1  409 ? -40.965 21.959  66.995  1.00 65.82  ?  409  GLU A CD  1 
ATOM   2788  O OE1 . GLU A  1  409 ? -41.024 21.180  67.971  1.00 64.16  ?  409  GLU A OE1 1 
ATOM   2789  O OE2 . GLU A  1  409 ? -40.304 23.019  67.011  1.00 67.61  -1 409  GLU A OE2 1 
ATOM   2790  N N   . ASN A  1  410 ? -43.908 17.903  64.779  1.00 61.67  ?  410  ASN A N   1 
ATOM   2791  C CA  . ASN A  1  410 ? -44.334 16.534  65.028  1.00 60.86  ?  410  ASN A CA  1 
ATOM   2792  C C   . ASN A  1  410 ? -45.652 16.270  64.315  1.00 61.45  ?  410  ASN A C   1 
ATOM   2793  O O   . ASN A  1  410 ? -46.591 17.066  64.419  1.00 61.06  ?  410  ASN A O   1 
ATOM   2794  C CB  . ASN A  1  410 ? -44.446 16.289  66.534  1.00 58.93  ?  410  ASN A CB  1 
ATOM   2795  C CG  . ASN A  1  410 ? -43.177 16.681  67.266  1.00 58.59  ?  410  ASN A CG  1 
ATOM   2796  O OD1 . ASN A  1  410 ? -42.085 16.526  66.727  1.00 59.99  ?  410  ASN A OD1 1 
ATOM   2797  N ND2 . ASN A  1  410 ? -43.305 17.197  68.487  1.00 57.29  ?  410  ASN A ND2 1 
ATOM   2798  N N   . LEU A  1  411 ? -45.711 15.162  63.580  1.00 60.00  ?  411  LEU A N   1 
ATOM   2799  C CA  . LEU A  1  411 ? -46.893 14.790  62.815  1.00 61.41  ?  411  LEU A CA  1 
ATOM   2800  C C   . LEU A  1  411 ? -47.116 13.295  62.956  1.00 61.40  ?  411  LEU A C   1 
ATOM   2801  O O   . LEU A  1  411 ? -46.211 12.503  62.684  1.00 61.55  ?  411  LEU A O   1 
ATOM   2802  C CB  . LEU A  1  411 ? -46.742 15.162  61.339  1.00 63.10  ?  411  LEU A CB  1 
ATOM   2803  C CG  . LEU A  1  411 ? -47.814 14.615  60.397  1.00 64.93  ?  411  LEU A CG  1 
ATOM   2804  C CD1 . LEU A  1  411 ? -49.167 15.220  60.713  1.00 65.84  ?  411  LEU A CD1 1 
ATOM   2805  C CD2 . LEU A  1  411 ? -47.434 14.871  58.951  1.00 66.59  ?  411  LEU A CD2 1 
ATOM   2806  N N   . THR A  1  412 ? -48.313 12.913  63.390  1.00 70.73  ?  412  THR A N   1 
ATOM   2807  C CA  . THR A  1  412 ? -48.618 11.521  63.687  1.00 71.32  ?  412  THR A CA  1 
ATOM   2808  C C   . THR A  1  412 ? -49.909 11.116  62.984  1.00 71.70  ?  412  THR A C   1 
ATOM   2809  O O   . THR A  1  412 ? -50.930 11.799  63.117  1.00 71.86  ?  412  THR A O   1 
ATOM   2810  C CB  . THR A  1  412 ? -48.726 11.326  65.202  1.00 70.72  ?  412  THR A CB  1 
ATOM   2811  O OG1 . THR A  1  412 ? -47.410 11.238  65.762  1.00 68.96  ?  412  THR A OG1 1 
ATOM   2812  C CG2 . THR A  1  412 ? -49.441 10.061  65.509  1.00 70.06  ?  412  THR A CG2 1 
ATOM   2813  N N   . LEU A  1  413 ? -49.864 9.995   62.241  1.00 71.16  ?  413  LEU A N   1 
ATOM   2814  C CA  . LEU A  1  413 ? -51.020 9.536   61.477  1.00 71.53  ?  413  LEU A CA  1 
ATOM   2815  C C   . LEU A  1  413 ? -51.264 8.033   61.618  1.00 71.34  ?  413  LEU A C   1 
ATOM   2816  O O   . LEU A  1  413 ? -51.944 7.447   60.767  1.00 71.64  ?  413  LEU A O   1 
ATOM   2817  C CB  . LEU A  1  413 ? -50.855 9.880   59.992  1.00 71.66  ?  413  LEU A CB  1 
ATOM   2818  C CG  . LEU A  1  413 ? -50.540 11.330  59.619  1.00 71.46  ?  413  LEU A CG  1 
ATOM   2819  C CD1 . LEU A  1  413 ? -49.703 11.376  58.354  1.00 71.33  ?  413  LEU A CD1 1 
ATOM   2820  C CD2 . LEU A  1  413 ? -51.823 12.123  59.447  1.00 71.42  ?  413  LEU A CD2 1 
ATOM   2821  N N   . ASP A  1  414 ? -50.750 7.403   62.673  1.00 74.68  ?  414  ASP A N   1 
ATOM   2822  C CA  . ASP A  1  414 ? -50.728 5.947   62.764  1.00 74.33  ?  414  ASP A CA  1 
ATOM   2823  C C   . ASP A  1  414 ? -52.125 5.343   62.693  1.00 74.93  ?  414  ASP A C   1 
ATOM   2824  O O   . ASP A  1  414 ? -53.092 5.908   63.208  1.00 75.26  ?  414  ASP A O   1 
ATOM   2825  C CB  . ASP A  1  414 ? -50.056 5.506   64.065  1.00 73.23  ?  414  ASP A CB  1 
ATOM   2826  C CG  . ASP A  1  414 ? -48.626 5.971   64.168  1.00 72.29  ?  414  ASP A CG  1 
ATOM   2827  O OD1 . ASP A  1  414 ? -48.172 6.670   63.240  1.00 72.78  ?  414  ASP A OD1 1 
ATOM   2828  O OD2 . ASP A  1  414 ? -47.961 5.649   65.176  1.00 70.99  -1 414  ASP A OD2 1 
ATOM   2829  N N   . ASP A  1  415 ? -52.218 4.179   62.042  1.00 79.60  ?  415  ASP A N   1 
ATOM   2830  C CA  . ASP A  1  415 ? -53.385 3.295   62.122  1.00 79.94  ?  415  ASP A CA  1 
ATOM   2831  C C   . ASP A  1  415 ? -54.675 3.992   61.678  1.00 80.44  ?  415  ASP A C   1 
ATOM   2832  O O   . ASP A  1  415 ? -55.624 4.170   62.445  1.00 80.53  ?  415  ASP A O   1 
ATOM   2833  C CB  . ASP A  1  415 ? -53.523 2.720   63.536  1.00 79.52  ?  415  ASP A CB  1 
ATOM   2834  C CG  . ASP A  1  415 ? -52.316 1.895   63.949  1.00 78.96  ?  415  ASP A CG  1 
ATOM   2835  O OD1 . ASP A  1  415 ? -51.964 0.942   63.217  1.00 79.20  ?  415  ASP A OD1 1 
ATOM   2836  O OD2 . ASP A  1  415 ? -51.717 2.204   65.003  1.00 78.25  -1 415  ASP A OD2 1 
ATOM   2837  N N   . ASN A  1  416 ? -54.689 4.384   60.407  1.00 80.90  ?  416  ASN A N   1 
ATOM   2838  C CA  . ASN A  1  416 ? -55.823 5.060   59.789  1.00 81.16  ?  416  ASN A CA  1 
ATOM   2839  C C   . ASN A  1  416 ? -55.984 4.493   58.385  1.00 81.21  ?  416  ASN A C   1 
ATOM   2840  O O   . ASN A  1  416 ? -55.401 3.459   58.044  1.00 81.18  ?  416  ASN A O   1 
ATOM   2841  C CB  . ASN A  1  416 ? -55.615 6.580   59.782  1.00 81.18  ?  416  ASN A CB  1 
ATOM   2842  C CG  . ASN A  1  416 ? -56.131 7.243   61.038  1.00 81.28  ?  416  ASN A CG  1 
ATOM   2843  O OD1 . ASN A  1  416 ? -57.305 7.601   61.128  1.00 81.45  ?  416  ASN A OD1 1 
ATOM   2844  N ND2 . ASN A  1  416 ? -55.253 7.410   62.020  1.00 81.09  ?  416  ASN A ND2 1 
ATOM   2845  N N   . HIS A  1  417 ? -56.799 5.152   57.569  1.00 87.06  ?  417  HIS A N   1 
ATOM   2846  C CA  . HIS A  1  417 ? -57.023 4.729   56.191  1.00 87.00  ?  417  HIS A CA  1 
ATOM   2847  C C   . HIS A  1  417 ? -56.678 5.843   55.206  1.00 86.81  ?  417  HIS A C   1 
ATOM   2848  O O   . HIS A  1  417 ? -57.363 6.047   54.200  1.00 86.62  ?  417  HIS A O   1 
ATOM   2849  C CB  . HIS A  1  417 ? -58.459 4.249   55.998  1.00 86.97  ?  417  HIS A CB  1 
ATOM   2850  C CG  . HIS A  1  417 ? -58.871 3.186   56.969  1.00 87.06  ?  417  HIS A CG  1 
ATOM   2851  N ND1 . HIS A  1  417 ? -58.372 1.901   56.922  1.00 87.09  ?  417  HIS A ND1 1 
ATOM   2852  C CD2 . HIS A  1  417 ? -59.729 3.219   58.016  1.00 87.09  ?  417  HIS A CD2 1 
ATOM   2853  C CE1 . HIS A  1  417 ? -58.907 1.188   57.896  1.00 87.06  ?  417  HIS A CE1 1 
ATOM   2854  N NE2 . HIS A  1  417 ? -59.735 1.963   58.574  1.00 87.05  ?  417  HIS A NE2 1 
ATOM   2855  N N   . PHE A  1  418 ? -55.602 6.573   55.484  1.00 82.01  ?  418  PHE A N   1 
ATOM   2856  C CA  . PHE A  1  418 ? -55.097 7.550   54.533  1.00 81.77  ?  418  PHE A CA  1 
ATOM   2857  C C   . PHE A  1  418 ? -54.562 6.850   53.287  1.00 81.97  ?  418  PHE A C   1 
ATOM   2858  O O   . PHE A  1  418 ? -54.130 5.695   53.330  1.00 82.04  ?  418  PHE A O   1 
ATOM   2859  C CB  . PHE A  1  418 ? -53.987 8.391   55.163  1.00 81.60  ?  418  PHE A CB  1 
ATOM   2860  C CG  . PHE A  1  418 ? -54.476 9.403   56.159  1.00 81.51  ?  418  PHE A CG  1 
ATOM   2861  C CD1 . PHE A  1  418 ? -55.277 10.460  55.760  1.00 81.25  ?  418  PHE A CD1 1 
ATOM   2862  C CD2 . PHE A  1  418 ? -54.120 9.307   57.496  1.00 81.67  ?  418  PHE A CD2 1 
ATOM   2863  C CE1 . PHE A  1  418 ? -55.723 11.395  56.680  1.00 81.09  ?  418  PHE A CE1 1 
ATOM   2864  C CE2 . PHE A  1  418 ? -54.562 10.239  58.416  1.00 81.64  ?  418  PHE A CE2 1 
ATOM   2865  C CZ  . PHE A  1  418 ? -55.363 11.284  58.008  1.00 81.34  ?  418  PHE A CZ  1 
ATOM   2866  N N   . GLU A  1  419 ? -54.601 7.563   52.165  1.00 87.51  ?  419  GLU A N   1 
ATOM   2867  C CA  . GLU A  1  419 ? -54.057 7.060   50.913  1.00 87.48  ?  419  GLU A CA  1 
ATOM   2868  C C   . GLU A  1  419 ? -53.511 8.245   50.119  1.00 87.21  ?  419  GLU A C   1 
ATOM   2869  O O   . GLU A  1  419 ? -53.612 9.399   50.543  1.00 87.03  ?  419  GLU A O   1 
ATOM   2870  C CB  . GLU A  1  419 ? -55.121 6.262   50.146  1.00 87.44  ?  419  GLU A CB  1 
ATOM   2871  C CG  . GLU A  1  419 ? -55.841 7.059   49.085  1.00 87.26  ?  419  GLU A CG  1 
ATOM   2872  C CD  . GLU A  1  419 ? -57.052 6.365   48.496  1.00 90.21  ?  419  GLU A CD  1 
ATOM   2873  O OE1 . GLU A  1  419 ? -57.492 5.335   49.047  1.00 90.73  ?  419  GLU A OE1 1 
ATOM   2874  O OE2 . GLU A  1  419 ? -57.562 6.857   47.465  1.00 93.31  -1 419  GLU A OE2 1 
ATOM   2875  N N   . GLY A  1  420 ? -52.912 7.953   48.965  1.00 88.22  ?  420  GLY A N   1 
ATOM   2876  C CA  . GLY A  1  420 ? -52.388 8.984   48.102  1.00 88.00  ?  420  GLY A CA  1 
ATOM   2877  C C   . GLY A  1  420 ? -50.938 9.302   48.396  1.00 88.23  ?  420  GLY A C   1 
ATOM   2878  O O   . GLY A  1  420 ? -50.311 8.701   49.274  1.00 88.48  ?  420  GLY A O   1 
ATOM   2879  N N   . PRO A  1  421 ? -50.376 10.258  47.665  1.00 84.84  ?  421  PRO A N   1 
ATOM   2880  C CA  . PRO A  1  421 ? -48.957 10.580  47.810  1.00 85.11  ?  421  PRO A CA  1 
ATOM   2881  C C   . PRO A  1  421 ? -48.720 11.630  48.891  1.00 85.13  ?  421  PRO A C   1 
ATOM   2882  O O   . PRO A  1  421 ? -49.650 12.196  49.467  1.00 84.81  ?  421  PRO A O   1 
ATOM   2883  C CB  . PRO A  1  421 ? -48.596 11.134  46.428  1.00 85.22  ?  421  PRO A CB  1 
ATOM   2884  C CG  . PRO A  1  421 ? -49.846 11.817  45.990  1.00 84.87  ?  421  PRO A CG  1 
ATOM   2885  C CD  . PRO A  1  421 ? -51.007 11.039  46.587  1.00 84.85  ?  421  PRO A CD  1 
ATOM   2886  N N   . VAL A  1  422 ? -47.447 11.884  49.146  1.00 83.23  ?  422  VAL A N   1 
ATOM   2887  C CA  . VAL A  1  422 ? -47.066 12.885  50.142  1.00 83.38  ?  422  VAL A CA  1 
ATOM   2888  C C   . VAL A  1  422 ? -47.161 14.269  49.507  1.00 83.46  ?  422  VAL A C   1 
ATOM   2889  O O   . VAL A  1  422 ? -46.650 14.467  48.392  1.00 83.84  ?  422  VAL A O   1 
ATOM   2890  C CB  . VAL A  1  422 ? -45.661 12.611  50.664  1.00 83.95  ?  422  VAL A CB  1 
ATOM   2891  C CG1 . VAL A  1  422 ? -45.455 13.277  52.018  1.00 84.00  ?  422  VAL A CG1 1 
ATOM   2892  C CG2 . VAL A  1  422 ? -45.446 11.117  50.776  1.00 83.79  ?  422  VAL A CG2 1 
ATOM   2893  N N   . PRO A  1  423 ? -47.818 15.229  50.155  1.00 87.61  ?  423  PRO A N   1 
ATOM   2894  C CA  . PRO A  1  423 ? -47.913 16.576  49.584  1.00 87.61  ?  423  PRO A CA  1 
ATOM   2895  C C   . PRO A  1  423 ? -46.551 17.247  49.504  1.00 88.66  ?  423  PRO A C   1 
ATOM   2896  O O   . PRO A  1  423 ? -45.615 16.923  50.238  1.00 89.32  ?  423  PRO A O   1 
ATOM   2897  C CB  . PRO A  1  423 ? -48.836 17.318  50.559  1.00 86.89  ?  423  PRO A CB  1 
ATOM   2898  C CG  . PRO A  1  423 ? -49.547 16.244  51.312  1.00 86.51  ?  423  PRO A CG  1 
ATOM   2899  C CD  . PRO A  1  423 ? -48.577 15.108  51.409  1.00 87.10  ?  423  PRO A CD  1 
ATOM   2900  N N   . LYS A  1  424 ? -46.461 18.216  48.593  1.00 88.88  ?  424  LYS A N   1 
ATOM   2901  C CA  . LYS A  1  424 ? -45.176 18.848  48.317  1.00 90.18  ?  424  LYS A CA  1 
ATOM   2902  C C   . LYS A  1  424 ? -44.735 19.731  49.477  1.00 90.70  ?  424  LYS A C   1 
ATOM   2903  O O   . LYS A  1  424 ? -43.531 19.874  49.726  1.00 92.08  ?  424  LYS A O   1 
ATOM   2904  C CB  . LYS A  1  424 ? -45.250 19.656  47.018  1.00 90.26  ?  424  LYS A CB  1 
ATOM   2905  C CG  . LYS A  1  424 ? -45.946 18.961  45.825  1.00 89.56  ?  424  LYS A CG  1 
ATOM   2906  C CD  . LYS A  1  424 ? -45.868 17.422  45.850  1.00 89.13  ?  424  LYS A CD  1 
ATOM   2907  C CE  . LYS A  1  424 ? -45.736 16.796  44.464  1.00 89.13  ?  424  LYS A CE  1 
ATOM   2908  N NZ  . LYS A  1  424 ? -45.758 15.301  44.557  1.00 88.77  ?  424  LYS A NZ  1 
ATOM   2909  N N   . SER A  1  425 ? -45.696 20.318  50.197  1.00 87.19  ?  425  SER A N   1 
ATOM   2910  C CA  . SER A  1  425 ? -45.374 21.125  51.370  1.00 87.43  ?  425  SER A CA  1 
ATOM   2911  C C   . SER A  1  425 ? -44.711 20.298  52.463  1.00 87.94  ?  425  SER A C   1 
ATOM   2912  O O   . SER A  1  425 ? -43.906 20.828  53.237  1.00 88.87  ?  425  SER A O   1 
ATOM   2913  C CB  . SER A  1  425 ? -46.640 21.789  51.913  1.00 85.90  ?  425  SER A CB  1 
ATOM   2914  O OG  . SER A  1  425 ? -47.518 22.146  50.857  1.00 85.15  ?  425  SER A OG  1 
ATOM   2915  N N   . LEU A  1  426 ? -45.049 19.008  52.559  1.00 83.13  ?  426  LEU A N   1 
ATOM   2916  C CA  . LEU A  1  426 ? -44.413 18.146  53.549  1.00 83.45  ?  426  LEU A CA  1 
ATOM   2917  C C   . LEU A  1  426 ? -43.029 17.688  53.106  1.00 84.98  ?  426  LEU A C   1 
ATOM   2918  O O   . LEU A  1  426 ? -42.167 17.432  53.954  1.00 85.75  ?  426  LEU A O   1 
ATOM   2919  C CB  . LEU A  1  426 ? -45.293 16.929  53.841  1.00 82.27  ?  426  LEU A CB  1 
ATOM   2920  C CG  . LEU A  1  426 ? -44.980 16.144  55.119  1.00 82.07  ?  426  LEU A CG  1 
ATOM   2921  C CD1 . LEU A  1  426 ? -44.475 17.059  56.226  1.00 82.27  ?  426  LEU A CD1 1 
ATOM   2922  C CD2 . LEU A  1  426 ? -46.203 15.379  55.580  1.00 81.01  ?  426  LEU A CD2 1 
ATOM   2923  N N   . ARG A  1  427 ? -42.803 17.564  51.795  1.00 82.43  ?  427  ARG A N   1 
ATOM   2924  C CA  . ARG A  1  427 ? -41.472 17.221  51.308  1.00 83.78  ?  427  ARG A CA  1 
ATOM   2925  C C   . ARG A  1  427 ? -40.473 18.328  51.617  1.00 85.42  ?  427  ARG A C   1 
ATOM   2926  O O   . ARG A  1  427 ? -39.349 18.057  52.055  1.00 86.44  ?  427  ARG A O   1 
ATOM   2927  C CB  . ARG A  1  427 ? -41.520 16.938  49.808  1.00 83.65  ?  427  ARG A CB  1 
ATOM   2928  C CG  . ARG A  1  427 ? -40.154 16.907  49.138  1.00 85.06  ?  427  ARG A CG  1 
ATOM   2929  C CD  . ARG A  1  427 ? -40.274 16.760  47.632  1.00 84.86  ?  427  ARG A CD  1 
ATOM   2930  N NE  . ARG A  1  427 ? -40.122 18.043  46.956  1.00 85.61  ?  427  ARG A NE  1 
ATOM   2931  C CZ  . ARG A  1  427 ? -40.844 18.426  45.912  1.00 84.97  ?  427  ARG A CZ  1 
ATOM   2932  N NH1 . ARG A  1  427 ? -41.770 17.640  45.387  1.00 83.73  ?  427  ARG A NH1 1 
ATOM   2933  N NH2 . ARG A  1  427 ? -40.623 19.623  45.375  1.00 85.55  ?  427  ARG A NH2 1 
ATOM   2934  N N   . ASP A  1  428 ? -40.872 19.580  51.417  1.00 84.28  ?  428  ASP A N   1 
ATOM   2935  C CA  . ASP A  1  428 ? -39.992 20.723  51.614  1.00 85.73  ?  428  ASP A CA  1 
ATOM   2936  C C   . ASP A  1  428 ? -40.018 21.260  53.041  1.00 85.93  ?  428  ASP A C   1 
ATOM   2937  O O   . ASP A  1  428 ? -39.363 22.272  53.314  1.00 86.98  ?  428  ASP A O   1 
ATOM   2938  C CB  . ASP A  1  428 ? -40.362 21.840  50.634  1.00 85.50  ?  428  ASP A CB  1 
ATOM   2939  C CG  . ASP A  1  428 ? -40.609 21.326  49.219  1.00 85.02  ?  428  ASP A CG  1 
ATOM   2940  O OD1 . ASP A  1  428 ? -40.014 20.298  48.830  1.00 85.42  ?  428  ASP A OD1 1 
ATOM   2941  O OD2 . ASP A  1  428 ? -41.406 21.953  48.491  1.00 84.12  -1 428  ASP A OD2 1 
ATOM   2942  N N   . CYS A  1  429 ? -40.756 20.618  53.949  1.00 81.41  ?  429  CYS A N   1 
ATOM   2943  C CA  . CYS A  1  429 ? -40.879 21.067  55.335  1.00 81.27  ?  429  CYS A CA  1 
ATOM   2944  C C   . CYS A  1  429 ? -39.658 20.604  56.123  1.00 82.85  ?  429  CYS A C   1 
ATOM   2945  O O   . CYS A  1  429 ? -39.522 19.415  56.426  1.00 82.31  ?  429  CYS A O   1 
ATOM   2946  C CB  . CYS A  1  429 ? -42.173 20.520  55.935  1.00 78.91  ?  429  CYS A CB  1 
ATOM   2947  S SG  . CYS A  1  429 ? -42.534 20.987  57.646  1.00 77.66  ?  429  CYS A SG  1 
ATOM   2948  N N   . LYS A  1  430 ? -38.779 21.542  56.478  1.00 76.74  ?  430  LYS A N   1 
ATOM   2949  C CA  . LYS A  1  430 ? -37.472 21.222  57.044  1.00 77.41  ?  430  LYS A CA  1 
ATOM   2950  C C   . LYS A  1  430 ? -37.451 21.193  58.569  1.00 76.83  ?  430  LYS A C   1 
ATOM   2951  O O   . LYS A  1  430 ? -36.408 20.878  59.152  1.00 76.75  ?  430  LYS A O   1 
ATOM   2952  C CB  . LYS A  1  430 ? -36.420 22.219  56.540  1.00 78.69  ?  430  LYS A CB  1 
ATOM   2953  C CG  . LYS A  1  430 ? -36.510 22.515  55.054  1.00 78.99  ?  430  LYS A CG  1 
ATOM   2954  C CD  . LYS A  1  430 ? -35.378 23.427  54.600  1.00 80.08  ?  430  LYS A CD  1 
ATOM   2955  C CE  . LYS A  1  430 ? -34.503 22.754  53.537  1.00 80.51  ?  430  LYS A CE  1 
ATOM   2956  N NZ  . LYS A  1  430 ? -33.667 23.724  52.753  1.00 81.42  ?  430  LYS A NZ  1 
ATOM   2957  N N   . SER A  1  431 ? -38.561 21.502  59.232  1.00 75.23  ?  431  SER A N   1 
ATOM   2958  C CA  . SER A  1  431 ? -38.594 21.566  60.687  1.00 74.15  ?  431  SER A CA  1 
ATOM   2959  C C   . SER A  1  431 ? -39.065 20.265  61.335  1.00 72.12  ?  431  SER A C   1 
ATOM   2960  O O   . SER A  1  431 ? -39.251 20.231  62.556  1.00 70.64  ?  431  SER A O   1 
ATOM   2961  C CB  . SER A  1  431 ? -39.484 22.726  61.150  1.00 73.46  ?  431  SER A CB  1 
ATOM   2962  O OG  . SER A  1  431 ? -40.816 22.576  60.688  1.00 71.10  ?  431  SER A OG  1 
ATOM   2963  N N   . LEU A  1  432 ? -39.242 19.197  60.558  1.00 70.92  ?  432  LEU A N   1 
ATOM   2964  C CA  . LEU A  1  432 ? -39.787 17.960  61.100  1.00 68.85  ?  432  LEU A CA  1 
ATOM   2965  C C   . LEU A  1  432 ? -38.850 17.354  62.140  1.00 67.68  ?  432  LEU A C   1 
ATOM   2966  O O   . LEU A  1  432 ? -37.624 17.396  61.999  1.00 68.57  ?  432  LEU A O   1 
ATOM   2967  C CB  . LEU A  1  432 ? -40.035 16.956  59.976  1.00 68.66  ?  432  LEU A CB  1 
ATOM   2968  C CG  . LEU A  1  432 ? -41.172 17.309  59.022  1.00 68.38  ?  432  LEU A CG  1 
ATOM   2969  C CD1 . LEU A  1  432 ? -41.243 16.293  57.904  1.00 68.53  ?  432  LEU A CD1 1 
ATOM   2970  C CD2 . LEU A  1  432 ? -42.489 17.382  59.768  1.00 65.96  ?  432  LEU A CD2 1 
ATOM   2971  N N   . ILE A  1  433 ? -39.443 16.805  63.202  1.00 64.60  ?  433  ILE A N   1 
ATOM   2972  C CA  . ILE A  1  433 ? -38.710 16.136  64.274  1.00 63.08  ?  433  ILE A CA  1 
ATOM   2973  C C   . ILE A  1  433 ? -39.190 14.694  64.390  1.00 60.92  ?  433  ILE A C   1 
ATOM   2974  O O   . ILE A  1  433 ? -38.395 13.754  64.281  1.00 60.58  ?  433  ILE A O   1 
ATOM   2975  C CB  . ILE A  1  433 ? -38.867 16.883  65.610  1.00 62.16  ?  433  ILE A CB  1 
ATOM   2976  C CG1 . ILE A  1  433 ? -38.381 18.322  65.465  1.00 64.58  ?  433  ILE A CG1 1 
ATOM   2977  C CG2 . ILE A  1  433 ? -38.099 16.177  66.716  1.00 60.87  ?  433  ILE A CG2 1 
ATOM   2978  C CD1 . ILE A  1  433 ? -38.319 19.067  66.768  1.00 64.13  ?  433  ILE A CD1 1 
ATOM   2979  N N   . ARG A  1  434 ? -40.485 14.511  64.639  1.00 63.10  ?  434  ARG A N   1 
ATOM   2980  C CA  . ARG A  1  434 ? -41.106 13.193  64.654  1.00 61.89  ?  434  ARG A CA  1 
ATOM   2981  C C   . ARG A  1  434 ? -42.154 13.117  63.554  1.00 63.42  ?  434  ARG A C   1 
ATOM   2982  O O   . ARG A  1  434 ? -43.044 13.969  63.480  1.00 63.62  ?  434  ARG A O   1 
ATOM   2983  C CB  . ARG A  1  434 ? -41.747 12.892  66.011  1.00 59.62  ?  434  ARG A CB  1 
ATOM   2984  C CG  . ARG A  1  434 ? -40.821 12.201  66.997  1.00 58.05  ?  434  ARG A CG  1 
ATOM   2985  C CD  . ARG A  1  434 ? -41.546 11.872  68.288  1.00 56.06  ?  434  ARG A CD  1 
ATOM   2986  N NE  . ARG A  1  434 ? -42.262 10.604  68.219  1.00 55.79  ?  434  ARG A NE  1 
ATOM   2987  C CZ  . ARG A  1  434 ? -41.785 9.451   68.671  1.00 54.85  ?  434  ARG A CZ  1 
ATOM   2988  N NH1 . ARG A  1  434 ? -40.575 9.362   69.199  1.00 54.18  ?  434  ARG A NH1 1 
ATOM   2989  N NH2 . ARG A  1  434 ? -42.544 8.361   68.598  1.00 55.00  ?  434  ARG A NH2 1 
ATOM   2990  N N   . VAL A  1  435 ? -42.043 12.097  62.705  1.00 63.51  ?  435  VAL A N   1 
ATOM   2991  C CA  . VAL A  1  435 ? -42.984 11.840  61.620  1.00 65.16  ?  435  VAL A CA  1 
ATOM   2992  C C   . VAL A  1  435 ? -43.413 10.383  61.723  1.00 64.32  ?  435  VAL A C   1 
ATOM   2993  O O   . VAL A  1  435 ? -42.572 9.480   61.652  1.00 63.31  ?  435  VAL A O   1 
ATOM   2994  C CB  . VAL A  1  435 ? -42.374 12.137  60.237  1.00 66.26  ?  435  VAL A CB  1 
ATOM   2995  C CG1 . VAL A  1  435 ? -43.463 12.279  59.184  1.00 66.55  ?  435  VAL A CG1 1 
ATOM   2996  C CG2 . VAL A  1  435 ? -41.542 13.406  60.285  1.00 66.86  ?  435  VAL A CG2 1 
ATOM   2997  N N   . ARG A  1  436 ? -44.712 10.151  61.906  1.00 69.61  ?  436  ARG A N   1 
ATOM   2998  C CA  . ARG A  1  436 ? -45.257 8.808   62.081  1.00 68.72  ?  436  ARG A CA  1 
ATOM   2999  C C   . ARG A  1  436 ? -46.342 8.580   61.037  1.00 69.67  ?  436  ARG A C   1 
ATOM   3000  O O   . ARG A  1  436 ? -47.413 9.192   61.106  1.00 70.24  ?  436  ARG A O   1 
ATOM   3001  C CB  . ARG A  1  436 ? -45.806 8.626   63.493  1.00 67.69  ?  436  ARG A CB  1 
ATOM   3002  C CG  . ARG A  1  436 ? -44.754 8.710   64.576  1.00 65.88  ?  436  ARG A CG  1 
ATOM   3003  C CD  . ARG A  1  436 ? -45.124 7.861   65.773  1.00 64.36  ?  436  ARG A CD  1 
ATOM   3004  N NE  . ARG A  1  436 ? -45.333 6.468   65.402  1.00 64.54  ?  436  ARG A NE  1 
ATOM   3005  C CZ  . ARG A  1  436 ? -44.773 5.438   66.020  1.00 63.35  ?  436  ARG A CZ  1 
ATOM   3006  N NH1 . ARG A  1  436 ? -43.952 5.611   67.044  1.00 61.68  ?  436  ARG A NH1 1 
ATOM   3007  N NH2 . ARG A  1  436 ? -45.036 4.204   65.597  1.00 63.96  ?  436  ARG A NH2 1 
ATOM   3008  N N   . PHE A  1  437 ? -46.067 7.692   60.082  1.00 70.58  ?  437  PHE A N   1 
ATOM   3009  C CA  . PHE A  1  437 ? -46.995 7.359   59.008  1.00 71.21  ?  437  PHE A CA  1 
ATOM   3010  C C   . PHE A  1  437 ? -47.514 5.930   59.121  1.00 71.02  ?  437  PHE A C   1 
ATOM   3011  O O   . PHE A  1  437 ? -48.248 5.475   58.236  1.00 71.51  ?  437  PHE A O   1 
ATOM   3012  C CB  . PHE A  1  437 ? -46.323 7.544   57.642  1.00 71.53  ?  437  PHE A CB  1 
ATOM   3013  C CG  . PHE A  1  437 ? -46.405 8.944   57.088  1.00 71.98  ?  437  PHE A CG  1 
ATOM   3014  C CD1 . PHE A  1  437 ? -46.397 10.047  57.921  1.00 72.02  ?  437  PHE A CD1 1 
ATOM   3015  C CD2 . PHE A  1  437 ? -46.480 9.149   55.717  1.00 72.25  ?  437  PHE A CD2 1 
ATOM   3016  C CE1 . PHE A  1  437 ? -46.461 11.329  57.396  1.00 72.22  ?  437  PHE A CE1 1 
ATOM   3017  C CE2 . PHE A  1  437 ? -46.550 10.425  55.190  1.00 72.45  ?  437  PHE A CE2 1 
ATOM   3018  C CZ  . PHE A  1  437 ? -46.542 11.515  56.029  1.00 72.40  ?  437  PHE A CZ  1 
ATOM   3019  N N   . LYS A  1  438 ? -47.163 5.225   60.197  1.00 71.12  ?  438  LYS A N   1 
ATOM   3020  C CA  . LYS A  1  438 ? -47.342 3.780   60.277  1.00 71.05  ?  438  LYS A CA  1 
ATOM   3021  C C   . LYS A  1  438 ? -48.794 3.371   60.054  1.00 71.83  ?  438  LYS A C   1 
ATOM   3022  O O   . LYS A  1  438 ? -49.723 4.031   60.525  1.00 72.04  ?  438  LYS A O   1 
ATOM   3023  C CB  . LYS A  1  438 ? -46.863 3.281   61.642  1.00 70.04  ?  438  LYS A CB  1 
ATOM   3024  C CG  . LYS A  1  438 ? -46.627 1.785   61.733  1.00 70.04  ?  438  LYS A CG  1 
ATOM   3025  C CD  . LYS A  1  438 ? -46.394 1.377   63.179  1.00 69.13  ?  438  LYS A CD  1 
ATOM   3026  C CE  . LYS A  1  438 ? -45.562 0.114   63.286  1.00 68.92  ?  438  LYS A CE  1 
ATOM   3027  N NZ  . LYS A  1  438 ? -46.312 -1.072  62.795  1.00 70.32  ?  438  LYS A NZ  1 
ATOM   3028  N N   . GLY A  1  439 ? -48.983 2.281   59.310  1.00 74.75  ?  439  GLY A N   1 
ATOM   3029  C CA  . GLY A  1  439 ? -50.299 1.692   59.138  1.00 75.34  ?  439  GLY A CA  1 
ATOM   3030  C C   . GLY A  1  439 ? -51.285 2.498   58.313  1.00 75.73  ?  439  GLY A C   1 
ATOM   3031  O O   . GLY A  1  439 ? -52.307 2.960   58.831  1.00 75.84  ?  439  GLY A O   1 
ATOM   3032  N N   . ASN A  1  440 ? -50.993 2.666   57.027  1.00 77.75  ?  440  ASN A N   1 
ATOM   3033  C CA  . ASN A  1  440 ? -51.865 3.389   56.109  1.00 77.98  ?  440  ASN A CA  1 
ATOM   3034  C C   . ASN A  1  440 ? -51.704 2.770   54.723  1.00 78.14  ?  440  ASN A C   1 
ATOM   3035  O O   . ASN A  1  440 ? -51.149 1.677   54.573  1.00 78.23  ?  440  ASN A O   1 
ATOM   3036  C CB  . ASN A  1  440 ? -51.543 4.892   56.113  1.00 77.83  ?  440  ASN A CB  1 
ATOM   3037  C CG  . ASN A  1  440 ? -52.153 5.627   57.301  1.00 77.81  ?  440  ASN A CG  1 
ATOM   3038  O OD1 . ASN A  1  440 ? -53.341 5.951   57.306  1.00 77.96  ?  440  ASN A OD1 1 
ATOM   3039  N ND2 . ASN A  1  440 ? -51.332 5.905   58.308  1.00 77.53  ?  440  ASN A ND2 1 
ATOM   3040  N N   . SER A  1  441 ? -52.205 3.464   53.706  1.00 82.64  ?  441  SER A N   1 
ATOM   3041  C CA  . SER A  1  441 ? -52.066 3.045   52.316  1.00 82.70  ?  441  SER A CA  1 
ATOM   3042  C C   . SER A  1  441 ? -51.392 4.129   51.485  1.00 82.53  ?  441  SER A C   1 
ATOM   3043  O O   . SER A  1  441 ? -51.732 4.348   50.320  1.00 82.46  ?  441  SER A O   1 
ATOM   3044  C CB  . SER A  1  441 ? -53.419 2.671   51.720  1.00 82.76  ?  441  SER A CB  1 
ATOM   3045  O OG  . SER A  1  441 ? -53.874 1.434   52.240  1.00 82.96  ?  441  SER A OG  1 
ATOM   3046  N N   . PHE A  1  442 ? -50.423 4.819   52.082  1.00 80.51  ?  442  PHE A N   1 
ATOM   3047  C CA  . PHE A  1  442 ? -49.674 5.839   51.363  1.00 80.39  ?  442  PHE A CA  1 
ATOM   3048  C C   . PHE A  1  442 ? -48.898 5.220   50.206  1.00 80.47  ?  442  PHE A C   1 
ATOM   3049  O O   . PHE A  1  442 ? -48.547 4.039   50.223  1.00 80.59  ?  442  PHE A O   1 
ATOM   3050  C CB  . PHE A  1  442 ? -48.712 6.555   52.306  1.00 80.29  ?  442  PHE A CB  1 
ATOM   3051  C CG  . PHE A  1  442 ? -49.385 7.474   53.275  1.00 80.22  ?  442  PHE A CG  1 
ATOM   3052  C CD1 . PHE A  1  442 ? -50.204 8.496   52.829  1.00 80.13  ?  442  PHE A CD1 1 
ATOM   3053  C CD2 . PHE A  1  442 ? -49.193 7.320   54.636  1.00 80.15  ?  442  PHE A CD2 1 
ATOM   3054  C CE1 . PHE A  1  442 ? -50.820 9.346   53.724  1.00 80.03  ?  442  PHE A CE1 1 
ATOM   3055  C CE2 . PHE A  1  442 ? -49.807 8.167   55.536  1.00 80.12  ?  442  PHE A CE2 1 
ATOM   3056  C CZ  . PHE A  1  442 ? -50.620 9.182   55.079  1.00 80.08  ?  442  PHE A CZ  1 
ATOM   3057  N N   . SER A  1  443 ? -48.617 6.038   49.197  1.00 79.57  ?  443  SER A N   1 
ATOM   3058  C CA  . SER A  1  443 ? -48.039 5.533   47.963  1.00 81.24  ?  443  SER A CA  1 
ATOM   3059  C C   . SER A  1  443 ? -47.109 6.580   47.369  1.00 80.17  ?  443  SER A C   1 
ATOM   3060  O O   . SER A  1  443 ? -47.002 7.705   47.866  1.00 78.63  ?  443  SER A O   1 
ATOM   3061  C CB  . SER A  1  443 ? -49.140 5.145   46.972  1.00 87.82  ?  443  SER A CB  1 
ATOM   3062  O OG  . SER A  1  443 ? -50.104 6.179   46.863  1.00 91.37  ?  443  SER A OG  1 
ATOM   3063  N N   . GLY A  1  444 ? -46.436 6.193   46.294  1.00 82.81  ?  444  GLY A N   1 
ATOM   3064  C CA  . GLY A  1  444 ? -45.542 7.068   45.566  1.00 82.80  ?  444  GLY A CA  1 
ATOM   3065  C C   . GLY A  1  444 ? -44.103 6.597   45.644  1.00 81.71  ?  444  GLY A C   1 
ATOM   3066  O O   . GLY A  1  444 ? -43.776 5.598   46.283  1.00 80.92  ?  444  GLY A O   1 
ATOM   3067  N N   . ASP A  1  445 ? -43.239 7.353   44.972  1.00 82.53  ?  445  ASP A N   1 
ATOM   3068  C CA  . ASP A  1  445 ? -41.816 7.046   44.939  1.00 82.30  ?  445  ASP A CA  1 
ATOM   3069  C C   . ASP A  1  445 ? -41.135 7.549   46.206  1.00 81.41  ?  445  ASP A C   1 
ATOM   3070  O O   . ASP A  1  445 ? -41.232 8.733   46.545  1.00 81.51  ?  445  ASP A O   1 
ATOM   3071  C CB  . ASP A  1  445 ? -41.170 7.675   43.709  1.00 83.51  ?  445  ASP A CB  1 
ATOM   3072  C CG  . ASP A  1  445 ? -39.784 7.148   43.457  1.00 83.73  ?  445  ASP A CG  1 
ATOM   3073  O OD1 . ASP A  1  445 ? -38.846 7.602   44.148  1.00 83.52  ?  445  ASP A OD1 1 
ATOM   3074  O OD2 . ASP A  1  445 ? -39.634 6.273   42.579  1.00 84.25  -1 445  ASP A OD2 1 
ATOM   3075  N N   . ILE A  1  446 ? -40.438 6.647   46.903  1.00 80.09  ?  446  ILE A N   1 
ATOM   3076  C CA  . ILE A  1  446 ? -39.888 6.999   48.210  1.00 79.18  ?  446  ILE A CA  1 
ATOM   3077  C C   . ILE A  1  446 ? -38.794 8.053   48.080  1.00 79.96  ?  446  ILE A C   1 
ATOM   3078  O O   . ILE A  1  446 ? -38.601 8.870   48.989  1.00 79.65  ?  446  ILE A O   1 
ATOM   3079  C CB  . ILE A  1  446 ? -39.390 5.734   48.941  1.00 78.02  ?  446  ILE A CB  1 
ATOM   3080  C CG1 . ILE A  1  446 ? -39.168 6.020   50.429  1.00 76.92  ?  446  ILE A CG1 1 
ATOM   3081  C CG2 . ILE A  1  446 ? -38.122 5.181   48.302  1.00 78.43  ?  446  ILE A CG2 1 
ATOM   3082  C CD1 . ILE A  1  446 ? -40.442 6.083   51.231  1.00 76.57  ?  446  ILE A CD1 1 
ATOM   3083  N N   . SER A  1  447 ? -38.075 8.073   46.956  1.00 83.61  ?  447  SER A N   1 
ATOM   3084  C CA  . SER A  1  447 ? -37.053 9.090   46.749  1.00 84.73  ?  447  SER A CA  1 
ATOM   3085  C C   . SER A  1  447 ? -37.636 10.412  46.268  1.00 85.39  ?  447  SER A C   1 
ATOM   3086  O O   . SER A  1  447 ? -36.971 11.447  46.388  1.00 86.03  ?  447  SER A O   1 
ATOM   3087  C CB  . SER A  1  447 ? -36.006 8.591   45.754  1.00 85.84  ?  447  SER A CB  1 
ATOM   3088  O OG  . SER A  1  447 ? -36.528 8.586   44.439  1.00 86.58  ?  447  SER A OG  1 
ATOM   3089  N N   . GLU A  1  448 ? -38.855 10.401  45.728  1.00 89.45  ?  448  GLU A N   1 
ATOM   3090  C CA  . GLU A  1  448 ? -39.533 11.625  45.322  1.00 89.91  ?  448  GLU A CA  1 
ATOM   3091  C C   . GLU A  1  448 ? -40.439 12.190  46.407  1.00 88.95  ?  448  GLU A C   1 
ATOM   3092  O O   . GLU A  1  448 ? -40.799 13.372  46.344  1.00 89.17  ?  448  GLU A O   1 
ATOM   3093  C CB  . GLU A  1  448 ? -40.366 11.374  44.061  1.00 90.55  ?  448  GLU A CB  1 
ATOM   3094  C CG  . GLU A  1  448 ? -39.907 12.138  42.831  1.00 91.86  ?  448  GLU A CG  1 
ATOM   3095  C CD  . GLU A  1  448 ? -40.559 11.614  41.565  1.00 93.46  ?  448  GLU A CD  1 
ATOM   3096  O OE1 . GLU A  1  448 ? -41.667 11.048  41.672  1.00 93.87  ?  448  GLU A OE1 1 
ATOM   3097  O OE2 . GLU A  1  448 ? -39.969 11.755  40.468  1.00 95.41  -1 448  GLU A OE2 1 
ATOM   3098  N N   . ALA A  1  449 ? -40.822 11.372  47.390  1.00 81.09  ?  449  ALA A N   1 
ATOM   3099  C CA  . ALA A  1  449 ? -41.770 11.802  48.411  1.00 80.27  ?  449  ALA A CA  1 
ATOM   3100  C C   . ALA A  1  449 ? -41.128 12.701  49.462  1.00 79.75  ?  449  ALA A C   1 
ATOM   3101  O O   . ALA A  1  449 ? -41.727 13.698  49.876  1.00 79.50  ?  449  ALA A O   1 
ATOM   3102  C CB  . ALA A  1  449 ? -42.397 10.579  49.078  1.00 79.54  ?  449  ALA A CB  1 
ATOM   3103  N N   . PHE A  1  450 ? -39.917 12.373  49.901  1.00 75.45  ?  450  PHE A N   1 
ATOM   3104  C CA  . PHE A  1  450 ? -39.298 13.016  51.052  1.00 74.89  ?  450  PHE A CA  1 
ATOM   3105  C C   . PHE A  1  450 ? -38.059 13.789  50.630  1.00 76.04  ?  450  PHE A C   1 
ATOM   3106  O O   . PHE A  1  450 ? -37.268 13.317  49.805  1.00 77.06  ?  450  PHE A O   1 
ATOM   3107  C CB  . PHE A  1  450 ? -38.934 11.981  52.118  1.00 73.83  ?  450  PHE A CB  1 
ATOM   3108  C CG  . PHE A  1  450 ? -40.112 11.218  52.635  1.00 72.91  ?  450  PHE A CG  1 
ATOM   3109  C CD1 . PHE A  1  450 ? -40.876 11.720  53.672  1.00 72.15  ?  450  PHE A CD1 1 
ATOM   3110  C CD2 . PHE A  1  450 ? -40.478 10.013  52.059  1.00 73.04  ?  450  PHE A CD2 1 
ATOM   3111  C CE1 . PHE A  1  450 ? -41.973 11.024  54.141  1.00 71.99  ?  450  PHE A CE1 1 
ATOM   3112  C CE2 . PHE A  1  450 ? -41.576 9.313   52.524  1.00 72.74  ?  450  PHE A CE2 1 
ATOM   3113  C CZ  . PHE A  1  450 ? -42.324 9.822   53.566  1.00 72.46  ?  450  PHE A CZ  1 
ATOM   3114  N N   . GLY A  1  451 ? -37.895 14.977  51.208  1.00 72.41  ?  451  GLY A N   1 
ATOM   3115  C CA  . GLY A  1  451 ? -36.759 15.822  50.899  1.00 73.49  ?  451  GLY A CA  1 
ATOM   3116  C C   . GLY A  1  451 ? -35.604 15.672  51.866  1.00 73.20  ?  451  GLY A C   1 
ATOM   3117  O O   . GLY A  1  451 ? -35.084 14.569  52.058  1.00 73.09  ?  451  GLY A O   1 
ATOM   3118  N N   . VAL A  1  452 ? -35.191 16.779  52.479  1.00 72.44  ?  452  VAL A N   1 
ATOM   3119  C CA  . VAL A  1  452 ? -34.097 16.789  53.440  1.00 71.87  ?  452  VAL A CA  1 
ATOM   3120  C C   . VAL A  1  452 ? -34.603 17.405  54.731  1.00 70.37  ?  452  VAL A C   1 
ATOM   3121  O O   . VAL A  1  452 ? -35.319 18.412  54.711  1.00 70.39  ?  452  VAL A O   1 
ATOM   3122  C CB  . VAL A  1  452 ? -32.870 17.563  52.922  1.00 73.05  ?  452  VAL A CB  1 
ATOM   3123  C CG1 . VAL A  1  452 ? -32.078 16.703  51.963  1.00 73.92  ?  452  VAL A CG1 1 
ATOM   3124  C CG2 . VAL A  1  452 ? -33.308 18.852  52.259  1.00 73.88  ?  452  VAL A CG2 1 
ATOM   3125  N N   . TYR A  1  453 ? -34.236 16.793  55.853  1.00 71.61  ?  453  TYR A N   1 
ATOM   3126  C CA  . TYR A  1  453 ? -34.739 17.201  57.161  1.00 69.90  ?  453  TYR A CA  1 
ATOM   3127  C C   . TYR A  1  453 ? -33.583 17.249  58.146  1.00 69.22  ?  453  TYR A C   1 
ATOM   3128  O O   . TYR A  1  453 ? -33.229 16.237  58.762  1.00 67.87  ?  453  TYR A O   1 
ATOM   3129  C CB  . TYR A  1  453 ? -35.843 16.258  57.634  1.00 68.32  ?  453  TYR A CB  1 
ATOM   3130  C CG  . TYR A  1  453 ? -36.864 15.976  56.556  1.00 69.26  ?  453  TYR A CG  1 
ATOM   3131  C CD1 . TYR A  1  453 ? -37.811 16.928  56.209  1.00 69.54  ?  453  TYR A CD1 1 
ATOM   3132  C CD2 . TYR A  1  453 ? -36.866 14.769  55.870  1.00 69.89  ?  453  TYR A CD2 1 
ATOM   3133  C CE1 . TYR A  1  453 ? -38.738 16.683  55.223  1.00 70.26  ?  453  TYR A CE1 1 
ATOM   3134  C CE2 . TYR A  1  453 ? -37.791 14.516  54.881  1.00 70.72  ?  453  TYR A CE2 1 
ATOM   3135  C CZ  . TYR A  1  453 ? -38.723 15.478  54.564  1.00 70.83  ?  453  TYR A CZ  1 
ATOM   3136  O OH  . TYR A  1  453 ? -39.647 15.233  53.580  1.00 71.47  ?  453  TYR A OH  1 
ATOM   3137  N N   . PRO A  1  454 ? -32.965 18.420  58.320  1.00 67.53  ?  454  PRO A N   1 
ATOM   3138  C CA  . PRO A  1  454 ? -31.818 18.521  59.238  1.00 67.37  ?  454  PRO A CA  1 
ATOM   3139  C C   . PRO A  1  454 ? -32.169 18.251  60.689  1.00 65.31  ?  454  PRO A C   1 
ATOM   3140  O O   . PRO A  1  454 ? -31.274 17.911  61.473  1.00 64.85  ?  454  PRO A O   1 
ATOM   3141  C CB  . PRO A  1  454 ? -31.339 19.969  59.051  1.00 69.32  ?  454  PRO A CB  1 
ATOM   3142  C CG  . PRO A  1  454 ? -32.093 20.503  57.867  1.00 70.23  ?  454  PRO A CG  1 
ATOM   3143  C CD  . PRO A  1  454 ? -33.360 19.733  57.788  1.00 68.84  ?  454  PRO A CD  1 
ATOM   3144  N N   . THR A  1  455 ? -33.430 18.415  61.079  1.00 69.87  ?  455  THR A N   1 
ATOM   3145  C CA  . THR A  1  455 ? -33.852 18.264  62.462  1.00 67.94  ?  455  THR A CA  1 
ATOM   3146  C C   . THR A  1  455 ? -34.610 16.970  62.714  1.00 65.90  ?  455  THR A C   1 
ATOM   3147  O O   . THR A  1  455 ? -35.156 16.789  63.807  1.00 64.17  ?  455  THR A O   1 
ATOM   3148  C CB  . THR A  1  455 ? -34.721 19.447  62.870  1.00 67.99  ?  455  THR A CB  1 
ATOM   3149  O OG1 . THR A  1  455 ? -35.744 19.631  61.883  1.00 68.31  ?  455  THR A OG1 1 
ATOM   3150  C CG2 . THR A  1  455 ? -33.877 20.711  62.976  1.00 70.03  ?  455  THR A CG2 1 
ATOM   3151  N N   . LEU A  1  456 ? -34.674 16.078  61.728  1.00 64.74  ?  456  LEU A N   1 
ATOM   3152  C CA  . LEU A  1  456 ? -35.453 14.855  61.873  1.00 63.29  ?  456  LEU A CA  1 
ATOM   3153  C C   . LEU A  1  456 ? -34.833 13.951  62.929  1.00 61.63  ?  456  LEU A C   1 
ATOM   3154  O O   . LEU A  1  456 ? -33.635 13.662  62.891  1.00 62.06  ?  456  LEU A O   1 
ATOM   3155  C CB  . LEU A  1  456 ? -35.541 14.124  60.535  1.00 64.77  ?  456  LEU A CB  1 
ATOM   3156  C CG  . LEU A  1  456 ? -36.541 12.976  60.453  1.00 64.31  ?  456  LEU A CG  1 
ATOM   3157  C CD1 . LEU A  1  456 ? -37.936 13.489  60.726  1.00 63.86  ?  456  LEU A CD1 1 
ATOM   3158  C CD2 . LEU A  1  456 ? -36.465 12.312  59.088  1.00 66.42  ?  456  LEU A CD2 1 
ATOM   3159  N N   . ASN A  1  457 ? -35.657 13.506  63.873  1.00 62.52  ?  457  ASN A N   1 
ATOM   3160  C CA  . ASN A  1  457 ? -35.235 12.640  64.965  1.00 60.95  ?  457  ASN A CA  1 
ATOM   3161  C C   . ASN A  1  457 ? -35.764 11.219  64.847  1.00 60.05  ?  457  ASN A C   1 
ATOM   3162  O O   . ASN A  1  457 ? -35.019 10.266  65.074  1.00 59.67  ?  457  ASN A O   1 
ATOM   3163  C CB  . ASN A  1  457 ? -35.677 13.237  66.305  1.00 59.66  ?  457  ASN A CB  1 
ATOM   3164  C CG  . ASN A  1  457 ? -35.546 12.255  67.454  1.00 58.05  ?  457  ASN A CG  1 
ATOM   3165  O OD1 . ASN A  1  457 ? -36.502 11.559  67.806  1.00 56.44  ?  457  ASN A OD1 1 
ATOM   3166  N ND2 . ASN A  1  457 ? -34.364 12.202  68.053  1.00 58.91  ?  457  ASN A ND2 1 
ATOM   3167  N N   . PHE A  1  458 ? -37.039 11.052  64.508  1.00 59.81  ?  458  PHE A N   1 
ATOM   3168  C CA  . PHE A  1  458 ? -37.688 9.750   64.482  1.00 59.77  ?  458  PHE A CA  1 
ATOM   3169  C C   . PHE A  1  458 ? -38.640 9.723   63.300  1.00 62.38  ?  458  PHE A C   1 
ATOM   3170  O O   . PHE A  1  458 ? -39.341 10.704  63.043  1.00 63.07  ?  458  PHE A O   1 
ATOM   3171  C CB  . PHE A  1  458 ? -38.439 9.503   65.801  1.00 57.77  ?  458  PHE A CB  1 
ATOM   3172  C CG  . PHE A  1  458 ? -39.011 8.119   65.957  1.00 57.88  ?  458  PHE A CG  1 
ATOM   3173  C CD1 . PHE A  1  458 ? -40.144 7.731   65.263  1.00 60.26  ?  458  PHE A CD1 1 
ATOM   3174  C CD2 . PHE A  1  458 ? -38.446 7.227   66.847  1.00 56.08  ?  458  PHE A CD2 1 
ATOM   3175  C CE1 . PHE A  1  458 ? -40.679 6.470   65.429  1.00 60.88  ?  458  PHE A CE1 1 
ATOM   3176  C CE2 . PHE A  1  458 ? -38.975 5.965   67.018  1.00 56.24  ?  458  PHE A CE2 1 
ATOM   3177  C CZ  . PHE A  1  458 ? -40.092 5.585   66.309  1.00 58.71  ?  458  PHE A CZ  1 
ATOM   3178  N N   . ILE A  1  459 ? -38.654 8.614   62.570  1.00 59.14  ?  459  ILE A N   1 
ATOM   3179  C CA  . ILE A  1  459 ? -39.586 8.465   61.458  1.00 62.42  ?  459  ILE A CA  1 
ATOM   3180  C C   . ILE A  1  459 ? -39.942 6.993   61.318  1.00 63.90  ?  459  ILE A C   1 
ATOM   3181  O O   . ILE A  1  459 ? -39.065 6.125   61.366  1.00 62.81  ?  459  ILE A O   1 
ATOM   3182  C CB  . ILE A  1  459 ? -39.016 9.039   60.143  1.00 63.91  ?  459  ILE A CB  1 
ATOM   3183  C CG1 . ILE A  1  459 ? -39.999 8.821   58.991  1.00 66.12  ?  459  ILE A CG1 1 
ATOM   3184  C CG2 . ILE A  1  459 ? -37.647 8.451   59.833  1.00 63.93  ?  459  ILE A CG2 1 
ATOM   3185  C CD1 . ILE A  1  459 ? -40.135 10.013  58.083  1.00 66.36  ?  459  ILE A CD1 1 
ATOM   3186  N N   . ASP A  1  460 ? -41.236 6.712   61.175  1.00 65.75  ?  460  ASP A N   1 
ATOM   3187  C CA  . ASP A  1  460 ? -41.728 5.347   60.998  1.00 67.29  ?  460  ASP A CA  1 
ATOM   3188  C C   . ASP A  1  460 ? -42.759 5.355   59.878  1.00 70.75  ?  460  ASP A C   1 
ATOM   3189  O O   . ASP A  1  460 ? -43.878 5.842   60.067  1.00 71.27  ?  460  ASP A O   1 
ATOM   3190  C CB  . ASP A  1  460 ? -42.328 4.803   62.297  1.00 65.05  ?  460  ASP A CB  1 
ATOM   3191  C CG  . ASP A  1  460 ? -42.671 3.325   62.212  1.00 65.52  ?  460  ASP A CG  1 
ATOM   3192  O OD1 . ASP A  1  460 ? -42.416 2.706   61.156  1.00 67.41  ?  460  ASP A OD1 1 
ATOM   3193  O OD2 . ASP A  1  460 ? -43.200 2.781   63.204  1.00 63.81  -1 460  ASP A OD2 1 
ATOM   3194  N N   . LEU A  1  461 ? -42.384 4.818   58.715  1.00 69.70  ?  461  LEU A N   1 
ATOM   3195  C CA  . LEU A  1  461 ? -43.267 4.750   57.558  1.00 70.00  ?  461  LEU A CA  1 
ATOM   3196  C C   . LEU A  1  461 ? -43.800 3.343   57.319  1.00 70.67  ?  461  LEU A C   1 
ATOM   3197  O O   . LEU A  1  461 ? -44.257 3.041   56.214  1.00 70.47  ?  461  LEU A O   1 
ATOM   3198  C CB  . LEU A  1  461 ? -42.546 5.254   56.307  1.00 68.49  ?  461  LEU A CB  1 
ATOM   3199  C CG  . LEU A  1  461 ? -41.679 6.504   56.462  1.00 67.47  ?  461  LEU A CG  1 
ATOM   3200  C CD1 . LEU A  1  461 ? -40.526 6.501   55.462  1.00 66.51  ?  461  LEU A CD1 1 
ATOM   3201  C CD2 . LEU A  1  461 ? -42.525 7.749   56.310  1.00 67.99  ?  461  LEU A CD2 1 
ATOM   3202  N N   . SER A  1  462 ? -43.757 2.481   58.331  1.00 70.67  ?  462  SER A N   1 
ATOM   3203  C CA  . SER A  1  462 ? -44.025 1.063   58.139  1.00 70.51  ?  462  SER A CA  1 
ATOM   3204  C C   . SER A  1  462 ? -45.480 0.808   57.749  1.00 71.85  ?  462  SER A C   1 
ATOM   3205  O O   . SER A  1  462 ? -46.378 1.617   58.004  1.00 73.06  ?  462  SER A O   1 
ATOM   3206  C CB  . SER A  1  462 ? -43.689 0.280   59.406  1.00 69.81  ?  462  SER A CB  1 
ATOM   3207  O OG  . SER A  1  462 ? -42.389 0.595   59.864  1.00 66.84  ?  462  SER A OG  1 
ATOM   3208  N N   . ASN A  1  463 ? -45.698 -0.346  57.112  1.00 73.46  ?  463  ASN A N   1 
ATOM   3209  C CA  . ASN A  1  463 ? -47.026 -0.805  56.703  1.00 74.48  ?  463  ASN A CA  1 
ATOM   3210  C C   . ASN A  1  463 ? -47.705 0.219   55.791  1.00 75.12  ?  463  ASN A C   1 
ATOM   3211  O O   . ASN A  1  463 ? -48.750 0.788   56.109  1.00 76.50  ?  463  ASN A O   1 
ATOM   3212  C CB  . ASN A  1  463 ? -47.895 -1.125  57.923  1.00 75.73  ?  463  ASN A CB  1 
ATOM   3213  C CG  . ASN A  1  463 ? -47.219 -2.081  58.886  1.00 74.81  ?  463  ASN A CG  1 
ATOM   3214  O OD1 . ASN A  1  463 ? -46.495 -2.986  58.476  1.00 73.52  ?  463  ASN A OD1 1 
ATOM   3215  N ND2 . ASN A  1  463 ? -47.450 -1.879  60.180  1.00 74.33  ?  463  ASN A ND2 1 
ATOM   3216  N N   . ASN A  1  464 ? -47.072 0.460   54.648  1.00 77.53  ?  464  ASN A N   1 
ATOM   3217  C CA  . ASN A  1  464 ? -47.588 1.381   53.645  1.00 78.00  ?  464  ASN A CA  1 
ATOM   3218  C C   . ASN A  1  464 ? -47.273 0.794   52.275  1.00 77.27  ?  464  ASN A C   1 
ATOM   3219  O O   . ASN A  1  464 ? -46.865 -0.365  52.155  1.00 76.51  ?  464  ASN A O   1 
ATOM   3220  C CB  . ASN A  1  464 ? -47.002 2.786   53.838  1.00 77.61  ?  464  ASN A CB  1 
ATOM   3221  C CG  . ASN A  1  464 ? -47.757 3.602   54.884  1.00 78.84  ?  464  ASN A CG  1 
ATOM   3222  O OD1 . ASN A  1  464 ? -48.892 4.024   54.660  1.00 79.98  ?  464  ASN A OD1 1 
ATOM   3223  N ND2 . ASN A  1  464 ? -47.124 3.827   56.030  1.00 78.61  ?  464  ASN A ND2 1 
ATOM   3224  N N   . ASN A  1  465 ? -47.463 1.597   51.232  1.00 83.22  ?  465  ASN A N   1 
ATOM   3225  C CA  . ASN A  1  465 ? -47.311 1.143   49.856  1.00 83.14  ?  465  ASN A CA  1 
ATOM   3226  C C   . ASN A  1  465 ? -46.320 2.016   49.089  1.00 82.58  ?  465  ASN A C   1 
ATOM   3227  O O   . ASN A  1  465 ? -46.516 2.321   47.909  1.00 83.28  ?  465  ASN A O   1 
ATOM   3228  C CB  . ASN A  1  465 ? -48.663 1.108   49.149  1.00 85.23  ?  465  ASN A CB  1 
ATOM   3229  C CG  . ASN A  1  465 ? -48.657 0.206   47.933  1.00 87.26  ?  465  ASN A CG  1 
ATOM   3230  O OD1 . ASN A  1  465 ? -48.035 -0.858  47.943  1.00 86.19  ?  465  ASN A OD1 1 
ATOM   3231  N ND2 . ASN A  1  465 ? -49.338 0.631   46.872  1.00 91.52  ?  465  ASN A ND2 1 
ATOM   3232  N N   . PHE A  1  466 ? -45.238 2.426   49.748  1.00 78.59  ?  466  PHE A N   1 
ATOM   3233  C CA  . PHE A  1  466 ? -44.203 3.185   49.060  1.00 78.25  ?  466  PHE A CA  1 
ATOM   3234  C C   . PHE A  1  466 ? -43.390 2.260   48.165  1.00 77.98  ?  466  PHE A C   1 
ATOM   3235  O O   . PHE A  1  466 ? -43.124 1.108   48.516  1.00 77.25  ?  466  PHE A O   1 
ATOM   3236  C CB  . PHE A  1  466 ? -43.282 3.874   50.065  1.00 77.32  ?  466  PHE A CB  1 
ATOM   3237  C CG  . PHE A  1  466 ? -43.927 5.006   50.808  1.00 77.74  ?  466  PHE A CG  1 
ATOM   3238  C CD1 . PHE A  1  466 ? -44.313 6.159   50.145  1.00 78.46  ?  466  PHE A CD1 1 
ATOM   3239  C CD2 . PHE A  1  466 ? -44.137 4.922   52.174  1.00 77.52  ?  466  PHE A CD2 1 
ATOM   3240  C CE1 . PHE A  1  466 ? -44.903 7.202   50.828  1.00 78.72  ?  466  PHE A CE1 1 
ATOM   3241  C CE2 . PHE A  1  466 ? -44.725 5.961   52.860  1.00 78.04  ?  466  PHE A CE2 1 
ATOM   3242  C CZ  . PHE A  1  466 ? -45.109 7.103   52.185  1.00 78.49  ?  466  PHE A CZ  1 
ATOM   3243  N N   . HIS A  1  467 ? -43.004 2.766   46.999  1.00 77.90  ?  467  HIS A N   1 
ATOM   3244  C CA  . HIS A  1  467 ? -42.165 2.041   46.053  1.00 78.09  ?  467  HIS A CA  1 
ATOM   3245  C C   . HIS A  1  467 ? -40.913 2.861   45.752  1.00 78.33  ?  467  HIS A C   1 
ATOM   3246  O O   . HIS A  1  467 ? -40.688 3.931   46.324  1.00 78.18  ?  467  HIS A O   1 
ATOM   3247  C CB  . HIS A  1  467 ? -42.941 1.703   44.773  1.00 79.39  ?  467  HIS A CB  1 
ATOM   3248  C CG  . HIS A  1  467 ? -43.245 2.887   43.906  1.00 80.55  ?  467  HIS A CG  1 
ATOM   3249  N ND1 . HIS A  1  467 ? -44.431 3.585   43.987  1.00 82.05  ?  467  HIS A ND1 1 
ATOM   3250  C CD2 . HIS A  1  467 ? -42.527 3.482   42.923  1.00 81.39  ?  467  HIS A CD2 1 
ATOM   3251  C CE1 . HIS A  1  467 ? -44.426 4.565   43.100  1.00 84.78  ?  467  HIS A CE1 1 
ATOM   3252  N NE2 . HIS A  1  467 ? -43.282 4.524   42.441  1.00 83.78  ?  467  HIS A NE2 1 
ATOM   3253  N N   . GLY A  1  468 ? -40.091 2.343   44.847  1.00 76.61  ?  468  GLY A N   1 
ATOM   3254  C CA  . GLY A  1  468 ? -38.869 3.023   44.475  1.00 77.28  ?  468  GLY A CA  1 
ATOM   3255  C C   . GLY A  1  468 ? -37.681 2.600   45.315  1.00 76.46  ?  468  GLY A C   1 
ATOM   3256  O O   . GLY A  1  468 ? -37.724 1.644   46.096  1.00 75.19  ?  468  GLY A O   1 
ATOM   3257  N N   . GLN A  1  469 ? -36.590 3.340   45.137  1.00 77.79  ?  469  GLN A N   1 
ATOM   3258  C CA  . GLN A  1  469 ? -35.329 3.068   45.809  1.00 77.45  ?  469  GLN A CA  1 
ATOM   3259  C C   . GLN A  1  469 ? -34.969 4.233   46.719  1.00 77.39  ?  469  GLN A C   1 
ATOM   3260  O O   . GLN A  1  469 ? -35.346 5.382   46.465  1.00 78.17  ?  469  GLN A O   1 
ATOM   3261  C CB  . GLN A  1  469 ? -34.204 2.830   44.805  1.00 78.83  ?  469  GLN A CB  1 
ATOM   3262  C CG  . GLN A  1  469 ? -33.861 4.045   43.968  1.00 80.39  ?  469  GLN A CG  1 
ATOM   3263  C CD  . GLN A  1  469 ? -32.405 4.069   43.564  1.00 81.35  ?  469  GLN A CD  1 
ATOM   3264  O OE1 . GLN A  1  469 ? -32.037 3.556   42.506  1.00 82.03  ?  469  GLN A OE1 1 
ATOM   3265  N NE2 . GLN A  1  469 ? -31.565 4.663   44.406  1.00 81.36  ?  469  GLN A NE2 1 
ATOM   3266  N N   . LEU A  1  470 ? -34.238 3.921   47.787  1.00 71.75  ?  470  LEU A N   1 
ATOM   3267  C CA  . LEU A  1  470 ? -33.968 4.908   48.824  1.00 71.57  ?  470  LEU A CA  1 
ATOM   3268  C C   . LEU A  1  470 ? -33.038 5.998   48.309  1.00 73.63  ?  470  LEU A C   1 
ATOM   3269  O O   . LEU A  1  470 ? -31.974 5.713   47.753  1.00 74.63  ?  470  LEU A O   1 
ATOM   3270  C CB  . LEU A  1  470 ? -33.356 4.233   50.049  1.00 69.97  ?  470  LEU A CB  1 
ATOM   3271  C CG  . LEU A  1  470 ? -34.319 3.382   50.871  1.00 67.70  ?  470  LEU A CG  1 
ATOM   3272  C CD1 . LEU A  1  470 ? -33.575 2.720   52.015  1.00 65.93  ?  470  LEU A CD1 1 
ATOM   3273  C CD2 . LEU A  1  470 ? -35.476 4.229   51.380  1.00 67.37  ?  470  LEU A CD2 1 
ATOM   3274  N N   . SER A  1  471 ? -33.445 7.250   48.501  1.00 72.45  ?  471  SER A N   1 
ATOM   3275  C CA  . SER A  1  471 ? -32.608 8.389   48.158  1.00 74.01  ?  471  SER A CA  1 
ATOM   3276  C C   . SER A  1  471 ? -31.497 8.549   49.187  1.00 73.88  ?  471  SER A C   1 
ATOM   3277  O O   . SER A  1  471 ? -31.703 8.324   50.382  1.00 72.81  ?  471  SER A O   1 
ATOM   3278  C CB  . SER A  1  471 ? -33.457 9.662   48.090  1.00 74.16  ?  471  SER A CB  1 
ATOM   3279  O OG  . SER A  1  471 ? -32.658 10.824  47.977  1.00 75.00  ?  471  SER A OG  1 
ATOM   3280  N N   . ALA A  1  472 ? -30.310 8.936   48.720  1.00 73.25  ?  472  ALA A N   1 
ATOM   3281  C CA  . ALA A  1  472 ? -29.217 9.234   49.640  1.00 71.83  ?  472  ALA A CA  1 
ATOM   3282  C C   . ALA A  1  472 ? -29.429 10.532  50.420  1.00 71.26  ?  472  ALA A C   1 
ATOM   3283  O O   . ALA A  1  472 ? -28.551 10.916  51.202  1.00 69.91  ?  472  ALA A O   1 
ATOM   3284  C CB  . ALA A  1  472 ? -27.893 9.293   48.877  1.00 71.48  ?  472  ALA A CB  1 
ATOM   3285  N N   . ASN A  1  473 ? -30.565 11.208  50.234  1.00 75.49  ?  473  ASN A N   1 
ATOM   3286  C CA  . ASN A  1  473 ? -30.859 12.422  50.987  1.00 74.94  ?  473  ASN A CA  1 
ATOM   3287  C C   . ASN A  1  473 ? -30.980 12.164  52.482  1.00 73.14  ?  473  ASN A C   1 
ATOM   3288  O O   . ASN A  1  473 ? -30.880 13.109  53.272  1.00 72.36  ?  473  ASN A O   1 
ATOM   3289  C CB  . ASN A  1  473 ? -32.151 13.065  50.476  1.00 75.75  ?  473  ASN A CB  1 
ATOM   3290  C CG  . ASN A  1  473 ? -31.970 13.752  49.141  1.00 77.05  ?  473  ASN A CG  1 
ATOM   3291  O OD1 . ASN A  1  473 ? -30.850 13.906  48.655  1.00 77.33  ?  473  ASN A OD1 1 
ATOM   3292  N ND2 . ASN A  1  473 ? -33.078 14.169  48.537  1.00 77.42  ?  473  ASN A ND2 1 
ATOM   3293  N N   . TRP A  1  474 ? -31.225 10.916  52.887  1.00 72.81  ?  474  TRP A N   1 
ATOM   3294  C CA  . TRP A  1  474 ? -31.421 10.634  54.304  1.00 70.69  ?  474  TRP A CA  1 
ATOM   3295  C C   . TRP A  1  474 ? -30.160 10.906  55.106  1.00 68.97  ?  474  TRP A C   1 
ATOM   3296  O O   . TRP A  1  474 ? -30.240 11.170  56.312  1.00 67.20  ?  474  TRP A O   1 
ATOM   3297  C CB  . TRP A  1  474 ? -31.868 9.185   54.500  1.00 70.42  ?  474  TRP A CB  1 
ATOM   3298  C CG  . TRP A  1  474 ? -33.219 8.889   53.934  1.00 71.39  ?  474  TRP A CG  1 
ATOM   3299  C CD1 . TRP A  1  474 ? -33.495 8.131   52.834  1.00 71.73  ?  474  TRP A CD1 1 
ATOM   3300  C CD2 . TRP A  1  474 ? -34.483 9.341   54.439  1.00 70.15  ?  474  TRP A CD2 1 
ATOM   3301  N NE1 . TRP A  1  474 ? -34.850 8.086   52.621  1.00 70.81  ?  474  TRP A NE1 1 
ATOM   3302  C CE2 . TRP A  1  474 ? -35.480 8.819   53.593  1.00 70.00  ?  474  TRP A CE2 1 
ATOM   3303  C CE3 . TRP A  1  474 ? -34.867 10.135  55.523  1.00 69.00  ?  474  TRP A CE3 1 
ATOM   3304  C CZ2 . TRP A  1  474 ? -36.837 9.066   53.795  1.00 69.30  ?  474  TRP A CZ2 1 
ATOM   3305  C CZ3 . TRP A  1  474 ? -36.215 10.381  55.721  1.00 68.25  ?  474  TRP A CZ3 1 
ATOM   3306  C CH2 . TRP A  1  474 ? -37.183 9.848   54.861  1.00 68.62  ?  474  TRP A CH2 1 
ATOM   3307  N N   . GLU A  1  475 ? -28.990 10.842  54.462  1.00 73.54  ?  475  GLU A N   1 
ATOM   3308  C CA  . GLU A  1  475 ? -27.744 11.097  55.176  1.00 72.60  ?  475  GLU A CA  1 
ATOM   3309  C C   . GLU A  1  475 ? -27.699 12.509  55.743  1.00 73.11  ?  475  GLU A C   1 
ATOM   3310  O O   . GLU A  1  475 ? -27.095 12.737  56.798  1.00 72.40  ?  475  GLU A O   1 
ATOM   3311  C CB  . GLU A  1  475 ? -26.550 10.859  54.255  1.00 73.52  ?  475  GLU A CB  1 
ATOM   3312  C CG  . GLU A  1  475 ? -25.228 10.807  54.991  1.00 73.09  ?  475  GLU A CG  1 
ATOM   3313  C CD  . GLU A  1  475 ? -24.175 11.688  54.360  1.00 74.44  ?  475  GLU A CD  1 
ATOM   3314  O OE1 . GLU A  1  475 ? -24.067 11.701  53.111  1.00 74.89  ?  475  GLU A OE1 1 
ATOM   3315  O OE2 . GLU A  1  475 ? -23.464 12.379  55.122  1.00 74.63  -1 475  GLU A OE2 1 
ATOM   3316  N N   . GLN A  1  476 ? -28.341 13.464  55.069  1.00 74.78  ?  476  GLN A N   1 
ATOM   3317  C CA  . GLN A  1  476 ? -28.323 14.846  55.529  1.00 75.42  ?  476  GLN A CA  1 
ATOM   3318  C C   . GLN A  1  476 ? -29.111 15.040  56.816  1.00 73.92  ?  476  GLN A C   1 
ATOM   3319  O O   . GLN A  1  476 ? -28.902 16.040  57.509  1.00 74.24  ?  476  GLN A O   1 
ATOM   3320  C CB  . GLN A  1  476 ? -28.853 15.764  54.429  1.00 77.02  ?  476  GLN A CB  1 
ATOM   3321  C CG  . GLN A  1  476 ? -28.007 15.718  53.169  1.00 78.11  ?  476  GLN A CG  1 
ATOM   3322  C CD  . GLN A  1  476 ? -28.476 16.693  52.120  1.00 79.41  ?  476  GLN A CD  1 
ATOM   3323  O OE1 . GLN A  1  476 ? -29.036 17.741  52.441  1.00 79.69  ?  476  GLN A OE1 1 
ATOM   3324  N NE2 . GLN A  1  476 ? -28.245 16.360  50.853  1.00 80.12  ?  476  GLN A NE2 1 
ATOM   3325  N N   . SER A  1  477 ? -30.002 14.109  57.156  1.00 72.46  ?  477  SER A N   1 
ATOM   3326  C CA  . SER A  1  477 ? -30.711 14.150  58.434  1.00 70.63  ?  477  SER A CA  1 
ATOM   3327  C C   . SER A  1  477 ? -29.800 13.632  59.550  1.00 69.14  ?  477  SER A C   1 
ATOM   3328  O O   . SER A  1  477 ? -30.064 12.619  60.196  1.00 67.51  ?  477  SER A O   1 
ATOM   3329  C CB  . SER A  1  477 ? -32.004 13.349  58.349  1.00 70.08  ?  477  SER A CB  1 
ATOM   3330  O OG  . SER A  1  477 ? -32.942 13.968  57.484  1.00 71.44  ?  477  SER A OG  1 
ATOM   3331  N N   . GLN A  1  478 ? -28.703 14.366  59.769  1.00 70.77  ?  478  GLN A N   1 
ATOM   3332  C CA  . GLN A  1  478 ? -27.635 13.934  60.667  1.00 70.08  ?  478  GLN A CA  1 
ATOM   3333  C C   . GLN A  1  478 ? -28.086 13.745  62.112  1.00 68.24  ?  478  GLN A C   1 
ATOM   3334  O O   . GLN A  1  478 ? -27.309 13.220  62.918  1.00 67.80  ?  478  GLN A O   1 
ATOM   3335  C CB  . GLN A  1  478 ? -26.481 14.937  60.616  1.00 71.91  ?  478  GLN A CB  1 
ATOM   3336  C CG  . GLN A  1  478 ? -25.554 14.752  59.425  1.00 73.57  ?  478  GLN A CG  1 
ATOM   3337  C CD  . GLN A  1  478 ? -24.602 13.574  59.590  1.00 72.94  ?  478  GLN A CD  1 
ATOM   3338  O OE1 . GLN A  1  478 ? -23.666 13.625  60.391  1.00 72.99  ?  478  GLN A OE1 1 
ATOM   3339  N NE2 . GLN A  1  478 ? -24.835 12.509  58.826  1.00 72.67  ?  478  GLN A NE2 1 
ATOM   3340  N N   . LYS A  1  479 ? -29.304 14.150  62.463  1.00 67.00  ?  479  LYS A N   1 
ATOM   3341  C CA  . LYS A  1  479 ? -29.818 13.970  63.812  1.00 65.39  ?  479  LYS A CA  1 
ATOM   3342  C C   . LYS A  1  479 ? -30.727 12.754  63.945  1.00 63.82  ?  479  LYS A C   1 
ATOM   3343  O O   . LYS A  1  479 ? -31.229 12.493  65.041  1.00 62.55  ?  479  LYS A O   1 
ATOM   3344  C CB  . LYS A  1  479 ? -30.564 15.231  64.262  1.00 65.54  ?  479  LYS A CB  1 
ATOM   3345  C CG  . LYS A  1  479 ? -29.696 16.477  64.332  1.00 67.29  ?  479  LYS A CG  1 
ATOM   3346  C CD  . LYS A  1  479 ? -28.445 16.230  65.155  1.00 67.51  ?  479  LYS A CD  1 
ATOM   3347  C CE  . LYS A  1  479 ? -27.688 17.524  65.410  1.00 69.36  ?  479  LYS A CE  1 
ATOM   3348  N NZ  . LYS A  1  479 ? -28.421 18.443  66.330  1.00 69.24  ?  479  LYS A NZ  1 
ATOM   3349  N N   . LEU A  1  480 ? -30.934 11.999  62.869  1.00 62.11  ?  480  LEU A N   1 
ATOM   3350  C CA  . LEU A  1  480 ? -31.846 10.861  62.905  1.00 61.09  ?  480  LEU A CA  1 
ATOM   3351  C C   . LEU A  1  480 ? -31.283 9.751   63.783  1.00 60.06  ?  480  LEU A C   1 
ATOM   3352  O O   . LEU A  1  480 ? -30.109 9.389   63.670  1.00 60.68  ?  480  LEU A O   1 
ATOM   3353  C CB  . LEU A  1  480 ? -32.093 10.343  61.487  1.00 62.43  ?  480  LEU A CB  1 
ATOM   3354  C CG  . LEU A  1  480 ? -33.292 9.421   61.264  1.00 62.51  ?  480  LEU A CG  1 
ATOM   3355  C CD1 . LEU A  1  480 ? -34.569 10.179  61.484  1.00 62.63  ?  480  LEU A CD1 1 
ATOM   3356  C CD2 . LEU A  1  480 ? -33.269 8.844   59.862  1.00 64.59  ?  480  LEU A CD2 1 
ATOM   3357  N N   . VAL A  1  481 ? -32.120 9.215   64.665  1.00 61.53  ?  481  VAL A N   1 
ATOM   3358  C CA  . VAL A  1  481 ? -31.724 8.094   65.506  1.00 60.87  ?  481  VAL A CA  1 
ATOM   3359  C C   . VAL A  1  481 ? -32.518 6.828   65.220  1.00 60.08  ?  481  VAL A C   1 
ATOM   3360  O O   . VAL A  1  481 ? -32.044 5.730   65.557  1.00 59.81  ?  481  VAL A O   1 
ATOM   3361  C CB  . VAL A  1  481 ? -31.832 8.458   67.001  1.00 59.96  ?  481  VAL A CB  1 
ATOM   3362  C CG1 . VAL A  1  481 ? -30.912 9.615   67.329  1.00 61.47  ?  481  VAL A CG1 1 
ATOM   3363  C CG2 . VAL A  1  481 ? -33.261 8.795   67.353  1.00 58.21  ?  481  VAL A CG2 1 
ATOM   3364  N N   . ALA A  1  482 ? -33.701 6.928   64.617  1.00 59.99  ?  482  ALA A N   1 
ATOM   3365  C CA  . ALA A  1  482 ? -34.528 5.768   64.312  1.00 60.24  ?  482  ALA A CA  1 
ATOM   3366  C C   . ALA A  1  482 ? -35.062 5.898   62.894  1.00 62.65  ?  482  ALA A C   1 
ATOM   3367  O O   . ALA A  1  482 ? -35.845 6.809   62.611  1.00 63.61  ?  482  ALA A O   1 
ATOM   3368  C CB  . ALA A  1  482 ? -35.680 5.645   65.311  1.00 58.82  ?  482  ALA A CB  1 
ATOM   3369  N N   . PHE A  1  483 ? -34.650 4.991   62.008  1.00 60.77  ?  483  PHE A N   1 
ATOM   3370  C CA  . PHE A  1  483 ? -35.151 4.934   60.634  1.00 63.16  ?  483  PHE A CA  1 
ATOM   3371  C C   . PHE A  1  483 ? -35.872 3.601   60.462  1.00 64.01  ?  483  PHE A C   1 
ATOM   3372  O O   . PHE A  1  483 ? -35.229 2.555   60.330  1.00 63.32  ?  483  PHE A O   1 
ATOM   3373  C CB  . PHE A  1  483 ? -34.015 5.085   59.624  1.00 63.41  ?  483  PHE A CB  1 
ATOM   3374  C CG  . PHE A  1  483 ? -34.482 5.368   58.222  1.00 65.56  ?  483  PHE A CG  1 
ATOM   3375  C CD1 . PHE A  1  483 ? -35.757 5.850   57.983  1.00 67.14  ?  483  PHE A CD1 1 
ATOM   3376  C CD2 . PHE A  1  483 ? -33.644 5.153   57.141  1.00 66.18  ?  483  PHE A CD2 1 
ATOM   3377  C CE1 . PHE A  1  483 ? -36.187 6.111   56.693  1.00 68.47  ?  483  PHE A CE1 1 
ATOM   3378  C CE2 . PHE A  1  483 ? -34.070 5.413   55.848  1.00 68.04  ?  483  PHE A CE2 1 
ATOM   3379  C CZ  . PHE A  1  483 ? -35.345 5.892   55.626  1.00 68.86  ?  483  PHE A CZ  1 
ATOM   3380  N N   . ILE A  1  484 ? -37.205 3.637   60.450  1.00 62.94  ?  484  ILE A N   1 
ATOM   3381  C CA  . ILE A  1  484 ? -38.030 2.432   60.409  1.00 63.97  ?  484  ILE A CA  1 
ATOM   3382  C C   . ILE A  1  484 ? -38.903 2.492   59.163  1.00 66.80  ?  484  ILE A C   1 
ATOM   3383  O O   . ILE A  1  484 ? -39.735 3.397   59.026  1.00 68.53  ?  484  ILE A O   1 
ATOM   3384  C CB  . ILE A  1  484 ? -38.881 2.288   61.681  1.00 62.93  ?  484  ILE A CB  1 
ATOM   3385  C CG1 . ILE A  1  484 ? -37.987 2.380   62.920  1.00 59.44  ?  484  ILE A CG1 1 
ATOM   3386  C CG2 . ILE A  1  484 ? -39.633 0.976   61.672  1.00 63.54  ?  484  ILE A CG2 1 
ATOM   3387  C CD1 . ILE A  1  484 ? -38.689 2.063   64.210  1.00 57.63  ?  484  ILE A CD1 1 
ATOM   3388  N N   . LEU A  1  485 ? -38.696 1.542   58.249  1.00 68.36  ?  485  LEU A N   1 
ATOM   3389  C CA  . LEU A  1  485 ? -39.363 1.528   56.947  1.00 69.15  ?  485  LEU A CA  1 
ATOM   3390  C C   . LEU A  1  485 ? -39.825 0.111   56.575  1.00 69.20  ?  485  LEU A C   1 
ATOM   3391  O O   . LEU A  1  485 ? -39.594 -0.364  55.462  1.00 68.45  ?  485  LEU A O   1 
ATOM   3392  C CB  . LEU A  1  485 ? -38.445 2.107   55.872  1.00 68.04  ?  485  LEU A CB  1 
ATOM   3393  C CG  . LEU A  1  485 ? -39.159 3.034   54.885  1.00 68.96  ?  485  LEU A CG  1 
ATOM   3394  C CD1 . LEU A  1  485 ? -38.184 3.684   53.911  1.00 68.68  ?  485  LEU A CD1 1 
ATOM   3395  C CD2 . LEU A  1  485 ? -40.283 2.325   54.160  1.00 69.80  ?  485  LEU A CD2 1 
ATOM   3396  N N   . SER A  1  486 ? -40.441 -0.611  57.509  1.00 69.73  ?  486  SER A N   1 
ATOM   3397  C CA  . SER A  1  486 ? -40.738 -2.010  57.221  1.00 69.44  ?  486  SER A CA  1 
ATOM   3398  C C   . SER A  1  486 ? -42.049 -2.164  56.444  1.00 70.93  ?  486  SER A C   1 
ATOM   3399  O O   . SER A  1  486 ? -42.897 -1.270  56.415  1.00 72.44  ?  486  SER A O   1 
ATOM   3400  C CB  . SER A  1  486 ? -40.795 -2.833  58.511  1.00 69.21  ?  486  SER A CB  1 
ATOM   3401  O OG  . SER A  1  486 ? -41.875 -2.436  59.341  1.00 70.92  ?  486  SER A OG  1 
ATOM   3402  N N   . ASN A  1  487 ? -42.181 -3.314  55.776  1.00 74.57  ?  487  ASN A N   1 
ATOM   3403  C CA  . ASN A  1  487 ? -43.414 -3.746  55.108  1.00 75.68  ?  487  ASN A CA  1 
ATOM   3404  C C   . ASN A  1  487 ? -43.899 -2.725  54.074  1.00 76.28  ?  487  ASN A C   1 
ATOM   3405  O O   . ASN A  1  487 ? -45.031 -2.239  54.114  1.00 77.77  ?  487  ASN A O   1 
ATOM   3406  C CB  . ASN A  1  487 ? -44.506 -4.043  56.139  1.00 77.38  ?  487  ASN A CB  1 
ATOM   3407  C CG  . ASN A  1  487 ? -45.667 -4.835  55.561  1.00 78.08  ?  487  ASN A CG  1 
ATOM   3408  O OD1 . ASN A  1  487 ? -45.486 -5.665  54.670  1.00 77.18  ?  487  ASN A OD1 1 
ATOM   3409  N ND2 . ASN A  1  487 ? -46.874 -4.567  56.085  1.00 79.74  ?  487  ASN A ND2 1 
ATOM   3410  N N   . ASN A  1  488 ? -43.018 -2.418  53.126  1.00 73.87  ?  488  ASN A N   1 
ATOM   3411  C CA  . ASN A  1  488 ? -43.367 -1.572  51.989  1.00 74.40  ?  488  ASN A CA  1 
ATOM   3412  C C   . ASN A  1  488 ? -42.993 -2.282  50.691  1.00 74.00  ?  488  ASN A C   1 
ATOM   3413  O O   . ASN A  1  488 ? -42.653 -3.469  50.706  1.00 73.35  ?  488  ASN A O   1 
ATOM   3414  C CB  . ASN A  1  488 ? -42.677 -0.210  52.091  1.00 74.07  ?  488  ASN A CB  1 
ATOM   3415  C CG  . ASN A  1  488 ? -43.503 0.821   52.854  1.00 75.16  ?  488  ASN A CG  1 
ATOM   3416  O OD1 . ASN A  1  488 ? -44.275 1.582   52.267  1.00 75.96  ?  488  ASN A OD1 1 
ATOM   3417  N ND2 . ASN A  1  488 ? -43.330 0.856   54.168  1.00 75.33  ?  488  ASN A ND2 1 
ATOM   3418  N N   . SER A  1  489 ? -43.085 -1.585  49.560  1.00 74.50  ?  489  SER A N   1 
ATOM   3419  C CA  . SER A  1  489 ? -42.719 -2.147  48.265  1.00 74.66  ?  489  SER A CA  1 
ATOM   3420  C C   . SER A  1  489 ? -41.384 -1.607  47.753  1.00 74.27  ?  489  SER A C   1 
ATOM   3421  O O   . SER A  1  489 ? -41.167 -1.529  46.541  1.00 75.07  ?  489  SER A O   1 
ATOM   3422  C CB  . SER A  1  489 ? -43.821 -1.884  47.243  1.00 76.09  ?  489  SER A CB  1 
ATOM   3423  O OG  . SER A  1  489 ? -45.086 -2.212  47.782  1.00 76.73  ?  489  SER A OG  1 
ATOM   3424  N N   . ILE A  1  490 ? -40.478 -1.238  48.653  1.00 71.45  ?  490  ILE A N   1 
ATOM   3425  C CA  . ILE A  1  490 ? -39.237 -0.584  48.247  1.00 71.47  ?  490  ILE A CA  1 
ATOM   3426  C C   . ILE A  1  490 ? -38.236 -1.603  47.722  1.00 71.25  ?  490  ILE A C   1 
ATOM   3427  O O   . ILE A  1  490 ? -38.083 -2.705  48.266  1.00 70.20  ?  490  ILE A O   1 
ATOM   3428  C CB  . ILE A  1  490 ? -38.661 0.242   49.406  1.00 70.73  ?  490  ILE A CB  1 
ATOM   3429  C CG1 . ILE A  1  490 ? -39.503 1.492   49.568  1.00 71.39  ?  490  ILE A CG1 1 
ATOM   3430  C CG2 . ILE A  1  490 ? -37.232 0.653   49.146  1.00 70.91  ?  490  ILE A CG2 1 
ATOM   3431  C CD1 . ILE A  1  490 ? -39.956 1.687   50.922  1.00 70.85  ?  490  ILE A CD1 1 
ATOM   3432  N N   . THR A  1  491 ? -37.556 -1.220  46.645  1.00 67.70  ?  491  THR A N   1 
ATOM   3433  C CA  . THR A  1  491 ? -36.602 -2.028  45.901  1.00 68.19  ?  491  THR A CA  1 
ATOM   3434  C C   . THR A  1  491 ? -35.247 -1.313  45.855  1.00 68.91  ?  491  THR A C   1 
ATOM   3435  O O   . THR A  1  491 ? -35.043 -0.275  46.492  1.00 68.80  ?  491  THR A O   1 
ATOM   3436  C CB  . THR A  1  491 ? -37.133 -2.306  44.494  1.00 69.59  ?  491  THR A CB  1 
ATOM   3437  O OG1 . THR A  1  491 ? -36.974 -1.131  43.690  1.00 70.89  ?  491  THR A OG1 1 
ATOM   3438  C CG2 . THR A  1  491 ? -38.605 -2.677  44.536  1.00 69.41  ?  491  THR A CG2 1 
ATOM   3439  N N   . GLY A  1  492 ? -34.315 -1.883  45.098  1.00 61.90  ?  492  GLY A N   1 
ATOM   3440  C CA  . GLY A  1  492 ? -33.004 -1.287  44.936  1.00 61.74  ?  492  GLY A CA  1 
ATOM   3441  C C   . GLY A  1  492 ? -32.025 -1.709  46.012  1.00 60.29  ?  492  GLY A C   1 
ATOM   3442  O O   . GLY A  1  492 ? -32.258 -2.637  46.790  1.00 58.52  ?  492  GLY A O   1 
ATOM   3443  N N   . ALA A  1  493 ? -30.892 -1.012  46.039  1.00 60.24  ?  493  ALA A N   1 
ATOM   3444  C CA  . ALA A  1  493 ? -29.821 -1.275  46.990  1.00 58.81  ?  493  ALA A CA  1 
ATOM   3445  C C   . ALA A  1  493 ? -29.801 -0.208  48.075  1.00 58.60  ?  493  ALA A C   1 
ATOM   3446  O O   . ALA A  1  493 ? -30.282 0.913   47.889  1.00 59.81  ?  493  ALA A O   1 
ATOM   3447  C CB  . ALA A  1  493 ? -28.458 -1.327  46.290  1.00 59.51  ?  493  ALA A CB  1 
ATOM   3448  N N   . ILE A  1  494 ? -29.229 -0.568  49.220  1.00 61.96  ?  494  ILE A N   1 
ATOM   3449  C CA  . ILE A  1  494 ? -29.086 0.378   50.321  1.00 61.79  ?  494  ILE A CA  1 
ATOM   3450  C C   . ILE A  1  494 ? -27.991 1.368   49.946  1.00 64.24  ?  494  ILE A C   1 
ATOM   3451  O O   . ILE A  1  494 ? -26.830 0.967   49.784  1.00 63.27  ?  494  ILE A O   1 
ATOM   3452  C CB  . ILE A  1  494 ? -28.750 -0.333  51.639  1.00 59.06  ?  494  ILE A CB  1 
ATOM   3453  C CG1 . ILE A  1  494 ? -29.846 -1.336  52.014  1.00 56.95  ?  494  ILE A CG1 1 
ATOM   3454  C CG2 . ILE A  1  494 ? -28.545 0.697   52.750  1.00 58.61  ?  494  ILE A CG2 1 
ATOM   3455  C CD1 . ILE A  1  494 ? -29.874 -1.677  53.489  1.00 54.58  ?  494  ILE A CD1 1 
ATOM   3456  N N   . PRO A  1  495 ? -28.303 2.654   49.814  1.00 65.90  ?  495  PRO A N   1 
ATOM   3457  C CA  . PRO A  1  495 ? -27.281 3.640   49.449  1.00 65.84  ?  495  PRO A CA  1 
ATOM   3458  C C   . PRO A  1  495 ? -26.155 3.658   50.465  1.00 62.66  ?  495  PRO A C   1 
ATOM   3459  O O   . PRO A  1  495 ? -26.404 3.623   51.678  1.00 61.41  ?  495  PRO A O   1 
ATOM   3460  C CB  . PRO A  1  495 ? -28.054 4.967   49.456  1.00 67.23  ?  495  PRO A CB  1 
ATOM   3461  C CG  . PRO A  1  495 ? -29.489 4.574   49.314  1.00 67.77  ?  495  PRO A CG  1 
ATOM   3462  C CD  . PRO A  1  495 ? -29.620 3.271   50.024  1.00 65.58  ?  495  PRO A CD  1 
ATOM   3463  N N   . PRO A  1  496 ? -24.905 3.728   50.011  1.00 64.87  ?  496  PRO A N   1 
ATOM   3464  C CA  . PRO A  1  496 ? -23.776 3.659   50.953  1.00 62.84  ?  496  PRO A CA  1 
ATOM   3465  C C   . PRO A  1  496 ? -23.766 4.772   51.985  1.00 63.11  ?  496  PRO A C   1 
ATOM   3466  O O   . PRO A  1  496 ? -23.237 4.573   53.085  1.00 62.44  ?  496  PRO A O   1 
ATOM   3467  C CB  . PRO A  1  496 ? -22.551 3.737   50.030  1.00 62.33  ?  496  PRO A CB  1 
ATOM   3468  C CG  . PRO A  1  496 ? -23.048 3.286   48.706  1.00 63.12  ?  496  PRO A CG  1 
ATOM   3469  C CD  . PRO A  1  496 ? -24.456 3.780   48.614  1.00 65.49  ?  496  PRO A CD  1 
ATOM   3470  N N   . GLU A  1  497 ? -24.320 5.943   51.661  1.00 68.25  ?  497  GLU A N   1 
ATOM   3471  C CA  . GLU A  1  497 ? -24.298 7.068   52.590  1.00 68.42  ?  497  GLU A CA  1 
ATOM   3472  C C   . GLU A  1  497 ? -25.102 6.796   53.856  1.00 67.55  ?  497  GLU A C   1 
ATOM   3473  O O   . GLU A  1  497 ? -24.923 7.503   54.855  1.00 67.33  ?  497  GLU A O   1 
ATOM   3474  C CB  . GLU A  1  497 ? -24.822 8.329   51.899  1.00 69.74  ?  497  GLU A CB  1 
ATOM   3475  C CG  . GLU A  1  497 ? -24.002 8.765   50.697  1.00 70.20  ?  497  GLU A CG  1 
ATOM   3476  C CD  . GLU A  1  497 ? -24.346 7.990   49.438  1.00 70.73  ?  497  GLU A CD  1 
ATOM   3477  O OE1 . GLU A  1  497 ? -25.361 7.261   49.443  1.00 71.42  ?  497  GLU A OE1 1 
ATOM   3478  O OE2 . GLU A  1  497 ? -23.598 8.107   48.445  1.00 70.60  -1 497  GLU A OE2 1 
ATOM   3479  N N   . ILE A  1  498 ? -25.980 5.791   53.837  1.00 65.25  ?  498  ILE A N   1 
ATOM   3480  C CA  . ILE A  1  498 ? -26.752 5.448   55.029  1.00 63.90  ?  498  ILE A CA  1 
ATOM   3481  C C   . ILE A  1  498 ? -25.826 5.043   56.167  1.00 62.93  ?  498  ILE A C   1 
ATOM   3482  O O   . ILE A  1  498 ? -26.082 5.350   57.336  1.00 62.05  ?  498  ILE A O   1 
ATOM   3483  C CB  . ILE A  1  498 ? -27.772 4.340   54.708  1.00 63.87  ?  498  ILE A CB  1 
ATOM   3484  C CG1 . ILE A  1  498 ? -28.716 4.793   53.593  1.00 66.66  ?  498  ILE A CG1 1 
ATOM   3485  C CG2 . ILE A  1  498 ? -28.561 3.970   55.945  1.00 61.93  ?  498  ILE A CG2 1 
ATOM   3486  C CD1 . ILE A  1  498 ? -29.668 5.890   54.014  1.00 67.19  ?  498  ILE A CD1 1 
ATOM   3487  N N   . TRP A  1  499 ? -24.750 4.323   55.852  1.00 65.19  ?  499  TRP A N   1 
ATOM   3488  C CA  . TRP A  1  499 ? -23.831 3.903   56.900  1.00 65.58  ?  499  TRP A CA  1 
ATOM   3489  C C   . TRP A  1  499 ? -23.053 5.070   57.493  1.00 66.49  ?  499  TRP A C   1 
ATOM   3490  O O   . TRP A  1  499 ? -22.472 4.921   58.571  1.00 67.12  ?  499  TRP A O   1 
ATOM   3491  C CB  . TRP A  1  499 ? -22.876 2.839   56.362  1.00 65.85  ?  499  TRP A CB  1 
ATOM   3492  C CG  . TRP A  1  499 ? -23.553 1.825   55.487  1.00 64.22  ?  499  TRP A CG  1 
ATOM   3493  C CD1 . TRP A  1  499 ? -23.200 1.482   54.213  1.00 63.77  ?  499  TRP A CD1 1 
ATOM   3494  C CD2 . TRP A  1  499 ? -24.699 1.020   55.815  1.00 63.09  ?  499  TRP A CD2 1 
ATOM   3495  N NE1 . TRP A  1  499 ? -24.055 0.521   53.727  1.00 62.90  ?  499  TRP A NE1 1 
ATOM   3496  C CE2 . TRP A  1  499 ? -24.981 0.218   54.691  1.00 62.50  ?  499  TRP A CE2 1 
ATOM   3497  C CE3 . TRP A  1  499 ? -25.512 0.901   56.947  1.00 62.64  ?  499  TRP A CE3 1 
ATOM   3498  C CZ2 . TRP A  1  499 ? -26.038 -0.692  54.667  1.00 61.94  ?  499  TRP A CZ2 1 
ATOM   3499  C CZ3 . TRP A  1  499 ? -26.567 0.003   56.916  1.00 61.41  ?  499  TRP A CZ3 1 
ATOM   3500  C CH2 . TRP A  1  499 ? -26.816 -0.785  55.784  1.00 61.19  ?  499  TRP A CH2 1 
ATOM   3501  N N   . ASN A  1  500 ? -23.039 6.226   56.834  1.00 76.32  ?  500  ASN A N   1 
ATOM   3502  C CA  . ASN A  1  500 ? -22.393 7.400   57.409  1.00 76.84  ?  500  ASN A CA  1 
ATOM   3503  C C   . ASN A  1  500 ? -23.293 8.150   58.388  1.00 75.80  ?  500  ASN A C   1 
ATOM   3504  O O   . ASN A  1  500 ? -22.870 9.177   58.930  1.00 76.17  ?  500  ASN A O   1 
ATOM   3505  C CB  . ASN A  1  500 ? -21.910 8.342   56.298  1.00 77.76  ?  500  ASN A CB  1 
ATOM   3506  C CG  . ASN A  1  500 ? -20.421 8.180   56.002  1.00 78.52  ?  500  ASN A CG  1 
ATOM   3507  O OD1 . ASN A  1  500 ? -19.693 7.545   56.767  1.00 78.99  ?  500  ASN A OD1 1 
ATOM   3508  N ND2 . ASN A  1  500 ? -19.965 8.755   54.886  1.00 78.80  ?  500  ASN A ND2 1 
ATOM   3509  N N   . MET A  1  501 ? -24.516 7.670   58.627  1.00 69.22  ?  501  MET A N   1 
ATOM   3510  C CA  . MET A  1  501 ? -25.404 8.249   59.637  1.00 68.03  ?  501  MET A CA  1 
ATOM   3511  C C   . MET A  1  501 ? -25.023 7.665   60.996  1.00 67.01  ?  501  MET A C   1 
ATOM   3512  O O   . MET A  1  501 ? -25.649 6.738   61.516  1.00 65.32  ?  501  MET A O   1 
ATOM   3513  C CB  . MET A  1  501 ? -26.862 7.979   59.292  1.00 66.94  ?  501  MET A CB  1 
ATOM   3514  C CG  . MET A  1  501 ? -27.200 8.113   57.818  1.00 67.55  ?  501  MET A CG  1 
ATOM   3515  S SD  . MET A  1  501 ? -28.974 8.067   57.489  1.00 67.08  ?  501  MET A SD  1 
ATOM   3516  C CE  . MET A  1  501 ? -29.627 8.769   59.001  1.00 67.32  ?  501  MET A CE  1 
ATOM   3517  N N   . THR A  1  502 ? -23.974 8.244   61.585  1.00 71.95  ?  502  THR A N   1 
ATOM   3518  C CA  . THR A  1  502 ? -23.362 7.675   62.781  1.00 71.39  ?  502  THR A CA  1 
ATOM   3519  C C   . THR A  1  502 ? -24.294 7.689   63.990  1.00 70.01  ?  502  THR A C   1 
ATOM   3520  O O   . THR A  1  502 ? -24.129 6.869   64.901  1.00 69.04  ?  502  THR A O   1 
ATOM   3521  C CB  . THR A  1  502 ? -22.079 8.431   63.112  1.00 73.37  ?  502  THR A CB  1 
ATOM   3522  O OG1 . THR A  1  502 ? -22.403 9.784   63.460  1.00 74.16  ?  502  THR A OG1 1 
ATOM   3523  C CG2 . THR A  1  502 ? -21.148 8.427   61.913  1.00 75.29  ?  502  THR A CG2 1 
ATOM   3524  N N   . GLN A  1  503 ? -25.268 8.598   64.030  1.00 71.97  ?  503  GLN A N   1 
ATOM   3525  C CA  . GLN A  1  503 ? -26.130 8.733   65.201  1.00 71.64  ?  503  GLN A CA  1 
ATOM   3526  C C   . GLN A  1  503 ? -27.257 7.708   65.245  1.00 70.18  ?  503  GLN A C   1 
ATOM   3527  O O   . GLN A  1  503 ? -28.013 7.686   66.223  1.00 70.28  ?  503  GLN A O   1 
ATOM   3528  C CB  . GLN A  1  503 ? -26.721 10.145  65.262  1.00 73.29  ?  503  GLN A CB  1 
ATOM   3529  C CG  . GLN A  1  503 ? -25.758 11.200  65.778  1.00 75.04  ?  503  GLN A CG  1 
ATOM   3530  C CD  . GLN A  1  503 ? -25.109 10.806  67.092  1.00 74.94  ?  503  GLN A CD  1 
ATOM   3531  O OE1 . GLN A  1  503 ? -25.770 10.283  67.990  1.00 74.26  ?  503  GLN A OE1 1 
ATOM   3532  N NE2 . GLN A  1  503 ? -23.808 11.056  67.212  1.00 75.92  ?  503  GLN A NE2 1 
ATOM   3533  N N   . LEU A  1  504 ? -27.385 6.860   64.228  1.00 69.09  ?  504  LEU A N   1 
ATOM   3534  C CA  . LEU A  1  504 ? -28.502 5.926   64.146  1.00 68.16  ?  504  LEU A CA  1 
ATOM   3535  C C   . LEU A  1  504 ? -28.399 4.854   65.230  1.00 66.99  ?  504  LEU A C   1 
ATOM   3536  O O   . LEU A  1  504 ? -27.347 4.233   65.409  1.00 66.25  ?  504  LEU A O   1 
ATOM   3537  C CB  . LEU A  1  504 ? -28.524 5.284   62.756  1.00 67.73  ?  504  LEU A CB  1 
ATOM   3538  C CG  . LEU A  1  504 ? -29.863 5.110   62.040  1.00 68.34  ?  504  LEU A CG  1 
ATOM   3539  C CD1 . LEU A  1  504 ? -30.506 6.458   61.761  1.00 70.19  ?  504  LEU A CD1 1 
ATOM   3540  C CD2 . LEU A  1  504 ? -29.667 4.336   60.747  1.00 68.00  ?  504  LEU A CD2 1 
ATOM   3541  N N   . SER A  1  505 ? -29.499 4.633   65.955  1.00 64.29  ?  505  SER A N   1 
ATOM   3542  C CA  . SER A  1  505 ? -29.556 3.582   66.963  1.00 63.59  ?  505  SER A CA  1 
ATOM   3543  C C   . SER A  1  505 ? -30.483 2.431   66.590  1.00 63.43  ?  505  SER A C   1 
ATOM   3544  O O   . SER A  1  505 ? -30.301 1.321   67.101  1.00 62.68  ?  505  SER A O   1 
ATOM   3545  C CB  . SER A  1  505 ? -29.994 4.167   68.319  1.00 64.89  ?  505  SER A CB  1 
ATOM   3546  O OG  . SER A  1  505 ? -29.699 3.298   69.407  1.00 64.42  ?  505  SER A OG  1 
ATOM   3547  N N   . GLN A  1  506 ? -31.458 2.661   65.713  1.00 58.35  ?  506  GLN A N   1 
ATOM   3548  C CA  . GLN A  1  506 ? -32.345 1.605   65.247  1.00 59.18  ?  506  GLN A CA  1 
ATOM   3549  C C   . GLN A  1  506 ? -32.577 1.774   63.754  1.00 59.74  ?  506  GLN A C   1 
ATOM   3550  O O   . GLN A  1  506 ? -32.872 2.880   63.291  1.00 61.04  ?  506  GLN A O   1 
ATOM   3551  C CB  . GLN A  1  506 ? -33.680 1.633   65.998  1.00 62.01  ?  506  GLN A CB  1 
ATOM   3552  C CG  . GLN A  1  506 ? -34.751 0.767   65.371  1.00 64.57  ?  506  GLN A CG  1 
ATOM   3553  C CD  . GLN A  1  506 ? -35.853 0.424   66.344  1.00 67.36  ?  506  GLN A CD  1 
ATOM   3554  O OE1 . GLN A  1  506 ? -36.023 1.097   67.356  1.00 67.46  ?  506  GLN A OE1 1 
ATOM   3555  N NE2 . GLN A  1  506 ? -36.606 -0.629  66.045  1.00 69.95  ?  506  GLN A NE2 1 
ATOM   3556  N N   . LEU A  1  507 ? -32.453 0.679   63.008  1.00 58.06  ?  507  LEU A N   1 
ATOM   3557  C CA  . LEU A  1  507 ? -32.639 0.690   61.561  1.00 58.79  ?  507  LEU A CA  1 
ATOM   3558  C C   . LEU A  1  507 ? -33.461 -0.529  61.182  1.00 60.55  ?  507  LEU A C   1 
ATOM   3559  O O   . LEU A  1  507 ? -33.032 -1.662  61.418  1.00 58.83  ?  507  LEU A O   1 
ATOM   3560  C CB  . LEU A  1  507 ? -31.293 0.686   60.830  1.00 56.27  ?  507  LEU A CB  1 
ATOM   3561  C CG  . LEU A  1  507 ? -31.276 0.522   59.306  1.00 56.98  ?  507  LEU A CG  1 
ATOM   3562  C CD1 . LEU A  1  507 ? -32.245 1.474   58.625  1.00 60.01  ?  507  LEU A CD1 1 
ATOM   3563  C CD2 . LEU A  1  507 ? -29.873 0.746   58.781  1.00 55.93  ?  507  LEU A CD2 1 
ATOM   3564  N N   . ASP A  1  508 ? -34.635 -0.302  60.598  1.00 56.42  ?  508  ASP A N   1 
ATOM   3565  C CA  . ASP A  1  508 ? -35.561 -1.382  60.263  1.00 59.95  ?  508  ASP A CA  1 
ATOM   3566  C C   . ASP A  1  508 ? -36.017 -1.218  58.817  1.00 62.30  ?  508  ASP A C   1 
ATOM   3567  O O   . ASP A  1  508 ? -36.874 -0.382  58.524  1.00 66.56  ?  508  ASP A O   1 
ATOM   3568  C CB  . ASP A  1  508 ? -36.750 -1.398  61.215  1.00 64.84  ?  508  ASP A CB  1 
ATOM   3569  C CG  . ASP A  1  508 ? -37.622 -2.625  61.035  1.00 68.56  ?  508  ASP A CG  1 
ATOM   3570  O OD1 . ASP A  1  508 ? -37.298 -3.468  60.169  1.00 66.99  ?  508  ASP A OD1 1 
ATOM   3571  O OD2 . ASP A  1  508 ? -38.627 -2.751  61.772  1.00 72.61  -1 508  ASP A OD2 1 
ATOM   3572  N N   . LEU A  1  509 ? -35.450 -2.028  57.922  1.00 63.75  ?  509  LEU A N   1 
ATOM   3573  C CA  . LEU A  1  509 ? -35.863 -2.085  56.525  1.00 64.01  ?  509  LEU A CA  1 
ATOM   3574  C C   . LEU A  1  509 ? -36.453 -3.450  56.179  1.00 64.41  ?  509  LEU A C   1 
ATOM   3575  O O   . LEU A  1  509 ? -36.421 -3.878  55.023  1.00 62.63  ?  509  LEU A O   1 
ATOM   3576  C CB  . LEU A  1  509 ? -34.691 -1.749  55.602  1.00 59.57  ?  509  LEU A CB  1 
ATOM   3577  C CG  . LEU A  1  509 ? -33.997 -0.416  55.883  1.00 59.21  ?  509  LEU A CG  1 
ATOM   3578  C CD1 . LEU A  1  509 ? -32.845 -0.206  54.938  1.00 55.78  ?  509  LEU A CD1 1 
ATOM   3579  C CD2 . LEU A  1  509 ? -34.978 0.723   55.760  1.00 62.39  ?  509  LEU A CD2 1 
ATOM   3580  N N   . SER A  1  510 ? -37.009 -4.135  57.175  1.00 64.63  ?  510  SER A N   1 
ATOM   3581  C CA  . SER A  1  510 ? -37.472 -5.503  57.003  1.00 65.20  ?  510  SER A CA  1 
ATOM   3582  C C   . SER A  1  510 ? -38.672 -5.574  56.058  1.00 67.45  ?  510  SER A C   1 
ATOM   3583  O O   . SER A  1  510 ? -39.355 -4.581  55.798  1.00 69.20  ?  510  SER A O   1 
ATOM   3584  C CB  . SER A  1  510 ? -37.840 -6.112  58.355  1.00 67.85  ?  510  SER A CB  1 
ATOM   3585  O OG  . SER A  1  510 ? -38.869 -5.366  58.972  1.00 72.13  ?  510  SER A OG  1 
ATOM   3586  N N   . SER A  1  511 ? -38.914 -6.780  55.538  1.00 66.26  ?  511  SER A N   1 
ATOM   3587  C CA  . SER A  1  511 ? -40.091 -7.082  54.719  1.00 68.16  ?  511  SER A CA  1 
ATOM   3588  C C   . SER A  1  511 ? -40.178 -6.174  53.494  1.00 66.92  ?  511  SER A C   1 
ATOM   3589  O O   . SER A  1  511 ? -41.215 -5.582  53.197  1.00 68.87  ?  511  SER A O   1 
ATOM   3590  C CB  . SER A  1  511 ? -41.369 -6.998  55.555  1.00 71.94  ?  511  SER A CB  1 
ATOM   3591  O OG  . SER A  1  511 ? -41.417 -8.056  56.496  1.00 72.69  ?  511  SER A OG  1 
ATOM   3592  N N   . ASN A  1  512 ? -39.065 -6.071  52.775  1.00 68.58  ?  512  ASN A N   1 
ATOM   3593  C CA  . ASN A  1  512 ? -38.995 -5.293  51.546  1.00 67.39  ?  512  ASN A CA  1 
ATOM   3594  C C   . ASN A  1  512 ? -38.300 -6.103  50.460  1.00 65.44  ?  512  ASN A C   1 
ATOM   3595  O O   . ASN A  1  512 ? -38.070 -7.306  50.626  1.00 65.28  ?  512  ASN A O   1 
ATOM   3596  C CB  . ASN A  1  512 ? -38.276 -3.963  51.779  1.00 65.86  ?  512  ASN A CB  1 
ATOM   3597  C CG  . ASN A  1  512 ? -39.209 -2.877  52.284  1.00 68.50  ?  512  ASN A CG  1 
ATOM   3598  O OD1 . ASN A  1  512 ? -39.876 -2.199  51.502  1.00 69.26  ?  512  ASN A OD1 1 
ATOM   3599  N ND2 . ASN A  1  512 ? -39.255 -2.706  53.599  1.00 70.24  ?  512  ASN A ND2 1 
ATOM   3600  N N   . ARG A  1  513 ? -37.982 -5.464  49.339  1.00 69.80  ?  513  ARG A N   1 
ATOM   3601  C CA  . ARG A  1  513 ? -37.335 -6.118  48.209  1.00 68.83  ?  513  ARG A CA  1 
ATOM   3602  C C   . ARG A  1  513 ? -35.986 -5.476  47.900  1.00 66.41  ?  513  ARG A C   1 
ATOM   3603  O O   . ARG A  1  513 ? -35.643 -5.236  46.743  1.00 66.54  ?  513  ARG A O   1 
ATOM   3604  C CB  . ARG A  1  513 ? -38.240 -6.091  46.981  1.00 70.99  ?  513  ARG A CB  1 
ATOM   3605  C CG  . ARG A  1  513 ? -39.546 -6.837  47.172  1.00 73.70  ?  513  ARG A CG  1 
ATOM   3606  C CD  . ARG A  1  513 ? -39.296 -8.272  47.610  1.00 73.52  ?  513  ARG A CD  1 
ATOM   3607  N NE  . ARG A  1  513 ? -40.100 -9.216  46.839  1.00 76.08  ?  513  ARG A NE  1 
ATOM   3608  C CZ  . ARG A  1  513 ? -39.961 -10.536 46.878  1.00 76.62  ?  513  ARG A CZ  1 
ATOM   3609  N NH1 . ARG A  1  513 ? -39.053 -11.113 47.652  1.00 74.68  ?  513  ARG A NH1 1 
ATOM   3610  N NH2 . ARG A  1  513 ? -40.753 -11.295 46.123  1.00 79.33  ?  513  ARG A NH2 1 
ATOM   3611  N N   . ILE A  1  514 ? -35.203 -5.198  48.938  1.00 63.97  ?  514  ILE A N   1 
ATOM   3612  C CA  . ILE A  1  514 ? -33.913 -4.535  48.781  1.00 62.10  ?  514  ILE A CA  1 
ATOM   3613  C C   . ILE A  1  514 ? -32.866 -5.557  48.355  1.00 61.11  ?  514  ILE A C   1 
ATOM   3614  O O   . ILE A  1  514 ? -32.833 -6.688  48.857  1.00 60.81  ?  514  ILE A O   1 
ATOM   3615  C CB  . ILE A  1  514 ? -33.510 -3.821  50.087  1.00 60.96  ?  514  ILE A CB  1 
ATOM   3616  C CG1 . ILE A  1  514 ? -34.577 -2.798  50.497  1.00 62.70  ?  514  ILE A CG1 1 
ATOM   3617  C CG2 . ILE A  1  514 ? -32.148 -3.151  49.953  1.00 59.59  ?  514  ILE A CG2 1 
ATOM   3618  C CD1 . ILE A  1  514 ? -34.873 -2.787  51.985  1.00 63.32  ?  514  ILE A CD1 1 
ATOM   3619  N N   . THR A  1  515 ? -31.999 -5.154  47.426  1.00 58.51  ?  515  THR A N   1 
ATOM   3620  C CA  . THR A  1  515 ? -30.991 -6.004  46.803  1.00 58.51  ?  515  THR A CA  1 
ATOM   3621  C C   . THR A  1  515 ? -29.593 -5.462  47.111  1.00 57.83  ?  515  THR A C   1 
ATOM   3622  O O   . THR A  1  515 ? -29.423 -4.516  47.887  1.00 57.19  ?  515  THR A O   1 
ATOM   3623  C CB  . THR A  1  515 ? -31.222 -6.102  45.294  1.00 60.94  ?  515  THR A CB  1 
ATOM   3624  O OG1 . THR A  1  515 ? -31.287 -4.785  44.740  1.00 61.74  ?  515  THR A OG1 1 
ATOM   3625  C CG2 . THR A  1  515 ? -32.510 -6.843  44.984  1.00 63.96  ?  515  THR A CG2 1 
ATOM   3626  N N   . GLY A  1  516 ? -28.587 -6.079  46.497  1.00 61.20  ?  516  GLY A N   1 
ATOM   3627  C CA  . GLY A  1  516 ? -27.204 -5.761  46.791  1.00 61.53  ?  516  GLY A CA  1 
ATOM   3628  C C   . GLY A  1  516 ? -26.691 -6.543  47.980  1.00 60.66  ?  516  GLY A C   1 
ATOM   3629  O O   . GLY A  1  516 ? -27.352 -7.439  48.508  1.00 59.65  ?  516  GLY A O   1 
ATOM   3630  N N   . GLU A  1  517 ? -25.477 -6.199  48.406  1.00 62.84  ?  517  GLU A N   1 
ATOM   3631  C CA  . GLU A  1  517 ? -24.857 -6.870  49.538  1.00 62.79  ?  517  GLU A CA  1 
ATOM   3632  C C   . GLU A  1  517 ? -24.359 -5.852  50.555  1.00 63.05  ?  517  GLU A C   1 
ATOM   3633  O O   . GLU A  1  517 ? -24.053 -4.707  50.216  1.00 64.16  ?  517  GLU A O   1 
ATOM   3634  C CB  . GLU A  1  517 ? -23.711 -7.797  49.092  1.00 65.05  ?  517  GLU A CB  1 
ATOM   3635  C CG  . GLU A  1  517 ? -22.615 -7.194  48.242  1.00 67.79  ?  517  GLU A CG  1 
ATOM   3636  C CD  . GLU A  1  517 ? -21.609 -8.259  47.817  1.00 70.04  ?  517  GLU A CD  1 
ATOM   3637  O OE1 . GLU A  1  517 ? -20.729 -8.615  48.633  1.00 72.07  ?  517  GLU A OE1 1 
ATOM   3638  O OE2 . GLU A  1  517 ? -21.706 -8.760  46.676  1.00 70.07  -1 517  GLU A OE2 1 
ATOM   3639  N N   . LEU A  1  518 ? -24.298 -6.282  51.812  1.00 60.74  ?  518  LEU A N   1 
ATOM   3640  C CA  . LEU A  1  518 ? -23.912 -5.383  52.896  1.00 60.72  ?  518  LEU A CA  1 
ATOM   3641  C C   . LEU A  1  518 ? -22.410 -5.130  52.861  1.00 64.25  ?  518  LEU A C   1 
ATOM   3642  O O   . LEU A  1  518 ? -21.626 -6.087  52.851  1.00 66.09  ?  518  LEU A O   1 
ATOM   3643  C CB  . LEU A  1  518 ? -24.313 -5.973  54.242  1.00 58.77  ?  518  LEU A CB  1 
ATOM   3644  C CG  . LEU A  1  518 ? -25.575 -5.391  54.872  1.00 56.28  ?  518  LEU A CG  1 
ATOM   3645  C CD1 . LEU A  1  518 ? -26.757 -5.546  53.936  1.00 55.55  ?  518  LEU A CD1 1 
ATOM   3646  C CD2 . LEU A  1  518 ? -25.850 -6.071  56.197  1.00 55.12  ?  518  LEU A CD2 1 
ATOM   3647  N N   . PRO A  1  519 ? -21.970 -3.876  52.846  1.00 61.39  ?  519  PRO A N   1 
ATOM   3648  C CA  . PRO A  1  519 ? -20.537 -3.585  52.758  1.00 65.63  ?  519  PRO A CA  1 
ATOM   3649  C C   . PRO A  1  519 ? -19.837 -3.791  54.095  1.00 66.37  ?  519  PRO A C   1 
ATOM   3650  O O   . PRO A  1  519 ? -20.461 -4.002  55.133  1.00 63.46  ?  519  PRO A O   1 
ATOM   3651  C CB  . PRO A  1  519 ? -20.514 -2.111  52.354  1.00 67.09  ?  519  PRO A CB  1 
ATOM   3652  C CG  . PRO A  1  519 ? -21.720 -1.556  53.005  1.00 63.98  ?  519  PRO A CG  1 
ATOM   3653  C CD  . PRO A  1  519 ? -22.771 -2.642  52.925  1.00 60.22  ?  519  PRO A CD  1 
ATOM   3654  N N   . GLU A  1  520 ? -18.506 -3.733  54.047  1.00 68.91  ?  520  GLU A N   1 
ATOM   3655  C CA  . GLU A  1  520 ? -17.720 -3.717  55.272  1.00 69.68  ?  520  GLU A CA  1 
ATOM   3656  C C   . GLU A  1  520 ? -17.755 -2.365  55.970  1.00 69.93  ?  520  GLU A C   1 
ATOM   3657  O O   . GLU A  1  520 ? -17.351 -2.275  57.133  1.00 69.34  ?  520  GLU A O   1 
ATOM   3658  C CB  . GLU A  1  520 ? -16.270 -4.117  54.982  1.00 72.86  ?  520  GLU A CB  1 
ATOM   3659  C CG  . GLU A  1  520 ? -16.095 -5.581  54.564  1.00 72.38  ?  520  GLU A CG  1 
ATOM   3660  C CD  . GLU A  1  520 ? -16.336 -6.567  55.707  1.00 69.64  ?  520  GLU A CD  1 
ATOM   3661  O OE1 . GLU A  1  520 ? -16.774 -6.126  56.790  1.00 68.01  ?  520  GLU A OE1 1 
ATOM   3662  O OE2 . GLU A  1  520 ? -16.089 -7.783  55.524  1.00 69.39  -1 520  GLU A OE2 1 
ATOM   3663  N N   . SER A  1  521 ? -18.231 -1.320  55.295  1.00 69.18  ?  521  SER A N   1 
ATOM   3664  C CA  . SER A  1  521 ? -18.505 -0.039  55.932  1.00 69.44  ?  521  SER A CA  1 
ATOM   3665  C C   . SER A  1  521 ? -19.663 -0.109  56.923  1.00 65.24  ?  521  SER A C   1 
ATOM   3666  O O   . SER A  1  521 ? -19.951 0.897   57.584  1.00 65.47  ?  521  SER A O   1 
ATOM   3667  C CB  . SER A  1  521 ? -18.791 1.015   54.863  1.00 71.19  ?  521  SER A CB  1 
ATOM   3668  O OG  . SER A  1  521 ? -18.989 2.288   55.446  1.00 72.10  ?  521  SER A OG  1 
ATOM   3669  N N   . ILE A  1  522 ? -20.335 -1.261  57.023  1.00 71.74  ?  522  ILE A N   1 
ATOM   3670  C CA  . ILE A  1  522 ? -21.413 -1.514  57.977  1.00 67.77  ?  522  ILE A CA  1 
ATOM   3671  C C   . ILE A  1  522 ? -20.971 -1.146  59.388  1.00 67.77  ?  522  ILE A C   1 
ATOM   3672  O O   . ILE A  1  522 ? -21.801 -0.829  60.245  1.00 65.49  ?  522  ILE A O   1 
ATOM   3673  C CB  . ILE A  1  522 ? -21.866 -2.989  57.908  1.00 65.04  ?  522  ILE A CB  1 
ATOM   3674  C CG1 . ILE A  1  522 ? -23.304 -3.161  58.407  1.00 61.46  ?  522  ILE A CG1 1 
ATOM   3675  C CG2 . ILE A  1  522 ? -20.910 -3.903  58.675  1.00 65.77  ?  522  ILE A CG2 1 
ATOM   3676  C CD1 . ILE A  1  522 ? -24.267 -2.228  57.781  1.00 61.04  ?  522  ILE A CD1 1 
ATOM   3677  N N   . SER A  1  523 ? -19.660 -1.173  59.634  1.00 70.50  ?  523  SER A N   1 
ATOM   3678  C CA  . SER A  1  523 ? -19.115 -0.913  60.958  1.00 70.16  ?  523  SER A CA  1 
ATOM   3679  C C   . SER A  1  523 ? -19.277 0.537   61.404  1.00 70.51  ?  523  SER A C   1 
ATOM   3680  O O   . SER A  1  523 ? -19.097 0.822   62.593  1.00 69.59  ?  523  SER A O   1 
ATOM   3681  C CB  . SER A  1  523 ? -17.638 -1.305  60.978  1.00 72.82  ?  523  SER A CB  1 
ATOM   3682  O OG  . SER A  1  523 ? -17.101 -1.178  62.277  1.00 72.41  ?  523  SER A OG  1 
ATOM   3683  N N   . ASN A  1  524 ? -19.634 1.448   60.494  1.00 68.81  ?  524  ASN A N   1 
ATOM   3684  C CA  . ASN A  1  524 ? -19.668 2.883   60.770  1.00 69.35  ?  524  ASN A CA  1 
ATOM   3685  C C   . ASN A  1  524 ? -20.794 3.308   61.705  1.00 66.33  ?  524  ASN A C   1 
ATOM   3686  O O   . ASN A  1  524 ? -20.787 4.459   62.160  1.00 66.54  ?  524  ASN A O   1 
ATOM   3687  C CB  . ASN A  1  524 ? -19.800 3.656   59.463  1.00 71.72  ?  524  ASN A CB  1 
ATOM   3688  C CG  . ASN A  1  524 ? -18.474 3.939   58.828  1.00 75.17  ?  524  ASN A CG  1 
ATOM   3689  O OD1 . ASN A  1  524 ? -17.461 3.345   59.198  1.00 75.93  ?  524  ASN A OD1 1 
ATOM   3690  N ND2 . ASN A  1  524 ? -18.463 4.847   57.859  1.00 76.94  ?  524  ASN A ND2 1 
ATOM   3691  N N   . ILE A  1  525 ? -21.744 2.422   62.005  1.00 69.85  ?  525  ILE A N   1 
ATOM   3692  C CA  . ILE A  1  525 ? -22.978 2.783   62.698  1.00 67.48  ?  525  ILE A CA  1 
ATOM   3693  C C   . ILE A  1  525 ? -22.988 2.171   64.093  1.00 65.96  ?  525  ILE A C   1 
ATOM   3694  O O   . ILE A  1  525 ? -24.052 1.834   64.622  1.00 64.17  ?  525  ILE A O   1 
ATOM   3695  C CB  . ILE A  1  525 ? -24.232 2.367   61.905  1.00 66.08  ?  525  ILE A CB  1 
ATOM   3696  C CG1 . ILE A  1  525 ? -24.116 0.933   61.398  1.00 65.40  ?  525  ILE A CG1 1 
ATOM   3697  C CG2 . ILE A  1  525 ? -24.477 3.325   60.755  1.00 67.79  ?  525  ILE A CG2 1 
ATOM   3698  C CD1 . ILE A  1  525 ? -25.298 0.506   60.555  1.00 64.17  ?  525  ILE A CD1 1 
ATOM   3699  N N   . ASN A  1  526 ? -21.799 2.017   64.687  1.00 69.59  ?  526  ASN A N   1 
ATOM   3700  C CA  . ASN A  1  526 ? -21.617 1.225   65.903  1.00 68.76  ?  526  ASN A CA  1 
ATOM   3701  C C   . ASN A  1  526 ? -22.556 1.619   67.044  1.00 67.65  ?  526  ASN A C   1 
ATOM   3702  O O   . ASN A  1  526 ? -22.710 0.847   67.998  1.00 66.99  ?  526  ASN A O   1 
ATOM   3703  C CB  . ASN A  1  526 ? -20.164 1.344   66.376  1.00 70.82  ?  526  ASN A CB  1 
ATOM   3704  C CG  . ASN A  1  526 ? -19.817 2.746   66.832  1.00 72.18  ?  526  ASN A CG  1 
ATOM   3705  O OD1 . ASN A  1  526 ? -20.510 3.708   66.501  1.00 71.99  ?  526  ASN A OD1 1 
ATOM   3706  N ND2 . ASN A  1  526 ? -18.745 2.869   67.609  1.00 73.72  ?  526  ASN A ND2 1 
ATOM   3707  N N   . ARG A  1  527 ? -23.188 2.793   66.972  1.00 70.45  ?  527  ARG A N   1 
ATOM   3708  C CA  . ARG A  1  527 ? -24.190 3.174   67.960  1.00 69.99  ?  527  ARG A CA  1 
ATOM   3709  C C   . ARG A  1  527 ? -25.481 2.374   67.836  1.00 68.54  ?  527  ARG A C   1 
ATOM   3710  O O   . ARG A  1  527 ? -26.377 2.544   68.669  1.00 68.71  ?  527  ARG A O   1 
ATOM   3711  C CB  . ARG A  1  527 ? -24.508 4.664   67.834  1.00 71.13  ?  527  ARG A CB  1 
ATOM   3712  C CG  . ARG A  1  527 ? -23.489 5.587   68.480  1.00 72.93  ?  527  ARG A CG  1 
ATOM   3713  C CD  . ARG A  1  527 ? -23.980 7.033   68.474  1.00 74.12  ?  527  ARG A CD  1 
ATOM   3714  N NE  . ARG A  1  527 ? -22.885 7.994   68.572  1.00 76.04  ?  527  ARG A NE  1 
ATOM   3715  C CZ  . ARG A  1  527 ? -22.419 8.489   69.713  1.00 77.35  ?  527  ARG A CZ  1 
ATOM   3716  N NH1 . ARG A  1  527 ? -22.929 8.131   70.882  1.00 78.40  ?  527  ARG A NH1 1 
ATOM   3717  N NH2 . ARG A  1  527 ? -21.414 9.363   69.679  1.00 80.82  ?  527  ARG A NH2 1 
ATOM   3718  N N   . ILE A  1  528 ? -25.605 1.519   66.820  1.00 67.32  ?  528  ILE A N   1 
ATOM   3719  C CA  . ILE A  1  528 ? -26.844 0.783   66.602  1.00 66.40  ?  528  ILE A CA  1 
ATOM   3720  C C   . ILE A  1  528 ? -27.051 -0.243  67.713  1.00 66.17  ?  528  ILE A C   1 
ATOM   3721  O O   . ILE A  1  528 ? -26.094 -0.782  68.285  1.00 66.20  ?  528  ILE A O   1 
ATOM   3722  C CB  . ILE A  1  528 ? -26.817 0.116   65.212  1.00 65.69  ?  528  ILE A CB  1 
ATOM   3723  C CG1 . ILE A  1  528 ? -28.197 -0.419  64.835  1.00 65.42  ?  528  ILE A CG1 1 
ATOM   3724  C CG2 . ILE A  1  528 ? -25.752 -0.980  65.136  1.00 65.39  ?  528  ILE A CG2 1 
ATOM   3725  C CD1 . ILE A  1  528 ? -28.574 -0.127  63.410  1.00 65.58  ?  528  ILE A CD1 1 
ATOM   3726  N N   . SER A  1  529 ? -28.320 -0.502  68.041  1.00 65.71  ?  529  SER A N   1 
ATOM   3727  C CA  . SER A  1  529 ? -28.661 -1.531  69.017  1.00 66.03  ?  529  SER A CA  1 
ATOM   3728  C C   . SER A  1  529 ? -29.733 -2.474  68.480  1.00 66.51  ?  529  SER A C   1 
ATOM   3729  O O   . SER A  1  529 ? -29.834 -3.624  68.921  1.00 66.83  ?  529  SER A O   1 
ATOM   3730  C CB  . SER A  1  529 ? -29.119 -0.890  70.327  1.00 67.26  ?  529  SER A CB  1 
ATOM   3731  O OG  . SER A  1  529 ? -30.189 0.006   70.097  1.00 68.37  ?  529  SER A OG  1 
ATOM   3732  N N   . LYS A  1  530 ? -30.546 -1.992  67.542  1.00 61.19  ?  530  LYS A N   1 
ATOM   3733  C CA  . LYS A  1  530 ? -31.531 -2.809  66.842  1.00 62.54  ?  530  LYS A CA  1 
ATOM   3734  C C   . LYS A  1  530 ? -31.267 -2.707  65.347  1.00 61.58  ?  530  LYS A C   1 
ATOM   3735  O O   . LYS A  1  530 ? -31.266 -1.603  64.791  1.00 61.46  ?  530  LYS A O   1 
ATOM   3736  C CB  . LYS A  1  530 ? -32.960 -2.367  67.169  1.00 65.53  ?  530  LYS A CB  1 
ATOM   3737  C CG  . LYS A  1  530 ? -33.757 -3.385  67.977  1.00 67.76  ?  530  LYS A CG  1 
ATOM   3738  C CD  . LYS A  1  530 ? -35.199 -2.929  68.197  1.00 71.34  ?  530  LYS A CD  1 
ATOM   3739  C CE  . LYS A  1  530 ? -36.014 -3.962  68.982  1.00 73.78  ?  530  LYS A CE  1 
ATOM   3740  N NZ  . LYS A  1  530 ? -37.488 -3.749  68.858  1.00 77.93  ?  530  LYS A NZ  1 
ATOM   3741  N N   . LEU A  1  531 ? -31.050 -3.851  64.699  1.00 58.53  ?  531  LEU A N   1 
ATOM   3742  C CA  . LEU A  1  531 ? -30.759 -3.906  63.268  1.00 57.50  ?  531  LEU A CA  1 
ATOM   3743  C C   . LEU A  1  531 ? -31.670 -4.952  62.642  1.00 59.52  ?  531  LEU A C   1 
ATOM   3744  O O   . LEU A  1  531 ? -31.476 -6.153  62.854  1.00 59.97  ?  531  LEU A O   1 
ATOM   3745  C CB  . LEU A  1  531 ? -29.285 -4.240  63.018  1.00 55.38  ?  531  LEU A CB  1 
ATOM   3746  C CG  . LEU A  1  531 ? -28.603 -3.648  61.783  1.00 54.53  ?  531  LEU A CG  1 
ATOM   3747  C CD1 . LEU A  1  531 ? -27.182 -4.148  61.681  1.00 54.15  ?  531  LEU A CD1 1 
ATOM   3748  C CD2 . LEU A  1  531 ? -29.355 -3.987  60.532  1.00 54.88  ?  531  LEU A CD2 1 
ATOM   3749  N N   . GLN A  1  532 ? -32.650 -4.505  61.862  1.00 54.73  ?  532  GLN A N   1 
ATOM   3750  C CA  . GLN A  1  532 ? -33.644 -5.397  61.270  1.00 57.75  ?  532  GLN A CA  1 
ATOM   3751  C C   . GLN A  1  532 ? -33.612 -5.223  59.757  1.00 56.88  ?  532  GLN A C   1 
ATOM   3752  O O   . GLN A  1  532 ? -34.262 -4.324  59.219  1.00 58.98  ?  532  GLN A O   1 
ATOM   3753  C CB  . GLN A  1  532 ? -35.032 -5.114  61.828  1.00 62.81  ?  532  GLN A CB  1 
ATOM   3754  C CG  . GLN A  1  532 ? -35.129 -5.200  63.338  1.00 63.90  ?  532  GLN A CG  1 
ATOM   3755  C CD  . GLN A  1  532 ? -36.368 -4.514  63.880  1.00 68.42  ?  532  GLN A CD  1 
ATOM   3756  O OE1 . GLN A  1  532 ? -36.275 -3.587  64.684  1.00 67.15  ?  532  GLN A OE1 1 
ATOM   3757  N NE2 . GLN A  1  532 ? -37.539 -4.969  63.444  1.00 73.55  ?  532  GLN A NE2 1 
ATOM   3758  N N   . LEU A  1  533 ? -32.852 -6.084  59.079  1.00 57.65  ?  533  LEU A N   1 
ATOM   3759  C CA  . LEU A  1  533 ? -32.811 -6.137  57.621  1.00 56.98  ?  533  LEU A CA  1 
ATOM   3760  C C   . LEU A  1  533 ? -33.435 -7.410  57.064  1.00 58.55  ?  533  LEU A C   1 
ATOM   3761  O O   . LEU A  1  533 ? -33.264 -7.702  55.876  1.00 57.79  ?  533  LEU A O   1 
ATOM   3762  C CB  . LEU A  1  533 ? -31.372 -6.003  57.122  1.00 53.79  ?  533  LEU A CB  1 
ATOM   3763  C CG  . LEU A  1  533 ? -30.677 -4.671  57.392  1.00 52.73  ?  533  LEU A CG  1 
ATOM   3764  C CD1 . LEU A  1  533 ? -29.268 -4.680  56.835  1.00 51.44  ?  533  LEU A CD1 1 
ATOM   3765  C CD2 . LEU A  1  533 ? -31.472 -3.510  56.822  1.00 54.52  ?  533  LEU A CD2 1 
ATOM   3766  N N   . ASN A  1  534 ? -34.156 -8.165  57.888  1.00 57.84  ?  534  ASN A N   1 
ATOM   3767  C CA  . ASN A  1  534 ? -34.689 -9.461  57.498  1.00 59.35  ?  534  ASN A CA  1 
ATOM   3768  C C   . ASN A  1  534 ? -35.727 -9.329  56.384  1.00 61.56  ?  534  ASN A C   1 
ATOM   3769  O O   . ASN A  1  534 ? -36.286 -8.259  56.136  1.00 62.99  ?  534  ASN A O   1 
ATOM   3770  C CB  . ASN A  1  534 ? -35.317 -10.166 58.704  1.00 61.92  ?  534  ASN A CB  1 
ATOM   3771  C CG  . ASN A  1  534 ? -36.320 -9.290  59.445  1.00 65.29  ?  534  ASN A CG  1 
ATOM   3772  O OD1 . ASN A  1  534 ? -35.984 -8.209  59.929  1.00 64.82  ?  534  ASN A OD1 1 
ATOM   3773  N ND2 . ASN A  1  534 ? -37.560 -9.757  59.529  1.00 68.81  ?  534  ASN A ND2 1 
ATOM   3774  N N   . GLY A  1  535 ? -35.981 -10.447 55.708  1.00 60.32  ?  535  GLY A N   1 
ATOM   3775  C CA  . GLY A  1  535 ? -37.015 -10.496 54.693  1.00 62.63  ?  535  GLY A CA  1 
ATOM   3776  C C   . GLY A  1  535 ? -36.752 -9.628  53.480  1.00 61.12  ?  535  GLY A C   1 
ATOM   3777  O O   . GLY A  1  535 ? -37.602 -8.821  53.090  1.00 62.90  ?  535  GLY A O   1 
ATOM   3778  N N   . ASN A  1  536 ? -35.582 -9.795  52.869  1.00 63.15  ?  536  ASN A N   1 
ATOM   3779  C CA  . ASN A  1  536 ? -35.173 -8.994  51.724  1.00 61.83  ?  536  ASN A CA  1 
ATOM   3780  C C   . ASN A  1  536 ? -34.467 -9.913  50.736  1.00 61.07  ?  536  ASN A C   1 
ATOM   3781  O O   . ASN A  1  536 ? -34.497 -11.140 50.874  1.00 61.81  ?  536  ASN A O   1 
ATOM   3782  C CB  . ASN A  1  536 ? -34.279 -7.829  52.167  1.00 59.57  ?  536  ASN A CB  1 
ATOM   3783  C CG  . ASN A  1  536 ? -35.070 -6.592  52.513  1.00 61.02  ?  536  ASN A CG  1 
ATOM   3784  O OD1 . ASN A  1  536 ? -35.579 -5.905  51.633  1.00 61.93  ?  536  ASN A OD1 1 
ATOM   3785  N ND2 . ASN A  1  536 ? -35.173 -6.296  53.801  1.00 61.63  ?  536  ASN A ND2 1 
ATOM   3786  N N   . ARG A  1  537 ? -33.821 -9.313  49.733  1.00 63.42  ?  537  ARG A N   1 
ATOM   3787  C CA  . ARG A  1  537 ? -33.048 -10.047 48.737  1.00 63.31  ?  537  ARG A CA  1 
ATOM   3788  C C   . ARG A  1  537 ? -31.568 -9.675  48.800  1.00 61.47  ?  537  ARG A C   1 
ATOM   3789  O O   . ARG A  1  537 ? -30.871 -9.680  47.782  1.00 61.83  ?  537  ARG A O   1 
ATOM   3790  C CB  . ARG A  1  537 ? -33.611 -9.809  47.335  1.00 64.99  ?  537  ARG A CB  1 
ATOM   3791  C CG  . ARG A  1  537 ? -35.130 -9.820  47.287  1.00 67.22  ?  537  ARG A CG  1 
ATOM   3792  C CD  . ARG A  1  537 ? -35.660 -10.494 46.032  1.00 69.45  ?  537  ARG A CD  1 
ATOM   3793  N NE  . ARG A  1  537 ? -35.631 -9.598  44.883  1.00 69.85  ?  537  ARG A NE  1 
ATOM   3794  C CZ  . ARG A  1  537 ? -35.679 -9.998  43.619  1.00 72.23  ?  537  ARG A CZ  1 
ATOM   3795  N NH1 . ARG A  1  537 ? -35.789 -11.278 43.302  1.00 75.98  ?  537  ARG A NH1 1 
ATOM   3796  N NH2 . ARG A  1  537 ? -35.608 -9.092  42.646  1.00 74.16  ?  537  ARG A NH2 1 
ATOM   3797  N N   . LEU A  1  538 ? -31.078 -9.366  50.001  1.00 61.14  ?  538  LEU A N   1 
ATOM   3798  C CA  . LEU A  1  538 ? -29.666 -9.060  50.186  1.00 60.10  ?  538  LEU A CA  1 
ATOM   3799  C C   . LEU A  1  538 ? -28.815 -10.298 49.936  1.00 60.69  ?  538  LEU A C   1 
ATOM   3800  O O   . LEU A  1  538 ? -29.148 -11.402 50.374  1.00 60.99  ?  538  LEU A O   1 
ATOM   3801  C CB  . LEU A  1  538 ? -29.415 -8.523  51.594  1.00 58.84  ?  538  LEU A CB  1 
ATOM   3802  C CG  . LEU A  1  538 ? -30.144 -7.229  51.956  1.00 58.52  ?  538  LEU A CG  1 
ATOM   3803  C CD1 . LEU A  1  538 ? -30.081 -6.979  53.456  1.00 57.62  ?  538  LEU A CD1 1 
ATOM   3804  C CD2 . LEU A  1  538 ? -29.572 -6.049  51.182  1.00 58.73  ?  538  LEU A CD2 1 
ATOM   3805  N N   . SER A  1  539 ? -27.689 -10.096 49.253  1.00 63.51  ?  539  SER A N   1 
ATOM   3806  C CA  . SER A  1  539 ? -26.872 -11.183 48.728  1.00 64.76  ?  539  SER A CA  1 
ATOM   3807  C C   . SER A  1  539 ? -25.424 -11.048 49.186  1.00 65.62  ?  539  SER A C   1 
ATOM   3808  O O   . SER A  1  539 ? -25.124 -10.264 50.094  1.00 65.25  ?  539  SER A O   1 
ATOM   3809  C CB  . SER A  1  539 ? -26.959 -11.232 47.198  1.00 66.06  ?  539  SER A CB  1 
ATOM   3810  O OG  . SER A  1  539 ? -26.927 -9.935  46.625  1.00 66.21  ?  539  SER A OG  1 
ATOM   3811  N N   . GLY A  1  540 ? -24.535 -11.863 48.613  1.00 64.92  ?  540  GLY A N   1 
ATOM   3812  C CA  . GLY A  1  540 ? -23.127 -11.836 48.955  1.00 66.89  ?  540  GLY A CA  1 
ATOM   3813  C C   . GLY A  1  540 ? -22.887 -12.363 50.360  1.00 66.88  ?  540  GLY A C   1 
ATOM   3814  O O   . GLY A  1  540 ? -23.735 -13.019 50.965  1.00 65.21  ?  540  GLY A O   1 
ATOM   3815  N N   . LYS A  1  541 ? -21.705 -12.064 50.884  1.00 64.30  ?  541  LYS A N   1 
ATOM   3816  C CA  . LYS A  1  541 ? -21.354 -12.558 52.206  1.00 65.00  ?  541  LYS A CA  1 
ATOM   3817  C C   . LYS A  1  541 ? -21.719 -11.532 53.274  1.00 64.68  ?  541  LYS A C   1 
ATOM   3818  O O   . LYS A  1  541 ? -21.838 -10.332 53.010  1.00 64.23  ?  541  LYS A O   1 
ATOM   3819  C CB  . LYS A  1  541 ? -19.863 -12.904 52.282  1.00 68.17  ?  541  LYS A CB  1 
ATOM   3820  C CG  . LYS A  1  541 ? -18.963 -11.753 52.704  1.00 70.33  ?  541  LYS A CG  1 
ATOM   3821  C CD  . LYS A  1  541 ? -17.497 -12.156 52.675  1.00 72.06  ?  541  LYS A CD  1 
ATOM   3822  C CE  . LYS A  1  541 ? -16.958 -12.166 51.251  1.00 74.68  ?  541  LYS A CE  1 
ATOM   3823  N NZ  . LYS A  1  541 ? -15.557 -12.669 51.185  1.00 76.18  ?  541  LYS A NZ  1 
ATOM   3824  N N   . ILE A  1  542 ? -21.908 -12.029 54.493  1.00 67.51  ?  542  ILE A N   1 
ATOM   3825  C CA  . ILE A  1  542 ? -22.186 -11.176 55.645  1.00 65.41  ?  542  ILE A CA  1 
ATOM   3826  C C   . ILE A  1  542 ? -20.890 -10.466 56.015  1.00 65.80  ?  542  ILE A C   1 
ATOM   3827  O O   . ILE A  1  542 ? -19.877 -11.133 56.264  1.00 66.98  ?  542  ILE A O   1 
ATOM   3828  C CB  . ILE A  1  542 ? -22.745 -11.987 56.825  1.00 63.66  ?  542  ILE A CB  1 
ATOM   3829  C CG1 . ILE A  1  542 ? -24.141 -12.519 56.492  1.00 62.50  ?  542  ILE A CG1 1 
ATOM   3830  C CG2 . ILE A  1  542 ? -22.768 -11.145 58.090  1.00 61.51  ?  542  ILE A CG2 1 
ATOM   3831  C CD1 . ILE A  1  542 ? -24.694 -13.453 57.530  1.00 61.68  ?  542  ILE A CD1 1 
ATOM   3832  N N   . PRO A  1  543 ? -20.864 -9.136  56.049  1.00 66.25  ?  543  PRO A N   1 
ATOM   3833  C CA  . PRO A  1  543 ? -19.609 -8.437  56.345  1.00 68.12  ?  543  PRO A CA  1 
ATOM   3834  C C   . PRO A  1  543 ? -19.133 -8.731  57.758  1.00 67.34  ?  543  PRO A C   1 
ATOM   3835  O O   . PRO A  1  543 ? -19.928 -8.834  58.693  1.00 64.79  ?  543  PRO A O   1 
ATOM   3836  C CB  . PRO A  1  543 ? -19.976 -6.960  56.170  1.00 67.97  ?  543  PRO A CB  1 
ATOM   3837  C CG  . PRO A  1  543 ? -21.447 -6.910  56.383  1.00 64.44  ?  543  PRO A CG  1 
ATOM   3838  C CD  . PRO A  1  543 ? -21.985 -8.205  55.848  1.00 64.22  ?  543  PRO A CD  1 
ATOM   3839  N N   . SER A  1  544 ? -17.817 -8.881  57.907  1.00 72.24  ?  544  SER A N   1 
ATOM   3840  C CA  . SER A  1  544 ? -17.245 -9.060  59.235  1.00 72.08  ?  544  SER A CA  1 
ATOM   3841  C C   . SER A  1  544 ? -17.248 -7.773  60.048  1.00 72.12  ?  544  SER A C   1 
ATOM   3842  O O   . SER A  1  544 ? -16.898 -7.808  61.232  1.00 71.79  ?  544  SER A O   1 
ATOM   3843  C CB  . SER A  1  544 ? -15.821 -9.604  59.127  1.00 74.97  ?  544  SER A CB  1 
ATOM   3844  O OG  . SER A  1  544 ? -14.927 -8.600  58.686  1.00 78.18  ?  544  SER A OG  1 
ATOM   3845  N N   . GLY A  1  545 ? -17.613 -6.644  59.436  1.00 74.16  ?  545  GLY A N   1 
ATOM   3846  C CA  . GLY A  1  545 ? -17.751 -5.396  60.165  1.00 73.75  ?  545  GLY A CA  1 
ATOM   3847  C C   . GLY A  1  545 ? -18.840 -5.417  61.215  1.00 70.06  ?  545  GLY A C   1 
ATOM   3848  O O   . GLY A  1  545 ? -18.878 -4.529  62.074  1.00 69.70  ?  545  GLY A O   1 
ATOM   3849  N N   . ILE A  1  546 ? -19.739 -6.405  61.158  1.00 72.32  ?  546  ILE A N   1 
ATOM   3850  C CA  . ILE A  1  546 ? -20.729 -6.588  62.210  1.00 69.70  ?  546  ILE A CA  1 
ATOM   3851  C C   . ILE A  1  546 ? -20.057 -6.871  63.548  1.00 70.18  ?  546  ILE A C   1 
ATOM   3852  O O   . ILE A  1  546 ? -20.664 -6.660  64.605  1.00 68.88  ?  546  ILE A O   1 
ATOM   3853  C CB  . ILE A  1  546 ? -21.712 -7.716  61.818  1.00 68.15  ?  546  ILE A CB  1 
ATOM   3854  C CG1 . ILE A  1  546 ? -22.270 -7.479  60.413  1.00 68.02  ?  546  ILE A CG1 1 
ATOM   3855  C CG2 . ILE A  1  546 ? -22.860 -7.807  62.803  1.00 66.38  ?  546  ILE A CG2 1 
ATOM   3856  C CD1 . ILE A  1  546 ? -23.175 -6.285  60.315  1.00 66.77  ?  546  ILE A CD1 1 
ATOM   3857  N N   . ARG A  1  547 ? -18.805 -7.336  63.529  1.00 71.93  ?  547  ARG A N   1 
ATOM   3858  C CA  . ARG A  1  547 ? -18.084 -7.586  64.773  1.00 72.66  ?  547  ARG A CA  1 
ATOM   3859  C C   . ARG A  1  547 ? -17.994 -6.330  65.633  1.00 72.81  ?  547  ARG A C   1 
ATOM   3860  O O   . ARG A  1  547 ? -18.066 -6.407  66.866  1.00 72.31  ?  547  ARG A O   1 
ATOM   3861  C CB  . ARG A  1  547 ? -16.686 -8.122  64.470  1.00 75.47  ?  547  ARG A CB  1 
ATOM   3862  C CG  . ARG A  1  547 ? -15.671 -7.814  65.564  1.00 77.12  ?  547  ARG A CG  1 
ATOM   3863  C CD  . ARG A  1  547 ? -14.257 -8.152  65.145  1.00 80.39  ?  547  ARG A CD  1 
ATOM   3864  N NE  . ARG A  1  547 ? -14.088 -8.058  63.700  1.00 81.89  ?  547  ARG A NE  1 
ATOM   3865  C CZ  . ARG A  1  547 ? -13.511 -7.040  63.077  1.00 84.23  ?  547  ARG A CZ  1 
ATOM   3866  N NH1 . ARG A  1  547 ? -13.012 -6.014  63.747  1.00 84.93  ?  547  ARG A NH1 1 
ATOM   3867  N NH2 . ARG A  1  547 ? -13.431 -7.054  61.748  1.00 85.95  ?  547  ARG A NH2 1 
ATOM   3868  N N   . LEU A  1  548 ? -17.861 -5.165  65.004  1.00 70.37  ?  548  LEU A N   1 
ATOM   3869  C CA  . LEU A  1  548 ? -17.558 -3.927  65.712  1.00 71.06  ?  548  LEU A CA  1 
ATOM   3870  C C   . LEU A  1  548 ? -18.798 -3.155  66.154  1.00 68.90  ?  548  LEU A C   1 
ATOM   3871  O O   . LEU A  1  548 ? -18.661 -2.063  66.717  1.00 69.44  ?  548  LEU A O   1 
ATOM   3872  C CB  . LEU A  1  548 ? -16.678 -3.032  64.838  1.00 73.67  ?  548  LEU A CB  1 
ATOM   3873  C CG  . LEU A  1  548 ? -15.280 -3.583  64.568  1.00 76.53  ?  548  LEU A CG  1 
ATOM   3874  C CD1 . LEU A  1  548 ? -14.544 -2.709  63.567  1.00 79.21  ?  548  LEU A CD1 1 
ATOM   3875  C CD2 . LEU A  1  548 ? -14.503 -3.700  65.868  1.00 77.23  ?  548  LEU A CD2 1 
ATOM   3876  N N   . LEU A  1  549 ? -19.996 -3.689  65.921  1.00 72.21  ?  549  LEU A N   1 
ATOM   3877  C CA  . LEU A  1  549 ? -21.234 -3.052  66.374  1.00 70.48  ?  549  LEU A CA  1 
ATOM   3878  C C   . LEU A  1  549 ? -21.583 -3.573  67.772  1.00 69.83  ?  549  LEU A C   1 
ATOM   3879  O O   . LEU A  1  549 ? -22.522 -4.340  67.982  1.00 68.61  ?  549  LEU A O   1 
ATOM   3880  C CB  . LEU A  1  549 ? -22.352 -3.303  65.367  1.00 68.99  ?  549  LEU A CB  1 
ATOM   3881  C CG  . LEU A  1  549 ? -21.967 -3.128  63.893  1.00 69.99  ?  549  LEU A CG  1 
ATOM   3882  C CD1 . LEU A  1  549 ? -23.063 -3.622  62.954  1.00 68.46  ?  549  LEU A CD1 1 
ATOM   3883  C CD2 . LEU A  1  549 ? -21.629 -1.676  63.600  1.00 71.53  ?  549  LEU A CD2 1 
ATOM   3884  N N   . THR A  1  550 ? -20.784 -3.136  68.749  1.00 74.03  ?  550  THR A N   1 
ATOM   3885  C CA  . THR A  1  550 ? -20.826 -3.760  70.069  1.00 74.08  ?  550  THR A CA  1 
ATOM   3886  C C   . THR A  1  550 ? -22.127 -3.475  70.814  1.00 73.05  ?  550  THR A C   1 
ATOM   3887  O O   . THR A  1  550 ? -22.573 -4.314  71.608  1.00 72.85  ?  550  THR A O   1 
ATOM   3888  C CB  . THR A  1  550 ? -19.631 -3.302  70.903  1.00 75.98  ?  550  THR A CB  1 
ATOM   3889  O OG1 . THR A  1  550 ? -19.661 -1.876  71.042  1.00 76.52  ?  550  THR A OG1 1 
ATOM   3890  C CG2 . THR A  1  550 ? -18.332 -3.715  70.232  1.00 77.58  ?  550  THR A CG2 1 
ATOM   3891  N N   . ASN A  1  551 ? -22.753 -2.305  70.580  1.00 76.13  ?  551  ASN A N   1 
ATOM   3892  C CA  . ASN A  1  551 ? -23.968 -1.892  71.302  1.00 75.81  ?  551  ASN A CA  1 
ATOM   3893  C C   . ASN A  1  551 ? -25.223 -2.627  70.842  1.00 74.79  ?  551  ASN A C   1 
ATOM   3894  O O   . ASN A  1  551 ? -26.335 -2.319  71.304  1.00 75.01  ?  551  ASN A O   1 
ATOM   3895  C CB  . ASN A  1  551 ? -24.176 -0.382  71.161  1.00 76.30  ?  551  ASN A CB  1 
ATOM   3896  C CG  . ASN A  1  551 ? -23.461 0.407   72.242  1.00 77.84  ?  551  ASN A CG  1 
ATOM   3897  O OD1 . ASN A  1  551 ? -22.286 0.750   72.106  1.00 78.74  ?  551  ASN A OD1 1 
ATOM   3898  N ND2 . ASN A  1  551 ? -24.165 0.680   73.336  1.00 78.53  ?  551  ASN A ND2 1 
ATOM   3899  N N   . LEU A  1  552 ? -25.018 -3.609  69.972  1.00 70.64  ?  552  LEU A N   1 
ATOM   3900  C CA  . LEU A  1  552 ? -26.098 -4.294  69.277  1.00 70.02  ?  552  LEU A CA  1 
ATOM   3901  C C   . LEU A  1  552 ? -26.814 -5.262  70.217  1.00 70.61  ?  552  LEU A C   1 
ATOM   3902  O O   . LEU A  1  552 ? -26.181 -6.137  70.818  1.00 70.90  ?  552  LEU A O   1 
ATOM   3903  C CB  . LEU A  1  552 ? -25.503 -5.013  68.072  1.00 69.53  ?  552  LEU A CB  1 
ATOM   3904  C CG  . LEU A  1  552 ? -26.255 -5.847  67.052  1.00 69.19  ?  552  LEU A CG  1 
ATOM   3905  C CD1 . LEU A  1  552 ? -27.284 -5.013  66.329  1.00 68.97  ?  552  LEU A CD1 1 
ATOM   3906  C CD2 . LEU A  1  552 ? -25.209 -6.351  66.082  1.00 69.10  ?  552  LEU A CD2 1 
ATOM   3907  N N   . GLU A  1  553 ? -28.133 -5.101  70.340  1.00 74.11  ?  553  GLU A N   1 
ATOM   3908  C CA  . GLU A  1  553 ? -28.971 -5.968  71.163  1.00 75.32  ?  553  GLU A CA  1 
ATOM   3909  C C   . GLU A  1  553 ? -29.745 -7.002  70.359  1.00 76.09  ?  553  GLU A C   1 
ATOM   3910  O O   . GLU A  1  553 ? -29.989 -8.105  70.861  1.00 76.99  ?  553  GLU A O   1 
ATOM   3911  C CB  . GLU A  1  553 ? -29.984 -5.142  71.964  1.00 76.56  ?  553  GLU A CB  1 
ATOM   3912  C CG  . GLU A  1  553 ? -29.386 -4.192  72.975  1.00 76.49  ?  553  GLU A CG  1 
ATOM   3913  C CD  . GLU A  1  553 ? -30.441 -3.320  73.626  1.00 77.88  ?  553  GLU A CD  1 
ATOM   3914  O OE1 . GLU A  1  553 ? -31.593 -3.789  73.760  1.00 79.23  ?  553  GLU A OE1 1 
ATOM   3915  O OE2 . GLU A  1  553 ? -30.122 -2.170  73.997  1.00 77.98  -1 553  GLU A OE2 1 
ATOM   3916  N N   . TYR A  1  554 ? -30.142 -6.664  69.133  1.00 64.38  ?  554  TYR A N   1 
ATOM   3917  C CA  . TYR A  1  554 ? -31.139 -7.427  68.385  1.00 66.28  ?  554  TYR A CA  1 
ATOM   3918  C C   . TYR A  1  554 ? -30.750 -7.392  66.913  1.00 65.37  ?  554  TYR A C   1 
ATOM   3919  O O   . TYR A  1  554 ? -30.789 -6.328  66.285  1.00 64.58  ?  554  TYR A O   1 
ATOM   3920  C CB  . TYR A  1  554 ? -32.539 -6.841  68.616  1.00 68.80  ?  554  TYR A CB  1 
ATOM   3921  C CG  . TYR A  1  554 ? -33.684 -7.525  67.890  1.00 72.23  ?  554  TYR A CG  1 
ATOM   3922  C CD1 . TYR A  1  554 ? -33.947 -7.252  66.551  1.00 73.31  ?  554  TYR A CD1 1 
ATOM   3923  C CD2 . TYR A  1  554 ? -34.521 -8.416  68.551  1.00 74.70  ?  554  TYR A CD2 1 
ATOM   3924  C CE1 . TYR A  1  554 ? -34.992 -7.861  65.887  1.00 77.59  ?  554  TYR A CE1 1 
ATOM   3925  C CE2 . TYR A  1  554 ? -35.574 -9.030  67.892  1.00 78.25  ?  554  TYR A CE2 1 
ATOM   3926  C CZ  . TYR A  1  554 ? -35.801 -8.747  66.559  1.00 79.93  ?  554  TYR A CZ  1 
ATOM   3927  O OH  . TYR A  1  554 ? -36.839 -9.345  65.882  1.00 82.86  ?  554  TYR A OH  1 
ATOM   3928  N N   . LEU A  1  555 ? -30.373 -8.551  66.368  1.00 65.55  ?  555  LEU A N   1 
ATOM   3929  C CA  . LEU A  1  555 ? -29.958 -8.693  64.976  1.00 64.90  ?  555  LEU A CA  1 
ATOM   3930  C C   . LEU A  1  555 ? -30.919 -9.609  64.233  1.00 68.00  ?  555  LEU A C   1 
ATOM   3931  O O   . LEU A  1  555 ? -31.147 -10.748 64.652  1.00 69.37  ?  555  LEU A O   1 
ATOM   3932  C CB  . LEU A  1  555 ? -28.544 -9.268  64.872  1.00 63.23  ?  555  LEU A CB  1 
ATOM   3933  C CG  . LEU A  1  555 ? -27.429 -8.368  64.347  1.00 61.27  ?  555  LEU A CG  1 
ATOM   3934  C CD1 . LEU A  1  555 ? -26.184 -9.187  64.042  1.00 61.22  ?  555  LEU A CD1 1 
ATOM   3935  C CD2 . LEU A  1  555 ? -27.880 -7.602  63.121  1.00 60.80  ?  555  LEU A CD2 1 
ATOM   3936  N N   . ASP A  1  556 ? -31.452 -9.133  63.116  1.00 63.53  ?  556  ASP A N   1 
ATOM   3937  C CA  . ASP A  1  556 ? -32.332 -9.939  62.279  1.00 64.66  ?  556  ASP A CA  1 
ATOM   3938  C C   . ASP A  1  556 ? -31.882 -9.793  60.835  1.00 62.18  ?  556  ASP A C   1 
ATOM   3939  O O   . ASP A  1  556 ? -32.057 -8.731  60.230  1.00 61.22  ?  556  ASP A O   1 
ATOM   3940  C CB  . ASP A  1  556 ? -33.794 -9.527  62.446  1.00 67.79  ?  556  ASP A CB  1 
ATOM   3941  C CG  . ASP A  1  556 ? -34.753 -10.657 62.135  1.00 69.95  ?  556  ASP A CG  1 
ATOM   3942  O OD1 . ASP A  1  556 ? -34.345 -11.593 61.417  1.00 68.47  ?  556  ASP A OD1 1 
ATOM   3943  O OD2 . ASP A  1  556 ? -35.909 -10.614 62.606  1.00 73.13  -1 556  ASP A OD2 1 
ATOM   3944  N N   . LEU A  1  557 ? -31.298 -10.858 60.288  1.00 63.53  ?  557  LEU A N   1 
ATOM   3945  C CA  . LEU A  1  557 ? -30.868 -10.888 58.896  1.00 61.96  ?  557  LEU A CA  1 
ATOM   3946  C C   . LEU A  1  557 ? -31.545 -12.008 58.120  1.00 63.22  ?  557  LEU A C   1 
ATOM   3947  O O   . LEU A  1  557 ? -31.119 -12.322 57.004  1.00 62.48  ?  557  LEU A O   1 
ATOM   3948  C CB  . LEU A  1  557 ? -29.344 -11.029 58.805  1.00 60.73  ?  557  LEU A CB  1 
ATOM   3949  C CG  . LEU A  1  557 ? -28.479 -9.956  59.469  1.00 59.97  ?  557  LEU A CG  1 
ATOM   3950  C CD1 . LEU A  1  557 ? -27.023 -10.370 59.464  1.00 60.74  ?  557  LEU A CD1 1 
ATOM   3951  C CD2 . LEU A  1  557 ? -28.649 -8.624  58.767  1.00 58.29  ?  557  LEU A CD2 1 
ATOM   3952  N N   . SER A  1  558 ? -32.594 -12.608 58.674  1.00 65.70  ?  558  SER A N   1 
ATOM   3953  C CA  . SER A  1  558 ? -33.152 -13.829 58.120  1.00 67.12  ?  558  SER A CA  1 
ATOM   3954  C C   . SER A  1  558 ? -33.946 -13.543 56.845  1.00 67.99  ?  558  SER A C   1 
ATOM   3955  O O   . SER A  1  558 ? -34.187 -12.393 56.466  1.00 67.72  ?  558  SER A O   1 
ATOM   3956  C CB  . SER A  1  558 ? -34.039 -14.526 59.153  1.00 69.54  ?  558  SER A CB  1 
ATOM   3957  O OG  . SER A  1  558 ? -35.196 -13.760 59.442  1.00 71.69  ?  558  SER A OG  1 
ATOM   3958  N N   . SER A  1  559 ? -34.338 -14.626 56.177  1.00 69.60  ?  559  SER A N   1 
ATOM   3959  C CA  . SER A  1  559 ? -35.120 -14.579 54.942  1.00 71.02  ?  559  SER A CA  1 
ATOM   3960  C C   . SER A  1  559 ? -34.455 -13.678 53.897  1.00 69.01  ?  559  SER A C   1 
ATOM   3961  O O   . SER A  1  559 ? -35.038 -12.718 53.386  1.00 69.56  ?  559  SER A O   1 
ATOM   3962  C CB  . SER A  1  559 ? -36.561 -14.145 55.230  1.00 73.98  ?  559  SER A CB  1 
ATOM   3963  O OG  . SER A  1  559 ? -37.260 -15.150 55.949  1.00 76.19  ?  559  SER A OG  1 
ATOM   3964  N N   . ASN A  1  560 ? -33.209 -14.019 53.578  1.00 68.87  ?  560  ASN A N   1 
ATOM   3965  C CA  . ASN A  1  560 ? -32.388 -13.244 52.659  1.00 67.16  ?  560  ASN A CA  1 
ATOM   3966  C C   . ASN A  1  560 ? -31.604 -14.225 51.799  1.00 67.31  ?  560  ASN A C   1 
ATOM   3967  O O   . ASN A  1  560 ? -31.885 -15.427 51.785  1.00 68.74  ?  560  ASN A O   1 
ATOM   3968  C CB  . ASN A  1  560 ? -31.484 -12.273 53.430  1.00 65.04  ?  560  ASN A CB  1 
ATOM   3969  C CG  . ASN A  1  560 ? -32.099 -10.895 53.572  1.00 64.83  ?  560  ASN A CG  1 
ATOM   3970  O OD1 . ASN A  1  560 ? -32.114 -10.109 52.627  1.00 64.58  ?  560  ASN A OD1 1 
ATOM   3971  N ND2 . ASN A  1  560 ? -32.619 -10.598 54.757  1.00 65.39  ?  560  ASN A ND2 1 
ATOM   3972  N N   . ARG A  1  561 ? -30.611 -13.714 51.071  1.00 66.59  ?  561  ARG A N   1 
ATOM   3973  C CA  . ARG A  1  561 ? -29.821 -14.538 50.163  1.00 67.30  ?  561  ARG A CA  1 
ATOM   3974  C C   . ARG A  1  561 ? -28.329 -14.447 50.469  1.00 66.54  ?  561  ARG A C   1 
ATOM   3975  O O   . ARG A  1  561 ? -27.505 -14.512 49.553  1.00 67.22  ?  561  ARG A O   1 
ATOM   3976  C CB  . ARG A  1  561 ? -30.088 -14.151 48.708  1.00 68.20  ?  561  ARG A CB  1 
ATOM   3977  C CG  . ARG A  1  561 ? -31.560 -13.994 48.372  1.00 69.50  ?  561  ARG A CG  1 
ATOM   3978  C CD  . ARG A  1  561 ? -31.795 -13.975 46.872  1.00 71.06  ?  561  ARG A CD  1 
ATOM   3979  N NE  . ARG A  1  561 ? -31.287 -12.755 46.251  1.00 70.27  ?  561  ARG A NE  1 
ATOM   3980  C CZ  . ARG A  1  561 ? -31.802 -12.192 45.164  1.00 71.45  ?  561  ARG A CZ  1 
ATOM   3981  N NH1 . ARG A  1  561 ? -32.851 -12.714 44.545  1.00 73.52  ?  561  ARG A NH1 1 
ATOM   3982  N NH2 . ARG A  1  561 ? -31.243 -11.083 44.680  1.00 70.90  ?  561  ARG A NH2 1 
ATOM   3983  N N   . PHE A  1  562 ? -27.960 -14.291 51.743  1.00 66.05  ?  562  PHE A N   1 
ATOM   3984  C CA  . PHE A  1  562 ? -26.549 -14.318 52.118  1.00 66.33  ?  562  PHE A CA  1 
ATOM   3985  C C   . PHE A  1  562 ? -25.960 -15.687 51.793  1.00 67.65  ?  562  PHE A C   1 
ATOM   3986  O O   . PHE A  1  562 ? -26.557 -16.719 52.109  1.00 67.95  ?  562  PHE A O   1 
ATOM   3987  C CB  . PHE A  1  562 ? -26.385 -13.990 53.605  1.00 65.76  ?  562  PHE A CB  1 
ATOM   3988  C CG  . PHE A  1  562 ? -26.755 -12.570 53.958  1.00 64.58  ?  562  PHE A CG  1 
ATOM   3989  C CD1 . PHE A  1  562 ? -25.986 -11.506 53.510  1.00 64.86  ?  562  PHE A CD1 1 
ATOM   3990  C CD2 . PHE A  1  562 ? -27.877 -12.298 54.728  1.00 63.70  ?  562  PHE A CD2 1 
ATOM   3991  C CE1 . PHE A  1  562 ? -26.329 -10.199 53.828  1.00 63.73  ?  562  PHE A CE1 1 
ATOM   3992  C CE2 . PHE A  1  562 ? -28.224 -10.994 55.049  1.00 62.66  ?  562  PHE A CE2 1 
ATOM   3993  C CZ  . PHE A  1  562 ? -27.449 -9.945  54.598  1.00 62.37  ?  562  PHE A CZ  1 
ATOM   3994  N N   . SER A  1  563 ? -24.786 -15.700 51.150  1.00 71.86  ?  563  SER A N   1 
ATOM   3995  C CA  . SER A  1  563 ? -24.367 -16.859 50.373  1.00 73.15  ?  563  SER A CA  1 
ATOM   3996  C C   . SER A  1  563 ? -23.132 -17.598 50.879  1.00 74.38  ?  563  SER A C   1 
ATOM   3997  O O   . SER A  1  563 ? -22.910 -18.738 50.450  1.00 75.27  ?  563  SER A O   1 
ATOM   3998  C CB  . SER A  1  563 ? -24.109 -16.448 48.913  1.00 74.00  ?  563  SER A CB  1 
ATOM   3999  O OG  . SER A  1  563 ? -25.321 -16.212 48.212  1.00 73.48  ?  563  SER A OG  1 
ATOM   4000  N N   . PHE A  1  564 ? -22.334 -17.015 51.762  1.00 72.55  ?  564  PHE A N   1 
ATOM   4001  C CA  . PHE A  1  564 ? -21.071 -17.640 52.142  1.00 74.13  ?  564  PHE A CA  1 
ATOM   4002  C C   . PHE A  1  564 ? -21.016 -17.855 53.652  1.00 73.58  ?  564  PHE A C   1 
ATOM   4003  O O   . PHE A  1  564 ? -21.963 -17.559 54.380  1.00 72.12  ?  564  PHE A O   1 
ATOM   4004  C CB  . PHE A  1  564 ? -19.889 -16.809 51.639  1.00 76.18  ?  564  PHE A CB  1 
ATOM   4005  C CG  . PHE A  1  564 ? -19.674 -16.913 50.157  1.00 77.03  ?  564  PHE A CG  1 
ATOM   4006  C CD1 . PHE A  1  564 ? -18.936 -17.956 49.625  1.00 78.17  ?  564  PHE A CD1 1 
ATOM   4007  C CD2 . PHE A  1  564 ? -20.223 -15.980 49.294  1.00 76.59  ?  564  PHE A CD2 1 
ATOM   4008  C CE1 . PHE A  1  564 ? -18.740 -18.063 48.265  1.00 79.00  ?  564  PHE A CE1 1 
ATOM   4009  C CE2 . PHE A  1  564 ? -20.031 -16.081 47.930  1.00 77.34  ?  564  PHE A CE2 1 
ATOM   4010  C CZ  . PHE A  1  564 ? -19.288 -17.124 47.415  1.00 78.61  ?  564  PHE A CZ  1 
ATOM   4011  N N   . GLU A  1  565 ? -19.888 -18.388 54.115  1.00 80.03  ?  565  GLU A N   1 
ATOM   4012  C CA  . GLU A  1  565 ? -19.757 -18.841 55.496  1.00 79.34  ?  565  GLU A CA  1 
ATOM   4013  C C   . GLU A  1  565 ? -19.859 -17.686 56.493  1.00 78.52  ?  565  GLU A C   1 
ATOM   4014  O O   . GLU A  1  565 ? -19.546 -16.533 56.182  1.00 79.09  ?  565  GLU A O   1 
ATOM   4015  C CB  . GLU A  1  565 ? -18.425 -19.569 55.675  1.00 80.63  ?  565  GLU A CB  1 
ATOM   4016  C CG  . GLU A  1  565 ? -17.234 -18.818 55.096  1.00 82.42  ?  565  GLU A CG  1 
ATOM   4017  C CD  . GLU A  1  565 ? -16.867 -19.286 53.695  1.00 83.90  ?  565  GLU A CD  1 
ATOM   4018  O OE1 . GLU A  1  565 ? -17.744 -19.842 52.998  1.00 83.15  ?  565  GLU A OE1 1 
ATOM   4019  O OE2 . GLU A  1  565 ? -15.698 -19.105 53.292  1.00 85.78  -1 565  GLU A OE2 1 
ATOM   4020  N N   . ILE A  1  566 ? -20.299 -18.018 57.708  1.00 74.75  ?  566  ILE A N   1 
ATOM   4021  C CA  . ILE A  1  566 ? -20.499 -17.042 58.792  1.00 73.55  ?  566  ILE A CA  1 
ATOM   4022  C C   . ILE A  1  566 ? -19.152 -16.481 59.229  1.00 74.25  ?  566  ILE A C   1 
ATOM   4023  O O   . ILE A  1  566 ? -18.191 -17.253 59.392  1.00 75.33  ?  566  ILE A O   1 
ATOM   4024  C CB  . ILE A  1  566 ? -21.214 -17.704 59.973  1.00 72.55  ?  566  ILE A CB  1 
ATOM   4025  C CG1 . ILE A  1  566 ? -22.613 -18.154 59.568  1.00 72.22  ?  566  ILE A CG1 1 
ATOM   4026  C CG2 . ILE A  1  566 ? -21.267 -16.761 61.174  1.00 71.45  ?  566  ILE A CG2 1 
ATOM   4027  C CD1 . ILE A  1  566 ? -23.416 -18.756 60.680  1.00 71.81  ?  566  ILE A CD1 1 
ATOM   4028  N N   . PRO A  1  567 ? -19.030 -15.174 59.453  1.00 75.17  ?  567  PRO A N   1 
ATOM   4029  C CA  . PRO A  1  567 ? -17.761 -14.616 59.929  1.00 76.23  ?  567  PRO A CA  1 
ATOM   4030  C C   . PRO A  1  567 ? -17.335 -15.254 61.237  1.00 75.97  ?  567  PRO A C   1 
ATOM   4031  O O   . PRO A  1  567 ? -18.075 -15.207 62.233  1.00 74.45  ?  567  PRO A O   1 
ATOM   4032  C CB  . PRO A  1  567 ? -18.070 -13.121 60.099  1.00 75.56  ?  567  PRO A CB  1 
ATOM   4033  C CG  . PRO A  1  567 ? -19.210 -12.865 59.184  1.00 74.73  ?  567  PRO A CG  1 
ATOM   4034  C CD  . PRO A  1  567 ? -20.029 -14.123 59.191  1.00 74.09  ?  567  PRO A CD  1 
ATOM   4035  N N   . PRO A  1  568 ? -16.151 -15.875 61.269  1.00 80.10  ?  568  PRO A N   1 
ATOM   4036  C CA  . PRO A  1  568 ? -15.684 -16.487 62.522  1.00 80.19  ?  568  PRO A CA  1 
ATOM   4037  C C   . PRO A  1  568 ? -15.359 -15.476 63.588  1.00 80.32  ?  568  PRO A C   1 
ATOM   4038  O O   . PRO A  1  568 ? -15.156 -15.858 64.746  1.00 80.31  ?  568  PRO A O   1 
ATOM   4039  C CB  . PRO A  1  568 ? -14.427 -17.255 62.091  1.00 82.29  ?  568  PRO A CB  1 
ATOM   4040  C CG  . PRO A  1  568 ? -14.017 -16.646 60.770  1.00 83.58  ?  568  PRO A CG  1 
ATOM   4041  C CD  . PRO A  1  568 ? -15.010 -15.580 60.390  1.00 82.36  ?  568  PRO A CD  1 
ATOM   4042  N N   . THR A  1  569 ? -15.321 -14.200 63.229  1.00 83.93  ?  569  THR A N   1 
ATOM   4043  C CA  . THR A  1  569 ? -14.890 -13.123 64.097  1.00 84.64  ?  569  THR A CA  1 
ATOM   4044  C C   . THR A  1  569 ? -16.045 -12.457 64.843  1.00 82.32  ?  569  THR A C   1 
ATOM   4045  O O   . THR A  1  569 ? -15.823 -11.464 65.547  1.00 82.67  ?  569  THR A O   1 
ATOM   4046  C CB  . THR A  1  569 ? -14.128 -12.102 63.252  1.00 86.89  ?  569  THR A CB  1 
ATOM   4047  O OG1 . THR A  1  569 ? -13.908 -10.908 64.005  1.00 87.49  ?  569  THR A OG1 1 
ATOM   4048  C CG2 . THR A  1  569 ? -14.919 -11.777 61.996  1.00 86.02  ?  569  THR A CG2 1 
ATOM   4049  N N   . LEU A  1  570 ? -17.269 -12.977 64.710  1.00 81.78  ?  570  LEU A N   1 
ATOM   4050  C CA  . LEU A  1  570 ? -18.429 -12.457 65.435  1.00 79.82  ?  570  LEU A CA  1 
ATOM   4051  C C   . LEU A  1  570 ? -18.453 -13.111 66.813  1.00 79.70  ?  570  LEU A C   1 
ATOM   4052  O O   . LEU A  1  570 ? -19.174 -14.078 67.071  1.00 79.01  ?  570  LEU A O   1 
ATOM   4053  C CB  . LEU A  1  570 ? -19.715 -12.732 64.662  1.00 78.36  ?  570  LEU A CB  1 
ATOM   4054  C CG  . LEU A  1  570 ? -20.121 -11.741 63.570  1.00 77.96  ?  570  LEU A CG  1 
ATOM   4055  C CD1 . LEU A  1  570 ? -21.388 -12.191 62.864  1.00 77.01  ?  570  LEU A CD1 1 
ATOM   4056  C CD2 . LEU A  1  570 ? -20.321 -10.365 64.163  1.00 77.31  ?  570  LEU A CD2 1 
ATOM   4057  N N   . ASN A  1  571 ? -17.625 -12.574 67.720  1.00 84.13  ?  571  ASN A N   1 
ATOM   4058  C CA  . ASN A  1  571 ? -17.553 -13.119 69.072  1.00 84.36  ?  571  ASN A CA  1 
ATOM   4059  C C   . ASN A  1  571 ? -17.493 -12.038 70.151  1.00 84.52  ?  571  ASN A C   1 
ATOM   4060  O O   . ASN A  1  571 ? -17.146 -12.347 71.298  1.00 86.61  ?  571  ASN A O   1 
ATOM   4061  C CB  . ASN A  1  571 ? -16.355 -14.058 69.229  1.00 86.25  ?  571  ASN A CB  1 
ATOM   4062  C CG  . ASN A  1  571 ? -15.077 -13.471 68.677  1.00 88.33  ?  571  ASN A CG  1 
ATOM   4063  O OD1 . ASN A  1  571 ? -14.842 -12.267 68.773  1.00 88.83  ?  571  ASN A OD1 1 
ATOM   4064  N ND2 . ASN A  1  571 ? -14.234 -14.323 68.100  1.00 89.83  ?  571  ASN A ND2 1 
ATOM   4065  N N   . ASN A  1  572 ? -17.821 -10.788 69.828  1.00 84.94  ?  572  ASN A N   1 
ATOM   4066  C CA  . ASN A  1  572 ? -17.656 -9.671  70.759  1.00 85.36  ?  572  ASN A CA  1 
ATOM   4067  C C   . ASN A  1  572 ? -18.905 -8.792  70.801  1.00 83.62  ?  572  ASN A C   1 
ATOM   4068  O O   . ASN A  1  572 ? -18.840 -7.564  70.700  1.00 83.75  ?  572  ASN A O   1 
ATOM   4069  C CB  . ASN A  1  572 ? -16.420 -8.846  70.420  1.00 87.33  ?  572  ASN A CB  1 
ATOM   4070  C CG  . ASN A  1  572 ? -16.049 -7.882  71.532  1.00 88.90  ?  572  ASN A CG  1 
ATOM   4071  O OD1 . ASN A  1  572 ? -15.758 -8.291  72.658  1.00 92.06  ?  572  ASN A OD1 1 
ATOM   4072  N ND2 . ASN A  1  572 ? -16.068 -6.592  71.221  1.00 88.40  ?  572  ASN A ND2 1 
ATOM   4073  N N   . LEU A  1  573 ? -20.073 -9.412  70.925  1.00 80.73  ?  573  LEU A N   1 
ATOM   4074  C CA  . LEU A  1  573 ? -21.284 -8.618  71.098  1.00 79.52  ?  573  LEU A CA  1 
ATOM   4075  C C   . LEU A  1  573 ? -21.826 -8.775  72.519  1.00 79.76  ?  573  LEU A C   1 
ATOM   4076  O O   . LEU A  1  573 ? -22.712 -9.607  72.760  1.00 79.42  ?  573  LEU A O   1 
ATOM   4077  C CB  . LEU A  1  573 ? -22.336 -9.028  70.069  1.00 78.34  ?  573  LEU A CB  1 
ATOM   4078  C CG  . LEU A  1  573 ? -21.915 -8.940  68.603  1.00 78.21  ?  573  LEU A CG  1 
ATOM   4079  C CD1 . LEU A  1  573 ? -23.099 -9.256  67.711  1.00 77.24  ?  573  LEU A CD1 1 
ATOM   4080  C CD2 . LEU A  1  573 ? -21.346 -7.568  68.282  1.00 78.59  ?  573  LEU A CD2 1 
ATOM   4081  N N   . PRO A  1  574 ? -21.333 -7.990  73.485  1.00 78.89  ?  574  PRO A N   1 
ATOM   4082  C CA  . PRO A  1  574 ? -21.682 -8.234  74.894  1.00 82.80  ?  574  PRO A CA  1 
ATOM   4083  C C   . PRO A  1  574 ? -23.100 -7.841  75.277  1.00 82.09  ?  574  PRO A C   1 
ATOM   4084  O O   . PRO A  1  574 ? -23.450 -7.944  76.458  1.00 86.57  ?  574  PRO A O   1 
ATOM   4085  C CB  . PRO A  1  574 ? -20.658 -7.377  75.650  1.00 87.43  ?  574  PRO A CB  1 
ATOM   4086  C CG  . PRO A  1  574 ? -20.405 -6.240  74.731  1.00 84.08  ?  574  PRO A CG  1 
ATOM   4087  C CD  . PRO A  1  574 ? -20.452 -6.818  73.336  1.00 79.66  ?  574  PRO A CD  1 
ATOM   4088  N N   . ARG A  1  575 ? -23.937 -7.405  74.339  1.00 82.89  ?  575  ARG A N   1 
ATOM   4089  C CA  . ARG A  1  575 ? -25.305 -7.031  74.658  1.00 82.65  ?  575  ARG A CA  1 
ATOM   4090  C C   . ARG A  1  575 ? -26.331 -7.698  73.757  1.00 81.22  ?  575  ARG A C   1 
ATOM   4091  O O   . ARG A  1  575 ? -27.521 -7.384  73.862  1.00 81.61  ?  575  ARG A O   1 
ATOM   4092  C CB  . ARG A  1  575 ? -25.476 -5.507  74.588  1.00 82.25  ?  575  ARG A CB  1 
ATOM   4093  C CG  . ARG A  1  575 ? -24.664 -4.764  75.628  1.00 86.28  ?  575  ARG A CG  1 
ATOM   4094  C CD  . ARG A  1  575 ? -24.821 -3.265  75.489  1.00 85.98  ?  575  ARG A CD  1 
ATOM   4095  N NE  . ARG A  1  575 ? -23.796 -2.552  76.242  1.00 90.82  ?  575  ARG A NE  1 
ATOM   4096  C CZ  . ARG A  1  575 ? -22.590 -2.255  75.776  1.00 90.85  ?  575  ARG A CZ  1 
ATOM   4097  N NH1 . ARG A  1  575 ? -22.229 -2.572  74.542  1.00 86.27  ?  575  ARG A NH1 1 
ATOM   4098  N NH2 . ARG A  1  575 ? -21.726 -1.621  76.565  1.00 96.30  ?  575  ARG A NH2 1 
ATOM   4099  N N   . LEU A  1  576 ? -25.910 -8.598  72.877  1.00 80.59  ?  576  LEU A N   1 
ATOM   4100  C CA  . LEU A  1  576 ? -26.824 -9.246  71.950  1.00 80.53  ?  576  LEU A CA  1 
ATOM   4101  C C   . LEU A  1  576 ? -27.579 -10.359 72.669  1.00 81.63  ?  576  LEU A C   1 
ATOM   4102  O O   . LEU A  1  576 ? -26.963 -11.285 73.208  1.00 81.92  ?  576  LEU A O   1 
ATOM   4103  C CB  . LEU A  1  576 ? -26.047 -9.791  70.753  1.00 79.93  ?  576  LEU A CB  1 
ATOM   4104  C CG  . LEU A  1  576 ? -26.851 -10.228 69.529  1.00 80.02  ?  576  LEU A CG  1 
ATOM   4105  C CD1 . LEU A  1  576 ? -27.224 -9.029  68.657  1.00 79.38  ?  576  LEU A CD1 1 
ATOM   4106  C CD2 . LEU A  1  576 ? -26.080 -11.272 68.724  1.00 80.00  ?  576  LEU A CD2 1 
ATOM   4107  N N   . TYR A  1  577 ? -28.910 -10.264 72.694  1.00 78.10  ?  577  TYR A N   1 
ATOM   4108  C CA  . TYR A  1  577 ? -29.749 -11.347 73.193  1.00 79.55  ?  577  TYR A CA  1 
ATOM   4109  C C   . TYR A  1  577 ? -30.528 -12.052 72.090  1.00 80.56  ?  577  TYR A C   1 
ATOM   4110  O O   . TYR A  1  577 ? -31.242 -13.019 72.380  1.00 82.01  ?  577  TYR A O   1 
ATOM   4111  C CB  . TYR A  1  577 ? -30.714 -10.842 74.283  1.00 80.75  ?  577  TYR A CB  1 
ATOM   4112  C CG  . TYR A  1  577 ? -31.759 -9.831  73.845  1.00 81.60  ?  577  TYR A CG  1 
ATOM   4113  C CD1 . TYR A  1  577 ? -32.937 -10.234 73.226  1.00 83.48  ?  577  TYR A CD1 1 
ATOM   4114  C CD2 . TYR A  1  577 ? -31.580 -8.475  74.084  1.00 80.96  ?  577  TYR A CD2 1 
ATOM   4115  C CE1 . TYR A  1  577 ? -33.894 -9.312  72.834  1.00 84.83  ?  577  TYR A CE1 1 
ATOM   4116  C CE2 . TYR A  1  577 ? -32.531 -7.547  73.697  1.00 81.95  ?  577  TYR A CE2 1 
ATOM   4117  C CZ  . TYR A  1  577 ? -33.686 -7.971  73.072  1.00 83.95  ?  577  TYR A CZ  1 
ATOM   4118  O OH  . TYR A  1  577 ? -34.634 -7.048  72.686  1.00 85.46  ?  577  TYR A OH  1 
ATOM   4119  N N   . TYR A  1  578 ? -30.414 -11.599 70.839  1.00 70.61  ?  578  TYR A N   1 
ATOM   4120  C CA  . TYR A  1  578 ? -31.201 -12.132 69.734  1.00 72.12  ?  578  TYR A CA  1 
ATOM   4121  C C   . TYR A  1  578 ? -30.379 -12.128 68.454  1.00 70.92  ?  578  TYR A C   1 
ATOM   4122  O O   . TYR A  1  578 ? -29.808 -11.099 68.083  1.00 69.42  ?  578  TYR A O   1 
ATOM   4123  C CB  . TYR A  1  578 ? -32.472 -11.306 69.536  1.00 74.05  ?  578  TYR A CB  1 
ATOM   4124  C CG  . TYR A  1  578 ? -33.417 -11.827 68.482  1.00 76.53  ?  578  TYR A CG  1 
ATOM   4125  C CD1 . TYR A  1  578 ? -33.289 -11.450 67.152  1.00 76.65  ?  578  TYR A CD1 1 
ATOM   4126  C CD2 . TYR A  1  578 ? -34.455 -12.673 68.823  1.00 78.73  ?  578  TYR A CD2 1 
ATOM   4127  C CE1 . TYR A  1  578 ? -34.163 -11.913 66.196  1.00 78.83  ?  578  TYR A CE1 1 
ATOM   4128  C CE2 . TYR A  1  578 ? -35.332 -13.139 67.877  1.00 80.78  ?  578  TYR A CE2 1 
ATOM   4129  C CZ  . TYR A  1  578 ? -35.184 -12.758 66.567  1.00 80.72  ?  578  TYR A CZ  1 
ATOM   4130  O OH  . TYR A  1  578 ? -36.066 -13.228 65.629  1.00 82.22  ?  578  TYR A OH  1 
ATOM   4131  N N   . MET A  1  579 ? -30.338 -13.271 67.775  1.00 76.06  ?  579  MET A N   1 
ATOM   4132  C CA  . MET A  1  579 ? -29.667 -13.372 66.483  1.00 75.31  ?  579  MET A CA  1 
ATOM   4133  C C   . MET A  1  579 ? -30.450 -14.347 65.620  1.00 76.97  ?  579  MET A C   1 
ATOM   4134  O O   . MET A  1  579 ? -30.563 -15.524 65.971  1.00 77.51  ?  579  MET A O   1 
ATOM   4135  C CB  . MET A  1  579 ? -28.219 -13.837 66.642  1.00 73.71  ?  579  MET A CB  1 
ATOM   4136  C CG  . MET A  1  579 ? -27.532 -14.148 65.320  1.00 73.38  ?  579  MET A CG  1 
ATOM   4137  S SD  . MET A  1  579 ? -25.836 -14.729 65.499  1.00 72.51  ?  579  MET A SD  1 
ATOM   4138  C CE  . MET A  1  579 ? -24.980 -13.158 65.608  1.00 71.08  ?  579  MET A CE  1 
ATOM   4139  N N   . ASN A  1  580 ? -30.992 -13.863 64.506  1.00 70.01  ?  580  ASN A N   1 
ATOM   4140  C CA  . ASN A  1  580 ? -31.781 -14.682 63.590  1.00 71.01  ?  580  ASN A CA  1 
ATOM   4141  C C   . ASN A  1  580 ? -31.145 -14.615 62.205  1.00 69.53  ?  580  ASN A C   1 
ATOM   4142  O O   . ASN A  1  580 ? -31.124 -13.548 61.580  1.00 68.74  ?  580  ASN A O   1 
ATOM   4143  C CB  . ASN A  1  580 ? -33.233 -14.201 63.561  1.00 73.12  ?  580  ASN A CB  1 
ATOM   4144  C CG  . ASN A  1  580 ? -34.176 -15.209 62.933  1.00 74.52  ?  580  ASN A CG  1 
ATOM   4145  O OD1 . ASN A  1  580 ? -33.746 -16.173 62.302  1.00 73.75  ?  580  ASN A OD1 1 
ATOM   4146  N ND2 . ASN A  1  580 ? -35.473 -14.986 63.100  1.00 76.90  ?  580  ASN A ND2 1 
ATOM   4147  N N   . LEU A  1  581 ? -30.631 -15.756 61.722  1.00 69.66  ?  581  LEU A N   1 
ATOM   4148  C CA  . LEU A  1  581 ? -29.996 -15.855 60.408  1.00 68.57  ?  581  LEU A CA  1 
ATOM   4149  C C   . LEU A  1  581 ? -30.694 -16.882 59.521  1.00 69.51  ?  581  LEU A C   1 
ATOM   4150  O O   . LEU A  1  581 ? -30.079 -17.458 58.624  1.00 69.14  ?  581  LEU A O   1 
ATOM   4151  C CB  . LEU A  1  581 ? -28.512 -16.199 60.542  1.00 67.84  ?  581  LEU A CB  1 
ATOM   4152  C CG  . LEU A  1  581 ? -27.670 -15.405 61.542  1.00 67.32  ?  581  LEU A CG  1 
ATOM   4153  C CD1 . LEU A  1  581 ? -26.221 -15.832 61.478  1.00 67.02  ?  581  LEU A CD1 1 
ATOM   4154  C CD2 . LEU A  1  581 ? -27.782 -13.923 61.279  1.00 66.71  ?  581  LEU A CD2 1 
ATOM   4155  N N   . SER A  1  582 ? -31.979 -17.113 59.761  1.00 74.09  ?  582  SER A N   1 
ATOM   4156  C CA  . SER A  1  582 ? -32.718 -18.182 59.104  1.00 75.61  ?  582  SER A CA  1 
ATOM   4157  C C   . SER A  1  582 ? -32.926 -17.887 57.615  1.00 75.50  ?  582  SER A C   1 
ATOM   4158  O O   . SER A  1  582 ? -32.870 -16.739 57.169  1.00 74.50  ?  582  SER A O   1 
ATOM   4159  C CB  . SER A  1  582 ? -34.061 -18.389 59.814  1.00 77.89  ?  582  SER A CB  1 
ATOM   4160  O OG  . SER A  1  582 ? -35.087 -18.779 58.921  1.00 79.67  ?  582  SER A OG  1 
ATOM   4161  N N   . ARG A  1  583 ? -33.160 -18.953 56.840  1.00 76.07  ?  583  ARG A N   1 
ATOM   4162  C CA  . ARG A  1  583 ? -33.588 -18.845 55.438  1.00 76.77  ?  583  ARG A CA  1 
ATOM   4163  C C   . ARG A  1  583 ? -32.588 -18.053 54.587  1.00 74.69  ?  583  ARG A C   1 
ATOM   4164  O O   . ARG A  1  583 ? -32.883 -16.975 54.062  1.00 74.20  ?  583  ARG A O   1 
ATOM   4165  C CB  . ARG A  1  583 ? -35.000 -18.254 55.342  1.00 78.70  ?  583  ARG A CB  1 
ATOM   4166  C CG  . ARG A  1  583 ? -36.063 -19.128 56.003  1.00 81.33  ?  583  ARG A CG  1 
ATOM   4167  C CD  . ARG A  1  583 ? -37.365 -18.364 56.245  1.00 83.42  ?  583  ARG A CD  1 
ATOM   4168  N NE  . ARG A  1  583 ? -38.418 -19.182 56.847  1.00 86.18  ?  583  ARG A NE  1 
ATOM   4169  C CZ  . ARG A  1  583 ? -38.346 -19.795 58.024  1.00 86.01  ?  583  ARG A CZ  1 
ATOM   4170  N NH1 . ARG A  1  583 ? -37.295 -19.659 58.819  1.00 83.41  ?  583  ARG A NH1 1 
ATOM   4171  N NH2 . ARG A  1  583 ? -39.364 -20.553 58.422  1.00 88.59  ?  583  ARG A NH2 1 
ATOM   4172  N N   . ASN A  1  584 ? -31.389 -18.617 54.463  1.00 75.33  ?  584  ASN A N   1 
ATOM   4173  C CA  . ASN A  1  584 ? -30.288 -18.023 53.713  1.00 73.85  ?  584  ASN A CA  1 
ATOM   4174  C C   . ASN A  1  584 ? -29.474 -19.161 53.098  1.00 74.58  ?  584  ASN A C   1 
ATOM   4175  O O   . ASN A  1  584 ? -29.932 -20.305 53.038  1.00 76.13  ?  584  ASN A O   1 
ATOM   4176  C CB  . ASN A  1  584 ? -29.436 -17.136 54.623  1.00 72.19  ?  584  ASN A CB  1 
ATOM   4177  C CG  . ASN A  1  584 ? -30.038 -15.769 54.864  1.00 71.33  ?  584  ASN A CG  1 
ATOM   4178  O OD1 . ASN A  1  584 ? -29.928 -14.874 54.034  1.00 70.59  ?  584  ASN A OD1 1 
ATOM   4179  N ND2 . ASN A  1  584 ? -30.664 -15.597 56.020  1.00 71.68  ?  584  ASN A ND2 1 
ATOM   4180  N N   . ASP A  1  585 ? -28.265 -18.848 52.616  1.00 80.38  ?  585  ASP A N   1 
ATOM   4181  C CA  . ASP A  1  585 ? -27.447 -19.803 51.867  1.00 81.41  ?  585  ASP A CA  1 
ATOM   4182  C C   . ASP A  1  585 ? -26.074 -20.036 52.493  1.00 81.24  ?  585  ASP A C   1 
ATOM   4183  O O   . ASP A  1  585 ? -25.146 -20.453 51.790  1.00 82.10  ?  585  ASP A O   1 
ATOM   4184  C CB  . ASP A  1  585 ? -27.270 -19.336 50.421  1.00 81.78  ?  585  ASP A CB  1 
ATOM   4185  C CG  . ASP A  1  585 ? -28.422 -19.739 49.529  1.00 83.13  ?  585  ASP A CG  1 
ATOM   4186  O OD1 . ASP A  1  585 ? -29.547 -19.908 50.047  1.00 83.47  -1 585  ASP A OD1 1 
ATOM   4187  O OD2 . ASP A  1  585 ? -28.201 -19.883 48.306  1.00 84.25  ?  585  ASP A OD2 1 
ATOM   4188  N N   . LEU A  1  586 ? -25.927 -19.775 53.792  1.00 79.29  ?  586  LEU A N   1 
ATOM   4189  C CA  . LEU A  1  586 ? -24.651 -19.959 54.477  1.00 79.55  ?  586  LEU A CA  1 
ATOM   4190  C C   . LEU A  1  586 ? -24.210 -21.418 54.420  1.00 80.79  ?  586  LEU A C   1 
ATOM   4191  O O   . LEU A  1  586 ? -25.007 -22.335 54.629  1.00 81.26  ?  586  LEU A O   1 
ATOM   4192  C CB  . LEU A  1  586 ? -24.750 -19.467 55.922  1.00 78.75  ?  586  LEU A CB  1 
ATOM   4193  C CG  . LEU A  1  586 ? -25.313 -18.044 56.037  1.00 77.61  ?  586  LEU A CG  1 
ATOM   4194  C CD1 . LEU A  1  586 ? -26.786 -18.052 56.231  1.00 77.22  ?  586  LEU A CD1 1 
ATOM   4195  C CD2 . LEU A  1  586 ? -24.687 -17.268 57.149  1.00 77.31  ?  586  LEU A CD2 1 
ATOM   4196  N N   . ASP A  1  587 ? -22.923 -21.628 54.128  1.00 87.62  ?  587  ASP A N   1 
ATOM   4197  C CA  . ASP A  1  587 ? -22.491 -22.862 53.483  1.00 88.87  ?  587  ASP A CA  1 
ATOM   4198  C C   . ASP A  1  587 ? -21.330 -23.569 54.175  1.00 89.78  ?  587  ASP A C   1 
ATOM   4199  O O   . ASP A  1  587 ? -20.615 -24.332 53.518  1.00 92.35  ?  587  ASP A O   1 
ATOM   4200  C CB  . ASP A  1  587 ? -22.098 -22.572 52.032  1.00 89.63  ?  587  ASP A CB  1 
ATOM   4201  C CG  . ASP A  1  587 ? -20.993 -21.528 51.927  1.00 89.97  ?  587  ASP A CG  1 
ATOM   4202  O OD1 . ASP A  1  587 ? -20.717 -20.842 52.937  1.00 89.48  ?  587  ASP A OD1 1 
ATOM   4203  O OD2 . ASP A  1  587 ? -20.391 -21.399 50.840  1.00 91.03  -1 587  ASP A OD2 1 
ATOM   4204  N N   . GLN A  1  588 ? -21.116 -23.371 55.470  1.00 90.70  ?  588  GLN A N   1 
ATOM   4205  C CA  . GLN A  1  588 ? -20.021 -24.088 56.119  1.00 92.27  ?  588  GLN A CA  1 
ATOM   4206  C C   . GLN A  1  588 ? -20.385 -24.346 57.579  1.00 91.84  ?  588  GLN A C   1 
ATOM   4207  O O   . GLN A  1  588 ? -21.548 -24.235 57.978  1.00 90.72  ?  588  GLN A O   1 
ATOM   4208  C CB  . GLN A  1  588 ? -18.694 -23.337 55.939  1.00 92.28  ?  588  GLN A CB  1 
ATOM   4209  C CG  . GLN A  1  588 ? -17.771 -24.029 54.937  1.00 95.19  ?  588  GLN A CG  1 
ATOM   4210  C CD  . GLN A  1  588 ? -16.564 -23.199 54.539  1.00 95.58  ?  588  GLN A CD  1 
ATOM   4211  O OE1 . GLN A  1  588 ? -16.578 -22.512 53.516  1.00 95.38  ?  588  GLN A OE1 1 
ATOM   4212  N NE2 . GLN A  1  588 ? -15.504 -23.272 55.338  1.00 96.68  ?  588  GLN A NE2 1 
ATOM   4213  N N   . THR A  1  589 ? -19.385 -24.726 58.371  1.00 89.07  ?  589  THR A N   1 
ATOM   4214  C CA  . THR A  1  589 ? -19.606 -25.111 59.757  1.00 89.84  ?  589  THR A CA  1 
ATOM   4215  C C   . THR A  1  589 ? -19.842 -23.887 60.634  1.00 86.70  ?  589  THR A C   1 
ATOM   4216  O O   . THR A  1  589 ? -19.381 -22.782 60.336  1.00 85.11  ?  589  THR A O   1 
ATOM   4217  C CB  . THR A  1  589 ? -18.406 -25.894 60.290  1.00 94.03  ?  589  THR A CB  1 
ATOM   4218  O OG1 . THR A  1  589 ? -17.315 -24.993 60.511  1.00 92.61  ?  589  THR A OG1 1 
ATOM   4219  C CG2 . THR A  1  589 ? -17.978 -26.947 59.292  1.00 98.45  ?  589  THR A CG2 1 
ATOM   4220  N N   . ILE A  1  590 ? -20.575 -24.096 61.724  1.00 85.71  ?  590  ILE A N   1 
ATOM   4221  C CA  . ILE A  1  590 ? -20.874 -23.032 62.679  1.00 83.07  ?  590  ILE A CA  1 
ATOM   4222  C C   . ILE A  1  590 ? -19.570 -22.623 63.353  1.00 83.85  ?  590  ILE A C   1 
ATOM   4223  O O   . ILE A  1  590 ? -18.868 -23.478 63.909  1.00 87.66  ?  590  ILE A O   1 
ATOM   4224  C CB  . ILE A  1  590 ? -21.923 -23.487 63.706  1.00 84.18  ?  590  ILE A CB  1 
ATOM   4225  C CG1 . ILE A  1  590 ? -23.134 -24.095 62.993  1.00 84.67  ?  590  ILE A CG1 1 
ATOM   4226  C CG2 . ILE A  1  590 ? -22.344 -22.329 64.612  1.00 81.65  ?  590  ILE A CG2 1 
ATOM   4227  C CD1 . ILE A  1  590 ? -24.081 -24.823 63.921  1.00 87.64  ?  590  ILE A CD1 1 
ATOM   4228  N N   . PRO A  1  591 ? -19.202 -21.347 63.320  1.00 82.64  ?  591  PRO A N   1 
ATOM   4229  C CA  . PRO A  1  591 ? -17.927 -20.932 63.914  1.00 84.22  ?  591  PRO A CA  1 
ATOM   4230  C C   . PRO A  1  591 ? -17.954 -21.005 65.433  1.00 86.59  ?  591  PRO A C   1 
ATOM   4231  O O   . PRO A  1  591 ? -18.993 -20.818 66.071  1.00 85.40  ?  591  PRO A O   1 
ATOM   4232  C CB  . PRO A  1  591 ? -17.767 -19.488 63.432  1.00 80.08  ?  591  PRO A CB  1 
ATOM   4233  C CG  . PRO A  1  591 ? -19.168 -19.019 63.209  1.00 77.33  ?  591  PRO A CG  1 
ATOM   4234  C CD  . PRO A  1  591 ? -19.937 -20.216 62.729  1.00 77.80  ?  591  PRO A CD  1 
ATOM   4235  N N   . GLU A  1  592 ? -16.781 -21.279 66.012  1.00 89.87  ?  592  GLU A N   1 
ATOM   4236  C CA  . GLU A  1  592 ? -16.661 -21.373 67.463  1.00 92.26  ?  592  GLU A CA  1 
ATOM   4237  C C   . GLU A  1  592 ? -16.833 -20.023 68.151  1.00 90.46  ?  592  GLU A C   1 
ATOM   4238  O O   . GLU A  1  592 ? -17.187 -19.987 69.334  1.00 92.07  ?  592  GLU A O   1 
ATOM   4239  C CB  . GLU A  1  592 ? -15.309 -21.982 67.841  1.00 95.08  ?  592  GLU A CB  1 
ATOM   4240  C CG  . GLU A  1  592 ? -15.309 -22.712 69.179  1.00 98.72  ?  592  GLU A CG  1 
ATOM   4241  C CD  . GLU A  1  592 ? -14.174 -22.273 70.087  1.00 100.24 ?  592  GLU A CD  1 
ATOM   4242  O OE1 . GLU A  1  592 ? -13.393 -21.386 69.678  1.00 98.48  ?  592  GLU A OE1 1 
ATOM   4243  O OE2 . GLU A  1  592 ? -14.070 -22.810 71.213  1.00 103.35 -1 592  GLU A OE2 1 
ATOM   4244  N N   . GLY A  1  593 ? -16.597 -18.917 67.442  1.00 90.98  ?  593  GLY A N   1 
ATOM   4245  C CA  . GLY A  1  593 ? -16.778 -17.598 68.025  1.00 89.33  ?  593  GLY A CA  1 
ATOM   4246  C C   . GLY A  1  593 ? -18.196 -17.301 68.475  1.00 88.64  ?  593  GLY A C   1 
ATOM   4247  O O   . GLY A  1  593 ? -18.397 -16.430 69.329  1.00 88.26  ?  593  GLY A O   1 
ATOM   4248  N N   . LEU A  1  594 ? -19.189 -17.998 67.915  1.00 87.64  ?  594  LEU A N   1 
ATOM   4249  C CA  . LEU A  1  594 ? -20.578 -17.743 68.285  1.00 87.24  ?  594  LEU A CA  1 
ATOM   4250  C C   . LEU A  1  594 ? -20.841 -18.093 69.747  1.00 89.86  ?  594  LEU A C   1 
ATOM   4251  O O   . LEU A  1  594 ? -21.605 -17.400 70.432  1.00 89.47  ?  594  LEU A O   1 
ATOM   4252  C CB  . LEU A  1  594 ? -21.519 -18.526 67.368  1.00 87.75  ?  594  LEU A CB  1 
ATOM   4253  C CG  . LEU A  1  594 ? -22.246 -17.726 66.286  1.00 88.84  ?  594  LEU A CG  1 
ATOM   4254  C CD1 . LEU A  1  594 ? -21.274 -16.798 65.579  1.00 82.66  ?  594  LEU A CD1 1 
ATOM   4255  C CD2 . LEU A  1  594 ? -22.936 -18.647 65.288  1.00 94.44  ?  594  LEU A CD2 1 
ATOM   4256  N N   . THR A  1  595 ? -20.213 -19.161 70.247  1.00 92.98  ?  595  THR A N   1 
ATOM   4257  C CA  . THR A  1  595 ? -20.452 -19.613 71.614  1.00 96.23  ?  595  THR A CA  1 
ATOM   4258  C C   . THR A  1  595 ? -19.906 -18.655 72.667  1.00 96.63  ?  595  THR A C   1 
ATOM   4259  O O   . THR A  1  595 ? -20.124 -18.892 73.861  1.00 99.38  ?  595  THR A O   1 
ATOM   4260  C CB  . THR A  1  595 ? -19.839 -20.998 71.826  1.00 99.68  ?  595  THR A CB  1 
ATOM   4261  O OG1 . THR A  1  595 ? -18.419 -20.873 71.966  1.00 100.40 ?  595  THR A OG1 1 
ATOM   4262  C CG2 . THR A  1  595 ? -20.143 -21.897 70.643  1.00 99.29  ?  595  THR A CG2 1 
ATOM   4263  N N   . LYS A  1  596 ? -19.200 -17.596 72.264  1.00 95.64  ?  596  LYS A N   1 
ATOM   4264  C CA  . LYS A  1  596 ? -18.624 -16.651 73.212  1.00 96.15  ?  596  LYS A CA  1 
ATOM   4265  C C   . LYS A  1  596 ? -19.520 -15.458 73.506  1.00 94.11  ?  596  LYS A C   1 
ATOM   4266  O O   . LYS A  1  596 ? -19.185 -14.659 74.387  1.00 94.82  ?  596  LYS A O   1 
ATOM   4267  C CB  . LYS A  1  596 ? -17.278 -16.132 72.699  1.00 95.09  ?  596  LYS A CB  1 
ATOM   4268  C CG  . LYS A  1  596 ? -16.321 -17.211 72.261  1.00 96.86  ?  596  LYS A CG  1 
ATOM   4269  C CD  . LYS A  1  596 ? -15.019 -16.603 71.776  1.00 95.92  ?  596  LYS A CD  1 
ATOM   4270  C CE  . LYS A  1  596 ? -14.230 -17.604 70.948  1.00 96.85  ?  596  LYS A CE  1 
ATOM   4271  N NZ  . LYS A  1  596 ? -13.010 -16.996 70.354  1.00 95.87  ?  596  LYS A NZ  1 
ATOM   4272  N N   . LEU A  1  597 ? -20.647 -15.320 72.822  1.00 94.24  ?  597  LEU A N   1 
ATOM   4273  C CA  . LEU A  1  597 ? -21.583 -14.245 73.131  1.00 92.55  ?  597  LEU A CA  1 
ATOM   4274  C C   . LEU A  1  597 ? -22.411 -14.740 74.311  1.00 95.59  ?  597  LEU A C   1 
ATOM   4275  O O   . LEU A  1  597 ? -23.289 -15.585 74.157  1.00 96.51  ?  597  LEU A O   1 
ATOM   4276  C CB  . LEU A  1  597 ? -22.446 -13.906 71.922  1.00 89.38  ?  597  LEU A CB  1 
ATOM   4277  C CG  . LEU A  1  597 ? -21.866 -13.948 70.508  1.00 87.25  ?  597  LEU A CG  1 
ATOM   4278  C CD1 . LEU A  1  597 ? -22.835 -13.381 69.479  1.00 84.37  ?  597  LEU A CD1 1 
ATOM   4279  C CD2 . LEU A  1  597 ? -20.609 -13.148 70.490  1.00 86.33  ?  597  LEU A CD2 1 
ATOM   4280  N N   . SER A  1  598 ? -22.076 -14.289 75.519  1.00 93.08  ?  598  SER A N   1 
ATOM   4281  C CA  . SER A  1  598 ? -22.660 -14.903 76.708  1.00 96.67  ?  598  SER A CA  1 
ATOM   4282  C C   . SER A  1  598 ? -24.162 -14.654 76.824  1.00 96.10  ?  598  SER A C   1 
ATOM   4283  O O   . SER A  1  598 ? -24.885 -15.487 77.384  1.00 98.75  ?  598  SER A O   1 
ATOM   4284  C CB  . SER A  1  598 ? -21.934 -14.398 77.954  1.00 99.08  ?  598  SER A CB  1 
ATOM   4285  O OG  . SER A  1  598 ? -21.995 -12.986 78.035  1.00 96.96  ?  598  SER A OG  1 
ATOM   4286  N N   . GLN A  1  599 ? -24.646 -13.523 76.323  1.00 95.51  ?  599  GLN A N   1 
ATOM   4287  C CA  . GLN A  1  599 ? -25.981 -13.041 76.645  1.00 95.24  ?  599  GLN A CA  1 
ATOM   4288  C C   . GLN A  1  599 ? -27.082 -13.480 75.673  1.00 93.78  ?  599  GLN A C   1 
ATOM   4289  O O   . GLN A  1  599 ? -28.213 -13.007 75.819  1.00 95.58  ?  599  GLN A O   1 
ATOM   4290  C CB  . GLN A  1  599 ? -25.969 -11.513 76.749  1.00 92.92  ?  599  GLN A CB  1 
ATOM   4291  C CG  . GLN A  1  599 ? -25.750 -10.988 78.162  1.00 95.65  ?  599  GLN A CG  1 
ATOM   4292  C CD  . GLN A  1  599 ? -24.326 -11.171 78.649  1.00 97.52  ?  599  GLN A CD  1 
ATOM   4293  O OE1 . GLN A  1  599 ? -23.983 -12.200 79.232  1.00 100.73 ?  599  GLN A OE1 1 
ATOM   4294  N NE2 . GLN A  1  599 ? -23.487 -10.167 78.415  1.00 95.64  ?  599  GLN A NE2 1 
ATOM   4295  N N   . LEU A  1  600 ? -26.807 -14.336 74.681  1.00 90.34  ?  600  LEU A N   1 
ATOM   4296  C CA  . LEU A  1  600 ? -27.885 -14.705 73.762  1.00 95.51  ?  600  LEU A CA  1 
ATOM   4297  C C   . LEU A  1  600 ? -29.007 -15.419 74.496  1.00 100.63 ?  600  LEU A C   1 
ATOM   4298  O O   . LEU A  1  600 ? -28.774 -16.295 75.334  1.00 100.98 ?  600  LEU A O   1 
ATOM   4299  C CB  . LEU A  1  600 ? -27.442 -15.615 72.610  1.00 97.15  ?  600  LEU A CB  1 
ATOM   4300  C CG  . LEU A  1  600 ? -26.485 -15.247 71.487  1.00 93.64  ?  600  LEU A CG  1 
ATOM   4301  C CD1 . LEU A  1  600 ? -25.190 -15.521 72.043  1.00 89.32  ?  600  LEU A CD1 1 
ATOM   4302  C CD2 . LEU A  1  600 ? -26.676 -16.110 70.260  1.00 97.76  ?  600  LEU A CD2 1 
ATOM   4303  N N   . GLN A  1  601 ? -30.233 -15.024 74.174  1.00 91.58  ?  601  GLN A N   1 
ATOM   4304  C CA  . GLN A  1  601 ? -31.423 -15.732 74.609  1.00 96.04  ?  601  GLN A CA  1 
ATOM   4305  C C   . GLN A  1  601 ? -32.011 -16.611 73.513  1.00 100.10 ?  601  GLN A C   1 
ATOM   4306  O O   . GLN A  1  601 ? -32.453 -17.730 73.792  1.00 102.14 ?  601  GLN A O   1 
ATOM   4307  C CB  . GLN A  1  601 ? -32.468 -14.726 75.097  1.00 96.69  ?  601  GLN A CB  1 
ATOM   4308  C CG  . GLN A  1  601 ? -33.902 -15.093 74.795  1.00 100.94 ?  601  GLN A CG  1 
ATOM   4309  C CD  . GLN A  1  601 ? -34.874 -14.446 75.760  1.00 101.11 ?  601  GLN A CD  1 
ATOM   4310  O OE1 . GLN A  1  601 ? -34.538 -13.475 76.443  1.00 98.23  ?  601  GLN A OE1 1 
ATOM   4311  N NE2 . GLN A  1  601 ? -36.084 -14.987 75.830  1.00 103.89 ?  601  GLN A NE2 1 
ATOM   4312  N N   . MET A  1  602 ? -32.006 -16.136 72.269  1.00 91.29  ?  602  MET A N   1 
ATOM   4313  C CA  . MET A  1  602 ? -32.527 -16.875 71.129  1.00 94.61  ?  602  MET A CA  1 
ATOM   4314  C C   . MET A  1  602 ? -31.491 -16.887 70.013  1.00 93.38  ?  602  MET A C   1 
ATOM   4315  O O   . MET A  1  602 ? -30.822 -15.878 69.766  1.00 90.63  ?  602  MET A O   1 
ATOM   4316  C CB  . MET A  1  602 ? -33.844 -16.261 70.636  1.00 97.19  ?  602  MET A CB  1 
ATOM   4317  C CG  . MET A  1  602 ? -35.008 -16.475 71.593  1.00 98.18  ?  602  MET A CG  1 
ATOM   4318  S SD  . MET A  1  602 ? -36.360 -15.289 71.393  1.00 98.97  ?  602  MET A SD  1 
ATOM   4319  C CE  . MET A  1  602 ? -37.299 -16.063 70.079  1.00 100.09 ?  602  MET A CE  1 
ATOM   4320  N N   . LEU A  1  603 ? -31.355 -18.036 69.346  1.00 90.28  ?  603  LEU A N   1 
ATOM   4321  C CA  . LEU A  1  603 ? -30.415 -18.198 68.238  1.00 89.06  ?  603  LEU A CA  1 
ATOM   4322  C C   . LEU A  1  603 ? -31.037 -19.130 67.208  1.00 91.52  ?  603  LEU A C   1 
ATOM   4323  O O   . LEU A  1  603 ? -31.222 -20.320 67.480  1.00 91.96  ?  603  LEU A O   1 
ATOM   4324  C CB  . LEU A  1  603 ? -29.076 -18.748 68.726  1.00 85.44  ?  603  LEU A CB  1 
ATOM   4325  C CG  . LEU A  1  603 ? -28.076 -19.112 67.632  1.00 83.73  ?  603  LEU A CG  1 
ATOM   4326  C CD1 . LEU A  1  603 ? -27.484 -17.858 67.014  1.00 80.87  ?  603  LEU A CD1 1 
ATOM   4327  C CD2 . LEU A  1  603 ? -26.986 -19.995 68.203  1.00 83.01  ?  603  LEU A CD2 1 
ATOM   4328  N N   . ASP A  1  604 ? -31.352 -18.597 66.029  1.00 81.44  ?  604  ASP A N   1 
ATOM   4329  C CA  . ASP A  1  604 ? -32.010 -19.352 64.966  1.00 82.15  ?  604  ASP A CA  1 
ATOM   4330  C C   . ASP A  1  604 ? -31.101 -19.374 63.741  1.00 80.75  ?  604  ASP A C   1 
ATOM   4331  O O   . ASP A  1  604 ? -30.870 -18.332 63.118  1.00 80.17  ?  604  ASP A O   1 
ATOM   4332  C CB  . ASP A  1  604 ? -33.372 -18.738 64.637  1.00 82.76  ?  604  ASP A CB  1 
ATOM   4333  C CG  . ASP A  1  604 ? -34.222 -19.627 63.747  1.00 81.58  ?  604  ASP A CG  1 
ATOM   4334  O OD1 . ASP A  1  604 ? -33.709 -20.652 63.248  1.00 80.99  ?  604  ASP A OD1 1 
ATOM   4335  O OD2 . ASP A  1  604 ? -35.410 -19.296 63.543  1.00 80.59  -1 604  ASP A OD2 1 
ATOM   4336  N N   . LEU A  1  605 ? -30.590 -20.560 63.389  1.00 80.00  ?  605  LEU A N   1 
ATOM   4337  C CA  . LEU A  1  605 ? -29.750 -20.733 62.206  1.00 78.64  ?  605  LEU A CA  1 
ATOM   4338  C C   . LEU A  1  605 ? -30.408 -21.627 61.160  1.00 79.87  ?  605  LEU A C   1 
ATOM   4339  O O   . LEU A  1  605 ? -29.716 -22.184 60.303  1.00 80.12  ?  605  LEU A O   1 
ATOM   4340  C CB  . LEU A  1  605 ? -28.380 -21.304 62.586  1.00 80.19  ?  605  LEU A CB  1 
ATOM   4341  C CG  . LEU A  1  605 ? -27.530 -20.556 63.614  1.00 79.56  ?  605  LEU A CG  1 
ATOM   4342  C CD1 . LEU A  1  605 ? -26.205 -21.260 63.842  1.00 81.44  ?  605  LEU A CD1 1 
ATOM   4343  C CD2 . LEU A  1  605 ? -27.289 -19.133 63.169  1.00 75.58  ?  605  LEU A CD2 1 
ATOM   4344  N N   . SER A  1  606 ? -31.729 -21.769 61.209  1.00 88.77  ?  606  SER A N   1 
ATOM   4345  C CA  . SER A  1  606 ? -32.415 -22.790 60.433  1.00 87.69  ?  606  SER A CA  1 
ATOM   4346  C C   . SER A  1  606 ? -32.451 -22.434 58.946  1.00 85.14  ?  606  SER A C   1 
ATOM   4347  O O   . SER A  1  606 ? -32.186 -21.301 58.536  1.00 84.11  ?  606  SER A O   1 
ATOM   4348  C CB  . SER A  1  606 ? -33.836 -22.993 60.956  1.00 87.91  ?  606  SER A CB  1 
ATOM   4349  O OG  . SER A  1  606 ? -34.594 -21.803 60.838  1.00 86.79  ?  606  SER A OG  1 
ATOM   4350  N N   . TYR A  1  607 ? -32.792 -23.440 58.136  1.00 95.02  ?  607  TYR A N   1 
ATOM   4351  C CA  . TYR A  1  607 ? -33.033 -23.271 56.703  1.00 91.89  ?  607  TYR A CA  1 
ATOM   4352  C C   . TYR A  1  607 ? -31.806 -22.697 55.991  1.00 91.57  ?  607  TYR A C   1 
ATOM   4353  O O   . TYR A  1  607 ? -31.825 -21.594 55.442  1.00 89.60  ?  607  TYR A O   1 
ATOM   4354  C CB  . TYR A  1  607 ? -34.277 -22.409 56.458  1.00 88.80  ?  607  TYR A CB  1 
ATOM   4355  C CG  . TYR A  1  607 ? -35.576 -23.125 56.764  1.00 88.06  ?  607  TYR A CG  1 
ATOM   4356  C CD1 . TYR A  1  607 ? -35.882 -23.531 58.059  1.00 90.62  ?  607  TYR A CD1 1 
ATOM   4357  C CD2 . TYR A  1  607 ? -36.499 -23.394 55.761  1.00 84.53  ?  607  TYR A CD2 1 
ATOM   4358  C CE1 . TYR A  1  607 ? -37.065 -24.187 58.346  1.00 89.99  ?  607  TYR A CE1 1 
ATOM   4359  C CE2 . TYR A  1  607 ? -37.687 -24.051 56.039  1.00 83.74  ?  607  TYR A CE2 1 
ATOM   4360  C CZ  . TYR A  1  607 ? -37.963 -24.444 57.334  1.00 86.63  ?  607  TYR A CZ  1 
ATOM   4361  O OH  . TYR A  1  607 ? -39.139 -25.097 57.622  1.00 88.12  ?  607  TYR A OH  1 
ATOM   4362  N N   . ASN A  1  608 ? -30.725 -23.475 56.019  1.00 88.00  ?  608  ASN A N   1 
ATOM   4363  C CA  . ASN A  1  608 ? -29.437 -23.060 55.478  1.00 87.76  ?  608  ASN A CA  1 
ATOM   4364  C C   . ASN A  1  608 ? -28.785 -24.263 54.805  1.00 87.48  ?  608  ASN A C   1 
ATOM   4365  O O   . ASN A  1  608 ? -29.402 -25.319 54.636  1.00 87.41  ?  608  ASN A O   1 
ATOM   4366  C CB  . ASN A  1  608 ? -28.543 -22.511 56.595  1.00 89.15  ?  608  ASN A CB  1 
ATOM   4367  C CG  . ASN A  1  608 ? -28.595 -21.012 56.711  1.00 88.87  ?  608  ASN A CG  1 
ATOM   4368  O OD1 . ASN A  1  608 ? -29.310 -20.330 55.975  1.00 87.38  ?  608  ASN A OD1 1 
ATOM   4369  N ND2 . ASN A  1  608 ? -27.879 -20.490 57.694  1.00 89.41  ?  608  ASN A ND2 1 
ATOM   4370  N N   . GLN A  1  609 ? -27.530 -24.085 54.394  1.00 94.78  ?  609  GLN A N   1 
ATOM   4371  C CA  . GLN A  1  609 ? -26.679 -25.173 53.927  1.00 94.24  ?  609  GLN A CA  1 
ATOM   4372  C C   . GLN A  1  609 ? -25.540 -25.444 54.907  1.00 93.94  ?  609  GLN A C   1 
ATOM   4373  O O   . GLN A  1  609 ? -24.460 -25.888 54.509  1.00 92.24  ?  609  GLN A O   1 
ATOM   4374  C CB  . GLN A  1  609 ? -26.123 -24.862 52.538  1.00 92.62  ?  609  GLN A CB  1 
ATOM   4375  C CG  . GLN A  1  609 ? -27.137 -25.004 51.410  1.00 91.86  ?  609  GLN A CG  1 
ATOM   4376  C CD  . GLN A  1  609 ? -26.719 -24.262 50.147  1.00 90.13  ?  609  GLN A CD  1 
ATOM   4377  O OE1 . GLN A  1  609 ? -25.553 -24.293 49.747  1.00 89.45  ?  609  GLN A OE1 1 
ATOM   4378  N NE2 . GLN A  1  609 ? -27.674 -23.580 49.517  1.00 88.64  ?  609  GLN A NE2 1 
ATOM   4379  N N   . LEU A  1  610 ? -25.767 -25.162 56.189  1.00 91.57  ?  610  LEU A N   1 
ATOM   4380  C CA  . LEU A  1  610 ? -24.752 -25.397 57.207  1.00 91.96  ?  610  LEU A CA  1 
ATOM   4381  C C   . LEU A  1  610 ? -24.400 -26.877 57.274  1.00 96.04  ?  610  LEU A C   1 
ATOM   4382  O O   . LEU A  1  610 ? -25.274 -27.743 57.182  1.00 98.41  ?  610  LEU A O   1 
ATOM   4383  C CB  . LEU A  1  610 ? -25.246 -24.913 58.573  1.00 91.78  ?  610  LEU A CB  1 
ATOM   4384  C CG  . LEU A  1  610 ? -25.446 -23.412 58.802  1.00 91.22  ?  610  LEU A CG  1 
ATOM   4385  C CD1 . LEU A  1  610 ? -25.712 -23.136 60.271  1.00 91.77  ?  610  LEU A CD1 1 
ATOM   4386  C CD2 . LEU A  1  610 ? -24.246 -22.625 58.326  1.00 87.70  ?  610  LEU A CD2 1 
ATOM   4387  N N   . ASP A  1  611 ? -23.109 -27.167 57.425  1.00 105.54 ?  611  ASP A N   1 
ATOM   4388  C CA  . ASP A  1  611 ? -22.652 -28.544 57.578  1.00 104.99 ?  611  ASP A CA  1 
ATOM   4389  C C   . ASP A  1  611 ? -21.704 -28.658 58.766  1.00 102.35 ?  611  ASP A C   1 
ATOM   4390  O O   . ASP A  1  611 ? -21.543 -27.701 59.531  1.00 101.07 ?  611  ASP A O   1 
ATOM   4391  C CB  . ASP A  1  611 ? -21.980 -29.043 56.296  1.00 103.53 ?  611  ASP A CB  1 
ATOM   4392  C CG  . ASP A  1  611 ? -20.627 -28.404 56.055  1.00 99.32  ?  611  ASP A CG  1 
ATOM   4393  O OD1 . ASP A  1  611 ? -20.454 -27.218 56.406  1.00 97.73  ?  611  ASP A OD1 1 
ATOM   4394  O OD2 . ASP A  1  611 ? -19.734 -29.086 55.512  1.00 97.61  -1 611  ASP A OD2 1 
ATOM   4395  N N   . GLY A  1  612 ? -21.084 -29.819 58.938  1.00 104.87 ?  612  GLY A N   1 
ATOM   4396  C CA  . GLY A  1  612 ? -20.195 -30.025 60.061  1.00 105.26 ?  612  GLY A CA  1 
ATOM   4397  C C   . GLY A  1  612 ? -20.930 -30.458 61.312  1.00 107.35 ?  612  GLY A C   1 
ATOM   4398  O O   . GLY A  1  612 ? -22.126 -30.767 61.310  1.00 108.41 ?  612  GLY A O   1 
ATOM   4399  N N   . GLU A  1  613 ? -20.185 -30.470 62.411  1.00 112.82 ?  613  GLU A N   1 
ATOM   4400  C CA  . GLU A  1  613 ? -20.668 -30.999 63.676  1.00 115.33 ?  613  GLU A CA  1 
ATOM   4401  C C   . GLU A  1  613 ? -21.057 -29.876 64.632  1.00 113.48 ?  613  GLU A C   1 
ATOM   4402  O O   . GLU A  1  613 ? -20.510 -28.771 64.583  1.00 110.72 ?  613  GLU A O   1 
ATOM   4403  C CB  . GLU A  1  613 ? -19.608 -31.892 64.323  1.00 118.30 ?  613  GLU A CB  1 
ATOM   4404  C CG  . GLU A  1  613 ? -19.295 -33.148 63.528  1.00 120.95 ?  613  GLU A CG  1 
ATOM   4405  C CD  . GLU A  1  613 ? -18.588 -34.197 64.362  1.00 124.82 ?  613  GLU A CD  1 
ATOM   4406  O OE1 . GLU A  1  613 ? -17.553 -33.866 64.977  1.00 124.90 ?  613  GLU A OE1 1 
ATOM   4407  O OE2 . GLU A  1  613 ? -19.071 -35.349 64.407  1.00 127.91 -1 613  GLU A OE2 1 
ATOM   4408  N N   . ILE A  1  614 ? -22.015 -30.178 65.506  1.00 112.55 ?  614  ILE A N   1 
ATOM   4409  C CA  . ILE A  1  614 ? -22.492 -29.225 66.503  1.00 111.27 ?  614  ILE A CA  1 
ATOM   4410  C C   . ILE A  1  614 ? -21.455 -29.158 67.619  1.00 112.70 ?  614  ILE A C   1 
ATOM   4411  O O   . ILE A  1  614 ? -21.296 -30.109 68.387  1.00 116.17 ?  614  ILE A O   1 
ATOM   4412  C CB  . ILE A  1  614 ? -23.869 -29.620 67.048  1.00 112.95 ?  614  ILE A CB  1 
ATOM   4413  C CG1 . ILE A  1  614 ? -24.761 -30.145 65.919  1.00 114.28 ?  614  ILE A CG1 1 
ATOM   4414  C CG2 . ILE A  1  614 ? -24.521 -28.438 67.748  1.00 112.28 ?  614  ILE A CG2 1 
ATOM   4415  C CD1 . ILE A  1  614 ? -26.233 -30.195 66.265  1.00 116.91 ?  614  ILE A CD1 1 
ATOM   4416  N N   . SER A  1  615 ? -20.745 -28.036 67.705  1.00 114.66 ?  615  SER A N   1 
ATOM   4417  C CA  . SER A  1  615 ? -19.707 -27.883 68.714  1.00 115.75 ?  615  SER A CA  1 
ATOM   4418  C C   . SER A  1  615 ? -20.305 -27.955 70.110  1.00 117.84 ?  615  SER A C   1 
ATOM   4419  O O   . SER A  1  615 ? -21.321 -27.315 70.399  1.00 116.65 ?  615  SER A O   1 
ATOM   4420  C CB  . SER A  1  615 ? -18.977 -26.553 68.531  1.00 112.61 ?  615  SER A CB  1 
ATOM   4421  O OG  . SER A  1  615 ? -18.083 -26.314 69.606  1.00 114.04 ?  615  SER A OG  1 
ATOM   4422  N N   . SER A  1  616 ? -19.664 -28.740 70.978  1.00 120.09 ?  616  SER A N   1 
ATOM   4423  C CA  . SER A  1  616 ? -20.105 -28.871 72.361  1.00 122.53 ?  616  SER A CA  1 
ATOM   4424  C C   . SER A  1  616 ? -19.925 -27.590 73.164  1.00 121.02 ?  616  SER A C   1 
ATOM   4425  O O   . SER A  1  616 ? -20.433 -27.509 74.287  1.00 122.73 ?  616  SER A O   1 
ATOM   4426  C CB  . SER A  1  616 ? -19.353 -30.015 73.041  1.00 126.57 ?  616  SER A CB  1 
ATOM   4427  O OG  . SER A  1  616 ? -20.147 -30.622 74.043  1.00 129.51 ?  616  SER A OG  1 
ATOM   4428  N N   . GLN A  1  617 ? -19.234 -26.588 72.620  1.00 122.09 ?  617  GLN A N   1 
ATOM   4429  C CA  . GLN A  1  617 ? -19.013 -25.348 73.353  1.00 120.79 ?  617  GLN A CA  1 
ATOM   4430  C C   . GLN A  1  617 ? -20.257 -24.476 73.423  1.00 118.59 ?  617  GLN A C   1 
ATOM   4431  O O   . GLN A  1  617 ? -20.213 -23.424 74.073  1.00 117.62 ?  617  GLN A O   1 
ATOM   4432  C CB  . GLN A  1  617 ? -17.851 -24.562 72.736  1.00 118.53 ?  617  GLN A CB  1 
ATOM   4433  C CG  . GLN A  1  617 ? -16.470 -25.234 72.837  1.00 120.91 ?  617  GLN A CG  1 
ATOM   4434  C CD  . GLN A  1  617 ? -16.056 -25.667 74.250  1.00 124.68 ?  617  GLN A CD  1 
ATOM   4435  O OE1 . GLN A  1  617 ? -16.780 -25.478 75.229  1.00 125.73 ?  617  GLN A OE1 1 
ATOM   4436  N NE2 . GLN A  1  617 ? -14.871 -26.260 74.348  1.00 126.89 ?  617  GLN A NE2 1 
ATOM   4437  N N   . PHE A  1  618 ? -21.350 -24.870 72.763  1.00 118.57 ?  618  PHE A N   1 
ATOM   4438  C CA  . PHE A  1  618 ? -22.622 -24.183 72.953  1.00 117.34 ?  618  PHE A CA  1 
ATOM   4439  C C   . PHE A  1  618 ? -23.136 -24.336 74.377  1.00 120.20 ?  618  PHE A C   1 
ATOM   4440  O O   . PHE A  1  618 ? -24.021 -23.580 74.795  1.00 119.42 ?  618  PHE A O   1 
ATOM   4441  C CB  . PHE A  1  618 ? -23.660 -24.703 71.957  1.00 116.99 ?  618  PHE A CB  1 
ATOM   4442  C CG  . PHE A  1  618 ? -23.645 -23.986 70.639  1.00 113.61 ?  618  PHE A CG  1 
ATOM   4443  C CD1 . PHE A  1  618 ? -22.625 -24.204 69.728  1.00 112.38 ?  618  PHE A CD1 1 
ATOM   4444  C CD2 . PHE A  1  618 ? -24.648 -23.089 70.311  1.00 114.90 ?  618  PHE A CD2 1 
ATOM   4445  C CE1 . PHE A  1  618 ? -22.606 -23.541 68.514  1.00 110.34 ?  618  PHE A CE1 1 
ATOM   4446  C CE2 . PHE A  1  618 ? -24.635 -22.424 69.098  1.00 114.78 ?  618  PHE A CE2 1 
ATOM   4447  C CZ  . PHE A  1  618 ? -23.613 -22.650 68.199  1.00 112.03 ?  618  PHE A CZ  1 
ATOM   4448  N N   . ARG A  1  619 ? -22.597 -25.300 75.127  1.00 120.85 ?  619  ARG A N   1 
ATOM   4449  C CA  . ARG A  1  619 ? -22.887 -25.423 76.549  1.00 123.91 ?  619  ARG A CA  1 
ATOM   4450  C C   . ARG A  1  619 ? -22.539 -24.153 77.317  1.00 122.90 ?  619  ARG A C   1 
ATOM   4451  O O   . ARG A  1  619 ? -23.105 -23.915 78.390  1.00 124.69 ?  619  ARG A O   1 
ATOM   4452  C CB  . ARG A  1  619 ? -22.116 -26.620 77.112  1.00 127.74 ?  619  ARG A CB  1 
ATOM   4453  C CG  . ARG A  1  619 ? -22.455 -27.009 78.539  1.00 131.55 ?  619  ARG A CG  1 
ATOM   4454  C CD  . ARG A  1  619 ? -21.262 -27.685 79.207  1.00 134.61 ?  619  ARG A CD  1 
ATOM   4455  N NE  . ARG A  1  619 ? -21.579 -28.165 80.547  1.00 138.55 ?  619  ARG A NE  1 
ATOM   4456  C CZ  . ARG A  1  619 ? -20.760 -28.079 81.588  1.00 140.90 ?  619  ARG A CZ  1 
ATOM   4457  N NH1 . ARG A  1  619 ? -19.561 -27.529 81.480  1.00 139.84 ?  619  ARG A NH1 1 
ATOM   4458  N NH2 . ARG A  1  619 ? -21.154 -28.555 82.766  1.00 144.59 ?  619  ARG A NH2 1 
ATOM   4459  N N   . SER A  1  620 ? -21.630 -23.327 76.788  1.00 122.01 ?  620  SER A N   1 
ATOM   4460  C CA  . SER A  1  620 ? -21.248 -22.086 77.453  1.00 121.08 ?  620  SER A CA  1 
ATOM   4461  C C   . SER A  1  620 ? -22.366 -21.048 77.460  1.00 118.79 ?  620  SER A C   1 
ATOM   4462  O O   . SER A  1  620 ? -22.367 -20.166 78.326  1.00 119.07 ?  620  SER A O   1 
ATOM   4463  C CB  . SER A  1  620 ? -20.002 -21.495 76.790  1.00 118.92 ?  620  SER A CB  1 
ATOM   4464  O OG  . SER A  1  620 ? -18.931 -22.421 76.799  1.00 121.20 ?  620  SER A OG  1 
ATOM   4465  N N   . LEU A  1  621 ? -23.322 -21.137 76.533  1.00 115.08 ?  621  LEU A N   1 
ATOM   4466  C CA  . LEU A  1  621 ? -24.391 -20.143 76.425  1.00 112.88 ?  621  LEU A CA  1 
ATOM   4467  C C   . LEU A  1  621 ? -25.394 -20.397 77.547  1.00 115.79 ?  621  LEU A C   1 
ATOM   4468  O O   . LEU A  1  621 ? -26.427 -21.051 77.376  1.00 116.85 ?  621  LEU A O   1 
ATOM   4469  C CB  . LEU A  1  621 ? -25.052 -20.204 75.054  1.00 110.38 ?  621  LEU A CB  1 
ATOM   4470  C CG  . LEU A  1  621 ? -24.145 -20.027 73.836  1.00 107.65 ?  621  LEU A CG  1 
ATOM   4471  C CD1 . LEU A  1  621 ? -24.952 -20.118 72.553  1.00 107.68 ?  621  LEU A CD1 1 
ATOM   4472  C CD2 . LEU A  1  621 ? -23.405 -18.708 73.909  1.00 105.06 ?  621  LEU A CD2 1 
ATOM   4473  N N   . GLN A  1  622 ? -25.070 -19.860 78.726  1.00 112.87 ?  622  GLN A N   1 
ATOM   4474  C CA  . GLN A  1  622 ? -25.823 -20.174 79.936  1.00 116.34 ?  622  GLN A CA  1 
ATOM   4475  C C   . GLN A  1  622 ? -27.216 -19.558 79.955  1.00 115.35 ?  622  GLN A C   1 
ATOM   4476  O O   . GLN A  1  622 ? -28.078 -20.041 80.695  1.00 118.22 ?  622  GLN A O   1 
ATOM   4477  C CB  . GLN A  1  622 ? -25.039 -19.719 81.166  1.00 118.54 ?  622  GLN A CB  1 
ATOM   4478  C CG  . GLN A  1  622 ? -23.780 -20.530 81.418  1.00 120.79 ?  622  GLN A CG  1 
ATOM   4479  C CD  . GLN A  1  622 ? -23.039 -20.078 82.657  1.00 123.27 ?  622  GLN A CD  1 
ATOM   4480  O OE1 . GLN A  1  622 ? -23.600 -19.394 83.515  1.00 124.25 ?  622  GLN A OE1 1 
ATOM   4481  N NE2 . GLN A  1  622 ? -21.770 -20.459 82.761  1.00 124.51 ?  622  GLN A NE2 1 
ATOM   4482  N N   . ASN A  1  623 ? -27.460 -18.512 79.173  1.00 112.86 ?  623  ASN A N   1 
ATOM   4483  C CA  . ASN A  1  623 ? -28.759 -17.852 79.151  1.00 111.87 ?  623  ASN A CA  1 
ATOM   4484  C C   . ASN A  1  623 ? -29.613 -18.256 77.957  1.00 111.86 ?  623  ASN A C   1 
ATOM   4485  O O   . ASN A  1  623 ? -30.711 -17.717 77.787  1.00 113.83 ?  623  ASN A O   1 
ATOM   4486  C CB  . ASN A  1  623 ? -28.575 -16.331 79.172  1.00 109.02 ?  623  ASN A CB  1 
ATOM   4487  C CG  . ASN A  1  623 ? -27.449 -15.896 80.091  1.00 110.26 ?  623  ASN A CG  1 
ATOM   4488  O OD1 . ASN A  1  623 ? -26.350 -16.449 80.048  1.00 111.07 ?  623  ASN A OD1 1 
ATOM   4489  N ND2 . ASN A  1  623 ? -27.718 -14.903 80.931  1.00 110.72 ?  623  ASN A ND2 1 
ATOM   4490  N N   . LEU A  1  624 ? -29.138 -19.186 77.131  1.00 107.29 ?  624  LEU A N   1 
ATOM   4491  C CA  . LEU A  1  624 ? -29.836 -19.549 75.903  1.00 105.48 ?  624  LEU A CA  1 
ATOM   4492  C C   . LEU A  1  624 ? -31.138 -20.276 76.227  1.00 108.41 ?  624  LEU A C   1 
ATOM   4493  O O   . LEU A  1  624 ? -31.132 -21.302 76.915  1.00 111.88 ?  624  LEU A O   1 
ATOM   4494  C CB  . LEU A  1  624 ? -28.931 -20.418 75.032  1.00 105.17 ?  624  LEU A CB  1 
ATOM   4495  C CG  . LEU A  1  624 ? -29.364 -20.738 73.600  1.00 106.80 ?  624  LEU A CG  1 
ATOM   4496  C CD1 . LEU A  1  624 ? -29.617 -19.461 72.836  1.00 106.99 ?  624  LEU A CD1 1 
ATOM   4497  C CD2 . LEU A  1  624 ? -28.311 -21.581 72.896  1.00 105.25 ?  624  LEU A CD2 1 
ATOM   4498  N N   . GLU A  1  625 ? -32.254 -19.738 75.735  1.00 106.93 ?  625  GLU A N   1 
ATOM   4499  C CA  . GLU A  1  625 ? -33.563 -20.350 75.919  1.00 109.95 ?  625  GLU A CA  1 
ATOM   4500  C C   . GLU A  1  625 ? -34.083 -21.066 74.682  1.00 112.36 ?  625  GLU A C   1 
ATOM   4501  O O   . GLU A  1  625 ? -34.862 -22.014 74.815  1.00 113.85 ?  625  GLU A O   1 
ATOM   4502  C CB  . GLU A  1  625 ? -34.587 -19.291 76.340  1.00 110.48 ?  625  GLU A CB  1 
ATOM   4503  C CG  . GLU A  1  625 ? -34.656 -19.055 77.836  1.00 108.93 ?  625  GLU A CG  1 
ATOM   4504  C CD  . GLU A  1  625 ? -35.343 -17.755 78.184  1.00 108.38 ?  625  GLU A CD  1 
ATOM   4505  O OE1 . GLU A  1  625 ? -36.533 -17.604 77.833  1.00 110.41 ?  625  GLU A OE1 1 
ATOM   4506  O OE2 . GLU A  1  625 ? -34.699 -16.888 78.813  1.00 105.38 -1 625  GLU A OE2 1 
ATOM   4507  N N   . ARG A  1  626 ? -33.672 -20.643 73.486  1.00 107.70 ?  626  ARG A N   1 
ATOM   4508  C CA  . ARG A  1  626 ? -34.193 -21.190 72.240  1.00 109.57 ?  626  ARG A CA  1 
ATOM   4509  C C   . ARG A  1  626 ? -33.057 -21.513 71.282  1.00 108.64 ?  626  ARG A C   1 
ATOM   4510  O O   . ARG A  1  626 ? -32.112 -20.731 71.137  1.00 106.86 ?  626  ARG A O   1 
ATOM   4511  C CB  . ARG A  1  626 ? -35.165 -20.215 71.565  1.00 110.71 ?  626  ARG A CB  1 
ATOM   4512  C CG  . ARG A  1  626 ? -36.447 -19.990 72.339  1.00 111.28 ?  626  ARG A CG  1 
ATOM   4513  C CD  . ARG A  1  626 ? -37.572 -19.516 71.434  1.00 111.80 ?  626  ARG A CD  1 
ATOM   4514  N NE  . ARG A  1  626 ? -38.873 -19.966 71.915  1.00 111.80 ?  626  ARG A NE  1 
ATOM   4515  C CZ  . ARG A  1  626 ? -40.000 -19.277 71.788  1.00 111.13 ?  626  ARG A CZ  1 
ATOM   4516  N NH1 . ARG A  1  626 ? -40.023 -18.093 71.195  1.00 110.53 ?  626  ARG A NH1 1 
ATOM   4517  N NH2 . ARG A  1  626 ? -41.130 -19.787 72.270  1.00 110.67 ?  626  ARG A NH2 1 
ATOM   4518  N N   . LEU A  1  627 ? -33.157 -22.671 70.632  1.00 103.14 ?  627  LEU A N   1 
ATOM   4519  C CA  . LEU A  1  627 ? -32.247 -23.057 69.565  1.00 102.32 ?  627  LEU A CA  1 
ATOM   4520  C C   . LEU A  1  627 ? -33.062 -23.630 68.415  1.00 103.55 ?  627  LEU A C   1 
ATOM   4521  O O   . LEU A  1  627 ? -34.013 -24.384 68.640  1.00 104.35 ?  627  LEU A O   1 
ATOM   4522  C CB  . LEU A  1  627 ? -31.221 -24.093 70.047  1.00 100.62 ?  627  LEU A CB  1 
ATOM   4523  C CG  . LEU A  1  627 ? -29.752 -23.671 70.009  1.00 97.58  ?  627  LEU A CG  1 
ATOM   4524  C CD1 . LEU A  1  627 ? -28.837 -24.877 70.164  1.00 100.18 ?  627  LEU A CD1 1 
ATOM   4525  C CD2 . LEU A  1  627 ? -29.450 -22.907 68.731  1.00 97.32  ?  627  LEU A CD2 1 
ATOM   4526  N N   . ASP A  1  628 ? -32.692 -23.271 67.186  1.00 94.04  ?  628  ASP A N   1 
ATOM   4527  C CA  . ASP A  1  628 ? -33.323 -23.830 65.991  1.00 94.09  ?  628  ASP A CA  1 
ATOM   4528  C C   . ASP A  1  628 ? -32.238 -24.051 64.950  1.00 92.58  ?  628  ASP A C   1 
ATOM   4529  O O   . ASP A  1  628 ? -31.754 -23.090 64.345  1.00 89.58  ?  628  ASP A O   1 
ATOM   4530  C CB  . ASP A  1  628 ? -34.418 -22.911 65.447  1.00 91.70  ?  628  ASP A CB  1 
ATOM   4531  C CG  . ASP A  1  628 ? -35.316 -23.604 64.432  1.00 92.79  ?  628  ASP A CG  1 
ATOM   4532  O OD1 . ASP A  1  628 ? -35.036 -24.768 64.074  1.00 95.21  ?  628  ASP A OD1 1 
ATOM   4533  O OD2 . ASP A  1  628 ? -36.307 -22.983 63.992  1.00 91.37  -1 628  ASP A OD2 1 
ATOM   4534  N N   . LEU A  1  629 ? -31.869 -25.316 64.732  1.00 92.52  ?  629  LEU A N   1 
ATOM   4535  C CA  . LEU A  1  629 ? -30.847 -25.688 63.759  1.00 91.76  ?  629  LEU A CA  1 
ATOM   4536  C C   . LEU A  1  629 ? -31.423 -26.548 62.641  1.00 93.07  ?  629  LEU A C   1 
ATOM   4537  O O   . LEU A  1  629 ? -30.670 -27.211 61.923  1.00 93.73  ?  629  LEU A O   1 
ATOM   4538  C CB  . LEU A  1  629 ? -29.691 -26.427 64.440  1.00 94.04  ?  629  LEU A CB  1 
ATOM   4539  C CG  . LEU A  1  629 ? -28.909 -25.773 65.582  1.00 93.50  ?  629  LEU A CG  1 
ATOM   4540  C CD1 . LEU A  1  629 ? -27.472 -26.250 65.574  1.00 94.31  ?  629  LEU A CD1 1 
ATOM   4541  C CD2 . LEU A  1  629 ? -28.936 -24.268 65.460  1.00 89.52  ?  629  LEU A CD2 1 
ATOM   4542  N N   . SER A  1  630 ? -32.745 -26.553 62.488  1.00 101.03 ?  630  SER A N   1 
ATOM   4543  C CA  . SER A  1  630 ? -33.409 -27.450 61.557  1.00 100.10 ?  630  SER A CA  1 
ATOM   4544  C C   . SER A  1  630 ? -33.109 -27.066 60.113  1.00 98.31  ?  630  SER A C   1 
ATOM   4545  O O   . SER A  1  630 ? -32.663 -25.955 59.815  1.00 97.84  ?  630  SER A O   1 
ATOM   4546  C CB  . SER A  1  630 ? -34.920 -27.443 61.787  1.00 100.02 ?  630  SER A CB  1 
ATOM   4547  O OG  . SER A  1  630 ? -35.479 -26.186 61.451  1.00 99.01  ?  630  SER A OG  1 
ATOM   4548  N N   . HIS A  1  631 ? -33.373 -28.011 59.209  1.00 104.57 ?  631  HIS A N   1 
ATOM   4549  C CA  . HIS A  1  631 ? -33.218 -27.807 57.770  1.00 102.51 ?  631  HIS A CA  1 
ATOM   4550  C C   . HIS A  1  631 ? -31.798 -27.352 57.424  1.00 102.55 ?  631  HIS A C   1 
ATOM   4551  O O   . HIS A  1  631 ? -31.564 -26.249 56.924  1.00 101.62 ?  631  HIS A O   1 
ATOM   4552  C CB  . HIS A  1  631 ? -34.274 -26.828 57.246  1.00 100.38 ?  631  HIS A CB  1 
ATOM   4553  C CG  . HIS A  1  631 ? -35.667 -27.375 57.296  1.00 99.34  ?  631  HIS A CG  1 
ATOM   4554  N ND1 . HIS A  1  631 ? -36.204 -27.934 58.436  1.00 101.30 ?  631  HIS A ND1 1 
ATOM   4555  C CD2 . HIS A  1  631 ? -36.623 -27.475 56.342  1.00 96.27  ?  631  HIS A CD2 1 
ATOM   4556  C CE1 . HIS A  1  631 ? -37.435 -28.343 58.186  1.00 99.69  ?  631  HIS A CE1 1 
ATOM   4557  N NE2 . HIS A  1  631 ? -37.714 -28.077 56.922  1.00 96.50  ?  631  HIS A NE2 1 
ATOM   4558  N N   . ASN A  1  632 ? -30.845 -28.230 57.730  1.00 99.85  ?  632  ASN A N   1 
ATOM   4559  C CA  . ASN A  1  632 ? -29.435 -28.011 57.435  1.00 98.36  ?  632  ASN A CA  1 
ATOM   4560  C C   . ASN A  1  632 ? -28.825 -29.346 57.017  1.00 101.72 ?  632  ASN A C   1 
ATOM   4561  O O   . ASN A  1  632 ? -29.536 -30.324 56.769  1.00 104.76 ?  632  ASN A O   1 
ATOM   4562  C CB  . ASN A  1  632 ? -28.717 -27.406 58.648  1.00 97.30  ?  632  ASN A CB  1 
ATOM   4563  C CG  . ASN A  1  632 ? -28.970 -25.924 58.792  1.00 94.88  ?  632  ASN A CG  1 
ATOM   4564  O OD1 . ASN A  1  632 ? -28.453 -25.124 58.022  1.00 93.86  ?  632  ASN A OD1 1 
ATOM   4565  N ND2 . ASN A  1  632 ? -29.770 -25.550 59.782  1.00 96.13  ?  632  ASN A ND2 1 
ATOM   4566  N N   . ASN A  1  633 ? -27.496 -29.384 56.920  1.00 106.16 ?  633  ASN A N   1 
ATOM   4567  C CA  . ASN A  1  633 ? -26.758 -30.621 56.685  1.00 105.53 ?  633  ASN A CA  1 
ATOM   4568  C C   . ASN A  1  633 ? -25.790 -30.907 57.830  1.00 104.93 ?  633  ASN A C   1 
ATOM   4569  O O   . ASN A  1  633 ? -24.706 -31.452 57.616  1.00 103.33 ?  633  ASN A O   1 
ATOM   4570  C CB  . ASN A  1  633 ? -26.018 -30.575 55.345  1.00 104.09 ?  633  ASN A CB  1 
ATOM   4571  C CG  . ASN A  1  633 ? -25.642 -31.967 54.824  1.00 103.67 ?  633  ASN A CG  1 
ATOM   4572  O OD1 . ASN A  1  633 ? -26.222 -32.976 55.229  1.00 104.62 ?  633  ASN A OD1 1 
ATOM   4573  N ND2 . ASN A  1  633 ? -24.670 -32.018 53.915  1.00 102.23 ?  633  ASN A ND2 1 
ATOM   4574  N N   . LEU A  1  634 ? -26.162 -30.526 59.052  1.00 107.51 ?  634  LEU A N   1 
ATOM   4575  C CA  . LEU A  1  634 ? -25.323 -30.826 60.205  1.00 106.43 ?  634  LEU A CA  1 
ATOM   4576  C C   . LEU A  1  634 ? -25.245 -32.332 60.416  1.00 106.53 ?  634  LEU A C   1 
ATOM   4577  O O   . LEU A  1  634 ? -26.230 -33.055 60.243  1.00 108.14 ?  634  LEU A O   1 
ATOM   4578  C CB  . LEU A  1  634 ? -25.867 -30.145 61.462  1.00 107.42 ?  634  LEU A CB  1 
ATOM   4579  C CG  . LEU A  1  634 ? -26.175 -28.651 61.380  1.00 107.76 ?  634  LEU A CG  1 
ATOM   4580  C CD1 . LEU A  1  634 ? -27.444 -28.331 62.155  1.00 109.97 ?  634  LEU A CD1 1 
ATOM   4581  C CD2 . LEU A  1  634 ? -24.997 -27.839 61.898  1.00 105.13 ?  634  LEU A CD2 1 
ATOM   4582  N N   . SER A  1  635 ? -24.058 -32.806 60.790  1.00 110.25 ?  635  SER A N   1 
ATOM   4583  C CA  . SER A  1  635 ? -23.828 -34.234 60.956  1.00 114.05 ?  635  SER A CA  1 
ATOM   4584  C C   . SER A  1  635 ? -23.250 -34.531 62.333  1.00 115.82 ?  635  SER A C   1 
ATOM   4585  O O   . SER A  1  635 ? -23.146 -33.634 63.175  1.00 114.09 ?  635  SER A O   1 
ATOM   4586  C CB  . SER A  1  635 ? -22.891 -34.750 59.865  1.00 114.54 ?  635  SER A CB  1 
ATOM   4587  O OG  . SER A  1  635 ? -21.655 -34.059 59.907  1.00 112.51 ?  635  SER A OG  1 
ATOM   4588  N N   . GLY A  1  636 ? -22.860 -35.779 62.566  1.00 118.47 ?  636  GLY A N   1 
ATOM   4589  C CA  . GLY A  1  636 ? -22.366 -36.181 63.864  1.00 120.65 ?  636  GLY A CA  1 
ATOM   4590  C C   . GLY A  1  636 ? -23.477 -36.333 64.886  1.00 122.16 ?  636  GLY A C   1 
ATOM   4591  O O   . GLY A  1  636 ? -24.668 -36.366 64.570  1.00 122.25 ?  636  GLY A O   1 
ATOM   4592  N N   . GLN A  1  637 ? -23.063 -36.436 66.143  1.00 126.21 ?  637  GLN A N   1 
ATOM   4593  C CA  . GLN A  1  637 ? -23.984 -36.620 67.254  1.00 128.09 ?  637  GLN A CA  1 
ATOM   4594  C C   . GLN A  1  637 ? -24.206 -35.305 67.991  1.00 125.29 ?  637  GLN A C   1 
ATOM   4595  O O   . GLN A  1  637 ? -23.329 -34.438 68.031  1.00 122.83 ?  637  GLN A O   1 
ATOM   4596  C CB  . GLN A  1  637 ? -23.460 -37.683 68.220  1.00 132.15 ?  637  GLN A CB  1 
ATOM   4597  C CG  . GLN A  1  637 ? -22.998 -38.954 67.528  1.00 134.97 ?  637  GLN A CG  1 
ATOM   4598  C CD  . GLN A  1  637 ? -22.840 -40.112 68.487  1.00 139.40 ?  637  GLN A CD  1 
ATOM   4599  O OE1 . GLN A  1  637 ? -22.953 -39.945 69.702  1.00 140.35 ?  637  GLN A OE1 1 
ATOM   4600  N NE2 . GLN A  1  637 ? -22.573 -41.298 67.949  1.00 142.29 ?  637  GLN A NE2 1 
ATOM   4601  N N   . ILE A  1  638 ? -25.401 -35.158 68.558  1.00 127.31 ?  638  ILE A N   1 
ATOM   4602  C CA  . ILE A  1  638 ? -25.720 -34.007 69.400  1.00 125.45 ?  638  ILE A CA  1 
ATOM   4603  C C   . ILE A  1  638 ? -24.865 -34.107 70.657  1.00 127.10 ?  638  ILE A C   1 
ATOM   4604  O O   . ILE A  1  638 ? -24.916 -35.129 71.357  1.00 130.88 ?  638  ILE A O   1 
ATOM   4605  C CB  . ILE A  1  638 ? -27.218 -33.949 69.739  1.00 126.40 ?  638  ILE A CB  1 
ATOM   4606  C CG1 . ILE A  1  638 ? -28.052 -33.828 68.462  1.00 124.96 ?  638  ILE A CG1 1 
ATOM   4607  C CG2 . ILE A  1  638 ? -27.507 -32.793 70.686  1.00 124.91 ?  638  ILE A CG2 1 
ATOM   4608  C CD1 . ILE A  1  638 ? -29.546 -33.819 68.703  1.00 126.11 ?  638  ILE A CD1 1 
ATOM   4609  N N   . PRO A  1  639 ? -24.063 -33.093 70.971  1.00 129.61 ?  639  PRO A N   1 
ATOM   4610  C CA  . PRO A  1  639 ? -23.129 -33.192 72.103  1.00 131.48 ?  639  PRO A CA  1 
ATOM   4611  C C   . PRO A  1  639 ? -23.865 -33.413 73.412  1.00 134.20 ?  639  PRO A C   1 
ATOM   4612  O O   . PRO A  1  639 ? -24.765 -32.636 73.769  1.00 132.96 ?  639  PRO A O   1 
ATOM   4613  C CB  . PRO A  1  639 ? -22.408 -31.834 72.087  1.00 127.99 ?  639  PRO A CB  1 
ATOM   4614  C CG  . PRO A  1  639 ? -23.301 -30.929 71.294  1.00 124.56 ?  639  PRO A CG  1 
ATOM   4615  C CD  . PRO A  1  639 ? -23.940 -31.807 70.266  1.00 125.36 ?  639  PRO A CD  1 
ATOM   4616  N N   . PRO A  1  640 ? -23.512 -34.470 74.153  1.00 132.67 ?  640  PRO A N   1 
ATOM   4617  C CA  . PRO A  1  640 ? -24.230 -34.779 75.403  1.00 135.69 ?  640  PRO A CA  1 
ATOM   4618  C C   . PRO A  1  640 ? -24.074 -33.729 76.495  1.00 134.96 ?  640  PRO A C   1 
ATOM   4619  O O   . PRO A  1  640 ? -24.768 -33.826 77.515  1.00 137.24 ?  640  PRO A O   1 
ATOM   4620  C CB  . PRO A  1  640 ? -23.620 -36.119 75.838  1.00 139.80 ?  640  PRO A CB  1 
ATOM   4621  C CG  . PRO A  1  640 ? -23.081 -36.714 74.585  1.00 139.18 ?  640  PRO A CG  1 
ATOM   4622  C CD  . PRO A  1  640 ? -22.590 -35.552 73.768  1.00 134.76 ?  640  PRO A CD  1 
ATOM   4623  N N   . SER A  1  641 ? -23.190 -32.742 76.327  1.00 137.77 ?  641  SER A N   1 
ATOM   4624  C CA  . SER A  1  641 ? -23.081 -31.661 77.300  1.00 137.01 ?  641  SER A CA  1 
ATOM   4625  C C   . SER A  1  641 ? -24.320 -30.774 77.336  1.00 135.08 ?  641  SER A C   1 
ATOM   4626  O O   . SER A  1  641 ? -24.458 -29.976 78.269  1.00 135.11 ?  641  SER A O   1 
ATOM   4627  C CB  . SER A  1  641 ? -21.848 -30.802 77.009  1.00 134.46 ?  641  SER A CB  1 
ATOM   4628  O OG  . SER A  1  641 ? -21.963 -30.152 75.755  1.00 130.54 ?  641  SER A OG  1 
ATOM   4629  N N   . PHE A  1  642 ? -25.217 -30.895 76.352  1.00 138.31 ?  642  PHE A N   1 
ATOM   4630  C CA  . PHE A  1  642 ? -26.393 -30.036 76.265  1.00 136.38 ?  642  PHE A CA  1 
ATOM   4631  C C   . PHE A  1  642 ? -27.426 -30.326 77.348  1.00 139.50 ?  642  PHE A C   1 
ATOM   4632  O O   . PHE A  1  642 ? -28.341 -29.515 77.536  1.00 138.31 ?  642  PHE A O   1 
ATOM   4633  C CB  . PHE A  1  642 ? -27.047 -30.179 74.887  1.00 134.48 ?  642  PHE A CB  1 
ATOM   4634  C CG  . PHE A  1  642 ? -26.389 -29.360 73.813  1.00 130.62 ?  642  PHE A CG  1 
ATOM   4635  C CD1 . PHE A  1  642 ? -25.122 -28.832 74.000  1.00 129.24 ?  642  PHE A CD1 1 
ATOM   4636  C CD2 . PHE A  1  642 ? -27.039 -29.118 72.614  1.00 128.53 ?  642  PHE A CD2 1 
ATOM   4637  C CE1 . PHE A  1  642 ? -24.515 -28.078 73.013  1.00 125.82 ?  642  PHE A CE1 1 
ATOM   4638  C CE2 . PHE A  1  642 ? -26.437 -28.364 71.623  1.00 125.07 ?  642  PHE A CE2 1 
ATOM   4639  C CZ  . PHE A  1  642 ? -25.173 -27.845 71.823  1.00 123.72 ?  642  PHE A CZ  1 
ATOM   4640  N N   . LYS A  1  643 ? -27.305 -31.450 78.059  1.00 133.85 ?  643  LYS A N   1 
ATOM   4641  C CA  . LYS A  1  643 ? -28.190 -31.720 79.187  1.00 137.15 ?  643  LYS A CA  1 
ATOM   4642  C C   . LYS A  1  643 ? -28.057 -30.673 80.287  1.00 136.93 ?  643  LYS A C   1 
ATOM   4643  O O   . LYS A  1  643 ? -28.975 -30.524 81.100  1.00 138.78 ?  643  LYS A O   1 
ATOM   4644  C CB  . LYS A  1  643 ? -27.913 -33.118 79.749  1.00 141.61 ?  643  LYS A CB  1 
ATOM   4645  C CG  . LYS A  1  643 ? -26.565 -33.266 80.435  1.00 142.89 ?  643  LYS A CG  1 
ATOM   4646  C CD  . LYS A  1  643 ? -26.319 -34.705 80.861  1.00 147.22 ?  643  LYS A CD  1 
ATOM   4647  C CE  . LYS A  1  643 ? -24.998 -34.845 81.599  1.00 148.73 ?  643  LYS A CE  1 
ATOM   4648  N NZ  . LYS A  1  643 ? -24.936 -33.964 82.800  1.00 149.27 ?  643  LYS A NZ  1 
ATOM   4649  N N   . ASP A  1  644 ? -26.942 -29.944 80.327  1.00 137.75 ?  644  ASP A N   1 
ATOM   4650  C CA  . ASP A  1  644 ? -26.672 -28.953 81.360  1.00 137.75 ?  644  ASP A CA  1 
ATOM   4651  C C   . ASP A  1  644 ? -27.150 -27.555 80.994  1.00 133.96 ?  644  ASP A C   1 
ATOM   4652  O O   . ASP A  1  644 ? -26.733 -26.588 81.640  1.00 133.28 ?  644  ASP A O   1 
ATOM   4653  C CB  . ASP A  1  644 ? -25.174 -28.900 81.666  1.00 138.03 ?  644  ASP A CB  1 
ATOM   4654  C CG  . ASP A  1  644 ? -24.607 -30.247 82.051  1.00 141.81 ?  644  ASP A CG  1 
ATOM   4655  O OD1 . ASP A  1  644 ? -25.376 -31.103 82.533  1.00 144.98 ?  644  ASP A OD1 1 
ATOM   4656  O OD2 . ASP A  1  644 ? -23.388 -30.447 81.874  1.00 141.74 -1 644  ASP A OD2 1 
ATOM   4657  N N   . MET A  1  645 ? -27.995 -27.413 79.979  1.00 135.77 ?  645  MET A N   1 
ATOM   4658  C CA  . MET A  1  645 ? -28.487 -26.097 79.572  1.00 132.15 ?  645  MET A CA  1 
ATOM   4659  C C   . MET A  1  645 ? -29.875 -25.920 80.186  1.00 133.71 ?  645  MET A C   1 
ATOM   4660  O O   . MET A  1  645 ? -30.899 -26.200 79.561  1.00 133.48 ?  645  MET A O   1 
ATOM   4661  C CB  . MET A  1  645 ? -28.463 -25.961 78.052  1.00 128.68 ?  645  MET A CB  1 
ATOM   4662  C CG  . MET A  1  645 ? -27.031 -25.764 77.540  1.00 126.73 ?  645  MET A CG  1 
ATOM   4663  S SD  . MET A  1  645 ? -26.732 -25.766 75.760  1.00 123.38 ?  645  MET A SD  1 
ATOM   4664  C CE  . MET A  1  645 ? -28.396 -25.740 75.120  1.00 123.14 ?  645  MET A CE  1 
ATOM   4665  N N   . LEU A  1  646 ? -29.889 -25.452 81.442  1.00 123.12 ?  646  LEU A N   1 
ATOM   4666  C CA  . LEU A  1  646 ? -31.122 -25.350 82.218  1.00 125.40 ?  646  LEU A CA  1 
ATOM   4667  C C   . LEU A  1  646 ? -32.056 -24.279 81.673  1.00 122.28 ?  646  LEU A C   1 
ATOM   4668  O O   . LEU A  1  646 ? -33.277 -24.388 81.830  1.00 123.67 ?  646  LEU A O   1 
ATOM   4669  C CB  . LEU A  1  646 ? -30.805 -25.045 83.683  1.00 128.27 ?  646  LEU A CB  1 
ATOM   4670  C CG  . LEU A  1  646 ? -29.908 -25.969 84.508  1.00 131.90 ?  646  LEU A CG  1 
ATOM   4671  C CD1 . LEU A  1  646 ? -28.433 -25.733 84.226  1.00 130.09 ?  646  LEU A CD1 1 
ATOM   4672  C CD2 . LEU A  1  646 ? -30.198 -25.765 85.980  1.00 135.52 ?  646  LEU A CD2 1 
ATOM   4673  N N   . ALA A  1  647 ? -31.508 -23.235 81.052  1.00 123.82 ?  647  ALA A N   1 
ATOM   4674  C CA  . ALA A  1  647 ? -32.344 -22.190 80.481  1.00 120.84 ?  647  ALA A CA  1 
ATOM   4675  C C   . ALA A  1  647 ? -32.984 -22.606 79.165  1.00 119.77 ?  647  ALA A C   1 
ATOM   4676  O O   . ALA A  1  647 ? -33.957 -21.976 78.742  1.00 120.79 ?  647  ALA A O   1 
ATOM   4677  C CB  . ALA A  1  647 ? -31.524 -20.916 80.267  1.00 117.35 ?  647  ALA A CB  1 
ATOM   4678  N N   . LEU A  1  648 ? -32.468 -23.649 78.520  1.00 118.29 ?  648  LEU A N   1 
ATOM   4679  C CA  . LEU A  1  648 ? -33.003 -24.085 77.237  1.00 119.64 ?  648  LEU A CA  1 
ATOM   4680  C C   . LEU A  1  648 ? -34.410 -24.647 77.403  1.00 122.02 ?  648  LEU A C   1 
ATOM   4681  O O   . LEU A  1  648 ? -34.647 -25.528 78.235  1.00 123.32 ?  648  LEU A O   1 
ATOM   4682  C CB  . LEU A  1  648 ? -32.085 -25.135 76.616  1.00 119.03 ?  648  LEU A CB  1 
ATOM   4683  C CG  . LEU A  1  648 ? -32.381 -25.527 75.168  1.00 120.63 ?  648  LEU A CG  1 
ATOM   4684  C CD1 . LEU A  1  648 ? -32.026 -24.408 74.207  1.00 120.27 ?  648  LEU A CD1 1 
ATOM   4685  C CD2 . LEU A  1  648 ? -31.652 -26.808 74.811  1.00 119.99 ?  648  LEU A CD2 1 
ATOM   4686  N N   . THR A  1  649 ? -35.351 -24.130 76.609  1.00 119.17 ?  649  THR A N   1 
ATOM   4687  C CA  . THR A  1  649 ? -36.733 -24.585 76.651  1.00 120.75 ?  649  THR A CA  1 
ATOM   4688  C C   . THR A  1  649 ? -37.271 -25.089 75.318  1.00 121.87 ?  649  THR A C   1 
ATOM   4689  O O   . THR A  1  649 ? -38.225 -25.875 75.323  1.00 122.55 ?  649  THR A O   1 
ATOM   4690  C CB  . THR A  1  649 ? -37.659 -23.461 77.149  1.00 120.83 ?  649  THR A CB  1 
ATOM   4691  O OG1 . THR A  1  649 ? -38.079 -22.661 76.038  1.00 121.36 ?  649  THR A OG1 1 
ATOM   4692  C CG2 . THR A  1  649 ? -36.947 -22.575 78.149  1.00 119.12 ?  649  THR A CG2 1 
ATOM   4693  N N   . HIS A  1  650 ? -36.699 -24.669 74.187  1.00 119.52 ?  650  HIS A N   1 
ATOM   4694  C CA  . HIS A  1  650 ? -37.198 -25.044 72.867  1.00 120.08 ?  650  HIS A CA  1 
ATOM   4695  C C   . HIS A  1  650 ? -36.018 -25.421 71.983  1.00 119.58 ?  650  HIS A C   1 
ATOM   4696  O O   . HIS A  1  650 ? -35.043 -24.669 71.894  1.00 118.84 ?  650  HIS A O   1 
ATOM   4697  C CB  . HIS A  1  650 ? -37.990 -23.899 72.202  1.00 120.18 ?  650  HIS A CB  1 
ATOM   4698  C CG  . HIS A  1  650 ? -39.263 -23.523 72.904  1.00 120.17 ?  650  HIS A CG  1 
ATOM   4699  N ND1 . HIS A  1  650 ? -39.386 -23.485 74.276  1.00 120.42 ?  650  HIS A ND1 1 
ATOM   4700  C CD2 . HIS A  1  650 ? -40.470 -23.153 72.412  1.00 119.41 ?  650  HIS A CD2 1 
ATOM   4701  C CE1 . HIS A  1  650 ? -40.613 -23.118 74.600  1.00 120.12 ?  650  HIS A CE1 1 
ATOM   4702  N NE2 . HIS A  1  650 ? -41.291 -22.909 73.487  1.00 119.38 ?  650  HIS A NE2 1 
ATOM   4703  N N   . VAL A  1  651 ? -36.110 -26.581 71.326  1.00 118.70 ?  651  VAL A N   1 
ATOM   4704  C CA  . VAL A  1  651 ? -35.092 -27.048 70.389  1.00 118.01 ?  651  VAL A CA  1 
ATOM   4705  C C   . VAL A  1  651 ? -35.780 -27.579 69.142  1.00 118.06 ?  651  VAL A C   1 
ATOM   4706  O O   . VAL A  1  651 ? -36.863 -28.169 69.219  1.00 118.34 ?  651  VAL A O   1 
ATOM   4707  C CB  . VAL A  1  651 ? -34.184 -28.148 70.982  1.00 117.28 ?  651  VAL A CB  1 
ATOM   4708  C CG1 . VAL A  1  651 ? -32.865 -28.210 70.224  1.00 115.90 ?  651  VAL A CG1 1 
ATOM   4709  C CG2 . VAL A  1  651 ? -33.930 -27.917 72.431  1.00 116.73 ?  651  VAL A CG2 1 
ATOM   4710  N N   . ASP A  1  652 ? -35.142 -27.375 67.993  1.00 111.96 ?  652  ASP A N   1 
ATOM   4711  C CA  . ASP A  1  652 ? -35.552 -28.015 66.750  1.00 111.33 ?  652  ASP A CA  1 
ATOM   4712  C C   . ASP A  1  652 ? -34.295 -28.415 65.998  1.00 110.49 ?  652  ASP A C   1 
ATOM   4713  O O   . ASP A  1  652 ? -33.430 -27.574 65.735  1.00 110.04 ?  652  ASP A O   1 
ATOM   4714  C CB  . ASP A  1  652 ? -36.425 -27.092 65.897  1.00 110.66 ?  652  ASP A CB  1 
ATOM   4715  C CG  . ASP A  1  652 ? -37.201 -27.844 64.829  1.00 109.31 ?  652  ASP A CG  1 
ATOM   4716  O OD1 . ASP A  1  652 ? -36.767 -28.947 64.433  1.00 109.14 ?  652  ASP A OD1 1 
ATOM   4717  O OD2 . ASP A  1  652 ? -38.247 -27.331 64.381  1.00 108.05 -1 652  ASP A OD2 1 
ATOM   4718  N N   . VAL A  1  653 ? -34.198 -29.699 65.664  1.00 107.64 ?  653  VAL A N   1 
ATOM   4719  C CA  . VAL A  1  653 ? -33.006 -30.276 65.056  1.00 107.61 ?  653  VAL A CA  1 
ATOM   4720  C C   . VAL A  1  653 ? -33.448 -31.056 63.820  1.00 108.80 ?  653  VAL A C   1 
ATOM   4721  O O   . VAL A  1  653 ? -32.638 -31.687 63.131  1.00 109.31 ?  653  VAL A O   1 
ATOM   4722  C CB  . VAL A  1  653 ? -32.264 -31.144 66.093  1.00 110.79 ?  653  VAL A CB  1 
ATOM   4723  C CG1 . VAL A  1  653 ? -30.993 -31.683 65.554  1.00 110.84 ?  653  VAL A CG1 1 
ATOM   4724  C CG2 . VAL A  1  653 ? -31.945 -30.320 67.319  1.00 109.83 ?  653  VAL A CG2 1 
ATOM   4725  N N   . SER A  1  654 ? -34.740 -30.968 63.507  1.00 113.69 ?  654  SER A N   1 
ATOM   4726  C CA  . SER A  1  654 ? -35.345 -31.741 62.431  1.00 112.70 ?  654  SER A CA  1 
ATOM   4727  C C   . SER A  1  654 ? -34.653 -31.490 61.093  1.00 111.31 ?  654  SER A C   1 
ATOM   4728  O O   . SER A  1  654 ? -34.028 -30.450 60.869  1.00 110.98 ?  654  SER A O   1 
ATOM   4729  C CB  . SER A  1  654 ? -36.830 -31.404 62.299  1.00 112.08 ?  654  SER A CB  1 
ATOM   4730  O OG  . SER A  1  654 ? -37.024 -30.044 61.952  1.00 111.15 ?  654  SER A OG  1 
ATOM   4731  N N   . HIS A  1  655 ? -34.776 -32.473 60.197  1.00 113.30 ?  655  HIS A N   1 
ATOM   4732  C CA  . HIS A  1  655 ? -34.283 -32.377 58.821  1.00 111.80 ?  655  HIS A CA  1 
ATOM   4733  C C   . HIS A  1  655 ? -32.780 -32.086 58.788  1.00 111.95 ?  655  HIS A C   1 
ATOM   4734  O O   . HIS A  1  655 ? -32.321 -31.052 58.297  1.00 111.24 ?  655  HIS A O   1 
ATOM   4735  C CB  . HIS A  1  655 ? -35.073 -31.326 58.029  1.00 110.02 ?  655  HIS A CB  1 
ATOM   4736  C CG  . HIS A  1  655 ? -36.516 -31.679 57.827  1.00 108.98 ?  655  HIS A CG  1 
ATOM   4737  N ND1 . HIS A  1  655 ? -37.433 -31.681 58.856  1.00 110.35 ?  655  HIS A ND1 1 
ATOM   4738  C CD2 . HIS A  1  655 ? -37.198 -32.040 56.715  1.00 108.67 ?  655  HIS A CD2 1 
ATOM   4739  C CE1 . HIS A  1  655 ? -38.618 -32.029 58.387  1.00 111.25 ?  655  HIS A CE1 1 
ATOM   4740  N NE2 . HIS A  1  655 ? -38.503 -32.252 57.090  1.00 110.84 ?  655  HIS A NE2 1 
ATOM   4741  N N   . ASN A  1  656 ? -32.017 -33.024 59.341  1.00 111.29 ?  656  ASN A N   1 
ATOM   4742  C CA  . ASN A  1  656 ? -30.566 -32.918 59.396  1.00 110.89 ?  656  ASN A CA  1 
ATOM   4743  C C   . ASN A  1  656 ? -29.975 -34.308 59.180  1.00 110.69 ?  656  ASN A C   1 
ATOM   4744  O O   . ASN A  1  656 ? -30.672 -35.248 58.782  1.00 113.67 ?  656  ASN A O   1 
ATOM   4745  C CB  . ASN A  1  656 ? -30.124 -32.286 60.721  1.00 111.47 ?  656  ASN A CB  1 
ATOM   4746  C CG  . ASN A  1  656 ? -29.756 -30.830 60.569  1.00 111.09 ?  656  ASN A CG  1 
ATOM   4747  O OD1 . ASN A  1  656 ? -28.650 -30.504 60.151  1.00 109.99 ?  656  ASN A OD1 1 
ATOM   4748  N ND2 . ASN A  1  656 ? -30.686 -29.943 60.901  1.00 111.85 ?  656  ASN A ND2 1 
ATOM   4749  N N   . ASN A  1  657 ? -28.673 -34.439 59.435  1.00 114.25 ?  657  ASN A N   1 
ATOM   4750  C CA  . ASN A  1  657 ? -27.939 -35.676 59.195  1.00 116.87 ?  657  ASN A CA  1 
ATOM   4751  C C   . ASN A  1  657 ? -27.304 -36.216 60.476  1.00 119.00 ?  657  ASN A C   1 
ATOM   4752  O O   . ASN A  1  657 ? -26.229 -36.816 60.441  1.00 120.25 ?  657  ASN A O   1 
ATOM   4753  C CB  . ASN A  1  657 ? -26.878 -35.457 58.116  1.00 115.11 ?  657  ASN A CB  1 
ATOM   4754  C CG  . ASN A  1  657 ? -26.350 -36.755 57.545  1.00 118.44 ?  657  ASN A CG  1 
ATOM   4755  O OD1 . ASN A  1  657 ? -27.109 -37.585 57.044  1.00 121.04 ?  657  ASN A OD1 1 
ATOM   4756  N ND2 . ASN A  1  657 ? -25.037 -36.941 57.627  1.00 118.58 ?  657  ASN A ND2 1 
ATOM   4757  N N   . LEU A  1  658 ? -27.955 -36.011 61.615  1.00 119.27 ?  658  LEU A N   1 
ATOM   4758  C CA  . LEU A  1  658 ? -27.372 -36.399 62.889  1.00 121.12 ?  658  LEU A CA  1 
ATOM   4759  C C   . LEU A  1  658 ? -27.774 -37.817 63.286  1.00 125.72 ?  658  LEU A C   1 
ATOM   4760  O O   . LEU A  1  658 ? -28.585 -38.477 62.632  1.00 127.61 ?  658  LEU A O   1 
ATOM   4761  C CB  . LEU A  1  658 ? -27.768 -35.399 63.970  1.00 119.46 ?  658  LEU A CB  1 
ATOM   4762  C CG  . LEU A  1  658 ? -27.369 -33.981 63.564  1.00 115.07 ?  658  LEU A CG  1 
ATOM   4763  C CD1 . LEU A  1  658 ? -28.465 -33.025 63.882  1.00 114.86 ?  658  LEU A CD1 1 
ATOM   4764  C CD2 . LEU A  1  658 ? -26.096 -33.545 64.265  1.00 113.99 ?  658  LEU A CD2 1 
ATOM   4765  N N   . GLN A  1  659 ? -27.185 -38.278 64.387  1.00 125.00 ?  659  GLN A N   1 
ATOM   4766  C CA  . GLN A  1  659 ? -27.376 -39.636 64.873  1.00 129.71 ?  659  GLN A CA  1 
ATOM   4767  C C   . GLN A  1  659 ? -27.017 -39.678 66.349  1.00 131.08 ?  659  GLN A C   1 
ATOM   4768  O O   . GLN A  1  659 ? -26.264 -38.837 66.847  1.00 128.71 ?  659  GLN A O   1 
ATOM   4769  C CB  . GLN A  1  659 ? -26.521 -40.632 64.084  1.00 131.75 ?  659  GLN A CB  1 
ATOM   4770  C CG  . GLN A  1  659 ? -25.027 -40.463 64.301  1.00 130.82 ?  659  GLN A CG  1 
ATOM   4771  C CD  . GLN A  1  659 ? -24.199 -41.203 63.270  1.00 132.07 ?  659  GLN A CD  1 
ATOM   4772  O OE1 . GLN A  1  659 ? -24.736 -41.782 62.326  1.00 133.40 ?  659  GLN A OE1 1 
ATOM   4773  N NE2 . GLN A  1  659 ? -22.882 -41.181 63.442  1.00 131.83 ?  659  GLN A NE2 1 
ATOM   4774  N N   . GLY A  1  660 ? -27.566 -40.669 67.045  1.00 134.58 ?  660  GLY A N   1 
ATOM   4775  C CA  . GLY A  1  660 ? -27.221 -40.903 68.427  1.00 136.60 ?  660  GLY A CA  1 
ATOM   4776  C C   . GLY A  1  660 ? -28.315 -40.495 69.392  1.00 137.07 ?  660  GLY A C   1 
ATOM   4777  O O   . GLY A  1  660 ? -29.271 -39.800 69.030  1.00 135.12 ?  660  GLY A O   1 
ATOM   4778  N N   . PRO A  1  661 ? -28.189 -40.923 70.648  1.00 139.83 ?  661  PRO A N   1 
ATOM   4779  C CA  . PRO A  1  661 ? -29.204 -40.580 71.652  1.00 140.74 ?  661  PRO A CA  1 
ATOM   4780  C C   . PRO A  1  661 ? -29.103 -39.133 72.109  1.00 137.02 ?  661  PRO A C   1 
ATOM   4781  O O   . PRO A  1  661 ? -28.024 -38.537 72.153  1.00 134.72 ?  661  PRO A O   1 
ATOM   4782  C CB  . PRO A  1  661 ? -28.897 -41.543 72.802  1.00 144.99 ?  661  PRO A CB  1 
ATOM   4783  C CG  . PRO A  1  661 ? -27.439 -41.810 72.671  1.00 144.72 ?  661  PRO A CG  1 
ATOM   4784  C CD  . PRO A  1  661 ? -27.156 -41.820 71.193  1.00 142.64 ?  661  PRO A CD  1 
ATOM   4785  N N   . ILE A  1  662 ? -30.256 -38.572 72.459  1.00 140.24 ?  662  ILE A N   1 
ATOM   4786  C CA  . ILE A  1  662 ? -30.353 -37.184 72.907  1.00 136.96 ?  662  ILE A CA  1 
ATOM   4787  C C   . ILE A  1  662 ? -29.979 -37.052 74.380  1.00 138.65 ?  662  ILE A C   1 
ATOM   4788  O O   . ILE A  1  662 ? -30.529 -37.771 75.228  1.00 142.44 ?  662  ILE A O   1 
ATOM   4789  C CB  . ILE A  1  662 ? -31.756 -36.608 72.645  1.00 135.95 ?  662  ILE A CB  1 
ATOM   4790  C CG1 . ILE A  1  662 ? -32.833 -37.434 73.358  1.00 140.33 ?  662  ILE A CG1 1 
ATOM   4791  C CG2 . ILE A  1  662 ? -32.024 -36.516 71.153  1.00 133.71 ?  662  ILE A CG2 1 
ATOM   4792  C CD1 . ILE A  1  662 ? -34.225 -36.861 73.240  1.00 139.79 ?  662  ILE A CD1 1 
ATOM   4793  N N   . PRO A  1  663 ? -29.004 -36.211 74.724  1.00 140.00 ?  663  PRO A N   1 
ATOM   4794  C CA  . PRO A  1  663 ? -28.912 -35.705 76.103  1.00 140.92 ?  663  PRO A CA  1 
ATOM   4795  C C   . PRO A  1  663 ? -30.251 -35.232 76.661  1.00 141.48 ?  663  PRO A C   1 
ATOM   4796  O O   . PRO A  1  663 ? -31.088 -34.676 75.939  1.00 139.28 ?  663  PRO A O   1 
ATOM   4797  C CB  . PRO A  1  663 ? -27.885 -34.564 75.981  1.00 137.18 ?  663  PRO A CB  1 
ATOM   4798  C CG  . PRO A  1  663 ? -27.713 -34.354 74.469  1.00 133.95 ?  663  PRO A CG  1 
ATOM   4799  C CD  . PRO A  1  663 ? -27.862 -35.735 73.935  1.00 136.85 ?  663  PRO A CD  1 
ATOM   4800  N N   . ASP A  1  664 ? -30.458 -35.463 77.954  1.00 141.04 ?  664  ASP A N   1 
ATOM   4801  C CA  . ASP A  1  664 ? -31.754 -35.307 78.610  1.00 142.83 ?  664  ASP A CA  1 
ATOM   4802  C C   . ASP A  1  664 ? -31.818 -33.958 79.327  1.00 140.78 ?  664  ASP A C   1 
ATOM   4803  O O   . ASP A  1  664 ? -31.133 -33.748 80.333  1.00 141.84 ?  664  ASP A O   1 
ATOM   4804  C CB  . ASP A  1  664 ? -31.975 -36.470 79.578  1.00 148.02 ?  664  ASP A CB  1 
ATOM   4805  C CG  . ASP A  1  664 ? -33.066 -36.201 80.595  1.00 150.31 ?  664  ASP A CG  1 
ATOM   4806  O OD1 . ASP A  1  664 ? -34.101 -35.604 80.237  1.00 148.94 ?  664  ASP A OD1 1 
ATOM   4807  O OD2 . ASP A  1  664 ? -32.880 -36.598 81.765  1.00 153.65 -1 664  ASP A OD2 1 
ATOM   4808  N N   . ASN A  1  665 ? -32.635 -33.042 78.805  1.00 144.04 ?  665  ASN A N   1 
ATOM   4809  C CA  . ASN A  1  665 ? -32.920 -31.786 79.488  1.00 142.51 ?  665  ASN A CA  1 
ATOM   4810  C C   . ASN A  1  665 ? -34.395 -31.454 79.305  1.00 142.54 ?  665  ASN A C   1 
ATOM   4811  O O   . ASN A  1  665 ? -35.127 -32.155 78.600  1.00 143.57 ?  665  ASN A O   1 
ATOM   4812  C CB  . ASN A  1  665 ? -32.025 -30.643 78.988  1.00 137.97 ?  665  ASN A CB  1 
ATOM   4813  C CG  . ASN A  1  665 ? -32.154 -30.396 77.494  1.00 134.46 ?  665  ASN A CG  1 
ATOM   4814  O OD1 . ASN A  1  665 ? -33.244 -30.460 76.925  1.00 134.41 ?  665  ASN A OD1 1 
ATOM   4815  N ND2 . ASN A  1  665 ? -31.033 -30.094 76.854  1.00 131.78 ?  665  ASN A ND2 1 
ATOM   4816  N N   . ALA A  1  666 ? -34.834 -30.376 79.960  1.00 142.58 ?  666  ALA A N   1 
ATOM   4817  C CA  . ALA A  1  666 ? -36.227 -29.963 79.839  1.00 142.64 ?  666  ALA A CA  1 
ATOM   4818  C C   . ALA A  1  666 ? -36.599 -29.659 78.391  1.00 139.21 ?  666  ALA A C   1 
ATOM   4819  O O   . ALA A  1  666 ? -37.713 -29.961 77.957  1.00 140.27 ?  666  ALA A O   1 
ATOM   4820  C CB  . ALA A  1  666 ? -36.495 -28.749 80.728  1.00 141.90 ?  666  ALA A CB  1 
ATOM   4821  N N   . ALA A  1  667 ? -35.682 -29.094 77.610  1.00 135.86 ?  667  ALA A N   1 
ATOM   4822  C CA  . ALA A  1  667 ? -36.081 -28.728 76.257  1.00 132.94 ?  667  ALA A CA  1 
ATOM   4823  C C   . ALA A  1  667 ? -36.345 -29.966 75.403  1.00 134.68 ?  667  ALA A C   1 
ATOM   4824  O O   . ALA A  1  667 ? -37.341 -30.017 74.672  1.00 134.55 ?  667  ALA A O   1 
ATOM   4825  C CB  . ALA A  1  667 ? -35.028 -27.831 75.623  1.00 129.75 ?  667  ALA A CB  1 
ATOM   4826  N N   . PHE A  1  668 ? -35.483 -30.984 75.503  1.00 133.85 ?  668  PHE A N   1 
ATOM   4827  C CA  . PHE A  1  668 ? -35.627 -32.173 74.663  1.00 135.58 ?  668  PHE A CA  1 
ATOM   4828  C C   . PHE A  1  668 ? -36.850 -33.000 75.046  1.00 139.70 ?  668  PHE A C   1 
ATOM   4829  O O   . PHE A  1  668 ? -37.533 -33.548 74.172  1.00 140.47 ?  668  PHE A O   1 
ATOM   4830  C CB  . PHE A  1  668 ? -34.358 -33.021 74.737  1.00 136.73 ?  668  PHE A CB  1 
ATOM   4831  C CG  . PHE A  1  668 ? -33.247 -32.527 73.850  1.00 133.04 ?  668  PHE A CG  1 
ATOM   4832  C CD1 . PHE A  1  668 ? -33.385 -32.537 72.471  1.00 131.00 ?  668  PHE A CD1 1 
ATOM   4833  C CD2 . PHE A  1  668 ? -32.063 -32.060 74.397  1.00 131.86 ?  668  PHE A CD2 1 
ATOM   4834  C CE1 . PHE A  1  668 ? -32.362 -32.085 71.655  1.00 127.81 ?  668  PHE A CE1 1 
ATOM   4835  C CE2 . PHE A  1  668 ? -31.038 -31.608 73.586  1.00 128.72 ?  668  PHE A CE2 1 
ATOM   4836  C CZ  . PHE A  1  668 ? -31.188 -31.620 72.214  1.00 126.68 ?  668  PHE A CZ  1 
ATOM   4837  N N   . ARG A  1  669 ? -37.132 -33.116 76.347  1.00 136.36 ?  669  ARG A N   1 
ATOM   4838  C CA  . ARG A  1  669 ? -38.228 -33.969 76.801  1.00 140.82 ?  669  ARG A CA  1 
ATOM   4839  C C   . ARG A  1  669 ? -39.574 -33.480 76.277  1.00 140.22 ?  669  ARG A C   1 
ATOM   4840  O O   . ARG A  1  669 ? -40.388 -34.277 75.798  1.00 142.69 ?  669  ARG A O   1 
ATOM   4841  C CB  . ARG A  1  669 ? -38.241 -34.031 78.329  1.00 143.93 ?  669  ARG A CB  1 
ATOM   4842  C CG  . ARG A  1  669 ? -37.059 -34.772 78.927  1.00 145.71 ?  669  ARG A CG  1 
ATOM   4843  C CD  . ARG A  1  669 ? -37.276 -35.053 80.407  1.00 149.77 ?  669  ARG A CD  1 
ATOM   4844  N NE  . ARG A  1  669 ? -36.166 -34.574 81.222  1.00 148.94 ?  669  ARG A NE  1 
ATOM   4845  C CZ  . ARG A  1  669 ? -36.288 -33.709 82.218  1.00 149.01 ?  669  ARG A CZ  1 
ATOM   4846  N NH1 . ARG A  1  669 ? -37.463 -33.204 82.555  1.00 149.81 ?  669  ARG A NH1 1 
ATOM   4847  N NH2 . ARG A  1  669 ? -35.203 -33.340 82.894  1.00 148.46 ?  669  ARG A NH2 1 
ATOM   4848  N N   . ASN A  1  670 ? -39.823 -32.176 76.353  1.00 143.72 ?  670  ASN A N   1 
ATOM   4849  C CA  . ASN A  1  670 ? -41.073 -31.586 75.888  1.00 142.93 ?  670  ASN A CA  1 
ATOM   4850  C C   . ASN A  1  670 ? -41.096 -31.315 74.391  1.00 139.52 ?  670  ASN A C   1 
ATOM   4851  O O   . ASN A  1  670 ? -42.089 -30.771 73.893  1.00 138.56 ?  670  ASN A O   1 
ATOM   4852  C CB  . ASN A  1  670 ? -41.350 -30.298 76.668  1.00 141.33 ?  670  ASN A CB  1 
ATOM   4853  C CG  . ASN A  1  670 ? -41.039 -30.443 78.145  1.00 144.22 ?  670  ASN A CG  1 
ATOM   4854  O OD1 . ASN A  1  670 ? -39.945 -30.860 78.524  1.00 144.61 ?  670  ASN A OD1 1 
ATOM   4855  N ND2 . ASN A  1  670 ? -42.000 -30.072 78.993  1.00 146.40 ?  670  ASN A ND2 1 
ATOM   4856  N N   . ALA A  1  671 ? -40.047 -31.685 73.665  1.00 133.56 ?  671  ALA A N   1 
ATOM   4857  C CA  . ALA A  1  671 ? -40.017 -31.434 72.235  1.00 130.39 ?  671  ALA A CA  1 
ATOM   4858  C C   . ALA A  1  671 ? -41.049 -32.304 71.518  1.00 133.14 ?  671  ALA A C   1 
ATOM   4859  O O   . ALA A  1  671 ? -41.179 -33.496 71.819  1.00 137.30 ?  671  ALA A O   1 
ATOM   4860  C CB  . ALA A  1  671 ? -38.623 -31.706 71.675  1.00 128.49 ?  671  ALA A CB  1 
ATOM   4861  N N   . PRO A  1  672 ? -41.789 -31.743 70.566  1.00 130.19 ?  672  PRO A N   1 
ATOM   4862  C CA  . PRO A  1  672 ? -42.759 -32.541 69.806  1.00 132.66 ?  672  PRO A CA  1 
ATOM   4863  C C   . PRO A  1  672 ? -42.053 -33.423 68.793  1.00 132.81 ?  672  PRO A C   1 
ATOM   4864  O O   . PRO A  1  672 ? -40.843 -33.269 68.564  1.00 130.46 ?  672  PRO A O   1 
ATOM   4865  C CB  . PRO A  1  672 ? -43.638 -31.484 69.117  1.00 129.91 ?  672  PRO A CB  1 
ATOM   4866  C CG  . PRO A  1  672 ? -42.888 -30.199 69.191  1.00 125.57 ?  672  PRO A CG  1 
ATOM   4867  C CD  . PRO A  1  672 ? -41.709 -30.346 70.106  1.00 125.81 ?  672  PRO A CD  1 
ATOM   4868  N N   . PRO A  1  673 ? -42.764 -34.370 68.173  1.00 132.38 ?  673  PRO A N   1 
ATOM   4869  C CA  . PRO A  1  673 ? -42.121 -35.217 67.155  1.00 132.76 ?  673  PRO A CA  1 
ATOM   4870  C C   . PRO A  1  673 ? -41.579 -34.445 65.964  1.00 128.09 ?  673  PRO A C   1 
ATOM   4871  O O   . PRO A  1  673 ? -40.681 -34.951 65.279  1.00 127.62 ?  673  PRO A O   1 
ATOM   4872  C CB  . PRO A  1  673 ? -43.246 -36.173 66.734  1.00 137.11 ?  673  PRO A CB  1 
ATOM   4873  C CG  . PRO A  1  673 ? -44.145 -36.228 67.914  1.00 140.22 ?  673  PRO A CG  1 
ATOM   4874  C CD  . PRO A  1  673 ? -44.120 -34.846 68.501  1.00 136.52 ?  673  PRO A CD  1 
ATOM   4875  N N   . ASP A  1  674 ? -42.097 -33.244 65.686  1.00 133.87 ?  674  ASP A N   1 
ATOM   4876  C CA  . ASP A  1  674 ? -41.566 -32.452 64.582  1.00 129.65 ?  674  ASP A CA  1 
ATOM   4877  C C   . ASP A  1  674 ? -40.111 -32.067 64.813  1.00 127.32 ?  674  ASP A C   1 
ATOM   4878  O O   . ASP A  1  674 ? -39.349 -31.934 63.852  1.00 125.38 ?  674  ASP A O   1 
ATOM   4879  C CB  . ASP A  1  674 ? -42.403 -31.189 64.370  1.00 126.92 ?  674  ASP A CB  1 
ATOM   4880  C CG  . ASP A  1  674 ? -43.878 -31.408 64.640  1.00 129.66 ?  674  ASP A CG  1 
ATOM   4881  O OD1 . ASP A  1  674 ? -44.450 -32.379 64.100  1.00 132.96 ?  674  ASP A OD1 1 
ATOM   4882  O OD2 . ASP A  1  674 ? -44.466 -30.597 65.388  1.00 128.98 -1 674  ASP A OD2 1 
ATOM   4883  N N   . ALA A  1  675 ? -39.707 -31.885 66.073  1.00 122.03 ?  675  ALA A N   1 
ATOM   4884  C CA  . ALA A  1  675 ? -38.376 -31.378 66.395  1.00 119.27 ?  675  ALA A CA  1 
ATOM   4885  C C   . ALA A  1  675 ? -37.256 -32.381 66.131  1.00 120.65 ?  675  ALA A C   1 
ATOM   4886  O O   . ALA A  1  675 ? -36.090 -32.036 66.346  1.00 118.65 ?  675  ALA A O   1 
ATOM   4887  C CB  . ALA A  1  675 ? -38.329 -30.930 67.857  1.00 119.82 ?  675  ALA A CB  1 
ATOM   4888  N N   . PHE A  1  676 ? -37.562 -33.600 65.678  1.00 119.84 ?  676  PHE A N   1 
ATOM   4889  C CA  . PHE A  1  676 ? -36.532 -34.580 65.355  1.00 121.32 ?  676  PHE A CA  1 
ATOM   4890  C C   . PHE A  1  676 ? -36.744 -35.225 63.987  1.00 122.14 ?  676  PHE A C   1 
ATOM   4891  O O   . PHE A  1  676 ? -36.085 -36.224 63.676  1.00 124.27 ?  676  PHE A O   1 
ATOM   4892  C CB  . PHE A  1  676 ? -36.465 -35.663 66.439  1.00 125.79 ?  676  PHE A CB  1 
ATOM   4893  C CG  . PHE A  1  676 ? -36.275 -35.123 67.834  1.00 125.59 ?  676  PHE A CG  1 
ATOM   4894  C CD1 . PHE A  1  676 ? -35.006 -34.862 68.327  1.00 124.11 ?  676  PHE A CD1 1 
ATOM   4895  C CD2 . PHE A  1  676 ? -37.366 -34.884 68.654  1.00 127.16 ?  676  PHE A CD2 1 
ATOM   4896  C CE1 . PHE A  1  676 ? -34.831 -34.372 69.612  1.00 124.20 ?  676  PHE A CE1 1 
ATOM   4897  C CE2 . PHE A  1  676 ? -37.196 -34.394 69.936  1.00 127.23 ?  676  PHE A CE2 1 
ATOM   4898  C CZ  . PHE A  1  676 ? -35.927 -34.138 70.415  1.00 125.77 ?  676  PHE A CZ  1 
ATOM   4899  N N   . GLU A  1  677 ? -37.630 -34.671 63.163  1.00 122.66 ?  677  GLU A N   1 
ATOM   4900  C CA  . GLU A  1  677 ? -37.989 -35.285 61.893  1.00 123.72 ?  677  GLU A CA  1 
ATOM   4901  C C   . GLU A  1  677 ? -36.819 -35.277 60.916  1.00 121.62 ?  677  GLU A C   1 
ATOM   4902  O O   . GLU A  1  677 ? -35.974 -34.379 60.926  1.00 118.24 ?  677  GLU A O   1 
ATOM   4903  C CB  . GLU A  1  677 ? -39.177 -34.552 61.271  1.00 122.29 ?  677  GLU A CB  1 
ATOM   4904  C CG  . GLU A  1  677 ? -40.531 -35.060 61.731  1.00 125.95 ?  677  GLU A CG  1 
ATOM   4905  C CD  . GLU A  1  677 ? -41.572 -35.006 60.634  1.00 126.34 ?  677  GLU A CD  1 
ATOM   4906  O OE1 . GLU A  1  677 ? -41.576 -34.012 59.872  1.00 122.51 ?  677  GLU A OE1 1 
ATOM   4907  O OE2 . GLU A  1  677 ? -42.382 -35.955 60.532  1.00 130.62 -1 677  GLU A OE2 1 
ATOM   4908  N N   . GLY A  1  678 ? -36.784 -36.295 60.060  1.00 122.34 ?  678  GLY A N   1 
ATOM   4909  C CA  . GLY A  1  678 ? -35.876 -36.299 58.925  1.00 120.62 ?  678  GLY A CA  1 
ATOM   4910  C C   . GLY A  1  678 ? -34.404 -36.295 59.270  1.00 119.33 ?  678  GLY A C   1 
ATOM   4911  O O   . GLY A  1  678 ? -33.607 -35.696 58.540  1.00 116.21 ?  678  GLY A O   1 
ATOM   4912  N N   . ASN A  1  679 ? -34.016 -36.934 60.368  1.00 121.77 ?  679  ASN A N   1 
ATOM   4913  C CA  . ASN A  1  679 ? -32.614 -37.155 60.676  1.00 121.46 ?  679  ASN A CA  1 
ATOM   4914  C C   . ASN A  1  679 ? -32.216 -38.558 60.221  1.00 125.39 ?  679  ASN A C   1 
ATOM   4915  O O   . ASN A  1  679 ? -33.005 -39.286 59.615  1.00 128.12 ?  679  ASN A O   1 
ATOM   4916  C CB  . ASN A  1  679 ? -32.348 -36.943 62.165  1.00 121.68 ?  679  ASN A CB  1 
ATOM   4917  C CG  . ASN A  1  679 ? -31.907 -35.531 62.475  1.00 117.17 ?  679  ASN A CG  1 
ATOM   4918  O OD1 . ASN A  1  679 ? -30.760 -35.160 62.230  1.00 115.00 ?  679  ASN A OD1 1 
ATOM   4919  N ND2 . ASN A  1  679 ? -32.820 -34.730 63.011  1.00 115.89 ?  679  ASN A ND2 1 
ATOM   4920  N N   . LYS A  1  680 ? -30.967 -38.938 60.493  1.00 125.82 ?  680  LYS A N   1 
ATOM   4921  C CA  . LYS A  1  680 ? -30.499 -40.232 60.008  1.00 129.45 ?  680  LYS A CA  1 
ATOM   4922  C C   . LYS A  1  680 ? -30.657 -41.356 61.033  1.00 133.91 ?  680  LYS A C   1 
ATOM   4923  O O   . LYS A  1  680 ? -31.381 -42.327 60.789  1.00 137.63 ?  680  LYS A O   1 
ATOM   4924  C CB  . LYS A  1  680 ? -29.027 -40.116 59.598  1.00 127.84 ?  680  LYS A CB  1 
ATOM   4925  C CG  . LYS A  1  680 ? -28.705 -40.611 58.204  1.00 128.62 ?  680  LYS A CG  1 
ATOM   4926  C CD  . LYS A  1  680 ? -27.215 -40.887 58.079  1.00 128.67 ?  680  LYS A CD  1 
ATOM   4927  C CE  . LYS A  1  680 ? -26.814 -41.139 56.638  1.00 128.81 ?  680  LYS A CE  1 
ATOM   4928  N NZ  . LYS A  1  680 ? -25.337 -41.242 56.497  1.00 128.52 ?  680  LYS A NZ  1 
ATOM   4929  N N   . ASP A  1  681 ? -29.994 -41.237 62.183  1.00 133.77 ?  681  ASP A N   1 
ATOM   4930  C CA  . ASP A  1  681 ? -29.962 -42.336 63.146  1.00 138.05 ?  681  ASP A CA  1 
ATOM   4931  C C   . ASP A  1  681 ? -30.109 -41.841 64.582  1.00 137.65 ?  681  ASP A C   1 
ATOM   4932  O O   . ASP A  1  681 ? -29.396 -42.297 65.482  1.00 139.38 ?  681  ASP A O   1 
ATOM   4933  C CB  . ASP A  1  681 ? -28.688 -43.160 62.987  1.00 139.78 ?  681  ASP A CB  1 
ATOM   4934  C CG  . ASP A  1  681 ? -28.929 -44.631 63.198  1.00 145.01 ?  681  ASP A CG  1 
ATOM   4935  O OD1 . ASP A  1  681 ? -29.880 -45.165 62.590  1.00 147.16 ?  681  ASP A OD1 1 
ATOM   4936  O OD2 . ASP A  1  681 ? -28.172 -45.250 63.971  1.00 147.10 -1 681  ASP A OD2 1 
ATOM   4937  N N   . LEU A  1  682 ? -31.023 -40.909 64.832  1.00 135.54 ?  682  LEU A N   1 
ATOM   4938  C CA  . LEU A  1  682 ? -31.176 -40.393 66.188  1.00 135.27 ?  682  LEU A CA  1 
ATOM   4939  C C   . LEU A  1  682 ? -31.843 -41.442 67.074  1.00 140.06 ?  682  LEU A C   1 
ATOM   4940  O O   . LEU A  1  682 ? -32.995 -41.821 66.844  1.00 142.12 ?  682  LEU A O   1 
ATOM   4941  C CB  . LEU A  1  682 ? -31.984 -39.099 66.179  1.00 131.84 ?  682  LEU A CB  1 
ATOM   4942  C CG  . LEU A  1  682 ? -31.249 -37.840 65.712  1.00 126.85 ?  682  LEU A CG  1 
ATOM   4943  C CD1 . LEU A  1  682 ? -32.172 -36.634 65.760  1.00 123.92 ?  682  LEU A CD1 1 
ATOM   4944  C CD2 . LEU A  1  682 ? -30.006 -37.593 66.552  1.00 126.10 ?  682  LEU A CD2 1 
ATOM   4945  N N   . CYS A  1  683 ? -31.119 -41.905 68.092  1.00 141.99 ?  683  CYS A N   1 
ATOM   4946  C CA  . CYS A  1  683 ? -31.638 -42.907 69.019  1.00 146.65 ?  683  CYS A CA  1 
ATOM   4947  C C   . CYS A  1  683 ? -32.688 -42.304 69.947  1.00 146.76 ?  683  CYS A C   1 
ATOM   4948  O O   . CYS A  1  683 ? -33.869 -42.641 69.870  1.00 148.95 ?  683  CYS A O   1 
ATOM   4949  C CB  . CYS A  1  683 ? -30.500 -43.521 69.840  1.00 148.56 ?  683  CYS A CB  1 
ATOM   4950  S SG  . CYS A  1  683 ? -31.040 -44.571 71.217  1.00 153.99 ?  683  CYS A SG  1 
ATOM   4951  N N   . ASN B  2  26  ? -47.708 7.221   79.968  1.00 78.51  ?  26   ASN B N   1 
ATOM   4952  C CA  . ASN B  2  26  ? -48.676 6.593   80.858  1.00 80.71  ?  26   ASN B CA  1 
ATOM   4953  C C   . ASN B  2  26  ? -48.013 6.154   82.154  1.00 82.79  ?  26   ASN B C   1 
ATOM   4954  O O   . ASN B  2  26  ? -46.947 6.653   82.512  1.00 82.45  ?  26   ASN B O   1 
ATOM   4955  C CB  . ASN B  2  26  ? -49.357 5.399   80.178  1.00 81.04  ?  26   ASN B CB  1 
ATOM   4956  C CG  . ASN B  2  26  ? -48.378 4.309   79.776  1.00 80.49  ?  26   ASN B CG  1 
ATOM   4957  O OD1 . ASN B  2  26  ? -47.169 4.533   79.698  1.00 79.52  ?  26   ASN B OD1 1 
ATOM   4958  N ND2 . ASN B  2  26  ? -48.902 3.119   79.510  1.00 81.00  ?  26   ASN B ND2 1 
ATOM   4959  N N   . ALA B  2  27  ? -48.657 5.216   82.852  1.00 80.44  ?  27   ALA B N   1 
ATOM   4960  C CA  . ALA B  2  27  ? -48.178 4.819   84.172  1.00 82.17  ?  27   ALA B CA  1 
ATOM   4961  C C   . ALA B  2  27  ? -46.832 4.116   84.088  1.00 80.14  ?  27   ALA B C   1 
ATOM   4962  O O   . ALA B  2  27  ? -45.935 4.381   84.896  1.00 80.88  ?  27   ALA B O   1 
ATOM   4963  C CB  . ALA B  2  27  ? -49.211 3.927   84.856  1.00 85.06  ?  27   ALA B CB  1 
ATOM   4964  N N   . GLU B  2  28  ? -46.671 3.220   83.115  1.00 88.94  ?  28   GLU B N   1 
ATOM   4965  C CA  . GLU B  2  28  ? -45.396 2.529   82.962  1.00 88.92  ?  28   GLU B CA  1 
ATOM   4966  C C   . GLU B  2  28  ? -44.293 3.492   82.540  1.00 87.66  ?  28   GLU B C   1 
ATOM   4967  O O   . GLU B  2  28  ? -43.145 3.360   82.980  1.00 88.56  ?  28   GLU B O   1 
ATOM   4968  C CB  . GLU B  2  28  ? -45.540 1.390   81.954  1.00 86.61  ?  28   GLU B CB  1 
ATOM   4969  C CG  . GLU B  2  28  ? -46.407 0.250   82.461  1.00 87.77  ?  28   GLU B CG  1 
ATOM   4970  C CD  . GLU B  2  28  ? -46.542 -0.869  81.454  1.00 85.19  ?  28   GLU B CD  1 
ATOM   4971  O OE1 . GLU B  2  28  ? -45.662 -0.972  80.575  1.00 82.84  ?  28   GLU B OE1 1 
ATOM   4972  O OE2 . GLU B  2  28  ? -47.515 -1.651  81.551  1.00 85.79  -1 28   GLU B OE2 1 
ATOM   4973  N N   . GLY B  2  29  ? -44.623 4.465   81.689  1.00 85.77  ?  29   GLY B N   1 
ATOM   4974  C CA  . GLY B  2  29  ? -43.626 5.435   81.264  1.00 83.64  ?  29   GLY B CA  1 
ATOM   4975  C C   . GLY B  2  29  ? -43.192 6.372   82.377  1.00 84.44  ?  29   GLY B C   1 
ATOM   4976  O O   . GLY B  2  29  ? -42.017 6.741   82.463  1.00 84.28  ?  29   GLY B O   1 
ATOM   4977  N N   . ASP B  2  30  ? -44.133 6.777   83.238  1.00 82.82  ?  30   ASP B N   1 
ATOM   4978  C CA  . ASP B  2  30  ? -43.774 7.615   84.379  1.00 83.21  ?  30   ASP B CA  1 
ATOM   4979  C C   . ASP B  2  30  ? -42.867 6.865   85.348  1.00 85.03  ?  30   ASP B C   1 
ATOM   4980  O O   . ASP B  2  30  ? -41.967 7.460   85.951  1.00 85.14  ?  30   ASP B O   1 
ATOM   4981  C CB  . ASP B  2  30  ? -45.034 8.103   85.102  1.00 83.46  ?  30   ASP B CB  1 
ATOM   4982  C CG  . ASP B  2  30  ? -45.904 9.002   84.238  1.00 81.71  ?  30   ASP B CG  1 
ATOM   4983  O OD1 . ASP B  2  30  ? -45.358 9.884   83.545  1.00 80.09  ?  30   ASP B OD1 1 
ATOM   4984  O OD2 . ASP B  2  30  ? -47.141 8.834   84.266  1.00 82.08  -1 30   ASP B OD2 1 
ATOM   4985  N N   . ALA B  2  31  ? -43.091 5.556   85.510  1.00 82.93  ?  31   ALA B N   1 
ATOM   4986  C CA  . ALA B  2  31  ? -42.252 4.762   86.403  1.00 84.63  ?  31   ALA B CA  1 
ATOM   4987  C C   . ALA B  2  31  ? -40.828 4.647   85.874  1.00 83.25  ?  31   ALA B C   1 
ATOM   4988  O O   . ALA B  2  31  ? -39.864 4.788   86.636  1.00 84.55  ?  31   ALA B O   1 
ATOM   4989  C CB  . ALA B  2  31  ? -42.861 3.377   86.595  1.00 85.81  ?  31   ALA B CB  1 
ATOM   4990  N N   . LEU B  2  32  ? -40.678 4.406   84.568  1.00 84.11  ?  32   LEU B N   1 
ATOM   4991  C CA  . LEU B  2  32  ? -39.347 4.359   83.974  1.00 83.70  ?  32   LEU B CA  1 
ATOM   4992  C C   . LEU B  2  32  ? -38.739 5.747   83.892  1.00 82.89  ?  32   LEU B C   1 
ATOM   4993  O O   . LEU B  2  32  ? -37.511 5.887   83.918  1.00 83.12  ?  32   LEU B O   1 
ATOM   4994  C CB  . LEU B  2  32  ? -39.399 3.726   82.583  1.00 83.00  ?  32   LEU B CB  1 
ATOM   4995  C CG  . LEU B  2  32  ? -39.474 2.198   82.536  1.00 81.84  ?  32   LEU B CG  1 
ATOM   4996  C CD1 . LEU B  2  32  ? -39.891 1.722   81.152  1.00 78.77  ?  32   LEU B CD1 1 
ATOM   4997  C CD2 . LEU B  2  32  ? -38.149 1.581   82.944  1.00 81.49  ?  32   LEU B CD2 1 
ATOM   4998  N N   . SER B  2  33  ? -39.570 6.786   83.813  1.00 79.92  ?  33   SER B N   1 
ATOM   4999  C CA  . SER B  2  33  ? -39.005 8.115   83.939  1.00 79.58  ?  33   SER B CA  1 
ATOM   5000  C C   . SER B  2  33  ? -38.407 8.303   85.325  1.00 82.27  ?  33   SER B C   1 
ATOM   5001  O O   . SER B  2  33  ? -37.279 8.790   85.435  1.00 82.62  ?  33   SER B O   1 
ATOM   5002  C CB  . SER B  2  33  ? -40.078 9.166   83.638  1.00 78.63  ?  33   SER B CB  1 
ATOM   5003  O OG  . SER B  2  33  ? -40.530 9.081   82.292  1.00 76.03  ?  33   SER B OG  1 
ATOM   5004  N N   . ALA B  2  34  ? -39.032 7.728   86.357  1.00 81.98  ?  34   ALA B N   1 
ATOM   5005  C CA  . ALA B  2  34  ? -38.516 7.912   87.710  1.00 86.11  ?  34   ALA B CA  1 
ATOM   5006  C C   . ALA B  2  34  ? -37.122 7.319   87.831  1.00 86.55  ?  34   ALA B C   1 
ATOM   5007  O O   . ALA B  2  34  ? -36.228 7.937   88.419  1.00 88.86  ?  34   ALA B O   1 
ATOM   5008  C CB  . ALA B  2  34  ? -39.456 7.291   88.741  1.00 89.42  ?  34   ALA B CB  1 
ATOM   5009  N N   . LEU B  2  35  ? -36.914 6.127   87.265  1.00 87.12  ?  35   LEU B N   1 
ATOM   5010  C CA  . LEU B  2  35  ? -35.577 5.540   87.218  1.00 87.96  ?  35   LEU B CA  1 
ATOM   5011  C C   . LEU B  2  35  ? -34.601 6.453   86.479  1.00 87.60  ?  35   LEU B C   1 
ATOM   5012  O O   . LEU B  2  35  ? -33.468 6.668   86.929  1.00 89.06  ?  35   LEU B O   1 
ATOM   5013  C CB  . LEU B  2  35  ? -35.649 4.165   86.547  1.00 87.32  ?  35   LEU B CB  1 
ATOM   5014  C CG  . LEU B  2  35  ? -34.615 3.070   86.834  1.00 88.25  ?  35   LEU B CG  1 
ATOM   5015  C CD1 . LEU B  2  35  ? -34.870 1.858   85.951  1.00 86.49  ?  35   LEU B CD1 1 
ATOM   5016  C CD2 . LEU B  2  35  ? -33.206 3.557   86.630  1.00 88.97  ?  35   LEU B CD2 1 
ATOM   5017  N N   . LYS B  2  36  ? -35.026 6.992   85.333  1.00 84.17  ?  36   LYS B N   1 
ATOM   5018  C CA  . LYS B  2  36  ? -34.165 7.867   84.544  1.00 83.29  ?  36   LYS B CA  1 
ATOM   5019  C C   . LYS B  2  36  ? -33.683 9.076   85.342  1.00 84.55  ?  36   LYS B C   1 
ATOM   5020  O O   . LYS B  2  36  ? -32.577 9.572   85.096  1.00 85.03  ?  36   LYS B O   1 
ATOM   5021  C CB  . LYS B  2  36  ? -34.913 8.312   83.282  1.00 80.92  ?  36   LYS B CB  1 
ATOM   5022  C CG  . LYS B  2  36  ? -34.211 9.366   82.430  1.00 79.72  ?  36   LYS B CG  1 
ATOM   5023  C CD  . LYS B  2  36  ? -35.168 9.934   81.389  1.00 76.46  ?  36   LYS B CD  1 
ATOM   5024  C CE  . LYS B  2  36  ? -34.507 10.999  80.545  1.00 74.71  ?  36   LYS B CE  1 
ATOM   5025  N NZ  . LYS B  2  36  ? -33.639 10.384  79.522  1.00 74.20  ?  36   LYS B NZ  1 
ATOM   5026  N N   . ASN B  2  37  ? -34.474 9.550   86.314  1.00 89.25  ?  37   ASN B N   1 
ATOM   5027  C CA  . ASN B  2  37  ? -34.068 10.688  87.136  1.00 90.43  ?  37   ASN B CA  1 
ATOM   5028  C C   . ASN B  2  37  ? -33.193 10.307  88.325  1.00 93.20  ?  37   ASN B C   1 
ATOM   5029  O O   . ASN B  2  37  ? -32.561 11.191  88.914  1.00 94.73  ?  37   ASN B O   1 
ATOM   5030  C CB  . ASN B  2  37  ? -35.287 11.464  87.671  1.00 89.67  ?  37   ASN B CB  1 
ATOM   5031  C CG  . ASN B  2  37  ? -36.171 12.053  86.565  1.00 87.01  ?  37   ASN B CG  1 
ATOM   5032  O OD1 . ASN B  2  37  ? -36.952 11.344  85.923  1.00 85.80  ?  37   ASN B OD1 1 
ATOM   5033  N ND2 . ASN B  2  37  ? -36.052 13.369  86.351  1.00 86.28  ?  37   ASN B ND2 1 
ATOM   5034  N N   . SER B  2  38  ? -33.157 9.036   88.716  1.00 96.46  ?  38   SER B N   1 
ATOM   5035  C CA  . SER B  2  38  ? -32.337 8.598   89.840  1.00 99.02  ?  38   SER B CA  1 
ATOM   5036  C C   . SER B  2  38  ? -30.979 8.049   89.423  1.00 100.11 ?  38   SER B C   1 
ATOM   5037  O O   . SER B  2  38  ? -30.166 7.721   90.294  1.00 102.40 ?  38   SER B O   1 
ATOM   5038  C CB  . SER B  2  38  ? -33.086 7.549   90.662  1.00 99.45  ?  38   SER B CB  1 
ATOM   5039  O OG  . SER B  2  38  ? -32.206 6.745   91.433  1.00 101.53 ?  38   SER B OG  1 
ATOM   5040  N N   . LEU B  2  39  ? -30.710 7.934   88.128  1.00 97.26  ?  39   LEU B N   1 
ATOM   5041  C CA  . LEU B  2  39  ? -29.443 7.409   87.644  1.00 97.48  ?  39   LEU B CA  1 
ATOM   5042  C C   . LEU B  2  39  ? -28.655 8.514   86.962  1.00 97.27  ?  39   LEU B C   1 
ATOM   5043  O O   . LEU B  2  39  ? -29.209 9.282   86.167  1.00 95.03  ?  39   LEU B O   1 
ATOM   5044  C CB  . LEU B  2  39  ? -29.641 6.243   86.673  1.00 95.23  ?  39   LEU B CB  1 
ATOM   5045  C CG  . LEU B  2  39  ? -30.066 4.884   87.216  1.00 95.62  ?  39   LEU B CG  1 
ATOM   5046  C CD1 . LEU B  2  39  ? -29.865 3.855   86.124  1.00 93.49  ?  39   LEU B CD1 1 
ATOM   5047  C CD2 . LEU B  2  39  ? -29.290 4.511   88.459  1.00 101.23 ?  39   LEU B CD2 1 
ATOM   5048  N N   . ALA B  2  40  ? -27.371 8.605   87.298  1.00 98.16  ?  40   ALA B N   1 
ATOM   5049  C CA  . ALA B  2  40  ? -26.442 9.453   86.565  1.00 98.90  ?  40   ALA B CA  1 
ATOM   5050  C C   . ALA B  2  40  ? -26.012 8.711   85.309  1.00 98.05  ?  40   ALA B C   1 
ATOM   5051  O O   . ALA B  2  40  ? -25.477 7.599   85.389  1.00 98.58  ?  40   ALA B O   1 
ATOM   5052  C CB  . ALA B  2  40  ? -25.232 9.812   87.424  1.00 102.00 ?  40   ALA B CB  1 
ATOM   5053  N N   . ASP B  2  41  ? -26.260 9.318   84.149  1.00 96.46  ?  41   ASP B N   1 
ATOM   5054  C CA  . ASP B  2  41  ? -26.034 8.687   82.851  1.00 95.55  ?  41   ASP B CA  1 
ATOM   5055  C C   . ASP B  2  41  ? -24.960 9.496   82.135  1.00 96.98  ?  41   ASP B C   1 
ATOM   5056  O O   . ASP B  2  41  ? -25.269 10.478  81.441  1.00 95.81  ?  41   ASP B O   1 
ATOM   5057  C CB  . ASP B  2  41  ? -27.331 8.633   82.042  1.00 92.75  ?  41   ASP B CB  1 
ATOM   5058  C CG  . ASP B  2  41  ? -27.173 7.930   80.704  1.00 91.67  ?  41   ASP B CG  1 
ATOM   5059  O OD1 . ASP B  2  41  ? -26.059 7.911   80.146  1.00 92.75  ?  41   ASP B OD1 1 
ATOM   5060  O OD2 . ASP B  2  41  ? -28.183 7.397   80.201  1.00 89.52  -1 41   ASP B OD2 1 
ATOM   5061  N N   . PRO B  2  42  ? -23.682 9.114   82.267  1.00 91.14  ?  42   PRO B N   1 
ATOM   5062  C CA  . PRO B  2  42  ? -22.619 9.829   81.549  1.00 96.50  ?  42   PRO B CA  1 
ATOM   5063  C C   . PRO B  2  42  ? -22.549 9.453   80.076  1.00 98.93  ?  42   PRO B C   1 
ATOM   5064  O O   . PRO B  2  42  ? -22.148 10.268  79.239  1.00 103.64 ?  42   PRO B O   1 
ATOM   5065  C CB  . PRO B  2  42  ? -21.350 9.406   82.299  1.00 98.11  ?  42   PRO B CB  1 
ATOM   5066  C CG  . PRO B  2  42  ? -21.672 8.045   82.826  1.00 94.15  ?  42   PRO B CG  1 
ATOM   5067  C CD  . PRO B  2  42  ? -23.150 8.047   83.135  1.00 89.73  ?  42   PRO B CD  1 
ATOM   5068  N N   . ASN B  2  43  ? -22.947 8.225   79.750  1.00 92.39  ?  43   ASN B N   1 
ATOM   5069  C CA  . ASN B  2  43  ? -22.832 7.697   78.397  1.00 94.31  ?  43   ASN B CA  1 
ATOM   5070  C C   . ASN B  2  43  ? -24.051 7.985   77.527  1.00 92.45  ?  43   ASN B C   1 
ATOM   5071  O O   . ASN B  2  43  ? -24.089 7.532   76.377  1.00 93.44  ?  43   ASN B O   1 
ATOM   5072  C CB  . ASN B  2  43  ? -22.574 6.188   78.450  1.00 91.96  ?  43   ASN B CB  1 
ATOM   5073  C CG  . ASN B  2  43  ? -21.099 5.858   78.564  1.00 96.10  ?  43   ASN B CG  1 
ATOM   5074  O OD1 . ASN B  2  43  ? -20.592 5.594   79.654  1.00 95.18  ?  43   ASN B OD1 1 
ATOM   5075  N ND2 . ASN B  2  43  ? -20.400 5.875   77.434  1.00 101.01 ?  43   ASN B ND2 1 
ATOM   5076  N N   . LYS B  2  44  ? -25.039 8.717   78.049  1.00 91.88  ?  44   LYS B N   1 
ATOM   5077  C CA  . LYS B  2  44  ? -26.221 9.148   77.291  1.00 90.26  ?  44   LYS B CA  1 
ATOM   5078  C C   . LYS B  2  44  ? -27.024 7.957   76.766  1.00 85.97  ?  44   LYS B C   1 
ATOM   5079  O O   . LYS B  2  44  ? -27.585 7.998   75.669  1.00 85.82  ?  44   LYS B O   1 
ATOM   5080  C CB  . LYS B  2  44  ? -25.834 10.093  76.149  1.00 95.94  ?  44   LYS B CB  1 
ATOM   5081  C CG  . LYS B  2  44  ? -25.229 11.417  76.605  1.00 100.31 ?  44   LYS B CG  1 
ATOM   5082  C CD  . LYS B  2  44  ? -25.851 11.897  77.910  1.00 96.35  ?  44   LYS B CD  1 
ATOM   5083  C CE  . LYS B  2  44  ? -25.101 13.091  78.483  1.00 99.80  ?  44   LYS B CE  1 
ATOM   5084  N NZ  . LYS B  2  44  ? -25.931 14.329  78.479  1.00 99.33  ?  44   LYS B NZ  1 
ATOM   5085  N N   . VAL B  2  45  ? -27.085 6.889   77.563  1.00 88.40  ?  45   VAL B N   1 
ATOM   5086  C CA  . VAL B  2  45  ? -27.860 5.709   77.182  1.00 84.75  ?  45   VAL B CA  1 
ATOM   5087  C C   . VAL B  2  45  ? -29.355 6.012   77.220  1.00 81.77  ?  45   VAL B C   1 
ATOM   5088  O O   . VAL B  2  45  ? -30.100 5.671   76.293  1.00 80.40  ?  45   VAL B O   1 
ATOM   5089  C CB  . VAL B  2  45  ? -27.503 4.520   78.090  1.00 83.19  ?  45   VAL B CB  1 
ATOM   5090  C CG1 . VAL B  2  45  ? -28.674 3.565   78.194  1.00 79.79  ?  45   VAL B CG1 1 
ATOM   5091  C CG2 . VAL B  2  45  ? -26.275 3.801   77.564  1.00 85.58  ?  45   VAL B CG2 1 
ATOM   5092  N N   . LEU B  2  46  ? -29.814 6.650   78.296  1.00 80.43  ?  46   LEU B N   1 
ATOM   5093  C CA  . LEU B  2  46  ? -31.233 6.869   78.545  1.00 78.10  ?  46   LEU B CA  1 
ATOM   5094  C C   . LEU B  2  46  ? -31.808 8.057   77.781  1.00 78.87  ?  46   LEU B C   1 
ATOM   5095  O O   . LEU B  2  46  ? -32.924 8.486   78.093  1.00 77.42  ?  46   LEU B O   1 
ATOM   5096  C CB  . LEU B  2  46  ? -31.475 7.055   80.047  1.00 77.41  ?  46   LEU B CB  1 
ATOM   5097  C CG  . LEU B  2  46  ? -31.358 5.797   80.911  1.00 76.59  ?  46   LEU B CG  1 
ATOM   5098  C CD1 . LEU B  2  46  ? -32.205 5.935   82.161  1.00 76.00  ?  46   LEU B CD1 1 
ATOM   5099  C CD2 . LEU B  2  46  ? -31.751 4.544   80.130  1.00 75.64  ?  46   LEU B CD2 1 
ATOM   5100  N N   . GLN B  2  47  ? -31.091 8.590   76.791  1.00 74.40  ?  47   GLN B N   1 
ATOM   5101  C CA  . GLN B  2  47  ? -31.548 9.803   76.120  1.00 76.01  ?  47   GLN B CA  1 
ATOM   5102  C C   . GLN B  2  47  ? -32.900 9.596   75.446  1.00 73.47  ?  47   GLN B C   1 
ATOM   5103  O O   . GLN B  2  47  ? -33.772 10.470  75.509  1.00 73.06  ?  47   GLN B O   1 
ATOM   5104  C CB  . GLN B  2  47  ? -30.503 10.259  75.102  1.00 80.79  ?  47   GLN B CB  1 
ATOM   5105  C CG  . GLN B  2  47  ? -31.071 11.108  73.986  1.00 82.83  ?  47   GLN B CG  1 
ATOM   5106  C CD  . GLN B  2  47  ? -30.185 12.283  73.656  1.00 89.17  ?  47   GLN B CD  1 
ATOM   5107  O OE1 . GLN B  2  47  ? -28.961 12.154  73.602  1.00 93.22  ?  47   GLN B OE1 1 
ATOM   5108  N NE2 . GLN B  2  47  ? -30.796 13.443  73.436  1.00 90.67  ?  47   GLN B NE2 1 
ATOM   5109  N N   . SER B  2  48  ? -33.098 8.439   74.811  1.00 72.44  ?  48   SER B N   1 
ATOM   5110  C CA  . SER B  2  48  ? -34.322 8.173   74.063  1.00 70.67  ?  48   SER B CA  1 
ATOM   5111  C C   . SER B  2  48  ? -35.566 8.151   74.943  1.00 68.61  ?  48   SER B C   1 
ATOM   5112  O O   . SER B  2  48  ? -36.681 8.175   74.408  1.00 67.80  ?  48   SER B O   1 
ATOM   5113  C CB  . SER B  2  48  ? -34.195 6.847   73.307  1.00 69.64  ?  48   SER B CB  1 
ATOM   5114  O OG  . SER B  2  48  ? -33.706 5.808   74.141  1.00 68.74  ?  48   SER B OG  1 
ATOM   5115  N N   . TRP B  2  49  ? -35.406 8.106   76.266  1.00 72.34  ?  49   TRP B N   1 
ATOM   5116  C CA  . TRP B  2  49  ? -36.529 7.966   77.195  1.00 71.15  ?  49   TRP B CA  1 
ATOM   5117  C C   . TRP B  2  49  ? -37.247 9.310   77.310  1.00 71.22  ?  49   TRP B C   1 
ATOM   5118  O O   . TRP B  2  49  ? -37.083 10.073  78.267  1.00 71.42  ?  49   TRP B O   1 
ATOM   5119  C CB  . TRP B  2  49  ? -36.041 7.457   78.548  1.00 71.13  ?  49   TRP B CB  1 
ATOM   5120  C CG  . TRP B  2  49  ? -35.584 6.019   78.525  1.00 71.05  ?  49   TRP B CG  1 
ATOM   5121  C CD1 . TRP B  2  49  ? -35.148 5.311   77.439  1.00 71.00  ?  49   TRP B CD1 1 
ATOM   5122  C CD2 . TRP B  2  49  ? -35.537 5.111   79.636  1.00 71.33  ?  49   TRP B CD2 1 
ATOM   5123  N NE1 . TRP B  2  49  ? -34.825 4.027   77.807  1.00 71.05  ?  49   TRP B NE1 1 
ATOM   5124  C CE2 . TRP B  2  49  ? -35.056 3.878   79.149  1.00 71.44  ?  49   TRP B CE2 1 
ATOM   5125  C CE3 . TRP B  2  49  ? -35.852 5.222   80.993  1.00 71.83  ?  49   TRP B CE3 1 
ATOM   5126  C CZ2 . TRP B  2  49  ? -34.883 2.767   79.972  1.00 72.22  ?  49   TRP B CZ2 1 
ATOM   5127  C CZ3 . TRP B  2  49  ? -35.679 4.117   81.808  1.00 72.74  ?  49   TRP B CZ3 1 
ATOM   5128  C CH2 . TRP B  2  49  ? -35.199 2.906   81.295  1.00 73.00  ?  49   TRP B CH2 1 
ATOM   5129  N N   . ASP B  2  50  ? -38.070 9.591   76.298  1.00 65.72  ?  50   ASP B N   1 
ATOM   5130  C CA  . ASP B  2  50  ? -38.832 10.834  76.215  1.00 65.69  ?  50   ASP B CA  1 
ATOM   5131  C C   . ASP B  2  50  ? -40.123 10.672  77.006  1.00 64.40  ?  50   ASP B C   1 
ATOM   5132  O O   . ASP B  2  50  ? -41.015 9.913   76.610  1.00 63.90  ?  50   ASP B O   1 
ATOM   5133  C CB  . ASP B  2  50  ? -39.116 11.184  74.757  1.00 66.47  ?  50   ASP B CB  1 
ATOM   5134  C CG  . ASP B  2  50  ? -39.877 12.487  74.602  1.00 66.63  ?  50   ASP B CG  1 
ATOM   5135  O OD1 . ASP B  2  50  ? -40.049 13.212  75.601  1.00 66.02  ?  50   ASP B OD1 1 
ATOM   5136  O OD2 . ASP B  2  50  ? -40.304 12.789  73.470  1.00 67.43  -1 50   ASP B OD2 1 
ATOM   5137  N N   . ALA B  2  51  ? -40.235 11.419  78.107  1.00 66.37  ?  51   ALA B N   1 
ATOM   5138  C CA  . ALA B  2  51  ? -41.325 11.232  79.056  1.00 65.75  ?  51   ALA B CA  1 
ATOM   5139  C C   . ALA B  2  51  ? -42.672 11.691  78.516  1.00 64.89  ?  51   ALA B C   1 
ATOM   5140  O O   . ALA B  2  51  ? -43.708 11.226  79.003  1.00 64.65  ?  51   ALA B O   1 
ATOM   5141  C CB  . ALA B  2  51  ? -41.011 11.971  80.356  1.00 65.99  ?  51   ALA B CB  1 
ATOM   5142  N N   . THR B  2  52  ? -42.690 12.583  77.530  1.00 64.96  ?  52   THR B N   1 
ATOM   5143  C CA  . THR B  2  52  ? -43.942 13.126  77.022  1.00 64.15  ?  52   THR B CA  1 
ATOM   5144  C C   . THR B  2  52  ? -44.615 12.216  76.000  1.00 64.26  ?  52   THR B C   1 
ATOM   5145  O O   . THR B  2  52  ? -45.600 12.630  75.379  1.00 63.89  ?  52   THR B O   1 
ATOM   5146  C CB  . THR B  2  52  ? -43.705 14.508  76.413  1.00 64.51  ?  52   THR B CB  1 
ATOM   5147  O OG1 . THR B  2  52  ? -42.945 14.373  75.208  1.00 66.06  ?  52   THR B OG1 1 
ATOM   5148  C CG2 . THR B  2  52  ? -42.938 15.380  77.382  1.00 64.65  ?  52   THR B CG2 1 
ATOM   5149  N N   . LEU B  2  53  ? -44.101 11.006  75.797  1.00 63.82  ?  53   LEU B N   1 
ATOM   5150  C CA  . LEU B  2  53  ? -44.755 10.044  74.925  1.00 64.34  ?  53   LEU B CA  1 
ATOM   5151  C C   . LEU B  2  53  ? -45.859 9.309   75.686  1.00 65.89  ?  53   LEU B C   1 
ATOM   5152  O O   . LEU B  2  53  ? -45.851 9.224   76.916  1.00 66.52  ?  53   LEU B O   1 
ATOM   5153  C CB  . LEU B  2  53  ? -43.737 9.045   74.364  1.00 63.82  ?  53   LEU B CB  1 
ATOM   5154  C CG  . LEU B  2  53  ? -42.955 9.375   73.087  1.00 63.03  ?  53   LEU B CG  1 
ATOM   5155  C CD1 . LEU B  2  53  ? -42.616 10.851  72.985  1.00 62.41  ?  53   LEU B CD1 1 
ATOM   5156  C CD2 . LEU B  2  53  ? -41.685 8.543   73.025  1.00 62.65  ?  53   LEU B CD2 1 
ATOM   5157  N N   . VAL B  2  54  ? -46.824 8.777   74.931  1.00 71.19  ?  54   VAL B N   1 
ATOM   5158  C CA  . VAL B  2  54  ? -47.918 8.022   75.542  1.00 71.18  ?  54   VAL B CA  1 
ATOM   5159  C C   . VAL B  2  54  ? -47.377 6.777   76.242  1.00 72.53  ?  54   VAL B C   1 
ATOM   5160  O O   . VAL B  2  54  ? -47.612 6.563   77.437  1.00 73.01  ?  54   VAL B O   1 
ATOM   5161  C CB  . VAL B  2  54  ? -48.982 7.669   74.485  1.00 70.34  ?  54   VAL B CB  1 
ATOM   5162  C CG1 . VAL B  2  54  ? -49.822 6.489   74.931  1.00 70.97  ?  54   VAL B CG1 1 
ATOM   5163  C CG2 . VAL B  2  54  ? -49.872 8.863   74.200  1.00 68.75  ?  54   VAL B CG2 1 
ATOM   5164  N N   . THR B  2  55  ? -46.628 5.949   75.517  1.00 75.06  ?  55   THR B N   1 
ATOM   5165  C CA  . THR B  2  55  ? -45.999 4.759   76.066  1.00 76.12  ?  55   THR B CA  1 
ATOM   5166  C C   . THR B  2  55  ? -44.502 4.788   75.795  1.00 75.83  ?  55   THR B C   1 
ATOM   5167  O O   . THR B  2  55  ? -44.050 5.417   74.830  1.00 74.93  ?  55   THR B O   1 
ATOM   5168  C CB  . THR B  2  55  ? -46.593 3.467   75.479  1.00 76.85  ?  55   THR B CB  1 
ATOM   5169  O OG1 . THR B  2  55  ? -46.153 3.300   74.127  1.00 75.58  ?  55   THR B OG1 1 
ATOM   5170  C CG2 . THR B  2  55  ? -48.100 3.498   75.514  1.00 76.64  ?  55   THR B CG2 1 
ATOM   5171  N N   . PRO B  2  56  ? -43.709 4.118   76.633  1.00 73.98  ?  56   PRO B N   1 
ATOM   5172  C CA  . PRO B  2  56  ? -42.260 4.050   76.408  1.00 73.76  ?  56   PRO B CA  1 
ATOM   5173  C C   . PRO B  2  56  ? -41.827 2.994   75.400  1.00 73.75  ?  56   PRO B C   1 
ATOM   5174  O O   . PRO B  2  56  ? -40.640 2.664   75.351  1.00 73.77  ?  56   PRO B O   1 
ATOM   5175  C CB  . PRO B  2  56  ? -41.724 3.718   77.811  1.00 74.95  ?  56   PRO B CB  1 
ATOM   5176  C CG  . PRO B  2  56  ? -42.816 2.943   78.445  1.00 76.45  ?  56   PRO B CG  1 
ATOM   5177  C CD  . PRO B  2  56  ? -44.089 3.565   77.947  1.00 75.52  ?  56   PRO B CD  1 
ATOM   5178  N N   . CYS B  2  57  ? -42.755 2.449   74.611  1.00 75.04  ?  57   CYS B N   1 
ATOM   5179  C CA  . CYS B  2  57  ? -42.438 1.332   73.728  1.00 75.04  ?  57   CYS B CA  1 
ATOM   5180  C C   . CYS B  2  57  ? -41.594 1.739   72.524  1.00 74.00  ?  57   CYS B C   1 
ATOM   5181  O O   . CYS B  2  57  ? -41.005 0.863   71.880  1.00 73.99  ?  57   CYS B O   1 
ATOM   5182  C CB  . CYS B  2  57  ? -43.729 0.662   73.260  1.00 75.08  ?  57   CYS B CB  1 
ATOM   5183  S SG  . CYS B  2  57  ? -44.711 -0.068  74.606  1.00 77.14  ?  57   CYS B SG  1 
ATOM   5184  N N   . THR B  2  58  ? -41.525 3.030   72.200  1.00 69.11  ?  58   THR B N   1 
ATOM   5185  C CA  . THR B  2  58  ? -40.638 3.516   71.150  1.00 68.93  ?  58   THR B CA  1 
ATOM   5186  C C   . THR B  2  58  ? -39.266 3.917   71.682  1.00 69.26  ?  58   THR B C   1 
ATOM   5187  O O   . THR B  2  58  ? -38.414 4.346   70.897  1.00 69.58  ?  58   THR B O   1 
ATOM   5188  C CB  . THR B  2  58  ? -41.272 4.705   70.407  1.00 68.89  ?  58   THR B CB  1 
ATOM   5189  O OG1 . THR B  2  58  ? -41.471 5.793   71.314  1.00 69.01  ?  58   THR B OG1 1 
ATOM   5190  C CG2 . THR B  2  58  ? -42.611 4.318   69.813  1.00 68.32  ?  58   THR B CG2 1 
ATOM   5191  N N   . TRP B  2  59  ? -39.034 3.799   72.989  1.00 68.72  ?  59   TRP B N   1 
ATOM   5192  C CA  . TRP B  2  59  ? -37.721 4.081   73.546  1.00 68.98  ?  59   TRP B CA  1 
ATOM   5193  C C   . TRP B  2  59  ? -36.762 2.945   73.222  1.00 69.03  ?  59   TRP B C   1 
ATOM   5194  O O   . TRP B  2  59  ? -37.171 1.828   72.891  1.00 68.99  ?  59   TRP B O   1 
ATOM   5195  C CB  . TRP B  2  59  ? -37.780 4.253   75.065  1.00 69.23  ?  59   TRP B CB  1 
ATOM   5196  C CG  . TRP B  2  59  ? -38.722 5.303   75.571  1.00 69.13  ?  59   TRP B CG  1 
ATOM   5197  C CD1 . TRP B  2  59  ? -39.466 6.172   74.831  1.00 68.85  ?  59   TRP B CD1 1 
ATOM   5198  C CD2 . TRP B  2  59  ? -39.016 5.591   76.943  1.00 69.40  ?  59   TRP B CD2 1 
ATOM   5199  N NE1 . TRP B  2  59  ? -40.208 6.980   75.657  1.00 68.70  ?  59   TRP B NE1 1 
ATOM   5200  C CE2 . TRP B  2  59  ? -39.947 6.643   76.958  1.00 69.04  ?  59   TRP B CE2 1 
ATOM   5201  C CE3 . TRP B  2  59  ? -38.583 5.057   78.158  1.00 70.08  ?  59   TRP B CE3 1 
ATOM   5202  C CZ2 . TRP B  2  59  ? -40.450 7.173   78.139  1.00 69.18  ?  59   TRP B CZ2 1 
ATOM   5203  C CZ3 . TRP B  2  59  ? -39.081 5.585   79.329  1.00 70.49  ?  59   TRP B CZ3 1 
ATOM   5204  C CH2 . TRP B  2  59  ? -40.005 6.631   79.313  1.00 69.99  ?  59   TRP B CH2 1 
ATOM   5205  N N   . PHE B  2  60  ? -35.467 3.240   73.321  1.00 68.36  ?  60   PHE B N   1 
ATOM   5206  C CA  . PHE B  2  60  ? -34.464 2.203   73.136  1.00 68.48  ?  60   PHE B CA  1 
ATOM   5207  C C   . PHE B  2  60  ? -34.226 1.457   74.445  1.00 68.71  ?  60   PHE B C   1 
ATOM   5208  O O   . PHE B  2  60  ? -34.529 1.949   75.536  1.00 68.87  ?  60   PHE B O   1 
ATOM   5209  C CB  . PHE B  2  60  ? -33.151 2.794   72.615  1.00 69.54  ?  60   PHE B CB  1 
ATOM   5210  C CG  . PHE B  2  60  ? -33.288 3.525   71.305  1.00 70.21  ?  60   PHE B CG  1 
ATOM   5211  C CD1 . PHE B  2  60  ? -34.028 2.988   70.267  1.00 69.34  ?  60   PHE B CD1 1 
ATOM   5212  C CD2 . PHE B  2  60  ? -32.677 4.752   71.118  1.00 72.36  ?  60   PHE B CD2 1 
ATOM   5213  C CE1 . PHE B  2  60  ? -34.156 3.663   69.074  1.00 70.12  ?  60   PHE B CE1 1 
ATOM   5214  C CE2 . PHE B  2  60  ? -32.805 5.432   69.929  1.00 73.73  ?  60   PHE B CE2 1 
ATOM   5215  C CZ  . PHE B  2  60  ? -33.543 4.887   68.905  1.00 72.36  ?  60   PHE B CZ  1 
ATOM   5216  N N   . HIS B  2  61  ? -33.691 0.242   74.321  1.00 76.20  ?  61   HIS B N   1 
ATOM   5217  C CA  . HIS B  2  61  ? -33.395 -0.657  75.434  1.00 76.99  ?  61   HIS B CA  1 
ATOM   5218  C C   . HIS B  2  61  ? -34.649 -1.117  76.173  1.00 77.93  ?  61   HIS B C   1 
ATOM   5219  O O   . HIS B  2  61  ? -34.543 -1.788  77.205  1.00 79.30  ?  61   HIS B O   1 
ATOM   5220  C CB  . HIS B  2  61  ? -32.396 -0.023  76.413  1.00 77.18  ?  61   HIS B CB  1 
ATOM   5221  C CG  . HIS B  2  61  ? -31.266 0.691   75.736  1.00 77.47  ?  61   HIS B CG  1 
ATOM   5222  N ND1 . HIS B  2  61  ? -30.334 0.039   74.956  1.00 78.15  ?  61   HIS B ND1 1 
ATOM   5223  C CD2 . HIS B  2  61  ? -30.925 2.002   75.710  1.00 78.10  ?  61   HIS B CD2 1 
ATOM   5224  C CE1 . HIS B  2  61  ? -29.465 0.916   74.484  1.00 79.59  ?  61   HIS B CE1 1 
ATOM   5225  N NE2 . HIS B  2  61  ? -29.801 2.114   74.927  1.00 79.76  ?  61   HIS B NE2 1 
ATOM   5226  N N   . VAL B  2  62  ? -35.832 -0.788  75.658  1.00 76.59  ?  62   VAL B N   1 
ATOM   5227  C CA  . VAL B  2  62  ? -37.106 -1.219  76.217  1.00 77.54  ?  62   VAL B CA  1 
ATOM   5228  C C   . VAL B  2  62  ? -37.908 -1.877  75.103  1.00 79.23  ?  62   VAL B C   1 
ATOM   5229  O O   . VAL B  2  62  ? -38.090 -1.282  74.036  1.00 79.40  ?  62   VAL B O   1 
ATOM   5230  C CB  . VAL B  2  62  ? -37.892 -0.033  76.811  1.00 77.68  ?  62   VAL B CB  1 
ATOM   5231  C CG1 . VAL B  2  62  ? -39.325 -0.436  77.114  1.00 79.85  ?  62   VAL B CG1 1 
ATOM   5232  C CG2 . VAL B  2  62  ? -37.202 0.493   78.054  1.00 76.81  ?  62   VAL B CG2 1 
ATOM   5233  N N   . THR B  2  63  ? -38.403 -3.086  75.352  1.00 79.73  ?  63   THR B N   1 
ATOM   5234  C CA  . THR B  2  63  ? -39.237 -3.793  74.389  1.00 82.49  ?  63   THR B CA  1 
ATOM   5235  C C   . THR B  2  63  ? -40.579 -4.131  75.030  1.00 85.51  ?  63   THR B C   1 
ATOM   5236  O O   . THR B  2  63  ? -40.641 -4.505  76.207  1.00 84.82  ?  63   THR B O   1 
ATOM   5237  C CB  . THR B  2  63  ? -38.548 -5.072  73.863  1.00 83.63  ?  63   THR B CB  1 
ATOM   5238  O OG1 . THR B  2  63  ? -38.741 -6.148  74.786  1.00 85.06  ?  63   THR B OG1 1 
ATOM   5239  C CG2 . THR B  2  63  ? -37.054 -4.850  73.668  1.00 81.64  ?  63   THR B CG2 1 
ATOM   5240  N N   . CYS B  2  64  ? -41.651 -3.971  74.257  1.00 82.43  ?  64   CYS B N   1 
ATOM   5241  C CA  . CYS B  2  64  ? -43.017 -4.216  74.697  1.00 86.25  ?  64   CYS B CA  1 
ATOM   5242  C C   . CYS B  2  64  ? -43.617 -5.409  73.967  1.00 89.98  ?  64   CYS B C   1 
ATOM   5243  O O   . CYS B  2  64  ? -43.135 -5.831  72.912  1.00 90.27  ?  64   CYS B O   1 
ATOM   5244  C CB  . CYS B  2  64  ? -43.913 -2.994  74.462  1.00 88.46  ?  64   CYS B CB  1 
ATOM   5245  S SG  . CYS B  2  64  ? -43.524 -1.522  75.424  1.00 85.63  ?  64   CYS B SG  1 
ATOM   5246  N N   . ASN B  2  65  ? -44.688 -5.949  74.543  1.00 87.17  ?  65   ASN B N   1 
ATOM   5247  C CA  . ASN B  2  65  ? -45.474 -6.976  73.880  1.00 90.61  ?  65   ASN B CA  1 
ATOM   5248  C C   . ASN B  2  65  ? -46.549 -6.301  73.029  1.00 92.74  ?  65   ASN B C   1 
ATOM   5249  O O   . ASN B  2  65  ? -46.541 -5.084  72.830  1.00 92.10  ?  65   ASN B O   1 
ATOM   5250  C CB  . ASN B  2  65  ? -46.051 -7.965  74.897  1.00 92.44  ?  65   ASN B CB  1 
ATOM   5251  C CG  . ASN B  2  65  ? -46.930 -7.304  75.949  1.00 93.20  ?  65   ASN B CG  1 
ATOM   5252  O OD1 . ASN B  2  65  ? -47.495 -6.231  75.737  1.00 93.89  ?  65   ASN B OD1 1 
ATOM   5253  N ND2 . ASN B  2  65  ? -47.052 -7.960  77.098  1.00 93.59  ?  65   ASN B ND2 1 
ATOM   5254  N N   . SER B  2  66  ? -47.488 -7.090  72.507  1.00 91.69  ?  66   SER B N   1 
ATOM   5255  C CA  . SER B  2  66  ? -48.499 -6.544  71.612  1.00 93.26  ?  66   SER B CA  1 
ATOM   5256  C C   . SER B  2  66  ? -49.436 -5.570  72.315  1.00 95.04  ?  66   SER B C   1 
ATOM   5257  O O   . SER B  2  66  ? -50.082 -4.759  71.642  1.00 95.13  ?  66   SER B O   1 
ATOM   5258  C CB  . SER B  2  66  ? -49.304 -7.680  70.980  1.00 95.46  ?  66   SER B CB  1 
ATOM   5259  O OG  . SER B  2  66  ? -49.639 -8.660  71.946  1.00 97.60  ?  66   SER B OG  1 
ATOM   5260  N N   . ASP B  2  67  ? -49.529 -5.630  73.642  1.00 94.72  ?  67   ASP B N   1 
ATOM   5261  C CA  . ASP B  2  67  ? -50.409 -4.756  74.405  1.00 97.43  ?  67   ASP B CA  1 
ATOM   5262  C C   . ASP B  2  67  ? -49.732 -3.468  74.858  1.00 95.60  ?  67   ASP B C   1 
ATOM   5263  O O   . ASP B  2  67  ? -50.320 -2.723  75.650  1.00 97.06  ?  67   ASP B O   1 
ATOM   5264  C CB  . ASP B  2  67  ? -50.961 -5.504  75.619  1.00 98.14  ?  67   ASP B CB  1 
ATOM   5265  C CG  . ASP B  2  67  ? -51.884 -6.634  75.229  1.00 100.23 ?  67   ASP B CG  1 
ATOM   5266  O OD1 . ASP B  2  67  ? -52.366 -6.634  74.076  1.00 101.58 ?  67   ASP B OD1 1 
ATOM   5267  O OD2 . ASP B  2  67  ? -52.137 -7.515  76.075  1.00 100.92 -1 67   ASP B OD2 1 
ATOM   5268  N N   . ASN B  2  68  ? -48.517 -3.193  74.378  1.00 93.14  ?  68   ASN B N   1 
ATOM   5269  C CA  . ASN B  2  68  ? -47.756 -1.996  74.744  1.00 90.71  ?  68   ASN B CA  1 
ATOM   5270  C C   . ASN B  2  68  ? -47.415 -1.962  76.233  1.00 89.55  ?  68   ASN B C   1 
ATOM   5271  O O   . ASN B  2  68  ? -47.250 -0.889  76.819  1.00 89.35  ?  68   ASN B O   1 
ATOM   5272  C CB  . ASN B  2  68  ? -48.489 -0.713  74.337  1.00 92.02  ?  68   ASN B CB  1 
ATOM   5273  C CG  . ASN B  2  68  ? -48.813 -0.672  72.858  1.00 91.36  ?  68   ASN B CG  1 
ATOM   5274  O OD1 . ASN B  2  68  ? -49.801 -1.254  72.414  1.00 92.96  ?  68   ASN B OD1 1 
ATOM   5275  N ND2 . ASN B  2  68  ? -47.980 0.019   72.087  1.00 88.83  ?  68   ASN B ND2 1 
ATOM   5276  N N   . SER B  2  69  ? -47.306 -3.131  76.857  1.00 96.41  ?  69   SER B N   1 
ATOM   5277  C CA  . SER B  2  69  ? -46.830 -3.243  78.228  1.00 93.52  ?  69   SER B CA  1 
ATOM   5278  C C   . SER B  2  69  ? -45.372 -3.672  78.206  1.00 88.14  ?  69   SER B C   1 
ATOM   5279  O O   . SER B  2  69  ? -44.996 -4.581  77.461  1.00 87.64  ?  69   SER B O   1 
ATOM   5280  C CB  . SER B  2  69  ? -47.665 -4.247  79.028  1.00 95.30  ?  69   SER B CB  1 
ATOM   5281  O OG  . SER B  2  69  ? -47.270 -4.281  80.393  1.00 93.73  ?  69   SER B OG  1 
ATOM   5282  N N   . VAL B  2  70  ? -44.552 -3.016  79.026  1.00 96.05  ?  70   VAL B N   1 
ATOM   5283  C CA  . VAL B  2  70  ? -43.113 -3.245  78.980  1.00 90.67  ?  70   VAL B CA  1 
ATOM   5284  C C   . VAL B  2  70  ? -42.801 -4.648  79.483  1.00 89.99  ?  70   VAL B C   1 
ATOM   5285  O O   . VAL B  2  70  ? -43.270 -5.064  80.552  1.00 90.89  ?  70   VAL B O   1 
ATOM   5286  C CB  . VAL B  2  70  ? -42.378 -2.176  79.801  1.00 86.84  ?  70   VAL B CB  1 
ATOM   5287  C CG1 . VAL B  2  70  ? -40.922 -2.563  80.011  1.00 81.80  ?  70   VAL B CG1 1 
ATOM   5288  C CG2 . VAL B  2  70  ? -42.479 -0.828  79.112  1.00 87.24  ?  70   VAL B CG2 1 
ATOM   5289  N N   . THR B  2  71  ? -41.996 -5.385  78.711  1.00 90.62  ?  71   THR B N   1 
ATOM   5290  C CA  . THR B  2  71  ? -41.584 -6.733  79.072  1.00 90.53  ?  71   THR B CA  1 
ATOM   5291  C C   . THR B  2  71  ? -40.083 -6.886  79.246  1.00 86.39  ?  71   THR B C   1 
ATOM   5292  O O   . THR B  2  71  ? -39.649 -7.863  79.868  1.00 85.96  ?  71   THR B O   1 
ATOM   5293  C CB  . THR B  2  71  ? -42.061 -7.748  78.018  1.00 94.66  ?  71   THR B CB  1 
ATOM   5294  O OG1 . THR B  2  71  ? -41.391 -7.507  76.774  1.00 94.23  ?  71   THR B OG1 1 
ATOM   5295  C CG2 . THR B  2  71  ? -43.564 -7.641  77.810  1.00 99.20  ?  71   THR B CG2 1 
ATOM   5296  N N   . ARG B  2  72  ? -39.283 -5.972  78.707  1.00 88.99  ?  72   ARG B N   1 
ATOM   5297  C CA  . ARG B  2  72  ? -37.839 -6.061  78.826  1.00 85.63  ?  72   ARG B CA  1 
ATOM   5298  C C   . ARG B  2  72  ? -37.250 -4.685  79.109  1.00 82.15  ?  72   ARG B C   1 
ATOM   5299  O O   . ARG B  2  72  ? -37.761 -3.670  78.624  1.00 82.43  ?  72   ARG B O   1 
ATOM   5300  C CB  . ARG B  2  72  ? -37.245 -6.667  77.552  1.00 86.99  ?  72   ARG B CB  1 
ATOM   5301  C CG  . ARG B  2  72  ? -35.809 -7.082  77.667  1.00 85.37  ?  72   ARG B CG  1 
ATOM   5302  C CD  . ARG B  2  72  ? -35.382 -7.895  76.459  1.00 87.70  ?  72   ARG B CD  1 
ATOM   5303  N NE  . ARG B  2  72  ? -34.423 -8.924  76.838  1.00 87.67  ?  72   ARG B NE  1 
ATOM   5304  C CZ  . ARG B  2  72  ? -34.658 -10.228 76.822  1.00 90.33  ?  72   ARG B CZ  1 
ATOM   5305  N NH1 . ARG B  2  72  ? -35.809 -10.720 76.392  1.00 93.49  ?  72   ARG B NH1 1 
ATOM   5306  N NH2 . ARG B  2  72  ? -33.715 -11.060 77.252  1.00 90.32  ?  72   ARG B NH2 1 
ATOM   5307  N N   . VAL B  2  73  ? -36.188 -4.656  79.912  1.00 88.82  ?  73   VAL B N   1 
ATOM   5308  C CA  . VAL B  2  73  ? -35.364 -3.466  80.128  1.00 86.00  ?  73   VAL B CA  1 
ATOM   5309  C C   . VAL B  2  73  ? -33.918 -3.938  80.006  1.00 84.84  ?  73   VAL B C   1 
ATOM   5310  O O   . VAL B  2  73  ? -33.370 -4.524  80.947  1.00 84.10  ?  73   VAL B O   1 
ATOM   5311  C CB  . VAL B  2  73  ? -35.624 -2.797  81.486  1.00 84.73  ?  73   VAL B CB  1 
ATOM   5312  C CG1 . VAL B  2  73  ? -34.733 -1.573  81.665  1.00 82.61  ?  73   VAL B CG1 1 
ATOM   5313  C CG2 . VAL B  2  73  ? -37.085 -2.404  81.615  1.00 87.01  ?  73   VAL B CG2 1 
ATOM   5314  N N   . ASP B  2  74  ? -33.301 -3.713  78.842  1.00 86.84  ?  74   ASP B N   1 
ATOM   5315  C CA  . ASP B  2  74  ? -31.946 -4.198  78.560  1.00 86.81  ?  74   ASP B CA  1 
ATOM   5316  C C   . ASP B  2  74  ? -30.960 -3.065  78.801  1.00 85.31  ?  74   ASP B C   1 
ATOM   5317  O O   . ASP B  2  74  ? -30.553 -2.347  77.887  1.00 85.78  ?  74   ASP B O   1 
ATOM   5318  C CB  . ASP B  2  74  ? -31.826 -4.707  77.133  1.00 88.86  ?  74   ASP B CB  1 
ATOM   5319  C CG  . ASP B  2  74  ? -32.777 -5.816  76.838  1.00 91.28  ?  74   ASP B CG  1 
ATOM   5320  O OD1 . ASP B  2  74  ? -32.510 -6.961  77.266  1.00 92.31  ?  74   ASP B OD1 1 
ATOM   5321  O OD2 . ASP B  2  74  ? -33.802 -5.532  76.184  1.00 92.59  -1 74   ASP B OD2 1 
ATOM   5322  N N   . LEU B  2  75  ? -30.577 -2.906  80.058  1.00 90.80  ?  75   LEU B N   1 
ATOM   5323  C CA  . LEU B  2  75  ? -29.667 -1.843  80.453  1.00 90.10  ?  75   LEU B CA  1 
ATOM   5324  C C   . LEU B  2  75  ? -28.348 -2.403  80.967  1.00 90.24  ?  75   LEU B C   1 
ATOM   5325  O O   . LEU B  2  75  ? -27.679 -1.770  81.785  1.00 89.93  ?  75   LEU B O   1 
ATOM   5326  C CB  . LEU B  2  75  ? -30.319 -0.948  81.504  1.00 88.80  ?  75   LEU B CB  1 
ATOM   5327  C CG  . LEU B  2  75  ? -31.191 0.188   80.971  1.00 89.11  ?  75   LEU B CG  1 
ATOM   5328  C CD1 . LEU B  2  75  ? -31.833 0.958   82.116  1.00 88.38  ?  75   LEU B CD1 1 
ATOM   5329  C CD2 . LEU B  2  75  ? -30.367 1.105   80.095  1.00 90.21  ?  75   LEU B CD2 1 
ATOM   5330  N N   . GLY B  2  76  ? -27.966 -3.592  80.508  1.00 94.07  ?  76   GLY B N   1 
ATOM   5331  C CA  . GLY B  2  76  ? -26.724 -4.186  80.970  1.00 95.75  ?  76   GLY B CA  1 
ATOM   5332  C C   . GLY B  2  76  ? -25.511 -3.487  80.378  1.00 97.00  ?  76   GLY B C   1 
ATOM   5333  O O   . GLY B  2  76  ? -25.479 -3.140  79.195  1.00 97.37  ?  76   GLY B O   1 
ATOM   5334  N N   . ASN B  2  77  ? -24.499 -3.284  81.225  1.00 99.42  ?  77   ASN B N   1 
ATOM   5335  C CA  . ASN B  2  77  ? -23.223 -2.698  80.814  1.00 101.55 ?  77   ASN B CA  1 
ATOM   5336  C C   . ASN B  2  77  ? -23.418 -1.308  80.207  1.00 102.91 ?  77   ASN B C   1 
ATOM   5337  O O   . ASN B  2  77  ? -22.934 -1.006  79.114  1.00 105.40 ?  77   ASN B O   1 
ATOM   5338  C CB  . ASN B  2  77  ? -22.484 -3.623  79.845  1.00 103.46 ?  77   ASN B CB  1 
ATOM   5339  C CG  . ASN B  2  77  ? -20.996 -3.661  80.103  1.00 105.03 ?  77   ASN B CG  1 
ATOM   5340  O OD1 . ASN B  2  77  ? -20.533 -4.337  81.020  1.00 103.89 ?  77   ASN B OD1 1 
ATOM   5341  N ND2 . ASN B  2  77  ? -20.236 -2.930  79.295  1.00 107.90 ?  77   ASN B ND2 1 
ATOM   5342  N N   . ALA B  2  78  ? -24.141 -0.455  80.932  1.00 101.91 ?  78   ALA B N   1 
ATOM   5343  C CA  . ALA B  2  78  ? -24.474 0.884   80.466  1.00 103.18 ?  78   ALA B CA  1 
ATOM   5344  C C   . ALA B  2  78  ? -23.697 1.983   81.178  1.00 104.74 ?  78   ALA B C   1 
ATOM   5345  O O   . ALA B  2  78  ? -23.941 3.165   80.908  1.00 106.29 ?  78   ALA B O   1 
ATOM   5346  C CB  . ALA B  2  78  ? -25.979 1.136   80.619  1.00 100.94 ?  78   ALA B CB  1 
ATOM   5347  N N   . ASN B  2  79  ? -22.772 1.628   82.075  1.00 104.34 ?  79   ASN B N   1 
ATOM   5348  C CA  . ASN B  2  79  ? -22.004 2.595   82.864  1.00 105.81 ?  79   ASN B CA  1 
ATOM   5349  C C   . ASN B  2  79  ? -22.914 3.544   83.639  1.00 104.47 ?  79   ASN B C   1 
ATOM   5350  O O   . ASN B  2  79  ? -22.564 4.702   83.877  1.00 106.70 ?  79   ASN B O   1 
ATOM   5351  C CB  . ASN B  2  79  ? -21.031 3.393   81.987  1.00 110.41 ?  79   ASN B CB  1 
ATOM   5352  C CG  . ASN B  2  79  ? -19.854 2.560   81.498  1.00 112.08 ?  79   ASN B CG  1 
ATOM   5353  O OD1 . ASN B  2  79  ? -19.473 1.569   82.123  1.00 110.03 ?  79   ASN B OD1 1 
ATOM   5354  N ND2 . ASN B  2  79  ? -19.271 2.965   80.375  1.00 115.95 ?  79   ASN B ND2 1 
ATOM   5355  N N   . LEU B  2  80  ? -24.090 3.058   84.030  1.00 109.02 ?  80   LEU B N   1 
ATOM   5356  C CA  . LEU B  2  80  ? -25.027 3.849   84.814  1.00 107.83 ?  80   LEU B CA  1 
ATOM   5357  C C   . LEU B  2  80  ? -24.588 3.912   86.271  1.00 106.65 ?  80   LEU B C   1 
ATOM   5358  O O   . LEU B  2  80  ? -24.101 2.928   86.834  1.00 104.83 ?  80   LEU B O   1 
ATOM   5359  C CB  . LEU B  2  80  ? -26.434 3.257   84.716  1.00 104.82 ?  80   LEU B CB  1 
ATOM   5360  C CG  . LEU B  2  80  ? -27.092 3.283   83.334  1.00 105.53 ?  80   LEU B CG  1 
ATOM   5361  C CD1 . LEU B  2  80  ? -28.341 2.410   83.297  1.00 102.74 ?  80   LEU B CD1 1 
ATOM   5362  C CD2 . LEU B  2  80  ? -27.422 4.713   82.928  1.00 108.13 ?  80   LEU B CD2 1 
ATOM   5363  N N   . SER B  2  81  ? -24.765 5.079   86.881  1.00 108.11 ?  81   SER B N   1 
ATOM   5364  C CA  . SER B  2  81  ? -24.486 5.263   88.295  1.00 107.28 ?  81   SER B CA  1 
ATOM   5365  C C   . SER B  2  81  ? -25.679 5.943   88.948  1.00 106.87 ?  81   SER B C   1 
ATOM   5366  O O   . SER B  2  81  ? -26.344 6.782   88.336  1.00 108.38 ?  81   SER B O   1 
ATOM   5367  C CB  . SER B  2  81  ? -23.220 6.091   88.514  1.00 110.42 ?  81   SER B CB  1 
ATOM   5368  O OG  . SER B  2  81  ? -22.958 6.240   89.896  1.00 109.98 ?  81   SER B OG  1 
ATOM   5369  N N   . GLY B  2  82  ? -25.948 5.574   90.186  1.00 111.18 ?  82   GLY B N   1 
ATOM   5370  C CA  . GLY B  2  82  ? -27.092 6.107   90.900  1.00 111.96 ?  82   GLY B CA  1 
ATOM   5371  C C   . GLY B  2  82  ? -27.683 5.045   91.812  1.00 110.99 ?  82   GLY B C   1 
ATOM   5372  O O   . GLY B  2  82  ? -26.988 4.121   92.230  1.00 109.42 ?  82   GLY B O   1 
ATOM   5373  N N   . GLN B  2  83  ? -28.974 5.203   92.111  1.00 108.46 ?  83   GLN B N   1 
ATOM   5374  C CA  . GLN B  2  83  ? -29.689 4.299   93.001  1.00 109.04 ?  83   GLN B CA  1 
ATOM   5375  C C   . GLN B  2  83  ? -30.977 3.823   92.348  1.00 109.97 ?  83   GLN B C   1 
ATOM   5376  O O   . GLN B  2  83  ? -31.617 4.558   91.592  1.00 111.67 ?  83   GLN B O   1 
ATOM   5377  C CB  . GLN B  2  83  ? -30.027 4.961   94.342  1.00 112.57 ?  83   GLN B CB  1 
ATOM   5378  C CG  . GLN B  2  83  ? -29.021 5.986   94.817  1.00 112.68 ?  83   GLN B CG  1 
ATOM   5379  C CD  . GLN B  2  83  ? -29.009 6.120   96.325  1.00 115.06 ?  83   GLN B CD  1 
ATOM   5380  O OE1 . GLN B  2  83  ? -30.014 5.867   96.992  1.00 117.95 ?  83   GLN B OE1 1 
ATOM   5381  N NE2 . GLN B  2  83  ? -27.864 6.508   96.874  1.00 114.33 ?  83   GLN B NE2 1 
ATOM   5382  N N   . LEU B  2  84  ? -31.357 2.587   92.662  1.00 105.41 ?  84   LEU B N   1 
ATOM   5383  C CA  . LEU B  2  84  ? -32.617 2.049   92.176  1.00 106.53 ?  84   LEU B CA  1 
ATOM   5384  C C   . LEU B  2  84  ? -33.790 2.830   92.767  1.00 111.81 ?  84   LEU B C   1 
ATOM   5385  O O   . LEU B  2  84  ? -33.647 3.624   93.700  1.00 114.60 ?  84   LEU B O   1 
ATOM   5386  C CB  . LEU B  2  84  ? -32.740 0.564   92.518  1.00 104.38 ?  84   LEU B CB  1 
ATOM   5387  C CG  . LEU B  2  84  ? -32.478 -0.448  91.399  1.00 101.18 ?  84   LEU B CG  1 
ATOM   5388  C CD1 . LEU B  2  84  ? -31.103 -0.248  90.789  1.00 98.66  ?  84   LEU B CD1 1 
ATOM   5389  C CD2 . LEU B  2  84  ? -32.639 -1.871  91.916  1.00 102.00 ?  84   LEU B CD2 1 
ATOM   5390  N N   . VAL B  2  85  ? -34.964 2.601   92.192  1.00 98.41  ?  85   VAL B N   1 
ATOM   5391  C CA  . VAL B  2  85  ? -36.160 3.378   92.482  1.00 103.71 ?  85   VAL B CA  1 
ATOM   5392  C C   . VAL B  2  85  ? -37.326 2.424   92.703  1.00 104.26 ?  85   VAL B C   1 
ATOM   5393  O O   . VAL B  2  85  ? -37.488 1.457   91.953  1.00 101.53 ?  85   VAL B O   1 
ATOM   5394  C CB  . VAL B  2  85  ? -36.413 4.366   91.324  1.00 105.72 ?  85   VAL B CB  1 
ATOM   5395  C CG1 . VAL B  2  85  ? -37.844 4.701   91.176  1.00 110.82 ?  85   VAL B CG1 1 
ATOM   5396  C CG2 . VAL B  2  85  ? -35.640 5.624   91.571  1.00 106.94 ?  85   VAL B CG2 1 
ATOM   5397  N N   . MET B  2  86  ? -38.140 2.688   93.736  1.00 110.39 ?  86   MET B N   1 
ATOM   5398  C CA  . MET B  2  86  ? -39.196 1.733   94.079  1.00 110.33 ?  86   MET B CA  1 
ATOM   5399  C C   . MET B  2  86  ? -40.220 1.577   92.962  1.00 111.37 ?  86   MET B C   1 
ATOM   5400  O O   . MET B  2  86  ? -40.898 0.545   92.901  1.00 110.37 ?  86   MET B O   1 
ATOM   5401  C CB  . MET B  2  86  ? -39.884 2.095   95.416  1.00 113.60 ?  86   MET B CB  1 
ATOM   5402  C CG  . MET B  2  86  ? -40.783 3.358   95.536  1.00 118.57 ?  86   MET B CG  1 
ATOM   5403  S SD  . MET B  2  86  ? -42.301 3.632   94.560  1.00 121.39 ?  86   MET B SD  1 
ATOM   5404  C CE  . MET B  2  86  ? -43.128 2.045   94.553  1.00 119.41 ?  86   MET B CE  1 
ATOM   5405  N N   . GLN B  2  87  ? -40.336 2.566   92.072  1.00 104.50 ?  87   GLN B N   1 
ATOM   5406  C CA  . GLN B  2  87  ? -41.322 2.554   90.995  1.00 105.93 ?  87   GLN B CA  1 
ATOM   5407  C C   . GLN B  2  87  ? -41.065 1.433   89.990  1.00 101.73 ?  87   GLN B C   1 
ATOM   5408  O O   . GLN B  2  87  ? -41.828 1.263   89.033  1.00 102.52 ?  87   GLN B O   1 
ATOM   5409  C CB  . GLN B  2  87  ? -41.358 3.912   90.280  1.00 109.54 ?  87   GLN B CB  1 
ATOM   5410  C CG  . GLN B  2  87  ? -41.816 5.128   91.122  1.00 114.17 ?  87   GLN B CG  1 
ATOM   5411  C CD  . GLN B  2  87  ? -40.833 5.570   92.204  1.00 114.38 ?  87   GLN B CD  1 
ATOM   5412  O OE1 . GLN B  2  87  ? -40.168 4.755   92.838  1.00 111.11 ?  87   GLN B OE1 1 
ATOM   5413  N NE2 . GLN B  2  87  ? -40.745 6.881   92.416  1.00 117.99 ?  87   GLN B NE2 1 
ATOM   5414  N N   . LEU B  2  88  ? -39.991 0.668   90.180  1.00 108.62 ?  88   LEU B N   1 
ATOM   5415  C CA  . LEU B  2  88  ? -39.745 -0.471  89.306  1.00 104.89 ?  88   LEU B CA  1 
ATOM   5416  C C   . LEU B  2  88  ? -40.813 -1.551  89.433  1.00 105.78 ?  88   LEU B C   1 
ATOM   5417  O O   . LEU B  2  88  ? -40.914 -2.406  88.545  1.00 104.29 ?  88   LEU B O   1 
ATOM   5418  C CB  . LEU B  2  88  ? -38.376 -1.078  89.603  1.00 100.57 ?  88   LEU B CB  1 
ATOM   5419  C CG  . LEU B  2  88  ? -37.181 -0.215  89.224  1.00 98.81  ?  88   LEU B CG  1 
ATOM   5420  C CD1 . LEU B  2  88  ? -35.898 -0.790  89.798  1.00 95.30  ?  88   LEU B CD1 1 
ATOM   5421  C CD2 . LEU B  2  88  ? -37.114 -0.135  87.725  1.00 97.36  ?  88   LEU B CD2 1 
ATOM   5422  N N   . GLY B  2  89  ? -41.601 -1.542  90.514  1.00 106.06 ?  89   GLY B N   1 
ATOM   5423  C CA  . GLY B  2  89  ? -42.693 -2.480  90.686  1.00 107.48 ?  89   GLY B CA  1 
ATOM   5424  C C   . GLY B  2  89  ? -43.952 -2.169  89.912  1.00 110.73 ?  89   GLY B C   1 
ATOM   5425  O O   . GLY B  2  89  ? -44.939 -2.901  90.026  1.00 112.37 ?  89   GLY B O   1 
ATOM   5426  N N   . GLN B  2  90  ? -43.946 -1.104  89.117  1.00 99.99  ?  90   GLN B N   1 
ATOM   5427  C CA  . GLN B  2  90  ? -45.103 -0.692  88.334  1.00 103.26 ?  90   GLN B CA  1 
ATOM   5428  C C   . GLN B  2  90  ? -45.119 -1.294  86.930  1.00 102.08 ?  90   GLN B C   1 
ATOM   5429  O O   . GLN B  2  90  ? -45.886 -0.829  86.080  1.00 104.60 ?  90   GLN B O   1 
ATOM   5430  C CB  . GLN B  2  90  ? -45.153 0.833   88.242  1.00 106.02 ?  90   GLN B CB  1 
ATOM   5431  C CG  . GLN B  2  90  ? -44.881 1.541   89.556  1.00 107.26 ?  90   GLN B CG  1 
ATOM   5432  C CD  . GLN B  2  90  ? -46.145 1.873   90.304  1.00 110.76 ?  90   GLN B CD  1 
ATOM   5433  O OE1 . GLN B  2  90  ? -46.755 2.914   90.071  1.00 113.60 ?  90   GLN B OE1 1 
ATOM   5434  N NE2 . GLN B  2  90  ? -46.544 0.994   91.216  1.00 110.54 ?  90   GLN B NE2 1 
ATOM   5435  N N   . LEU B  2  91  ? -44.280 -2.294  86.660  1.00 102.12 ?  91   LEU B N   1 
ATOM   5436  C CA  . LEU B  2  91  ? -44.289 -2.962  85.365  1.00 101.40 ?  91   LEU B CA  1 
ATOM   5437  C C   . LEU B  2  91  ? -44.808 -4.384  85.534  1.00 101.89 ?  91   LEU B C   1 
ATOM   5438  O O   . LEU B  2  91  ? -44.009 -5.324  85.634  1.00 99.20  ?  91   LEU B O   1 
ATOM   5439  C CB  . LEU B  2  91  ? -42.889 -2.982  84.753  1.00 97.35  ?  91   LEU B CB  1 
ATOM   5440  C CG  . LEU B  2  91  ? -42.209 -1.667  84.370  1.00 96.55  ?  91   LEU B CG  1 
ATOM   5441  C CD1 . LEU B  2  91  ? -43.225 -0.634  83.916  1.00 100.74 ?  91   LEU B CD1 1 
ATOM   5442  C CD2 . LEU B  2  91  ? -41.375 -1.141  85.528  1.00 95.14  ?  91   LEU B CD2 1 
ATOM   5443  N N   . PRO B  2  92  ? -46.130 -4.583  85.566  1.00 102.36 ?  92   PRO B N   1 
ATOM   5444  C CA  . PRO B  2  92  ? -46.662 -5.926  85.863  1.00 103.39 ?  92   PRO B CA  1 
ATOM   5445  C C   . PRO B  2  92  ? -46.191 -7.007  84.900  1.00 102.38 ?  92   PRO B C   1 
ATOM   5446  O O   . PRO B  2  92  ? -46.034 -8.164  85.312  1.00 101.93 ?  92   PRO B O   1 
ATOM   5447  C CB  . PRO B  2  92  ? -48.182 -5.720  85.791  1.00 107.64 ?  92   PRO B CB  1 
ATOM   5448  C CG  . PRO B  2  92  ? -48.360 -4.532  84.902  1.00 108.77 ?  92   PRO B CG  1 
ATOM   5449  C CD  . PRO B  2  92  ? -47.190 -3.635  85.181  1.00 105.90 ?  92   PRO B CD  1 
ATOM   5450  N N   . ASN B  2  93  ? -45.942 -6.665  83.637  1.00 101.09 ?  93   ASN B N   1 
ATOM   5451  C CA  . ASN B  2  93  ? -45.577 -7.641  82.619  1.00 100.99 ?  93   ASN B CA  1 
ATOM   5452  C C   . ASN B  2  93  ? -44.076 -7.706  82.367  1.00 96.76  ?  93   ASN B C   1 
ATOM   5453  O O   . ASN B  2  93  ? -43.645 -8.392  81.436  1.00 96.62  ?  93   ASN B O   1 
ATOM   5454  C CB  . ASN B  2  93  ? -46.309 -7.330  81.313  1.00 104.40 ?  93   ASN B CB  1 
ATOM   5455  C CG  . ASN B  2  93  ? -47.801 -7.561  81.417  1.00 108.83 ?  93   ASN B CG  1 
ATOM   5456  O OD1 . ASN B  2  93  ? -48.257 -8.693  81.593  1.00 110.46 ?  93   ASN B OD1 1 
ATOM   5457  N ND2 . ASN B  2  93  ? -48.572 -6.485  81.317  1.00 110.77 ?  93   ASN B ND2 1 
ATOM   5458  N N   . LEU B  2  94  ? -43.274 -7.036  83.188  1.00 104.34 ?  94   LEU B N   1 
ATOM   5459  C CA  . LEU B  2  94  ? -41.831 -6.973  82.982  1.00 100.34 ?  94   LEU B CA  1 
ATOM   5460  C C   . LEU B  2  94  ? -41.203 -8.333  83.277  1.00 99.16  ?  94   LEU B C   1 
ATOM   5461  O O   . LEU B  2  94  ? -41.059 -8.729  84.438  1.00 99.40  ?  94   LEU B O   1 
ATOM   5462  C CB  . LEU B  2  94  ? -41.241 -5.877  83.861  1.00 98.04  ?  94   LEU B CB  1 
ATOM   5463  C CG  . LEU B  2  94  ? -39.746 -5.796  84.129  1.00 94.17  ?  94   LEU B CG  1 
ATOM   5464  C CD1 . LEU B  2  94  ? -39.007 -5.250  82.924  1.00 92.36  ?  94   LEU B CD1 1 
ATOM   5465  C CD2 . LEU B  2  94  ? -39.558 -4.892  85.315  1.00 93.52  ?  94   LEU B CD2 1 
ATOM   5466  N N   . GLN B  2  95  ? -40.820 -9.044  82.218  1.00 102.07 ?  95   GLN B N   1 
ATOM   5467  C CA  . GLN B  2  95  ? -40.286 -10.394 82.334  1.00 101.91 ?  95   GLN B CA  1 
ATOM   5468  C C   . GLN B  2  95  ? -38.776 -10.423 82.529  1.00 98.44  ?  95   GLN B C   1 
ATOM   5469  O O   . GLN B  2  95  ? -38.268 -11.299 83.237  1.00 97.78  ?  95   GLN B O   1 
ATOM   5470  C CB  . GLN B  2  95  ? -40.653 -11.204 81.087  1.00 104.82 ?  95   GLN B CB  1 
ATOM   5471  C CG  . GLN B  2  95  ? -42.145 -11.232 80.799  1.00 108.75 ?  95   GLN B CG  1 
ATOM   5472  C CD  . GLN B  2  95  ? -42.485 -11.839 79.455  1.00 111.71 ?  95   GLN B CD  1 
ATOM   5473  O OE1 . GLN B  2  95  ? -41.650 -12.485 78.821  1.00 111.12 ?  95   GLN B OE1 1 
ATOM   5474  N NE2 . GLN B  2  95  ? -43.726 -11.652 79.021  1.00 115.21 ?  95   GLN B NE2 1 
ATOM   5475  N N   . TYR B  2  96  ? -38.043 -9.494  81.918  1.00 95.71  ?  96   TYR B N   1 
ATOM   5476  C CA  . TYR B  2  96  ? -36.586 -9.485  81.979  1.00 96.33  ?  96   TYR B CA  1 
ATOM   5477  C C   . TYR B  2  96  ? -36.115 -8.105  82.407  1.00 95.11  ?  96   TYR B C   1 
ATOM   5478  O O   . TYR B  2  96  ? -36.415 -7.108  81.741  1.00 93.00  ?  96   TYR B O   1 
ATOM   5479  C CB  . TYR B  2  96  ? -35.972 -9.876  80.629  1.00 95.91  ?  96   TYR B CB  1 
ATOM   5480  C CG  . TYR B  2  96  ? -36.329 -11.280 80.190  1.00 97.61  ?  96   TYR B CG  1 
ATOM   5481  C CD1 . TYR B  2  96  ? -37.536 -11.545 79.557  1.00 96.91  ?  96   TYR B CD1 1 
ATOM   5482  C CD2 . TYR B  2  96  ? -35.462 -12.341 80.412  1.00 100.47 ?  96   TYR B CD2 1 
ATOM   5483  C CE1 . TYR B  2  96  ? -37.870 -12.824 79.160  1.00 98.89  ?  96   TYR B CE1 1 
ATOM   5484  C CE2 . TYR B  2  96  ? -35.786 -13.624 80.018  1.00 102.50 ?  96   TYR B CE2 1 
ATOM   5485  C CZ  . TYR B  2  96  ? -36.991 -13.860 79.392  1.00 101.64 ?  96   TYR B CZ  1 
ATOM   5486  O OH  . TYR B  2  96  ? -37.319 -15.136 78.997  1.00 104.07 ?  96   TYR B OH  1 
ATOM   5487  N N   . LEU B  2  97  ? -35.382 -8.051  83.513  1.00 98.87  ?  97   LEU B N   1 
ATOM   5488  C CA  . LEU B  2  97  ? -34.866 -6.805  84.068  1.00 100.72 ?  97   LEU B CA  1 
ATOM   5489  C C   . LEU B  2  97  ? -33.342 -6.921  84.120  1.00 101.56 ?  97   LEU B C   1 
ATOM   5490  O O   . LEU B  2  97  ? -32.795 -7.585  85.005  1.00 101.49 ?  97   LEU B O   1 
ATOM   5491  C CB  . LEU B  2  97  ? -35.479 -6.547  85.444  1.00 101.08 ?  97   LEU B CB  1 
ATOM   5492  C CG  . LEU B  2  97  ? -35.534 -5.111  85.949  1.00 103.13 ?  97   LEU B CG  1 
ATOM   5493  C CD1 . LEU B  2  97  ? -36.616 -4.888  86.971  1.00 103.74 ?  97   LEU B CD1 1 
ATOM   5494  C CD2 . LEU B  2  97  ? -34.219 -4.908  86.594  1.00 104.34 ?  97   LEU B CD2 1 
ATOM   5495  N N   . GLU B  2  98  ? -32.657 -6.274  83.174  1.00 101.66 ?  98   GLU B N   1 
ATOM   5496  C CA  . GLU B  2  98  ? -31.205 -6.382  83.022  1.00 102.35 ?  98   GLU B CA  1 
ATOM   5497  C C   . GLU B  2  98  ? -30.553 -5.068  83.450  1.00 103.65 ?  98   GLU B C   1 
ATOM   5498  O O   . GLU B  2  98  ? -30.427 -4.140  82.646  1.00 104.65 ?  98   GLU B O   1 
ATOM   5499  C CB  . GLU B  2  98  ? -30.844 -6.725  81.579  1.00 102.85 ?  98   GLU B CB  1 
ATOM   5500  C CG  . GLU B  2  98  ? -31.705 -7.807  80.958  1.00 101.88 ?  98   GLU B CG  1 
ATOM   5501  C CD  . GLU B  2  98  ? -31.642 -9.105  81.730  1.00 100.62 ?  98   GLU B CD  1 
ATOM   5502  O OE1 . GLU B  2  98  ? -30.533 -9.489  82.164  1.00 102.99 ?  98   GLU B OE1 1 
ATOM   5503  O OE2 . GLU B  2  98  ? -32.702 -9.743  81.899  1.00 99.48  -1 98   GLU B OE2 1 
ATOM   5504  N N   . LEU B  2  99  ? -30.124 -4.994  84.712  1.00 104.70 ?  99   LEU B N   1 
ATOM   5505  C CA  . LEU B  2  99  ? -29.378 -3.844  85.215  1.00 106.36 ?  99   LEU B CA  1 
ATOM   5506  C C   . LEU B  2  99  ? -27.935 -4.196  85.574  1.00 107.90 ?  99   LEU B C   1 
ATOM   5507  O O   . LEU B  2  99  ? -27.282 -3.440  86.301  1.00 109.82 ?  99   LEU B O   1 
ATOM   5508  C CB  . LEU B  2  99  ? -30.069 -3.214  86.427  1.00 106.97 ?  99   LEU B CB  1 
ATOM   5509  C CG  . LEU B  2  99  ? -31.153 -2.157  86.200  1.00 107.42 ?  99   LEU B CG  1 
ATOM   5510  C CD1 . LEU B  2  99  ? -32.187 -2.225  87.293  1.00 108.21 ?  99   LEU B CD1 1 
ATOM   5511  C CD2 . LEU B  2  99  ? -30.560 -0.785  86.156  1.00 109.14 ?  99   LEU B CD2 1 
ATOM   5512  N N   . TYR B  2  100 ? -27.424 -5.321  85.080  1.00 108.13 ?  100  TYR B N   1 
ATOM   5513  C CA  . TYR B  2  100 ? -26.126 -5.823  85.506  1.00 112.76 ?  100  TYR B CA  1 
ATOM   5514  C C   . TYR B  2  100 ? -24.982 -4.973  84.949  1.00 114.58 ?  100  TYR B C   1 
ATOM   5515  O O   . TYR B  2  100 ? -25.145 -4.206  83.995  1.00 112.30 ?  100  TYR B O   1 
ATOM   5516  C CB  . TYR B  2  100 ? -25.956 -7.285  85.081  1.00 114.44 ?  100  TYR B CB  1 
ATOM   5517  C CG  . TYR B  2  100 ? -25.980 -7.529  83.581  1.00 112.77 ?  100  TYR B CG  1 
ATOM   5518  C CD1 . TYR B  2  100 ? -24.827 -7.403  82.815  1.00 115.25 ?  100  TYR B CD1 1 
ATOM   5519  C CD2 . TYR B  2  100 ? -27.155 -7.901  82.936  1.00 109.24 ?  100  TYR B CD2 1 
ATOM   5520  C CE1 . TYR B  2  100 ? -24.844 -7.627  81.448  1.00 114.11 ?  100  TYR B CE1 1 
ATOM   5521  C CE2 . TYR B  2  100 ? -27.181 -8.129  81.569  1.00 108.04 ?  100  TYR B CE2 1 
ATOM   5522  C CZ  . TYR B  2  100 ? -26.022 -7.991  80.832  1.00 110.42 ?  100  TYR B CZ  1 
ATOM   5523  O OH  . TYR B  2  100 ? -26.039 -8.212  79.474  1.00 111.81 ?  100  TYR B OH  1 
ATOM   5524  N N   . SER B  2  101 ? -23.810 -5.120  85.577  1.00 119.36 ?  101  SER B N   1 
ATOM   5525  C CA  . SER B  2  101 ? -22.557 -4.499  85.131  1.00 122.61 ?  101  SER B CA  1 
ATOM   5526  C C   . SER B  2  101 ? -22.665 -2.971  85.056  1.00 121.01 ?  101  SER B C   1 
ATOM   5527  O O   . SER B  2  101 ? -22.539 -2.356  83.994  1.00 119.97 ?  101  SER B O   1 
ATOM   5528  C CB  . SER B  2  101 ? -22.107 -5.088  83.788  1.00 123.23 ?  101  SER B CB  1 
ATOM   5529  O OG  . SER B  2  101 ? -21.118 -4.277  83.172  1.00 125.74 ?  101  SER B OG  1 
ATOM   5530  N N   . ASN B  2  102 ? -22.904 -2.364  86.215  1.00 121.26 ?  102  ASN B N   1 
ATOM   5531  C CA  . ASN B  2  102 ? -22.959 -0.912  86.334  1.00 120.63 ?  102  ASN B CA  1 
ATOM   5532  C C   . ASN B  2  102 ? -22.369 -0.517  87.686  1.00 124.48 ?  102  ASN B C   1 
ATOM   5533  O O   . ASN B  2  102 ? -21.852 -1.355  88.433  1.00 127.82 ?  102  ASN B O   1 
ATOM   5534  C CB  . ASN B  2  102 ? -24.396 -0.402  86.154  1.00 115.42 ?  102  ASN B CB  1 
ATOM   5535  C CG  . ASN B  2  102 ? -24.866 -0.466  84.709  1.00 112.27 ?  102  ASN B CG  1 
ATOM   5536  O OD1 . ASN B  2  102 ? -24.377 0.269   83.849  1.00 112.93 ?  102  ASN B OD1 1 
ATOM   5537  N ND2 . ASN B  2  102 ? -25.828 -1.342  84.438  1.00 109.25 ?  102  ASN B ND2 1 
ATOM   5538  N N   . ASN B  2  103 ? -22.445 0.775   87.998  1.00 124.44 ?  103  ASN B N   1 
ATOM   5539  C CA  . ASN B  2  103 ? -21.960 1.334   89.256  1.00 128.09 ?  103  ASN B CA  1 
ATOM   5540  C C   . ASN B  2  103 ? -23.123 1.877   90.082  1.00 125.24 ?  103  ASN B C   1 
ATOM   5541  O O   . ASN B  2  103 ? -23.030 2.928   90.718  1.00 126.78 ?  103  ASN B O   1 
ATOM   5542  C CB  . ASN B  2  103 ? -20.916 2.421   89.004  1.00 131.84 ?  103  ASN B CB  1 
ATOM   5543  C CG  . ASN B  2  103 ? -20.166 2.820   90.266  1.00 136.92 ?  103  ASN B CG  1 
ATOM   5544  O OD1 . ASN B  2  103 ? -19.711 1.968   91.029  1.00 140.01 ?  103  ASN B OD1 1 
ATOM   5545  N ND2 . ASN B  2  103 ? -20.038 4.124   90.490  1.00 138.22 ?  103  ASN B ND2 1 
ATOM   5546  N N   . ILE B  2  104 ? -24.236 1.158   90.067  1.00 121.53 ?  104  ILE B N   1 
ATOM   5547  C CA  . ILE B  2  104 ? -25.426 1.568   90.799  1.00 119.10 ?  104  ILE B CA  1 
ATOM   5548  C C   . ILE B  2  104 ? -25.249 1.223   92.271  1.00 122.39 ?  104  ILE B C   1 
ATOM   5549  O O   . ILE B  2  104 ? -24.696 0.172   92.617  1.00 125.00 ?  104  ILE B O   1 
ATOM   5550  C CB  . ILE B  2  104 ? -26.674 0.894   90.202  1.00 115.45 ?  104  ILE B CB  1 
ATOM   5551  C CG1 . ILE B  2  104 ? -26.698 1.094   88.685  1.00 114.70 ?  104  ILE B CG1 1 
ATOM   5552  C CG2 . ILE B  2  104 ? -27.937 1.444   90.834  1.00 115.60 ?  104  ILE B CG2 1 
ATOM   5553  C CD1 . ILE B  2  104 ? -27.651 0.178   87.966  1.00 112.57 ?  104  ILE B CD1 1 
ATOM   5554  N N   . THR B  2  105 ? -25.707 2.117   93.143  1.00 122.70 ?  105  THR B N   1 
ATOM   5555  C CA  . THR B  2  105 ? -25.560 1.982   94.588  1.00 126.22 ?  105  THR B CA  1 
ATOM   5556  C C   . THR B  2  105 ? -26.942 1.972   95.248  1.00 123.93 ?  105  THR B C   1 
ATOM   5557  O O   . THR B  2  105 ? -27.979 1.964   94.578  1.00 120.34 ?  105  THR B O   1 
ATOM   5558  C CB  . THR B  2  105 ? -24.682 3.102   95.161  1.00 130.15 ?  105  THR B CB  1 
ATOM   5559  O OG1 . THR B  2  105 ? -25.495 4.235   95.490  1.00 128.68 ?  105  THR B OG1 1 
ATOM   5560  C CG2 . THR B  2  105 ? -23.610 3.525   94.160  1.00 131.47 ?  105  THR B CG2 1 
ATOM   5561  N N   . GLY B  2  106 ? -26.943 1.969   96.575  1.00 128.03 ?  106  GLY B N   1 
ATOM   5562  C CA  . GLY B  2  106 ? -28.175 1.946   97.337  1.00 126.97 ?  106  GLY B CA  1 
ATOM   5563  C C   . GLY B  2  106 ? -28.652 0.534   97.621  1.00 127.06 ?  106  GLY B C   1 
ATOM   5564  O O   . GLY B  2  106 ? -27.895 -0.440  97.570  1.00 129.15 ?  106  GLY B O   1 
ATOM   5565  N N   . THR B  2  107 ? -29.942 0.430   97.925  1.00 131.50 ?  107  THR B N   1 
ATOM   5566  C CA  . THR B  2  107 ? -30.552 -0.838  98.295  1.00 131.00 ?  107  THR B CA  1 
ATOM   5567  C C   . THR B  2  107 ? -31.525 -1.314  97.224  1.00 129.86 ?  107  THR B C   1 
ATOM   5568  O O   . THR B  2  107 ? -31.827 -0.618  96.249  1.00 130.14 ?  107  THR B O   1 
ATOM   5569  C CB  . THR B  2  107 ? -31.280 -0.733  99.641  1.00 133.85 ?  107  THR B CB  1 
ATOM   5570  O OG1 . THR B  2  107 ? -31.747 -2.031  100.033 1.00 133.83 ?  107  THR B OG1 1 
ATOM   5571  C CG2 . THR B  2  107 ? -32.469 0.206   99.527  1.00 136.71 ?  107  THR B CG2 1 
ATOM   5572  N N   . ILE B  2  108 ? -32.002 -2.534  97.434  1.00 130.66 ?  108  ILE B N   1 
ATOM   5573  C CA  . ILE B  2  108 ? -33.004 -3.153  96.573  1.00 130.04 ?  108  ILE B CA  1 
ATOM   5574  C C   . ILE B  2  108 ? -34.380 -2.829  97.154  1.00 133.87 ?  108  ILE B C   1 
ATOM   5575  O O   . ILE B  2  108 ? -34.671 -3.245  98.287  1.00 135.69 ?  108  ILE B O   1 
ATOM   5576  C CB  . ILE B  2  108 ? -32.770 -4.666  96.495  1.00 127.83 ?  108  ILE B CB  1 
ATOM   5577  C CG1 . ILE B  2  108 ? -31.404 -4.963  95.864  1.00 125.56 ?  108  ILE B CG1 1 
ATOM   5578  C CG2 . ILE B  2  108 ? -33.851 -5.352  95.734  1.00 126.97 ?  108  ILE B CG2 1 
ATOM   5579  C CD1 . ILE B  2  108 ? -31.038 -6.439  95.841  1.00 128.22 ?  108  ILE B CD1 1 
ATOM   5580  N N   . PRO B  2  109 ? -35.232 -2.080  96.446  1.00 130.13 ?  109  PRO B N   1 
ATOM   5581  C CA  . PRO B  2  109 ? -36.542 -1.712  97.013  1.00 133.78 ?  109  PRO B CA  1 
ATOM   5582  C C   . PRO B  2  109 ? -37.515 -2.883  96.965  1.00 131.76 ?  109  PRO B C   1 
ATOM   5583  O O   . PRO B  2  109 ? -37.789 -3.427  95.895  1.00 127.84 ?  109  PRO B O   1 
ATOM   5584  C CB  . PRO B  2  109 ? -37.013 -0.563  96.114  1.00 133.98 ?  109  PRO B CB  1 
ATOM   5585  C CG  . PRO B  2  109 ? -36.294 -0.777  94.814  1.00 130.35 ?  109  PRO B CG  1 
ATOM   5586  C CD  . PRO B  2  109 ? -34.985 -1.450  95.136  1.00 128.45 ?  109  PRO B CD  1 
ATOM   5587  N N   . GLU B  2  110 ? -38.125 -3.202  98.108  1.00 137.11 ?  110  GLU B N   1 
ATOM   5588  C CA  . GLU B  2  110 ? -38.940 -4.411  98.172  1.00 135.08 ?  110  GLU B CA  1 
ATOM   5589  C C   . GLU B  2  110 ? -40.135 -4.370  97.227  1.00 131.32 ?  110  GLU B C   1 
ATOM   5590  O O   . GLU B  2  110 ? -40.775 -5.408  97.023  1.00 129.29 ?  110  GLU B O   1 
ATOM   5591  C CB  . GLU B  2  110 ? -39.420 -4.650  99.603  1.00 138.91 ?  110  GLU B CB  1 
ATOM   5592  C CG  . GLU B  2  110 ? -40.490 -3.695  100.068 1.00 140.23 ?  110  GLU B CG  1 
ATOM   5593  C CD  . GLU B  2  110 ? -40.793 -3.877  101.531 1.00 144.27 ?  110  GLU B CD  1 
ATOM   5594  O OE1 . GLU B  2  110 ? -40.929 -5.040  101.962 1.00 145.39 ?  110  GLU B OE1 1 
ATOM   5595  O OE2 . GLU B  2  110 ? -40.883 -2.862  102.251 1.00 146.78 -1 110  GLU B OE2 1 
ATOM   5596  N N   . GLN B  2  111 ? -40.435 -3.213  96.630  1.00 132.96 ?  111  GLN B N   1 
ATOM   5597  C CA  . GLN B  2  111 ? -41.527 -3.114  95.672  1.00 129.12 ?  111  GLN B CA  1 
ATOM   5598  C C   . GLN B  2  111 ? -41.266 -3.878  94.380  1.00 125.36 ?  111  GLN B C   1 
ATOM   5599  O O   . GLN B  2  111 ? -42.180 -3.973  93.555  1.00 122.42 ?  111  GLN B O   1 
ATOM   5600  C CB  . GLN B  2  111 ? -41.813 -1.644  95.355  1.00 129.14 ?  111  GLN B CB  1 
ATOM   5601  C CG  . GLN B  2  111 ? -42.315 -0.864  96.549  1.00 132.05 ?  111  GLN B CG  1 
ATOM   5602  C CD  . GLN B  2  111 ? -43.311 -1.658  97.370  1.00 132.62 ?  111  GLN B CD  1 
ATOM   5603  O OE1 . GLN B  2  111 ? -43.003 -2.107  98.475  1.00 135.78 ?  111  GLN B OE1 1 
ATOM   5604  N NE2 . GLN B  2  111 ? -44.511 -1.842  96.832  1.00 130.65 ?  111  GLN B NE2 1 
ATOM   5605  N N   . LEU B  2  112 ? -40.054 -4.410  94.170  1.00 127.72 ?  112  LEU B N   1 
ATOM   5606  C CA  . LEU B  2  112 ? -39.836 -5.273  93.011  1.00 124.04 ?  112  LEU B CA  1 
ATOM   5607  C C   . LEU B  2  112 ? -40.596 -6.587  93.121  1.00 122.36 ?  112  LEU B C   1 
ATOM   5608  O O   . LEU B  2  112 ? -40.743 -7.285  92.112  1.00 119.36 ?  112  LEU B O   1 
ATOM   5609  C CB  . LEU B  2  112 ? -38.350 -5.559  92.772  1.00 124.33 ?  112  LEU B CB  1 
ATOM   5610  C CG  . LEU B  2  112 ? -37.348 -4.410  92.652  1.00 126.43 ?  112  LEU B CG  1 
ATOM   5611  C CD1 . LEU B  2  112 ? -36.294 -4.573  93.681  1.00 128.71 ?  112  LEU B CD1 1 
ATOM   5612  C CD2 . LEU B  2  112 ? -36.716 -4.361  91.278  1.00 124.43 ?  112  LEU B CD2 1 
ATOM   5613  N N   . GLY B  2  113 ? -41.065 -6.947  94.316  1.00 125.32 ?  113  GLY B N   1 
ATOM   5614  C CA  . GLY B  2  113 ? -41.939 -8.097  94.468  1.00 125.68 ?  113  GLY B CA  1 
ATOM   5615  C C   . GLY B  2  113 ? -43.306 -7.936  93.831  1.00 124.75 ?  113  GLY B C   1 
ATOM   5616  O O   . GLY B  2  113 ? -44.055 -8.916  93.758  1.00 126.04 ?  113  GLY B O   1 
ATOM   5617  N N   . ASN B  2  114 ? -43.645 -6.730  93.373  1.00 124.27 ?  114  ASN B N   1 
ATOM   5618  C CA  . ASN B  2  114 ? -44.895 -6.473  92.669  1.00 123.57 ?  114  ASN B CA  1 
ATOM   5619  C C   . ASN B  2  114 ? -44.837 -6.860  91.194  1.00 119.99 ?  114  ASN B C   1 
ATOM   5620  O O   . ASN B  2  114 ? -45.845 -6.711  90.494  1.00 119.80 ?  114  ASN B O   1 
ATOM   5621  C CB  . ASN B  2  114 ? -45.272 -4.991  92.795  1.00 124.01 ?  114  ASN B CB  1 
ATOM   5622  C CG  . ASN B  2  114 ? -45.884 -4.654  94.144  1.00 127.98 ?  114  ASN B CG  1 
ATOM   5623  O OD1 . ASN B  2  114 ? -46.186 -5.542  94.940  1.00 131.07 ?  114  ASN B OD1 1 
ATOM   5624  N ND2 . ASN B  2  114 ? -46.066 -3.364  94.406  1.00 128.68 ?  114  ASN B ND2 1 
ATOM   5625  N N   . LEU B  2  115 ? -43.694 -7.346  90.704  1.00 116.87 ?  115  LEU B N   1 
ATOM   5626  C CA  . LEU B  2  115 ? -43.560 -7.781  89.313  1.00 115.19 ?  115  LEU B CA  1 
ATOM   5627  C C   . LEU B  2  115 ? -44.179 -9.173  89.189  1.00 113.38 ?  115  LEU B C   1 
ATOM   5628  O O   . LEU B  2  115 ? -43.498 -10.202 89.219  1.00 111.58 ?  115  LEU B O   1 
ATOM   5629  C CB  . LEU B  2  115 ? -42.097 -7.766  88.887  1.00 113.71 ?  115  LEU B CB  1 
ATOM   5630  C CG  . LEU B  2  115 ? -41.412 -6.397  88.964  1.00 115.93 ?  115  LEU B CG  1 
ATOM   5631  C CD1 . LEU B  2  115 ? -39.905 -6.525  88.812  1.00 114.36 ?  115  LEU B CD1 1 
ATOM   5632  C CD2 . LEU B  2  115 ? -41.974 -5.451  87.928  1.00 118.23 ?  115  LEU B CD2 1 
ATOM   5633  N N   . THR B  2  116 ? -45.510 -9.186  89.040  1.00 117.70 ?  116  THR B N   1 
ATOM   5634  C CA  . THR B  2  116 ? -46.269 -10.437 89.046  1.00 116.59 ?  116  THR B CA  1 
ATOM   5635  C C   . THR B  2  116 ? -45.755 -11.405 87.994  1.00 114.35 ?  116  THR B C   1 
ATOM   5636  O O   . THR B  2  116 ? -45.483 -12.574 88.288  1.00 113.47 ?  116  THR B O   1 
ATOM   5637  C CB  . THR B  2  116 ? -47.754 -10.158 88.815  1.00 117.75 ?  116  THR B CB  1 
ATOM   5638  O OG1 . THR B  2  116 ? -48.290 -9.446  89.937  1.00 120.30 ?  116  THR B OG1 1 
ATOM   5639  C CG2 . THR B  2  116 ? -48.517 -11.468 88.631  1.00 116.39 ?  116  THR B CG2 1 
ATOM   5640  N N   . GLU B  2  117 ? -45.596 -10.935 86.765  1.00 114.96 ?  117  GLU B N   1 
ATOM   5641  C CA  . GLU B  2  117 ? -44.982 -11.734 85.716  1.00 113.24 ?  117  GLU B CA  1 
ATOM   5642  C C   . GLU B  2  117 ? -43.515 -11.355 85.655  1.00 113.02 ?  117  GLU B C   1 
ATOM   5643  O O   . GLU B  2  117 ? -43.181 -10.179 85.478  1.00 113.80 ?  117  GLU B O   1 
ATOM   5644  C CB  . GLU B  2  117 ? -45.640 -11.526 84.356  1.00 112.45 ?  117  GLU B CB  1 
ATOM   5645  C CG  . GLU B  2  117 ? -45.598 -12.776 83.458  1.00 111.23 ?  117  GLU B CG  1 
ATOM   5646  C CD  . GLU B  2  117 ? -44.192 -13.266 83.039  1.00 111.13 ?  117  GLU B CD  1 
ATOM   5647  O OE1 . GLU B  2  117 ? -43.181 -12.553 83.221  1.00 111.40 ?  117  GLU B OE1 1 
ATOM   5648  O OE2 . GLU B  2  117 ? -44.109 -14.397 82.510  1.00 111.00 -1 117  GLU B OE2 1 
ATOM   5649  N N   . LEU B  2  118 ? -42.649 -12.353 85.798  1.00 114.60 ?  118  LEU B N   1 
ATOM   5650  C CA  . LEU B  2  118 ? -41.232 -12.098 85.991  1.00 114.23 ?  118  LEU B CA  1 
ATOM   5651  C C   . LEU B  2  118 ? -40.399 -13.355 85.738  1.00 113.77 ?  118  LEU B C   1 
ATOM   5652  O O   . LEU B  2  118 ? -40.670 -14.404 86.326  1.00 114.08 ?  118  LEU B O   1 
ATOM   5653  C CB  . LEU B  2  118 ? -41.048 -11.548 87.408  1.00 114.81 ?  118  LEU B CB  1 
ATOM   5654  C CG  . LEU B  2  118 ? -39.700 -10.999 87.816  1.00 114.50 ?  118  LEU B CG  1 
ATOM   5655  C CD1 . LEU B  2  118 ? -38.780 -12.166 88.173  1.00 113.70 ?  118  LEU B CD1 1 
ATOM   5656  C CD2 . LEU B  2  118 ? -39.193 -10.170 86.636  1.00 114.49 ?  118  LEU B CD2 1 
ATOM   5657  N N   . VAL B  2  119 ? -39.380 -13.286 84.881  1.00 111.61 ?  119  VAL B N   1 
ATOM   5658  C CA  . VAL B  2  119 ? -38.579 -14.456 84.538  1.00 112.14 ?  119  VAL B CA  1 
ATOM   5659  C C   . VAL B  2  119 ? -37.128 -14.307 84.991  1.00 111.90 ?  119  VAL B C   1 
ATOM   5660  O O   . VAL B  2  119 ? -36.585 -15.186 85.669  1.00 112.51 ?  119  VAL B O   1 
ATOM   5661  C CB  . VAL B  2  119 ? -38.658 -14.768 83.026  1.00 112.92 ?  119  VAL B CB  1 
ATOM   5662  C CG1 . VAL B  2  119 ? -37.509 -15.675 82.600  1.00 114.37 ?  119  VAL B CG1 1 
ATOM   5663  C CG2 . VAL B  2  119 ? -40.001 -15.419 82.696  1.00 113.38 ?  119  VAL B CG2 1 
ATOM   5664  N N   . SER B  2  120 ? -36.484 -13.200 84.628  1.00 115.42 ?  120  SER B N   1 
ATOM   5665  C CA  . SER B  2  120 ? -35.066 -12.986 84.897  1.00 115.19 ?  120  SER B CA  1 
ATOM   5666  C C   . SER B  2  120 ? -34.852 -11.747 85.757  1.00 114.55 ?  120  SER B C   1 
ATOM   5667  O O   . SER B  2  120 ? -35.394 -10.679 85.456  1.00 114.66 ?  120  SER B O   1 
ATOM   5668  C CB  . SER B  2  120 ? -34.287 -12.851 83.588  1.00 115.53 ?  120  SER B CB  1 
ATOM   5669  O OG  . SER B  2  120 ? -32.905 -13.084 83.783  1.00 115.94 ?  120  SER B OG  1 
ATOM   5670  N N   . LEU B  2  121 ? -34.023 -11.885 86.794  1.00 115.31 ?  121  LEU B N   1 
ATOM   5671  C CA  . LEU B  2  121 ? -33.611 -10.779 87.664  1.00 115.39 ?  121  LEU B CA  1 
ATOM   5672  C C   . LEU B  2  121 ? -32.088 -10.753 87.696  1.00 115.45 ?  121  LEU B C   1 
ATOM   5673  O O   . LEU B  2  121 ? -31.462 -11.560 88.389  1.00 115.70 ?  121  LEU B O   1 
ATOM   5674  C CB  . LEU B  2  121 ? -34.180 -10.913 89.075  1.00 115.80 ?  121  LEU B CB  1 
ATOM   5675  C CG  . LEU B  2  121 ? -35.383 -10.047 89.452  1.00 116.61 ?  121  LEU B CG  1 
ATOM   5676  C CD1 . LEU B  2  121 ? -35.008 -8.592  89.663  1.00 117.98 ?  121  LEU B CD1 1 
ATOM   5677  C CD2 . LEU B  2  121 ? -36.317 -10.095 88.340  1.00 116.37 ?  121  LEU B CD2 1 
ATOM   5678  N N   . ASP B  2  122 ? -31.492 -9.833  86.945  1.00 118.26 ?  122  ASP B N   1 
ATOM   5679  C CA  . ASP B  2  122 ? -30.040 -9.758  86.794  1.00 118.53 ?  122  ASP B CA  1 
ATOM   5680  C C   . ASP B  2  122 ? -29.555 -8.411  87.323  1.00 119.30 ?  122  ASP B C   1 
ATOM   5681  O O   . ASP B  2  122 ? -29.559 -7.411  86.596  1.00 119.91 ?  122  ASP B O   1 
ATOM   5682  C CB  . ASP B  2  122 ? -29.642 -9.965  85.338  1.00 118.62 ?  122  ASP B CB  1 
ATOM   5683  C CG  . ASP B  2  122 ? -29.867 -11.389 84.879  1.00 119.01 ?  122  ASP B CG  1 
ATOM   5684  O OD1 . ASP B  2  122 ? -31.040 -11.816 84.840  1.00 118.72 ?  122  ASP B OD1 1 
ATOM   5685  O OD2 . ASP B  2  122 ? -28.876 -12.082 84.565  1.00 120.25 -1 122  ASP B OD2 1 
ATOM   5686  N N   . LEU B  2  123 ? -29.132 -8.395  88.590  1.00 118.25 ?  123  LEU B N   1 
ATOM   5687  C CA  . LEU B  2  123 ? -28.578 -7.210  89.234  1.00 119.59 ?  123  LEU B CA  1 
ATOM   5688  C C   . LEU B  2  123 ? -27.107 -7.390  89.601  1.00 119.54 ?  123  LEU B C   1 
ATOM   5689  O O   . LEU B  2  123 ? -26.581 -6.637  90.427  1.00 120.58 ?  123  LEU B O   1 
ATOM   5690  C CB  . LEU B  2  123 ? -29.387 -6.840  90.482  1.00 120.76 ?  123  LEU B CB  1 
ATOM   5691  C CG  . LEU B  2  123 ? -30.904 -6.609  90.426  1.00 121.43 ?  123  LEU B CG  1 
ATOM   5692  C CD1 . LEU B  2  123 ? -31.284 -5.719  89.254  1.00 122.53 ?  123  LEU B CD1 1 
ATOM   5693  C CD2 . LEU B  2  123 ? -31.692 -7.908  90.398  1.00 119.64 ?  123  LEU B CD2 1 
ATOM   5694  N N   . TYR B  2  124 ? -26.428 -8.356  88.987  1.00 119.53 ?  124  TYR B N   1 
ATOM   5695  C CA  . TYR B  2  124 ? -25.065 -8.692  89.369  1.00 119.85 ?  124  TYR B CA  1 
ATOM   5696  C C   . TYR B  2  124 ? -24.078 -7.616  88.911  1.00 120.21 ?  124  TYR B C   1 
ATOM   5697  O O   . TYR B  2  124 ? -24.386 -6.766  88.071  1.00 120.28 ?  124  TYR B O   1 
ATOM   5698  C CB  . TYR B  2  124 ? -24.671 -10.064 88.808  1.00 120.16 ?  124  TYR B CB  1 
ATOM   5699  C CG  . TYR B  2  124 ? -24.765 -10.224 87.297  1.00 120.46 ?  124  TYR B CG  1 
ATOM   5700  C CD1 . TYR B  2  124 ? -25.945 -10.646 86.692  1.00 120.02 ?  124  TYR B CD1 1 
ATOM   5701  C CD2 . TYR B  2  124 ? -23.663 -9.987  86.481  1.00 121.38 ?  124  TYR B CD2 1 
ATOM   5702  C CE1 . TYR B  2  124 ? -26.029 -10.808 85.310  1.00 120.51 ?  124  TYR B CE1 1 
ATOM   5703  C CE2 . TYR B  2  124 ? -23.739 -10.145 85.100  1.00 122.13 ?  124  TYR B CE2 1 
ATOM   5704  C CZ  . TYR B  2  124 ? -24.924 -10.556 84.521  1.00 121.68 ?  124  TYR B CZ  1 
ATOM   5705  O OH  . TYR B  2  124 ? -25.008 -10.715 83.154  1.00 122.51 ?  124  TYR B OH  1 
ATOM   5706  N N   . LEU B  2  125 ? -22.875 -7.663  89.493  1.00 123.28 ?  125  LEU B N   1 
ATOM   5707  C CA  . LEU B  2  125 ? -21.768 -6.757  89.162  1.00 123.38 ?  125  LEU B CA  1 
ATOM   5708  C C   . LEU B  2  125 ? -22.133 -5.284  89.392  1.00 123.70 ?  125  LEU B C   1 
ATOM   5709  O O   . LEU B  2  125 ? -22.159 -4.468  88.467  1.00 123.66 ?  125  LEU B O   1 
ATOM   5710  C CB  . LEU B  2  125 ? -21.294 -6.988  87.721  1.00 123.48 ?  125  LEU B CB  1 
ATOM   5711  C CG  . LEU B  2  125 ? -20.571 -8.308  87.438  1.00 124.48 ?  125  LEU B CG  1 
ATOM   5712  C CD1 . LEU B  2  125 ? -20.457 -8.554  85.938  1.00 125.51 ?  125  LEU B CD1 1 
ATOM   5713  C CD2 . LEU B  2  125 ? -19.200 -8.327  88.098  1.00 124.81 ?  125  LEU B CD2 1 
ATOM   5714  N N   . ASN B  2  126 ? -22.408 -4.952  90.654  1.00 121.68 ?  126  ASN B N   1 
ATOM   5715  C CA  . ASN B  2  126 ? -22.774 -3.588  91.033  1.00 123.16 ?  126  ASN B CA  1 
ATOM   5716  C C   . ASN B  2  126 ? -22.233 -3.282  92.431  1.00 124.14 ?  126  ASN B C   1 
ATOM   5717  O O   . ASN B  2  126 ? -21.408 -4.022  92.979  1.00 123.27 ?  126  ASN B O   1 
ATOM   5718  C CB  . ASN B  2  126 ? -24.295 -3.402  90.959  1.00 124.49 ?  126  ASN B CB  1 
ATOM   5719  C CG  . ASN B  2  126 ? -24.738 -2.731  89.678  1.00 124.70 ?  126  ASN B CG  1 
ATOM   5720  O OD1 . ASN B  2  126 ? -24.512 -1.539  89.478  1.00 125.87 ?  126  ASN B OD1 1 
ATOM   5721  N ND2 . ASN B  2  126 ? -25.373 -3.496  88.801  1.00 123.59 ?  126  ASN B ND2 1 
ATOM   5722  N N   . ASN B  2  127 ? -22.694 -2.156  92.991  1.00 127.42 ?  127  ASN B N   1 
ATOM   5723  C CA  . ASN B  2  127 ? -22.313 -1.651  94.308  1.00 129.12 ?  127  ASN B CA  1 
ATOM   5724  C C   . ASN B  2  127 ? -23.540 -1.624  95.225  1.00 131.80 ?  127  ASN B C   1 
ATOM   5725  O O   . ASN B  2  127 ? -23.660 -0.820  96.148  1.00 134.71 ?  127  ASN B O   1 
ATOM   5726  C CB  . ASN B  2  127 ? -21.653 -0.274  94.137  1.00 130.01 ?  127  ASN B CB  1 
ATOM   5727  C CG  . ASN B  2  127 ? -21.328 0.438   95.451  1.00 132.28 ?  127  ASN B CG  1 
ATOM   5728  O OD1 . ASN B  2  127 ? -22.196 0.961   96.150  1.00 135.49 ?  127  ASN B OD1 1 
ATOM   5729  N ND2 . ASN B  2  127 ? -20.051 0.450   95.789  1.00 130.92 ?  127  ASN B ND2 1 
ATOM   5730  N N   . LEU B  2  128 ? -24.458 -2.552  95.011  1.00 130.04 ?  128  LEU B N   1 
ATOM   5731  C CA  . LEU B  2  128 ? -25.669 -2.560  95.815  1.00 132.14 ?  128  LEU B CA  1 
ATOM   5732  C C   . LEU B  2  128 ? -25.365 -3.041  97.230  1.00 132.20 ?  128  LEU B C   1 
ATOM   5733  O O   . LEU B  2  128 ? -24.463 -3.851  97.458  1.00 129.99 ?  128  LEU B O   1 
ATOM   5734  C CB  . LEU B  2  128 ? -26.737 -3.446  95.170  1.00 130.44 ?  128  LEU B CB  1 
ATOM   5735  C CG  . LEU B  2  128 ? -27.671 -2.828  94.119  1.00 131.76 ?  128  LEU B CG  1 
ATOM   5736  C CD1 . LEU B  2  128 ? -26.907 -2.066  93.052  1.00 131.82 ?  128  LEU B CD1 1 
ATOM   5737  C CD2 . LEU B  2  128 ? -28.596 -3.867  93.474  1.00 129.27 ?  128  LEU B CD2 1 
ATOM   5738  N N   . SER B  2  129 ? -26.138 -2.535  98.187  1.00 134.55 ?  129  SER B N   1 
ATOM   5739  C CA  . SER B  2  129 ? -25.955 -2.854  99.593  1.00 134.99 ?  129  SER B CA  1 
ATOM   5740  C C   . SER B  2  129 ? -27.307 -3.136  100.236 1.00 135.82 ?  129  SER B C   1 
ATOM   5741  O O   . SER B  2  129 ? -28.364 -2.983  99.618  1.00 136.30 ?  129  SER B O   1 
ATOM   5742  C CB  . SER B  2  129 ? -25.233 -1.720  100.334 1.00 138.03 ?  129  SER B CB  1 
ATOM   5743  O OG  . SER B  2  129 ? -26.039 -0.557  100.410 1.00 142.25 ?  129  SER B OG  1 
ATOM   5744  N N   . GLY B  2  130 ? -27.261 -3.541  101.501 1.00 142.73 ?  130  GLY B N   1 
ATOM   5745  C CA  . GLY B  2  130 ? -28.458 -3.854  102.241 1.00 143.17 ?  130  GLY B CA  1 
ATOM   5746  C C   . GLY B  2  130 ? -28.861 -5.306  102.087 1.00 139.75 ?  130  GLY B C   1 
ATOM   5747  O O   . GLY B  2  130 ? -28.124 -6.125  101.530 1.00 137.34 ?  130  GLY B O   1 
ATOM   5748  N N   . PRO B  2  131 ? -30.044 -5.648  102.577 1.00 139.50 ?  131  PRO B N   1 
ATOM   5749  C CA  . PRO B  2  131 ? -30.492 -7.042  102.580 1.00 136.96 ?  131  PRO B CA  1 
ATOM   5750  C C   . PRO B  2  131 ? -31.095 -7.448  101.238 1.00 135.05 ?  131  PRO B C   1 
ATOM   5751  O O   . PRO B  2  131 ? -31.190 -6.660  100.297 1.00 135.60 ?  131  PRO B O   1 
ATOM   5752  C CB  . PRO B  2  131 ? -31.545 -7.055  103.687 1.00 138.34 ?  131  PRO B CB  1 
ATOM   5753  C CG  . PRO B  2  131 ? -32.140 -5.690  103.619 1.00 140.95 ?  131  PRO B CG  1 
ATOM   5754  C CD  . PRO B  2  131 ? -31.013 -4.758  103.241 1.00 142.36 ?  131  PRO B CD  1 
ATOM   5755  N N   . ILE B  2  132 ? -31.473 -8.722  101.164 1.00 135.39 ?  132  ILE B N   1 
ATOM   5756  C CA  . ILE B  2  132 ? -32.265 -9.264  100.064 1.00 132.73 ?  132  ILE B CA  1 
ATOM   5757  C C   . ILE B  2  132 ? -33.727 -9.233  100.509 1.00 134.09 ?  132  ILE B C   1 
ATOM   5758  O O   . ILE B  2  132 ? -34.100 -9.998  101.415 1.00 137.81 ?  132  ILE B O   1 
ATOM   5759  C CB  . ILE B  2  132 ? -31.819 -10.688 99.698  1.00 133.41 ?  132  ILE B CB  1 
ATOM   5760  C CG1 . ILE B  2  132 ? -30.584 -10.651 98.792  1.00 131.12 ?  132  ILE B CG1 1 
ATOM   5761  C CG2 . ILE B  2  132 ? -32.929 -11.461 99.012  1.00 132.45 ?  132  ILE B CG2 1 
ATOM   5762  C CD1 . ILE B  2  132 ? -29.301 -10.339 99.522  1.00 133.07 ?  132  ILE B CD1 1 
ATOM   5763  N N   . PRO B  2  133 ? -34.556 -8.341  99.970  1.00 133.97 ?  133  PRO B N   1 
ATOM   5764  C CA  . PRO B  2  133 ? -35.950 -8.249  100.422 1.00 135.09 ?  133  PRO B CA  1 
ATOM   5765  C C   . PRO B  2  133 ? -36.646 -9.601  100.389 1.00 133.67 ?  133  PRO B C   1 
ATOM   5766  O O   . PRO B  2  133 ? -36.526 -10.361 99.428  1.00 131.95 ?  133  PRO B O   1 
ATOM   5767  C CB  . PRO B  2  133 ? -36.578 -7.266  99.427  1.00 136.05 ?  133  PRO B CB  1 
ATOM   5768  C CG  . PRO B  2  133 ? -35.423 -6.602  98.702  1.00 136.13 ?  133  PRO B CG  1 
ATOM   5769  C CD  . PRO B  2  133 ? -34.138 -7.128  99.258  1.00 135.17 ?  133  PRO B CD  1 
ATOM   5770  N N   . SER B  2  134 ? -37.376 -9.902  101.466 1.00 139.31 ?  134  SER B N   1 
ATOM   5771  C CA  . SER B  2  134 ? -38.152 -11.133 101.533 1.00 138.79 ?  134  SER B CA  1 
ATOM   5772  C C   . SER B  2  134 ? -39.334 -11.131 100.575 1.00 138.62 ?  134  SER B C   1 
ATOM   5773  O O   . SER B  2  134 ? -39.932 -12.190 100.349 1.00 138.20 ?  134  SER B O   1 
ATOM   5774  C CB  . SER B  2  134 ? -38.642 -11.357 102.961 1.00 142.64 ?  134  SER B CB  1 
ATOM   5775  O OG  . SER B  2  134 ? -39.549 -10.335 103.336 1.00 143.48 ?  134  SER B OG  1 
ATOM   5776  N N   . THR B  2  135 ? -39.686 -9.971  100.016 1.00 135.33 ?  135  THR B N   1 
ATOM   5777  C CA  . THR B  2  135 ? -40.799 -9.870  99.082  1.00 133.68 ?  135  THR B CA  1 
ATOM   5778  C C   . THR B  2  135 ? -40.522 -10.545 97.747  1.00 131.20 ?  135  THR B C   1 
ATOM   5779  O O   . THR B  2  135 ? -41.460 -10.716 96.965  1.00 130.96 ?  135  THR B O   1 
ATOM   5780  C CB  . THR B  2  135 ? -41.162 -8.404  98.836  1.00 134.81 ?  135  THR B CB  1 
ATOM   5781  O OG1 . THR B  2  135 ? -39.967 -7.624  98.717  1.00 134.88 ?  135  THR B OG1 1 
ATOM   5782  C CG2 . THR B  2  135 ? -42.011 -7.869  99.985  1.00 137.34 ?  135  THR B CG2 1 
ATOM   5783  N N   . LEU B  2  136 ? -39.274 -10.915 97.451  1.00 135.80 ?  136  LEU B N   1 
ATOM   5784  C CA  . LEU B  2  136 ? -39.017 -11.584 96.180  1.00 134.14 ?  136  LEU B CA  1 
ATOM   5785  C C   . LEU B  2  136 ? -39.646 -12.967 96.107  1.00 133.88 ?  136  LEU B C   1 
ATOM   5786  O O   . LEU B  2  136 ? -39.679 -13.555 95.020  1.00 133.01 ?  136  LEU B O   1 
ATOM   5787  C CB  . LEU B  2  136 ? -37.515 -11.689 95.902  1.00 132.94 ?  136  LEU B CB  1 
ATOM   5788  C CG  . LEU B  2  136 ? -36.616 -10.545 96.362  1.00 133.70 ?  136  LEU B CG  1 
ATOM   5789  C CD1 . LEU B  2  136 ? -35.183 -11.016 96.408  1.00 132.76 ?  136  LEU B CD1 1 
ATOM   5790  C CD2 . LEU B  2  136 ? -36.755 -9.333  95.456  1.00 134.29 ?  136  LEU B CD2 1 
ATOM   5791  N N   . GLY B  2  137 ? -40.137 -13.501 97.226  1.00 132.75 ?  137  GLY B N   1 
ATOM   5792  C CA  . GLY B  2  137 ? -40.866 -14.752 97.184  1.00 133.22 ?  137  GLY B CA  1 
ATOM   5793  C C   . GLY B  2  137 ? -42.200 -14.678 96.470  1.00 133.58 ?  137  GLY B C   1 
ATOM   5794  O O   . GLY B  2  137 ? -42.801 -15.726 96.218  1.00 133.91 ?  137  GLY B O   1 
ATOM   5795  N N   . ARG B  2  138 ? -42.673 -13.477 96.132  1.00 131.53 ?  138  ARG B N   1 
ATOM   5796  C CA  . ARG B  2  138 ? -43.911 -13.349 95.372  1.00 132.02 ?  138  ARG B CA  1 
ATOM   5797  C C   . ARG B  2  138 ? -43.708 -13.563 93.877  1.00 130.59 ?  138  ARG B C   1 
ATOM   5798  O O   . ARG B  2  138 ? -44.689 -13.787 93.161  1.00 130.80 ?  138  ARG B O   1 
ATOM   5799  C CB  . ARG B  2  138 ? -44.546 -11.977 95.618  1.00 133.57 ?  138  ARG B CB  1 
ATOM   5800  C CG  . ARG B  2  138 ? -44.344 -11.443 97.028  1.00 134.90 ?  138  ARG B CG  1 
ATOM   5801  C CD  . ARG B  2  138 ? -45.614 -10.851 97.611  1.00 137.42 ?  138  ARG B CD  1 
ATOM   5802  N NE  . ARG B  2  138 ? -45.980 -9.598  96.962  1.00 138.31 ?  138  ARG B NE  1 
ATOM   5803  C CZ  . ARG B  2  138 ? -47.129 -9.392  96.334  1.00 139.46 ?  138  ARG B CZ  1 
ATOM   5804  N NH1 . ARG B  2  138 ? -48.054 -10.336 96.261  1.00 139.76 ?  138  ARG B NH1 1 
ATOM   5805  N NH2 . ARG B  2  138 ? -47.357 -8.211  95.766  1.00 140.57 ?  138  ARG B NH2 1 
ATOM   5806  N N   . LEU B  2  139 ? -42.466 -13.492 93.390  1.00 129.59 ?  139  LEU B N   1 
ATOM   5807  C CA  . LEU B  2  139 ? -42.160 -13.731 91.978  1.00 128.44 ?  139  LEU B CA  1 
ATOM   5808  C C   . LEU B  2  139 ? -42.034 -15.238 91.746  1.00 128.16 ?  139  LEU B C   1 
ATOM   5809  O O   . LEU B  2  139 ? -40.947 -15.790 91.564  1.00 127.63 ?  139  LEU B O   1 
ATOM   5810  C CB  . LEU B  2  139 ? -40.878 -13.016 91.573  1.00 127.51 ?  139  LEU B CB  1 
ATOM   5811  C CG  . LEU B  2  139 ? -40.564 -11.654 92.189  1.00 128.24 ?  139  LEU B CG  1 
ATOM   5812  C CD1 . LEU B  2  139 ? -39.140 -11.248 91.862  1.00 127.33 ?  139  LEU B CD1 1 
ATOM   5813  C CD2 . LEU B  2  139 ? -41.538 -10.607 91.696  1.00 129.52 ?  139  LEU B CD2 1 
ATOM   5814  N N   . LYS B  2  140 ? -43.188 -15.907 91.737  1.00 128.15 ?  140  LYS B N   1 
ATOM   5815  C CA  . LYS B  2  140 ? -43.186 -17.359 91.598  1.00 128.40 ?  140  LYS B CA  1 
ATOM   5816  C C   . LYS B  2  140 ? -42.748 -17.817 90.212  1.00 127.75 ?  140  LYS B C   1 
ATOM   5817  O O   . LYS B  2  140 ? -42.435 -19.000 90.041  1.00 128.30 ?  140  LYS B O   1 
ATOM   5818  C CB  . LYS B  2  140 ? -44.567 -17.936 91.891  1.00 129.38 ?  140  LYS B CB  1 
ATOM   5819  C CG  . LYS B  2  140 ? -45.237 -17.463 93.164  1.00 130.52 ?  140  LYS B CG  1 
ATOM   5820  C CD  . LYS B  2  140 ? -44.472 -17.827 94.424  1.00 131.16 ?  140  LYS B CD  1 
ATOM   5821  C CE  . LYS B  2  140 ? -45.309 -17.510 95.659  1.00 132.75 ?  140  LYS B CE  1 
ATOM   5822  N NZ  . LYS B  2  140 ? -46.608 -18.242 95.673  1.00 134.51 ?  140  LYS B NZ  1 
ATOM   5823  N N   . LYS B  2  141 ? -42.746 -16.922 89.220  1.00 123.75 ?  141  LYS B N   1 
ATOM   5824  C CA  . LYS B  2  141 ? -42.352 -17.254 87.855  1.00 121.54 ?  141  LYS B CA  1 
ATOM   5825  C C   . LYS B  2  141 ? -40.850 -17.138 87.635  1.00 120.43 ?  141  LYS B C   1 
ATOM   5826  O O   . LYS B  2  141 ? -40.372 -17.428 86.531  1.00 119.04 ?  141  LYS B O   1 
ATOM   5827  C CB  . LYS B  2  141 ? -43.057 -16.351 86.815  1.00 118.19 ?  141  LYS B CB  1 
ATOM   5828  C CG  . LYS B  2  141 ? -44.567 -15.926 86.909  1.00 118.36 ?  141  LYS B CG  1 
ATOM   5829  C CD  . LYS B  2  141 ? -45.563 -16.996 87.383  1.00 121.93 ?  141  LYS B CD  1 
ATOM   5830  C CE  . LYS B  2  141 ? -45.781 -16.941 88.918  1.00 125.16 ?  141  LYS B CE  1 
ATOM   5831  N NZ  . LYS B  2  141 ? -46.946 -17.747 89.460  1.00 128.96 ?  141  LYS B NZ  1 
ATOM   5832  N N   . LEU B  2  142 ? -40.112 -16.731 88.661  1.00 121.61 ?  142  LEU B N   1 
ATOM   5833  C CA  . LEU B  2  142 ? -38.693 -16.456 88.538  1.00 121.28 ?  142  LEU B CA  1 
ATOM   5834  C C   . LEU B  2  142 ? -37.930 -17.721 88.168  1.00 122.48 ?  142  LEU B C   1 
ATOM   5835  O O   . LEU B  2  142 ? -38.064 -18.758 88.825  1.00 123.53 ?  142  LEU B O   1 
ATOM   5836  C CB  . LEU B  2  142 ? -38.192 -15.880 89.861  1.00 120.92 ?  142  LEU B CB  1 
ATOM   5837  C CG  . LEU B  2  142 ? -36.735 -16.033 90.278  1.00 120.93 ?  142  LEU B CG  1 
ATOM   5838  C CD1 . LEU B  2  142 ? -35.827 -15.448 89.231  1.00 120.43 ?  142  LEU B CD1 1 
ATOM   5839  C CD2 . LEU B  2  142 ? -36.497 -15.360 91.610  1.00 120.68 ?  142  LEU B CD2 1 
ATOM   5840  N N   . ARG B  2  143 ? -37.142 -17.628 87.099  1.00 120.61 ?  143  ARG B N   1 
ATOM   5841  C CA  . ARG B  2  143 ? -36.225 -18.678 86.678  1.00 122.53 ?  143  ARG B CA  1 
ATOM   5842  C C   . ARG B  2  143 ? -34.784 -18.385 87.075  1.00 122.55 ?  143  ARG B C   1 
ATOM   5843  O O   . ARG B  2  143 ? -34.102 -19.254 87.620  1.00 123.96 ?  143  ARG B O   1 
ATOM   5844  C CB  . ARG B  2  143 ? -36.294 -18.870 85.161  1.00 123.78 ?  143  ARG B CB  1 
ATOM   5845  C CG  . ARG B  2  143 ? -37.665 -19.139 84.584  1.00 123.75 ?  143  ARG B CG  1 
ATOM   5846  C CD  . ARG B  2  143 ? -37.488 -19.871 83.266  1.00 126.25 ?  143  ARG B CD  1 
ATOM   5847  N NE  . ARG B  2  143 ? -38.680 -19.856 82.428  1.00 125.90 ?  143  ARG B NE  1 
ATOM   5848  C CZ  . ARG B  2  143 ? -38.804 -20.558 81.310  1.00 128.18 ?  143  ARG B CZ  1 
ATOM   5849  N NH1 . ARG B  2  143 ? -37.836 -21.351 80.885  1.00 131.41 ?  143  ARG B NH1 1 
ATOM   5850  N NH2 . ARG B  2  143 ? -39.928 -20.464 80.605  1.00 127.42 ?  143  ARG B NH2 1 
ATOM   5851  N N   . PHE B  2  144 ? -34.301 -17.178 86.789  1.00 119.69 ?  144  PHE B N   1 
ATOM   5852  C CA  . PHE B  2  144 ? -32.895 -16.830 86.935  1.00 119.74 ?  144  PHE B CA  1 
ATOM   5853  C C   . PHE B  2  144 ? -32.745 -15.631 87.861  1.00 118.20 ?  144  PHE B C   1 
ATOM   5854  O O   . PHE B  2  144 ? -33.340 -14.576 87.617  1.00 116.45 ?  144  PHE B O   1 
ATOM   5855  C CB  . PHE B  2  144 ? -32.267 -16.519 85.570  1.00 120.41 ?  144  PHE B CB  1 
ATOM   5856  C CG  . PHE B  2  144 ? -32.753 -17.409 84.457  1.00 122.61 ?  144  PHE B CG  1 
ATOM   5857  C CD1 . PHE B  2  144 ? -32.385 -18.744 84.404  1.00 125.71 ?  144  PHE B CD1 1 
ATOM   5858  C CD2 . PHE B  2  144 ? -33.581 -16.910 83.466  1.00 121.95 ?  144  PHE B CD2 1 
ATOM   5859  C CE1 . PHE B  2  144 ? -32.834 -19.564 83.383  1.00 128.35 ?  144  PHE B CE1 1 
ATOM   5860  C CE2 . PHE B  2  144 ? -34.032 -17.725 82.444  1.00 124.34 ?  144  PHE B CE2 1 
ATOM   5861  C CZ  . PHE B  2  144 ? -33.659 -19.053 82.404  1.00 127.68 ?  144  PHE B CZ  1 
ATOM   5862  N N   . LEU B  2  145 ? -31.931 -15.786 88.904  1.00 123.96 ?  145  LEU B N   1 
ATOM   5863  C CA  . LEU B  2  145 ? -31.644 -14.709 89.848  1.00 122.80 ?  145  LEU B CA  1 
ATOM   5864  C C   . LEU B  2  145 ? -30.141 -14.681 90.089  1.00 123.36 ?  145  LEU B C   1 
ATOM   5865  O O   . LEU B  2  145 ? -29.586 -15.612 90.681  1.00 125.86 ?  145  LEU B O   1 
ATOM   5866  C CB  . LEU B  2  145 ? -32.405 -14.902 91.162  1.00 123.64 ?  145  LEU B CB  1 
ATOM   5867  C CG  . LEU B  2  145 ? -32.231 -13.814 92.226  1.00 123.85 ?  145  LEU B CG  1 
ATOM   5868  C CD1 . LEU B  2  145 ? -33.554 -13.551 92.914  1.00 124.35 ?  145  LEU B CD1 1 
ATOM   5869  C CD2 . LEU B  2  145 ? -31.172 -14.193 93.250  1.00 126.98 ?  145  LEU B CD2 1 
ATOM   5870  N N   . ARG B  2  146 ? -29.487 -13.612 89.637  1.00 124.57 ?  146  ARG B N   1 
ATOM   5871  C CA  . ARG B  2  146 ? -28.042 -13.457 89.764  1.00 125.23 ?  146  ARG B CA  1 
ATOM   5872  C C   . ARG B  2  146 ? -27.743 -12.118 90.424  1.00 124.53 ?  146  ARG B C   1 
ATOM   5873  O O   . ARG B  2  146 ? -28.062 -11.064 89.863  1.00 124.08 ?  146  ARG B O   1 
ATOM   5874  C CB  . ARG B  2  146 ? -27.356 -13.552 88.397  1.00 126.13 ?  146  ARG B CB  1 
ATOM   5875  C CG  . ARG B  2  146 ? -27.614 -14.863 87.670  1.00 127.86 ?  146  ARG B CG  1 
ATOM   5876  C CD  . ARG B  2  146 ? -27.247 -14.761 86.200  1.00 128.99 ?  146  ARG B CD  1 
ATOM   5877  N NE  . ARG B  2  146 ? -27.838 -15.835 85.411  1.00 130.88 ?  146  ARG B NE  1 
ATOM   5878  C CZ  . ARG B  2  146 ? -28.984 -15.736 84.752  1.00 130.03 ?  146  ARG B CZ  1 
ATOM   5879  N NH1 . ARG B  2  146 ? -29.699 -14.623 84.772  1.00 127.36 ?  146  ARG B NH1 1 
ATOM   5880  N NH2 . ARG B  2  146 ? -29.423 -16.779 84.053  1.00 132.38 ?  146  ARG B NH2 1 
ATOM   5881  N N   . LEU B  2  147 ? -27.121 -12.163 91.611  1.00 136.94 ?  147  LEU B N   1 
ATOM   5882  C CA  . LEU B  2  147 ? -26.826 -10.963 92.390  1.00 134.23 ?  147  LEU B CA  1 
ATOM   5883  C C   . LEU B  2  147 ? -25.362 -10.894 92.817  1.00 133.50 ?  147  LEU B C   1 
ATOM   5884  O O   . LEU B  2  147 ? -25.026 -10.120 93.719  1.00 131.68 ?  147  LEU B O   1 
ATOM   5885  C CB  . LEU B  2  147 ? -27.720 -10.882 93.632  1.00 134.24 ?  147  LEU B CB  1 
ATOM   5886  C CG  . LEU B  2  147 ? -29.214 -11.187 93.516  1.00 133.59 ?  147  LEU B CG  1 
ATOM   5887  C CD1 . LEU B  2  147 ? -29.894 -11.054 94.875  1.00 132.81 ?  147  LEU B CD1 1 
ATOM   5888  C CD2 . LEU B  2  147 ? -29.875 -10.281 92.492  1.00 126.15 ?  147  LEU B CD2 1 
ATOM   5889  N N   . ASN B  2  148 ? -24.484 -11.667 92.184  1.00 140.31 ?  148  ASN B N   1 
ATOM   5890  C CA  . ASN B  2  148 ? -23.122 -11.812 92.677  1.00 138.70 ?  148  ASN B CA  1 
ATOM   5891  C C   . ASN B  2  148 ? -22.316 -10.528 92.469  1.00 134.66 ?  148  ASN B C   1 
ATOM   5892  O O   . ASN B  2  148 ? -22.746 -9.586  91.796  1.00 132.70 ?  148  ASN B O   1 
ATOM   5893  C CB  . ASN B  2  148 ? -22.429 -12.986 91.988  1.00 137.21 ?  148  ASN B CB  1 
ATOM   5894  C CG  . ASN B  2  148 ? -22.411 -12.848 90.483  1.00 133.20 ?  148  ASN B CG  1 
ATOM   5895  O OD1 . ASN B  2  148 ? -23.452 -12.910 89.828  1.00 133.41 ?  148  ASN B OD1 1 
ATOM   5896  N ND2 . ASN B  2  148 ? -21.224 -12.651 89.923  1.00 128.71 ?  148  ASN B ND2 1 
ATOM   5897  N N   . ASN B  2  149 ? -21.123 -10.511 93.065  1.00 139.85 ?  149  ASN B N   1 
ATOM   5898  C CA  . ASN B  2  149 ? -20.183 -9.391  92.983  1.00 135.44 ?  149  ASN B CA  1 
ATOM   5899  C C   . ASN B  2  149 ? -20.841 -8.073  93.397  1.00 133.99 ?  149  ASN B C   1 
ATOM   5900  O O   . ASN B  2  149 ? -20.949 -7.120  92.623  1.00 130.26 ?  149  ASN B O   1 
ATOM   5901  C CB  . ASN B  2  149 ? -19.573 -9.298  91.583  1.00 131.37 ?  149  ASN B CB  1 
ATOM   5902  C CG  . ASN B  2  149 ? -18.397 -10.238 91.401  1.00 131.85 ?  149  ASN B CG  1 
ATOM   5903  O OD1 . ASN B  2  149 ? -18.468 -11.414 91.759  1.00 134.71 ?  149  ASN B OD1 1 
ATOM   5904  N ND2 . ASN B  2  149 ? -17.304 -9.721  90.852  1.00 129.68 ?  149  ASN B ND2 1 
ATOM   5905  N N   . ASN B  2  150 ? -21.280 -8.036  94.654  1.00 137.12 ?  150  ASN B N   1 
ATOM   5906  C CA  . ASN B  2  150 ? -21.956 -6.872  95.211  1.00 135.28 ?  150  ASN B CA  1 
ATOM   5907  C C   . ASN B  2  150 ? -21.599 -6.759  96.689  1.00 139.64 ?  150  ASN B C   1 
ATOM   5908  O O   . ASN B  2  150 ? -20.855 -7.579  97.236  1.00 143.52 ?  150  ASN B O   1 
ATOM   5909  C CB  . ASN B  2  150 ? -23.473 -6.967  95.013  1.00 135.76 ?  150  ASN B CB  1 
ATOM   5910  C CG  . ASN B  2  150 ? -23.942 -6.275  93.756  1.00 131.62 ?  150  ASN B CG  1 
ATOM   5911  O OD1 . ASN B  2  150 ? -24.232 -5.079  93.762  1.00 126.07 ?  150  ASN B OD1 1 
ATOM   5912  N ND2 . ASN B  2  150 ? -24.017 -7.025  92.663  1.00 133.73 ?  150  ASN B ND2 1 
ATOM   5913  N N   . SER B  2  151 ? -22.143 -5.727  97.337  1.00 135.01 ?  151  SER B N   1 
ATOM   5914  C CA  . SER B  2  151 ? -21.936 -5.481  98.759  1.00 140.31 ?  151  SER B CA  1 
ATOM   5915  C C   . SER B  2  151 ? -23.160 -5.855  99.591  1.00 142.41 ?  151  SER B C   1 
ATOM   5916  O O   . SER B  2  151 ? -23.403 -5.257  100.645 1.00 145.57 ?  151  SER B O   1 
ATOM   5917  C CB  . SER B  2  151 ? -21.556 -4.019  98.992  1.00 140.22 ?  151  SER B CB  1 
ATOM   5918  O OG  . SER B  2  151 ? -21.119 -3.813  100.322 1.00 145.70 ?  151  SER B OG  1 
ATOM   5919  N N   . LEU B  2  152 ? -23.937 -6.832  99.130  1.00 143.87 ?  152  LEU B N   1 
ATOM   5920  C CA  . LEU B  2  152 ? -25.145 -7.244  99.832  1.00 145.70 ?  152  LEU B CA  1 
ATOM   5921  C C   . LEU B  2  152 ? -24.788 -7.928  101.148 1.00 151.86 ?  152  LEU B C   1 
ATOM   5922  O O   . LEU B  2  152 ? -23.787 -8.643  101.242 1.00 154.25 ?  152  LEU B O   1 
ATOM   5923  C CB  . LEU B  2  152 ? -25.967 -8.189  98.950  1.00 143.20 ?  152  LEU B CB  1 
ATOM   5924  C CG  . LEU B  2  152 ? -27.025 -7.606  98.003  1.00 138.88 ?  152  LEU B CG  1 
ATOM   5925  C CD1 . LEU B  2  152 ? -26.518 -6.365  97.295  1.00 134.19 ?  152  LEU B CD1 1 
ATOM   5926  C CD2 . LEU B  2  152 ? -27.454 -8.645  96.974  1.00 140.82 ?  152  LEU B CD2 1 
ATOM   5927  N N   . SER B  2  153 ? -25.621 -7.712  102.166 1.00 149.33 ?  153  SER B N   1 
ATOM   5928  C CA  . SER B  2  153 ? -25.374 -8.239  103.504 1.00 155.55 ?  153  SER B CA  1 
ATOM   5929  C C   . SER B  2  153 ? -26.690 -8.656  104.145 1.00 157.28 ?  153  SER B C   1 
ATOM   5930  O O   . SER B  2  153 ? -27.648 -7.877  104.157 1.00 155.44 ?  153  SER B O   1 
ATOM   5931  C CB  . SER B  2  153 ? -24.662 -7.202  104.382 1.00 158.61 ?  153  SER B CB  1 
ATOM   5932  O OG  . SER B  2  153 ? -25.370 -5.974  104.397 1.00 156.59 ?  153  SER B OG  1 
ATOM   5933  N N   . GLY B  2  154 ? -26.735 -9.870  104.668 1.00 163.36 ?  154  GLY B N   1 
ATOM   5934  C CA  . GLY B  2  154 ? -27.928 -10.375 105.327 1.00 165.57 ?  154  GLY B CA  1 
ATOM   5935  C C   . GLY B  2  154 ? -27.987 -11.893 105.246 1.00 167.49 ?  154  GLY B C   1 
ATOM   5936  O O   . GLY B  2  154 ? -26.957 -12.560 105.169 1.00 169.30 ?  154  GLY B O   1 
ATOM   5937  N N   . GLU B  2  155 ? -29.214 -12.414 105.280 1.00 164.63 ?  155  GLU B N   1 
ATOM   5938  C CA  . GLU B  2  155 ? -29.474 -13.842 105.173 1.00 166.41 ?  155  GLU B CA  1 
ATOM   5939  C C   . GLU B  2  155 ? -30.485 -14.086 104.061 1.00 161.56 ?  155  GLU B C   1 
ATOM   5940  O O   . GLU B  2  155 ? -31.311 -13.222 103.754 1.00 158.15 ?  155  GLU B O   1 
ATOM   5941  C CB  . GLU B  2  155 ? -29.991 -14.411 106.503 1.00 172.36 ?  155  GLU B CB  1 
ATOM   5942  C CG  . GLU B  2  155 ? -30.196 -15.918 106.527 1.00 175.15 ?  155  GLU B CG  1 
ATOM   5943  C CD  . GLU B  2  155 ? -30.585 -16.426 107.901 1.00 181.45 ?  155  GLU B CD  1 
ATOM   5944  O OE1 . GLU B  2  155 ? -31.457 -15.803 108.542 1.00 182.14 ?  155  GLU B OE1 1 
ATOM   5945  O OE2 . GLU B  2  155 ? -30.021 -17.449 108.341 1.00 185.90 -1 155  GLU B OE2 1 
ATOM   5946  N N   . ILE B  2  156 ? -30.415 -15.270 103.459 1.00 161.22 ?  156  ILE B N   1 
ATOM   5947  C CA  . ILE B  2  156 ? -31.286 -15.629 102.340 1.00 158.39 ?  156  ILE B CA  1 
ATOM   5948  C C   . ILE B  2  156 ? -32.686 -15.923 102.869 1.00 159.35 ?  156  ILE B C   1 
ATOM   5949  O O   . ILE B  2  156 ? -32.854 -16.802 103.728 1.00 163.43 ?  156  ILE B O   1 
ATOM   5950  C CB  . ILE B  2  156 ? -30.726 -16.826 101.552 1.00 159.99 ?  156  ILE B CB  1 
ATOM   5951  C CG1 . ILE B  2  156 ? -29.403 -16.461 100.875 1.00 159.17 ?  156  ILE B CG1 1 
ATOM   5952  C CG2 . ILE B  2  156 ? -31.732 -17.291 100.509 1.00 159.15 ?  156  ILE B CG2 1 
ATOM   5953  C CD1 . ILE B  2  156 ? -28.169 -16.757 101.706 1.00 161.00 ?  156  ILE B CD1 1 
ATOM   5954  N N   . PRO B  2  157 ? -33.709 -15.201 102.406 1.00 156.79 ?  157  PRO B N   1 
ATOM   5955  C CA  . PRO B  2  157 ? -35.067 -15.427 102.918 1.00 157.17 ?  157  PRO B CA  1 
ATOM   5956  C C   . PRO B  2  157 ? -35.575 -16.828 102.609 1.00 159.25 ?  157  PRO B C   1 
ATOM   5957  O O   . PRO B  2  157 ? -35.284 -17.406 101.558 1.00 158.36 ?  157  PRO B O   1 
ATOM   5958  C CB  . PRO B  2  157 ? -35.912 -14.368 102.198 1.00 151.66 ?  157  PRO B CB  1 
ATOM   5959  C CG  . PRO B  2  157 ? -34.968 -13.397 101.608 1.00 148.81 ?  157  PRO B CG  1 
ATOM   5960  C CD  . PRO B  2  157 ? -33.586 -13.963 101.617 1.00 151.99 ?  157  PRO B CD  1 
ATOM   5961  N N   . ARG B  2  158 ? -36.355 -17.368 103.551 1.00 159.47 ?  158  ARG B N   1 
ATOM   5962  C CA  . ARG B  2  158 ? -37.036 -18.639 103.337 1.00 161.07 ?  158  ARG B CA  1 
ATOM   5963  C C   . ARG B  2  158 ? -38.037 -18.558 102.193 1.00 156.10 ?  158  ARG B C   1 
ATOM   5964  O O   . ARG B  2  158 ? -38.339 -19.583 101.570 1.00 156.00 ?  158  ARG B O   1 
ATOM   5965  C CB  . ARG B  2  158 ? -37.732 -19.079 104.631 1.00 166.70 ?  158  ARG B CB  1 
ATOM   5966  C CG  . ARG B  2  158 ? -38.635 -20.309 104.513 1.00 168.70 ?  158  ARG B CG  1 
ATOM   5967  C CD  . ARG B  2  158 ? -40.105 -19.921 104.353 1.00 166.59 ?  158  ARG B CD  1 
ATOM   5968  N NE  . ARG B  2  158 ? -40.887 -20.975 103.715 1.00 166.42 ?  158  ARG B NE  1 
ATOM   5969  C CZ  . ARG B  2  158 ? -42.134 -20.830 103.288 1.00 164.12 ?  158  ARG B CZ  1 
ATOM   5970  N NH1 . ARG B  2  158 ? -42.772 -19.676 103.393 1.00 161.65 ?  158  ARG B NH1 1 
ATOM   5971  N NH2 . ARG B  2  158 ? -42.757 -21.870 102.739 1.00 164.51 ?  158  ARG B NH2 1 
ATOM   5972  N N   . SER B  2  159 ? -38.542 -17.359 101.889 1.00 157.08 ?  159  SER B N   1 
ATOM   5973  C CA  . SER B  2  159 ? -39.539 -17.217 100.835 1.00 152.53 ?  159  SER B CA  1 
ATOM   5974  C C   . SER B  2  159 ? -38.987 -17.639 99.483  1.00 151.02 ?  159  SER B C   1 
ATOM   5975  O O   . SER B  2  159 ? -39.733 -18.164 98.647  1.00 149.14 ?  159  SER B O   1 
ATOM   5976  C CB  . SER B  2  159 ? -40.040 -15.774 100.774 1.00 148.43 ?  159  SER B CB  1 
ATOM   5977  O OG  . SER B  2  159 ? -38.985 -14.878 100.475 1.00 146.01 ?  159  SER B OG  1 
ATOM   5978  N N   . LEU B  2  160 ? -37.688 -17.429 99.253  1.00 151.64 ?  160  LEU B N   1 
ATOM   5979  C CA  . LEU B  2  160 ? -37.079 -17.808 97.983  1.00 152.28 ?  160  LEU B CA  1 
ATOM   5980  C C   . LEU B  2  160 ? -37.130 -19.312 97.742  1.00 155.80 ?  160  LEU B C   1 
ATOM   5981  O O   . LEU B  2  160 ? -36.906 -19.755 96.609  1.00 156.04 ?  160  LEU B O   1 
ATOM   5982  C CB  . LEU B  2  160 ? -35.628 -17.318 97.924  1.00 154.21 ?  160  LEU B CB  1 
ATOM   5983  C CG  . LEU B  2  160 ? -35.402 -15.803 97.932  1.00 150.19 ?  160  LEU B CG  1 
ATOM   5984  C CD1 . LEU B  2  160 ? -33.917 -15.472 98.002  1.00 152.41 ?  160  LEU B CD1 1 
ATOM   5985  C CD2 . LEU B  2  160 ? -36.036 -15.162 96.708  1.00 144.94 ?  160  LEU B CD2 1 
ATOM   5986  N N   . THR B  2  161 ? -37.411 -20.104 98.778  1.00 148.11 ?  161  THR B N   1 
ATOM   5987  C CA  . THR B  2  161 ? -37.473 -21.552 98.640  1.00 151.26 ?  161  THR B CA  1 
ATOM   5988  C C   . THR B  2  161 ? -38.814 -22.051 98.116  1.00 150.13 ?  161  THR B C   1 
ATOM   5989  O O   . THR B  2  161 ? -38.926 -23.237 97.792  1.00 152.19 ?  161  THR B O   1 
ATOM   5990  C CB  . THR B  2  161 ? -37.172 -22.225 99.983  1.00 157.94 ?  161  THR B CB  1 
ATOM   5991  O OG1 . THR B  2  161 ? -38.244 -21.978 100.902 1.00 160.08 ?  161  THR B OG1 1 
ATOM   5992  C CG2 . THR B  2  161 ? -35.877 -21.682 100.569 1.00 159.33 ?  161  THR B CG2 1 
ATOM   5993  N N   . ALA B  2  162 ? -39.824 -21.190 98.015  1.00 149.08 ?  162  ALA B N   1 
ATOM   5994  C CA  . ALA B  2  162 ? -41.162 -21.613 97.623  1.00 147.48 ?  162  ALA B CA  1 
ATOM   5995  C C   . ALA B  2  162 ? -41.505 -21.280 96.177  1.00 142.23 ?  162  ALA B C   1 
ATOM   5996  O O   . ALA B  2  162 ? -42.632 -21.554 95.748  1.00 140.67 ?  162  ALA B O   1 
ATOM   5997  C CB  . ALA B  2  162 ? -42.203 -20.983 98.554  1.00 148.85 ?  162  ALA B CB  1 
ATOM   5998  N N   . VAL B  2  163 ? -40.569 -20.709 95.415  1.00 143.89 ?  163  VAL B N   1 
ATOM   5999  C CA  . VAL B  2  163 ? -40.887 -20.246 94.067  1.00 139.63 ?  163  VAL B CA  1 
ATOM   6000  C C   . VAL B  2  163 ? -41.068 -21.424 93.114  1.00 140.77 ?  163  VAL B C   1 
ATOM   6001  O O   . VAL B  2  163 ? -41.937 -21.395 92.233  1.00 136.14 ?  163  VAL B O   1 
ATOM   6002  C CB  . VAL B  2  163 ? -39.798 -19.273 93.575  1.00 139.84 ?  163  VAL B CB  1 
ATOM   6003  C CG1 . VAL B  2  163 ? -38.412 -19.857 93.809  1.00 146.33 ?  163  VAL B CG1 1 
ATOM   6004  C CG2 . VAL B  2  163 ? -39.994 -18.942 92.105  1.00 135.49 ?  163  VAL B CG2 1 
ATOM   6005  N N   . LEU B  2  164 ? -40.205 -22.439 93.231  1.00 144.06 ?  164  LEU B N   1 
ATOM   6006  C CA  . LEU B  2  164 ? -40.276 -23.740 92.562  1.00 144.25 ?  164  LEU B CA  1 
ATOM   6007  C C   . LEU B  2  164 ? -40.030 -23.623 91.062  1.00 141.66 ?  164  LEU B C   1 
ATOM   6008  O O   . LEU B  2  164 ? -39.944 -24.636 90.361  1.00 140.11 ?  164  LEU B O   1 
ATOM   6009  C CB  . LEU B  2  164 ? -41.619 -24.448 92.830  1.00 142.68 ?  164  LEU B CB  1 
ATOM   6010  C CG  . LEU B  2  164 ? -42.916 -24.204 92.032  1.00 137.79 ?  164  LEU B CG  1 
ATOM   6011  C CD1 . LEU B  2  164 ? -43.019 -24.999 90.722  1.00 135.95 ?  164  LEU B CD1 1 
ATOM   6012  C CD2 . LEU B  2  164 ? -44.136 -24.477 92.908  1.00 138.57 ?  164  LEU B CD2 1 
ATOM   6013  N N   . THR B  2  165 ? -39.872 -22.400 90.569  1.00 140.92 ?  165  THR B N   1 
ATOM   6014  C CA  . THR B  2  165 ? -39.530 -22.174 89.174  1.00 138.19 ?  165  THR B CA  1 
ATOM   6015  C C   . THR B  2  165 ? -38.061 -21.840 88.988  1.00 137.90 ?  165  THR B C   1 
ATOM   6016  O O   . THR B  2  165 ? -37.538 -21.998 87.880  1.00 131.86 ?  165  THR B O   1 
ATOM   6017  C CB  . THR B  2  165 ? -40.393 -21.049 88.587  1.00 133.01 ?  165  THR B CB  1 
ATOM   6018  O OG1 . THR B  2  165 ? -41.701 -21.096 89.172  1.00 129.14 ?  165  THR B OG1 1 
ATOM   6019  C CG2 . THR B  2  165 ? -40.523 -21.205 87.081  1.00 126.29 ?  165  THR B CG2 1 
ATOM   6020  N N   . LEU B  2  166 ? -37.403 -21.386 90.052  1.00 133.90 ?  166  LEU B N   1 
ATOM   6021  C CA  . LEU B  2  166 ? -36.008 -20.975 89.989  1.00 133.64 ?  166  LEU B CA  1 
ATOM   6022  C C   . LEU B  2  166 ? -35.133 -22.113 89.476  1.00 130.64 ?  166  LEU B C   1 
ATOM   6023  O O   . LEU B  2  166 ? -35.199 -23.240 89.974  1.00 135.16 ?  166  LEU B O   1 
ATOM   6024  C CB  . LEU B  2  166 ? -35.561 -20.524 91.380  1.00 138.44 ?  166  LEU B CB  1 
ATOM   6025  C CG  . LEU B  2  166 ? -34.101 -20.303 91.768  1.00 139.47 ?  166  LEU B CG  1 
ATOM   6026  C CD1 . LEU B  2  166 ? -33.334 -19.564 90.698  1.00 135.85 ?  166  LEU B CD1 1 
ATOM   6027  C CD2 . LEU B  2  166 ? -34.052 -19.535 93.073  1.00 142.37 ?  166  LEU B CD2 1 
ATOM   6028  N N   . GLN B  2  167 ? -34.322 -21.810 88.468  1.00 137.30 ?  167  GLN B N   1 
ATOM   6029  C CA  . GLN B  2  167 ? -33.416 -22.774 87.859  1.00 133.13 ?  167  GLN B CA  1 
ATOM   6030  C C   . GLN B  2  167 ? -31.950 -22.424 88.048  1.00 133.20 ?  167  GLN B C   1 
ATOM   6031  O O   . GLN B  2  167 ? -31.133 -23.321 88.268  1.00 133.74 ?  167  GLN B O   1 
ATOM   6032  C CB  . GLN B  2  167 ? -33.719 -22.896 86.357  1.00 124.72 ?  167  GLN B CB  1 
ATOM   6033  C CG  . GLN B  2  167 ? -35.086 -23.475 86.030  1.00 123.80 ?  167  GLN B CG  1 
ATOM   6034  C CD  . GLN B  2  167 ? -35.015 -24.942 85.652  1.00 125.24 ?  167  GLN B CD  1 
ATOM   6035  O OE1 . GLN B  2  167 ? -34.732 -25.797 86.491  1.00 130.45 ?  167  GLN B OE1 1 
ATOM   6036  N NE2 . GLN B  2  167 ? -35.269 -25.242 84.382  1.00 122.60 ?  167  GLN B NE2 1 
ATOM   6037  N N   . VAL B  2  168 ? -31.595 -21.141 87.987  1.00 133.07 ?  168  VAL B N   1 
ATOM   6038  C CA  . VAL B  2  168 ? -30.208 -20.693 88.060  1.00 132.58 ?  168  VAL B CA  1 
ATOM   6039  C C   . VAL B  2  168 ? -30.107 -19.617 89.130  1.00 138.62 ?  168  VAL B C   1 
ATOM   6040  O O   . VAL B  2  168 ? -30.852 -18.631 89.099  1.00 139.50 ?  168  VAL B O   1 
ATOM   6041  C CB  . VAL B  2  168 ? -29.706 -20.153 86.706  1.00 124.37 ?  168  VAL B CB  1 
ATOM   6042  C CG1 . VAL B  2  168 ? -28.234 -19.784 86.795  1.00 124.16 ?  168  VAL B CG1 1 
ATOM   6043  C CG2 . VAL B  2  168 ? -29.941 -21.171 85.596  1.00 118.87 ?  168  VAL B CG2 1 
ATOM   6044  N N   . LEU B  2  169 ? -29.163 -19.789 90.052  1.00 134.18 ?  169  LEU B N   1 
ATOM   6045  C CA  . LEU B  2  169 ? -29.077 -18.974 91.254  1.00 139.51 ?  169  LEU B CA  1 
ATOM   6046  C C   . LEU B  2  169 ? -27.611 -18.734 91.598  1.00 139.09 ?  169  LEU B C   1 
ATOM   6047  O O   . LEU B  2  169 ? -26.791 -19.651 91.503  1.00 137.64 ?  169  LEU B O   1 
ATOM   6048  C CB  . LEU B  2  169 ? -29.841 -19.673 92.392  1.00 143.92 ?  169  LEU B CB  1 
ATOM   6049  C CG  . LEU B  2  169 ? -30.249 -19.004 93.700  1.00 147.87 ?  169  LEU B CG  1 
ATOM   6050  C CD1 . LEU B  2  169 ? -29.031 -18.765 94.526  1.00 148.66 ?  169  LEU B CD1 1 
ATOM   6051  C CD2 . LEU B  2  169 ? -30.978 -17.703 93.440  1.00 147.60 ?  169  LEU B CD2 1 
ATOM   6052  N N   . ASP B  2  170 ? -27.280 -17.497 91.975  1.00 146.32 ?  170  ASP B N   1 
ATOM   6053  C CA  . ASP B  2  170 ? -25.893 -17.119 92.250  1.00 145.19 ?  170  ASP B CA  1 
ATOM   6054  C C   . ASP B  2  170 ? -25.866 -15.922 93.192  1.00 147.44 ?  170  ASP B C   1 
ATOM   6055  O O   . ASP B  2  170 ? -26.339 -14.843 92.823  1.00 146.94 ?  170  ASP B O   1 
ATOM   6056  C CB  . ASP B  2  170 ? -25.159 -16.791 90.941  1.00 139.78 ?  170  ASP B CB  1 
ATOM   6057  C CG  . ASP B  2  170 ? -23.652 -16.666 91.119  1.00 137.98 ?  170  ASP B CG  1 
ATOM   6058  O OD1 . ASP B  2  170 ? -23.127 -17.129 92.154  1.00 140.57 ?  170  ASP B OD1 1 
ATOM   6059  O OD2 . ASP B  2  170 ? -22.993 -16.095 90.224  1.00 133.64 -1 170  ASP B OD2 1 
ATOM   6060  N N   . LEU B  2  171 ? -25.306 -16.101 94.396  1.00 144.10 ?  171  LEU B N   1 
ATOM   6061  C CA  . LEU B  2  171 ? -25.034 -15.004 95.327  1.00 145.18 ?  171  LEU B CA  1 
ATOM   6062  C C   . LEU B  2  171 ? -23.563 -14.939 95.728  1.00 148.14 ?  171  LEU B C   1 
ATOM   6063  O O   . LEU B  2  171 ? -23.234 -14.603 96.868  1.00 151.87 ?  171  LEU B O   1 
ATOM   6064  C CB  . LEU B  2  171 ? -25.870 -15.090 96.603  1.00 148.90 ?  171  LEU B CB  1 
ATOM   6065  C CG  . LEU B  2  171 ? -27.393 -15.058 96.650  1.00 148.22 ?  171  LEU B CG  1 
ATOM   6066  C CD1 . LEU B  2  171 ? -27.995 -14.127 95.598  1.00 145.54 ?  171  LEU B CD1 1 
ATOM   6067  C CD2 . LEU B  2  171 ? -27.957 -16.452 96.582  1.00 150.52 ?  171  LEU B CD2 1 
ATOM   6068  N N   . SER B  2  172 ? -22.656 -15.262 94.812  1.00 153.32 ?  172  SER B N   1 
ATOM   6069  C CA  . SER B  2  172 ? -21.243 -15.252 95.162  1.00 151.68 ?  172  SER B CA  1 
ATOM   6070  C C   . SER B  2  172 ? -20.756 -13.830 95.444  1.00 149.80 ?  172  SER B C   1 
ATOM   6071  O O   . SER B  2  172 ? -21.401 -12.839 95.092  1.00 148.66 ?  172  SER B O   1 
ATOM   6072  C CB  . SER B  2  172 ? -20.406 -15.877 94.048  1.00 149.11 ?  172  SER B CB  1 
ATOM   6073  O OG  . SER B  2  172 ? -19.029 -15.850 94.382  1.00 150.91 ?  172  SER B OG  1 
ATOM   6074  N N   . ASN B  2  173 ? -19.603 -13.745 96.114  1.00 153.06 ?  173  ASN B N   1 
ATOM   6075  C CA  . ASN B  2  173 ? -18.877 -12.484 96.295  1.00 151.84 ?  173  ASN B CA  1 
ATOM   6076  C C   . ASN B  2  173 ? -19.708 -11.445 97.048  1.00 151.58 ?  173  ASN B C   1 
ATOM   6077  O O   . ASN B  2  173 ? -19.651 -10.248 96.757  1.00 148.55 ?  173  ASN B O   1 
ATOM   6078  C CB  . ASN B  2  173 ? -18.407 -11.926 94.948  1.00 146.96 ?  173  ASN B CB  1 
ATOM   6079  C CG  . ASN B  2  173 ? -16.920 -11.617 94.927  1.00 148.18 ?  173  ASN B CG  1 
ATOM   6080  O OD1 . ASN B  2  173 ? -16.359 -11.143 95.915  1.00 151.68 ?  173  ASN B OD1 1 
ATOM   6081  N ND2 . ASN B  2  173 ? -16.278 -11.874 93.793  1.00 145.71 ?  173  ASN B ND2 1 
ATOM   6082  N N   . ASN B  2  174 ? -20.492 -11.900 98.022  1.00 151.81 ?  174  ASN B N   1 
ATOM   6083  C CA  . ASN B  2  174 ? -21.296 -11.002 98.835  1.00 152.08 ?  174  ASN B CA  1 
ATOM   6084  C C   . ASN B  2  174 ? -21.129 -11.375 100.304 1.00 158.29 ?  174  ASN B C   1 
ATOM   6085  O O   . ASN B  2  174 ? -21.174 -12.568 100.649 1.00 161.59 ?  174  ASN B O   1 
ATOM   6086  C CB  . ASN B  2  174 ? -22.769 -11.076 98.430  1.00 149.91 ?  174  ASN B CB  1 
ATOM   6087  C CG  . ASN B  2  174 ? -23.082 -10.292 97.185  1.00 146.73 ?  174  ASN B CG  1 
ATOM   6088  O OD1 . ASN B  2  174 ? -23.285 -9.084  97.239  1.00 143.47 ?  174  ASN B OD1 1 
ATOM   6089  N ND2 . ASN B  2  174 ? -23.146 -10.980 96.053  1.00 147.28 ?  174  ASN B ND2 1 
ATOM   6090  N N   . PRO B  2  175 ? -20.931 -10.404 101.194 1.00 156.88 ?  175  PRO B N   1 
ATOM   6091  C CA  . PRO B  2  175 ? -20.781 -10.716 102.634 1.00 163.16 ?  175  PRO B CA  1 
ATOM   6092  C C   . PRO B  2  175 ? -22.107 -10.970 103.347 1.00 164.63 ?  175  PRO B C   1 
ATOM   6093  O O   . PRO B  2  175 ? -22.582 -10.173 104.166 1.00 166.09 ?  175  PRO B O   1 
ATOM   6094  C CB  . PRO B  2  175 ? -20.056 -9.472  103.161 1.00 164.36 ?  175  PRO B CB  1 
ATOM   6095  C CG  . PRO B  2  175 ? -20.514 -8.371  102.265 1.00 158.65 ?  175  PRO B CG  1 
ATOM   6096  C CD  . PRO B  2  175 ? -20.649 -8.987  100.899 1.00 154.00 ?  175  PRO B CD  1 
ATOM   6097  N N   . LEU B  2  176 ? -22.738 -12.109 103.051 1.00 165.42 ?  176  LEU B N   1 
ATOM   6098  C CA  . LEU B  2  176 ? -23.932 -12.514 103.781 1.00 167.54 ?  176  LEU B CA  1 
ATOM   6099  C C   . LEU B  2  176 ? -23.569 -13.375 104.988 1.00 174.32 ?  176  LEU B C   1 
ATOM   6100  O O   . LEU B  2  176 ? -22.399 -13.614 105.298 1.00 177.49 ?  176  LEU B O   1 
ATOM   6101  C CB  . LEU B  2  176 ? -24.926 -13.277 102.902 1.00 164.26 ?  176  LEU B CB  1 
ATOM   6102  C CG  . LEU B  2  176 ? -25.586 -12.733 101.633 1.00 157.64 ?  176  LEU B CG  1 
ATOM   6103  C CD1 . LEU B  2  176 ? -26.231 -11.374 101.842 1.00 155.48 ?  176  LEU B CD1 1 
ATOM   6104  C CD2 . LEU B  2  176 ? -24.633 -12.690 100.504 1.00 154.33 ?  176  LEU B CD2 1 
ATOM   6105  N N   . THR B  2  177 ? -24.603 -13.851 105.677 1.00 171.76 ?  177  THR B N   1 
ATOM   6106  C CA  . THR B  2  177 ? -24.459 -14.667 106.872 1.00 178.35 ?  177  THR B CA  1 
ATOM   6107  C C   . THR B  2  177 ? -25.578 -15.701 106.901 1.00 179.18 ?  177  THR B C   1 
ATOM   6108  O O   . THR B  2  177 ? -26.536 -15.635 106.126 1.00 174.82 ?  177  THR B O   1 
ATOM   6109  C CB  . THR B  2  177 ? -24.492 -13.808 108.144 1.00 182.00 ?  177  THR B CB  1 
ATOM   6110  O OG1 . THR B  2  177 ? -25.533 -12.829 108.032 1.00 178.62 ?  177  THR B OG1 1 
ATOM   6111  C CG2 . THR B  2  177 ? -23.159 -13.101 108.353 1.00 183.27 ?  177  THR B CG2 1 
ATOM   6112  N N   . GLY B  2  178 ? -25.447 -16.665 107.809 1.00 182.00 ?  178  GLY B N   1 
ATOM   6113  C CA  . GLY B  2  178 ? -26.446 -17.698 107.984 1.00 183.80 ?  178  GLY B CA  1 
ATOM   6114  C C   . GLY B  2  178 ? -26.164 -18.948 107.169 1.00 183.61 ?  178  GLY B C   1 
ATOM   6115  O O   . GLY B  2  178 ? -25.355 -18.966 106.239 1.00 180.83 ?  178  GLY B O   1 
ATOM   6116  N N   . ASP B  2  179 ? -26.867 -20.017 107.531 1.00 184.62 ?  179  ASP B N   1 
ATOM   6117  C CA  . ASP B  2  179 ? -26.698 -21.301 106.870 1.00 185.36 ?  179  ASP B CA  1 
ATOM   6118  C C   . ASP B  2  179 ? -27.479 -21.342 105.559 1.00 179.36 ?  179  ASP B C   1 
ATOM   6119  O O   . ASP B  2  179 ? -28.460 -20.618 105.364 1.00 175.70 ?  179  ASP B O   1 
ATOM   6120  C CB  . ASP B  2  179 ? -27.144 -22.436 107.789 1.00 191.57 ?  179  ASP B CB  1 
ATOM   6121  C CG  . ASP B  2  179 ? -26.422 -22.417 109.117 1.00 197.80 ?  179  ASP B CG  1 
ATOM   6122  O OD1 . ASP B  2  179 ? -25.235 -22.803 109.153 1.00 200.44 ?  179  ASP B OD1 1 
ATOM   6123  O OD2 . ASP B  2  179 ? -27.037 -22.007 110.122 1.00 200.20 -1 179  ASP B OD2 1 
ATOM   6124  N N   . ILE B  2  180 ? -27.024 -22.203 104.652 1.00 178.59 ?  180  ILE B N   1 
ATOM   6125  C CA  . ILE B  2  180 ? -27.603 -22.308 103.314 1.00 173.09 ?  180  ILE B CA  1 
ATOM   6126  C C   . ILE B  2  180 ? -29.005 -22.896 103.432 1.00 173.69 ?  180  ILE B C   1 
ATOM   6127  O O   . ILE B  2  180 ? -29.171 -24.029 103.906 1.00 178.54 ?  180  ILE B O   1 
ATOM   6128  C CB  . ILE B  2  180 ? -26.717 -23.153 102.384 1.00 172.90 ?  180  ILE B CB  1 
ATOM   6129  C CG1 . ILE B  2  180 ? -25.500 -22.347 101.919 1.00 170.32 ?  180  ILE B CG1 1 
ATOM   6130  C CG2 . ILE B  2  180 ? -27.511 -23.643 101.183 1.00 168.96 ?  180  ILE B CG2 1 
ATOM   6131  C CD1 . ILE B  2  180 ? -24.331 -22.365 102.884 1.00 175.44 ?  180  ILE B CD1 1 
ATOM   6132  N N   . PRO B  2  181 ? -30.036 -22.163 103.016 1.00 172.76 ?  181  PRO B N   1 
ATOM   6133  C CA  . PRO B  2  181 ? -31.445 -22.581 103.196 1.00 173.30 ?  181  PRO B CA  1 
ATOM   6134  C C   . PRO B  2  181 ? -31.969 -23.566 102.152 1.00 171.68 ?  181  PRO B C   1 
ATOM   6135  O O   . PRO B  2  181 ? -32.633 -23.216 101.177 1.00 167.09 ?  181  PRO B O   1 
ATOM   6136  C CB  . PRO B  2  181 ? -32.193 -21.248 103.133 1.00 168.91 ?  181  PRO B CB  1 
ATOM   6137  C CG  . PRO B  2  181 ? -31.372 -20.419 102.203 1.00 165.00 ?  181  PRO B CG  1 
ATOM   6138  C CD  . PRO B  2  181 ? -29.932 -20.829 102.398 1.00 167.02 ?  181  PRO B CD  1 
ATOM   6139  N N   . VAL B  2  182 ? -31.669 -24.849 102.349 1.00 172.74 ?  182  VAL B N   1 
ATOM   6140  C CA  . VAL B  2  182 ? -32.232 -25.907 101.508 1.00 172.36 ?  182  VAL B CA  1 
ATOM   6141  C C   . VAL B  2  182 ? -33.550 -26.310 102.164 1.00 174.95 ?  182  VAL B C   1 
ATOM   6142  O O   . VAL B  2  182 ? -33.619 -27.245 102.964 1.00 180.79 ?  182  VAL B O   1 
ATOM   6143  C CB  . VAL B  2  182 ? -31.273 -27.084 101.349 1.00 176.34 ?  182  VAL B CB  1 
ATOM   6144  C CG1 . VAL B  2  182 ? -31.905 -28.186 100.510 1.00 176.37 ?  182  VAL B CG1 1 
ATOM   6145  C CG2 . VAL B  2  182 ? -29.968 -26.617 100.727 1.00 173.82 ?  182  VAL B CG2 1 
ATOM   6146  N N   . ASN B  2  183 ? -34.613 -25.579 101.827 1.00 170.68 ?  183  ASN B N   1 
ATOM   6147  C CA  . ASN B  2  183 ? -35.963 -25.867 102.297 1.00 172.38 ?  183  ASN B CA  1 
ATOM   6148  C C   . ASN B  2  183 ? -36.807 -26.568 101.241 1.00 170.17 ?  183  ASN B C   1 
ATOM   6149  O O   . ASN B  2  183 ? -37.992 -26.823 101.479 1.00 171.17 ?  183  ASN B O   1 
ATOM   6150  C CB  . ASN B  2  183 ? -36.654 -24.571 102.750 1.00 169.79 ?  183  ASN B CB  1 
ATOM   6151  C CG  . ASN B  2  183 ? -37.663 -24.798 103.866 1.00 174.06 ?  183  ASN B CG  1 
ATOM   6152  O OD1 . ASN B  2  183 ? -38.773 -24.264 103.834 1.00 171.86 ?  183  ASN B OD1 1 
ATOM   6153  N ND2 . ASN B  2  183 ? -37.279 -25.590 104.859 1.00 180.35 ?  183  ASN B ND2 1 
ATOM   6154  N N   . GLY B  2  184 ? -36.224 -26.878 100.086 1.00 169.07 ?  184  GLY B N   1 
ATOM   6155  C CA  . GLY B  2  184 ? -36.915 -27.556 99.008  1.00 167.06 ?  184  GLY B CA  1 
ATOM   6156  C C   . GLY B  2  184 ? -37.128 -26.643 97.820  1.00 159.94 ?  184  GLY B C   1 
ATOM   6157  O O   . GLY B  2  184 ? -38.064 -25.840 97.816  1.00 156.94 ?  184  GLY B O   1 
ATOM   6158  N N   . SER B  2  185 ? -36.273 -26.822 96.805  1.00 163.97 ?  185  SER B N   1 
ATOM   6159  C CA  . SER B  2  185 ? -36.065 -26.014 95.599  1.00 159.45 ?  185  SER B CA  1 
ATOM   6160  C C   . SER B  2  185 ? -34.578 -25.693 95.538  1.00 159.66 ?  185  SER B C   1 
ATOM   6161  O O   . SER B  2  185 ? -33.946 -25.805 94.484  1.00 156.93 ?  185  SER B O   1 
ATOM   6162  C CB  . SER B  2  185 ? -36.878 -24.715 95.560  1.00 158.30 ?  185  SER B CB  1 
ATOM   6163  O OG  . SER B  2  185 ? -38.208 -24.956 95.130  1.00 156.29 ?  185  SER B OG  1 
ATOM   6164  N N   . PHE B  2  186 ? -34.019 -25.299 96.683  1.00 158.92 ?  186  PHE B N   1 
ATOM   6165  C CA  . PHE B  2  186 ? -32.583 -25.119 96.850  1.00 158.66 ?  186  PHE B CA  1 
ATOM   6166  C C   . PHE B  2  186 ? -31.846 -26.443 96.973  1.00 159.42 ?  186  PHE B C   1 
ATOM   6167  O O   . PHE B  2  186 ? -30.618 -26.440 97.108  1.00 160.00 ?  186  PHE B O   1 
ATOM   6168  C CB  . PHE B  2  186 ? -32.291 -24.256 98.083  1.00 159.44 ?  186  PHE B CB  1 
ATOM   6169  C CG  . PHE B  2  186 ? -32.635 -22.798 97.911  1.00 159.03 ?  186  PHE B CG  1 
ATOM   6170  C CD1 . PHE B  2  186 ? -33.918 -22.406 97.568  1.00 159.18 ?  186  PHE B CD1 1 
ATOM   6171  C CD2 . PHE B  2  186 ? -31.675 -21.819 98.113  1.00 158.95 ?  186  PHE B CD2 1 
ATOM   6172  C CE1 . PHE B  2  186 ? -34.234 -21.072 97.414  1.00 159.36 ?  186  PHE B CE1 1 
ATOM   6173  C CE2 . PHE B  2  186 ? -31.988 -20.480 97.963  1.00 159.14 ?  186  PHE B CE2 1 
ATOM   6174  C CZ  . PHE B  2  186 ? -33.271 -20.108 97.614  1.00 159.40 ?  186  PHE B CZ  1 
ATOM   6175  N N   . SER B  2  187 ? -32.569 -27.565 96.943  1.00 159.74 ?  187  SER B N   1 
ATOM   6176  C CA  . SER B  2  187 ? -31.950 -28.881 97.023  1.00 162.02 ?  187  SER B CA  1 
ATOM   6177  C C   . SER B  2  187 ? -31.140 -29.214 95.780  1.00 161.73 ?  187  SER B C   1 
ATOM   6178  O O   . SER B  2  187 ? -30.221 -30.037 95.852  1.00 163.77 ?  187  SER B O   1 
ATOM   6179  C CB  . SER B  2  187 ? -33.024 -29.947 97.243  1.00 163.28 ?  187  SER B CB  1 
ATOM   6180  O OG  . SER B  2  187 ? -34.056 -29.830 96.277  1.00 161.50 ?  187  SER B OG  1 
ATOM   6181  N N   . LEU B  2  188 ? -31.464 -28.597 94.648  1.00 158.54 ?  188  LEU B N   1 
ATOM   6182  C CA  . LEU B  2  188 ? -30.832 -28.903 93.376  1.00 158.43 ?  188  LEU B CA  1 
ATOM   6183  C C   . LEU B  2  188 ? -29.573 -28.085 93.121  1.00 158.05 ?  188  LEU B C   1 
ATOM   6184  O O   . LEU B  2  188 ? -28.861 -28.365 92.151  1.00 158.50 ?  188  LEU B O   1 
ATOM   6185  C CB  . LEU B  2  188 ? -31.823 -28.678 92.224  1.00 156.49 ?  188  LEU B CB  1 
ATOM   6186  C CG  . LEU B  2  188 ? -33.171 -29.412 92.216  1.00 156.72 ?  188  LEU B CG  1 
ATOM   6187  C CD1 . LEU B  2  188 ? -34.204 -28.749 93.120  1.00 155.71 ?  188  LEU B CD1 1 
ATOM   6188  C CD2 . LEU B  2  188 ? -33.703 -29.516 90.795  1.00 155.64 ?  188  LEU B CD2 1 
ATOM   6189  N N   . PHE B  2  189 ? -29.280 -27.093 93.955  1.00 156.36 ?  189  PHE B N   1 
ATOM   6190  C CA  . PHE B  2  189 ? -28.199 -26.161 93.677  1.00 155.92 ?  189  PHE B CA  1 
ATOM   6191  C C   . PHE B  2  189 ? -26.887 -26.610 94.321  1.00 158.32 ?  189  PHE B C   1 
ATOM   6192  O O   . PHE B  2  189 ? -26.860 -27.392 95.274  1.00 160.17 ?  189  PHE B O   1 
ATOM   6193  C CB  . PHE B  2  189 ? -28.582 -24.754 94.134  1.00 154.29 ?  189  PHE B CB  1 
ATOM   6194  C CG  . PHE B  2  189 ? -29.726 -24.163 93.354  1.00 151.95 ?  189  PHE B CG  1 
ATOM   6195  C CD1 . PHE B  2  189 ? -31.039 -24.454 93.688  1.00 152.04 ?  189  PHE B CD1 1 
ATOM   6196  C CD2 . PHE B  2  189 ? -29.488 -23.345 92.263  1.00 151.00 ?  189  PHE B CD2 1 
ATOM   6197  C CE1 . PHE B  2  189 ? -32.091 -23.921 92.964  1.00 151.36 ?  189  PHE B CE1 1 
ATOM   6198  C CE2 . PHE B  2  189 ? -30.538 -22.817 91.531  1.00 150.38 ?  189  PHE B CE2 1 
ATOM   6199  C CZ  . PHE B  2  189 ? -31.840 -23.102 91.886  1.00 150.54 ?  189  PHE B CZ  1 
ATOM   6200  N N   . THR B  2  190 ? -25.790 -26.084 93.777  1.00 162.98 ?  190  THR B N   1 
ATOM   6201  C CA  . THR B  2  190 ? -24.402 -26.485 93.944  1.00 165.06 ?  190  THR B CA  1 
ATOM   6202  C C   . THR B  2  190 ? -23.607 -25.355 94.603  1.00 165.17 ?  190  THR B C   1 
ATOM   6203  O O   . THR B  2  190 ? -23.959 -24.182 94.441  1.00 163.34 ?  190  THR B O   1 
ATOM   6204  C CB  . THR B  2  190 ? -23.829 -26.835 92.555  1.00 165.40 ?  190  THR B CB  1 
ATOM   6205  O OG1 . THR B  2  190 ? -24.552 -27.949 92.014  1.00 166.16 ?  190  THR B OG1 1 
ATOM   6206  C CG2 . THR B  2  190 ? -22.344 -27.178 92.574  1.00 167.90 ?  190  THR B CG2 1 
ATOM   6207  N N   . PRO B  2  191 ? -22.535 -25.674 95.377  1.00 162.79 ?  191  PRO B N   1 
ATOM   6208  C CA  . PRO B  2  191 ? -21.804 -24.627 96.114  1.00 163.26 ?  191  PRO B CA  1 
ATOM   6209  C C   . PRO B  2  191 ? -21.318 -23.426 95.309  1.00 162.10 ?  191  PRO B C   1 
ATOM   6210  O O   . PRO B  2  191 ? -21.012 -22.390 95.909  1.00 162.19 ?  191  PRO B O   1 
ATOM   6211  C CB  . PRO B  2  191 ? -20.612 -25.396 96.712  1.00 166.24 ?  191  PRO B CB  1 
ATOM   6212  C CG  . PRO B  2  191 ? -20.677 -26.796 96.122  1.00 167.28 ?  191  PRO B CG  1 
ATOM   6213  C CD  . PRO B  2  191 ? -22.127 -27.006 95.850  1.00 165.32 ?  191  PRO B CD  1 
ATOM   6214  N N   . ILE B  2  192 ? -21.225 -23.526 93.978  1.00 161.10 ?  192  ILE B N   1 
ATOM   6215  C CA  . ILE B  2  192 ? -20.840 -22.352 93.194  1.00 160.10 ?  192  ILE B CA  1 
ATOM   6216  C C   . ILE B  2  192 ? -21.902 -21.263 93.308  1.00 157.76 ?  192  ILE B C   1 
ATOM   6217  O O   . ILE B  2  192 ? -21.602 -20.069 93.176  1.00 157.31 ?  192  ILE B O   1 
ATOM   6218  C CB  . ILE B  2  192 ? -20.579 -22.750 91.725  1.00 160.03 ?  192  ILE B CB  1 
ATOM   6219  C CG1 . ILE B  2  192 ? -19.488 -23.818 91.648  1.00 162.81 ?  192  ILE B CG1 1 
ATOM   6220  C CG2 . ILE B  2  192 ? -20.173 -21.540 90.890  1.00 159.23 ?  192  ILE B CG2 1 
ATOM   6221  C CD1 . ILE B  2  192 ? -19.101 -24.192 90.234  1.00 163.39 ?  192  ILE B CD1 1 
ATOM   6222  N N   . SER B  2  193 ? -23.151 -21.649 93.585  1.00 156.83 ?  193  SER B N   1 
ATOM   6223  C CA  . SER B  2  193 ? -24.208 -20.669 93.812  1.00 154.96 ?  193  SER B CA  1 
ATOM   6224  C C   . SER B  2  193 ? -23.991 -19.878 95.099  1.00 155.95 ?  193  SER B C   1 
ATOM   6225  O O   . SER B  2  193 ? -24.474 -18.746 95.216  1.00 154.97 ?  193  SER B O   1 
ATOM   6226  C CB  . SER B  2  193 ? -25.567 -21.369 93.851  1.00 153.84 ?  193  SER B CB  1 
ATOM   6227  O OG  . SER B  2  193 ? -25.822 -22.056 92.638  1.00 153.10 ?  193  SER B OG  1 
ATOM   6228  N N   . PHE B  2  194 ? -23.274 -20.453 96.071  1.00 160.65 ?  194  PHE B N   1 
ATOM   6229  C CA  . PHE B  2  194 ? -23.074 -19.835 97.379  1.00 162.04 ?  194  PHE B CA  1 
ATOM   6230  C C   . PHE B  2  194 ? -21.597 -19.614 97.703  1.00 164.21 ?  194  PHE B C   1 
ATOM   6231  O O   . PHE B  2  194 ? -21.242 -19.474 98.878  1.00 166.06 ?  194  PHE B O   1 
ATOM   6232  C CB  . PHE B  2  194 ? -23.721 -20.681 98.482  1.00 163.02 ?  194  PHE B CB  1 
ATOM   6233  C CG  . PHE B  2  194 ? -25.206 -20.887 98.314  1.00 161.30 ?  194  PHE B CG  1 
ATOM   6234  C CD1 . PHE B  2  194 ? -25.693 -21.938 97.552  1.00 160.53 ?  194  PHE B CD1 1 
ATOM   6235  C CD2 . PHE B  2  194 ? -26.115 -20.043 98.936  1.00 161.68 ?  194  PHE B CD2 1 
ATOM   6236  C CE1 . PHE B  2  194 ? -27.055 -22.135 97.403  1.00 159.93 ?  194  PHE B CE1 1 
ATOM   6237  C CE2 . PHE B  2  194 ? -27.479 -20.235 98.791  1.00 161.16 ?  194  PHE B CE2 1 
ATOM   6238  C CZ  . PHE B  2  194 ? -27.949 -21.283 98.023  1.00 160.17 ?  194  PHE B CZ  1 
ATOM   6239  N N   . ALA B  2  195 ? -20.727 -19.574 96.697  1.00 162.15 ?  195  ALA B N   1 
ATOM   6240  C CA  . ALA B  2  195 ? -19.295 -19.467 96.951  1.00 164.47 ?  195  ALA B CA  1 
ATOM   6241  C C   . ALA B  2  195 ? -18.905 -18.053 97.378  1.00 165.05 ?  195  ALA B C   1 
ATOM   6242  O O   . ALA B  2  195 ? -19.497 -17.062 96.942  1.00 163.47 ?  195  ALA B O   1 
ATOM   6243  C CB  . ALA B  2  195 ? -18.503 -19.873 95.709  1.00 164.69 ?  195  ALA B CB  1 
ATOM   6244  N N   . ASN B  2  196 ? -17.893 -17.972 98.250  1.00 163.47 ?  196  ASN B N   1 
ATOM   6245  C CA  . ASN B  2  196 ? -17.318 -16.699 98.702  1.00 164.76 ?  196  ASN B CA  1 
ATOM   6246  C C   . ASN B  2  196 ? -18.352 -15.828 99.410  1.00 164.06 ?  196  ASN B C   1 
ATOM   6247  O O   . ASN B  2  196 ? -18.235 -14.600 99.446  1.00 164.44 ?  196  ASN B O   1 
ATOM   6248  C CB  . ASN B  2  196 ? -16.670 -15.931 97.546  1.00 164.44 ?  196  ASN B CB  1 
ATOM   6249  C CG  . ASN B  2  196 ? -15.563 -15.005 98.011  1.00 166.91 ?  196  ASN B CG  1 
ATOM   6250  O OD1 . ASN B  2  196 ? -14.857 -15.299 98.975  1.00 169.27 ?  196  ASN B OD1 1 
ATOM   6251  N ND2 . ASN B  2  196 ? -15.410 -13.877 97.328  1.00 166.58 ?  196  ASN B ND2 1 
ATOM   6252  N N   . THR B  2  197 ? -19.373 -16.463 99.978  1.00 170.99 ?  197  THR B N   1 
ATOM   6253  C CA  . THR B  2  197 ? -20.507 -15.767 100.562 1.00 170.33 ?  197  THR B CA  1 
ATOM   6254  C C   . THR B  2  197 ? -20.386 -15.583 102.070 1.00 172.92 ?  197  THR B C   1 
ATOM   6255  O O   . THR B  2  197 ? -21.183 -14.840 102.655 1.00 173.09 ?  197  THR B O   1 
ATOM   6256  C CB  . THR B  2  197 ? -21.792 -16.536 100.223 1.00 168.13 ?  197  THR B CB  1 
ATOM   6257  O OG1 . THR B  2  197 ? -21.734 -16.962 98.857  1.00 166.26 ?  197  THR B OG1 1 
ATOM   6258  C CG2 . THR B  2  197 ? -23.007 -15.670 100.389 1.00 166.98 ?  197  THR B CG2 1 
ATOM   6259  N N   . LYS B  2  198 ? -19.396 -16.216 102.704 1.00 172.31 ?  198  LYS B N   1 
ATOM   6260  C CA  . LYS B  2  198 ? -19.212 -16.155 104.155 1.00 175.10 ?  198  LYS B CA  1 
ATOM   6261  C C   . LYS B  2  198 ? -20.459 -16.629 104.899 1.00 174.85 ?  198  LYS B C   1 
ATOM   6262  O O   . LYS B  2  198 ? -20.738 -16.185 106.016 1.00 176.81 ?  198  LYS B O   1 
ATOM   6263  C CB  . LYS B  2  198 ? -18.812 -14.746 104.610 1.00 176.82 ?  198  LYS B CB  1 
ATOM   6264  C CG  . LYS B  2  198 ? -17.699 -14.122 103.780 1.00 177.05 ?  198  LYS B CG  1 
ATOM   6265  C CD  . LYS B  2  198 ? -17.542 -12.639 104.079 1.00 178.50 ?  198  LYS B CD  1 
ATOM   6266  C CE  . LYS B  2  198 ? -16.582 -11.982 103.099 1.00 178.52 ?  198  LYS B CE  1 
ATOM   6267  N NZ  . LYS B  2  198 ? -16.436 -10.522 103.349 1.00 180.18 ?  198  LYS B NZ  1 
ATOM   6268  N N   . LEU B  2  199 ? -21.223 -17.532 104.276 1.00 177.85 ?  199  LEU B N   1 
ATOM   6269  C CA  . LEU B  2  199 ? -22.441 -18.040 104.899 1.00 177.67 ?  199  LEU B CA  1 
ATOM   6270  C C   . LEU B  2  199 ? -22.120 -18.953 106.076 1.00 180.37 ?  199  LEU B C   1 
ATOM   6271  O O   . LEU B  2  199 ? -22.658 -18.780 107.176 1.00 182.09 ?  199  LEU B O   1 
ATOM   6272  C CB  . LEU B  2  199 ? -23.290 -18.777 103.862 1.00 174.90 ?  199  LEU B CB  1 
ATOM   6273  C CG  . LEU B  2  199 ? -24.091 -17.908 102.892 1.00 172.24 ?  199  LEU B CG  1 
ATOM   6274  C CD1 . LEU B  2  199 ? -24.998 -18.759 102.022 1.00 169.94 ?  199  LEU B CD1 1 
ATOM   6275  C CD2 . LEU B  2  199 ? -24.896 -16.856 103.633 1.00 172.83 ?  199  LEU B CD2 1 
ATOM   6276  N N   . THR B  2  200 ? -21.244 -19.929 105.865 1.00 178.45 ?  200  THR B N   1 
ATOM   6277  C CA  . THR B  2  200 ? -20.890 -20.878 106.912 1.00 181.13 ?  200  THR B CA  1 
ATOM   6278  C C   . THR B  2  200 ? -19.386 -21.113 106.941 1.00 183.00 ?  200  THR B C   1 
ATOM   6279  O O   . THR B  2  200 ? -18.602 -20.166 106.902 1.00 183.66 ?  200  THR B O   1 
ATOM   6280  C CB  . THR B  2  200 ? -21.611 -22.225 106.721 1.00 180.44 ?  200  THR B CB  1 
ATOM   6281  O OG1 . THR B  2  200 ? -23.027 -22.011 106.680 1.00 178.84 ?  200  THR B OG1 1 
ATOM   6282  C CG2 . THR B  2  200 ? -21.279 -23.170 107.864 1.00 183.51 ?  200  THR B CG2 1 
ATOM   6283  N N   . PRO C  3  1   ? -42.472 30.154  96.978  1.00 78.09  ?  1    PRO C N   1 
ATOM   6284  C CA  . PRO C  3  1   ? -43.619 31.030  96.709  1.00 77.29  ?  1    PRO C CA  1 
ATOM   6285  C C   . PRO C  3  1   ? -44.853 30.257  96.250  1.00 79.64  ?  1    PRO C C   1 
ATOM   6286  O O   . PRO C  3  1   ? -44.729 29.321  95.460  1.00 78.64  ?  1    PRO C O   1 
ATOM   6287  C CB  . PRO C  3  1   ? -43.107 31.947  95.597  1.00 73.93  ?  1    PRO C CB  1 
ATOM   6288  C CG  . PRO C  3  1   ? -42.035 31.145  94.897  1.00 73.75  ?  1    PRO C CG  1 
ATOM   6289  C CD  . PRO C  3  1   ? -41.562 30.050  95.824  1.00 76.48  ?  1    PRO C CD  1 
ATOM   6290  N N   . VAL C  3  2   ? -46.024 30.650  96.754  1.00 74.88  ?  2    VAL C N   1 
ATOM   6291  C CA  . VAL C  3  2   ? -47.269 29.979  96.397  1.00 73.99  ?  2    VAL C CA  1 
ATOM   6292  C C   . VAL C  3  2   ? -47.576 30.230  94.927  1.00 70.91  ?  2    VAL C C   1 
ATOM   6293  O O   . VAL C  3  2   ? -47.616 31.380  94.472  1.00 69.37  ?  2    VAL C O   1 
ATOM   6294  C CB  . VAL C  3  2   ? -48.415 30.459  97.299  1.00 74.91  ?  2    VAL C CB  1 
ATOM   6295  C CG1 . VAL C  3  2   ? -49.759 30.126  96.673  1.00 73.48  ?  2    VAL C CG1 1 
ATOM   6296  C CG2 . VAL C  3  2   ? -48.294 29.843  98.681  1.00 78.29  ?  2    VAL C CG2 1 
ATOM   6297  N N   . ARG C  3  3   ? -47.775 29.153  94.173  1.00 73.84  ?  3    ARG C N   1 
ATOM   6298  C CA  . ARG C  3  3   ? -48.070 29.230  92.750  1.00 71.70  ?  3    ARG C CA  1 
ATOM   6299  C C   . ARG C  3  3   ? -49.362 28.483  92.447  1.00 69.49  ?  3    ARG C C   1 
ATOM   6300  O O   . ARG C  3  3   ? -49.879 27.726  93.271  1.00 70.96  ?  3    ARG C O   1 
ATOM   6301  C CB  . ARG C  3  3   ? -46.921 28.649  91.912  1.00 71.69  ?  3    ARG C CB  1 
ATOM   6302  C CG  . ARG C  3  3   ? -45.534 28.865  92.495  1.00 71.41  ?  3    ARG C CG  1 
ATOM   6303  C CD  . ARG C  3  3   ? -44.525 27.896  91.904  1.00 69.55  ?  3    ARG C CD  1 
ATOM   6304  N NE  . ARG C  3  3   ? -43.439 27.604  92.833  1.00 70.74  ?  3    ARG C NE  1 
ATOM   6305  C CZ  . ARG C  3  3   ? -43.439 26.596  93.697  1.00 73.10  ?  3    ARG C CZ  1 
ATOM   6306  N NH1 . ARG C  3  3   ? -44.459 25.755  93.780  1.00 73.46  ?  3    ARG C NH1 1 
ATOM   6307  N NH2 . ARG C  3  3   ? -42.385 26.423  94.494  1.00 75.41  ?  3    ARG C NH2 1 
ATOM   6308  N N   . SER C  3  4   ? -49.882 28.705  91.245  1.00 66.01  ?  4    SER C N   1 
ATOM   6309  C CA  . SER C  3  4   ? -51.038 27.970  90.753  1.00 65.11  ?  4    SER C CA  1 
ATOM   6310  C C   . SER C  3  4   ? -50.598 26.752  89.945  1.00 64.98  ?  4    SER C C   1 
ATOM   6311  O O   . SER C  3  4   ? -49.515 26.731  89.353  1.00 67.27  ?  4    SER C O   1 
ATOM   6312  C CB  . SER C  3  4   ? -51.921 28.866  89.888  1.00 63.21  ?  4    SER C CB  1 
ATOM   6313  O OG  . SER C  3  4   ? -51.401 28.944  88.573  1.00 61.40  ?  4    SER C OG  1 
ATOM   6314  N N   . SER C  3  5   ? -51.456 25.738  89.915  1.00 66.00  ?  5    SER C N   1 
ATOM   6315  C CA  . SER C  3  5   ? -51.124 24.521  89.190  1.00 66.15  ?  5    SER C CA  1 
ATOM   6316  C C   . SER C  3  5   ? -51.196 24.755  87.685  1.00 63.84  ?  5    SER C C   1 
ATOM   6317  O O   . SER C  3  5   ? -52.007 25.543  87.192  1.00 62.65  ?  5    SER C O   1 
ATOM   6318  C CB  . SER C  3  5   ? -52.061 23.382  89.597  1.00 68.28  ?  5    SER C CB  1 
ATOM   6319  O OG  . SER C  3  5   ? -53.417 23.734  89.397  1.00 68.03  ?  5    SER C OG  1 
ATOM   6320  N N   . GLN C  3  6   ? -50.323 24.063  86.956  1.00 71.10  ?  6    GLN C N   1 
ATOM   6321  C CA  . GLN C  3  6   ? -50.236 24.159  85.504  1.00 71.07  ?  6    GLN C CA  1 
ATOM   6322  C C   . GLN C  3  6   ? -50.706 22.851  84.884  1.00 71.29  ?  6    GLN C C   1 
ATOM   6323  O O   . GLN C  3  6   ? -50.282 21.770  85.308  1.00 70.61  ?  6    GLN C O   1 
ATOM   6324  C CB  . GLN C  3  6   ? -48.805 24.470  85.060  1.00 72.26  ?  6    GLN C CB  1 
ATOM   6325  C CG  . GLN C  3  6   ? -48.284 25.817  85.542  1.00 70.79  ?  6    GLN C CG  1 
ATOM   6326  C CD  . GLN C  3  6   ? -48.591 26.950  84.567  1.00 67.55  ?  6    GLN C CD  1 
ATOM   6327  O OE1 . GLN C  3  6   ? -48.830 28.092  84.974  1.00 65.92  ?  6    GLN C OE1 1 
ATOM   6328  N NE2 . GLN C  3  6   ? -48.584 26.638  83.273  1.00 66.69  ?  6    GLN C NE2 1 
ATOM   6329  N N   . SER C  3  7   ? -51.575 22.948  83.880  1.00 68.41  ?  7    SER C N   1 
ATOM   6330  C CA  . SER C  3  7   ? -52.067 21.749  83.213  1.00 68.03  ?  7    SER C CA  1 
ATOM   6331  C C   . SER C  3  7   ? -50.963 21.124  82.369  1.00 71.99  ?  7    SER C C   1 
ATOM   6332  O O   . SER C  3  7   ? -50.268 21.816  81.618  1.00 73.64  ?  7    SER C O   1 
ATOM   6333  C CB  . SER C  3  7   ? -53.285 22.066  82.344  1.00 65.02  ?  7    SER C CB  1 
ATOM   6334  O OG  . SER C  3  7   ? -54.057 20.893  82.109  1.00 64.51  ?  7    SER C OG  1 
ATOM   6335  N N   . SER C  3  8   ? -50.806 19.811  82.497  1.00 66.29  ?  8    SER C N   1 
ATOM   6336  C CA  . SER C  3  8   ? -49.809 19.073  81.742  1.00 68.13  ?  8    SER C CA  1 
ATOM   6337  C C   . SER C  3  8   ? -50.367 18.660  80.388  1.00 70.54  ?  8    SER C C   1 
ATOM   6338  O O   . SER C  3  8   ? -51.558 18.370  80.245  1.00 69.00  ?  8    SER C O   1 
ATOM   6339  C CB  . SER C  3  8   ? -49.349 17.836  82.511  1.00 66.57  ?  8    SER C CB  1 
ATOM   6340  O OG  . SER C  3  8   ? -48.040 17.465  82.123  1.00 65.97  ?  8    SER C OG  1 
ATOM   6341  N N   . GLN C  3  9   ? -49.491 18.649  79.389  1.00 66.07  ?  9    GLN C N   1 
ATOM   6342  C CA  . GLN C  3  9   ? -49.908 18.349  78.029  1.00 68.31  ?  9    GLN C CA  1 
ATOM   6343  C C   . GLN C  3  9   ? -50.268 16.874  77.875  1.00 68.87  ?  9    GLN C C   1 
ATOM   6344  O O   . GLN C  3  9   ? -49.784 16.006  78.608  1.00 67.49  ?  9    GLN C O   1 
ATOM   6345  C CB  . GLN C  3  9   ? -48.802 18.721  77.044  1.00 68.37  ?  9    GLN C CB  1 
ATOM   6346  C CG  . GLN C  3  9   ? -49.317 19.146  75.684  1.00 70.68  ?  9    GLN C CG  1 
ATOM   6347  C CD  . GLN C  3  9   ? -48.336 20.020  74.927  1.00 65.48  ?  9    GLN C CD  1 
ATOM   6348  O OE1 . GLN C  3  9   ? -48.466 21.248  74.892  1.00 62.01  ?  9    GLN C OE1 1 
ATOM   6349  N NE2 . GLN C  3  9   ? -47.342 19.387  74.311  1.00 63.43  ?  9    GLN C NE2 1 
ATOM   6350  N N   . ALA C  3  10  ? -51.126 16.597  76.900  1.00 64.33  ?  10   ALA C N   1 
ATOM   6351  C CA  . ALA C  3  10  ? -51.537 15.231  76.630  1.00 65.35  ?  10   ALA C CA  1 
ATOM   6352  C C   . ALA C  3  10  ? -50.377 14.426  76.055  1.00 65.88  ?  10   ALA C C   1 
ATOM   6353  O O   . ALA C  3  10  ? -49.449 14.964  75.441  1.00 64.96  ?  10   ALA C O   1 
ATOM   6354  C CB  . ALA C  3  10  ? -52.723 15.210  75.666  1.00 66.45  ?  10   ALA C CB  1 
ATOM   6355  N N   . GLY C  3  11  ? -50.444 13.113  76.250  1.00 68.11  ?  11   GLY C N   1 
ATOM   6356  C CA  . GLY C  3  11  ? -49.405 12.246  75.729  1.00 68.48  ?  11   GLY C CA  1 
ATOM   6357  C C   . GLY C  3  11  ? -49.435 12.194  74.211  1.00 72.21  ?  11   GLY C C   1 
ATOM   6358  O O   . GLY C  3  11  ? -50.496 12.110  73.589  1.00 74.28  ?  11   GLY C O   1 
ATOM   6359  N N   . GLY C  3  12  ? -48.247 12.254  73.611  1.00 68.38  ?  12   GLY C N   1 
ATOM   6360  C CA  . GLY C  3  12  ? -48.115 12.167  72.170  1.00 70.95  ?  12   GLY C CA  1 
ATOM   6361  C C   . GLY C  3  12  ? -47.591 10.827  71.697  1.00 71.24  ?  12   GLY C C   1 
ATOM   6362  O O   . GLY C  3  12  ? -47.003 10.069  72.475  1.00 68.22  ?  12   GLY C O   1 
ATOM   6363  N N   . ARG C  3  13  ? -47.802 10.520  70.423  1.00 74.97  ?  13   ARG C N   1 
ATOM   6364  C CA  . ARG C  3  13  ? -47.310 9.274   69.854  1.00 74.95  ?  13   ARG C CA  1 
ATOM   6365  C C   . ARG C  3  13  ? -46.124 9.526   68.927  1.00 70.52  ?  13   ARG C C   1 
ATOM   6366  O O   . ARG C  3  13  ? -45.111 8.826   68.993  1.00 65.38  ?  13   ARG C O   1 
ATOM   6367  C CB  . ARG C  3  13  ? -48.427 8.549   69.101  1.00 79.88  ?  13   ARG C CB  1 
ATOM   6368  C CG  . ARG C  3  13  ? -47.984 7.248   68.456  1.00 78.73  ?  13   ARG C CG  1 
ATOM   6369  C CD  . ARG C  3  13  ? -48.560 6.040   69.180  1.00 76.21  ?  13   ARG C CD  1 
ATOM   6370  N NE  . ARG C  3  13  ? -48.399 4.813   68.407  1.00 76.13  ?  13   ARG C NE  1 
ATOM   6371  C CZ  . ARG C  3  13  ? -49.378 4.211   67.741  1.00 77.26  ?  13   ARG C CZ  1 
ATOM   6372  N NH1 . ARG C  3  13  ? -50.611 4.692   67.740  1.00 78.10  ?  13   ARG C NH1 1 
ATOM   6373  N NH2 . ARG C  3  13  ? -49.112 3.102   67.057  1.00 77.27  ?  13   ARG C NH2 1 
ATOM   6374  N N   . THR D  1  47  ? -39.046 -32.597 33.058  1.00 55.07  ?  47   THR D N   1 
ATOM   6375  C CA  . THR D  1  47  ? -40.247 -32.627 33.881  1.00 56.78  ?  47   THR D CA  1 
ATOM   6376  C C   . THR D  1  47  ? -41.278 -31.653 33.330  1.00 58.83  ?  47   THR D C   1 
ATOM   6377  O O   . THR D  1  47  ? -41.004 -30.916 32.382  1.00 58.80  ?  47   THR D O   1 
ATOM   6378  C CB  . THR D  1  47  ? -39.950 -32.279 35.366  1.00 55.30  ?  47   THR D CB  1 
ATOM   6379  O OG1 . THR D  1  47  ? -39.862 -30.859 35.530  1.00 54.36  ?  47   THR D OG1 1 
ATOM   6380  C CG2 . THR D  1  47  ? -38.653 -32.913 35.824  1.00 52.81  ?  47   THR D CG2 1 
ATOM   6381  N N   . VAL D  1  48  ? -42.469 -31.668 33.925  1.00 58.94  ?  48   VAL D N   1 
ATOM   6382  C CA  . VAL D  1  48  ? -43.512 -30.722 33.550  1.00 60.58  ?  48   VAL D CA  1 
ATOM   6383  C C   . VAL D  1  48  ? -43.362 -29.400 34.295  1.00 60.24  ?  48   VAL D C   1 
ATOM   6384  O O   . VAL D  1  48  ? -43.673 -28.340 33.740  1.00 60.15  ?  48   VAL D O   1 
ATOM   6385  C CB  . VAL D  1  48  ? -44.899 -31.338 33.789  1.00 61.93  ?  48   VAL D CB  1 
ATOM   6386  C CG1 . VAL D  1  48  ? -45.976 -30.499 33.127  1.00 62.53  ?  48   VAL D CG1 1 
ATOM   6387  C CG2 . VAL D  1  48  ? -44.934 -32.770 33.272  1.00 61.66  ?  48   VAL D CG2 1 
ATOM   6388  N N   . GLU D  1  49  ? -42.877 -29.433 35.537  1.00 66.22  ?  49   GLU D N   1 
ATOM   6389  C CA  . GLU D  1  49  ? -42.626 -28.189 36.257  1.00 63.83  ?  49   GLU D CA  1 
ATOM   6390  C C   . GLU D  1  49  ? -41.498 -27.399 35.605  1.00 60.76  ?  49   GLU D C   1 
ATOM   6391  O O   . GLU D  1  49  ? -41.585 -26.170 35.486  1.00 59.25  ?  49   GLU D O   1 
ATOM   6392  C CB  . GLU D  1  49  ? -42.300 -28.485 37.722  1.00 62.91  ?  49   GLU D CB  1 
ATOM   6393  C CG  . GLU D  1  49  ? -43.301 -29.405 38.419  1.00 65.65  ?  49   GLU D CG  1 
ATOM   6394  C CD  . GLU D  1  49  ? -42.964 -30.893 38.264  1.00 65.88  ?  49   GLU D CD  1 
ATOM   6395  O OE1 . GLU D  1  49  ? -41.762 -31.241 38.211  1.00 63.67  ?  49   GLU D OE1 1 
ATOM   6396  O OE2 . GLU D  1  49  ? -43.906 -31.717 38.192  1.00 67.94  -1 49   GLU D OE2 1 
ATOM   6397  N N   . GLU D  1  50  ? -40.432 -28.088 35.181  1.00 59.17  ?  50   GLU D N   1 
ATOM   6398  C CA  . GLU D  1  50  ? -39.347 -27.430 34.456  1.00 56.55  ?  50   GLU D CA  1 
ATOM   6399  C C   . GLU D  1  50  ? -39.863 -26.745 33.198  1.00 57.51  ?  50   GLU D C   1 
ATOM   6400  O O   . GLU D  1  50  ? -39.583 -25.566 32.958  1.00 55.17  ?  50   GLU D O   1 
ATOM   6401  C CB  . GLU D  1  50  ? -38.270 -28.452 34.091  1.00 55.81  ?  50   GLU D CB  1 
ATOM   6402  C CG  . GLU D  1  50  ? -37.346 -28.857 35.219  1.00 53.73  ?  50   GLU D CG  1 
ATOM   6403  C CD  . GLU D  1  50  ? -36.481 -30.048 34.846  1.00 53.29  ?  50   GLU D CD  1 
ATOM   6404  O OE1 . GLU D  1  50  ? -36.771 -30.699 33.819  1.00 55.00  ?  50   GLU D OE1 1 
ATOM   6405  O OE2 . GLU D  1  50  ? -35.501 -30.328 35.570  1.00 51.40  -1 50   GLU D OE2 1 
ATOM   6406  N N   . ALA D  1  51  ? -40.637 -27.472 32.388  1.00 56.19  ?  51   ALA D N   1 
ATOM   6407  C CA  . ALA D  1  51  ? -41.113 -26.934 31.118  1.00 57.37  ?  51   ALA D CA  1 
ATOM   6408  C C   . ALA D  1  51  ? -41.983 -25.699 31.323  1.00 55.88  ?  51   ALA D C   1 
ATOM   6409  O O   . ALA D  1  51  ? -41.818 -24.686 30.632  1.00 53.61  ?  51   ALA D O   1 
ATOM   6410  C CB  . ALA D  1  51  ? -41.882 -28.011 30.356  1.00 60.47  ?  51   ALA D CB  1 
ATOM   6411  N N   . ASN D  1  52  ? -42.914 -25.761 32.279  1.00 58.95  ?  52   ASN D N   1 
ATOM   6412  C CA  . ASN D  1  52  ? -43.792 -24.619 32.509  1.00 57.69  ?  52   ASN D CA  1 
ATOM   6413  C C   . ASN D  1  52  ? -43.016 -23.407 33.011  1.00 54.05  ?  52   ASN D C   1 
ATOM   6414  O O   . ASN D  1  52  ? -43.353 -22.267 32.665  1.00 52.42  ?  52   ASN D O   1 
ATOM   6415  C CB  . ASN D  1  52  ? -44.901 -25.000 33.491  1.00 59.92  ?  52   ASN D CB  1 
ATOM   6416  C CG  . ASN D  1  52  ? -46.027 -25.774 32.827  1.00 62.78  ?  52   ASN D CG  1 
ATOM   6417  O OD1 . ASN D  1  52  ? -46.731 -25.246 31.967  1.00 61.80  ?  52   ASN D OD1 1 
ATOM   6418  N ND2 . ASN D  1  52  ? -46.207 -27.027 33.231  1.00 65.51  ?  52   ASN D ND2 1 
ATOM   6419  N N   . ALA D  1  53  ? -41.959 -23.632 33.793  1.00 57.87  ?  53   ALA D N   1 
ATOM   6420  C CA  . ALA D  1  53  ? -41.160 -22.521 34.292  1.00 54.86  ?  53   ALA D CA  1 
ATOM   6421  C C   . ALA D  1  53  ? -40.430 -21.812 33.155  1.00 52.58  ?  53   ALA D C   1 
ATOM   6422  O O   . ALA D  1  53  ? -40.405 -20.575 33.105  1.00 50.78  ?  53   ALA D O   1 
ATOM   6423  C CB  . ALA D  1  53  ? -40.180 -23.024 35.349  1.00 54.17  ?  53   ALA D CB  1 
ATOM   6424  N N   . LEU D  1  54  ? -39.828 -22.579 32.237  1.00 54.25  ?  54   LEU D N   1 
ATOM   6425  C CA  . LEU D  1  54  ? -39.240 -21.994 31.032  1.00 52.57  ?  54   LEU D CA  1 
ATOM   6426  C C   . LEU D  1  54  ? -40.290 -21.251 30.216  1.00 52.89  ?  54   LEU D C   1 
ATOM   6427  O O   . LEU D  1  54  ? -40.022 -20.171 29.675  1.00 50.65  ?  54   LEU D O   1 
ATOM   6428  C CB  . LEU D  1  54  ? -38.588 -23.082 30.175  1.00 53.87  ?  54   LEU D CB  1 
ATOM   6429  C CG  . LEU D  1  54  ? -37.106 -23.412 30.371  1.00 51.98  ?  54   LEU D CG  1 
ATOM   6430  C CD1 . LEU D  1  54  ? -36.252 -22.161 30.320  1.00 48.43  ?  54   LEU D CD1 1 
ATOM   6431  C CD2 . LEU D  1  54  ? -36.893 -24.137 31.662  1.00 52.11  ?  54   LEU D CD2 1 
ATOM   6432  N N   . LEU D  1  55  ? -41.490 -21.826 30.109  1.00 55.19  ?  55   LEU D N   1 
ATOM   6433  C CA  . LEU D  1  55  ? -42.552 -21.218 29.314  1.00 55.25  ?  55   LEU D CA  1 
ATOM   6434  C C   . LEU D  1  55  ? -42.958 -19.861 29.879  1.00 53.30  ?  55   LEU D C   1 
ATOM   6435  O O   . LEU D  1  55  ? -43.301 -18.940 29.124  1.00 51.91  ?  55   LEU D O   1 
ATOM   6436  C CB  . LEU D  1  55  ? -43.748 -22.169 29.259  1.00 58.38  ?  55   LEU D CB  1 
ATOM   6437  C CG  . LEU D  1  55  ? -44.363 -22.469 27.894  1.00 59.00  ?  55   LEU D CG  1 
ATOM   6438  C CD1 . LEU D  1  55  ? -43.292 -22.693 26.839  1.00 58.25  ?  55   LEU D CD1 1 
ATOM   6439  C CD2 . LEU D  1  55  ? -45.265 -23.686 27.999  1.00 61.86  ?  55   LEU D CD2 1 
ATOM   6440  N N   . LYS D  1  56  ? -42.935 -19.722 31.208  1.00 60.12  ?  56   LYS D N   1 
ATOM   6441  C CA  . LYS D  1  56  ? -43.220 -18.430 31.825  1.00 58.72  ?  56   LYS D CA  1 
ATOM   6442  C C   . LYS D  1  56  ? -42.132 -17.413 31.507  1.00 55.94  ?  56   LYS D C   1 
ATOM   6443  O O   . LYS D  1  56  ? -42.427 -16.256 31.187  1.00 54.68  ?  56   LYS D O   1 
ATOM   6444  C CB  . LYS D  1  56  ? -43.373 -18.598 33.333  1.00 59.84  ?  56   LYS D CB  1 
ATOM   6445  C CG  . LYS D  1  56  ? -44.377 -17.654 33.946  1.00 60.16  ?  56   LYS D CG  1 
ATOM   6446  C CD  . LYS D  1  56  ? -44.275 -17.657 35.460  1.00 61.19  ?  56   LYS D CD  1 
ATOM   6447  C CE  . LYS D  1  56  ? -43.528 -16.424 35.973  1.00 59.64  ?  56   LYS D CE  1 
ATOM   6448  N NZ  . LYS D  1  56  ? -43.813 -16.153 37.418  1.00 61.29  ?  56   LYS D NZ  1 
ATOM   6449  N N   . TRP D  1  57  ? -40.868 -17.834 31.582  1.00 58.60  ?  57   TRP D N   1 
ATOM   6450  C CA  . TRP D  1  57  ? -39.760 -16.952 31.228  1.00 56.07  ?  57   TRP D CA  1 
ATOM   6451  C C   . TRP D  1  57  ? -39.849 -16.510 29.773  1.00 55.06  ?  57   TRP D C   1 
ATOM   6452  O O   . TRP D  1  57  ? -39.631 -15.334 29.460  1.00 53.32  ?  57   TRP D O   1 
ATOM   6453  C CB  . TRP D  1  57  ? -38.432 -17.664 31.493  1.00 55.37  ?  57   TRP D CB  1 
ATOM   6454  C CG  . TRP D  1  57  ? -37.222 -16.862 31.132  1.00 52.91  ?  57   TRP D CG  1 
ATOM   6455  C CD1 . TRP D  1  57  ? -36.971 -15.565 31.466  1.00 51.70  ?  57   TRP D CD1 1 
ATOM   6456  C CD2 . TRP D  1  57  ? -36.090 -17.307 30.372  1.00 51.66  ?  57   TRP D CD2 1 
ATOM   6457  N NE1 . TRP D  1  57  ? -35.755 -15.171 30.959  1.00 49.74  ?  57   TRP D NE1 1 
ATOM   6458  C CE2 . TRP D  1  57  ? -35.194 -16.222 30.284  1.00 49.54  ?  57   TRP D CE2 1 
ATOM   6459  C CE3 . TRP D  1  57  ? -35.747 -18.516 29.756  1.00 52.45  ?  57   TRP D CE3 1 
ATOM   6460  C CZ2 . TRP D  1  57  ? -33.976 -16.309 29.606  1.00 47.90  ?  57   TRP D CZ2 1 
ATOM   6461  C CZ3 . TRP D  1  57  ? -34.533 -18.602 29.081  1.00 50.93  ?  57   TRP D CZ3 1 
ATOM   6462  C CH2 . TRP D  1  57  ? -33.665 -17.506 29.013  1.00 48.53  ?  57   TRP D CH2 1 
ATOM   6463  N N   . LYS D  1  58  ? -40.176 -17.442 28.870  1.00 52.71  ?  58   LYS D N   1 
ATOM   6464  C CA  . LYS D  1  58  ? -40.236 -17.122 27.447  1.00 52.01  ?  58   LYS D CA  1 
ATOM   6465  C C   . LYS D  1  58  ? -41.276 -16.047 27.152  1.00 51.51  ?  58   LYS D C   1 
ATOM   6466  O O   . LYS D  1  58  ? -41.108 -15.262 26.211  1.00 50.37  ?  58   LYS D O   1 
ATOM   6467  C CB  . LYS D  1  58  ? -40.529 -18.395 26.642  1.00 54.22  ?  58   LYS D CB  1 
ATOM   6468  C CG  . LYS D  1  58  ? -40.538 -18.222 25.126  1.00 53.73  ?  58   LYS D CG  1 
ATOM   6469  C CD  . LYS D  1  58  ? -41.959 -18.103 24.602  1.00 54.62  ?  58   LYS D CD  1 
ATOM   6470  C CE  . LYS D  1  58  ? -42.016 -18.211 23.092  1.00 54.42  ?  58   LYS D CE  1 
ATOM   6471  N NZ  . LYS D  1  58  ? -41.983 -19.629 22.663  1.00 56.69  ?  58   LYS D NZ  1 
ATOM   6472  N N   . SER D  1  59  ? -42.338 -15.976 27.958  1.00 56.22  ?  59   SER D N   1 
ATOM   6473  C CA  . SER D  1  59  ? -43.414 -15.025 27.708  1.00 55.86  ?  59   SER D CA  1 
ATOM   6474  C C   . SER D  1  59  ? -43.014 -13.578 27.981  1.00 53.83  ?  59   SER D C   1 
ATOM   6475  O O   . SER D  1  59  ? -43.754 -12.670 27.585  1.00 53.22  ?  59   SER D O   1 
ATOM   6476  C CB  . SER D  1  59  ? -44.626 -15.382 28.559  1.00 57.86  ?  59   SER D CB  1 
ATOM   6477  O OG  . SER D  1  59  ? -44.400 -15.004 29.902  1.00 57.89  ?  59   SER D OG  1 
ATOM   6478  N N   . THR D  1  60  ? -41.883 -13.343 28.646  1.00 55.85  ?  60   THR D N   1 
ATOM   6479  C CA  . THR D  1  60  ? -41.400 -11.995 28.923  1.00 54.24  ?  60   THR D CA  1 
ATOM   6480  C C   . THR D  1  60  ? -40.544 -11.426 27.799  1.00 52.28  ?  60   THR D C   1 
ATOM   6481  O O   . THR D  1  60  ? -40.150 -10.257 27.875  1.00 51.03  ?  60   THR D O   1 
ATOM   6482  C CB  . THR D  1  60  ? -40.593 -11.971 30.226  1.00 54.44  ?  60   THR D CB  1 
ATOM   6483  O OG1 . THR D  1  60  ? -39.244 -12.379 29.958  1.00 53.33  ?  60   THR D OG1 1 
ATOM   6484  C CG2 . THR D  1  60  ? -41.209 -12.901 31.262  1.00 56.55  ?  60   THR D CG2 1 
ATOM   6485  N N   . PHE D  1  61  ? -40.250 -12.213 26.767  1.00 55.18  ?  61   PHE D N   1 
ATOM   6486  C CA  . PHE D  1  61  ? -39.328 -11.776 25.728  1.00 53.45  ?  61   PHE D CA  1 
ATOM   6487  C C   . PHE D  1  61  ? -39.950 -10.674 24.873  1.00 52.52  ?  61   PHE D C   1 
ATOM   6488  O O   . PHE D  1  61  ? -41.157 -10.656 24.618  1.00 53.35  ?  61   PHE D O   1 
ATOM   6489  C CB  . PHE D  1  61  ? -38.921 -12.959 24.846  1.00 54.03  ?  61   PHE D CB  1 
ATOM   6490  C CG  . PHE D  1  61  ? -38.117 -14.012 25.565  1.00 54.72  ?  61   PHE D CG  1 
ATOM   6491  C CD1 . PHE D  1  61  ? -37.529 -13.743 26.790  1.00 54.19  ?  61   PHE D CD1 1 
ATOM   6492  C CD2 . PHE D  1  61  ? -37.954 -15.276 25.016  1.00 56.07  ?  61   PHE D CD2 1 
ATOM   6493  C CE1 . PHE D  1  61  ? -36.790 -14.714 27.456  1.00 54.66  ?  61   PHE D CE1 1 
ATOM   6494  C CE2 . PHE D  1  61  ? -37.219 -16.247 25.676  1.00 56.74  ?  61   PHE D CE2 1 
ATOM   6495  C CZ  . PHE D  1  61  ? -36.636 -15.963 26.899  1.00 55.83  ?  61   PHE D CZ  1 
ATOM   6496  N N   . THR D  1  62  ? -39.103 -9.747  24.430  1.00 64.93  ?  62   THR D N   1 
ATOM   6497  C CA  . THR D  1  62  ? -39.514 -8.557  23.699  1.00 63.87  ?  62   THR D CA  1 
ATOM   6498  C C   . THR D  1  62  ? -39.144 -8.660  22.224  1.00 63.04  ?  62   THR D C   1 
ATOM   6499  O O   . THR D  1  62  ? -38.164 -9.317  21.857  1.00 62.81  ?  62   THR D O   1 
ATOM   6500  C CB  . THR D  1  62  ? -38.858 -7.315  24.298  1.00 62.80  ?  62   THR D CB  1 
ATOM   6501  O OG1 . THR D  1  62  ? -38.862 -7.432  25.724  1.00 63.75  ?  62   THR D OG1 1 
ATOM   6502  C CG2 . THR D  1  62  ? -39.613 -6.052  23.889  1.00 62.21  ?  62   THR D CG2 1 
ATOM   6503  N N   . ASN D  1  63  ? -39.938 -7.987  21.383  1.00 72.12  ?  63   ASN D N   1 
ATOM   6504  C CA  . ASN D  1  63  ? -39.687 -7.884  19.943  1.00 71.32  ?  63   ASN D CA  1 
ATOM   6505  C C   . ASN D  1  63  ? -39.608 -9.254  19.273  1.00 72.38  ?  63   ASN D C   1 
ATOM   6506  O O   . ASN D  1  63  ? -38.908 -9.420  18.272  1.00 71.86  ?  63   ASN D O   1 
ATOM   6507  C CB  . ASN D  1  63  ? -38.406 -7.092  19.647  1.00 69.89  ?  63   ASN D CB  1 
ATOM   6508  C CG  . ASN D  1  63  ? -38.542 -5.599  19.928  1.00 69.99  ?  63   ASN D CG  1 
ATOM   6509  O OD1 . ASN D  1  63  ? -39.646 -5.057  19.986  1.00 71.70  ?  63   ASN D OD1 1 
ATOM   6510  N ND2 . ASN D  1  63  ? -37.395 -4.928  20.093  1.00 69.10  ?  63   ASN D ND2 1 
ATOM   6511  N N   . GLN D  1  64  ? -40.316 -10.245 19.807  1.00 63.94  ?  64   GLN D N   1 
ATOM   6512  C CA  . GLN D  1  64  ? -40.204 -11.610 19.308  1.00 65.32  ?  64   GLN D CA  1 
ATOM   6513  C C   . GLN D  1  64  ? -41.049 -11.789 18.053  1.00 65.69  ?  64   GLN D C   1 
ATOM   6514  O O   . GLN D  1  64  ? -42.213 -11.384 18.018  1.00 65.83  ?  64   GLN D O   1 
ATOM   6515  C CB  . GLN D  1  64  ? -40.632 -12.609 20.385  1.00 67.17  ?  64   GLN D CB  1 
ATOM   6516  C CG  . GLN D  1  64  ? -39.647 -13.758 20.611  1.00 68.05  ?  64   GLN D CG  1 
ATOM   6517  C CD  . GLN D  1  64  ? -38.217 -13.278 20.814  1.00 66.45  ?  64   GLN D CD  1 
ATOM   6518  O OE1 . GLN D  1  64  ? -37.946 -12.409 21.647  1.00 65.40  ?  64   GLN D OE1 1 
ATOM   6519  N NE2 . GLN D  1  64  ? -37.295 -13.840 20.041  1.00 66.36  ?  64   GLN D NE2 1 
ATOM   6520  N N   . THR D  1  65  ? -40.453 -12.371 17.015  1.00 63.37  ?  65   THR D N   1 
ATOM   6521  C CA  . THR D  1  65  ? -41.174 -12.667 15.787  1.00 63.76  ?  65   THR D CA  1 
ATOM   6522  C C   . THR D  1  65  ? -41.771 -14.069 15.822  1.00 65.93  ?  65   THR D C   1 
ATOM   6523  O O   . THR D  1  65  ? -41.360 -14.932 16.601  1.00 67.21  ?  65   THR D O   1 
ATOM   6524  C CB  . THR D  1  65  ? -40.265 -12.546 14.570  1.00 62.88  ?  65   THR D CB  1 
ATOM   6525  O OG1 . THR D  1  65  ? -41.064 -12.644 13.384  1.00 63.03  ?  65   THR D OG1 1 
ATOM   6526  C CG2 . THR D  1  65  ? -39.225 -13.660 14.572  1.00 63.96  ?  65   THR D CG2 1 
ATOM   6527  N N   . SER D  1  66  ? -42.757 -14.287 14.949  1.00 65.33  ?  66   SER D N   1 
ATOM   6528  C CA  . SER D  1  66  ? -43.406 -15.590 14.852  1.00 67.30  ?  66   SER D CA  1 
ATOM   6529  C C   . SER D  1  66  ? -42.495 -16.660 14.268  1.00 68.24  ?  66   SER D C   1 
ATOM   6530  O O   . SER D  1  66  ? -42.814 -17.849 14.366  1.00 70.05  ?  66   SER D O   1 
ATOM   6531  C CB  . SER D  1  66  ? -44.677 -15.481 14.007  1.00 67.17  ?  66   SER D CB  1 
ATOM   6532  O OG  . SER D  1  66  ? -45.461 -16.658 14.111  1.00 69.00  ?  66   SER D OG  1 
ATOM   6533  N N   . SER D  1  67  ? -41.375 -16.272 13.679  1.00 64.38  ?  67   SER D N   1 
ATOM   6534  C CA  . SER D  1  67  ? -40.505 -17.199 12.978  1.00 65.21  ?  67   SER D CA  1 
ATOM   6535  C C   . SER D  1  67  ? -39.403 -17.767 13.858  1.00 66.10  ?  67   SER D C   1 
ATOM   6536  O O   . SER D  1  67  ? -38.624 -18.597 13.381  1.00 67.00  ?  67   SER D O   1 
ATOM   6537  C CB  . SER D  1  67  ? -39.890 -16.500 11.765  1.00 63.66  ?  67   SER D CB  1 
ATOM   6538  O OG  . SER D  1  67  ? -38.619 -15.963 12.094  1.00 62.54  ?  67   SER D OG  1 
ATOM   6539  N N   . SER D  1  68  ? -39.305 -17.343 15.114  1.00 56.01  ?  68   SER D N   1 
ATOM   6540  C CA  . SER D  1  68  ? -38.175 -17.757 15.932  1.00 55.18  ?  68   SER D CA  1 
ATOM   6541  C C   . SER D  1  68  ? -38.216 -19.259 16.188  1.00 56.50  ?  68   SER D C   1 
ATOM   6542  O O   . SER D  1  68  ? -39.270 -19.896 16.125  1.00 57.78  ?  68   SER D O   1 
ATOM   6543  C CB  . SER D  1  68  ? -38.150 -17.001 17.259  1.00 54.22  ?  68   SER D CB  1 
ATOM   6544  O OG  . SER D  1  68  ? -39.077 -17.553 18.162  1.00 55.08  ?  68   SER D OG  1 
ATOM   6545  N N   . LYS D  1  69  ? -37.034 -19.827 16.450  1.00 53.06  ?  69   LYS D N   1 
ATOM   6546  C CA  . LYS D  1  69  ? -36.926 -21.259 16.704  1.00 55.55  ?  69   LYS D CA  1 
ATOM   6547  C C   . LYS D  1  69  ? -37.642 -21.672 17.977  1.00 56.91  ?  69   LYS D C   1 
ATOM   6548  O O   . LYS D  1  69  ? -37.951 -22.858 18.139  1.00 59.04  ?  69   LYS D O   1 
ATOM   6549  C CB  . LYS D  1  69  ? -35.455 -21.683 16.773  1.00 55.94  ?  69   LYS D CB  1 
ATOM   6550  C CG  . LYS D  1  69  ? -34.783 -21.812 15.413  1.00 55.61  ?  69   LYS D CG  1 
ATOM   6551  C CD  . LYS D  1  69  ? -33.372 -21.249 15.449  1.00 54.43  ?  69   LYS D CD  1 
ATOM   6552  C CE  . LYS D  1  69  ? -32.600 -21.547 14.165  1.00 54.60  ?  69   LYS D CE  1 
ATOM   6553  N NZ  . LYS D  1  69  ? -31.165 -21.113 14.231  1.00 53.74  ?  69   LYS D NZ  1 
ATOM   6554  N N   . LEU D  1  70  ? -37.920 -20.727 18.877  1.00 51.34  ?  70   LEU D N   1 
ATOM   6555  C CA  . LEU D  1  70  ? -38.609 -21.053 20.121  1.00 52.61  ?  70   LEU D CA  1 
ATOM   6556  C C   . LEU D  1  70  ? -40.102 -21.360 19.921  1.00 53.69  ?  70   LEU D C   1 
ATOM   6557  O O   . LEU D  1  70  ? -40.803 -21.580 20.922  1.00 54.80  ?  70   LEU D O   1 
ATOM   6558  C CB  . LEU D  1  70  ? -38.433 -19.920 21.134  1.00 50.65  ?  70   LEU D CB  1 
ATOM   6559  C CG  . LEU D  1  70  ? -37.011 -19.556 21.569  1.00 49.05  ?  70   LEU D CG  1 
ATOM   6560  C CD1 . LEU D  1  70  ? -37.042 -18.886 22.923  1.00 47.70  ?  70   LEU D CD1 1 
ATOM   6561  C CD2 . LEU D  1  70  ? -36.129 -20.768 21.627  1.00 50.93  ?  70   LEU D CD2 1 
ATOM   6562  N N   . SER D  1  71  ? -40.594 -21.402 18.680  1.00 51.70  ?  71   SER D N   1 
ATOM   6563  C CA  . SER D  1  71  ? -41.962 -21.839 18.433  1.00 53.07  ?  71   SER D CA  1 
ATOM   6564  C C   . SER D  1  71  ? -42.196 -23.266 18.893  1.00 54.24  ?  71   SER D C   1 
ATOM   6565  O O   . SER D  1  71  ? -43.348 -23.646 19.129  1.00 55.31  ?  71   SER D O   1 
ATOM   6566  C CB  . SER D  1  71  ? -42.296 -21.739 16.949  1.00 54.49  ?  71   SER D CB  1 
ATOM   6567  O OG  . SER D  1  71  ? -41.942 -20.471 16.446  1.00 54.34  ?  71   SER D OG  1 
ATOM   6568  N N   . SER D  1  72  ? -41.136 -24.068 19.007  1.00 53.44  ?  72   SER D N   1 
ATOM   6569  C CA  . SER D  1  72  ? -41.272 -25.466 19.390  1.00 55.64  ?  72   SER D CA  1 
ATOM   6570  C C   . SER D  1  72  ? -41.608 -25.660 20.865  1.00 57.02  ?  72   SER D C   1 
ATOM   6571  O O   . SER D  1  72  ? -41.884 -26.796 21.267  1.00 58.78  ?  72   SER D O   1 
ATOM   6572  C CB  . SER D  1  72  ? -39.987 -26.224 19.056  1.00 56.14  ?  72   SER D CB  1 
ATOM   6573  O OG  . SER D  1  72  ? -38.862 -25.582 19.625  1.00 55.50  ?  72   SER D OG  1 
ATOM   6574  N N   . TRP D  1  73  ? -41.592 -24.602 21.676  1.00 55.49  ?  73   TRP D N   1 
ATOM   6575  C CA  . TRP D  1  73  ? -41.909 -24.727 23.099  1.00 56.75  ?  73   TRP D CA  1 
ATOM   6576  C C   . TRP D  1  73  ? -43.427 -24.694 23.256  1.00 57.24  ?  73   TRP D C   1 
ATOM   6577  O O   . TRP D  1  73  ? -44.023 -23.647 23.509  1.00 56.02  ?  73   TRP D O   1 
ATOM   6578  C CB  . TRP D  1  73  ? -41.243 -23.612 23.901  1.00 55.16  ?  73   TRP D CB  1 
ATOM   6579  C CG  . TRP D  1  73  ? -39.739 -23.688 23.953  1.00 54.64  ?  73   TRP D CG  1 
ATOM   6580  C CD1 . TRP D  1  73  ? -38.921 -24.400 23.122  1.00 55.22  ?  73   TRP D CD1 1 
ATOM   6581  C CD2 . TRP D  1  73  ? -38.874 -23.020 24.885  1.00 53.01  ?  73   TRP D CD2 1 
ATOM   6582  N NE1 . TRP D  1  73  ? -37.603 -24.218 23.479  1.00 54.51  ?  73   TRP D NE1 1 
ATOM   6583  C CE2 . TRP D  1  73  ? -37.549 -23.375 24.557  1.00 52.84  ?  73   TRP D CE2 1 
ATOM   6584  C CE3 . TRP D  1  73  ? -39.093 -22.158 25.963  1.00 51.27  ?  73   TRP D CE3 1 
ATOM   6585  C CZ2 . TRP D  1  73  ? -36.451 -22.900 25.269  1.00 50.54  ?  73   TRP D CZ2 1 
ATOM   6586  C CZ3 . TRP D  1  73  ? -38.000 -21.688 26.668  1.00 48.90  ?  73   TRP D CZ3 1 
ATOM   6587  C CH2 . TRP D  1  73  ? -36.697 -22.061 26.318  1.00 48.30  ?  73   TRP D CH2 1 
ATOM   6588  N N   . VAL D  1  74  ? -44.077 -25.851 23.131  1.00 60.50  ?  74   VAL D N   1 
ATOM   6589  C CA  . VAL D  1  74  ? -45.534 -25.828 23.096  1.00 60.75  ?  74   VAL D CA  1 
ATOM   6590  C C   . VAL D  1  74  ? -46.154 -26.615 24.244  1.00 62.76  ?  74   VAL D C   1 
ATOM   6591  O O   . VAL D  1  74  ? -46.870 -26.043 25.077  1.00 62.92  ?  74   VAL D O   1 
ATOM   6592  C CB  . VAL D  1  74  ? -46.048 -26.354 21.745  1.00 60.37  ?  74   VAL D CB  1 
ATOM   6593  C CG1 . VAL D  1  74  ? -47.561 -26.238 21.675  1.00 60.41  ?  74   VAL D CG1 1 
ATOM   6594  C CG2 . VAL D  1  74  ? -45.414 -25.588 20.611  1.00 58.42  ?  74   VAL D CG2 1 
ATOM   6595  N N   . ASN D  1  75  ? -45.891 -27.927 24.314  1.00 65.92  ?  75   ASN D N   1 
ATOM   6596  C CA  . ASN D  1  75  ? -46.586 -28.523 25.449  1.00 67.55  ?  75   ASN D CA  1 
ATOM   6597  C C   . ASN D  1  75  ? -45.600 -28.888 26.553  1.00 68.55  ?  75   ASN D C   1 
ATOM   6598  O O   . ASN D  1  75  ? -44.481 -29.334 26.271  1.00 68.40  ?  75   ASN D O   1 
ATOM   6599  C CB  . ASN D  1  75  ? -47.427 -29.750 25.055  1.00 68.45  ?  75   ASN D CB  1 
ATOM   6600  C CG  . ASN D  1  75  ? -46.609 -31.003 24.907  1.00 69.13  ?  75   ASN D CG  1 
ATOM   6601  O OD1 . ASN D  1  75  ? -45.470 -30.952 24.459  1.00 68.46  ?  75   ASN D OD1 1 
ATOM   6602  N ND2 . ASN D  1  75  ? -47.183 -32.142 25.288  1.00 70.36  ?  75   ASN D ND2 1 
ATOM   6603  N N   . PRO D  1  76  ? -45.960 -28.656 27.816  1.00 66.38  ?  76   PRO D N   1 
ATOM   6604  C CA  . PRO D  1  76  ? -44.991 -28.845 28.901  1.00 67.17  ?  76   PRO D CA  1 
ATOM   6605  C C   . PRO D  1  76  ? -44.753 -30.293 29.276  1.00 68.10  ?  76   PRO D C   1 
ATOM   6606  O O   . PRO D  1  76  ? -43.883 -30.558 30.118  1.00 68.30  ?  76   PRO D O   1 
ATOM   6607  C CB  . PRO D  1  76  ? -45.623 -28.071 30.070  1.00 67.74  ?  76   PRO D CB  1 
ATOM   6608  C CG  . PRO D  1  76  ? -46.634 -27.161 29.431  1.00 66.52  ?  76   PRO D CG  1 
ATOM   6609  C CD  . PRO D  1  76  ? -47.159 -27.945 28.275  1.00 66.38  ?  76   PRO D CD  1 
ATOM   6610  N N   . ASN D  1  77  ? -45.488 -31.232 28.690  1.00 70.42  ?  77   ASN D N   1 
ATOM   6611  C CA  . ASN D  1  77  ? -45.288 -32.634 29.018  1.00 70.95  ?  77   ASN D CA  1 
ATOM   6612  C C   . ASN D  1  77  ? -43.947 -33.131 28.492  1.00 70.09  ?  77   ASN D C   1 
ATOM   6613  O O   . ASN D  1  77  ? -43.500 -32.743 27.407  1.00 69.35  ?  77   ASN D O   1 
ATOM   6614  C CB  . ASN D  1  77  ? -46.421 -33.486 28.450  1.00 71.51  ?  77   ASN D CB  1 
ATOM   6615  C CG  . ASN D  1  77  ? -47.616 -33.556 29.382  1.00 72.46  ?  77   ASN D CG  1 
ATOM   6616  O OD1 . ASN D  1  77  ? -47.497 -33.298 30.581  1.00 72.85  ?  77   ASN D OD1 1 
ATOM   6617  N ND2 . ASN D  1  77  ? -48.775 -33.911 28.837  1.00 72.83  ?  77   ASN D ND2 1 
ATOM   6618  N N   . THR D  1  78  ? -43.306 -34.003 29.272  1.00 75.18  ?  78   THR D N   1 
ATOM   6619  C CA  . THR D  1  78  ? -42.183 -34.765 28.756  1.00 74.18  ?  78   THR D CA  1 
ATOM   6620  C C   . THR D  1  78  ? -42.664 -35.607 27.576  1.00 74.52  ?  78   THR D C   1 
ATOM   6621  O O   . THR D  1  78  ? -43.863 -35.745 27.319  1.00 75.46  ?  78   THR D O   1 
ATOM   6622  C CB  . THR D  1  78  ? -41.576 -35.648 29.853  1.00 73.51  ?  78   THR D CB  1 
ATOM   6623  O OG1 . THR D  1  78  ? -41.508 -34.910 31.081  1.00 73.46  ?  78   THR D OG1 1 
ATOM   6624  C CG2 . THR D  1  78  ? -40.172 -36.095 29.487  1.00 71.91  ?  78   THR D CG2 1 
ATOM   6625  N N   . SER D  1  79  ? -41.706 -36.145 26.833  1.00 71.07  ?  79   SER D N   1 
ATOM   6626  C CA  . SER D  1  79  ? -41.866 -36.839 25.566  1.00 71.10  ?  79   SER D CA  1 
ATOM   6627  C C   . SER D  1  79  ? -42.150 -35.855 24.446  1.00 71.34  ?  79   SER D C   1 
ATOM   6628  O O   . SER D  1  79  ? -42.222 -36.271 23.285  1.00 70.92  ?  79   SER D O   1 
ATOM   6629  C CB  . SER D  1  79  ? -42.990 -37.894 25.576  1.00 71.76  ?  79   SER D CB  1 
ATOM   6630  O OG  . SER D  1  79  ? -44.270 -37.287 25.655  1.00 72.97  ?  79   SER D OG  1 
ATOM   6631  N N   . SER D  1  80  ? -42.332 -34.571 24.741  1.00 65.69  ?  80   SER D N   1 
ATOM   6632  C CA  . SER D  1  80  ? -42.234 -33.538 23.724  1.00 64.79  ?  80   SER D CA  1 
ATOM   6633  C C   . SER D  1  80  ? -41.252 -32.491 24.220  1.00 63.96  ?  80   SER D C   1 
ATOM   6634  O O   . SER D  1  80  ? -40.502 -31.901 23.434  1.00 62.97  ?  80   SER D O   1 
ATOM   6635  C CB  . SER D  1  80  ? -43.601 -32.936 23.418  1.00 64.80  ?  80   SER D CB  1 
ATOM   6636  O OG  . SER D  1  80  ? -43.540 -32.025 22.339  1.00 63.48  ?  80   SER D OG  1 
ATOM   6637  N N   . PHE D  1  81  ? -41.262 -32.257 25.536  1.00 58.96  ?  81   PHE D N   1 
ATOM   6638  C CA  . PHE D  1  81  ? -40.277 -31.368 26.148  1.00 58.30  ?  81   PHE D CA  1 
ATOM   6639  C C   . PHE D  1  81  ? -38.864 -31.870 25.894  1.00 57.30  ?  81   PHE D C   1 
ATOM   6640  O O   . PHE D  1  81  ? -37.975 -31.098 25.516  1.00 56.37  ?  81   PHE D O   1 
ATOM   6641  C CB  . PHE D  1  81  ? -40.528 -31.251 27.653  1.00 58.98  ?  81   PHE D CB  1 
ATOM   6642  C CG  . PHE D  1  81  ? -39.520 -30.385 28.386  1.00 58.28  ?  81   PHE D CG  1 
ATOM   6643  C CD1 . PHE D  1  81  ? -39.434 -29.022 28.143  1.00 58.08  ?  81   PHE D CD1 1 
ATOM   6644  C CD2 . PHE D  1  81  ? -38.688 -30.934 29.349  1.00 57.18  ?  81   PHE D CD2 1 
ATOM   6645  C CE1 . PHE D  1  81  ? -38.525 -28.230 28.842  1.00 57.06  ?  81   PHE D CE1 1 
ATOM   6646  C CE2 . PHE D  1  81  ? -37.781 -30.147 30.044  1.00 55.20  ?  81   PHE D CE2 1 
ATOM   6647  C CZ  . PHE D  1  81  ? -37.701 -28.798 29.791  1.00 54.67  ?  81   PHE D CZ  1 
ATOM   6648  N N   . CYS D  1  82  ? -38.641 -33.166 26.097  1.00 63.74  ?  82   CYS D N   1 
ATOM   6649  C CA  . CYS D  1  82  ? -37.319 -33.766 25.992  1.00 62.46  ?  82   CYS D CA  1 
ATOM   6650  C C   . CYS D  1  82  ? -36.978 -34.254 24.591  1.00 62.32  ?  82   CYS D C   1 
ATOM   6651  O O   . CYS D  1  82  ? -35.909 -34.843 24.408  1.00 61.23  ?  82   CYS D O   1 
ATOM   6652  C CB  . CYS D  1  82  ? -37.194 -34.933 26.980  1.00 62.07  ?  82   CYS D CB  1 
ATOM   6653  S SG  . CYS D  1  82  ? -37.152 -34.416 28.710  1.00 61.50  ?  82   CYS D SG  1 
ATOM   6654  N N   . THR D  1  83  ? -37.853 -34.051 23.606  1.00 58.59  ?  83   THR D N   1 
ATOM   6655  C CA  . THR D  1  83  ? -37.529 -34.489 22.254  1.00 58.41  ?  83   THR D CA  1 
ATOM   6656  C C   . THR D  1  83  ? -37.702 -33.408 21.191  1.00 57.99  ?  83   THR D C   1 
ATOM   6657  O O   . THR D  1  83  ? -37.006 -33.430 20.172  1.00 57.21  ?  83   THR D O   1 
ATOM   6658  C CB  . THR D  1  83  ? -38.375 -35.704 21.879  1.00 58.81  ?  83   THR D CB  1 
ATOM   6659  O OG1 . THR D  1  83  ? -39.721 -35.500 22.319  1.00 59.98  ?  83   THR D OG1 1 
ATOM   6660  C CG2 . THR D  1  83  ? -37.821 -36.950 22.539  1.00 58.03  ?  83   THR D CG2 1 
ATOM   6661  N N   . SER D  1  84  ? -38.623 -32.468 21.390  1.00 55.48  ?  84   SER D N   1 
ATOM   6662  C CA  . SER D  1  84  ? -39.001 -31.567 20.310  1.00 55.29  ?  84   SER D CA  1 
ATOM   6663  C C   . SER D  1  84  ? -38.742 -30.095 20.591  1.00 54.15  ?  84   SER D C   1 
ATOM   6664  O O   . SER D  1  84  ? -38.798 -29.290 19.653  1.00 53.78  ?  84   SER D O   1 
ATOM   6665  C CB  . SER D  1  84  ? -40.487 -31.751 19.956  1.00 56.61  ?  84   SER D CB  1 
ATOM   6666  O OG  . SER D  1  84  ? -41.315 -30.865 20.691  1.00 56.25  ?  84   SER D OG  1 
ATOM   6667  N N   . TRP D  1  85  ? -38.464 -29.715 21.835  1.00 56.23  ?  85   TRP D N   1 
ATOM   6668  C CA  . TRP D  1  85  ? -38.217 -28.316 22.158  1.00 55.23  ?  85   TRP D CA  1 
ATOM   6669  C C   . TRP D  1  85  ? -36.811 -27.922 21.724  1.00 54.14  ?  85   TRP D C   1 
ATOM   6670  O O   . TRP D  1  85  ? -35.828 -28.551 22.130  1.00 54.44  ?  85   TRP D O   1 
ATOM   6671  C CB  . TRP D  1  85  ? -38.391 -28.070 23.655  1.00 56.05  ?  85   TRP D CB  1 
ATOM   6672  C CG  . TRP D  1  85  ? -39.808 -27.998 24.117  1.00 56.80  ?  85   TRP D CG  1 
ATOM   6673  C CD1 . TRP D  1  85  ? -40.881 -28.662 23.595  1.00 57.34  ?  85   TRP D CD1 1 
ATOM   6674  C CD2 . TRP D  1  85  ? -40.310 -27.223 25.213  1.00 57.04  ?  85   TRP D CD2 1 
ATOM   6675  N NE1 . TRP D  1  85  ? -42.022 -28.343 24.297  1.00 57.89  ?  85   TRP D NE1 1 
ATOM   6676  C CE2 . TRP D  1  85  ? -41.696 -27.461 25.295  1.00 57.73  ?  85   TRP D CE2 1 
ATOM   6677  C CE3 . TRP D  1  85  ? -39.721 -26.345 26.130  1.00 56.51  ?  85   TRP D CE3 1 
ATOM   6678  C CZ2 . TRP D  1  85  ? -42.500 -26.855 26.256  1.00 58.06  ?  85   TRP D CZ2 1 
ATOM   6679  C CZ3 . TRP D  1  85  ? -40.521 -25.748 27.084  1.00 56.44  ?  85   TRP D CZ3 1 
ATOM   6680  C CH2 . TRP D  1  85  ? -41.894 -26.005 27.139  1.00 57.44  ?  85   TRP D CH2 1 
ATOM   6681  N N   . TYR D  1  86  ? -36.717 -26.869 20.912  1.00 56.47  ?  86   TYR D N   1 
ATOM   6682  C CA  . TYR D  1  86  ? -35.423 -26.422 20.414  1.00 55.30  ?  86   TYR D CA  1 
ATOM   6683  C C   . TYR D  1  86  ? -34.532 -25.977 21.566  1.00 55.15  ?  86   TYR D C   1 
ATOM   6684  O O   . TYR D  1  86  ? -34.954 -25.209 22.435  1.00 54.62  ?  86   TYR D O   1 
ATOM   6685  C CB  . TYR D  1  86  ? -35.600 -25.275 19.416  1.00 53.30  ?  86   TYR D CB  1 
ATOM   6686  C CG  . TYR D  1  86  ? -34.291 -24.722 18.885  1.00 51.93  ?  86   TYR D CG  1 
ATOM   6687  C CD1 . TYR D  1  86  ? -33.636 -23.678 19.530  1.00 50.27  ?  86   TYR D CD1 1 
ATOM   6688  C CD2 . TYR D  1  86  ? -33.711 -25.246 17.739  1.00 52.07  ?  86   TYR D CD2 1 
ATOM   6689  C CE1 . TYR D  1  86  ? -32.439 -23.178 19.050  1.00 48.86  ?  86   TYR D CE1 1 
ATOM   6690  C CE2 . TYR D  1  86  ? -32.518 -24.753 17.250  1.00 50.98  ?  86   TYR D CE2 1 
ATOM   6691  C CZ  . TYR D  1  86  ? -31.883 -23.721 17.905  1.00 49.46  ?  86   TYR D CZ  1 
ATOM   6692  O OH  . TYR D  1  86  ? -30.688 -23.242 17.403  1.00 48.28  ?  86   TYR D OH  1 
ATOM   6693  N N   . GLY D  1  87  ? -33.298 -26.473 21.574  1.00 51.66  ?  87   GLY D N   1 
ATOM   6694  C CA  . GLY D  1  87  ? -32.315 -26.019 22.530  1.00 51.26  ?  87   GLY D CA  1 
ATOM   6695  C C   . GLY D  1  87  ? -32.366 -26.661 23.897  1.00 52.00  ?  87   GLY D C   1 
ATOM   6696  O O   . GLY D  1  87  ? -31.615 -26.232 24.781  1.00 48.63  ?  87   GLY D O   1 
ATOM   6697  N N   . VAL D  1  88  ? -33.224 -27.660 24.119  1.00 51.03  ?  88   VAL D N   1 
ATOM   6698  C CA  . VAL D  1  88  ? -33.254 -28.346 25.407  1.00 50.49  ?  88   VAL D CA  1 
ATOM   6699  C C   . VAL D  1  88  ? -32.889 -29.813 25.212  1.00 50.23  ?  88   VAL D C   1 
ATOM   6700  O O   . VAL D  1  88  ? -33.168 -30.420 24.172  1.00 51.19  ?  88   VAL D O   1 
ATOM   6701  C CB  . VAL D  1  88  ? -34.621 -28.220 26.125  1.00 52.21  ?  88   VAL D CB  1 
ATOM   6702  C CG1 . VAL D  1  88  ? -35.167 -26.807 26.020  1.00 52.19  ?  88   VAL D CG1 1 
ATOM   6703  C CG2 . VAL D  1  88  ? -35.605 -29.207 25.565  1.00 53.70  ?  88   VAL D CG2 1 
ATOM   6704  N N   . ALA D  1  89  ? -32.255 -30.381 26.233  1.00 51.86  ?  89   ALA D N   1 
ATOM   6705  C CA  . ALA D  1  89  ? -31.899 -31.791 26.227  1.00 51.62  ?  89   ALA D CA  1 
ATOM   6706  C C   . ALA D  1  89  ? -32.017 -32.313 27.647  1.00 50.70  ?  89   ALA D C   1 
ATOM   6707  O O   . ALA D  1  89  ? -31.650 -31.619 28.599  1.00 48.90  ?  89   ALA D O   1 
ATOM   6708  C CB  . ALA D  1  89  ? -30.482 -32.017 25.689  1.00 49.96  ?  89   ALA D CB  1 
ATOM   6709  N N   . CYS D  1  90  ? -32.523 -33.533 27.790  1.00 51.29  ?  90   CYS D N   1 
ATOM   6710  C CA  . CYS D  1  90  ? -32.792 -34.087 29.104  1.00 50.76  ?  90   CYS D CA  1 
ATOM   6711  C C   . CYS D  1  90  ? -31.918 -35.298 29.389  1.00 49.33  ?  90   CYS D C   1 
ATOM   6712  O O   . CYS D  1  90  ? -31.457 -35.988 28.475  1.00 49.34  ?  90   CYS D O   1 
ATOM   6713  C CB  . CYS D  1  90  ? -34.243 -34.511 29.247  1.00 53.12  ?  90   CYS D CB  1 
ATOM   6714  S SG  . CYS D  1  90  ? -35.465 -33.276 28.854  1.00 55.27  ?  90   CYS D SG  1 
ATOM   6715  N N   . SER D  1  91  ? -31.708 -35.546 30.679  1.00 49.99  ?  91   SER D N   1 
ATOM   6716  C CA  . SER D  1  91  ? -31.231 -36.825 31.187  1.00 49.11  ?  91   SER D CA  1 
ATOM   6717  C C   . SER D  1  91  ? -32.232 -37.295 32.232  1.00 50.12  ?  91   SER D C   1 
ATOM   6718  O O   . SER D  1  91  ? -32.587 -36.533 33.137  1.00 50.08  ?  91   SER D O   1 
ATOM   6719  C CB  . SER D  1  91  ? -29.816 -36.710 31.782  1.00 46.99  ?  91   SER D CB  1 
ATOM   6720  O OG  . SER D  1  91  ? -29.337 -37.954 32.274  1.00 47.36  ?  91   SER D OG  1 
ATOM   6721  N N   . LEU D  1  92  ? -32.716 -38.527 32.079  1.00 48.47  ?  92   LEU D N   1 
ATOM   6722  C CA  . LEU D  1  92  ? -33.702 -39.103 32.997  1.00 49.37  ?  92   LEU D CA  1 
ATOM   6723  C C   . LEU D  1  92  ? -34.926 -38.195 33.158  1.00 48.76  ?  92   LEU D C   1 
ATOM   6724  O O   . LEU D  1  92  ? -35.505 -38.074 34.239  1.00 48.86  ?  92   LEU D O   1 
ATOM   6725  C CB  . LEU D  1  92  ? -33.065 -39.416 34.355  1.00 49.62  ?  92   LEU D CB  1 
ATOM   6726  C CG  . LEU D  1  92  ? -31.836 -40.328 34.340  1.00 50.45  ?  92   LEU D CG  1 
ATOM   6727  C CD1 . LEU D  1  92  ? -31.252 -40.481 35.731  1.00 50.76  ?  92   LEU D CD1 1 
ATOM   6728  C CD2 . LEU D  1  92  ? -32.173 -41.690 33.759  1.00 52.15  ?  92   LEU D CD2 1 
ATOM   6729  N N   . GLY D  1  93  ? -35.331 -37.553 32.065  1.00 50.90  ?  93   GLY D N   1 
ATOM   6730  C CA  . GLY D  1  93  ? -36.532 -36.741 32.065  1.00 52.85  ?  93   GLY D CA  1 
ATOM   6731  C C   . GLY D  1  93  ? -36.395 -35.343 32.626  1.00 52.30  ?  93   GLY D C   1 
ATOM   6732  O O   . GLY D  1  93  ? -37.404 -34.638 32.725  1.00 53.89  ?  93   GLY D O   1 
ATOM   6733  N N   . SER D  1  94  ? -35.186 -34.895 32.953  1.00 55.41  ?  94   SER D N   1 
ATOM   6734  C CA  . SER D  1  94  ? -34.976 -33.568 33.515  1.00 54.27  ?  94   SER D CA  1 
ATOM   6735  C C   . SER D  1  94  ? -33.980 -32.798 32.660  1.00 52.70  ?  94   SER D C   1 
ATOM   6736  O O   . SER D  1  94  ? -33.011 -33.373 32.152  1.00 51.62  ?  94   SER D O   1 
ATOM   6737  C CB  . SER D  1  94  ? -34.466 -33.648 34.956  1.00 52.64  ?  94   SER D CB  1 
ATOM   6738  O OG  . SER D  1  94  ? -34.005 -32.381 35.398  1.00 51.03  ?  94   SER D OG  1 
ATOM   6739  N N   . ILE D  1  95  ? -34.217 -31.492 32.511  1.00 53.12  ?  95   ILE D N   1 
ATOM   6740  C CA  . ILE D  1  95  ? -33.372 -30.673 31.649  1.00 51.64  ?  95   ILE D CA  1 
ATOM   6741  C C   . ILE D  1  95  ? -31.988 -30.534 32.270  1.00 48.50  ?  95   ILE D C   1 
ATOM   6742  O O   . ILE D  1  95  ? -31.840 -30.144 33.436  1.00 47.25  ?  95   ILE D O   1 
ATOM   6743  C CB  . ILE D  1  95  ? -34.020 -29.303 31.382  1.00 51.93  ?  95   ILE D CB  1 
ATOM   6744  C CG1 . ILE D  1  95  ? -33.133 -28.470 30.455  1.00 50.29  ?  95   ILE D CG1 1 
ATOM   6745  C CG2 . ILE D  1  95  ? -34.294 -28.546 32.672  1.00 50.54  ?  95   ILE D CG2 1 
ATOM   6746  C CD1 . ILE D  1  95  ? -33.767 -27.187 29.989  1.00 50.49  ?  95   ILE D CD1 1 
ATOM   6747  N N   . ILE D  1  96  ? -30.966 -30.886 31.497  1.00 48.96  ?  96   ILE D N   1 
ATOM   6748  C CA  . ILE D  1  96  ? -29.580 -30.710 31.911  1.00 47.82  ?  96   ILE D CA  1 
ATOM   6749  C C   . ILE D  1  96  ? -28.805 -29.815 30.964  1.00 46.92  ?  96   ILE D C   1 
ATOM   6750  O O   . ILE D  1  96  ? -27.665 -29.444 31.283  1.00 46.45  ?  96   ILE D O   1 
ATOM   6751  C CB  . ILE D  1  96  ? -28.855 -32.066 32.058  1.00 48.69  ?  96   ILE D CB  1 
ATOM   6752  C CG1 . ILE D  1  96  ? -28.876 -32.820 30.729  1.00 49.20  ?  96   ILE D CG1 1 
ATOM   6753  C CG2 . ILE D  1  96  ? -29.499 -32.906 33.147  1.00 49.64  ?  96   ILE D CG2 1 
ATOM   6754  C CD1 . ILE D  1  96  ? -27.854 -33.917 30.640  1.00 49.98  ?  96   ILE D CD1 1 
ATOM   6755  N N   . ARG D  1  97  ? -29.398 -29.425 29.836  1.00 53.08  ?  97   ARG D N   1 
ATOM   6756  C CA  . ARG D  1  97  ? -28.708 -28.713 28.770  1.00 52.29  ?  97   ARG D CA  1 
ATOM   6757  C C   . ARG D  1  97  ? -29.661 -27.710 28.134  1.00 53.65  ?  97   ARG D C   1 
ATOM   6758  O O   . ARG D  1  97  ? -30.748 -28.085 27.682  1.00 56.80  ?  97   ARG D O   1 
ATOM   6759  C CB  . ARG D  1  97  ? -28.190 -29.699 27.718  1.00 53.61  ?  97   ARG D CB  1 
ATOM   6760  C CG  . ARG D  1  97  ? -27.470 -29.064 26.544  1.00 53.33  ?  97   ARG D CG  1 
ATOM   6761  C CD  . ARG D  1  97  ? -26.770 -30.130 25.709  1.00 54.17  ?  97   ARG D CD  1 
ATOM   6762  N NE  . ARG D  1  97  ? -25.915 -30.992 26.524  1.00 52.40  ?  97   ARG D NE  1 
ATOM   6763  C CZ  . ARG D  1  97  ? -25.215 -32.017 26.052  1.00 52.59  ?  97   ARG D CZ  1 
ATOM   6764  N NH1 . ARG D  1  97  ? -25.246 -32.343 24.770  1.00 54.30  ?  97   ARG D NH1 1 
ATOM   6765  N NH2 . ARG D  1  97  ? -24.470 -32.739 26.890  1.00 51.01  ?  97   ARG D NH2 1 
ATOM   6766  N N   . LEU D  1  98  ? -29.246 -26.441 28.096  1.00 50.05  ?  98   LEU D N   1 
ATOM   6767  C CA  . LEU D  1  98  ? -30.017 -25.359 27.486  1.00 50.66  ?  98   LEU D CA  1 
ATOM   6768  C C   . LEU D  1  98  ? -29.088 -24.594 26.553  1.00 49.07  ?  98   LEU D C   1 
ATOM   6769  O O   . LEU D  1  98  ? -28.163 -23.917 27.011  1.00 45.79  ?  98   LEU D O   1 
ATOM   6770  C CB  . LEU D  1  98  ? -30.612 -24.435 28.550  1.00 48.92  ?  98   LEU D CB  1 
ATOM   6771  C CG  . LEU D  1  98  ? -31.503 -23.294 28.054  1.00 49.03  ?  98   LEU D CG  1 
ATOM   6772  C CD1 . LEU D  1  98  ? -32.828 -23.827 27.527  1.00 52.83  ?  98   LEU D CD1 1 
ATOM   6773  C CD2 . LEU D  1  98  ? -31.738 -22.273 29.154  1.00 46.89  ?  98   LEU D CD2 1 
ATOM   6774  N N   . ASN D  1  99  ? -29.326 -24.717 25.248  1.00 52.30  ?  99   ASN D N   1 
ATOM   6775  C CA  . ASN D  1  99  ? -28.457 -24.171 24.205  1.00 51.60  ?  99   ASN D CA  1 
ATOM   6776  C C   . ASN D  1  99  ? -29.272 -23.217 23.341  1.00 52.31  ?  99   ASN D C   1 
ATOM   6777  O O   . ASN D  1  99  ? -29.985 -23.654 22.434  1.00 56.00  ?  99   ASN D O   1 
ATOM   6778  C CB  . ASN D  1  99  ? -27.866 -25.298 23.366  1.00 54.42  ?  99   ASN D CB  1 
ATOM   6779  C CG  . ASN D  1  99  ? -26.740 -24.836 22.459  1.00 53.50  ?  99   ASN D CG  1 
ATOM   6780  O OD1 . ASN D  1  99  ? -26.266 -23.703 22.549  1.00 50.25  ?  99   ASN D OD1 1 
ATOM   6781  N ND2 . ASN D  1  99  ? -26.312 -25.727 21.568  1.00 55.91  ?  99   ASN D ND2 1 
ATOM   6782  N N   . LEU D  1  100 ? -29.159 -21.920 23.598  1.00 50.11  ?  100  LEU D N   1 
ATOM   6783  C CA  . LEU D  1  100 ? -29.932 -20.919 22.877  1.00 49.59  ?  100  LEU D CA  1 
ATOM   6784  C C   . LEU D  1  100 ? -29.018 -19.876 22.250  1.00 46.86  ?  100  LEU D C   1 
ATOM   6785  O O   . LEU D  1  100 ? -29.333 -18.685 22.212  1.00 44.76  ?  100  LEU D O   1 
ATOM   6786  C CB  . LEU D  1  100 ? -30.959 -20.260 23.793  1.00 48.44  ?  100  LEU D CB  1 
ATOM   6787  C CG  . LEU D  1  100 ? -32.095 -21.148 24.300  1.00 51.34  ?  100  LEU D CG  1 
ATOM   6788  C CD1 . LEU D  1  100 ? -32.982 -20.373 25.251  1.00 50.05  ?  100  LEU D CD1 1 
ATOM   6789  C CD2 . LEU D  1  100 ? -32.902 -21.694 23.140  1.00 54.52  ?  100  LEU D CD2 1 
ATOM   6790  N N   . THR D  1  101 ? -27.863 -20.317 21.760  1.00 48.18  ?  101  THR D N   1 
ATOM   6791  C CA  . THR D  1  101 ? -26.961 -19.429 21.044  1.00 46.02  ?  101  THR D CA  1 
ATOM   6792  C C   . THR D  1  101 ? -27.645 -18.882 19.805  1.00 46.70  ?  101  THR D C   1 
ATOM   6793  O O   . THR D  1  101 ? -28.286 -19.627 19.062  1.00 49.59  ?  101  THR D O   1 
ATOM   6794  C CB  . THR D  1  101 ? -25.696 -20.179 20.635  1.00 47.04  ?  101  THR D CB  1 
ATOM   6795  O OG1 . THR D  1  101 ? -25.208 -20.930 21.749  1.00 46.56  ?  101  THR D OG1 1 
ATOM   6796  C CG2 . THR D  1  101 ? -24.625 -19.203 20.183  1.00 44.31  ?  101  THR D CG2 1 
ATOM   6797  N N   . ASN D  1  102 ? -27.502 -17.577 19.588  1.00 48.77  ?  102  ASN D N   1 
ATOM   6798  C CA  . ASN D  1  102 ? -27.904 -16.930 18.340  1.00 48.73  ?  102  ASN D CA  1 
ATOM   6799  C C   . ASN D  1  102 ? -29.337 -17.280 17.952  1.00 50.63  ?  102  ASN D C   1 
ATOM   6800  O O   . ASN D  1  102 ? -29.637 -17.576 16.793  1.00 52.00  ?  102  ASN D O   1 
ATOM   6801  C CB  . ASN D  1  102 ? -26.938 -17.287 17.216  1.00 49.69  ?  102  ASN D CB  1 
ATOM   6802  C CG  . ASN D  1  102 ? -26.920 -16.255 16.127  1.00 48.37  ?  102  ASN D CG  1 
ATOM   6803  O OD1 . ASN D  1  102 ? -25.992 -16.208 15.326  1.00 48.32  ?  102  ASN D OD1 1 
ATOM   6804  N ND2 . ASN D  1  102 ? -27.947 -15.411 16.088  1.00 47.44  ?  102  ASN D ND2 1 
ATOM   6805  N N   . THR D  1  103 ? -30.230 -17.236 18.933  1.00 49.51  ?  103  THR D N   1 
ATOM   6806  C CA  . THR D  1  103 ? -31.638 -17.513 18.703  1.00 51.14  ?  103  THR D CA  1 
ATOM   6807  C C   . THR D  1  103 ? -32.447 -16.259 18.413  1.00 49.43  ?  103  THR D C   1 
ATOM   6808  O O   . THR D  1  103 ? -33.617 -16.370 18.026  1.00 50.45  ?  103  THR D O   1 
ATOM   6809  C CB  . THR D  1  103 ? -32.237 -18.235 19.912  1.00 52.54  ?  103  THR D CB  1 
ATOM   6810  O OG1 . THR D  1  103 ? -31.259 -19.113 20.477  1.00 53.41  ?  103  THR D OG1 1 
ATOM   6811  C CG2 . THR D  1  103 ? -33.437 -19.056 19.494  1.00 55.14  ?  103  THR D CG2 1 
ATOM   6812  N N   . GLY D  1  104 ? -31.864 -15.076 18.601  1.00 53.26  ?  104  GLY D N   1 
ATOM   6813  C CA  . GLY D  1  104 ? -32.609 -13.847 18.419  1.00 51.92  ?  104  GLY D CA  1 
ATOM   6814  C C   . GLY D  1  104 ? -33.439 -13.431 19.610  1.00 51.72  ?  104  GLY D C   1 
ATOM   6815  O O   . GLY D  1  104 ? -34.380 -12.650 19.452  1.00 51.38  ?  104  GLY D O   1 
ATOM   6816  N N   . ILE D  1  105 ? -33.114 -13.918 20.800  1.00 54.12  ?  105  ILE D N   1 
ATOM   6817  C CA  . ILE D  1  105 ? -33.905 -13.637 21.992  1.00 54.30  ?  105  ILE D CA  1 
ATOM   6818  C C   . ILE D  1  105 ? -33.577 -12.239 22.498  1.00 52.39  ?  105  ILE D C   1 
ATOM   6819  O O   . ILE D  1  105 ? -32.419 -11.806 22.472  1.00 50.95  ?  105  ILE D O   1 
ATOM   6820  C CB  . ILE D  1  105 ? -33.637 -14.703 23.071  1.00 55.35  ?  105  ILE D CB  1 
ATOM   6821  C CG1 . ILE D  1  105 ? -33.870 -16.103 22.504  1.00 57.71  ?  105  ILE D CG1 1 
ATOM   6822  C CG2 . ILE D  1  105 ? -34.514 -14.473 24.289  1.00 55.87  ?  105  ILE D CG2 1 
ATOM   6823  C CD1 . ILE D  1  105 ? -33.853 -17.190 23.547  1.00 59.21  ?  105  ILE D CD1 1 
ATOM   6824  N N   . GLU D  1  106 ? -34.604 -11.522 22.952  1.00 61.76  ?  106  GLU D N   1 
ATOM   6825  C CA  . GLU D  1  106 ? -34.445 -10.199 23.543  1.00 60.61  ?  106  GLU D CA  1 
ATOM   6826  C C   . GLU D  1  106 ? -35.173 -10.170 24.878  1.00 61.67  ?  106  GLU D C   1 
ATOM   6827  O O   . GLU D  1  106 ? -36.392 -10.366 24.921  1.00 62.85  ?  106  GLU D O   1 
ATOM   6828  C CB  . GLU D  1  106 ? -34.985 -9.116  22.607  1.00 59.91  ?  106  GLU D CB  1 
ATOM   6829  C CG  . GLU D  1  106 ? -34.681 -7.699  23.054  1.00 58.90  ?  106  GLU D CG  1 
ATOM   6830  C CD  . GLU D  1  106 ? -35.381 -6.658  22.198  1.00 58.37  ?  106  GLU D CD  1 
ATOM   6831  O OE1 . GLU D  1  106 ? -35.133 -6.627  20.973  1.00 57.73  ?  106  GLU D OE1 1 
ATOM   6832  O OE2 . GLU D  1  106 ? -36.168 -5.860  22.752  1.00 58.65  -1 106  GLU D OE2 1 
ATOM   6833  N N   . GLY D  1  107 ? -34.438 -9.924  25.962  1.00 51.16  ?  107  GLY D N   1 
ATOM   6834  C CA  . GLY D  1  107 ? -35.054 -9.923  27.274  1.00 52.45  ?  107  GLY D CA  1 
ATOM   6835  C C   . GLY D  1  107 ? -34.092 -9.795  28.437  1.00 52.51  ?  107  GLY D C   1 
ATOM   6836  O O   . GLY D  1  107 ? -33.100 -9.066  28.352  1.00 51.48  ?  107  GLY D O   1 
ATOM   6837  N N   . THR D  1  108 ? -34.382 -10.497 29.532  1.00 47.91  ?  108  THR D N   1 
ATOM   6838  C CA  . THR D  1  108 ? -33.626 -10.365 30.769  1.00 48.58  ?  108  THR D CA  1 
ATOM   6839  C C   . THR D  1  108 ? -33.683 -11.685 31.530  1.00 49.77  ?  108  THR D C   1 
ATOM   6840  O O   . THR D  1  108 ? -34.579 -12.503 31.318  1.00 50.50  ?  108  THR D O   1 
ATOM   6841  C CB  . THR D  1  108 ? -34.183 -9.192  31.589  1.00 49.80  ?  108  THR D CB  1 
ATOM   6842  O OG1 . THR D  1  108 ? -34.007 -7.985  30.840  1.00 48.59  ?  108  THR D OG1 1 
ATOM   6843  C CG2 . THR D  1  108 ? -33.488 -9.040  32.938  1.00 51.35  ?  108  THR D CG2 1 
ATOM   6844  N N   . PHE D  1  109 ? -32.700 -11.904 32.405  1.00 50.47  ?  109  PHE D N   1 
ATOM   6845  C CA  . PHE D  1  109 ? -32.683 -13.068 33.282  1.00 51.77  ?  109  PHE D CA  1 
ATOM   6846  C C   . PHE D  1  109 ? -33.407 -12.820 34.608  1.00 54.35  ?  109  PHE D C   1 
ATOM   6847  O O   . PHE D  1  109 ? -33.177 -13.553 35.577  1.00 55.87  ?  109  PHE D O   1 
ATOM   6848  C CB  . PHE D  1  109 ? -31.238 -13.509 33.542  1.00 51.03  ?  109  PHE D CB  1 
ATOM   6849  C CG  . PHE D  1  109 ? -30.442 -13.734 32.289  1.00 48.63  ?  109  PHE D CG  1 
ATOM   6850  C CD1 . PHE D  1  109 ? -30.944 -14.524 31.269  1.00 48.05  ?  109  PHE D CD1 1 
ATOM   6851  C CD2 . PHE D  1  109 ? -29.199 -13.144 32.123  1.00 47.39  ?  109  PHE D CD2 1 
ATOM   6852  C CE1 . PHE D  1  109 ? -30.222 -14.726 30.112  1.00 46.42  ?  109  PHE D CE1 1 
ATOM   6853  C CE2 . PHE D  1  109 ? -28.471 -13.345 30.967  1.00 45.35  ?  109  PHE D CE2 1 
ATOM   6854  C CZ  . PHE D  1  109 ? -28.983 -14.136 29.961  1.00 44.91  ?  109  PHE D CZ  1 
ATOM   6855  N N   . GLU D  1  110 ? -34.269 -11.800 34.674  1.00 58.20  ?  110  GLU D N   1 
ATOM   6856  C CA  . GLU D  1  110 ? -34.955 -11.494 35.927  1.00 60.79  ?  110  GLU D CA  1 
ATOM   6857  C C   . GLU D  1  110 ? -35.961 -12.577 36.291  1.00 62.07  ?  110  GLU D C   1 
ATOM   6858  O O   . GLU D  1  110 ? -36.050 -12.986 37.454  1.00 64.32  ?  110  GLU D O   1 
ATOM   6859  C CB  . GLU D  1  110 ? -35.646 -10.134 35.837  1.00 60.88  ?  110  GLU D CB  1 
ATOM   6860  C CG  . GLU D  1  110 ? -36.366 -9.728  37.116  1.00 63.54  ?  110  GLU D CG  1 
ATOM   6861  C CD  . GLU D  1  110 ? -35.523 -8.813  37.988  1.00 65.08  ?  110  GLU D CD  1 
ATOM   6862  O OE1 . GLU D  1  110 ? -34.675 -8.080  37.428  1.00 63.77  ?  110  GLU D OE1 1 
ATOM   6863  O OE2 . GLU D  1  110 ? -35.706 -8.825  39.228  1.00 67.84  -1 110  GLU D OE2 1 
ATOM   6864  N N   . ASP D  1  111 ? -36.724 -13.055 35.310  1.00 55.32  ?  111  ASP D N   1 
ATOM   6865  C CA  . ASP D  1  111 ? -37.670 -14.142 35.519  1.00 56.67  ?  111  ASP D CA  1 
ATOM   6866  C C   . ASP D  1  111 ? -37.130 -15.476 35.022  1.00 56.04  ?  111  ASP D C   1 
ATOM   6867  O O   . ASP D  1  111 ? -37.903 -16.345 34.607  1.00 56.76  ?  111  ASP D O   1 
ATOM   6868  C CB  . ASP D  1  111 ? -38.999 -13.813 34.849  1.00 56.74  ?  111  ASP D CB  1 
ATOM   6869  C CG  . ASP D  1  111 ? -39.764 -12.759 35.601  1.00 57.86  ?  111  ASP D CG  1 
ATOM   6870  O OD1 . ASP D  1  111 ? -40.121 -13.019 36.768  1.00 59.91  ?  111  ASP D OD1 1 
ATOM   6871  O OD2 . ASP D  1  111 ? -39.986 -11.669 35.037  1.00 56.77  -1 111  ASP D OD2 1 
ATOM   6872  N N   . PHE D  1  112 ? -35.817 -15.645 35.035  1.00 52.38  ?  112  PHE D N   1 
ATOM   6873  C CA  . PHE D  1  112 ? -35.233 -16.949 34.762  1.00 51.94  ?  112  PHE D CA  1 
ATOM   6874  C C   . PHE D  1  112 ? -35.588 -17.908 35.892  1.00 54.10  ?  112  PHE D C   1 
ATOM   6875  O O   . PHE D  1  112 ? -35.472 -17.541 37.067  1.00 55.58  ?  112  PHE D O   1 
ATOM   6876  C CB  . PHE D  1  112 ? -33.718 -16.845 34.606  1.00 50.18  ?  112  PHE D CB  1 
ATOM   6877  C CG  . PHE D  1  112 ? -33.093 -18.065 33.994  1.00 49.26  ?  112  PHE D CG  1 
ATOM   6878  C CD1 . PHE D  1  112 ? -33.294 -18.365 32.656  1.00 48.52  ?  112  PHE D CD1 1 
ATOM   6879  C CD2 . PHE D  1  112 ? -32.313 -18.917 34.756  1.00 49.57  ?  112  PHE D CD2 1 
ATOM   6880  C CE1 . PHE D  1  112 ? -32.727 -19.487 32.092  1.00 48.31  ?  112  PHE D CE1 1 
ATOM   6881  C CE2 . PHE D  1  112 ? -31.742 -20.039 34.197  1.00 48.84  ?  112  PHE D CE2 1 
ATOM   6882  C CZ  . PHE D  1  112 ? -31.949 -20.325 32.863  1.00 48.33  ?  112  PHE D CZ  1 
ATOM   6883  N N   . PRO D  1  113 ? -36.026 -19.124 35.592  1.00 51.15  ?  113  PRO D N   1 
ATOM   6884  C CA  . PRO D  1  113 ? -36.475 -20.031 36.668  1.00 53.34  ?  113  PRO D CA  1 
ATOM   6885  C C   . PRO D  1  113 ? -35.317 -20.721 37.379  1.00 53.21  ?  113  PRO D C   1 
ATOM   6886  O O   . PRO D  1  113 ? -35.101 -21.934 37.268  1.00 53.34  ?  113  PRO D O   1 
ATOM   6887  C CB  . PRO D  1  113 ? -37.370 -21.013 35.909  1.00 54.34  ?  113  PRO D CB  1 
ATOM   6888  C CG  . PRO D  1  113 ? -36.744 -21.097 34.553  1.00 52.66  ?  113  PRO D CG  1 
ATOM   6889  C CD  . PRO D  1  113 ? -36.196 -19.720 34.256  1.00 50.58  ?  113  PRO D CD  1 
ATOM   6890  N N   . PHE D  1  114 ? -34.571 -19.934 38.160  1.00 53.26  ?  114  PHE D N   1 
ATOM   6891  C CA  . PHE D  1  114 ? -33.416 -20.470 38.876  1.00 53.49  ?  114  PHE D CA  1 
ATOM   6892  C C   . PHE D  1  114 ? -33.817 -21.611 39.803  1.00 55.64  ?  114  PHE D C   1 
ATOM   6893  O O   . PHE D  1  114 ? -33.094 -22.609 39.923  1.00 55.18  ?  114  PHE D O   1 
ATOM   6894  C CB  . PHE D  1  114 ? -32.732 -19.359 39.673  1.00 54.66  ?  114  PHE D CB  1 
ATOM   6895  C CG  . PHE D  1  114 ? -32.220 -18.235 38.827  1.00 52.53  ?  114  PHE D CG  1 
ATOM   6896  C CD1 . PHE D  1  114 ? -31.028 -18.365 38.127  1.00 50.04  ?  114  PHE D CD1 1 
ATOM   6897  C CD2 . PHE D  1  114 ? -32.923 -17.048 38.729  1.00 53.02  ?  114  PHE D CD2 1 
ATOM   6898  C CE1 . PHE D  1  114 ? -30.550 -17.334 37.344  1.00 48.18  ?  114  PHE D CE1 1 
ATOM   6899  C CE2 . PHE D  1  114 ? -32.450 -16.012 37.942  1.00 51.11  ?  114  PHE D CE2 1 
ATOM   6900  C CZ  . PHE D  1  114 ? -31.262 -16.156 37.251  1.00 48.75  ?  114  PHE D CZ  1 
ATOM   6901  N N   . SER D  1  115 ? -34.971 -21.486 40.458  1.00 57.32  ?  115  SER D N   1 
ATOM   6902  C CA  . SER D  1  115 ? -35.427 -22.485 41.414  1.00 59.56  ?  115  SER D CA  1 
ATOM   6903  C C   . SER D  1  115 ? -35.949 -23.755 40.758  1.00 58.95  ?  115  SER D C   1 
ATOM   6904  O O   . SER D  1  115 ? -36.073 -24.775 41.443  1.00 60.29  ?  115  SER D O   1 
ATOM   6905  C CB  . SER D  1  115 ? -36.520 -21.892 42.304  1.00 62.34  ?  115  SER D CB  1 
ATOM   6906  O OG  . SER D  1  115 ? -36.028 -20.774 43.020  1.00 63.81  ?  115  SER D OG  1 
ATOM   6907  N N   . SER D  1  116 ? -36.227 -23.735 39.458  1.00 55.74  ?  116  SER D N   1 
ATOM   6908  C CA  . SER D  1  116 ? -36.939 -24.830 38.819  1.00 56.41  ?  116  SER D CA  1 
ATOM   6909  C C   . SER D  1  116 ? -36.040 -25.768 38.020  1.00 55.03  ?  116  SER D C   1 
ATOM   6910  O O   . SER D  1  116 ? -36.497 -26.851 37.637  1.00 56.22  ?  116  SER D O   1 
ATOM   6911  C CB  . SER D  1  116 ? -38.035 -24.275 37.900  1.00 56.85  ?  116  SER D CB  1 
ATOM   6912  O OG  . SER D  1  116 ? -38.671 -23.151 38.483  1.00 57.48  ?  116  SER D OG  1 
ATOM   6913  N N   . LEU D  1  117 ? -34.785 -25.396 37.762  1.00 55.25  ?  117  LEU D N   1 
ATOM   6914  C CA  . LEU D  1  117 ? -33.889 -26.162 36.892  1.00 53.88  ?  117  LEU D CA  1 
ATOM   6915  C C   . LEU D  1  117 ? -32.639 -26.609 37.644  1.00 52.93  ?  117  LEU D C   1 
ATOM   6916  O O   . LEU D  1  117 ? -31.518 -26.225 37.289  1.00 51.02  ?  117  LEU D O   1 
ATOM   6917  C CB  . LEU D  1  117 ? -33.501 -25.339 35.667  1.00 52.14  ?  117  LEU D CB  1 
ATOM   6918  C CG  . LEU D  1  117 ? -34.647 -24.623 34.968  1.00 53.01  ?  117  LEU D CG  1 
ATOM   6919  C CD1 . LEU D  1  117 ? -34.115 -23.848 33.778  1.00 51.23  ?  117  LEU D CD1 1 
ATOM   6920  C CD2 . LEU D  1  117 ? -35.698 -25.635 34.556  1.00 55.67  ?  117  LEU D CD2 1 
ATOM   6921  N N   . PRO D  1  118 ? -32.791 -27.447 38.675  1.00 54.57  ?  118  PRO D N   1 
ATOM   6922  C CA  . PRO D  1  118 ? -31.631 -27.781 39.512  1.00 54.04  ?  118  PRO D CA  1 
ATOM   6923  C C   . PRO D  1  118 ? -30.563 -28.584 38.794  1.00 52.31  ?  118  PRO D C   1 
ATOM   6924  O O   . PRO D  1  118 ? -29.427 -28.633 39.281  1.00 51.45  ?  118  PRO D O   1 
ATOM   6925  C CB  . PRO D  1  118 ? -32.252 -28.586 40.659  1.00 56.15  ?  118  PRO D CB  1 
ATOM   6926  C CG  . PRO D  1  118 ? -33.435 -29.232 40.038  1.00 57.15  ?  118  PRO D CG  1 
ATOM   6927  C CD  . PRO D  1  118 ? -33.982 -28.228 39.059  1.00 56.77  ?  118  PRO D CD  1 
ATOM   6928  N N   . ASN D  1  119 ? -30.876 -29.205 37.659  1.00 54.17  ?  119  ASN D N   1 
ATOM   6929  C CA  . ASN D  1  119 ? -29.968 -30.151 37.026  1.00 53.16  ?  119  ASN D CA  1 
ATOM   6930  C C   . ASN D  1  119 ? -29.237 -29.575 35.816  1.00 51.53  ?  119  ASN D C   1 
ATOM   6931  O O   . ASN D  1  119 ? -28.629 -30.335 35.056  1.00 51.12  ?  119  ASN D O   1 
ATOM   6932  C CB  . ASN D  1  119 ? -30.728 -31.422 36.637  1.00 54.76  ?  119  ASN D CB  1 
ATOM   6933  C CG  . ASN D  1  119 ? -31.104 -32.265 37.846  1.00 55.90  ?  119  ASN D CG  1 
ATOM   6934  O OD1 . ASN D  1  119 ? -30.321 -32.387 38.793  1.00 55.21  ?  119  ASN D OD1 1 
ATOM   6935  N ND2 . ASN D  1  119 ? -32.307 -32.847 37.818  1.00 57.84  ?  119  ASN D ND2 1 
ATOM   6936  N N   . LEU D  1  120 ? -29.275 -28.259 35.623  1.00 52.45  ?  120  LEU D N   1 
ATOM   6937  C CA  . LEU D  1  120 ? -28.555 -27.646 34.515  1.00 50.79  ?  120  LEU D CA  1 
ATOM   6938  C C   . LEU D  1  120 ? -27.062 -27.924 34.639  1.00 49.17  ?  120  LEU D C   1 
ATOM   6939  O O   . LEU D  1  120 ? -26.475 -27.766 35.713  1.00 48.85  ?  120  LEU D O   1 
ATOM   6940  C CB  . LEU D  1  120 ? -28.805 -26.139 34.489  1.00 49.92  ?  120  LEU D CB  1 
ATOM   6941  C CG  . LEU D  1  120 ? -30.155 -25.667 33.961  1.00 51.19  ?  120  LEU D CG  1 
ATOM   6942  C CD1 . LEU D  1  120 ? -30.228 -24.146 33.968  1.00 50.01  ?  120  LEU D CD1 1 
ATOM   6943  C CD2 . LEU D  1  120 ? -30.388 -26.214 32.571  1.00 52.08  ?  120  LEU D CD2 1 
ATOM   6944  N N   . THR D  1  121 ? -26.456 -28.370 33.537  1.00 49.96  ?  121  THR D N   1 
ATOM   6945  C CA  . THR D  1  121 ? -25.012 -28.564 33.465  1.00 48.42  ?  121  THR D CA  1 
ATOM   6946  C C   . THR D  1  121 ? -24.361 -27.894 32.262  1.00 47.11  ?  121  THR D C   1 
ATOM   6947  O O   . THR D  1  121 ? -23.134 -27.736 32.266  1.00 45.65  ?  121  THR D O   1 
ATOM   6948  C CB  . THR D  1  121 ? -24.662 -30.062 33.433  1.00 49.15  ?  121  THR D CB  1 
ATOM   6949  O OG1 . THR D  1  121 ? -25.017 -30.600 32.159  1.00 50.22  ?  121  THR D OG1 1 
ATOM   6950  C CG2 . THR D  1  121 ? -25.417 -30.831 34.508  1.00 50.54  ?  121  THR D CG2 1 
ATOM   6951  N N   . PHE D  1  122 ? -25.124 -27.510 31.237  1.00 49.82  ?  122  PHE D N   1 
ATOM   6952  C CA  . PHE D  1  122 ? -24.609 -26.805 30.066  1.00 48.92  ?  122  PHE D CA  1 
ATOM   6953  C C   . PHE D  1  122 ? -25.549 -25.651 29.757  1.00 49.02  ?  122  PHE D C   1 
ATOM   6954  O O   . PHE D  1  122 ? -26.722 -25.877 29.446  1.00 51.10  ?  122  PHE D O   1 
ATOM   6955  C CB  . PHE D  1  122 ? -24.505 -27.747 28.858  1.00 50.62  ?  122  PHE D CB  1 
ATOM   6956  C CG  . PHE D  1  122 ? -24.033 -27.077 27.579  1.00 50.38  ?  122  PHE D CG  1 
ATOM   6957  C CD1 . PHE D  1  122 ? -24.907 -26.340 26.780  1.00 51.66  ?  122  PHE D CD1 1 
ATOM   6958  C CD2 . PHE D  1  122 ? -22.714 -27.201 27.166  1.00 49.19  ?  122  PHE D CD2 1 
ATOM   6959  C CE1 . PHE D  1  122 ? -24.465 -25.730 25.605  1.00 51.77  ?  122  PHE D CE1 1 
ATOM   6960  C CE2 . PHE D  1  122 ? -22.269 -26.597 25.987  1.00 49.23  ?  122  PHE D CE2 1 
ATOM   6961  C CZ  . PHE D  1  122 ? -23.145 -25.862 25.210  1.00 50.56  ?  122  PHE D CZ  1 
ATOM   6962  N N   . VAL D  1  123 ? -25.033 -24.424 29.788  1.00 46.51  ?  123  VAL D N   1 
ATOM   6963  C CA  . VAL D  1  123 ? -25.835 -23.241 29.494  1.00 46.30  ?  123  VAL D CA  1 
ATOM   6964  C C   . VAL D  1  123 ? -25.063 -22.362 28.520  1.00 44.74  ?  123  VAL D C   1 
ATOM   6965  O O   . VAL D  1  123 ? -23.956 -21.909 28.837  1.00 42.85  ?  123  VAL D O   1 
ATOM   6966  C CB  . VAL D  1  123 ? -26.190 -22.447 30.764  1.00 45.69  ?  123  VAL D CB  1 
ATOM   6967  C CG1 . VAL D  1  123 ? -26.867 -21.135 30.395  1.00 45.26  ?  123  VAL D CG1 1 
ATOM   6968  C CG2 . VAL D  1  123 ? -27.095 -23.262 31.659  1.00 47.58  ?  123  VAL D CG2 1 
ATOM   6969  N N   . ASP D  1  124 ? -25.655 -22.103 27.349  1.00 46.78  ?  124  ASP D N   1 
ATOM   6970  C CA  . ASP D  1  124 ? -25.118 -21.153 26.374  1.00 45.56  ?  124  ASP D CA  1 
ATOM   6971  C C   . ASP D  1  124 ? -26.257 -20.249 25.911  1.00 46.07  ?  124  ASP D C   1 
ATOM   6972  O O   . ASP D  1  124 ? -27.146 -20.687 25.172  1.00 48.59  ?  124  ASP D O   1 
ATOM   6973  C CB  . ASP D  1  124 ? -24.465 -21.866 25.181  1.00 46.98  ?  124  ASP D CB  1 
ATOM   6974  C CG  . ASP D  1  124 ? -23.657 -20.909 24.278  1.00 45.51  ?  124  ASP D CG  1 
ATOM   6975  O OD1 . ASP D  1  124 ? -24.102 -19.761 24.047  1.00 44.42  ?  124  ASP D OD1 1 
ATOM   6976  O OD2 . ASP D  1  124 ? -22.571 -21.302 23.786  1.00 45.48  -1 124  ASP D OD2 1 
ATOM   6977  N N   . LEU D  1  125 ? -26.218 -18.985 26.337  1.00 45.31  ?  125  LEU D N   1 
ATOM   6978  C CA  . LEU D  1  125 ? -27.182 -17.976 25.912  1.00 45.37  ?  125  LEU D CA  1 
ATOM   6979  C C   . LEU D  1  125 ? -26.518 -16.865 25.101  1.00 43.64  ?  125  LEU D C   1 
ATOM   6980  O O   . LEU D  1  125 ? -27.054 -15.752 25.008  1.00 43.03  ?  125  LEU D O   1 
ATOM   6981  C CB  . LEU D  1  125 ? -27.911 -17.397 27.126  1.00 45.23  ?  125  LEU D CB  1 
ATOM   6982  C CG  . LEU D  1  125 ? -28.568 -18.472 27.986  1.00 46.99  ?  125  LEU D CG  1 
ATOM   6983  C CD1 . LEU D  1  125 ? -29.001 -17.895 29.309  1.00 47.02  ?  125  LEU D CD1 1 
ATOM   6984  C CD2 . LEU D  1  125 ? -29.746 -19.089 27.248  1.00 49.39  ?  125  LEU D CD2 1 
ATOM   6985  N N   . SER D  1  126 ? -25.368 -17.157 24.499  1.00 46.46  ?  126  SER D N   1 
ATOM   6986  C CA  . SER D  1  126 ? -24.563 -16.148 23.831  1.00 44.80  ?  126  SER D CA  1 
ATOM   6987  C C   . SER D  1  126 ? -25.195 -15.701 22.512  1.00 45.60  ?  126  SER D C   1 
ATOM   6988  O O   . SER D  1  126 ? -26.046 -16.381 21.931  1.00 47.78  ?  126  SER D O   1 
ATOM   6989  C CB  . SER D  1  126 ? -23.156 -16.685 23.587  1.00 44.22  ?  126  SER D CB  1 
ATOM   6990  O OG  . SER D  1  126 ? -23.209 -17.860 22.798  1.00 46.47  ?  126  SER D OG  1 
ATOM   6991  N N   . MET D  1  127 ? -24.753 -14.529 22.045  1.00 45.15  ?  127  MET D N   1 
ATOM   6992  C CA  . MET D  1  127 ? -25.181 -13.951 20.772  1.00 45.54  ?  127  MET D CA  1 
ATOM   6993  C C   . MET D  1  127 ? -26.691 -13.718 20.730  1.00 46.55  ?  127  MET D C   1 
ATOM   6994  O O   . MET D  1  127 ? -27.396 -14.183 19.833  1.00 48.22  ?  127  MET D O   1 
ATOM   6995  C CB  . MET D  1  127 ? -24.734 -14.824 19.598  1.00 47.15  ?  127  MET D CB  1 
ATOM   6996  C CG  . MET D  1  127 ? -23.267 -14.681 19.260  1.00 46.09  ?  127  MET D CG  1 
ATOM   6997  S SD  . MET D  1  127 ? -22.900 -15.390 17.649  1.00 48.59  ?  127  MET D SD  1 
ATOM   6998  C CE  . MET D  1  127 ? -22.863 -17.137 18.038  1.00 51.36  ?  127  MET D CE  1 
ATOM   6999  N N   . ASN D  1  128 ? -27.170 -12.967 21.720  1.00 45.72  ?  128  ASN D N   1 
ATOM   7000  C CA  . ASN D  1  128 ? -28.572 -12.571 21.833  1.00 46.53  ?  128  ASN D CA  1 
ATOM   7001  C C   . ASN D  1  128 ? -28.610 -11.129 22.327  1.00 45.29  ?  128  ASN D C   1 
ATOM   7002  O O   . ASN D  1  128 ? -27.591 -10.430 22.348  1.00 44.00  ?  128  ASN D O   1 
ATOM   7003  C CB  . ASN D  1  128 ? -29.344 -13.524 22.755  1.00 48.02  ?  128  ASN D CB  1 
ATOM   7004  C CG  . ASN D  1  128 ? -29.551 -14.888 22.134  1.00 50.03  ?  128  ASN D CG  1 
ATOM   7005  O OD1 . ASN D  1  128 ? -30.274 -15.025 21.149  1.00 51.28  ?  128  ASN D OD1 1 
ATOM   7006  N ND2 . ASN D  1  128 ? -28.917 -15.906 22.707  1.00 50.56  ?  128  ASN D ND2 1 
ATOM   7007  N N   . ARG D  1  129 ? -29.789 -10.672 22.731  1.00 54.79  ?  129  ARG D N   1 
ATOM   7008  C CA  . ARG D  1  129 ? -29.978 -9.312  23.214  1.00 54.24  ?  129  ARG D CA  1 
ATOM   7009  C C   . ARG D  1  129 ? -30.482 -9.328  24.651  1.00 55.16  ?  129  ARG D C   1 
ATOM   7010  O O   . ARG D  1  129 ? -31.425 -8.621  25.010  1.00 55.78  ?  129  ARG D O   1 
ATOM   7011  C CB  . ARG D  1  129 ? -30.930 -8.535  22.311  1.00 54.29  ?  129  ARG D CB  1 
ATOM   7012  C CG  . ARG D  1  129 ? -30.707 -8.781  20.837  1.00 54.00  ?  129  ARG D CG  1 
ATOM   7013  C CD  . ARG D  1  129 ? -31.262 -7.655  19.999  1.00 53.52  ?  129  ARG D CD  1 
ATOM   7014  N NE  . ARG D  1  129 ? -30.540 -6.409  20.226  1.00 52.42  ?  129  ARG D NE  1 
ATOM   7015  C CZ  . ARG D  1  129 ? -31.095 -5.290  20.677  1.00 52.38  ?  129  ARG D CZ  1 
ATOM   7016  N NH1 . ARG D  1  129 ? -32.388 -5.228  20.969  1.00 53.17  ?  129  ARG D NH1 1 
ATOM   7017  N NH2 . ARG D  1  129 ? -30.334 -4.207  20.837  1.00 51.69  ?  129  ARG D NH2 1 
ATOM   7018  N N   . PHE D  1  130 ? -29.877 -10.180 25.476  1.00 47.26  ?  130  PHE D N   1 
ATOM   7019  C CA  . PHE D  1  130 ? -30.177 -10.190 26.901  1.00 48.33  ?  130  PHE D CA  1 
ATOM   7020  C C   . PHE D  1  130 ? -29.529 -8.984  27.570  1.00 48.20  ?  130  PHE D C   1 
ATOM   7021  O O   . PHE D  1  130 ? -28.363 -8.666  27.313  1.00 47.17  ?  130  PHE D O   1 
ATOM   7022  C CB  . PHE D  1  130 ? -29.676 -11.484 27.551  1.00 48.70  ?  130  PHE D CB  1 
ATOM   7023  C CG  . PHE D  1  130 ? -30.514 -12.688 27.230  1.00 49.74  ?  130  PHE D CG  1 
ATOM   7024  C CD1 . PHE D  1  130 ? -31.816 -12.785 27.690  1.00 51.27  ?  130  PHE D CD1 1 
ATOM   7025  C CD2 . PHE D  1  130 ? -29.998 -13.724 26.469  1.00 49.58  ?  130  PHE D CD2 1 
ATOM   7026  C CE1 . PHE D  1  130 ? -32.592 -13.890 27.390  1.00 52.62  ?  130  PHE D CE1 1 
ATOM   7027  C CE2 . PHE D  1  130 ? -30.767 -14.834 26.166  1.00 51.21  ?  130  PHE D CE2 1 
ATOM   7028  C CZ  . PHE D  1  130 ? -32.065 -14.918 26.629  1.00 52.75  ?  130  PHE D CZ  1 
ATOM   7029  N N   . SER D  1  131 ? -30.286 -8.313  28.429  1.00 46.10  ?  131  SER D N   1 
ATOM   7030  C CA  . SER D  1  131 ? -29.814 -7.139  29.143  1.00 46.76  ?  131  SER D CA  1 
ATOM   7031  C C   . SER D  1  131 ? -30.131 -7.295  30.624  1.00 48.92  ?  131  SER D C   1 
ATOM   7032  O O   . SER D  1  131 ? -30.792 -8.249  31.046  1.00 49.71  ?  131  SER D O   1 
ATOM   7033  C CB  . SER D  1  131 ? -30.445 -5.863  28.580  1.00 46.51  ?  131  SER D CB  1 
ATOM   7034  O OG  . SER D  1  131 ? -31.851 -5.903  28.737  1.00 47.35  ?  131  SER D OG  1 
ATOM   7035  N N   . GLY D  1  132 ? -29.664 -6.336  31.416  1.00 45.25  ?  132  GLY D N   1 
ATOM   7036  C CA  . GLY D  1  132 ? -29.808 -6.427  32.854  1.00 46.67  ?  132  GLY D CA  1 
ATOM   7037  C C   . GLY D  1  132 ? -28.512 -6.826  33.524  1.00 46.74  ?  132  GLY D C   1 
ATOM   7038  O O   . GLY D  1  132 ? -27.435 -6.432  33.066  1.00 46.07  ?  132  GLY D O   1 
ATOM   7039  N N   . THR D  1  133 ? -28.593 -7.607  34.598  1.00 45.42  ?  133  THR D N   1 
ATOM   7040  C CA  . THR D  1  133 ? -27.418 -7.961  35.381  1.00 46.91  ?  133  THR D CA  1 
ATOM   7041  C C   . THR D  1  133 ? -27.326 -9.477  35.541  1.00 46.41  ?  133  THR D C   1 
ATOM   7042  O O   . THR D  1  133 ? -28.259 -10.221 35.224  1.00 45.50  ?  133  THR D O   1 
ATOM   7043  C CB  . THR D  1  133 ? -27.436 -7.264  36.751  1.00 50.85  ?  133  THR D CB  1 
ATOM   7044  O OG1 . THR D  1  133 ? -28.701 -7.478  37.383  1.00 52.41  ?  133  THR D OG1 1 
ATOM   7045  C CG2 . THR D  1  133 ? -27.218 -5.771  36.591  1.00 51.19  ?  133  THR D CG2 1 
ATOM   7046  N N   . ILE D  1  134 ? -26.165 -9.930  36.008  1.00 48.69  ?  134  ILE D N   1 
ATOM   7047  C CA  . ILE D  1  134 ? -25.933 -11.342 36.301  1.00 48.42  ?  134  ILE D CA  1 
ATOM   7048  C C   . ILE D  1  134 ? -26.356 -11.585 37.744  1.00 52.35  ?  134  ILE D C   1 
ATOM   7049  O O   . ILE D  1  134 ? -25.710 -11.106 38.681  1.00 55.57  ?  134  ILE D O   1 
ATOM   7050  C CB  . ILE D  1  134 ? -24.467 -11.735 36.075  1.00 47.24  ?  134  ILE D CB  1 
ATOM   7051  C CG1 . ILE D  1  134 ? -24.046 -11.417 34.640  1.00 43.72  ?  134  ILE D CG1 1 
ATOM   7052  C CG2 . ILE D  1  134 ? -24.245 -13.218 36.388  1.00 46.80  ?  134  ILE D CG2 1 
ATOM   7053  C CD1 . ILE D  1  134 ? -22.584 -11.666 34.370  1.00 42.57  ?  134  ILE D CD1 1 
ATOM   7054  N N   . SER D  1  135 ? -27.438 -12.334 37.926  1.00 49.27  ?  135  SER D N   1 
ATOM   7055  C CA  . SER D  1  135 ? -27.983 -12.536 39.258  1.00 53.20  ?  135  SER D CA  1 
ATOM   7056  C C   . SER D  1  135 ? -27.066 -13.423 40.096  1.00 55.00  ?  135  SER D C   1 
ATOM   7057  O O   . SER D  1  135 ? -26.394 -14.310 39.569  1.00 52.38  ?  135  SER D O   1 
ATOM   7058  C CB  . SER D  1  135 ? -29.360 -13.182 39.176  1.00 52.90  ?  135  SER D CB  1 
ATOM   7059  O OG  . SER D  1  135 ? -29.876 -13.422 40.472  1.00 56.84  ?  135  SER D OG  1 
ATOM   7060  N N   . PRO D  1  136 ? -27.030 -13.211 41.412  1.00 52.11  ?  136  PRO D N   1 
ATOM   7061  C CA  . PRO D  1  136 ? -26.322 -14.162 42.282  1.00 52.50  ?  136  PRO D CA  1 
ATOM   7062  C C   . PRO D  1  136 ? -26.875 -15.576 42.206  1.00 52.05  ?  136  PRO D C   1 
ATOM   7063  O O   . PRO D  1  136 ? -26.156 -16.522 42.559  1.00 52.08  ?  136  PRO D O   1 
ATOM   7064  C CB  . PRO D  1  136 ? -26.509 -13.560 43.682  1.00 58.15  ?  136  PRO D CB  1 
ATOM   7065  C CG  . PRO D  1  136 ? -26.726 -12.106 43.435  1.00 58.45  ?  136  PRO D CG  1 
ATOM   7066  C CD  . PRO D  1  136 ? -27.501 -12.030 42.153  1.00 53.52  ?  136  PRO D CD  1 
ATOM   7067  N N   . GLU D  1  137 ? -28.128 -15.740 41.757  1.00 59.38  ?  137  GLU D N   1 
ATOM   7068  C CA  . GLU D  1  137 ? -28.760 -17.057 41.683  1.00 58.27  ?  137  GLU D CA  1 
ATOM   7069  C C   . GLU D  1  137 ? -28.012 -18.001 40.749  1.00 54.32  ?  137  GLU D C   1 
ATOM   7070  O O   . GLU D  1  137 ? -28.097 -19.225 40.910  1.00 54.03  ?  137  GLU D O   1 
ATOM   7071  C CB  . GLU D  1  137 ? -30.214 -16.928 41.225  1.00 57.76  ?  137  GLU D CB  1 
ATOM   7072  C CG  . GLU D  1  137 ? -31.049 -15.990 42.057  1.00 61.35  ?  137  GLU D CG  1 
ATOM   7073  C CD  . GLU D  1  137 ? -31.630 -16.665 43.273  1.00 65.07  ?  137  GLU D CD  1 
ATOM   7074  O OE1 . GLU D  1  137 ? -30.852 -16.947 44.212  1.00 67.33  ?  137  GLU D OE1 1 
ATOM   7075  O OE2 . GLU D  1  137 ? -32.856 -16.924 43.284  1.00 65.65  -1 137  GLU D OE2 1 
ATOM   7076  N N   . TRP D  1  138 ? -27.290 -17.459 39.763  1.00 53.63  ?  138  TRP D N   1 
ATOM   7077  C CA  . TRP D  1  138 ? -26.584 -18.310 38.813  1.00 50.19  ?  138  TRP D CA  1 
ATOM   7078  C C   . TRP D  1  138 ? -25.627 -19.261 39.521  1.00 50.80  ?  138  TRP D C   1 
ATOM   7079  O O   . TRP D  1  138 ? -25.325 -20.340 38.996  1.00 48.82  ?  138  TRP D O   1 
ATOM   7080  C CB  . TRP D  1  138 ? -25.823 -17.452 37.804  1.00 47.70  ?  138  TRP D CB  1 
ATOM   7081  C CG  . TRP D  1  138 ? -26.688 -16.830 36.755  1.00 46.11  ?  138  TRP D CG  1 
ATOM   7082  C CD1 . TRP D  1  138 ? -27.043 -15.516 36.661  1.00 46.70  ?  138  TRP D CD1 1 
ATOM   7083  C CD2 . TRP D  1  138 ? -27.300 -17.492 35.640  1.00 44.13  ?  138  TRP D CD2 1 
ATOM   7084  N NE1 . TRP D  1  138 ? -27.844 -15.318 35.561  1.00 44.89  ?  138  TRP D NE1 1 
ATOM   7085  C CE2 . TRP D  1  138 ? -28.016 -16.515 34.917  1.00 43.55  ?  138  TRP D CE2 1 
ATOM   7086  C CE3 . TRP D  1  138 ? -27.316 -18.815 35.185  1.00 43.30  ?  138  TRP D CE3 1 
ATOM   7087  C CZ2 . TRP D  1  138 ? -28.741 -16.820 33.765  1.00 42.39  ?  138  TRP D CZ2 1 
ATOM   7088  C CZ3 . TRP D  1  138 ? -28.034 -19.115 34.041  1.00 42.44  ?  138  TRP D CZ3 1 
ATOM   7089  C CH2 . TRP D  1  138 ? -28.736 -18.122 33.344  1.00 42.09  ?  138  TRP D CH2 1 
ATOM   7090  N N   . GLY D  1  139 ? -25.164 -18.897 40.720  1.00 53.28  ?  139  GLY D N   1 
ATOM   7091  C CA  . GLY D  1  139 ? -24.271 -19.728 41.500  1.00 54.15  ?  139  GLY D CA  1 
ATOM   7092  C C   . GLY D  1  139 ? -24.922 -20.891 42.208  1.00 55.58  ?  139  GLY D C   1 
ATOM   7093  O O   . GLY D  1  139 ? -24.247 -21.626 42.937  1.00 56.40  ?  139  GLY D O   1 
ATOM   7094  N N   . ARG D  1  140 ? -26.224 -21.088 42.011  1.00 56.30  ?  140  ARG D N   1 
ATOM   7095  C CA  . ARG D  1  140 ? -26.937 -22.186 42.645  1.00 57.85  ?  140  ARG D CA  1 
ATOM   7096  C C   . ARG D  1  140 ? -26.958 -23.457 41.807  1.00 55.15  ?  140  ARG D C   1 
ATOM   7097  O O   . ARG D  1  140 ? -27.275 -24.522 42.346  1.00 56.15  ?  140  ARG D O   1 
ATOM   7098  C CB  . ARG D  1  140 ? -28.374 -21.768 42.968  1.00 60.19  ?  140  ARG D CB  1 
ATOM   7099  C CG  . ARG D  1  140 ? -28.472 -20.620 43.965  1.00 63.93  ?  140  ARG D CG  1 
ATOM   7100  C CD  . ARG D  1  140 ? -29.753 -20.695 44.788  1.00 67.18  ?  140  ARG D CD  1 
ATOM   7101  N NE  . ARG D  1  140 ? -30.940 -20.366 44.003  1.00 66.07  ?  140  ARG D NE  1 
ATOM   7102  C CZ  . ARG D  1  140 ? -32.055 -21.086 43.991  1.00 66.14  ?  140  ARG D CZ  1 
ATOM   7103  N NH1 . ARG D  1  140 ? -32.173 -22.192 44.711  1.00 67.17  ?  140  ARG D NH1 1 
ATOM   7104  N NH2 . ARG D  1  140 ? -33.078 -20.687 43.238  1.00 65.04  ?  140  ARG D NH2 1 
ATOM   7105  N N   . PHE D  1  141 ? -26.623 -23.384 40.516  1.00 54.68  ?  141  PHE D N   1 
ATOM   7106  C CA  . PHE D  1  141 ? -26.635 -24.562 39.646  1.00 52.80  ?  141  PHE D CA  1 
ATOM   7107  C C   . PHE D  1  141 ? -25.394 -25.400 39.951  1.00 52.18  ?  141  PHE D C   1 
ATOM   7108  O O   . PHE D  1  141 ? -24.355 -25.309 39.293  1.00 50.21  ?  141  PHE D O   1 
ATOM   7109  C CB  . PHE D  1  141 ? -26.693 -24.146 38.183  1.00 50.37  ?  141  PHE D CB  1 
ATOM   7110  C CG  . PHE D  1  141 ? -27.945 -23.411 37.816  1.00 50.88  ?  141  PHE D CG  1 
ATOM   7111  C CD1 . PHE D  1  141 ? -29.173 -24.052 37.843  1.00 52.27  ?  141  PHE D CD1 1 
ATOM   7112  C CD2 . PHE D  1  141 ? -27.900 -22.079 37.446  1.00 50.07  ?  141  PHE D CD2 1 
ATOM   7113  C CE1 . PHE D  1  141 ? -30.338 -23.376 37.503  1.00 52.86  ?  141  PHE D CE1 1 
ATOM   7114  C CE2 . PHE D  1  141 ? -29.062 -21.395 37.105  1.00 50.55  ?  141  PHE D CE2 1 
ATOM   7115  C CZ  . PHE D  1  141 ? -30.282 -22.047 37.135  1.00 51.94  ?  141  PHE D CZ  1 
ATOM   7116  N N   . SER D  1  142 ? -25.519 -26.243 40.980  1.00 52.97  ?  142  SER D N   1 
ATOM   7117  C CA  . SER D  1  142 ? -24.372 -26.975 41.505  1.00 52.63  ?  142  SER D CA  1 
ATOM   7118  C C   . SER D  1  142 ? -23.804 -27.982 40.515  1.00 50.38  ?  142  SER D C   1 
ATOM   7119  O O   . SER D  1  142 ? -22.689 -28.476 40.725  1.00 49.60  ?  142  SER D O   1 
ATOM   7120  C CB  . SER D  1  142 ? -24.756 -27.694 42.795  1.00 54.76  ?  142  SER D CB  1 
ATOM   7121  O OG  . SER D  1  142 ? -25.741 -28.679 42.543  1.00 54.82  ?  142  SER D OG  1 
ATOM   7122  N N   . LYS D  1  143 ? -24.541 -28.318 39.462  1.00 50.69  ?  143  LYS D N   1 
ATOM   7123  C CA  . LYS D  1  143 ? -24.057 -29.260 38.466  1.00 49.28  ?  143  LYS D CA  1 
ATOM   7124  C C   . LYS D  1  143 ? -23.496 -28.577 37.229  1.00 47.52  ?  143  LYS D C   1 
ATOM   7125  O O   . LYS D  1  143 ? -23.059 -29.269 36.306  1.00 46.71  ?  143  LYS D O   1 
ATOM   7126  C CB  . LYS D  1  143 ? -25.178 -30.220 38.061  1.00 50.22  ?  143  LYS D CB  1 
ATOM   7127  C CG  . LYS D  1  143 ? -25.618 -31.169 39.160  1.00 51.67  ?  143  LYS D CG  1 
ATOM   7128  C CD  . LYS D  1  143 ? -26.630 -32.163 38.631  1.00 52.59  ?  143  LYS D CD  1 
ATOM   7129  C CE  . LYS D  1  143 ? -26.956 -33.210 39.668  1.00 53.76  ?  143  LYS D CE  1 
ATOM   7130  N NZ  . LYS D  1  143 ? -27.868 -34.247 39.120  1.00 54.71  ?  143  LYS D NZ  1 
ATOM   7131  N N   . LEU D  1  144 ? -23.490 -27.244 37.195  1.00 50.73  ?  144  LEU D N   1 
ATOM   7132  C CA  . LEU D  1  144 ? -23.104 -26.509 35.997  1.00 48.96  ?  144  LEU D CA  1 
ATOM   7133  C C   . LEU D  1  144 ? -21.624 -26.715 35.691  1.00 47.58  ?  144  LEU D C   1 
ATOM   7134  O O   . LEU D  1  144 ? -20.770 -26.555 36.570  1.00 47.71  ?  144  LEU D O   1 
ATOM   7135  C CB  . LEU D  1  144 ? -23.407 -25.022 36.176  1.00 48.79  ?  144  LEU D CB  1 
ATOM   7136  C CG  . LEU D  1  144 ? -23.416 -24.161 34.912  1.00 47.14  ?  144  LEU D CG  1 
ATOM   7137  C CD1 . LEU D  1  144 ? -24.534 -24.589 33.980  1.00 47.64  ?  144  LEU D CD1 1 
ATOM   7138  C CD2 . LEU D  1  144 ? -23.532 -22.679 35.254  1.00 47.03  ?  144  LEU D CD2 1 
ATOM   7139  N N   . GLU D  1  145 ? -21.327 -27.089 34.443  1.00 49.05  ?  145  GLU D N   1 
ATOM   7140  C CA  . GLU D  1  145 ? -19.961 -27.266 33.963  1.00 47.82  ?  145  GLU D CA  1 
ATOM   7141  C C   . GLU D  1  145 ? -19.564 -26.288 32.867  1.00 46.39  ?  145  GLU D C   1 
ATOM   7142  O O   . GLU D  1  145 ? -18.377 -25.988 32.735  1.00 45.31  ?  145  GLU D O   1 
ATOM   7143  C CB  . GLU D  1  145 ? -19.755 -28.696 33.441  1.00 48.34  ?  145  GLU D CB  1 
ATOM   7144  C CG  . GLU D  1  145 ? -20.367 -29.767 34.320  1.00 49.70  ?  145  GLU D CG  1 
ATOM   7145  C CD  . GLU D  1  145 ? -20.140 -31.172 33.789  1.00 50.12  ?  145  GLU D CD  1 
ATOM   7146  O OE1 . GLU D  1  145 ? -20.031 -31.337 32.555  1.00 50.12  ?  145  GLU D OE1 1 
ATOM   7147  O OE2 . GLU D  1  145 ? -20.087 -32.116 34.607  1.00 50.57  -1 145  GLU D OE2 1 
ATOM   7148  N N   . TYR D  1  146 ? -20.521 -25.787 32.086  1.00 43.25  ?  146  TYR D N   1 
ATOM   7149  C CA  . TYR D  1  146 ? -20.270 -24.878 30.972  1.00 42.09  ?  146  TYR D CA  1 
ATOM   7150  C C   . TYR D  1  146 ? -21.218 -23.693 31.102  1.00 41.92  ?  146  TYR D C   1 
ATOM   7151  O O   . TYR D  1  146 ? -22.441 -23.873 31.104  1.00 43.14  ?  146  TYR D O   1 
ATOM   7152  C CB  . TYR D  1  146 ? -20.478 -25.600 29.636  1.00 43.02  ?  146  TYR D CB  1 
ATOM   7153  C CG  . TYR D  1  146 ? -20.042 -24.829 28.412  1.00 42.25  ?  146  TYR D CG  1 
ATOM   7154  C CD1 . TYR D  1  146 ? -18.730 -24.883 27.964  1.00 41.35  ?  146  TYR D CD1 1 
ATOM   7155  C CD2 . TYR D  1  146 ? -20.947 -24.060 27.696  1.00 42.66  ?  146  TYR D CD2 1 
ATOM   7156  C CE1 . TYR D  1  146 ? -18.330 -24.185 26.846  1.00 40.88  ?  146  TYR D CE1 1 
ATOM   7157  C CE2 . TYR D  1  146 ? -20.559 -23.359 26.576  1.00 42.23  ?  146  TYR D CE2 1 
ATOM   7158  C CZ  . TYR D  1  146 ? -19.250 -23.424 26.155  1.00 41.35  ?  146  TYR D CZ  1 
ATOM   7159  O OH  . TYR D  1  146 ? -18.870 -22.717 25.037  1.00 41.12  ?  146  TYR D OH  1 
ATOM   7160  N N   . PHE D  1  147 ? -20.662 -22.487 31.208  1.00 42.34  ?  147  PHE D N   1 
ATOM   7161  C CA  . PHE D  1  147 ? -21.445 -21.280 31.466  1.00 42.31  ?  147  PHE D CA  1 
ATOM   7162  C C   . PHE D  1  147 ? -21.030 -20.218 30.457  1.00 40.87  ?  147  PHE D C   1 
ATOM   7163  O O   . PHE D  1  147 ? -19.888 -19.752 30.485  1.00 39.87  ?  147  PHE D O   1 
ATOM   7164  C CB  . PHE D  1  147 ? -21.233 -20.795 32.906  1.00 43.08  ?  147  PHE D CB  1 
ATOM   7165  C CG  . PHE D  1  147 ? -22.235 -19.768 33.361  1.00 44.00  ?  147  PHE D CG  1 
ATOM   7166  C CD1 . PHE D  1  147 ? -23.541 -19.806 32.905  1.00 44.46  ?  147  PHE D CD1 1 
ATOM   7167  C CD2 . PHE D  1  147 ? -21.867 -18.759 34.245  1.00 44.94  ?  147  PHE D CD2 1 
ATOM   7168  C CE1 . PHE D  1  147 ? -24.463 -18.855 33.317  1.00 45.43  ?  147  PHE D CE1 1 
ATOM   7169  C CE2 . PHE D  1  147 ? -22.786 -17.809 34.661  1.00 46.31  ?  147  PHE D CE2 1 
ATOM   7170  C CZ  . PHE D  1  147 ? -24.085 -17.858 34.195  1.00 46.35  ?  147  PHE D CZ  1 
ATOM   7171  N N   . ASP D  1  148 ? -21.950 -19.826 29.573  1.00 45.04  ?  148  ASP D N   1 
ATOM   7172  C CA  . ASP D  1  148 ? -21.634 -18.879 28.505  1.00 43.90  ?  148  ASP D CA  1 
ATOM   7173  C C   . ASP D  1  148 ? -22.757 -17.863 28.368  1.00 44.14  ?  148  ASP D C   1 
ATOM   7174  O O   . ASP D  1  148 ? -23.866 -18.217 27.956  1.00 45.32  ?  148  ASP D O   1 
ATOM   7175  C CB  . ASP D  1  148 ? -21.411 -19.606 27.171  1.00 44.34  ?  148  ASP D CB  1 
ATOM   7176  C CG  . ASP D  1  148 ? -20.688 -18.736 26.131  1.00 43.19  ?  148  ASP D CG  1 
ATOM   7177  O OD1 . ASP D  1  148 ? -20.761 -17.487 26.221  1.00 42.19  ?  148  ASP D OD1 1 
ATOM   7178  O OD2 . ASP D  1  148 ? -20.034 -19.309 25.222  1.00 43.60  -1 148  ASP D OD2 1 
ATOM   7179  N N   . LEU D  1  149 ? -22.449 -16.595 28.660  1.00 42.06  ?  149  LEU D N   1 
ATOM   7180  C CA  . LEU D  1  149 ? -23.375 -15.481 28.481  1.00 42.27  ?  149  LEU D CA  1 
ATOM   7181  C C   . LEU D  1  149 ? -22.801 -14.411 27.553  1.00 41.02  ?  149  LEU D C   1 
ATOM   7182  O O   . LEU D  1  149 ? -23.239 -13.255 27.594  1.00 41.13  ?  149  LEU D O   1 
ATOM   7183  C CB  . LEU D  1  149 ? -23.736 -14.858 29.832  1.00 43.44  ?  149  LEU D CB  1 
ATOM   7184  C CG  . LEU D  1  149 ? -24.612 -15.648 30.809  1.00 45.11  ?  149  LEU D CG  1 
ATOM   7185  C CD1 . LEU D  1  149 ? -25.027 -14.770 31.982  1.00 46.83  ?  149  LEU D CD1 1 
ATOM   7186  C CD2 . LEU D  1  149 ? -25.833 -16.235 30.112  1.00 45.61  ?  149  LEU D CD2 1 
ATOM   7187  N N   . SER D  1  150 ? -21.850 -14.779 26.694  1.00 44.53  ?  150  SER D N   1 
ATOM   7188  C CA  . SER D  1  150 ? -21.084 -13.804 25.928  1.00 43.42  ?  150  SER D CA  1 
ATOM   7189  C C   . SER D  1  150 ? -21.953 -13.103 24.875  1.00 43.50  ?  150  SER D C   1 
ATOM   7190  O O   . SER D  1  150 ? -23.066 -13.531 24.554  1.00 44.50  ?  150  SER D O   1 
ATOM   7191  C CB  . SER D  1  150 ? -19.885 -14.483 25.266  1.00 42.77  ?  150  SER D CB  1 
ATOM   7192  O OG  . SER D  1  150 ? -19.247 -15.359 26.177  1.00 42.93  ?  150  SER D OG  1 
ATOM   7193  N N   . ILE D  1  151 ? -21.411 -12.003 24.334  1.00 42.44  ?  151  ILE D N   1 
ATOM   7194  C CA  . ILE D  1  151 ? -22.015 -11.238 23.243  1.00 42.42  ?  151  ILE D CA  1 
ATOM   7195  C C   . ILE D  1  151 ? -23.482 -10.943 23.541  1.00 43.35  ?  151  ILE D C   1 
ATOM   7196  O O   . ILE D  1  151 ? -24.389 -11.569 22.978  1.00 44.24  ?  151  ILE D O   1 
ATOM   7197  C CB  . ILE D  1  151 ? -21.848 -11.971 21.899  1.00 42.73  ?  151  ILE D CB  1 
ATOM   7198  C CG1 . ILE D  1  151 ? -20.396 -12.415 21.717  1.00 42.10  ?  151  ILE D CG1 1 
ATOM   7199  C CG2 . ILE D  1  151 ? -22.258 -11.069 20.751  1.00 42.72  ?  151  ILE D CG2 1 
ATOM   7200  C CD1 . ILE D  1  151 ? -20.175 -13.280 20.511  1.00 43.22  ?  151  ILE D CD1 1 
ATOM   7201  N N   . ASN D  1  152 ? -23.710 -10.011 24.457  1.00 45.24  ?  152  ASN D N   1 
ATOM   7202  C CA  . ASN D  1  152 ? -25.028 -9.572  24.914  1.00 46.29  ?  152  ASN D CA  1 
ATOM   7203  C C   . ASN D  1  152 ? -24.887 -8.103  25.300  1.00 46.47  ?  152  ASN D C   1 
ATOM   7204  O O   . ASN D  1  152 ? -23.907 -7.447  24.934  1.00 45.76  ?  152  ASN D O   1 
ATOM   7205  C CB  . ASN D  1  152 ? -25.530 -10.454 26.074  1.00 47.37  ?  152  ASN D CB  1 
ATOM   7206  C CG  . ASN D  1  152 ? -26.229 -11.729 25.601  1.00 47.92  ?  152  ASN D CG  1 
ATOM   7207  O OD1 . ASN D  1  152 ? -27.185 -11.680 24.830  1.00 48.46  ?  152  ASN D OD1 1 
ATOM   7208  N ND2 . ASN D  1  152 ? -25.748 -12.878 26.071  1.00 48.12  ?  152  ASN D ND2 1 
ATOM   7209  N N   . GLN D  1  153 ? -25.857 -7.574  26.035  1.00 47.31  ?  153  GLN D N   1 
ATOM   7210  C CA  . GLN D  1  153 ? -25.734 -6.227  26.588  1.00 48.11  ?  153  GLN D CA  1 
ATOM   7211  C C   . GLN D  1  153 ? -25.959 -6.246  28.097  1.00 50.02  ?  153  GLN D C   1 
ATOM   7212  O O   . GLN D  1  153 ? -26.696 -5.434  28.656  1.00 51.37  ?  153  GLN D O   1 
ATOM   7213  C CB  . GLN D  1  153 ? -26.682 -5.263  25.895  1.00 48.04  ?  153  GLN D CB  1 
ATOM   7214  C CG  . GLN D  1  153 ? -26.628 -5.360  24.389  1.00 46.69  ?  153  GLN D CG  1 
ATOM   7215  C CD  . GLN D  1  153 ? -27.914 -5.894  23.806  1.00 46.86  ?  153  GLN D CD  1 
ATOM   7216  O OE1 . GLN D  1  153 ? -28.960 -5.875  24.461  1.00 47.87  ?  153  GLN D OE1 1 
ATOM   7217  N NE2 . GLN D  1  153 ? -27.853 -6.367  22.567  1.00 46.16  ?  153  GLN D NE2 1 
ATOM   7218  N N   . LEU D  1  154 ? -25.319 -7.191  28.781  1.00 45.52  ?  154  LEU D N   1 
ATOM   7219  C CA  . LEU D  1  154 ? -25.388 -7.236  30.235  1.00 47.78  ?  154  LEU D CA  1 
ATOM   7220  C C   . LEU D  1  154 ? -24.532 -6.130  30.849  1.00 49.33  ?  154  LEU D C   1 
ATOM   7221  O O   . LEU D  1  154 ? -23.543 -5.679  30.262  1.00 48.38  ?  154  LEU D O   1 
ATOM   7222  C CB  . LEU D  1  154 ? -24.912 -8.593  30.751  1.00 47.79  ?  154  LEU D CB  1 
ATOM   7223  C CG  . LEU D  1  154 ? -25.523 -9.837  30.109  1.00 46.46  ?  154  LEU D CG  1 
ATOM   7224  C CD1 . LEU D  1  154 ? -25.011 -11.076 30.824  1.00 46.81  ?  154  LEU D CD1 1 
ATOM   7225  C CD2 . LEU D  1  154 ? -27.047 -9.773  30.132  1.00 47.34  ?  154  LEU D CD2 1 
ATOM   7226  N N   . VAL D  1  155 ? -24.918 -5.697  32.051  1.00 46.14  ?  155  VAL D N   1 
ATOM   7227  C CA  . VAL D  1  155 ? -24.235 -4.637  32.780  1.00 48.45  ?  155  VAL D CA  1 
ATOM   7228  C C   . VAL D  1  155 ? -24.117 -5.044  34.244  1.00 51.71  ?  155  VAL D C   1 
ATOM   7229  O O   . VAL D  1  155 ? -24.595 -6.102  34.661  1.00 51.97  ?  155  VAL D O   1 
ATOM   7230  C CB  . VAL D  1  155 ? -24.960 -3.284  32.657  1.00 48.94  ?  155  VAL D CB  1 
ATOM   7231  C CG1 . VAL D  1  155 ? -24.724 -2.685  31.293  1.00 46.43  ?  155  VAL D CG1 1 
ATOM   7232  C CG2 . VAL D  1  155 ? -26.436 -3.463  32.906  1.00 49.25  ?  155  VAL D CG2 1 
ATOM   7233  N N   . GLY D  1  156 ? -23.487 -4.182  35.035  1.00 48.48  ?  156  GLY D N   1 
ATOM   7234  C CA  . GLY D  1  156 ? -23.301 -4.463  36.442  1.00 50.42  ?  156  GLY D CA  1 
ATOM   7235  C C   . GLY D  1  156 ? -22.074 -5.302  36.714  1.00 51.26  ?  156  GLY D C   1 
ATOM   7236  O O   . GLY D  1  156 ? -21.270 -5.611  35.832  1.00 48.80  ?  156  GLY D O   1 
ATOM   7237  N N   . GLU D  1  157 ? -21.930 -5.672  37.981  1.00 50.04  ?  157  GLU D N   1 
ATOM   7238  C CA  . GLU D  1  157 ? -20.767 -6.411  38.442  1.00 51.93  ?  157  GLU D CA  1 
ATOM   7239  C C   . GLU D  1  157 ? -20.984 -7.918  38.316  1.00 50.22  ?  157  GLU D C   1 
ATOM   7240  O O   . GLU D  1  157 ? -22.089 -8.399  38.052  1.00 48.19  ?  157  GLU D O   1 
ATOM   7241  C CB  . GLU D  1  157 ? -20.443 -6.034  39.884  1.00 57.17  ?  157  GLU D CB  1 
ATOM   7242  C CG  . GLU D  1  157 ? -20.293 -4.540  40.100  1.00 58.13  ?  157  GLU D CG  1 
ATOM   7243  C CD  . GLU D  1  157 ? -19.559 -4.210  41.382  1.00 62.13  ?  157  GLU D CD  1 
ATOM   7244  O OE1 . GLU D  1  157 ? -18.965 -5.134  41.979  1.00 64.01  ?  157  GLU D OE1 1 
ATOM   7245  O OE2 . GLU D  1  157 ? -19.569 -3.029  41.789  1.00 63.11  -1 157  GLU D OE2 1 
ATOM   7246  N N   . ILE D  1  158 ? -19.899 -8.665  38.494  1.00 49.92  ?  158  ILE D N   1 
ATOM   7247  C CA  . ILE D  1  158 ? -19.956 -10.123 38.507  1.00 47.92  ?  158  ILE D CA  1 
ATOM   7248  C C   . ILE D  1  158 ? -20.220 -10.562 39.942  1.00 52.70  ?  158  ILE D C   1 
ATOM   7249  O O   . ILE D  1  158 ? -19.493 -10.151 40.855  1.00 57.57  ?  158  ILE D O   1 
ATOM   7250  C CB  . ILE D  1  158 ? -18.659 -10.737 37.954  1.00 45.28  ?  158  ILE D CB  1 
ATOM   7251  C CG1 . ILE D  1  158 ? -18.577 -10.533 36.440  1.00 40.97  ?  158  ILE D CG1 1 
ATOM   7252  C CG2 . ILE D  1  158 ? -18.569 -12.214 38.309  1.00 43.84  ?  158  ILE D CG2 1 
ATOM   7253  C CD1 . ILE D  1  158 ? -17.177 -10.685 35.888  1.00 39.97  ?  158  ILE D CD1 1 
ATOM   7254  N N   . PRO D  1  159 ? -21.245 -11.375 40.196  1.00 48.76  ?  159  PRO D N   1 
ATOM   7255  C CA  . PRO D  1  159 ? -21.548 -11.747 41.575  1.00 52.97  ?  159  PRO D CA  1 
ATOM   7256  C C   . PRO D  1  159 ? -20.470 -12.648 42.146  1.00 53.18  ?  159  PRO D C   1 
ATOM   7257  O O   . PRO D  1  159 ? -19.864 -13.453 41.419  1.00 49.29  ?  159  PRO D O   1 
ATOM   7258  C CB  . PRO D  1  159 ? -22.892 -12.486 41.454  1.00 50.95  ?  159  PRO D CB  1 
ATOM   7259  C CG  . PRO D  1  159 ? -22.922 -12.984 40.055  1.00 48.01  ?  159  PRO D CG  1 
ATOM   7260  C CD  . PRO D  1  159 ? -22.174 -11.982 39.230  1.00 47.59  ?  159  PRO D CD  1 
ATOM   7261  N N   . PRO D  1  160 ? -20.188 -12.544 43.449  1.00 53.17  ?  160  PRO D N   1 
ATOM   7262  C CA  . PRO D  1  160 ? -19.262 -13.498 44.083  1.00 53.73  ?  160  PRO D CA  1 
ATOM   7263  C C   . PRO D  1  160 ? -19.807 -14.909 44.144  1.00 53.37  ?  160  PRO D C   1 
ATOM   7264  O O   . PRO D  1  160 ? -19.030 -15.853 44.342  1.00 53.57  ?  160  PRO D O   1 
ATOM   7265  C CB  . PRO D  1  160 ? -19.069 -12.926 45.496  1.00 55.64  ?  160  PRO D CB  1 
ATOM   7266  C CG  . PRO D  1  160 ? -19.693 -11.565 45.479  1.00 56.73  ?  160  PRO D CG  1 
ATOM   7267  C CD  . PRO D  1  160 ? -20.741 -11.590 44.419  1.00 56.12  ?  160  PRO D CD  1 
ATOM   7268  N N   . GLU D  1  161 ? -21.123 -15.078 44.005  1.00 60.03  ?  161  GLU D N   1 
ATOM   7269  C CA  . GLU D  1  161 ? -21.738 -16.398 44.049  1.00 57.98  ?  161  GLU D CA  1 
ATOM   7270  C C   . GLU D  1  161 ? -21.298 -17.284 42.892  1.00 52.46  ?  161  GLU D C   1 
ATOM   7271  O O   . GLU D  1  161 ? -21.408 -18.510 42.997  1.00 51.02  ?  161  GLU D O   1 
ATOM   7272  C CB  . GLU D  1  161 ? -23.263 -16.258 44.048  1.00 59.45  ?  161  GLU D CB  1 
ATOM   7273  C CG  . GLU D  1  161 ? -23.858 -15.934 45.409  1.00 65.32  ?  161  GLU D CG  1 
ATOM   7274  C CD  . GLU D  1  161 ? -23.850 -14.447 45.738  1.00 70.01  ?  161  GLU D CD  1 
ATOM   7275  O OE1 . GLU D  1  161 ? -23.264 -13.659 44.964  1.00 68.65  ?  161  GLU D OE1 1 
ATOM   7276  O OE2 . GLU D  1  161 ? -24.431 -14.067 46.778  1.00 75.27  -1 161  GLU D OE2 1 
ATOM   7277  N N   . LEU D  1  162 ? -20.804 -16.696 41.794  1.00 55.84  ?  162  LEU D N   1 
ATOM   7278  C CA  . LEU D  1  162 ? -20.316 -17.501 40.681  1.00 51.13  ?  162  LEU D CA  1 
ATOM   7279  C C   . LEU D  1  162 ? -19.227 -18.455 41.135  1.00 50.57  ?  162  LEU D C   1 
ATOM   7280  O O   . LEU D  1  162 ? -19.075 -19.538 40.562  1.00 47.88  ?  162  LEU D O   1 
ATOM   7281  C CB  . LEU D  1  162 ? -19.800 -16.606 39.555  1.00 48.82  ?  162  LEU D CB  1 
ATOM   7282  C CG  . LEU D  1  162 ? -20.840 -15.791 38.788  1.00 48.12  ?  162  LEU D CG  1 
ATOM   7283  C CD1 . LEU D  1  162 ? -20.282 -15.320 37.453  1.00 44.74  ?  162  LEU D CD1 1 
ATOM   7284  C CD2 . LEU D  1  162 ? -22.105 -16.603 38.587  1.00 47.15  ?  162  LEU D CD2 1 
ATOM   7285  N N   . GLY D  1  163 ? -18.481 -18.085 42.177  1.00 52.15  ?  163  GLY D N   1 
ATOM   7286  C CA  . GLY D  1  163 ? -17.462 -18.955 42.732  1.00 51.76  ?  163  GLY D CA  1 
ATOM   7287  C C   . GLY D  1  163 ? -18.001 -20.233 43.346  1.00 52.22  ?  163  GLY D C   1 
ATOM   7288  O O   . GLY D  1  163 ? -17.211 -21.142 43.628  1.00 51.36  ?  163  GLY D O   1 
ATOM   7289  N N   . LYS D  1  164 ? -19.318 -20.325 43.554  1.00 53.07  ?  164  LYS D N   1 
ATOM   7290  C CA  . LYS D  1  164 ? -19.951 -21.509 44.126  1.00 53.77  ?  164  LYS D CA  1 
ATOM   7291  C C   . LYS D  1  164 ? -20.136 -22.639 43.121  1.00 50.47  ?  164  LYS D C   1 
ATOM   7292  O O   . LYS D  1  164 ? -20.591 -23.720 43.515  1.00 50.88  ?  164  LYS D O   1 
ATOM   7293  C CB  . LYS D  1  164 ? -21.313 -21.142 44.723  1.00 56.81  ?  164  LYS D CB  1 
ATOM   7294  C CG  . LYS D  1  164 ? -21.236 -20.447 46.064  1.00 61.12  ?  164  LYS D CG  1 
ATOM   7295  C CD  . LYS D  1  164 ? -22.556 -20.555 46.811  1.00 64.25  ?  164  LYS D CD  1 
ATOM   7296  C CE  . LYS D  1  164 ? -23.637 -19.708 46.154  1.00 64.68  ?  164  LYS D CE  1 
ATOM   7297  N NZ  . LYS D  1  164 ? -24.986 -19.896 46.773  1.00 67.55  ?  164  LYS D NZ  1 
ATOM   7298  N N   . LEU D  1  165 ? -19.785 -22.427 41.850  1.00 54.44  ?  165  LEU D N   1 
ATOM   7299  C CA  . LEU D  1  165 ? -19.967 -23.434 40.802  1.00 51.74  ?  165  LEU D CA  1 
ATOM   7300  C C   . LEU D  1  165 ? -18.753 -24.366 40.769  1.00 50.48  ?  165  LEU D C   1 
ATOM   7301  O O   . LEU D  1  165 ? -17.944 -24.367 39.840  1.00 48.30  ?  165  LEU D O   1 
ATOM   7302  C CB  . LEU D  1  165 ? -20.190 -22.759 39.456  1.00 49.40  ?  165  LEU D CB  1 
ATOM   7303  C CG  . LEU D  1  165 ? -21.363 -21.784 39.393  1.00 50.34  ?  165  LEU D CG  1 
ATOM   7304  C CD1 . LEU D  1  165 ? -21.392 -21.070 38.049  1.00 47.83  ?  165  LEU D CD1 1 
ATOM   7305  C CD2 . LEU D  1  165 ? -22.670 -22.516 39.651  1.00 51.49  ?  165  LEU D CD2 1 
ATOM   7306  N N   . SER D  1  166 ? -18.661 -25.195 41.814  1.00 54.34  ?  166  SER D N   1 
ATOM   7307  C CA  . SER D  1  166 ? -17.486 -26.032 42.035  1.00 53.33  ?  166  SER D CA  1 
ATOM   7308  C C   . SER D  1  166 ? -17.233 -27.025 40.910  1.00 50.94  ?  166  SER D C   1 
ATOM   7309  O O   . SER D  1  166 ? -16.123 -27.555 40.815  1.00 49.82  ?  166  SER D O   1 
ATOM   7310  C CB  . SER D  1  166 ? -17.633 -26.802 43.340  1.00 55.00  ?  166  SER D CB  1 
ATOM   7311  O OG  . SER D  1  166 ? -18.715 -27.709 43.240  1.00 55.13  ?  166  SER D OG  1 
ATOM   7312  N N   . ASN D  1  167 ? -18.232 -27.319 40.082  1.00 54.32  ?  167  ASN D N   1 
ATOM   7313  C CA  . ASN D  1  167 ? -18.063 -28.250 38.974  1.00 52.67  ?  167  ASN D CA  1 
ATOM   7314  C C   . ASN D  1  167 ? -17.874 -27.553 37.634  1.00 51.11  ?  167  ASN D C   1 
ATOM   7315  O O   . ASN D  1  167 ? -17.830 -28.228 36.601  1.00 50.19  ?  167  ASN D O   1 
ATOM   7316  C CB  . ASN D  1  167 ? -19.261 -29.202 38.890  1.00 53.39  ?  167  ASN D CB  1 
ATOM   7317  C CG  . ASN D  1  167 ? -19.154 -30.359 39.864  1.00 54.19  ?  167  ASN D CG  1 
ATOM   7318  O OD1 . ASN D  1  167 ? -18.205 -31.144 39.811  1.00 53.30  ?  167  ASN D OD1 1 
ATOM   7319  N ND2 . ASN D  1  167 ? -20.132 -30.472 40.761  1.00 55.87  ?  167  ASN D ND2 1 
ATOM   7320  N N   . LEU D  1  168 ? -17.781 -26.227 37.624  1.00 51.32  ?  168  LEU D N   1 
ATOM   7321  C CA  . LEU D  1  168 ? -17.619 -25.494 36.377  1.00 49.64  ?  168  LEU D CA  1 
ATOM   7322  C C   . LEU D  1  168 ? -16.263 -25.780 35.745  1.00 48.30  ?  168  LEU D C   1 
ATOM   7323  O O   . LEU D  1  168 ? -15.240 -25.876 36.428  1.00 48.52  ?  168  LEU D O   1 
ATOM   7324  C CB  . LEU D  1  168 ? -17.780 -23.996 36.617  1.00 49.82  ?  168  LEU D CB  1 
ATOM   7325  C CG  . LEU D  1  168 ? -18.084 -23.133 35.393  1.00 48.22  ?  168  LEU D CG  1 
ATOM   7326  C CD1 . LEU D  1  168 ? -19.557 -23.218 35.020  1.00 48.59  ?  168  LEU D CD1 1 
ATOM   7327  C CD2 . LEU D  1  168 ? -17.674 -21.694 35.657  1.00 48.28  ?  168  LEU D CD2 1 
ATOM   7328  N N   . ASP D  1  169 ? -16.267 -25.932 34.429  1.00 52.08  ?  169  ASP D N   1 
ATOM   7329  C CA  . ASP D  1  169 ? -15.059 -26.154 33.651  1.00 51.00  ?  169  ASP D CA  1 
ATOM   7330  C C   . ASP D  1  169 ? -14.742 -24.990 32.722  1.00 49.72  ?  169  ASP D C   1 
ATOM   7331  O O   . ASP D  1  169 ? -13.571 -24.641 32.541  1.00 48.98  ?  169  ASP D O   1 
ATOM   7332  C CB  . ASP D  1  169 ? -15.223 -27.453 32.854  1.00 51.31  ?  169  ASP D CB  1 
ATOM   7333  C CG  . ASP D  1  169 ? -14.329 -27.525 31.648  1.00 50.51  ?  169  ASP D CG  1 
ATOM   7334  O OD1 . ASP D  1  169 ? -13.113 -27.245 31.769  1.00 49.77  ?  169  ASP D OD1 1 
ATOM   7335  O OD2 . ASP D  1  169 ? -14.866 -27.841 30.563  1.00 50.92  -1 169  ASP D OD2 1 
ATOM   7336  N N   . THR D  1  170 ? -15.764 -24.342 32.170  1.00 44.55  ?  170  THR D N   1 
ATOM   7337  C CA  . THR D  1  170 ? -15.591 -23.252 31.225  1.00 43.34  ?  170  THR D CA  1 
ATOM   7338  C C   . THR D  1  170 ? -16.491 -22.092 31.619  1.00 43.38  ?  170  THR D C   1 
ATOM   7339  O O   . THR D  1  170 ? -17.679 -22.293 31.894  1.00 44.23  ?  170  THR D O   1 
ATOM   7340  C CB  . THR D  1  170 ? -15.930 -23.719 29.818  1.00 43.34  ?  170  THR D CB  1 
ATOM   7341  O OG1 . THR D  1  170 ? -15.032 -24.772 29.451  1.00 43.68  ?  170  THR D OG1 1 
ATOM   7342  C CG2 . THR D  1  170 ? -15.822 -22.563 28.841  1.00 42.27  ?  170  THR D CG2 1 
ATOM   7343  N N   . LEU D  1  171 ? -15.933 -20.882 31.635  1.00 41.28  ?  171  LEU D N   1 
ATOM   7344  C CA  . LEU D  1  171 ? -16.688 -19.676 31.951  1.00 41.58  ?  171  LEU D CA  1 
ATOM   7345  C C   . LEU D  1  171 ? -16.446 -18.650 30.851  1.00 40.24  ?  171  LEU D C   1 
ATOM   7346  O O   . LEU D  1  171 ? -15.302 -18.243 30.620  1.00 39.83  ?  171  LEU D O   1 
ATOM   7347  C CB  . LEU D  1  171 ? -16.290 -19.120 33.324  1.00 43.11  ?  171  LEU D CB  1 
ATOM   7348  C CG  . LEU D  1  171 ? -16.887 -17.774 33.748  1.00 44.25  ?  171  LEU D CG  1 
ATOM   7349  C CD1 . LEU D  1  171 ? -18.404 -17.827 33.754  1.00 44.78  ?  171  LEU D CD1 1 
ATOM   7350  C CD2 . LEU D  1  171 ? -16.351 -17.345 35.105  1.00 46.74  ?  171  LEU D CD2 1 
ATOM   7351  N N   . HIS D  1  172 ? -17.517 -18.251 30.165  1.00 44.90  ?  172  HIS D N   1 
ATOM   7352  C CA  . HIS D  1  172 ? -17.457 -17.266 29.090  1.00 43.84  ?  172  HIS D CA  1 
ATOM   7353  C C   . HIS D  1  172 ? -18.432 -16.144 29.404  1.00 44.35  ?  172  HIS D C   1 
ATOM   7354  O O   . HIS D  1  172 ? -19.646 -16.368 29.422  1.00 44.99  ?  172  HIS D O   1 
ATOM   7355  C CB  . HIS D  1  172 ? -17.802 -17.891 27.736  1.00 43.56  ?  172  HIS D CB  1 
ATOM   7356  C CG  . HIS D  1  172 ? -16.790 -18.879 27.245  1.00 43.51  ?  172  HIS D CG  1 
ATOM   7357  N ND1 . HIS D  1  172 ? -16.984 -19.641 26.112  1.00 44.33  ?  172  HIS D ND1 1 
ATOM   7358  C CD2 . HIS D  1  172 ? -15.577 -19.232 27.733  1.00 43.22  ?  172  HIS D CD2 1 
ATOM   7359  C CE1 . HIS D  1  172 ? -15.933 -20.418 25.922  1.00 44.47  ?  172  HIS D CE1 1 
ATOM   7360  N NE2 . HIS D  1  172 ? -15.064 -20.188 26.890  1.00 43.60  ?  172  HIS D NE2 1 
ATOM   7361  N N   . LEU D  1  173 ? -17.907 -14.943 29.631  1.00 41.73  ?  173  LEU D N   1 
ATOM   7362  C CA  . LEU D  1  173 ? -18.691 -13.753 29.963  1.00 42.71  ?  173  LEU D CA  1 
ATOM   7363  C C   . LEU D  1  173 ? -18.262 -12.588 29.082  1.00 41.83  ?  173  LEU D C   1 
ATOM   7364  O O   . LEU D  1  173 ? -18.040 -11.466 29.542  1.00 43.03  ?  173  LEU D O   1 
ATOM   7365  C CB  . LEU D  1  173 ? -18.563 -13.391 31.440  1.00 45.12  ?  173  LEU D CB  1 
ATOM   7366  C CG  . LEU D  1  173 ? -19.316 -14.267 32.437  1.00 46.58  ?  173  LEU D CG  1 
ATOM   7367  C CD1 . LEU D  1  173 ? -18.918 -13.920 33.859  1.00 49.60  ?  173  LEU D CD1 1 
ATOM   7368  C CD2 . LEU D  1  173 ? -20.809 -14.106 32.236  1.00 46.82  ?  173  LEU D CD2 1 
ATOM   7369  N N   . VAL D  1  174 ? -18.140 -12.849 27.791  1.00 45.13  ?  174  VAL D N   1 
ATOM   7370  C CA  . VAL D  1  174 ? -17.327 -12.032 26.901  1.00 44.21  ?  174  VAL D CA  1 
ATOM   7371  C C   . VAL D  1  174 ? -18.181 -11.028 26.144  1.00 44.04  ?  174  VAL D C   1 
ATOM   7372  O O   . VAL D  1  174 ? -19.362 -11.259 25.874  1.00 44.24  ?  174  VAL D O   1 
ATOM   7373  C CB  . VAL D  1  174 ? -16.561 -12.948 25.926  1.00 43.12  ?  174  VAL D CB  1 
ATOM   7374  C CG1 . VAL D  1  174 ? -15.450 -12.214 25.313  1.00 42.46  ?  174  VAL D CG1 1 
ATOM   7375  C CG2 . VAL D  1  174 ? -16.020 -14.158 26.663  1.00 43.43  ?  174  VAL D CG2 1 
ATOM   7376  N N   . GLU D  1  175 ? -17.561 -9.906  25.769  1.00 46.13  ?  175  GLU D N   1 
ATOM   7377  C CA  . GLU D  1  175 ? -18.174 -8.913  24.887  1.00 45.87  ?  175  GLU D CA  1 
ATOM   7378  C C   . GLU D  1  175 ? -19.492 -8.396  25.459  1.00 46.95  ?  175  GLU D C   1 
ATOM   7379  O O   . GLU D  1  175 ? -20.535 -8.386  24.797  1.00 46.76  ?  175  GLU D O   1 
ATOM   7380  C CB  . GLU D  1  175 ? -18.356 -9.472  23.478  1.00 44.90  ?  175  GLU D CB  1 
ATOM   7381  C CG  . GLU D  1  175 ? -17.054 -9.569  22.714  1.00 44.14  ?  175  GLU D CG  1 
ATOM   7382  C CD  . GLU D  1  175 ? -17.253 -9.791  21.230  1.00 43.98  ?  175  GLU D CD  1 
ATOM   7383  O OE1 . GLU D  1  175 ? -18.328 -9.440  20.696  1.00 44.37  ?  175  GLU D OE1 1 
ATOM   7384  O OE2 . GLU D  1  175 ? -16.318 -10.310 20.589  1.00 43.81  -1 175  GLU D OE2 1 
ATOM   7385  N N   . ASN D  1  176 ? -19.429 -8.001  26.728  1.00 43.70  ?  176  ASN D N   1 
ATOM   7386  C CA  . ASN D  1  176 ? -20.502 -7.329  27.446  1.00 45.29  ?  176  ASN D CA  1 
ATOM   7387  C C   . ASN D  1  176 ? -19.914 -6.056  28.036  1.00 47.03  ?  176  ASN D C   1 
ATOM   7388  O O   . ASN D  1  176 ? -18.763 -5.715  27.741  1.00 46.80  ?  176  ASN D O   1 
ATOM   7389  C CB  . ASN D  1  176 ? -21.081 -8.237  28.534  1.00 46.44  ?  176  ASN D CB  1 
ATOM   7390  C CG  . ASN D  1  176 ? -22.020 -9.290  27.977  1.00 45.40  ?  176  ASN D CG  1 
ATOM   7391  O OD1 . ASN D  1  176 ? -23.124 -8.976  27.543  1.00 45.47  ?  176  ASN D OD1 1 
ATOM   7392  N ND2 . ASN D  1  176 ? -21.581 -10.546 27.981  1.00 44.75  ?  176  ASN D ND2 1 
ATOM   7393  N N   . LYS D  1  177 ? -20.673 -5.353  28.869  1.00 46.39  ?  177  LYS D N   1 
ATOM   7394  C CA  . LYS D  1  177 ? -20.200 -4.121  29.485  1.00 48.65  ?  177  LYS D CA  1 
ATOM   7395  C C   . LYS D  1  177 ? -20.206 -4.237  31.003  1.00 51.82  ?  177  LYS D C   1 
ATOM   7396  O O   . LYS D  1  177 ? -20.583 -3.305  31.713  1.00 54.18  ?  177  LYS D O   1 
ATOM   7397  C CB  . LYS D  1  177 ? -21.037 -2.926  29.027  1.00 48.61  ?  177  LYS D CB  1 
ATOM   7398  C CG  . LYS D  1  177 ? -20.815 -2.500  27.565  1.00 46.30  ?  177  LYS D CG  1 
ATOM   7399  C CD  . LYS D  1  177 ? -19.373 -2.735  27.083  1.00 45.44  ?  177  LYS D CD  1 
ATOM   7400  C CE  . LYS D  1  177 ? -19.272 -2.840  25.540  1.00 42.96  ?  177  LYS D CE  1 
ATOM   7401  N NZ  . LYS D  1  177 ? -19.209 -4.265  24.996  1.00 41.24  ?  177  LYS D NZ  1 
ATOM   7402  N N   . LEU D  1  178 ? -19.762 -5.385  31.515  1.00 43.81  ?  178  LEU D N   1 
ATOM   7403  C CA  . LEU D  1  178 ? -19.699 -5.593  32.956  1.00 47.24  ?  178  LEU D CA  1 
ATOM   7404  C C   . LEU D  1  178 ? -18.617 -4.712  33.566  1.00 50.34  ?  178  LEU D C   1 
ATOM   7405  O O   . LEU D  1  178 ? -17.552 -4.523  32.977  1.00 49.51  ?  178  LEU D O   1 
ATOM   7406  C CB  . LEU D  1  178 ? -19.425 -7.066  33.276  1.00 46.71  ?  178  LEU D CB  1 
ATOM   7407  C CG  . LEU D  1  178 ? -20.330 -8.123  32.635  1.00 43.76  ?  178  LEU D CG  1 
ATOM   7408  C CD1 . LEU D  1  178 ? -19.836 -9.526  32.962  1.00 43.21  ?  178  LEU D CD1 1 
ATOM   7409  C CD2 . LEU D  1  178 ? -21.788 -7.940  33.065  1.00 44.84  ?  178  LEU D CD2 1 
ATOM   7410  N N   . ASN D  1  179 ? -18.897 -4.161  34.747  1.00 51.46  ?  179  ASN D N   1 
ATOM   7411  C CA  . ASN D  1  179 ? -17.966 -3.272  35.427  1.00 54.82  ?  179  ASN D CA  1 
ATOM   7412  C C   . ASN D  1  179 ? -17.727 -3.752  36.853  1.00 59.05  ?  179  ASN D C   1 
ATOM   7413  O O   . ASN D  1  179 ? -18.382 -4.670  37.345  1.00 59.59  ?  179  ASN D O   1 
ATOM   7414  C CB  . ASN D  1  179 ? -18.457 -1.814  35.417  1.00 55.18  ?  179  ASN D CB  1 
ATOM   7415  C CG  . ASN D  1  179 ? -19.788 -1.615  36.140  1.00 56.29  ?  179  ASN D CG  1 
ATOM   7416  O OD1 . ASN D  1  179 ? -20.465 -2.572  36.525  1.00 56.48  ?  179  ASN D OD1 1 
ATOM   7417  N ND2 . ASN D  1  179 ? -20.167 -0.347  36.316  1.00 56.98  ?  179  ASN D ND2 1 
ATOM   7418  N N   . GLY D  1  180 ? -16.760 -3.128  37.507  1.00 51.48  ?  180  GLY D N   1 
ATOM   7419  C CA  . GLY D  1  180 ? -16.365 -3.511  38.845  1.00 55.33  ?  180  GLY D CA  1 
ATOM   7420  C C   . GLY D  1  180 ? -15.081 -4.315  38.848  1.00 56.32  ?  180  GLY D C   1 
ATOM   7421  O O   . GLY D  1  180 ? -14.393 -4.468  37.835  1.00 54.49  ?  180  GLY D O   1 
ATOM   7422  N N   . SER D  1  181 ? -14.762 -4.843  40.024  1.00 57.88  ?  181  SER D N   1 
ATOM   7423  C CA  . SER D  1  181 ? -13.602 -5.701  40.214  1.00 57.31  ?  181  SER D CA  1 
ATOM   7424  C C   . SER D  1  181 ? -14.019 -7.164  40.164  1.00 56.06  ?  181  SER D C   1 
ATOM   7425  O O   . SER D  1  181 ? -15.149 -7.517  40.507  1.00 57.50  ?  181  SER D O   1 
ATOM   7426  C CB  . SER D  1  181 ? -12.911 -5.404  41.546  1.00 58.70  ?  181  SER D CB  1 
ATOM   7427  O OG  . SER D  1  181 ? -12.113 -4.237  41.454  1.00 58.76  ?  181  SER D OG  1 
ATOM   7428  N N   . ILE D  1  182 ? -13.096 -8.015  39.730  1.00 58.21  ?  182  ILE D N   1 
ATOM   7429  C CA  . ILE D  1  182 ? -13.342 -9.454  39.704  1.00 55.14  ?  182  ILE D CA  1 
ATOM   7430  C C   . ILE D  1  182 ? -13.362 -9.965  41.140  1.00 57.23  ?  182  ILE D C   1 
ATOM   7431  O O   . ILE D  1  182 ? -12.387 -9.762  41.877  1.00 58.02  ?  182  ILE D O   1 
ATOM   7432  C CB  . ILE D  1  182 ? -12.287 -10.188 38.865  1.00 50.44  ?  182  ILE D CB  1 
ATOM   7433  C CG1 . ILE D  1  182 ? -12.203 -9.576  37.470  1.00 48.27  ?  182  ILE D CG1 1 
ATOM   7434  C CG2 . ILE D  1  182 ? -12.612 -11.668 38.777  1.00 47.28  ?  182  ILE D CG2 1 
ATOM   7435  C CD1 . ILE D  1  182 ? -11.174 -10.229 36.590  1.00 44.23  ?  182  ILE D CD1 1 
ATOM   7436  N N   . PRO D  1  183 ? -14.435 -10.616 41.585  1.00 54.46  ?  183  PRO D N   1 
ATOM   7437  C CA  . PRO D  1  183 ? -14.499 -11.055 42.984  1.00 56.67  ?  183  PRO D CA  1 
ATOM   7438  C C   . PRO D  1  183 ? -13.428 -12.090 43.295  1.00 54.36  ?  183  PRO D C   1 
ATOM   7439  O O   . PRO D  1  183 ? -13.070 -12.922 42.459  1.00 52.86  ?  183  PRO D O   1 
ATOM   7440  C CB  . PRO D  1  183 ? -15.905 -11.657 43.107  1.00 57.48  ?  183  PRO D CB  1 
ATOM   7441  C CG  . PRO D  1  183 ? -16.653 -11.172 41.910  1.00 56.61  ?  183  PRO D CG  1 
ATOM   7442  C CD  . PRO D  1  183 ? -15.639 -11.001 40.832  1.00 53.04  ?  183  PRO D CD  1 
ATOM   7443  N N   . SER D  1  184 ? -12.919 -12.032 44.527  1.00 62.86  ?  184  SER D N   1 
ATOM   7444  C CA  . SER D  1  184 ? -11.907 -12.992 44.955  1.00 61.02  ?  184  SER D CA  1 
ATOM   7445  C C   . SER D  1  184 ? -12.445 -14.415 44.951  1.00 59.32  ?  184  SER D C   1 
ATOM   7446  O O   . SER D  1  184 ? -11.673 -15.367 44.796  1.00 56.80  ?  184  SER D O   1 
ATOM   7447  C CB  . SER D  1  184 ? -11.399 -12.630 46.347  1.00 63.51  ?  184  SER D CB  1 
ATOM   7448  O OG  . SER D  1  184 ? -11.358 -11.224 46.514  1.00 65.74  ?  184  SER D OG  1 
ATOM   7449  N N   . GLU D  1  185 ? -13.758 -14.581 45.118  1.00 60.97  ?  185  GLU D N   1 
ATOM   7450  C CA  . GLU D  1  185 ? -14.373 -15.902 45.184  1.00 59.65  ?  185  GLU D CA  1 
ATOM   7451  C C   . GLU D  1  185 ? -14.297 -16.665 43.866  1.00 55.41  ?  185  GLU D C   1 
ATOM   7452  O O   . GLU D  1  185 ? -14.571 -17.871 43.854  1.00 53.91  ?  185  GLU D O   1 
ATOM   7453  C CB  . GLU D  1  185 ? -15.832 -15.778 45.627  1.00 62.36  ?  185  GLU D CB  1 
ATOM   7454  C CG  . GLU D  1  185 ? -16.020 -15.378 47.086  1.00 66.42  ?  185  GLU D CG  1 
ATOM   7455  C CD  . GLU D  1  185 ? -15.786 -13.894 47.335  1.00 68.97  ?  185  GLU D CD  1 
ATOM   7456  O OE1 . GLU D  1  185 ? -15.766 -13.113 46.359  1.00 68.32  ?  185  GLU D OE1 1 
ATOM   7457  O OE2 . GLU D  1  185 ? -15.630 -13.509 48.514  1.00 71.43  -1 185  GLU D OE2 1 
ATOM   7458  N N   . ILE D  1  186 ? -13.943 -16.002 42.762  1.00 59.81  ?  186  ILE D N   1 
ATOM   7459  C CA  . ILE D  1  186 ? -13.732 -16.720 41.507  1.00 55.64  ?  186  ILE D CA  1 
ATOM   7460  C C   . ILE D  1  186 ? -12.610 -17.742 41.659  1.00 54.01  ?  186  ILE D C   1 
ATOM   7461  O O   . ILE D  1  186 ? -12.595 -18.771 40.969  1.00 51.35  ?  186  ILE D O   1 
ATOM   7462  C CB  . ILE D  1  186 ? -13.455 -15.722 40.364  1.00 54.16  ?  186  ILE D CB  1 
ATOM   7463  C CG1 . ILE D  1  186 ? -14.588 -14.700 40.279  1.00 56.22  ?  186  ILE D CG1 1 
ATOM   7464  C CG2 . ILE D  1  186 ? -13.313 -16.437 39.032  1.00 49.96  ?  186  ILE D CG2 1 
ATOM   7465  C CD1 . ILE D  1  186 ? -15.937 -15.319 40.004  1.00 55.28  ?  186  ILE D CD1 1 
ATOM   7466  N N   . GLY D  1  187 ? -11.673 -17.496 42.579  1.00 55.92  ?  187  GLY D N   1 
ATOM   7467  C CA  . GLY D  1  187 ? -10.599 -18.428 42.863  1.00 54.66  ?  187  GLY D CA  1 
ATOM   7468  C C   . GLY D  1  187 ? -11.032 -19.734 43.496  1.00 54.64  ?  187  GLY D C   1 
ATOM   7469  O O   . GLY D  1  187 ? -10.186 -20.601 43.737  1.00 53.89  ?  187  GLY D O   1 
ATOM   7470  N N   . ARG D  1  188 ? -12.320 -19.894 43.789  1.00 56.83  ?  188  ARG D N   1 
ATOM   7471  C CA  . ARG D  1  188 ? -12.845 -21.153 44.295  1.00 56.75  ?  188  ARG D CA  1 
ATOM   7472  C C   . ARG D  1  188 ? -13.191 -22.138 43.186  1.00 53.94  ?  188  ARG D C   1 
ATOM   7473  O O   . ARG D  1  188 ? -13.547 -23.282 43.488  1.00 53.63  ?  188  ARG D O   1 
ATOM   7474  C CB  . ARG D  1  188 ? -14.085 -20.893 45.151  1.00 59.77  ?  188  ARG D CB  1 
ATOM   7475  C CG  . ARG D  1  188 ? -13.815 -20.129 46.434  1.00 62.88  ?  188  ARG D CG  1 
ATOM   7476  C CD  . ARG D  1  188 ? -15.036 -20.166 47.341  1.00 65.83  ?  188  ARG D CD  1 
ATOM   7477  N NE  . ARG D  1  188 ? -14.865 -19.348 48.535  1.00 68.89  ?  188  ARG D NE  1 
ATOM   7478  C CZ  . ARG D  1  188 ? -15.570 -19.492 49.649  1.00 71.36  ?  188  ARG D CZ  1 
ATOM   7479  N NH1 . ARG D  1  188 ? -16.509 -20.418 49.757  1.00 71.38  ?  188  ARG D NH1 1 
ATOM   7480  N NH2 . ARG D  1  188 ? -15.332 -18.683 50.677  1.00 73.75  ?  188  ARG D NH2 1 
ATOM   7481  N N   . LEU D  1  189 ? -13.090 -21.730 41.919  1.00 56.92  ?  189  LEU D N   1 
ATOM   7482  C CA  . LEU D  1  189 ? -13.422 -22.594 40.785  1.00 54.38  ?  189  LEU D CA  1 
ATOM   7483  C C   . LEU D  1  189 ? -12.261 -23.560 40.525  1.00 52.68  ?  189  LEU D C   1 
ATOM   7484  O O   . LEU D  1  189 ? -11.504 -23.445 39.558  1.00 50.87  ?  189  LEU D O   1 
ATOM   7485  C CB  . LEU D  1  189 ? -13.750 -21.756 39.558  1.00 52.80  ?  189  LEU D CB  1 
ATOM   7486  C CG  . LEU D  1  189 ? -14.911 -20.776 39.707  1.00 54.19  ?  189  LEU D CG  1 
ATOM   7487  C CD1 . LEU D  1  189 ? -15.189 -20.104 38.389  1.00 52.05  ?  189  LEU D CD1 1 
ATOM   7488  C CD2 . LEU D  1  189 ? -16.145 -21.494 40.199  1.00 55.35  ?  189  LEU D CD2 1 
ATOM   7489  N N   . THR D  1  190 ? -12.143 -24.541 41.425  1.00 57.46  ?  190  THR D N   1 
ATOM   7490  C CA  . THR D  1  190 ? -10.981 -25.428 41.451  1.00 56.21  ?  190  THR D CA  1 
ATOM   7491  C C   . THR D  1  190 ? -10.854 -26.266 40.181  1.00 54.08  ?  190  THR D C   1 
ATOM   7492  O O   . THR D  1  190 ? -9.746  -26.683 39.821  1.00 52.89  ?  190  THR D O   1 
ATOM   7493  C CB  . THR D  1  190 ? -11.067 -26.322 42.692  1.00 57.32  ?  190  THR D CB  1 
ATOM   7494  O OG1 . THR D  1  190 ? -10.804 -25.529 43.853  1.00 59.08  ?  190  THR D OG1 1 
ATOM   7495  C CG2 . THR D  1  190 ? -10.067 -27.470 42.644  1.00 56.06  ?  190  THR D CG2 1 
ATOM   7496  N N   . LYS D  1  191 ? -11.957 -26.508 39.478  1.00 55.67  ?  191  LYS D N   1 
ATOM   7497  C CA  . LYS D  1  191 ? -11.944 -27.370 38.304  1.00 54.14  ?  191  LYS D CA  1 
ATOM   7498  C C   . LYS D  1  191 ? -11.929 -26.606 36.986  1.00 52.96  ?  191  LYS D C   1 
ATOM   7499  O O   . LYS D  1  191 ? -11.890 -27.240 35.927  1.00 51.98  ?  191  LYS D O   1 
ATOM   7500  C CB  . LYS D  1  191 ? -13.156 -28.306 38.330  1.00 54.67  ?  191  LYS D CB  1 
ATOM   7501  C CG  . LYS D  1  191 ? -13.043 -29.426 39.341  1.00 55.35  ?  191  LYS D CG  1 
ATOM   7502  C CD  . LYS D  1  191 ? -14.173 -30.436 39.183  1.00 55.75  ?  191  LYS D CD  1 
ATOM   7503  C CE  . LYS D  1  191 ? -14.174 -31.461 40.316  1.00 56.55  ?  191  LYS D CE  1 
ATOM   7504  N NZ  . LYS D  1  191 ? -15.335 -32.394 40.229  1.00 57.15  ?  191  LYS D NZ  1 
ATOM   7505  N N   . VAL D  1  192 ? -11.951 -25.272 37.014  1.00 52.27  ?  192  VAL D N   1 
ATOM   7506  C CA  . VAL D  1  192 ? -12.063 -24.508 35.776  1.00 50.96  ?  192  VAL D CA  1 
ATOM   7507  C C   . VAL D  1  192 ? -10.781 -24.645 34.954  1.00 49.71  ?  192  VAL D C   1 
ATOM   7508  O O   . VAL D  1  192 ? -9.673  -24.774 35.495  1.00 49.89  ?  192  VAL D O   1 
ATOM   7509  C CB  . VAL D  1  192 ? -12.398 -23.034 36.078  1.00 51.47  ?  192  VAL D CB  1 
ATOM   7510  C CG1 . VAL D  1  192 ? -11.153 -22.238 36.463  1.00 51.76  ?  192  VAL D CG1 1 
ATOM   7511  C CG2 . VAL D  1  192 ? -13.093 -22.403 34.893  1.00 50.15  ?  192  VAL D CG2 1 
ATOM   7512  N N   . THR D  1  193 ? -10.937 -24.669 33.624  1.00 48.49  ?  193  THR D N   1 
ATOM   7513  C CA  . THR D  1  193 ? -9.800  -24.734 32.714  1.00 47.56  ?  193  THR D CA  1 
ATOM   7514  C C   . THR D  1  193 ? -9.697  -23.544 31.772  1.00 46.56  ?  193  THR D C   1 
ATOM   7515  O O   . THR D  1  193 ? -8.599  -23.278 31.267  1.00 45.99  ?  193  THR D O   1 
ATOM   7516  C CB  . THR D  1  193 ? -9.835  -26.016 31.861  1.00 47.54  ?  193  THR D CB  1 
ATOM   7517  O OG1 . THR D  1  193 ? -11.027 -26.039 31.066  1.00 47.67  ?  193  THR D OG1 1 
ATOM   7518  C CG2 . THR D  1  193 ? -9.786  -27.249 32.732  1.00 48.27  ?  193  THR D CG2 1 
ATOM   7519  N N   . GLU D  1  194 ? -10.798 -22.837 31.509  1.00 45.80  ?  194  GLU D N   1 
ATOM   7520  C CA  . GLU D  1  194 ? -10.776 -21.648 30.668  1.00 44.81  ?  194  GLU D CA  1 
ATOM   7521  C C   . GLU D  1  194 ? -11.671 -20.584 31.282  1.00 45.10  ?  194  GLU D C   1 
ATOM   7522  O O   . GLU D  1  194 ? -12.792 -20.878 31.710  1.00 45.76  ?  194  GLU D O   1 
ATOM   7523  C CB  . GLU D  1  194 ? -11.234 -21.964 29.240  1.00 44.31  ?  194  GLU D CB  1 
ATOM   7524  C CG  . GLU D  1  194 ? -11.377 -20.735 28.360  1.00 43.38  ?  194  GLU D CG  1 
ATOM   7525  C CD  . GLU D  1  194 ? -11.418 -21.072 26.880  1.00 43.40  ?  194  GLU D CD  1 
ATOM   7526  O OE1 . GLU D  1  194 ? -10.379 -21.513 26.343  1.00 43.55  ?  194  GLU D OE1 1 
ATOM   7527  O OE2 . GLU D  1  194 ? -12.481 -20.884 26.249  1.00 43.64  -1 194  GLU D OE2 1 
ATOM   7528  N N   . ILE D  1  195 ? -11.172 -19.352 31.330  1.00 42.60  ?  195  ILE D N   1 
ATOM   7529  C CA  . ILE D  1  195 ? -11.941 -18.200 31.779  1.00 43.25  ?  195  ILE D CA  1 
ATOM   7530  C C   . ILE D  1  195 ? -11.766 -17.096 30.749  1.00 42.16  ?  195  ILE D C   1 
ATOM   7531  O O   . ILE D  1  195 ? -10.633 -16.717 30.435  1.00 41.80  ?  195  ILE D O   1 
ATOM   7532  C CB  . ILE D  1  195 ? -11.496 -17.719 33.173  1.00 45.24  ?  195  ILE D CB  1 
ATOM   7533  C CG1 . ILE D  1  195 ? -11.858 -18.757 34.243  1.00 46.55  ?  195  ILE D CG1 1 
ATOM   7534  C CG2 . ILE D  1  195 ? -12.110 -16.362 33.482  1.00 46.51  ?  195  ILE D CG2 1 
ATOM   7535  C CD1 . ILE D  1  195 ? -11.309 -18.447 35.619  1.00 48.87  ?  195  ILE D CD1 1 
ATOM   7536  N N   . ALA D  1  196 ? -12.877 -16.576 30.232  1.00 44.64  ?  196  ALA D N   1 
ATOM   7537  C CA  . ALA D  1  196 ? -12.852 -15.513 29.230  1.00 43.72  ?  196  ALA D CA  1 
ATOM   7538  C C   . ALA D  1  196 ? -13.831 -14.425 29.655  1.00 44.68  ?  196  ALA D C   1 
ATOM   7539  O O   . ALA D  1  196 ? -15.042 -14.664 29.712  1.00 44.84  ?  196  ALA D O   1 
ATOM   7540  C CB  . ALA D  1  196 ? -13.199 -16.055 27.844  1.00 42.48  ?  196  ALA D CB  1 
ATOM   7541  N N   . ILE D  1  197 ? -13.301 -13.248 29.999  1.00 41.36  ?  197  ILE D N   1 
ATOM   7542  C CA  . ILE D  1  197 ? -14.114 -12.090 30.363  1.00 42.90  ?  197  ILE D CA  1 
ATOM   7543  C C   . ILE D  1  197 ? -13.684 -10.878 29.542  1.00 42.54  ?  197  ILE D C   1 
ATOM   7544  O O   . ILE D  1  197 ? -13.864 -9.732  29.967  1.00 44.58  ?  197  ILE D O   1 
ATOM   7545  C CB  . ILE D  1  197 ? -14.029 -11.793 31.873  1.00 46.19  ?  197  ILE D CB  1 
ATOM   7546  C CG1 . ILE D  1  197 ? -13.838 -13.079 32.668  1.00 46.44  ?  197  ILE D CG1 1 
ATOM   7547  C CG2 . ILE D  1  197 ? -15.295 -11.104 32.359  1.00 48.11  ?  197  ILE D CG2 1 
ATOM   7548  C CD1 . ILE D  1  197 ? -13.518 -12.839 34.115  1.00 49.93  ?  197  ILE D CD1 1 
ATOM   7549  N N   . TYR D  1  198 ? -13.084 -11.107 28.381  1.00 45.61  ?  198  TYR D N   1 
ATOM   7550  C CA  . TYR D  1  198 ? -12.477 -9.990  27.671  1.00 45.49  ?  198  TYR D CA  1 
ATOM   7551  C C   . TYR D  1  198 ? -13.532 -9.098  27.009  1.00 45.15  ?  198  TYR D C   1 
ATOM   7552  O O   . TYR D  1  198 ? -14.695 -9.473  26.843  1.00 44.57  ?  198  TYR D O   1 
ATOM   7553  C CB  . TYR D  1  198 ? -11.454 -10.486 26.641  1.00 43.74  ?  198  TYR D CB  1 
ATOM   7554  C CG  . TYR D  1  198 ? -11.967 -11.405 25.553  1.00 42.03  ?  198  TYR D CG  1 
ATOM   7555  C CD1 . TYR D  1  198 ? -12.517 -10.893 24.386  1.00 41.29  ?  198  TYR D CD1 1 
ATOM   7556  C CD2 . TYR D  1  198 ? -11.828 -12.785 25.661  1.00 41.73  ?  198  TYR D CD2 1 
ATOM   7557  C CE1 . TYR D  1  198 ? -12.958 -11.733 23.370  1.00 40.72  ?  198  TYR D CE1 1 
ATOM   7558  C CE2 . TYR D  1  198 ? -12.266 -13.633 24.655  1.00 41.19  ?  198  TYR D CE2 1 
ATOM   7559  C CZ  . TYR D  1  198 ? -12.832 -13.105 23.516  1.00 40.90  ?  198  TYR D CZ  1 
ATOM   7560  O OH  . TYR D  1  198 ? -13.266 -13.962 22.531  1.00 41.33  ?  198  TYR D OH  1 
ATOM   7561  N N   . ASP D  1  199 ? -13.101 -7.886  26.646  1.00 48.40  ?  199  ASP D N   1 
ATOM   7562  C CA  . ASP D  1  199 ? -13.954 -6.860  26.039  1.00 48.29  ?  199  ASP D CA  1 
ATOM   7563  C C   . ASP D  1  199 ? -15.120 -6.489  26.960  1.00 49.95  ?  199  ASP D C   1 
ATOM   7564  O O   . ASP D  1  199 ? -16.299 -6.613  26.611  1.00 49.12  ?  199  ASP D O   1 
ATOM   7565  C CB  . ASP D  1  199 ? -14.448 -7.296  24.656  1.00 46.03  ?  199  ASP D CB  1 
ATOM   7566  C CG  . ASP D  1  199 ? -14.997 -6.138  23.841  1.00 45.93  ?  199  ASP D CG  1 
ATOM   7567  O OD1 . ASP D  1  199 ? -15.025 -4.994  24.355  1.00 47.42  ?  199  ASP D OD1 1 
ATOM   7568  O OD2 . ASP D  1  199 ? -15.388 -6.374  22.678  1.00 44.72  -1 199  ASP D OD2 1 
ATOM   7569  N N   . ASN D  1  200 ? -14.758 -6.006  28.147  1.00 44.62  ?  200  ASN D N   1 
ATOM   7570  C CA  . ASN D  1  200 ? -15.706 -5.608  29.183  1.00 47.00  ?  200  ASN D CA  1 
ATOM   7571  C C   . ASN D  1  200 ? -15.229 -4.282  29.770  1.00 50.21  ?  200  ASN D C   1 
ATOM   7572  O O   . ASN D  1  200 ? -14.361 -3.610  29.205  1.00 50.14  ?  200  ASN D O   1 
ATOM   7573  C CB  . ASN D  1  200 ? -15.853 -6.712  30.238  1.00 48.10  ?  200  ASN D CB  1 
ATOM   7574  C CG  . ASN D  1  200 ? -16.968 -7.694  29.905  1.00 45.92  ?  200  ASN D CG  1 
ATOM   7575  O OD1 . ASN D  1  200 ? -18.142 -7.419  30.147  1.00 46.55  ?  200  ASN D OD1 1 
ATOM   7576  N ND2 . ASN D  1  200 ? -16.604 -8.845  29.354  1.00 43.65  ?  200  ASN D ND2 1 
ATOM   7577  N N   . LEU D  1  201 ? -15.835 -3.869  30.884  1.00 43.29  ?  201  LEU D N   1 
ATOM   7578  C CA  . LEU D  1  201 ? -15.453 -2.645  31.583  1.00 45.14  ?  201  LEU D CA  1 
ATOM   7579  C C   . LEU D  1  201 ? -14.878 -2.949  32.965  1.00 48.39  ?  201  LEU D C   1 
ATOM   7580  O O   . LEU D  1  201 ? -15.059 -2.171  33.903  1.00 51.54  ?  201  LEU D O   1 
ATOM   7581  C CB  . LEU D  1  201 ? -16.647 -1.699  31.709  1.00 45.67  ?  201  LEU D CB  1 
ATOM   7582  C CG  . LEU D  1  201 ? -17.262 -1.184  30.410  1.00 45.16  ?  201  LEU D CG  1 
ATOM   7583  C CD1 . LEU D  1  201 ? -18.693 -0.767  30.648  1.00 45.95  ?  201  LEU D CD1 1 
ATOM   7584  C CD2 . LEU D  1  201 ? -16.461 -0.026  29.881  1.00 45.70  ?  201  LEU D CD2 1 
ATOM   7585  N N   . LEU D  1  202 ? -14.188 -4.079  33.101  1.00 44.98  ?  202  LEU D N   1 
ATOM   7586  C CA  . LEU D  1  202 ? -13.664 -4.497  34.394  1.00 49.40  ?  202  LEU D CA  1 
ATOM   7587  C C   . LEU D  1  202 ? -12.604 -3.521  34.898  1.00 53.25  ?  202  LEU D C   1 
ATOM   7588  O O   . LEU D  1  202 ? -11.861 -2.916  34.123  1.00 52.15  ?  202  LEU D O   1 
ATOM   7589  C CB  . LEU D  1  202 ? -13.070 -5.905  34.300  1.00 47.50  ?  202  LEU D CB  1 
ATOM   7590  C CG  . LEU D  1  202 ? -13.953 -7.114  34.624  1.00 45.63  ?  202  LEU D CG  1 
ATOM   7591  C CD1 . LEU D  1  202 ? -15.348 -6.967  34.039  1.00 43.15  ?  202  LEU D CD1 1 
ATOM   7592  C CD2 . LEU D  1  202 ? -13.296 -8.385  34.108  1.00 42.44  ?  202  LEU D CD2 1 
ATOM   7593  N N   . THR D  1  203 ? -12.553 -3.361  36.216  1.00 52.41  ?  203  THR D N   1 
ATOM   7594  C CA  . THR D  1  203 ? -11.603 -2.487  36.891  1.00 54.03  ?  203  THR D CA  1 
ATOM   7595  C C   . THR D  1  203 ? -10.909 -3.265  38.004  1.00 55.33  ?  203  THR D C   1 
ATOM   7596  O O   . THR D  1  203 ? -11.206 -4.437  38.260  1.00 55.06  ?  203  THR D O   1 
ATOM   7597  C CB  . THR D  1  203 ? -12.289 -1.239  37.465  1.00 54.78  ?  203  THR D CB  1 
ATOM   7598  O OG1 . THR D  1  203 ? -13.201 -1.622  38.505  1.00 56.38  ?  203  THR D OG1 1 
ATOM   7599  C CG2 . THR D  1  203 ? -13.048 -0.494  36.385  1.00 52.23  ?  203  THR D CG2 1 
ATOM   7600  N N   . GLY D  1  204 ? -9.974  -2.600  38.675  1.00 57.92  ?  204  GLY D N   1 
ATOM   7601  C CA  . GLY D  1  204 ? -9.290  -3.183  39.804  1.00 58.51  ?  204  GLY D CA  1 
ATOM   7602  C C   . GLY D  1  204 ? -8.246  -4.209  39.415  1.00 56.13  ?  204  GLY D C   1 
ATOM   7603  O O   . GLY D  1  204 ? -7.975  -4.444  38.233  1.00 54.02  ?  204  GLY D O   1 
ATOM   7604  N N   . PRO D  1  205 ? -7.626  -4.831  40.411  1.00 57.32  ?  205  PRO D N   1 
ATOM   7605  C CA  . PRO D  1  205 ? -6.547  -5.780  40.135  1.00 54.66  ?  205  PRO D CA  1 
ATOM   7606  C C   . PRO D  1  205 ? -7.069  -7.141  39.695  1.00 52.20  ?  205  PRO D C   1 
ATOM   7607  O O   . PRO D  1  205 ? -8.238  -7.488  39.879  1.00 52.91  ?  205  PRO D O   1 
ATOM   7608  C CB  . PRO D  1  205 ? -5.826  -5.884  41.482  1.00 55.87  ?  205  PRO D CB  1 
ATOM   7609  C CG  . PRO D  1  205 ? -6.898  -5.652  42.474  1.00 58.46  ?  205  PRO D CG  1 
ATOM   7610  C CD  . PRO D  1  205 ? -7.837  -4.647  41.857  1.00 59.69  ?  205  PRO D CD  1 
ATOM   7611  N N   . ILE D  1  206 ? -6.169  -7.907  39.093  1.00 57.03  ?  206  ILE D N   1 
ATOM   7612  C CA  . ILE D  1  206 ? -6.424  -9.340  38.915  1.00 54.34  ?  206  ILE D CA  1 
ATOM   7613  C C   . ILE D  1  206 ? -6.372  -10.015 40.281  1.00 55.63  ?  206  ILE D C   1 
ATOM   7614  O O   . ILE D  1  206 ? -5.395  -9.821  41.025  1.00 56.59  ?  206  ILE D O   1 
ATOM   7615  C CB  . ILE D  1  206 ? -5.401  -9.950  37.958  1.00 50.93  ?  206  ILE D CB  1 
ATOM   7616  C CG1 . ILE D  1  206 ? -5.681  -9.501  36.525  1.00 49.15  ?  206  ILE D CG1 1 
ATOM   7617  C CG2 . ILE D  1  206 ? -5.439  -11.457 38.048  1.00 48.63  ?  206  ILE D CG2 1 
ATOM   7618  C CD1 . ILE D  1  206 ? -4.488  -9.614  35.610  1.00 46.79  ?  206  ILE D CD1 1 
ATOM   7619  N N   . PRO D  1  207 ? -7.391  -10.774 40.674  1.00 56.09  ?  207  PRO D N   1 
ATOM   7620  C CA  . PRO D  1  207 ? -7.401  -11.342 42.029  1.00 57.68  ?  207  PRO D CA  1 
ATOM   7621  C C   . PRO D  1  207 ? -6.241  -12.303 42.236  1.00 55.73  ?  207  PRO D C   1 
ATOM   7622  O O   . PRO D  1  207 ? -6.045  -13.245 41.465  1.00 52.86  ?  207  PRO D O   1 
ATOM   7623  C CB  . PRO D  1  207 ? -8.753  -12.061 42.100  1.00 57.71  ?  207  PRO D CB  1 
ATOM   7624  C CG  . PRO D  1  207 ? -9.588  -11.413 41.035  1.00 57.34  ?  207  PRO D CG  1 
ATOM   7625  C CD  . PRO D  1  207 ? -8.630  -11.071 39.938  1.00 55.00  ?  207  PRO D CD  1 
ATOM   7626  N N   . SER D  1  208 ? -5.469  -12.059 43.296  1.00 58.94  ?  208  SER D N   1 
ATOM   7627  C CA  . SER D  1  208 ? -4.339  -12.928 43.602  1.00 57.22  ?  208  SER D CA  1 
ATOM   7628  C C   . SER D  1  208 ? -4.777  -14.339 43.980  1.00 56.14  ?  208  SER D C   1 
ATOM   7629  O O   . SER D  1  208 ? -3.949  -15.257 43.966  1.00 54.22  ?  208  SER D O   1 
ATOM   7630  C CB  . SER D  1  208 ? -3.495  -12.317 44.717  1.00 58.82  ?  208  SER D CB  1 
ATOM   7631  O OG  . SER D  1  208 ? -4.310  -11.931 45.805  1.00 61.39  ?  208  SER D OG  1 
ATOM   7632  N N   . SER D  1  209 ? -6.053  -14.532 44.318  1.00 59.35  ?  209  SER D N   1 
ATOM   7633  C CA  . SER D  1  209 ? -6.574  -15.871 44.571  1.00 58.33  ?  209  SER D CA  1 
ATOM   7634  C C   . SER D  1  209 ? -6.604  -16.730 43.314  1.00 55.28  ?  209  SER D C   1 
ATOM   7635  O O   . SER D  1  209 ? -6.863  -17.936 43.415  1.00 54.10  ?  209  SER D O   1 
ATOM   7636  C CB  . SER D  1  209 ? -7.977  -15.785 45.181  1.00 60.64  ?  209  SER D CB  1 
ATOM   7637  O OG  . SER D  1  209 ? -8.893  -15.174 44.289  1.00 60.86  ?  209  SER D OG  1 
ATOM   7638  N N   . PHE D  1  210 ? -6.351  -16.138 42.142  1.00 57.14  ?  210  PHE D N   1 
ATOM   7639  C CA  . PHE D  1  210 ? -6.287  -16.899 40.902  1.00 54.08  ?  210  PHE D CA  1 
ATOM   7640  C C   . PHE D  1  210 ? -5.215  -17.977 40.947  1.00 52.42  ?  210  PHE D C   1 
ATOM   7641  O O   . PHE D  1  210 ? -5.272  -18.923 40.152  1.00 50.76  ?  210  PHE D O   1 
ATOM   7642  C CB  . PHE D  1  210 ? -6.034  -15.967 39.718  1.00 52.97  ?  210  PHE D CB  1 
ATOM   7643  C CG  . PHE D  1  210 ? -7.287  -15.404 39.107  1.00 52.97  ?  210  PHE D CG  1 
ATOM   7644  C CD1 . PHE D  1  210 ? -8.447  -15.285 39.855  1.00 55.06  ?  210  PHE D CD1 1 
ATOM   7645  C CD2 . PHE D  1  210 ? -7.306  -14.994 37.784  1.00 50.91  ?  210  PHE D CD2 1 
ATOM   7646  C CE1 . PHE D  1  210 ? -9.606  -14.763 39.293  1.00 55.10  ?  210  PHE D CE1 1 
ATOM   7647  C CE2 . PHE D  1  210 ? -8.461  -14.473 37.215  1.00 50.73  ?  210  PHE D CE2 1 
ATOM   7648  C CZ  . PHE D  1  210 ? -9.610  -14.356 37.970  1.00 52.83  ?  210  PHE D CZ  1 
ATOM   7649  N N   . GLY D  1  211 ? -4.232  -17.846 41.842  1.00 53.53  ?  211  GLY D N   1 
ATOM   7650  C CA  . GLY D  1  211 ? -3.233  -18.886 42.015  1.00 54.82  ?  211  GLY D CA  1 
ATOM   7651  C C   . GLY D  1  211 ? -3.808  -20.216 42.452  1.00 55.30  ?  211  GLY D C   1 
ATOM   7652  O O   . GLY D  1  211 ? -3.145  -21.249 42.304  1.00 56.07  ?  211  GLY D O   1 
ATOM   7653  N N   . ASN D  1  212 ? -5.027  -20.215 42.993  1.00 60.43  ?  212  ASN D N   1 
ATOM   7654  C CA  . ASN D  1  212 ? -5.702  -21.439 43.401  1.00 60.17  ?  212  ASN D CA  1 
ATOM   7655  C C   . ASN D  1  212 ? -6.324  -22.197 42.235  1.00 58.30  ?  212  ASN D C   1 
ATOM   7656  O O   . ASN D  1  212 ? -6.687  -23.366 42.403  1.00 57.74  ?  212  ASN D O   1 
ATOM   7657  C CB  . ASN D  1  212 ? -6.777  -21.113 44.442  1.00 62.63  ?  212  ASN D CB  1 
ATOM   7658  C CG  . ASN D  1  212 ? -6.187  -20.590 45.743  1.00 64.50  ?  212  ASN D CG  1 
ATOM   7659  O OD1 . ASN D  1  212 ? -4.972  -20.624 45.944  1.00 63.75  ?  212  ASN D OD1 1 
ATOM   7660  N ND2 . ASN D  1  212 ? -7.048  -20.111 46.638  1.00 66.96  ?  212  ASN D ND2 1 
ATOM   7661  N N   . LEU D  1  213 ? -6.432  -21.576 41.059  1.00 57.02  ?  213  LEU D N   1 
ATOM   7662  C CA  . LEU D  1  213 ? -7.039  -22.209 39.888  1.00 55.22  ?  213  LEU D CA  1 
ATOM   7663  C C   . LEU D  1  213 ? -6.002  -23.087 39.188  1.00 53.32  ?  213  LEU D C   1 
ATOM   7664  O O   . LEU D  1  213 ? -5.557  -22.809 38.074  1.00 52.01  ?  213  LEU D O   1 
ATOM   7665  C CB  . LEU D  1  213 ? -7.587  -21.155 38.938  1.00 54.82  ?  213  LEU D CB  1 
ATOM   7666  C CG  . LEU D  1  213 ? -8.534  -20.112 39.523  1.00 56.85  ?  213  LEU D CG  1 
ATOM   7667  C CD1 . LEU D  1  213 ? -8.734  -18.976 38.536  1.00 56.10  ?  213  LEU D CD1 1 
ATOM   7668  C CD2 . LEU D  1  213 ? -9.858  -20.758 39.872  1.00 57.48  ?  213  LEU D CD2 1 
ATOM   7669  N N   . THR D  1  214 ? -5.640  -24.185 39.861  1.00 59.26  ?  214  THR D N   1 
ATOM   7670  C CA  . THR D  1  214 ? -4.519  -25.009 39.408  1.00 57.94  ?  214  THR D CA  1 
ATOM   7671  C C   . THR D  1  214 ? -4.785  -25.657 38.053  1.00 56.58  ?  214  THR D C   1 
ATOM   7672  O O   . THR D  1  214 ? -3.846  -25.881 37.279  1.00 56.13  ?  214  THR D O   1 
ATOM   7673  C CB  . THR D  1  214 ? -4.200  -26.087 40.441  1.00 59.20  ?  214  THR D CB  1 
ATOM   7674  O OG1 . THR D  1  214 ? -5.384  -26.841 40.725  1.00 59.13  ?  214  THR D OG1 1 
ATOM   7675  C CG2 . THR D  1  214 ? -3.680  -25.460 41.722  1.00 60.71  ?  214  THR D CG2 1 
ATOM   7676  N N   . LYS D  1  215 ? -6.043  -25.958 37.743  1.00 56.64  ?  215  LYS D N   1 
ATOM   7677  C CA  . LYS D  1  215 ? -6.377  -26.621 36.489  1.00 55.56  ?  215  LYS D CA  1 
ATOM   7678  C C   . LYS D  1  215 ? -6.490  -25.662 35.308  1.00 54.82  ?  215  LYS D C   1 
ATOM   7679  O O   . LYS D  1  215 ? -6.765  -26.116 34.194  1.00 54.11  ?  215  LYS D O   1 
ATOM   7680  C CB  . LYS D  1  215 ? -7.689  -27.392 36.644  1.00 56.01  ?  215  LYS D CB  1 
ATOM   7681  C CG  . LYS D  1  215 ? -7.637  -28.504 37.678  1.00 56.60  ?  215  LYS D CG  1 
ATOM   7682  C CD  . LYS D  1  215 ? -7.041  -29.774 37.092  1.00 56.78  ?  215  LYS D CD  1 
ATOM   7683  C CE  . LYS D  1  215 ? -6.426  -30.660 38.172  1.00 58.91  ?  215  LYS D CE  1 
ATOM   7684  N NZ  . LYS D  1  215 ? -5.593  -31.758 37.599  1.00 60.15  ?  215  LYS D NZ  1 
ATOM   7685  N N   . LEU D  1  216 ? -6.298  -24.362 35.518  1.00 50.77  ?  216  LEU D N   1 
ATOM   7686  C CA  . LEU D  1  216 ? -6.477  -23.378 34.456  1.00 49.23  ?  216  LEU D CA  1 
ATOM   7687  C C   . LEU D  1  216 ? -5.453  -23.583 33.346  1.00 49.19  ?  216  LEU D C   1 
ATOM   7688  O O   . LEU D  1  216 ? -4.268  -23.787 33.619  1.00 50.33  ?  216  LEU D O   1 
ATOM   7689  C CB  . LEU D  1  216 ? -6.350  -21.968 35.038  1.00 49.03  ?  216  LEU D CB  1 
ATOM   7690  C CG  . LEU D  1  216 ? -6.819  -20.776 34.208  1.00 47.56  ?  216  LEU D CG  1 
ATOM   7691  C CD1 . LEU D  1  216 ? -8.319  -20.820 34.013  1.00 46.61  ?  216  LEU D CD1 1 
ATOM   7692  C CD2 . LEU D  1  216 ? -6.414  -19.490 34.895  1.00 47.86  ?  216  LEU D CD2 1 
ATOM   7693  N N   . VAL D  1  217 ? -5.909  -23.539 32.089  1.00 51.14  ?  217  VAL D N   1 
ATOM   7694  C CA  . VAL D  1  217 ? -5.022  -23.563 30.930  1.00 50.44  ?  217  VAL D CA  1 
ATOM   7695  C C   . VAL D  1  217 ? -5.094  -22.269 30.129  1.00 49.77  ?  217  VAL D C   1 
ATOM   7696  O O   . VAL D  1  217 ? -4.068  -21.779 29.646  1.00 49.46  ?  217  VAL D O   1 
ATOM   7697  C CB  . VAL D  1  217 ? -5.281  -24.786 30.016  1.00 50.46  ?  217  VAL D CB  1 
ATOM   7698  C CG1 . VAL D  1  217 ? -5.284  -26.067 30.834  1.00 51.00  ?  217  VAL D CG1 1 
ATOM   7699  C CG2 . VAL D  1  217 ? -6.568  -24.652 29.237  1.00 50.44  ?  217  VAL D CG2 1 
ATOM   7700  N N   . ASN D  1  218 ? -6.287  -21.699 29.969  1.00 47.16  ?  218  ASN D N   1 
ATOM   7701  C CA  . ASN D  1  218 ? -6.500  -20.497 29.173  1.00 46.38  ?  218  ASN D CA  1 
ATOM   7702  C C   . ASN D  1  218 ? -7.076  -19.399 30.052  1.00 46.72  ?  218  ASN D C   1 
ATOM   7703  O O   . ASN D  1  218 ? -8.063  -19.623 30.757  1.00 47.30  ?  218  ASN D O   1 
ATOM   7704  C CB  . ASN D  1  218 ? -7.453  -20.767 28.006  1.00 45.97  ?  218  ASN D CB  1 
ATOM   7705  C CG  . ASN D  1  218 ? -6.869  -21.709 26.983  1.00 46.29  ?  218  ASN D CG  1 
ATOM   7706  O OD1 . ASN D  1  218 ? -5.691  -22.061 27.052  1.00 46.48  ?  218  ASN D OD1 1 
ATOM   7707  N ND2 . ASN D  1  218 ? -7.684  -22.111 26.014  1.00 46.69  ?  218  ASN D ND2 1 
ATOM   7708  N N   . LEU D  1  219 ? -6.471  -18.216 30.012  1.00 41.81  ?  219  LEU D N   1 
ATOM   7709  C CA  . LEU D  1  219 ? -6.994  -17.054 30.726  1.00 41.86  ?  219  LEU D CA  1 
ATOM   7710  C C   . LEU D  1  219 ? -7.043  -15.879 29.761  1.00 41.08  ?  219  LEU D C   1 
ATOM   7711  O O   . LEU D  1  219 ? -5.998  -15.383 29.332  1.00 41.09  ?  219  LEU D O   1 
ATOM   7712  C CB  . LEU D  1  219 ? -6.143  -16.722 31.956  1.00 43.30  ?  219  LEU D CB  1 
ATOM   7713  C CG  . LEU D  1  219 ? -6.693  -15.651 32.910  1.00 44.34  ?  219  LEU D CG  1 
ATOM   7714  C CD1 . LEU D  1  219 ? -8.154  -15.902 33.209  1.00 44.22  ?  219  LEU D CD1 1 
ATOM   7715  C CD2 . LEU D  1  219 ? -5.899  -15.598 34.204  1.00 46.11  ?  219  LEU D CD2 1 
ATOM   7716  N N   . TYR D  1  220 ? -8.250  -15.425 29.430  1.00 45.33  ?  220  TYR D N   1 
ATOM   7717  C CA  . TYR D  1  220 ? -8.451  -14.330 28.486  1.00 44.66  ?  220  TYR D CA  1 
ATOM   7718  C C   . TYR D  1  220 ? -9.112  -13.164 29.211  1.00 46.14  ?  220  TYR D C   1 
ATOM   7719  O O   . TYR D  1  220 ? -10.289 -13.249 29.576  1.00 46.52  ?  220  TYR D O   1 
ATOM   7720  C CB  . TYR D  1  220 ? -9.304  -14.787 27.304  1.00 43.29  ?  220  TYR D CB  1 
ATOM   7721  C CG  . TYR D  1  220 ? -8.727  -15.966 26.558  1.00 42.78  ?  220  TYR D CG  1 
ATOM   7722  C CD1 . TYR D  1  220 ? -7.372  -16.025 26.262  1.00 42.74  ?  220  TYR D CD1 1 
ATOM   7723  C CD2 . TYR D  1  220 ? -9.535  -17.014 26.142  1.00 42.82  ?  220  TYR D CD2 1 
ATOM   7724  C CE1 . TYR D  1  220 ? -6.839  -17.095 25.583  1.00 42.79  ?  220  TYR D CE1 1 
ATOM   7725  C CE2 . TYR D  1  220 ? -9.011  -18.085 25.460  1.00 43.12  ?  220  TYR D CE2 1 
ATOM   7726  C CZ  . TYR D  1  220 ? -7.663  -18.120 25.185  1.00 43.11  ?  220  TYR D CZ  1 
ATOM   7727  O OH  . TYR D  1  220 ? -7.138  -19.189 24.507  1.00 43.80  ?  220  TYR D OH  1 
ATOM   7728  N N   . LEU D  1  221 ? -8.368  -12.062 29.397  1.00 39.15  ?  221  LEU D N   1 
ATOM   7729  C CA  . LEU D  1  221 ? -8.894  -10.908 30.124  1.00 39.54  ?  221  LEU D CA  1 
ATOM   7730  C C   . LEU D  1  221 ? -8.590  -9.585  29.419  1.00 39.42  ?  221  LEU D C   1 
ATOM   7731  O O   . LEU D  1  221 ? -8.558  -8.530  30.065  1.00 40.08  ?  221  LEU D O   1 
ATOM   7732  C CB  . LEU D  1  221 ? -8.344  -10.859 31.555  1.00 40.65  ?  221  LEU D CB  1 
ATOM   7733  C CG  . LEU D  1  221 ? -8.672  -12.026 32.489  1.00 41.07  ?  221  LEU D CG  1 
ATOM   7734  C CD1 . LEU D  1  221 ? -8.000  -11.845 33.841  1.00 42.39  ?  221  LEU D CD1 1 
ATOM   7735  C CD2 . LEU D  1  221 ? -10.176 -12.180 32.657  1.00 40.68  ?  221  LEU D CD2 1 
ATOM   7736  N N   . PHE D  1  222 ? -8.389  -9.608  28.103  1.00 44.30  ?  222  PHE D N   1 
ATOM   7737  C CA  . PHE D  1  222 ? -7.952  -8.394  27.429  1.00 44.79  ?  222  PHE D CA  1 
ATOM   7738  C C   . PHE D  1  222 ? -9.127  -7.436  27.201  1.00 45.31  ?  222  PHE D C   1 
ATOM   7739  O O   . PHE D  1  222 ? -10.290 -7.761  27.447  1.00 44.96  ?  222  PHE D O   1 
ATOM   7740  C CB  . PHE D  1  222 ? -7.231  -8.719  26.111  1.00 42.49  ?  222  PHE D CB  1 
ATOM   7741  C CG  . PHE D  1  222 ? -7.955  -9.692  25.213  1.00 40.29  ?  222  PHE D CG  1 
ATOM   7742  C CD1 . PHE D  1  222 ? -7.841  -11.062 25.406  1.00 39.66  ?  222  PHE D CD1 1 
ATOM   7743  C CD2 . PHE D  1  222 ? -8.707  -9.235  24.142  1.00 39.34  ?  222  PHE D CD2 1 
ATOM   7744  C CE1 . PHE D  1  222 ? -8.490  -11.955 24.566  1.00 38.67  ?  222  PHE D CE1 1 
ATOM   7745  C CE2 . PHE D  1  222 ? -9.354  -10.122 23.301  1.00 38.31  ?  222  PHE D CE2 1 
ATOM   7746  C CZ  . PHE D  1  222 ? -9.245  -11.483 23.514  1.00 38.16  ?  222  PHE D CZ  1 
ATOM   7747  N N   . ILE D  1  223 ? -8.793  -6.219  26.757  1.00 44.03  ?  223  ILE D N   1 
ATOM   7748  C CA  . ILE D  1  223 ? -9.752  -5.146  26.490  1.00 44.61  ?  223  ILE D CA  1 
ATOM   7749  C C   . ILE D  1  223 ? -10.583 -4.867  27.736  1.00 47.31  ?  223  ILE D C   1 
ATOM   7750  O O   . ILE D  1  223 ? -11.777 -5.182  27.791  1.00 46.30  ?  223  ILE D O   1 
ATOM   7751  C CB  . ILE D  1  223 ? -10.649 -5.477  25.280  1.00 41.53  ?  223  ILE D CB  1 
ATOM   7752  C CG1 . ILE D  1  223 ? -9.792  -5.947  24.098  1.00 39.59  ?  223  ILE D CG1 1 
ATOM   7753  C CG2 . ILE D  1  223 ? -11.486 -4.268  24.886  1.00 41.95  ?  223  ILE D CG2 1 
ATOM   7754  C CD1 . ILE D  1  223 ? -10.587 -6.464  22.929  1.00 38.31  ?  223  ILE D CD1 1 
ATOM   7755  N N   . ASN D  1  224 ? -9.956  -4.260  28.736  1.00 45.96  ?  224  ASN D N   1 
ATOM   7756  C CA  . ASN D  1  224 ? -10.597 -3.936  30.007  1.00 49.65  ?  224  ASN D CA  1 
ATOM   7757  C C   . ASN D  1  224 ? -9.843  -2.756  30.614  1.00 54.32  ?  224  ASN D C   1 
ATOM   7758  O O   . ASN D  1  224 ? -9.031  -2.108  29.944  1.00 54.18  ?  224  ASN D O   1 
ATOM   7759  C CB  . ASN D  1  224 ? -10.626 -5.154  30.940  1.00 50.18  ?  224  ASN D CB  1 
ATOM   7760  C CG  . ASN D  1  224 ? -11.876 -6.008  30.763  1.00 47.26  ?  224  ASN D CG  1 
ATOM   7761  O OD1 . ASN D  1  224 ? -12.976 -5.610  31.149  1.00 48.38  ?  224  ASN D OD1 1 
ATOM   7762  N ND2 . ASN D  1  224 ? -11.707 -7.194  30.189  1.00 43.71  ?  224  ASN D ND2 1 
ATOM   7763  N N   . SER D  1  225 ? -10.117 -2.466  31.886  1.00 49.62  ?  225  SER D N   1 
ATOM   7764  C CA  . SER D  1  225 ? -9.392  -1.424  32.603  1.00 53.52  ?  225  SER D CA  1 
ATOM   7765  C C   . SER D  1  225 ? -8.847  -1.944  33.926  1.00 56.54  ?  225  SER D C   1 
ATOM   7766  O O   . SER D  1  225 ? -8.791  -1.204  34.911  1.00 58.01  ?  225  SER D O   1 
ATOM   7767  C CB  . SER D  1  225 ? -10.273 -0.196  32.838  1.00 53.30  ?  225  SER D CB  1 
ATOM   7768  O OG  . SER D  1  225 ? -10.341 0.628   31.684  1.00 50.72  ?  225  SER D OG  1 
ATOM   7769  N N   . LEU D  1  226 ? -8.441  -3.214  33.960  1.00 54.16  ?  226  LEU D N   1 
ATOM   7770  C CA  . LEU D  1  226 ? -7.786  -3.768  35.138  1.00 54.23  ?  226  LEU D CA  1 
ATOM   7771  C C   . LEU D  1  226 ? -6.520  -2.980  35.441  1.00 54.85  ?  226  LEU D C   1 
ATOM   7772  O O   . LEU D  1  226 ? -5.839  -2.490  34.539  1.00 54.04  ?  226  LEU D O   1 
ATOM   7773  C CB  . LEU D  1  226 ? -7.441  -5.244  34.921  1.00 50.47  ?  226  LEU D CB  1 
ATOM   7774  C CG  . LEU D  1  226 ? -8.594  -6.188  34.578  1.00 48.44  ?  226  LEU D CG  1 
ATOM   7775  C CD1 . LEU D  1  226 ? -8.082  -7.561  34.178  1.00 45.98  ?  226  LEU D CD1 1 
ATOM   7776  C CD2 . LEU D  1  226 ? -9.534  -6.298  35.752  1.00 51.22  ?  226  LEU D CD2 1 
ATOM   7777  N N   . SER D  1  227 ? -6.200  -2.862  36.724  1.00 54.91  ?  227  SER D N   1 
ATOM   7778  C CA  . SER D  1  227 ? -5.140  -1.974  37.173  1.00 55.88  ?  227  SER D CA  1 
ATOM   7779  C C   . SER D  1  227 ? -4.256  -2.688  38.187  1.00 56.05  ?  227  SER D C   1 
ATOM   7780  O O   . SER D  1  227 ? -4.532  -3.814  38.607  1.00 55.43  ?  227  SER D O   1 
ATOM   7781  C CB  . SER D  1  227 ? -5.720  -0.689  37.775  1.00 58.21  ?  227  SER D CB  1 
ATOM   7782  O OG  . SER D  1  227 ? -6.634  -0.992  38.815  1.00 59.61  ?  227  SER D OG  1 
ATOM   7783  N N   . GLY D  1  228 ? -3.167  -2.019  38.565  1.00 63.87  ?  228  GLY D N   1 
ATOM   7784  C CA  . GLY D  1  228 ? -2.242  -2.563  39.534  1.00 63.79  ?  228  GLY D CA  1 
ATOM   7785  C C   . GLY D  1  228 ? -1.246  -3.522  38.910  1.00 61.11  ?  228  GLY D C   1 
ATOM   7786  O O   . GLY D  1  228 ? -1.148  -3.672  37.688  1.00 59.31  ?  228  GLY D O   1 
ATOM   7787  N N   . SER D  1  229 ? -0.499  -4.191  39.782  1.00 66.15  ?  229  SER D N   1 
ATOM   7788  C CA  . SER D  1  229 ? 0.524   -5.135  39.358  1.00 63.68  ?  229  SER D CA  1 
ATOM   7789  C C   . SER D  1  229 ? -0.068  -6.517  39.093  1.00 61.56  ?  229  SER D C   1 
ATOM   7790  O O   . SER D  1  229 ? -1.116  -6.893  39.625  1.00 62.25  ?  229  SER D O   1 
ATOM   7791  C CB  . SER D  1  229 ? 1.626   -5.237  40.410  1.00 64.06  ?  229  SER D CB  1 
ATOM   7792  O OG  . SER D  1  229 ? 2.151   -3.957  40.706  1.00 65.81  ?  229  SER D OG  1 
ATOM   7793  N N   . ILE D  1  230 ? 0.621   -7.270  38.245  1.00 66.12  ?  230  ILE D N   1 
ATOM   7794  C CA  . ILE D  1  230 ? 0.214   -8.650  37.958  1.00 63.76  ?  230  ILE D CA  1 
ATOM   7795  C C   . ILE D  1  230 ? 0.495   -9.519  39.181  1.00 64.06  ?  230  ILE D C   1 
ATOM   7796  O O   . ILE D  1  230 ? 1.612   -9.474  39.725  1.00 64.33  ?  230  ILE D O   1 
ATOM   7797  C CB  . ILE D  1  230 ? 0.951   -9.174  36.726  1.00 60.97  ?  230  ILE D CB  1 
ATOM   7798  C CG1 . ILE D  1  230 ? 0.949   -8.119  35.618  1.00 60.97  ?  230  ILE D CG1 1 
ATOM   7799  C CG2 . ILE D  1  230 ? 0.310   -10.453 36.231  1.00 58.48  ?  230  ILE D CG2 1 
ATOM   7800  C CD1 . ILE D  1  230 ? 1.673   -8.556  34.368  1.00 58.39  ?  230  ILE D CD1 1 
ATOM   7801  N N   . PRO D  1  231 ? -0.471  -10.301 39.662  1.00 61.45  ?  231  PRO D N   1 
ATOM   7802  C CA  . PRO D  1  231 ? -0.207  -11.152 40.829  1.00 61.69  ?  231  PRO D CA  1 
ATOM   7803  C C   . PRO D  1  231 ? 0.842   -12.203 40.500  1.00 59.31  ?  231  PRO D C   1 
ATOM   7804  O O   . PRO D  1  231 ? 0.770   -12.876 39.471  1.00 57.18  ?  231  PRO D O   1 
ATOM   7805  C CB  . PRO D  1  231 ? -1.572  -11.789 41.125  1.00 61.96  ?  231  PRO D CB  1 
ATOM   7806  C CG  . PRO D  1  231 ? -2.569  -10.998 40.343  1.00 62.49  ?  231  PRO D CG  1 
ATOM   7807  C CD  . PRO D  1  231 ? -1.843  -10.463 39.156  1.00 61.08  ?  231  PRO D CD  1 
ATOM   7808  N N   . SER D  1  232 ? 1.820   -12.352 41.394  1.00 68.05  ?  232  SER D N   1 
ATOM   7809  C CA  . SER D  1  232 ? 2.908   -13.290 41.138  1.00 66.05  ?  232  SER D CA  1 
ATOM   7810  C C   . SER D  1  232 ? 2.452   -14.745 41.176  1.00 64.55  ?  232  SER D C   1 
ATOM   7811  O O   . SER D  1  232 ? 3.162   -15.614 40.654  1.00 62.75  ?  232  SER D O   1 
ATOM   7812  C CB  . SER D  1  232 ? 4.038   -13.075 42.144  1.00 66.80  ?  232  SER D CB  1 
ATOM   7813  O OG  . SER D  1  232 ? 3.524   -12.682 43.403  1.00 68.69  ?  232  SER D OG  1 
ATOM   7814  N N   . GLU D  1  233 ? 1.294   -15.029 41.785  1.00 64.79  ?  233  GLU D N   1 
ATOM   7815  C CA  . GLU D  1  233 ? 0.772   -16.392 41.817  1.00 63.51  ?  233  GLU D CA  1 
ATOM   7816  C C   . GLU D  1  233 ? 0.415   -16.904 40.431  1.00 61.51  ?  233  GLU D C   1 
ATOM   7817  O O   . GLU D  1  233 ? 0.365   -18.123 40.228  1.00 60.06  ?  233  GLU D O   1 
ATOM   7818  C CB  . GLU D  1  233 ? -0.464  -16.475 42.713  1.00 65.09  ?  233  GLU D CB  1 
ATOM   7819  C CG  . GLU D  1  233 ? -0.191  -16.314 44.191  1.00 66.80  ?  233  GLU D CG  1 
ATOM   7820  C CD  . GLU D  1  233 ? 0.084   -14.881 44.570  1.00 68.74  ?  233  GLU D CD  1 
ATOM   7821  O OE1 . GLU D  1  233 ? -0.702  -14.003 44.160  1.00 69.95  ?  233  GLU D OE1 1 
ATOM   7822  O OE2 . GLU D  1  233 ? 1.083   -14.634 45.275  1.00 69.08  -1 233  GLU D OE2 1 
ATOM   7823  N N   . ILE D  1  234 ? 0.162   -16.001 39.479  1.00 61.61  ?  234  ILE D N   1 
ATOM   7824  C CA  . ILE D  1  234 ? -0.175  -16.416 38.122  1.00 59.57  ?  234  ILE D CA  1 
ATOM   7825  C C   . ILE D  1  234 ? 0.926   -17.298 37.544  1.00 57.80  ?  234  ILE D C   1 
ATOM   7826  O O   . ILE D  1  234 ? 0.651   -18.258 36.814  1.00 56.22  ?  234  ILE D O   1 
ATOM   7827  C CB  . ILE D  1  234 ? -0.433  -15.179 37.241  1.00 59.71  ?  234  ILE D CB  1 
ATOM   7828  C CG1 . ILE D  1  234 ? -1.536  -14.308 37.849  1.00 61.76  ?  234  ILE D CG1 1 
ATOM   7829  C CG2 . ILE D  1  234 ? -0.768  -15.585 35.810  1.00 57.36  ?  234  ILE D CG2 1 
ATOM   7830  C CD1 . ILE D  1  234 ? -2.929  -14.739 37.476  1.00 60.98  ?  234  ILE D CD1 1 
ATOM   7831  N N   . GLY D  1  235 ? 2.184   -17.011 37.887  1.00 64.34  ?  235  GLY D N   1 
ATOM   7832  C CA  . GLY D  1  235 ? 3.308   -17.775 37.367  1.00 63.24  ?  235  GLY D CA  1 
ATOM   7833  C C   . GLY D  1  235 ? 3.433   -19.185 37.916  1.00 63.91  ?  235  GLY D C   1 
ATOM   7834  O O   . GLY D  1  235 ? 4.276   -19.948 37.430  1.00 64.58  ?  235  GLY D O   1 
ATOM   7835  N N   . ASN D  1  236 ? 2.624   -19.551 38.906  1.00 65.41  ?  236  ASN D N   1 
ATOM   7836  C CA  . ASN D  1  236 ? 2.684   -20.879 39.498  1.00 66.80  ?  236  ASN D CA  1 
ATOM   7837  C C   . ASN D  1  236 ? 1.588   -21.808 38.992  1.00 65.53  ?  236  ASN D C   1 
ATOM   7838  O O   . ASN D  1  236 ? 1.457   -22.928 39.495  1.00 66.63  ?  236  ASN D O   1 
ATOM   7839  C CB  . ASN D  1  236 ? 2.627   -20.766 41.018  1.00 68.65  ?  236  ASN D CB  1 
ATOM   7840  C CG  . ASN D  1  236 ? 3.880   -20.145 41.593  1.00 70.53  ?  236  ASN D CG  1 
ATOM   7841  O OD1 . ASN D  1  236 ? 3.815   -19.304 42.488  1.00 71.38  ?  236  ASN D OD1 1 
ATOM   7842  N ND2 . ASN D  1  236 ? 5.033   -20.551 41.073  1.00 71.35  ?  236  ASN D ND2 1 
ATOM   7843  N N   . LEU D  1  237 ? 0.813   -21.383 38.008  1.00 63.79  ?  237  LEU D N   1 
ATOM   7844  C CA  . LEU D  1  237 ? -0.208  -22.246 37.434  1.00 62.70  ?  237  LEU D CA  1 
ATOM   7845  C C   . LEU D  1  237 ? 0.448   -23.290 36.537  1.00 62.96  ?  237  LEU D C   1 
ATOM   7846  O O   . LEU D  1  237 ? 1.067   -22.925 35.532  1.00 62.32  ?  237  LEU D O   1 
ATOM   7847  C CB  . LEU D  1  237 ? -1.205  -21.416 36.649  1.00 61.76  ?  237  LEU D CB  1 
ATOM   7848  C CG  . LEU D  1  237 ? -1.936  -20.432 37.557  1.00 63.41  ?  237  LEU D CG  1 
ATOM   7849  C CD1 . LEU D  1  237 ? -2.684  -19.368 36.757  1.00 63.31  ?  237  LEU D CD1 1 
ATOM   7850  C CD2 . LEU D  1  237 ? -2.862  -21.202 38.475  1.00 64.17  ?  237  LEU D CD2 1 
ATOM   7851  N N   . PRO D  1  238 ? 0.331   -24.583 36.847  1.00 65.61  ?  238  PRO D N   1 
ATOM   7852  C CA  . PRO D  1  238 ? 1.139   -25.589 36.142  1.00 66.45  ?  238  PRO D CA  1 
ATOM   7853  C C   . PRO D  1  238 ? 0.642   -25.920 34.741  1.00 64.92  ?  238  PRO D C   1 
ATOM   7854  O O   . PRO D  1  238 ? 1.447   -26.236 33.858  1.00 65.20  ?  238  PRO D O   1 
ATOM   7855  C CB  . PRO D  1  238 ? 1.043   -26.809 37.065  1.00 68.26  ?  238  PRO D CB  1 
ATOM   7856  C CG  . PRO D  1  238 ? -0.294  -26.662 37.714  1.00 67.46  ?  238  PRO D CG  1 
ATOM   7857  C CD  . PRO D  1  238 ? -0.525  -25.182 37.885  1.00 66.28  ?  238  PRO D CD  1 
ATOM   7858  N N   . ASN D  1  239 ? -0.672  -25.872 34.522  1.00 64.25  ?  239  ASN D N   1 
ATOM   7859  C CA  . ASN D  1  239 ? -1.253  -26.254 33.241  1.00 63.01  ?  239  ASN D CA  1 
ATOM   7860  C C   . ASN D  1  239 ? -1.527  -25.067 32.327  1.00 61.21  ?  239  ASN D C   1 
ATOM   7861  O O   . ASN D  1  239 ? -2.032  -25.264 31.217  1.00 60.29  ?  239  ASN D O   1 
ATOM   7862  C CB  . ASN D  1  239 ? -2.550  -27.044 33.461  1.00 62.76  ?  239  ASN D CB  1 
ATOM   7863  C CG  . ASN D  1  239 ? -2.376  -28.194 34.437  1.00 64.64  ?  239  ASN D CG  1 
ATOM   7864  O OD1 . ASN D  1  239 ? -1.253  -28.562 34.786  1.00 66.25  ?  239  ASN D OD1 1 
ATOM   7865  N ND2 . ASN D  1  239 ? -3.489  -28.771 34.880  1.00 64.57  ?  239  ASN D ND2 1 
ATOM   7866  N N   . LEU D  1  240 ? -1.206  -23.850 32.762  1.00 55.83  ?  240  LEU D N   1 
ATOM   7867  C CA  . LEU D  1  240 ? -1.466  -22.667 31.950  1.00 54.98  ?  240  LEU D CA  1 
ATOM   7868  C C   . LEU D  1  240 ? -0.740  -22.761 30.612  1.00 54.46  ?  240  LEU D C   1 
ATOM   7869  O O   . LEU D  1  240 ? 0.445   -23.107 30.557  1.00 55.06  ?  240  LEU D O   1 
ATOM   7870  C CB  . LEU D  1  240 ? -1.032  -21.413 32.710  1.00 55.52  ?  240  LEU D CB  1 
ATOM   7871  C CG  . LEU D  1  240 ? -1.456  -20.070 32.113  1.00 55.27  ?  240  LEU D CG  1 
ATOM   7872  C CD1 . LEU D  1  240 ? -2.955  -19.881 32.254  1.00 55.32  ?  240  LEU D CD1 1 
ATOM   7873  C CD2 . LEU D  1  240 ? -0.702  -18.920 32.764  1.00 56.26  ?  240  LEU D CD2 1 
ATOM   7874  N N   . ARG D  1  241 ? -1.463  -22.469 29.530  1.00 58.12  ?  241  ARG D N   1 
ATOM   7875  C CA  . ARG D  1  241 ? -0.906  -22.476 28.182  1.00 57.81  ?  241  ARG D CA  1 
ATOM   7876  C C   . ARG D  1  241 ? -0.956  -21.110 27.517  1.00 57.33  ?  241  ARG D C   1 
ATOM   7877  O O   . ARG D  1  241 ? 0.038   -20.679 26.922  1.00 57.32  ?  241  ARG D O   1 
ATOM   7878  C CB  . ARG D  1  241 ? -1.638  -23.503 27.308  1.00 57.99  ?  241  ARG D CB  1 
ATOM   7879  C CG  . ARG D  1  241 ? -1.787  -24.864 27.960  1.00 58.44  ?  241  ARG D CG  1 
ATOM   7880  C CD  . ARG D  1  241 ? -1.081  -25.945 27.161  1.00 59.09  ?  241  ARG D CD  1 
ATOM   7881  N NE  . ARG D  1  241 ? -1.133  -25.683 25.727  1.00 59.09  ?  241  ARG D NE  1 
ATOM   7882  C CZ  . ARG D  1  241 ? -0.209  -26.076 24.857  1.00 59.60  ?  241  ARG D CZ  1 
ATOM   7883  N NH1 . ARG D  1  241 ? 0.854   -26.771 25.242  1.00 60.33  ?  241  ARG D NH1 1 
ATOM   7884  N NH2 . ARG D  1  241 ? -0.350  -25.756 23.571  1.00 60.08  ?  241  ARG D NH2 1 
ATOM   7885  N N   . GLU D  1  242 ? -2.092  -20.422 27.579  1.00 50.66  ?  242  GLU D N   1 
ATOM   7886  C CA  . GLU D  1  242 ? -2.255  -19.115 26.956  1.00 50.11  ?  242  GLU D CA  1 
ATOM   7887  C C   . GLU D  1  242 ? -2.625  -18.095 28.022  1.00 50.34  ?  242  GLU D C   1 
ATOM   7888  O O   . GLU D  1  242 ? -3.536  -18.331 28.821  1.00 50.65  ?  242  GLU D O   1 
ATOM   7889  C CB  . GLU D  1  242 ? -3.319  -19.146 25.855  1.00 49.66  ?  242  GLU D CB  1 
ATOM   7890  C CG  . GLU D  1  242 ? -3.278  -20.390 24.988  1.00 50.27  ?  242  GLU D CG  1 
ATOM   7891  C CD  . GLU D  1  242 ? -3.891  -20.173 23.611  1.00 50.43  ?  242  GLU D CD  1 
ATOM   7892  O OE1 . GLU D  1  242 ? -5.014  -19.635 23.527  1.00 49.99  ?  242  GLU D OE1 1 
ATOM   7893  O OE2 . GLU D  1  242 ? -3.251  -20.546 22.607  1.00 51.28  -1 242  GLU D OE2 1 
ATOM   7894  N N   . LEU D  1  243 ? -1.906  -16.974 28.039  1.00 42.68  ?  243  LEU D N   1 
ATOM   7895  C CA  . LEU D  1  243 ? -2.150  -15.885 28.981  1.00 42.77  ?  243  LEU D CA  1 
ATOM   7896  C C   . LEU D  1  243 ? -2.216  -14.585 28.190  1.00 41.97  ?  243  LEU D C   1 
ATOM   7897  O O   . LEU D  1  243 ? -1.193  -14.110 27.687  1.00 42.18  ?  243  LEU D O   1 
ATOM   7898  C CB  . LEU D  1  243 ? -1.058  -15.828 30.051  1.00 44.16  ?  243  LEU D CB  1 
ATOM   7899  C CG  . LEU D  1  243 ? -1.204  -14.747 31.125  1.00 44.62  ?  243  LEU D CG  1 
ATOM   7900  C CD1 . LEU D  1  243 ? -2.556  -14.848 31.812  1.00 44.30  ?  243  LEU D CD1 1 
ATOM   7901  C CD2 . LEU D  1  243 ? -0.083  -14.827 32.148  1.00 46.25  ?  243  LEU D CD2 1 
ATOM   7902  N N   . CYS D  1  244 ? -3.414  -14.007 28.081  1.00 45.23  ?  244  CYS D N   1 
ATOM   7903  C CA  . CYS D  1  244 ? -3.644  -12.768 27.332  1.00 45.04  ?  244  CYS D CA  1 
ATOM   7904  C C   . CYS D  1  244 ? -4.161  -11.687 28.278  1.00 46.83  ?  244  CYS D C   1 
ATOM   7905  O O   . CYS D  1  244 ? -5.357  -11.633 28.577  1.00 46.98  ?  244  CYS D O   1 
ATOM   7906  C CB  . CYS D  1  244 ? -4.634  -12.987 26.193  1.00 43.53  ?  244  CYS D CB  1 
ATOM   7907  S SG  . CYS D  1  244 ? -4.108  -14.176 24.961  1.00 42.56  ?  244  CYS D SG  1 
ATOM   7908  N N   . LEU D  1  245 ? -3.267  -10.806 28.724  1.00 41.67  ?  245  LEU D N   1 
ATOM   7909  C CA  . LEU D  1  245 ? -3.628  -9.687  29.584  1.00 42.64  ?  245  LEU D CA  1 
ATOM   7910  C C   . LEU D  1  245 ? -3.453  -8.347  28.878  1.00 42.95  ?  245  LEU D C   1 
ATOM   7911  O O   . LEU D  1  245 ? -3.322  -7.313  29.543  1.00 45.61  ?  245  LEU D O   1 
ATOM   7912  C CB  . LEU D  1  245 ? -2.799  -9.715  30.867  1.00 44.40  ?  245  LEU D CB  1 
ATOM   7913  C CG  . LEU D  1  245 ? -2.773  -11.027 31.645  1.00 44.41  ?  245  LEU D CG  1 
ATOM   7914  C CD1 . LEU D  1  245 ? -2.013  -10.865 32.951  1.00 46.36  ?  245  LEU D CD1 1 
ATOM   7915  C CD2 . LEU D  1  245 ? -4.184  -11.482 31.903  1.00 43.96  ?  245  LEU D CD2 1 
ATOM   7916  N N   . ASP D  1  246 ? -3.438  -8.350  27.545  1.00 46.22  ?  246  ASP D N   1 
ATOM   7917  C CA  . ASP D  1  246 ? -3.174  -7.142  26.777  1.00 46.94  ?  246  ASP D CA  1 
ATOM   7918  C C   . ASP D  1  246 ? -4.324  -6.144  26.907  1.00 48.46  ?  246  ASP D C   1 
ATOM   7919  O O   . ASP D  1  246 ? -5.441  -6.486  27.299  1.00 48.17  ?  246  ASP D O   1 
ATOM   7920  C CB  . ASP D  1  246 ? -2.943  -7.468  25.298  1.00 44.26  ?  246  ASP D CB  1 
ATOM   7921  C CG  . ASP D  1  246 ? -4.033  -8.356  24.710  1.00 41.93  ?  246  ASP D CG  1 
ATOM   7922  O OD1 . ASP D  1  246 ? -4.130  -9.522  25.147  1.00 41.25  ?  246  ASP D OD1 1 
ATOM   7923  O OD2 . ASP D  1  246 ? -4.782  -7.902  23.812  1.00 41.03  -1 246  ASP D OD2 1 
ATOM   7924  N N   . ARG D  1  247 ? -4.024  -4.886  26.577  1.00 48.28  ?  247  ARG D N   1 
ATOM   7925  C CA  . ARG D  1  247 ? -5.016  -3.815  26.522  1.00 49.90  ?  247  ARG D CA  1 
ATOM   7926  C C   . ARG D  1  247 ? -5.730  -3.643  27.863  1.00 53.15  ?  247  ARG D C   1 
ATOM   7927  O O   . ARG D  1  247 ? -6.948  -3.808  27.980  1.00 52.32  ?  247  ARG D O   1 
ATOM   7928  C CB  . ARG D  1  247 ? -6.016  -4.061  25.389  1.00 46.29  ?  247  ARG D CB  1 
ATOM   7929  C CG  . ARG D  1  247 ? -5.431  -3.841  24.009  1.00 44.36  ?  247  ARG D CG  1 
ATOM   7930  C CD  . ARG D  1  247 ? -6.357  -4.345  22.925  1.00 41.24  ?  247  ARG D CD  1 
ATOM   7931  N NE  . ARG D  1  247 ? -6.225  -5.784  22.749  1.00 39.29  ?  247  ARG D NE  1 
ATOM   7932  C CZ  . ARG D  1  247 ? -6.783  -6.473  21.764  1.00 37.32  ?  247  ARG D CZ  1 
ATOM   7933  N NH1 . ARG D  1  247 ? -7.526  -5.881  20.842  1.00 36.76  ?  247  ARG D NH1 1 
ATOM   7934  N NH2 . ARG D  1  247 ? -6.593  -7.791  21.706  1.00 36.36  ?  247  ARG D NH2 1 
ATOM   7935  N N   . ASN D  1  248 ? -4.942  -3.305  28.881  1.00 50.52  ?  248  ASN D N   1 
ATOM   7936  C CA  . ASN D  1  248 ? -5.465  -3.008  30.210  1.00 54.69  ?  248  ASN D CA  1 
ATOM   7937  C C   . ASN D  1  248 ? -4.639  -1.863  30.788  1.00 58.69  ?  248  ASN D C   1 
ATOM   7938  O O   . ASN D  1  248 ? -3.848  -1.231  30.082  1.00 58.71  ?  248  ASN D O   1 
ATOM   7939  C CB  . ASN D  1  248 ? -5.454  -4.264  31.093  1.00 53.18  ?  248  ASN D CB  1 
ATOM   7940  C CG  . ASN D  1  248 ? -6.799  -4.978  31.108  1.00 51.43  ?  248  ASN D CG  1 
ATOM   7941  O OD1 . ASN D  1  248 ? -7.716  -4.566  31.812  1.00 54.44  ?  248  ASN D OD1 1 
ATOM   7942  N ND2 . ASN D  1  248 ? -6.916  -6.057  30.340  1.00 46.78  ?  248  ASN D ND2 1 
ATOM   7943  N N   . ASN D  1  249 ? -4.837  -1.564  32.068  1.00 63.67  ?  249  ASN D N   1 
ATOM   7944  C CA  . ASN D  1  249 ? -4.088  -0.511  32.743  1.00 65.36  ?  249  ASN D CA  1 
ATOM   7945  C C   . ASN D  1  249 ? -3.216  -1.091  33.850  1.00 65.23  ?  249  ASN D C   1 
ATOM   7946  O O   . ASN D  1  249 ? -3.055  -0.498  34.920  1.00 67.01  ?  249  ASN D O   1 
ATOM   7947  C CB  . ASN D  1  249 ? -5.029  0.563   33.286  1.00 67.07  ?  249  ASN D CB  1 
ATOM   7948  C CG  . ASN D  1  249 ? -5.122  1.762   32.364  1.00 66.61  ?  249  ASN D CG  1 
ATOM   7949  O OD1 . ASN D  1  249 ? -4.288  2.670   32.412  1.00 67.16  ?  249  ASN D OD1 1 
ATOM   7950  N ND2 . ASN D  1  249 ? -6.134  1.767   31.508  1.00 65.08  ?  249  ASN D ND2 1 
ATOM   7951  N N   . LEU D  1  250 ? -2.633  -2.258  33.597  1.00 61.14  ?  250  LEU D N   1 
ATOM   7952  C CA  . LEU D  1  250 ? -1.733  -2.869  34.564  1.00 60.75  ?  250  LEU D CA  1 
ATOM   7953  C C   . LEU D  1  250 ? -0.466  -2.036  34.710  1.00 61.68  ?  250  LEU D C   1 
ATOM   7954  O O   . LEU D  1  250 ? 0.046   -1.479  33.736  1.00 61.26  ?  250  LEU D O   1 
ATOM   7955  C CB  . LEU D  1  250 ? -1.376  -4.290  34.133  1.00 57.41  ?  250  LEU D CB  1 
ATOM   7956  C CG  . LEU D  1  250 ? -2.541  -5.273  34.071  1.00 55.93  ?  250  LEU D CG  1 
ATOM   7957  C CD1 . LEU D  1  250 ? -2.120  -6.561  33.388  1.00 52.12  ?  250  LEU D CD1 1 
ATOM   7958  C CD2 . LEU D  1  250 ? -3.052  -5.545  35.472  1.00 57.80  ?  250  LEU D CD2 1 
ATOM   7959  N N   . THR D  1  251 ? 0.040   -1.957  35.934  1.00 61.08  ?  251  THR D N   1 
ATOM   7960  C CA  . THR D  1  251 ? 1.270   -1.246  36.253  1.00 61.97  ?  251  THR D CA  1 
ATOM   7961  C C   . THR D  1  251 ? 2.251   -2.208  36.920  1.00 60.90  ?  251  THR D C   1 
ATOM   7962  O O   . THR D  1  251 ? 1.984   -3.403  37.067  1.00 59.38  ?  251  THR D O   1 
ATOM   7963  C CB  . THR D  1  251 ? 0.986   -0.042  37.157  1.00 64.71  ?  251  THR D CB  1 
ATOM   7964  O OG1 . THR D  1  251 ? 0.651   -0.498  38.476  1.00 65.63  ?  251  THR D OG1 1 
ATOM   7965  C CG2 . THR D  1  251 ? -0.168  0.775   36.605  1.00 65.58  ?  251  THR D CG2 1 
ATOM   7966  N N   . GLY D  1  252 ? 3.401   -1.673  37.324  1.00 64.81  ?  252  GLY D N   1 
ATOM   7967  C CA  . GLY D  1  252 ? 4.378   -2.457  38.052  1.00 63.96  ?  252  GLY D CA  1 
ATOM   7968  C C   . GLY D  1  252 ? 5.244   -3.326  37.158  1.00 61.51  ?  252  GLY D C   1 
ATOM   7969  O O   . GLY D  1  252 ? 5.202   -3.264  35.925  1.00 60.38  ?  252  GLY D O   1 
ATOM   7970  N N   . LYS D  1  253 ? 6.042   -4.162  37.814  1.00 66.91  ?  253  LYS D N   1 
ATOM   7971  C CA  . LYS D  1  253 ? 7.002   -5.027  37.146  1.00 64.73  ?  253  LYS D CA  1 
ATOM   7972  C C   . LYS D  1  253 ? 6.359   -6.345  36.720  1.00 62.59  ?  253  LYS D C   1 
ATOM   7973  O O   . LYS D  1  253 ? 5.341   -6.776  37.265  1.00 62.80  ?  253  LYS D O   1 
ATOM   7974  C CB  . LYS D  1  253 ? 8.191   -5.311  38.064  1.00 64.70  ?  253  LYS D CB  1 
ATOM   7975  C CG  . LYS D  1  253 ? 9.204   -4.187  38.139  1.00 65.97  ?  253  LYS D CG  1 
ATOM   7976  C CD  . LYS D  1  253 ? 10.381  -4.566  39.026  1.00 65.60  ?  253  LYS D CD  1 
ATOM   7977  C CE  . LYS D  1  253 ? 11.645  -4.807  38.203  1.00 64.43  ?  253  LYS D CE  1 
ATOM   7978  N NZ  . LYS D  1  253 ? 12.628  -3.679  38.264  1.00 65.57  ?  253  LYS D NZ  1 
ATOM   7979  N N   . ILE D  1  254 ? 6.968   -6.978  35.727  1.00 62.50  ?  254  ILE D N   1 
ATOM   7980  C CA  . ILE D  1  254 ? 6.552   -8.331  35.339  1.00 60.28  ?  254  ILE D CA  1 
ATOM   7981  C C   . ILE D  1  254 ? 7.062   -9.323  36.380  1.00 60.00  ?  254  ILE D C   1 
ATOM   7982  O O   . ILE D  1  254 ? 8.267   -9.323  36.690  1.00 60.26  ?  254  ILE D O   1 
ATOM   7983  C CB  . ILE D  1  254 ? 7.082   -8.675  33.947  1.00 58.34  ?  254  ILE D CB  1 
ATOM   7984  C CG1 . ILE D  1  254 ? 6.402   -7.813  32.884  1.00 58.29  ?  254  ILE D CG1 1 
ATOM   7985  C CG2 . ILE D  1  254 ? 6.874   -10.150 33.652  1.00 56.17  ?  254  ILE D CG2 1 
ATOM   7986  C CD1 . ILE D  1  254 ? 6.982   -7.998  31.509  1.00 56.61  ?  254  ILE D CD1 1 
ATOM   7987  N N   . PRO D  1  255 ? 6.205   -10.170 36.947  1.00 63.57  ?  255  PRO D N   1 
ATOM   7988  C CA  . PRO D  1  255 ? 6.657   -11.074 38.014  1.00 63.37  ?  255  PRO D CA  1 
ATOM   7989  C C   . PRO D  1  255 ? 7.683   -12.079 37.508  1.00 61.55  ?  255  PRO D C   1 
ATOM   7990  O O   . PRO D  1  255 ? 7.461   -12.779 36.517  1.00 59.90  ?  255  PRO D O   1 
ATOM   7991  C CB  . PRO D  1  255 ? 5.364   -11.764 38.468  1.00 63.27  ?  255  PRO D CB  1 
ATOM   7992  C CG  . PRO D  1  255 ? 4.260   -10.868 37.992  1.00 64.21  ?  255  PRO D CG  1 
ATOM   7993  C CD  . PRO D  1  255 ? 4.755   -10.275 36.713  1.00 63.44  ?  255  PRO D CD  1 
ATOM   7994  N N   . SER D  1  256 ? 8.821   -12.144 38.205  1.00 64.70  ?  256  SER D N   1 
ATOM   7995  C CA  . SER D  1  256 ? 9.847   -13.125 37.873  1.00 65.13  ?  256  SER D CA  1 
ATOM   7996  C C   . SER D  1  256 ? 9.356   -14.554 38.062  1.00 65.07  ?  256  SER D C   1 
ATOM   7997  O O   . SER D  1  256 ? 9.989   -15.492 37.564  1.00 65.44  ?  256  SER D O   1 
ATOM   7998  C CB  . SER D  1  256 ? 11.090  -12.886 38.726  1.00 67.84  ?  256  SER D CB  1 
ATOM   7999  O OG  . SER D  1  256 ? 10.752  -12.809 40.100  1.00 69.44  ?  256  SER D OG  1 
ATOM   8000  N N   . SER D  1  257 ? 8.243   -14.734 38.775  1.00 68.55  ?  257  SER D N   1 
ATOM   8001  C CA  . SER D  1  257 ? 7.621   -16.045 38.903  1.00 68.32  ?  257  SER D CA  1 
ATOM   8002  C C   . SER D  1  257 ? 7.186   -16.604 37.557  1.00 66.22  ?  257  SER D C   1 
ATOM   8003  O O   . SER D  1  257 ? 6.999   -17.821 37.433  1.00 66.29  ?  257  SER D O   1 
ATOM   8004  C CB  . SER D  1  257 ? 6.425   -15.952 39.848  1.00 68.19  ?  257  SER D CB  1 
ATOM   8005  O OG  . SER D  1  257 ? 6.689   -15.017 40.881  1.00 69.76  ?  257  SER D OG  1 
ATOM   8006  N N   . PHE D  1  258 ? 7.023   -15.744 36.547  1.00 63.06  ?  258  PHE D N   1 
ATOM   8007  C CA  . PHE D  1  258 ? 6.621   -16.206 35.225  1.00 61.21  ?  258  PHE D CA  1 
ATOM   8008  C C   . PHE D  1  258 ? 7.610   -17.204 34.641  1.00 62.00  ?  258  PHE D C   1 
ATOM   8009  O O   . PHE D  1  258 ? 7.246   -17.963 33.736  1.00 60.95  ?  258  PHE D O   1 
ATOM   8010  C CB  . PHE D  1  258 ? 6.454   -15.014 34.280  1.00 60.55  ?  258  PHE D CB  1 
ATOM   8011  C CG  . PHE D  1  258 ? 5.100   -14.365 34.352  1.00 61.03  ?  258  PHE D CG  1 
ATOM   8012  C CD1 . PHE D  1  258 ? 4.369   -14.379 35.530  1.00 62.22  ?  258  PHE D CD1 1 
ATOM   8013  C CD2 . PHE D  1  258 ? 4.554   -13.743 33.242  1.00 60.41  ?  258  PHE D CD2 1 
ATOM   8014  C CE1 . PHE D  1  258 ? 3.118   -13.783 35.598  1.00 62.95  ?  258  PHE D CE1 1 
ATOM   8015  C CE2 . PHE D  1  258 ? 3.303   -13.147 33.305  1.00 60.89  ?  258  PHE D CE2 1 
ATOM   8016  C CZ  . PHE D  1  258 ? 2.587   -13.168 34.485  1.00 62.25  ?  258  PHE D CZ  1 
ATOM   8017  N N   . GLY D  1  259 ? 8.843   -17.240 35.148  1.00 63.52  ?  259  GLY D N   1 
ATOM   8018  C CA  . GLY D  1  259 ? 9.807   -18.221 34.688  1.00 64.60  ?  259  GLY D CA  1 
ATOM   8019  C C   . GLY D  1  259 ? 9.409   -19.657 34.963  1.00 65.16  ?  259  GLY D C   1 
ATOM   8020  O O   . GLY D  1  259 ? 10.011  -20.568 34.383  1.00 65.81  ?  259  GLY D O   1 
ATOM   8021  N N   . ASN D  1  260 ? 8.421   -19.880 35.834  1.00 65.41  ?  260  ASN D N   1 
ATOM   8022  C CA  . ASN D  1  260 ? 7.933   -21.222 36.121  1.00 65.94  ?  260  ASN D CA  1 
ATOM   8023  C C   . ASN D  1  260 ? 6.882   -21.700 35.131  1.00 63.89  ?  260  ASN D C   1 
ATOM   8024  O O   . ASN D  1  260 ? 6.567   -22.895 35.120  1.00 64.32  ?  260  ASN D O   1 
ATOM   8025  C CB  . ASN D  1  260 ? 7.359   -21.282 37.535  1.00 66.95  ?  260  ASN D CB  1 
ATOM   8026  C CG  . ASN D  1  260 ? 8.326   -20.769 38.572  1.00 69.16  ?  260  ASN D CG  1 
ATOM   8027  O OD1 . ASN D  1  260 ? 9.526   -21.033 38.500  1.00 70.78  ?  260  ASN D OD1 1 
ATOM   8028  N ND2 . ASN D  1  260 ? 7.813   -20.024 39.542  1.00 69.40  ?  260  ASN D ND2 1 
ATOM   8029  N N   . LEU D  1  261 ? 6.342   -20.808 34.302  1.00 62.51  ?  261  LEU D N   1 
ATOM   8030  C CA  . LEU D  1  261 ? 5.282   -21.163 33.361  1.00 60.64  ?  261  LEU D CA  1 
ATOM   8031  C C   . LEU D  1  261 ? 5.918   -21.923 32.200  1.00 60.75  ?  261  LEU D C   1 
ATOM   8032  O O   . LEU D  1  261 ? 6.144   -21.397 31.107  1.00 59.69  ?  261  LEU D O   1 
ATOM   8033  C CB  . LEU D  1  261 ? 4.546   -19.918 32.884  1.00 58.73  ?  261  LEU D CB  1 
ATOM   8034  C CG  . LEU D  1  261 ? 3.755   -19.132 33.923  1.00 58.54  ?  261  LEU D CG  1 
ATOM   8035  C CD1 . LEU D  1  261 ? 3.426   -17.761 33.382  1.00 58.02  ?  261  LEU D CD1 1 
ATOM   8036  C CD2 . LEU D  1  261 ? 2.492   -19.881 34.277  1.00 58.13  ?  261  LEU D CD2 1 
ATOM   8037  N N   . LYS D  1  262 ? 6.220   -23.196 32.455  1.00 62.63  ?  262  LYS D N   1 
ATOM   8038  C CA  . LYS D  1  262 ? 6.937   -24.017 31.488  1.00 63.22  ?  262  LYS D CA  1 
ATOM   8039  C C   . LYS D  1  262 ? 6.043   -24.582 30.391  1.00 61.83  ?  262  LYS D C   1 
ATOM   8040  O O   . LYS D  1  262 ? 6.565   -25.146 29.425  1.00 62.19  ?  262  LYS D O   1 
ATOM   8041  C CB  . LYS D  1  262 ? 7.654   -25.163 32.204  1.00 65.65  ?  262  LYS D CB  1 
ATOM   8042  C CG  . LYS D  1  262 ? 8.614   -24.708 33.289  1.00 67.43  ?  262  LYS D CG  1 
ATOM   8043  C CD  . LYS D  1  262 ? 9.882   -24.122 32.700  1.00 67.94  ?  262  LYS D CD  1 
ATOM   8044  C CE  . LYS D  1  262 ? 10.534  -25.088 31.730  1.00 68.72  ?  262  LYS D CE  1 
ATOM   8045  N NZ  . LYS D  1  262 ? 12.021  -24.964 31.736  1.00 70.58  ?  262  LYS D NZ  1 
ATOM   8046  N N   . ASN D  1  263 ? 4.722   -24.473 30.520  1.00 68.72  ?  263  ASN D N   1 
ATOM   8047  C CA  . ASN D  1  263 ? 3.809   -24.948 29.492  1.00 67.48  ?  263  ASN D CA  1 
ATOM   8048  C C   . ASN D  1  263 ? 3.188   -23.828 28.673  1.00 65.45  ?  263  ASN D C   1 
ATOM   8049  O O   . ASN D  1  263 ? 2.498   -24.115 27.687  1.00 64.50  ?  263  ASN D O   1 
ATOM   8050  C CB  . ASN D  1  263 ? 2.683   -25.783 30.119  1.00 67.54  ?  263  ASN D CB  1 
ATOM   8051  C CG  . ASN D  1  263 ? 3.073   -27.234 30.319  1.00 69.38  ?  263  ASN D CG  1 
ATOM   8052  O OD1 . ASN D  1  263 ? 3.863   -27.791 29.553  1.00 70.22  ?  263  ASN D OD1 1 
ATOM   8053  N ND2 . ASN D  1  263 ? 2.514   -27.857 31.353  1.00 70.15  ?  263  ASN D ND2 1 
ATOM   8054  N N   . VAL D  1  264 ? 3.411   -22.570 29.052  1.00 56.93  ?  264  VAL D N   1 
ATOM   8055  C CA  . VAL D  1  264 ? 2.788   -21.449 28.362  1.00 55.24  ?  264  VAL D CA  1 
ATOM   8056  C C   . VAL D  1  264 ? 3.411   -21.289 26.984  1.00 54.96  ?  264  VAL D C   1 
ATOM   8057  O O   . VAL D  1  264 ? 4.638   -21.235 26.839  1.00 55.79  ?  264  VAL D O   1 
ATOM   8058  C CB  . VAL D  1  264 ? 2.935   -20.163 29.187  1.00 55.37  ?  264  VAL D CB  1 
ATOM   8059  C CG1 . VAL D  1  264 ? 2.667   -18.941 28.320  1.00 54.62  ?  264  VAL D CG1 1 
ATOM   8060  C CG2 . VAL D  1  264 ? 2.001   -20.201 30.383  1.00 55.63  ?  264  VAL D CG2 1 
ATOM   8061  N N   . THR D  1  265 ? 2.563   -21.211 25.960  1.00 50.60  ?  265  THR D N   1 
ATOM   8062  C CA  . THR D  1  265 ? 3.023   -21.010 24.597  1.00 50.72  ?  265  THR D CA  1 
ATOM   8063  C C   . THR D  1  265 ? 2.712   -19.626 24.044  1.00 50.31  ?  265  THR D C   1 
ATOM   8064  O O   . THR D  1  265 ? 3.389   -19.193 23.108  1.00 50.61  ?  265  THR D O   1 
ATOM   8065  C CB  . THR D  1  265 ? 2.406   -22.067 23.672  1.00 51.22  ?  265  THR D CB  1 
ATOM   8066  O OG1 . THR D  1  265 ? 0.980   -22.019 23.786  1.00 50.92  ?  265  THR D OG1 1 
ATOM   8067  C CG2 . THR D  1  265 ? 2.876   -23.448 24.070  1.00 51.69  ?  265  THR D CG2 1 
ATOM   8068  N N   . LEU D  1  266 ? 1.716   -18.928 24.591  1.00 46.15  ?  266  LEU D N   1 
ATOM   8069  C CA  . LEU D  1  266 ? 1.342   -17.590 24.147  1.00 45.68  ?  266  LEU D CA  1 
ATOM   8070  C C   . LEU D  1  266 ? 1.278   -16.655 25.344  1.00 45.68  ?  266  LEU D C   1 
ATOM   8071  O O   . LEU D  1  266 ? 0.628   -16.973 26.344  1.00 45.77  ?  266  LEU D O   1 
ATOM   8072  C CB  . LEU D  1  266 ? -0.009  -17.604 23.431  1.00 45.24  ?  266  LEU D CB  1 
ATOM   8073  C CG  . LEU D  1  266 ? -0.660  -16.231 23.270  1.00 44.57  ?  266  LEU D CG  1 
ATOM   8074  C CD1 . LEU D  1  266 ? 0.139   -15.376 22.295  1.00 44.71  ?  266  LEU D CD1 1 
ATOM   8075  C CD2 . LEU D  1  266 ? -2.109  -16.368 22.823  1.00 44.17  ?  266  LEU D CD2 1 
ATOM   8076  N N   . LEU D  1  267 ? 1.949   -15.507 25.246  1.00 42.74  ?  267  LEU D N   1 
ATOM   8077  C CA  . LEU D  1  267 ? 1.918   -14.499 26.308  1.00 42.99  ?  267  LEU D CA  1 
ATOM   8078  C C   . LEU D  1  267 ? 1.718   -13.120 25.682  1.00 42.21  ?  267  LEU D C   1 
ATOM   8079  O O   . LEU D  1  267 ? 2.682   -12.470 25.270  1.00 42.52  ?  267  LEU D O   1 
ATOM   8080  C CB  . LEU D  1  267 ? 3.186   -14.538 27.153  1.00 44.44  ?  267  LEU D CB  1 
ATOM   8081  C CG  . LEU D  1  267 ? 3.173   -13.557 28.328  1.00 44.99  ?  267  LEU D CG  1 
ATOM   8082  C CD1 . LEU D  1  267 ? 1.897   -13.709 29.145  1.00 44.64  ?  267  LEU D CD1 1 
ATOM   8083  C CD2 . LEU D  1  267 ? 4.399   -13.743 29.203  1.00 46.67  ?  267  LEU D CD2 1 
ATOM   8084  N N   . ASN D  1  268 ? 0.468   -12.674 25.625  1.00 45.49  ?  268  ASN D N   1 
ATOM   8085  C CA  . ASN D  1  268 ? 0.132   -11.333 25.169  1.00 45.71  ?  268  ASN D CA  1 
ATOM   8086  C C   . ASN D  1  268 ? -0.133  -10.460 26.387  1.00 47.41  ?  268  ASN D C   1 
ATOM   8087  O O   . ASN D  1  268 ? -1.059  -10.732 27.159  1.00 47.64  ?  268  ASN D O   1 
ATOM   8088  C CB  . ASN D  1  268 ? -1.092  -11.354 24.256  1.00 44.42  ?  268  ASN D CB  1 
ATOM   8089  C CG  . ASN D  1  268 ? -0.798  -11.949 22.902  1.00 43.59  ?  268  ASN D CG  1 
ATOM   8090  O OD1 . ASN D  1  268 ? 0.360   -12.063 22.498  1.00 44.00  ?  268  ASN D OD1 1 
ATOM   8091  N ND2 . ASN D  1  268 ? -1.848  -12.322 22.181  1.00 42.83  ?  268  ASN D ND2 1 
ATOM   8092  N N   . MET D  1  269 ? 0.690   -9.427  26.569  1.00 44.43  ?  269  MET D N   1 
ATOM   8093  C CA  . MET D  1  269 ? 0.447   -8.428  27.604  1.00 46.89  ?  269  MET D CA  1 
ATOM   8094  C C   . MET D  1  269 ? 0.694   -7.025  27.072  1.00 48.34  ?  269  MET D C   1 
ATOM   8095  O O   . MET D  1  269 ? 1.010   -6.118  27.854  1.00 51.13  ?  269  MET D O   1 
ATOM   8096  C CB  . MET D  1  269 ? 1.318   -8.660  28.839  1.00 48.52  ?  269  MET D CB  1 
ATOM   8097  C CG  . MET D  1  269 ? 1.234   -10.059 29.395  1.00 47.41  ?  269  MET D CG  1 
ATOM   8098  S SD  . MET D  1  269 ? 1.770   -10.146 31.108  1.00 49.72  ?  269  MET D SD  1 
ATOM   8099  C CE  . MET D  1  269 ? 3.487   -9.647  30.965  1.00 50.51  ?  269  MET D CE  1 
ATOM   8100  N N   . PHE D  1  270 ? 0.571   -6.838  25.762  1.00 46.75  ?  270  PHE D N   1 
ATOM   8101  C CA  . PHE D  1  270 ? 0.885   -5.572  25.132  1.00 48.02  ?  270  PHE D CA  1 
ATOM   8102  C C   . PHE D  1  270 ? -0.161  -4.518  25.483  1.00 50.07  ?  270  PHE D C   1 
ATOM   8103  O O   . PHE D  1  270 ? -1.249  -4.816  25.983  1.00 49.87  ?  270  PHE D O   1 
ATOM   8104  C CB  . PHE D  1  270 ? 0.989   -5.740  23.617  1.00 45.86  ?  270  PHE D CB  1 
ATOM   8105  C CG  . PHE D  1  270 ? -0.216  -6.384  22.980  1.00 43.69  ?  270  PHE D CG  1 
ATOM   8106  C CD1 . PHE D  1  270 ? -1.279  -5.611  22.535  1.00 43.51  ?  270  PHE D CD1 1 
ATOM   8107  C CD2 . PHE D  1  270 ? -0.268  -7.759  22.791  1.00 42.47  ?  270  PHE D CD2 1 
ATOM   8108  C CE1 . PHE D  1  270 ? -2.375  -6.197  21.937  1.00 41.85  ?  270  PHE D CE1 1 
ATOM   8109  C CE2 . PHE D  1  270 ? -1.363  -8.347  22.192  1.00 41.31  ?  270  PHE D CE2 1 
ATOM   8110  C CZ  . PHE D  1  270 ? -2.418  -7.564  21.767  1.00 40.97  ?  270  PHE D CZ  1 
ATOM   8111  N N   . GLU D  1  271 ? 0.196   -3.261  25.212  1.00 52.03  ?  271  GLU D N   1 
ATOM   8112  C CA  . GLU D  1  271 ? -0.652  -2.098  25.476  1.00 54.96  ?  271  GLU D CA  1 
ATOM   8113  C C   . GLU D  1  271 ? -1.081  -2.051  26.941  1.00 57.84  ?  271  GLU D C   1 
ATOM   8114  O O   . GLU D  1  271 ? -2.263  -2.110  27.279  1.00 58.17  ?  271  GLU D O   1 
ATOM   8115  C CB  . GLU D  1  271 ? -1.867  -2.088  24.551  1.00 52.39  ?  271  GLU D CB  1 
ATOM   8116  C CG  . GLU D  1  271 ? -1.517  -2.140  23.093  1.00 49.66  ?  271  GLU D CG  1 
ATOM   8117  C CD  . GLU D  1  271 ? -2.484  -1.355  22.244  1.00 48.72  ?  271  GLU D CD  1 
ATOM   8118  O OE1 . GLU D  1  271 ? -3.264  -0.549  22.797  1.00 50.45  ?  271  GLU D OE1 1 
ATOM   8119  O OE2 . GLU D  1  271 ? -2.476  -1.560  21.016  1.00 46.35  -1 271  GLU D OE2 1 
ATOM   8120  N N   . ASN D  1  272 ? -0.080  -1.969  27.811  1.00 54.91  ?  272  ASN D N   1 
ATOM   8121  C CA  . ASN D  1  272 ? -0.284  -1.796  29.243  1.00 57.44  ?  272  ASN D CA  1 
ATOM   8122  C C   . ASN D  1  272 ? 0.624   -0.682  29.738  1.00 60.09  ?  272  ASN D C   1 
ATOM   8123  O O   . ASN D  1  272 ? 1.253   0.015   28.936  1.00 60.44  ?  272  ASN D O   1 
ATOM   8124  C CB  . ASN D  1  272 ? -0.012  -3.098  29.999  1.00 55.44  ?  272  ASN D CB  1 
ATOM   8125  C CG  . ASN D  1  272 ? -1.259  -3.944  30.172  1.00 54.06  ?  272  ASN D CG  1 
ATOM   8126  O OD1 . ASN D  1  272 ? -2.083  -3.687  31.049  1.00 56.29  ?  272  ASN D OD1 1 
ATOM   8127  N ND2 . ASN D  1  272 ? -1.407  -4.958  29.328  1.00 50.35  ?  272  ASN D ND2 1 
ATOM   8128  N N   . GLN D  1  273 ? 0.699   -0.498  31.050  1.00 57.88  ?  273  GLN D N   1 
ATOM   8129  C CA  . GLN D  1  273 ? 1.626   0.455   31.641  1.00 59.64  ?  273  GLN D CA  1 
ATOM   8130  C C   . GLN D  1  273 ? 2.689   -0.244  32.482  1.00 59.00  ?  273  GLN D C   1 
ATOM   8131  O O   . GLN D  1  273 ? 3.174   0.315   33.469  1.00 60.67  ?  273  GLN D O   1 
ATOM   8132  C CB  . GLN D  1  273 ? 0.870   1.486   32.471  1.00 62.02  ?  273  GLN D CB  1 
ATOM   8133  C CG  . GLN D  1  273 ? -0.177  2.237   31.686  1.00 62.48  ?  273  GLN D CG  1 
ATOM   8134  C CD  . GLN D  1  273 ? -0.469  3.583   32.292  1.00 64.21  ?  273  GLN D CD  1 
ATOM   8135  O OE1 . GLN D  1  273 ? 0.399   4.455   32.335  1.00 64.91  ?  273  GLN D OE1 1 
ATOM   8136  N NE2 . GLN D  1  273 ? -1.694  3.762   32.776  1.00 64.77  ?  273  GLN D NE2 1 
ATOM   8137  N N   . LEU D  1  274 ? 3.056   -1.467  32.094  1.00 60.60  ?  274  LEU D N   1 
ATOM   8138  C CA  . LEU D  1  274 ? 4.096   -2.213  32.790  1.00 59.83  ?  274  LEU D CA  1 
ATOM   8139  C C   . LEU D  1  274 ? 5.411   -1.441  32.774  1.00 60.84  ?  274  LEU D C   1 
ATOM   8140  O O   . LEU D  1  274 ? 5.741   -0.746  31.810  1.00 60.97  ?  274  LEU D O   1 
ATOM   8141  C CB  . LEU D  1  274 ? 4.292   -3.586  32.143  1.00 56.73  ?  274  LEU D CB  1 
ATOM   8142  C CG  . LEU D  1  274 ? 3.063   -4.489  32.057  1.00 55.19  ?  274  LEU D CG  1 
ATOM   8143  C CD1 . LEU D  1  274 ? 3.226   -5.554  30.978  1.00 51.89  ?  274  LEU D CD1 1 
ATOM   8144  C CD2 . LEU D  1  274 ? 2.801   -5.131  33.404  1.00 55.83  ?  274  LEU D CD2 1 
ATOM   8145  N N   . SER D  1  275 ? 6.166   -1.567  33.859  1.00 60.63  ?  275  SER D N   1 
ATOM   8146  C CA  . SER D  1  275 ? 7.378   -0.790  34.056  1.00 61.77  ?  275  SER D CA  1 
ATOM   8147  C C   . SER D  1  275 ? 8.494   -1.704  34.546  1.00 60.60  ?  275  SER D C   1 
ATOM   8148  O O   . SER D  1  275 ? 8.308   -2.909  34.737  1.00 59.00  ?  275  SER D O   1 
ATOM   8149  C CB  . SER D  1  275 ? 7.136   0.355   35.047  1.00 64.35  ?  275  SER D CB  1 
ATOM   8150  O OG  . SER D  1  275 ? 6.852   -0.148  36.343  1.00 64.75  ?  275  SER D OG  1 
ATOM   8151  N N   . GLY D  1  276 ? 9.668   -1.117  34.746  1.00 66.50  ?  276  GLY D N   1 
ATOM   8152  C CA  . GLY D  1  276 ? 10.811  -1.877  35.199  1.00 65.49  ?  276  GLY D CA  1 
ATOM   8153  C C   . GLY D  1  276 ? 11.547  -2.541  34.048  1.00 63.62  ?  276  GLY D C   1 
ATOM   8154  O O   . GLY D  1  276 ? 11.452  -2.138  32.884  1.00 63.39  ?  276  GLY D O   1 
ATOM   8155  N N   . GLU D  1  277 ? 12.280  -3.595  34.388  1.00 69.56  ?  277  GLU D N   1 
ATOM   8156  C CA  . GLU D  1  277 ? 13.093  -4.325  33.429  1.00 67.85  ?  277  GLU D CA  1 
ATOM   8157  C C   . GLU D  1  277 ? 12.528  -5.723  33.228  1.00 65.79  ?  277  GLU D C   1 
ATOM   8158  O O   . GLU D  1  277 ? 12.039  -6.345  34.176  1.00 65.64  ?  277  GLU D O   1 
ATOM   8159  C CB  . GLU D  1  277 ? 14.545  -4.414  33.897  1.00 67.96  ?  277  GLU D CB  1 
ATOM   8160  C CG  . GLU D  1  277 ? 15.057  -3.149  34.559  1.00 70.00  ?  277  GLU D CG  1 
ATOM   8161  C CD  . GLU D  1  277 ? 16.570  -3.062  34.546  1.00 69.98  ?  277  GLU D CD  1 
ATOM   8162  O OE1 . GLU D  1  277 ? 17.230  -4.124  34.618  1.00 68.78  ?  277  GLU D OE1 1 
ATOM   8163  O OE2 . GLU D  1  277 ? 17.097  -1.932  34.460  1.00 71.36  -1 277  GLU D OE2 1 
ATOM   8164  N N   . ILE D  1  278 ? 12.595  -6.207  31.991  1.00 58.61  ?  278  ILE D N   1 
ATOM   8165  C CA  . ILE D  1  278 ? 12.116  -7.546  31.660  1.00 57.56  ?  278  ILE D CA  1 
ATOM   8166  C C   . ILE D  1  278 ? 12.918  -8.565  32.458  1.00 59.37  ?  278  ILE D C   1 
ATOM   8167  O O   . ILE D  1  278 ? 14.148  -8.628  32.318  1.00 60.68  ?  278  ILE D O   1 
ATOM   8168  C CB  . ILE D  1  278 ? 12.222  -7.830  30.156  1.00 56.03  ?  278  ILE D CB  1 
ATOM   8169  C CG1 . ILE D  1  278 ? 11.363  -6.839  29.361  1.00 54.37  ?  278  ILE D CG1 1 
ATOM   8170  C CG2 . ILE D  1  278 ? 11.816  -9.265  29.879  1.00 55.32  ?  278  ILE D CG2 1 
ATOM   8171  C CD1 . ILE D  1  278 ? 11.604  -6.850  27.857  1.00 53.18  ?  278  ILE D CD1 1 
ATOM   8172  N N   . PRO D  1  279 ? 12.278  -9.367  33.303  1.00 64.42  ?  279  PRO D N   1 
ATOM   8173  C CA  . PRO D  1  279 ? 13.024  -10.303 34.156  1.00 64.55  ?  279  PRO D CA  1 
ATOM   8174  C C   . PRO D  1  279 ? 13.770  -11.330 33.325  1.00 64.49  ?  279  PRO D C   1 
ATOM   8175  O O   . PRO D  1  279 ? 13.188  -11.952 32.422  1.00 62.82  ?  279  PRO D O   1 
ATOM   8176  C CB  . PRO D  1  279 ? 11.928  -10.958 35.011  1.00 64.36  ?  279  PRO D CB  1 
ATOM   8177  C CG  . PRO D  1  279 ? 10.661  -10.754 34.242  1.00 63.40  ?  279  PRO D CG  1 
ATOM   8178  C CD  . PRO D  1  279 ? 10.821  -9.466  33.496  1.00 64.27  ?  279  PRO D CD  1 
ATOM   8179  N N   . PRO D  1  280 ? 15.060  -11.543 33.604  1.00 69.13  ?  280  PRO D N   1 
ATOM   8180  C CA  . PRO D  1  280 ? 15.827  -12.541 32.838  1.00 69.43  ?  280  PRO D CA  1 
ATOM   8181  C C   . PRO D  1  280 ? 15.277  -13.947 32.958  1.00 69.25  ?  280  PRO D C   1 
ATOM   8182  O O   . PRO D  1  280 ? 15.615  -14.803 32.130  1.00 69.06  ?  280  PRO D O   1 
ATOM   8183  C CB  . PRO D  1  280 ? 17.235  -12.444 33.442  1.00 72.11  ?  280  PRO D CB  1 
ATOM   8184  C CG  . PRO D  1  280 ? 17.284  -11.102 34.086  1.00 72.71  ?  280  PRO D CG  1 
ATOM   8185  C CD  . PRO D  1  280 ? 15.900  -10.840 34.588  1.00 71.40  ?  280  PRO D CD  1 
ATOM   8186  N N   . GLU D  1  281 ? 14.440  -14.209 33.965  1.00 72.22  ?  281  GLU D N   1 
ATOM   8187  C CA  . GLU D  1  281 ? 13.815  -15.509 34.162  1.00 72.09  ?  281  GLU D CA  1 
ATOM   8188  C C   . GLU D  1  281 ? 12.855  -15.869 33.037  1.00 69.65  ?  281  GLU D C   1 
ATOM   8189  O O   . GLU D  1  281 ? 12.491  -17.042 32.910  1.00 69.56  ?  281  GLU D O   1 
ATOM   8190  C CB  . GLU D  1  281 ? 13.081  -15.543 35.512  1.00 72.80  ?  281  GLU D CB  1 
ATOM   8191  C CG  . GLU D  1  281 ? 13.907  -15.067 36.721  1.00 75.34  ?  281  GLU D CG  1 
ATOM   8192  C CD  . GLU D  1  281 ? 14.080  -13.552 36.774  1.00 75.21  ?  281  GLU D CD  1 
ATOM   8193  O OE1 . GLU D  1  281 ? 14.198  -12.932 35.695  1.00 73.75  ?  281  GLU D OE1 1 
ATOM   8194  O OE2 . GLU D  1  281 ? 14.089  -12.977 37.884  1.00 76.66  -1 281  GLU D OE2 1 
ATOM   8195  N N   . ILE D  1  282 ? 12.460  -14.900 32.209  1.00 65.94  ?  282  ILE D N   1 
ATOM   8196  C CA  . ILE D  1  282 ? 11.550  -15.188 31.106  1.00 63.79  ?  282  ILE D CA  1 
ATOM   8197  C C   . ILE D  1  282 ? 12.163  -16.204 30.153  1.00 64.01  ?  282  ILE D C   1 
ATOM   8198  O O   . ILE D  1  282 ? 11.446  -17.006 29.541  1.00 62.97  ?  282  ILE D O   1 
ATOM   8199  C CB  . ILE D  1  282 ? 11.165  -13.880 30.389  1.00 62.19  ?  282  ILE D CB  1 
ATOM   8200  C CG1 . ILE D  1  282 ? 10.020  -13.196 31.136  1.00 62.13  ?  282  ILE D CG1 1 
ATOM   8201  C CG2 . ILE D  1  282 ? 10.785  -14.137 28.939  1.00 60.67  ?  282  ILE D CG2 1 
ATOM   8202  C CD1 . ILE D  1  282 ? 9.361   -12.092 30.361  1.00 62.15  ?  282  ILE D CD1 1 
ATOM   8203  N N   . GLY D  1  283 ? 13.493  -16.213 30.032  1.00 66.01  ?  283  GLY D N   1 
ATOM   8204  C CA  . GLY D  1  283 ? 14.166  -17.201 29.208  1.00 66.58  ?  283  GLY D CA  1 
ATOM   8205  C C   . GLY D  1  283 ? 13.901  -18.634 29.624  1.00 67.47  ?  283  GLY D C   1 
ATOM   8206  O O   . GLY D  1  283 ? 14.122  -19.553 28.829  1.00 67.63  ?  283  GLY D O   1 
ATOM   8207  N N   . ASN D  1  284 ? 13.440  -18.848 30.858  1.00 69.78  ?  284  ASN D N   1 
ATOM   8208  C CA  . ASN D  1  284 ? 13.054  -20.180 31.301  1.00 70.57  ?  284  ASN D CA  1 
ATOM   8209  C C   . ASN D  1  284 ? 11.675  -20.597 30.801  1.00 68.59  ?  284  ASN D C   1 
ATOM   8210  O O   . ASN D  1  284 ? 11.270  -21.741 31.036  1.00 69.13  ?  284  ASN D O   1 
ATOM   8211  C CB  . ASN D  1  284 ? 13.091  -20.261 32.827  1.00 72.25  ?  284  ASN D CB  1 
ATOM   8212  C CG  . ASN D  1  284 ? 14.363  -20.903 33.346  1.00 75.03  ?  284  ASN D CG  1 
ATOM   8213  O OD1 . ASN D  1  284 ? 14.800  -21.935 32.840  1.00 75.87  ?  284  ASN D OD1 1 
ATOM   8214  N ND2 . ASN D  1  284 ? 14.956  -20.295 34.372  1.00 76.65  ?  284  ASN D ND2 1 
ATOM   8215  N N   . MET D  1  285 ? 10.947  -19.705 30.126  1.00 63.62  ?  285  MET D N   1 
ATOM   8216  C CA  . MET D  1  285 ? 9.664   -20.045 29.507  1.00 61.79  ?  285  MET D CA  1 
ATOM   8217  C C   . MET D  1  285 ? 9.927   -20.777 28.191  1.00 61.55  ?  285  MET D C   1 
ATOM   8218  O O   . MET D  1  285 ? 9.645   -20.291 27.093  1.00 60.10  ?  285  MET D O   1 
ATOM   8219  C CB  . MET D  1  285 ? 8.826   -18.794 29.279  1.00 59.92  ?  285  MET D CB  1 
ATOM   8220  C CG  . MET D  1  285 ? 8.353   -18.109 30.550  1.00 60.11  ?  285  MET D CG  1 
ATOM   8221  S SD  . MET D  1  285 ? 6.839   -17.159 30.300  1.00 57.87  ?  285  MET D SD  1 
ATOM   8222  C CE  . MET D  1  285 ? 7.494   -15.497 30.247  1.00 58.42  ?  285  MET D CE  1 
ATOM   8223  N N   . THR D  1  286 ? 10.454  -21.992 28.324  1.00 59.98  ?  286  THR D N   1 
ATOM   8224  C CA  . THR D  1  286 ? 10.964  -22.766 27.192  1.00 60.39  ?  286  THR D CA  1 
ATOM   8225  C C   . THR D  1  286 ? 9.863   -23.318 26.292  1.00 59.00  ?  286  THR D C   1 
ATOM   8226  O O   . THR D  1  286 ? 10.164  -24.098 25.372  1.00 59.50  ?  286  THR D O   1 
ATOM   8227  C CB  . THR D  1  286 ? 11.837  -23.915 27.693  1.00 62.83  ?  286  THR D CB  1 
ATOM   8228  O OG1 . THR D  1  286 ? 11.030  -24.820 28.453  1.00 63.23  ?  286  THR D OG1 1 
ATOM   8229  C CG2 . THR D  1  286 ? 12.970  -23.387 28.568  1.00 64.47  ?  286  THR D CG2 1 
ATOM   8230  N N   . ALA D  1  287 ? 8.598   -22.974 26.521  1.00 57.67  ?  287  ALA D N   1 
ATOM   8231  C CA  . ALA D  1  287 ? 7.512   -23.390 25.649  1.00 56.37  ?  287  ALA D CA  1 
ATOM   8232  C C   . ALA D  1  287 ? 6.942   -22.245 24.832  1.00 54.45  ?  287  ALA D C   1 
ATOM   8233  O O   . ALA D  1  287 ? 6.020   -22.469 24.043  1.00 53.46  ?  287  ALA D O   1 
ATOM   8234  C CB  . ALA D  1  287 ? 6.392   -24.039 26.467  1.00 56.23  ?  287  ALA D CB  1 
ATOM   8235  N N   . LEU D  1  288 ? 7.461   -21.029 25.000  1.00 56.00  ?  288  LEU D N   1 
ATOM   8236  C CA  . LEU D  1  288 ? 6.877   -19.864 24.346  1.00 54.51  ?  288  LEU D CA  1 
ATOM   8237  C C   . LEU D  1  288 ? 6.966   -19.978 22.830  1.00 54.62  ?  288  LEU D C   1 
ATOM   8238  O O   . LEU D  1  288 ? 8.027   -20.267 22.272  1.00 55.34  ?  288  LEU D O   1 
ATOM   8239  C CB  . LEU D  1  288 ? 7.578   -18.585 24.811  1.00 54.66  ?  288  LEU D CB  1 
ATOM   8240  C CG  . LEU D  1  288 ? 7.015   -17.871 26.044  1.00 54.54  ?  288  LEU D CG  1 
ATOM   8241  C CD1 . LEU D  1  288 ? 7.858   -16.654 26.419  1.00 55.10  ?  288  LEU D CD1 1 
ATOM   8242  C CD2 . LEU D  1  288 ? 5.571   -17.473 25.806  1.00 53.62  ?  288  LEU D CD2 1 
ATOM   8243  N N   . ASP D  1  289 ? 5.842   -19.743 22.167  1.00 50.70  ?  289  ASP D N   1 
ATOM   8244  C CA  . ASP D  1  289 ? 5.775   -19.617 20.720  1.00 51.47  ?  289  ASP D CA  1 
ATOM   8245  C C   . ASP D  1  289 ? 5.649   -18.167 20.269  1.00 51.16  ?  289  ASP D C   1 
ATOM   8246  O O   . ASP D  1  289 ? 6.288   -17.767 19.292  1.00 51.94  ?  289  ASP D O   1 
ATOM   8247  C CB  . ASP D  1  289 ? 4.594   -20.432 20.190  1.00 51.89  ?  289  ASP D CB  1 
ATOM   8248  C CG  . ASP D  1  289 ? 4.146   -19.979 18.828  1.00 52.81  ?  289  ASP D CG  1 
ATOM   8249  O OD1 . ASP D  1  289 ? 4.798   -20.360 17.830  1.00 54.29  ?  289  ASP D OD1 1 
ATOM   8250  O OD2 . ASP D  1  289 ? 3.149   -19.230 18.761  1.00 52.17  -1 289  ASP D OD2 1 
ATOM   8251  N N   . THR D  1  290 ? 4.843   -17.367 20.971  1.00 47.16  ?  290  THR D N   1 
ATOM   8252  C CA  . THR D  1  290 ? 4.661   -15.951 20.681  1.00 46.74  ?  290  THR D CA  1 
ATOM   8253  C C   . THR D  1  290 ? 4.777   -15.165 21.979  1.00 46.31  ?  290  THR D C   1 
ATOM   8254  O O   . THR D  1  290 ? 4.180   -15.543 22.992  1.00 45.98  ?  290  THR D O   1 
ATOM   8255  C CB  . THR D  1  290 ? 3.299   -15.690 20.030  1.00 46.28  ?  290  THR D CB  1 
ATOM   8256  O OG1 . THR D  1  290 ? 3.295   -16.217 18.700  1.00 47.40  ?  290  THR D OG1 1 
ATOM   8257  C CG2 . THR D  1  290 ? 3.008   -14.197 19.978  1.00 45.65  ?  290  THR D CG2 1 
ATOM   8258  N N   . LEU D  1  291 ? 5.555   -14.085 21.953  1.00 46.87  ?  291  LEU D N   1 
ATOM   8259  C CA  . LEU D  1  291 ? 5.725   -13.204 23.101  1.00 47.19  ?  291  LEU D CA  1 
ATOM   8260  C C   . LEU D  1  291 ? 5.535   -11.767 22.642  1.00 47.38  ?  291  LEU D C   1 
ATOM   8261  O O   . LEU D  1  291 ? 6.277   -11.288 21.779  1.00 47.82  ?  291  LEU D O   1 
ATOM   8262  C CB  . LEU D  1  291 ? 7.106   -13.387 23.734  1.00 48.11  ?  291  LEU D CB  1 
ATOM   8263  C CG  . LEU D  1  291 ? 7.448   -12.386 24.840  1.00 49.12  ?  291  LEU D CG  1 
ATOM   8264  C CD1 . LEU D  1  291 ? 6.495   -12.545 26.027  1.00 49.12  ?  291  LEU D CD1 1 
ATOM   8265  C CD2 . LEU D  1  291 ? 8.907   -12.521 25.271  1.00 50.06  ?  291  LEU D CD2 1 
ATOM   8266  N N   . SER D  1  292 ? 4.562   -11.075 23.223  1.00 45.32  ?  292  SER D N   1 
ATOM   8267  C CA  . SER D  1  292 ? 4.216   -9.723  22.796  1.00 45.66  ?  292  SER D CA  1 
ATOM   8268  C C   . SER D  1  292 ? 4.076   -8.825  24.018  1.00 47.14  ?  292  SER D C   1 
ATOM   8269  O O   . SER D  1  292 ? 3.161   -9.008  24.829  1.00 47.13  ?  292  SER D O   1 
ATOM   8270  C CB  . SER D  1  292 ? 2.935   -9.723  21.967  1.00 44.43  ?  292  SER D CB  1 
ATOM   8271  O OG  . SER D  1  292 ? 2.584   -8.403  21.590  1.00 44.88  ?  292  SER D OG  1 
ATOM   8272  N N   . LEU D  1  293 ? 4.982   -7.855  24.147  1.00 45.17  ?  293  LEU D N   1 
ATOM   8273  C CA  . LEU D  1  293 ? 4.949   -6.879  25.230  1.00 47.38  ?  293  LEU D CA  1 
ATOM   8274  C C   . LEU D  1  293 ? 5.045   -5.460  24.686  1.00 48.94  ?  293  LEU D C   1 
ATOM   8275  O O   . LEU D  1  293 ? 5.627   -4.583  25.329  1.00 51.35  ?  293  LEU D O   1 
ATOM   8276  C CB  . LEU D  1  293 ? 6.069   -7.138  26.240  1.00 48.59  ?  293  LEU D CB  1 
ATOM   8277  C CG  . LEU D  1  293 ? 6.223   -8.571  26.764  1.00 47.39  ?  293  LEU D CG  1 
ATOM   8278  C CD1 . LEU D  1  293 ? 7.643   -8.837  27.215  1.00 48.17  ?  293  LEU D CD1 1 
ATOM   8279  C CD2 . LEU D  1  293 ? 5.258   -8.844  27.899  1.00 47.76  ?  293  LEU D CD2 1 
ATOM   8280  N N   . HIS D  1  294 ? 4.485   -5.221  23.500  1.00 47.85  ?  294  HIS D N   1 
ATOM   8281  C CA  . HIS D  1  294 ? 4.654   -3.935  22.841  1.00 49.36  ?  294  HIS D CA  1 
ATOM   8282  C C   . HIS D  1  294 ? 3.722   -2.882  23.437  1.00 51.57  ?  294  HIS D C   1 
ATOM   8283  O O   . HIS D  1  294 ? 2.733   -3.195  24.106  1.00 51.36  ?  294  HIS D O   1 
ATOM   8284  C CB  . HIS D  1  294 ? 4.441   -4.072  21.328  1.00 47.42  ?  294  HIS D CB  1 
ATOM   8285  C CG  . HIS D  1  294 ? 3.008   -4.188  20.905  1.00 45.83  ?  294  HIS D CG  1 
ATOM   8286  N ND1 . HIS D  1  294 ? 2.168   -3.100  20.806  1.00 46.85  ?  294  HIS D ND1 1 
ATOM   8287  C CD2 . HIS D  1  294 ? 2.282   -5.259  20.505  1.00 43.50  ?  294  HIS D CD2 1 
ATOM   8288  C CE1 . HIS D  1  294 ? 0.981   -3.498  20.385  1.00 44.85  ?  294  HIS D CE1 1 
ATOM   8289  N NE2 . HIS D  1  294 ? 1.023   -4.804  20.195  1.00 42.90  ?  294  HIS D NE2 1 
ATOM   8290  N N   . THR D  1  295 ? 4.064   -1.613  23.191  1.00 49.94  ?  295  THR D N   1 
ATOM   8291  C CA  . THR D  1  295 ? 3.320   -0.464  23.716  1.00 53.15  ?  295  THR D CA  1 
ATOM   8292  C C   . THR D  1  295 ? 3.200   -0.543  25.245  1.00 55.00  ?  295  THR D C   1 
ATOM   8293  O O   . THR D  1  295 ? 2.110   -0.646  25.816  1.00 55.47  ?  295  THR D O   1 
ATOM   8294  C CB  . THR D  1  295 ? 1.940   -0.328  23.050  1.00 51.85  ?  295  THR D CB  1 
ATOM   8295  O OG1 . THR D  1  295 ? 2.051   -0.542  21.637  1.00 48.92  ?  295  THR D OG1 1 
ATOM   8296  C CG2 . THR D  1  295 ? 1.377   1.062   23.273  1.00 55.79  ?  295  THR D CG2 1 
ATOM   8297  N N   . ASN D  1  296 ? 4.356   -0.504  25.904  1.00 55.33  ?  296  ASN D N   1 
ATOM   8298  C CA  . ASN D  1  296 ? 4.428   -0.536  27.362  1.00 56.75  ?  296  ASN D CA  1 
ATOM   8299  C C   . ASN D  1  296 ? 5.435   0.519   27.801  1.00 59.08  ?  296  ASN D C   1 
ATOM   8300  O O   . ASN D  1  296 ? 5.889   1.342   27.000  1.00 59.90  ?  296  ASN D O   1 
ATOM   8301  C CB  . ASN D  1  296 ? 4.802   -1.936  27.864  1.00 54.40  ?  296  ASN D CB  1 
ATOM   8302  C CG  . ASN D  1  296 ? 3.588   -2.796  28.151  1.00 52.99  ?  296  ASN D CG  1 
ATOM   8303  O OD1 . ASN D  1  296 ? 3.059   -2.796  29.263  1.00 54.37  ?  296  ASN D OD1 1 
ATOM   8304  N ND2 . ASN D  1  296 ? 3.129   -3.523  27.139  1.00 50.18  ?  296  ASN D ND2 1 
ATOM   8305  N N   . LYS D  1  297 ? 5.778   0.512   29.084  1.00 56.44  ?  297  LYS D N   1 
ATOM   8306  C CA  . LYS D  1  297 ? 6.740   1.456   29.637  1.00 58.30  ?  297  LYS D CA  1 
ATOM   8307  C C   . LYS D  1  297 ? 7.947   0.723   30.211  1.00 57.49  ?  297  LYS D C   1 
ATOM   8308  O O   . LYS D  1  297 ? 8.501   1.100   31.246  1.00 58.85  ?  297  LYS D O   1 
ATOM   8309  C CB  . LYS D  1  297 ? 6.078   2.360   30.674  1.00 60.52  ?  297  LYS D CB  1 
ATOM   8310  C CG  . LYS D  1  297 ? 5.181   3.409   30.029  1.00 61.58  ?  297  LYS D CG  1 
ATOM   8311  C CD  . LYS D  1  297 ? 4.508   4.315   31.038  1.00 63.46  ?  297  LYS D CD  1 
ATOM   8312  C CE  . LYS D  1  297 ? 3.573   5.291   30.334  1.00 63.94  ?  297  LYS D CE  1 
ATOM   8313  N NZ  . LYS D  1  297 ? 2.596   5.911   31.271  1.00 65.14  ?  297  LYS D NZ  1 
ATOM   8314  N N   . LEU D  1  298 ? 8.376   -0.326  29.513  1.00 61.23  ?  298  LEU D N   1 
ATOM   8315  C CA  . LEU D  1  298 ? 9.508   -1.132  29.945  1.00 60.29  ?  298  LEU D CA  1 
ATOM   8316  C C   . LEU D  1  298 ? 10.816  -0.387  29.703  1.00 61.34  ?  298  LEU D C   1 
ATOM   8317  O O   . LEU D  1  298 ? 10.938  0.414   28.774  1.00 61.93  ?  298  LEU D O   1 
ATOM   8318  C CB  . LEU D  1  298 ? 9.524   -2.467  29.196  1.00 57.49  ?  298  LEU D CB  1 
ATOM   8319  C CG  . LEU D  1  298 ? 8.770   -3.666  29.781  1.00 55.99  ?  298  LEU D CG  1 
ATOM   8320  C CD1 . LEU D  1  298 ? 7.478   -3.254  30.443  1.00 57.19  ?  298  LEU D CD1 1 
ATOM   8321  C CD2 . LEU D  1  298 ? 8.480   -4.676  28.692  1.00 53.28  ?  298  LEU D CD2 1 
ATOM   8322  N N   . THR D  1  299 ? 11.801  -0.655  30.558  1.00 65.00  ?  299  THR D N   1 
ATOM   8323  C CA  . THR D  1  299 ? 13.111  -0.027  30.457  1.00 65.92  ?  299  THR D CA  1 
ATOM   8324  C C   . THR D  1  299 ? 14.191  -1.077  30.683  1.00 64.56  ?  299  THR D C   1 
ATOM   8325  O O   . THR D  1  299 ? 13.909  -2.223  31.047  1.00 63.11  ?  299  THR D O   1 
ATOM   8326  C CB  . THR D  1  299 ? 13.272  1.121   31.464  1.00 68.23  ?  299  THR D CB  1 
ATOM   8327  O OG1 . THR D  1  299 ? 12.913  0.663   32.774  1.00 68.34  ?  299  THR D OG1 1 
ATOM   8328  C CG2 . THR D  1  299 ? 12.394  2.304   31.081  1.00 69.73  ?  299  THR D CG2 1 
ATOM   8329  N N   . GLY D  1  300 ? 15.443  -0.673  30.465  1.00 67.06  ?  300  GLY D N   1 
ATOM   8330  C CA  . GLY D  1  300 ? 16.571  -1.560  30.626  1.00 65.97  ?  300  GLY D CA  1 
ATOM   8331  C C   . GLY D  1  300 ? 16.909  -2.281  29.336  1.00 64.39  ?  300  GLY D C   1 
ATOM   8332  O O   . GLY D  1  300 ? 16.261  -2.085  28.304  1.00 64.03  ?  300  GLY D O   1 
ATOM   8333  N N   . PRO D  1  301 ? 17.925  -3.138  29.371  1.00 64.63  ?  301  PRO D N   1 
ATOM   8334  C CA  . PRO D  1  301 ? 18.327  -3.863  28.162  1.00 63.27  ?  301  PRO D CA  1 
ATOM   8335  C C   . PRO D  1  301 ? 17.445  -5.075  27.902  1.00 61.36  ?  301  PRO D C   1 
ATOM   8336  O O   . PRO D  1  301 ? 16.705  -5.543  28.768  1.00 60.95  ?  301  PRO D O   1 
ATOM   8337  C CB  . PRO D  1  301 ? 19.760  -4.294  28.481  1.00 63.24  ?  301  PRO D CB  1 
ATOM   8338  C CG  . PRO D  1  301 ? 19.740  -4.494  29.958  1.00 63.59  ?  301  PRO D CG  1 
ATOM   8339  C CD  . PRO D  1  301 ? 18.804  -3.442  30.513  1.00 64.85  ?  301  PRO D CD  1 
ATOM   8340  N N   . ILE D  1  302 ? 17.540  -5.582  26.681  1.00 58.14  ?  302  ILE D N   1 
ATOM   8341  C CA  . ILE D  1  302 ? 16.854  -6.835  26.345  1.00 56.97  ?  302  ILE D CA  1 
ATOM   8342  C C   . ILE D  1  302 ? 17.564  -7.991  27.042  1.00 58.56  ?  302  ILE D C   1 
ATOM   8343  O O   . ILE D  1  302 ? 18.801  -8.089  26.964  1.00 60.08  ?  302  ILE D O   1 
ATOM   8344  C CB  . ILE D  1  302 ? 16.826  -7.035  24.829  1.00 55.60  ?  302  ILE D CB  1 
ATOM   8345  C CG1 . ILE D  1  302 ? 16.071  -5.888  24.152  1.00 54.87  ?  302  ILE D CG1 1 
ATOM   8346  C CG2 . ILE D  1  302 ? 16.196  -8.368  24.478  1.00 54.68  ?  302  ILE D CG2 1 
ATOM   8347  C CD1 . ILE D  1  302 ? 16.161  -5.901  22.645  1.00 54.03  ?  302  ILE D CD1 1 
ATOM   8348  N N   . PRO D  1  303 ? 16.848  -8.876  27.740  1.00 60.59  ?  303  PRO D N   1 
ATOM   8349  C CA  . PRO D  1  303 ? 17.526  -9.967  28.458  1.00 61.15  ?  303  PRO D CA  1 
ATOM   8350  C C   . PRO D  1  303 ? 18.169  -10.949 27.491  1.00 61.25  ?  303  PRO D C   1 
ATOM   8351  O O   . PRO D  1  303 ? 17.516  -11.470 26.585  1.00 59.68  ?  303  PRO D O   1 
ATOM   8352  C CB  . PRO D  1  303 ? 16.398  -10.625 29.262  1.00 60.65  ?  303  PRO D CB  1 
ATOM   8353  C CG  . PRO D  1  303 ? 15.152  -10.257 28.542  1.00 58.94  ?  303  PRO D CG  1 
ATOM   8354  C CD  . PRO D  1  303 ? 15.390  -8.901  27.942  1.00 59.99  ?  303  PRO D CD  1 
ATOM   8355  N N   . SER D  1  304 ? 19.466  -11.198 27.697  1.00 64.39  ?  304  SER D N   1 
ATOM   8356  C CA  . SER D  1  304 ? 20.198  -12.144 26.861  1.00 64.90  ?  304  SER D CA  1 
ATOM   8357  C C   . SER D  1  304 ? 19.668  -13.566 26.995  1.00 64.85  ?  304  SER D C   1 
ATOM   8358  O O   . SER D  1  304 ? 19.983  -14.418 26.155  1.00 64.91  ?  304  SER D O   1 
ATOM   8359  C CB  . SER D  1  304 ? 21.688  -12.105 27.208  1.00 67.39  ?  304  SER D CB  1 
ATOM   8360  O OG  . SER D  1  304 ? 21.893  -12.368 28.585  1.00 69.24  ?  304  SER D OG  1 
ATOM   8361  N N   . THR D  1  305 ? 18.869  -13.839 28.027  1.00 65.07  ?  305  THR D N   1 
ATOM   8362  C CA  . THR D  1  305 ? 18.316  -15.170 28.240  1.00 65.12  ?  305  THR D CA  1 
ATOM   8363  C C   . THR D  1  305 ? 17.251  -15.542 27.214  1.00 62.88  ?  305  THR D C   1 
ATOM   8364  O O   . THR D  1  305 ? 16.855  -16.711 27.160  1.00 62.94  ?  305  THR D O   1 
ATOM   8365  C CB  . THR D  1  305 ? 17.748  -15.267 29.657  1.00 65.79  ?  305  THR D CB  1 
ATOM   8366  O OG1 . THR D  1  305 ? 16.719  -14.285 29.831  1.00 64.11  ?  305  THR D OG1 1 
ATOM   8367  C CG2 . THR D  1  305 ? 18.839  -15.006 30.671  1.00 68.34  ?  305  THR D CG2 1 
ATOM   8368  N N   . LEU D  1  306 ? 16.788  -14.591 26.395  1.00 62.56  ?  306  LEU D N   1 
ATOM   8369  C CA  . LEU D  1  306 ? 15.753  -14.889 25.410  1.00 60.57  ?  306  LEU D CA  1 
ATOM   8370  C C   . LEU D  1  306 ? 16.227  -15.885 24.362  1.00 60.90  ?  306  LEU D C   1 
ATOM   8371  O O   . LEU D  1  306 ? 15.395  -16.550 23.734  1.00 59.82  ?  306  LEU D O   1 
ATOM   8372  C CB  . LEU D  1  306 ? 15.286  -13.604 24.722  1.00 58.97  ?  306  LEU D CB  1 
ATOM   8373  C CG  . LEU D  1  306 ? 14.485  -12.606 25.561  1.00 58.60  ?  306  LEU D CG  1 
ATOM   8374  C CD1 . LEU D  1  306 ? 13.624  -11.750 24.659  1.00 58.25  ?  306  LEU D CD1 1 
ATOM   8375  C CD2 . LEU D  1  306 ? 13.625  -13.311 26.601  1.00 58.38  ?  306  LEU D CD2 1 
ATOM   8376  N N   . GLY D  1  307 ? 17.539  -16.005 24.158  1.00 61.61  ?  307  GLY D N   1 
ATOM   8377  C CA  . GLY D  1  307 ? 18.063  -16.992 23.231  1.00 62.25  ?  307  GLY D CA  1 
ATOM   8378  C C   . GLY D  1  307 ? 17.808  -18.425 23.644  1.00 63.17  ?  307  GLY D C   1 
ATOM   8379  O O   . GLY D  1  307 ? 17.956  -19.327 22.812  1.00 63.52  ?  307  GLY D O   1 
ATOM   8380  N N   . ASN D  1  308 ? 17.427  -18.657 24.902  1.00 64.93  ?  308  ASN D N   1 
ATOM   8381  C CA  . ASN D  1  308 ? 17.162  -20.015 25.363  1.00 65.94  ?  308  ASN D CA  1 
ATOM   8382  C C   . ASN D  1  308 ? 15.840  -20.562 24.841  1.00 64.22  ?  308  ASN D C   1 
ATOM   8383  O O   . ASN D  1  308 ? 15.675  -21.785 24.780  1.00 65.00  ?  308  ASN D O   1 
ATOM   8384  C CB  . ASN D  1  308 ? 17.175  -20.067 26.891  1.00 67.19  ?  308  ASN D CB  1 
ATOM   8385  C CG  . ASN D  1  308 ? 18.572  -19.902 27.468  1.00 69.56  ?  308  ASN D CG  1 
ATOM   8386  O OD1 . ASN D  1  308 ? 19.561  -19.818 26.732  1.00 70.31  ?  308  ASN D OD1 1 
ATOM   8387  N ND2 . ASN D  1  308 ? 18.660  -19.859 28.793  1.00 70.89  ?  308  ASN D ND2 1 
ATOM   8388  N N   . ILE D  1  309 ? 14.902  -19.695 24.462  1.00 61.31  ?  309  ILE D N   1 
ATOM   8389  C CA  . ILE D  1  309 ? 13.594  -20.139 23.995  1.00 59.74  ?  309  ILE D CA  1 
ATOM   8390  C C   . ILE D  1  309 ? 13.705  -20.513 22.524  1.00 59.36  ?  309  ILE D C   1 
ATOM   8391  O O   . ILE D  1  309 ? 13.575  -19.658 21.639  1.00 58.13  ?  309  ILE D O   1 
ATOM   8392  C CB  . ILE D  1  309 ? 12.518  -19.060 24.223  1.00 57.84  ?  309  ILE D CB  1 
ATOM   8393  C CG1 . ILE D  1  309 ? 12.636  -18.478 25.636  1.00 58.50  ?  309  ILE D CG1 1 
ATOM   8394  C CG2 . ILE D  1  309 ? 11.117  -19.626 23.978  1.00 56.53  ?  309  ILE D CG2 1 
ATOM   8395  C CD1 . ILE D  1  309 ? 11.884  -17.184 25.829  1.00 57.00  ?  309  ILE D CD1 1 
ATOM   8396  N N   . LYS D  1  310 ? 13.956  -21.795 22.256  1.00 58.00  ?  310  LYS D N   1 
ATOM   8397  C CA  . LYS D  1  310 ? 14.151  -22.267 20.891  1.00 58.07  ?  310  LYS D CA  1 
ATOM   8398  C C   . LYS D  1  310 ? 12.850  -22.412 20.113  1.00 56.43  ?  310  LYS D C   1 
ATOM   8399  O O   . LYS D  1  310 ? 12.897  -22.613 18.894  1.00 56.36  ?  310  LYS D O   1 
ATOM   8400  C CB  . LYS D  1  310 ? 14.891  -23.603 20.903  1.00 60.26  ?  310  LYS D CB  1 
ATOM   8401  C CG  . LYS D  1  310 ? 16.198  -23.589 21.682  1.00 62.25  ?  310  LYS D CG  1 
ATOM   8402  C CD  . LYS D  1  310 ? 17.111  -22.443 21.266  1.00 62.11  ?  310  LYS D CD  1 
ATOM   8403  C CE  . LYS D  1  310 ? 18.548  -22.716 21.705  1.00 64.55  ?  310  LYS D CE  1 
ATOM   8404  N NZ  . LYS D  1  310 ? 19.489  -21.607 21.383  1.00 64.62  ?  310  LYS D NZ  1 
ATOM   8405  N N   . THR D  1  311 ? 11.702  -22.325 20.779  1.00 55.76  ?  311  THR D N   1 
ATOM   8406  C CA  . THR D  1  311 ? 10.405  -22.390 20.121  1.00 54.37  ?  311  THR D CA  1 
ATOM   8407  C C   . THR D  1  311 ? 9.847   -21.021 19.752  1.00 53.73  ?  311  THR D C   1 
ATOM   8408  O O   . THR D  1  311 ? 8.880   -20.952 18.985  1.00 54.12  ?  311  THR D O   1 
ATOM   8409  C CB  . THR D  1  311 ? 9.399   -23.113 21.019  1.00 54.18  ?  311  THR D CB  1 
ATOM   8410  O OG1 . THR D  1  311 ? 9.408   -22.511 22.317  1.00 54.06  ?  311  THR D OG1 1 
ATOM   8411  C CG2 . THR D  1  311 ? 9.766   -24.568 21.154  1.00 55.93  ?  311  THR D CG2 1 
ATOM   8412  N N   . LEU D  1  312 ? 10.427  -19.941 20.271  1.00 53.85  ?  312  LEU D N   1 
ATOM   8413  C CA  . LEU D  1  312 ? 9.847   -18.613 20.108  1.00 53.49  ?  312  LEU D CA  1 
ATOM   8414  C C   . LEU D  1  312 ? 9.897   -18.187 18.645  1.00 54.51  ?  312  LEU D C   1 
ATOM   8415  O O   . LEU D  1  312 ? 10.977  -18.088 18.055  1.00 55.47  ?  312  LEU D O   1 
ATOM   8416  C CB  . LEU D  1  312 ? 10.592  -17.616 20.992  1.00 53.19  ?  312  LEU D CB  1 
ATOM   8417  C CG  . LEU D  1  312 ? 10.138  -16.158 20.964  1.00 52.90  ?  312  LEU D CG  1 
ATOM   8418  C CD1 . LEU D  1  312 ? 8.775   -15.994 21.616  1.00 51.96  ?  312  LEU D CD1 1 
ATOM   8419  C CD2 . LEU D  1  312 ? 11.176  -15.294 21.657  1.00 53.30  ?  312  LEU D CD2 1 
ATOM   8420  N N   . ALA D  1  313 ? 8.731   -17.943 18.051  1.00 48.80  ?  313  ALA D N   1 
ATOM   8421  C CA  . ALA D  1  313 ? 8.650   -17.581 16.643  1.00 50.01  ?  313  ALA D CA  1 
ATOM   8422  C C   . ALA D  1  313 ? 8.262   -16.131 16.399  1.00 49.45  ?  313  ALA D C   1 
ATOM   8423  O O   . ALA D  1  313 ? 8.655   -15.563 15.376  1.00 50.51  ?  313  ALA D O   1 
ATOM   8424  C CB  . ALA D  1  313 ? 7.659   -18.492 15.910  1.00 50.97  ?  313  ALA D CB  1 
ATOM   8425  N N   . VAL D  1  314 ? 7.481   -15.528 17.291  1.00 48.55  ?  314  VAL D N   1 
ATOM   8426  C CA  . VAL D  1  314 ? 7.084   -14.131 17.183  1.00 47.84  ?  314  VAL D CA  1 
ATOM   8427  C C   . VAL D  1  314 ? 7.570   -13.409 18.430  1.00 47.41  ?  314  VAL D C   1 
ATOM   8428  O O   . VAL D  1  314 ? 7.406   -13.914 19.546  1.00 47.17  ?  314  VAL D O   1 
ATOM   8429  C CB  . VAL D  1  314 ? 5.562   -13.985 17.016  1.00 46.99  ?  314  VAL D CB  1 
ATOM   8430  C CG1 . VAL D  1  314 ? 5.179   -12.523 16.830  1.00 46.33  ?  314  VAL D CG1 1 
ATOM   8431  C CG2 . VAL D  1  314 ? 5.084   -14.822 15.844  1.00 48.22  ?  314  VAL D CG2 1 
ATOM   8432  N N   . LEU D  1  315 ? 8.188   -12.244 18.241  1.00 46.99  ?  315  LEU D N   1 
ATOM   8433  C CA  . LEU D  1  315 ? 8.660   -11.426 19.356  1.00 47.02  ?  315  LEU D CA  1 
ATOM   8434  C C   . LEU D  1  315 ? 8.346   -9.970  19.045  1.00 47.18  ?  315  LEU D C   1 
ATOM   8435  O O   . LEU D  1  315 ? 8.967   -9.375  18.160  1.00 47.97  ?  315  LEU D O   1 
ATOM   8436  C CB  . LEU D  1  315 ? 10.157  -11.615 19.595  1.00 48.03  ?  315  LEU D CB  1 
ATOM   8437  C CG  . LEU D  1  315 ? 10.748  -10.801 20.748  1.00 48.62  ?  315  LEU D CG  1 
ATOM   8438  C CD1 . LEU D  1  315 ? 9.967   -11.053 22.019  1.00 48.08  ?  315  LEU D CD1 1 
ATOM   8439  C CD2 . LEU D  1  315 ? 12.209  -11.144 20.953  1.00 49.53  ?  315  LEU D CD2 1 
ATOM   8440  N N   . HIS D  1  316 ? 7.386   -9.401  19.767  1.00 46.88  ?  316  HIS D N   1 
ATOM   8441  C CA  . HIS D  1  316 ? 6.991   -8.004  19.606  1.00 47.31  ?  316  HIS D CA  1 
ATOM   8442  C C   . HIS D  1  316 ? 7.340   -7.265  20.896  1.00 48.59  ?  316  HIS D C   1 
ATOM   8443  O O   . HIS D  1  316 ? 6.624   -7.369  21.896  1.00 48.49  ?  316  HIS D O   1 
ATOM   8444  C CB  . HIS D  1  316 ? 5.504   -7.890  19.282  1.00 46.16  ?  316  HIS D CB  1 
ATOM   8445  C CG  . HIS D  1  316 ? 5.136   -8.410  17.929  1.00 45.54  ?  316  HIS D CG  1 
ATOM   8446  N ND1 . HIS D  1  316 ? 3.835   -8.451  17.476  1.00 44.61  ?  316  HIS D ND1 1 
ATOM   8447  C CD2 . HIS D  1  316 ? 5.898   -8.914  16.930  1.00 46.17  ?  316  HIS D CD2 1 
ATOM   8448  C CE1 . HIS D  1  316 ? 3.812   -8.952  16.254  1.00 44.91  ?  316  HIS D CE1 1 
ATOM   8449  N NE2 . HIS D  1  316 ? 5.051   -9.241  15.899  1.00 45.98  ?  316  HIS D NE2 1 
ATOM   8450  N N   . LEU D  1  317 ? 8.454   -6.531  20.875  1.00 45.39  ?  317  LEU D N   1 
ATOM   8451  C CA  . LEU D  1  317 ? 8.851   -5.684  21.993  1.00 46.34  ?  317  LEU D CA  1 
ATOM   8452  C C   . LEU D  1  317 ? 8.889   -4.211  21.613  1.00 46.44  ?  317  LEU D C   1 
ATOM   8453  O O   . LEU D  1  317 ? 9.450   -3.403  22.363  1.00 48.54  ?  317  LEU D O   1 
ATOM   8454  C CB  . LEU D  1  317 ? 10.220  -6.105  22.540  1.00 47.72  ?  317  LEU D CB  1 
ATOM   8455  C CG  . LEU D  1  317 ? 10.394  -7.536  23.052  1.00 48.13  ?  317  LEU D CG  1 
ATOM   8456  C CD1 . LEU D  1  317 ? 11.756  -7.719  23.713  1.00 49.82  ?  317  LEU D CD1 1 
ATOM   8457  C CD2 . LEU D  1  317 ? 9.277   -7.884  24.012  1.00 47.77  ?  317  LEU D CD2 1 
ATOM   8458  N N   . TYR D  1  318 ? 8.297   -3.836  20.483  1.00 49.65  ?  318  TYR D N   1 
ATOM   8459  C CA  . TYR D  1  318 ? 8.419   -2.474  19.995  1.00 51.53  ?  318  TYR D CA  1 
ATOM   8460  C C   . TYR D  1  318 ? 7.586   -1.512  20.842  1.00 53.42  ?  318  TYR D C   1 
ATOM   8461  O O   . TYR D  1  318 ? 6.745   -1.916  21.649  1.00 52.90  ?  318  TYR D O   1 
ATOM   8462  C CB  . TYR D  1  318 ? 8.012   -2.397  18.527  1.00 50.31  ?  318  TYR D CB  1 
ATOM   8463  C CG  . TYR D  1  318 ? 6.577   -2.780  18.234  1.00 48.34  ?  318  TYR D CG  1 
ATOM   8464  C CD1 . TYR D  1  318 ? 5.569   -1.823  18.236  1.00 47.51  ?  318  TYR D CD1 1 
ATOM   8465  C CD2 . TYR D  1  318 ? 6.237   -4.094  17.926  1.00 47.63  ?  318  TYR D CD2 1 
ATOM   8466  C CE1 . TYR D  1  318 ? 4.264   -2.162  17.949  1.00 45.78  ?  318  TYR D CE1 1 
ATOM   8467  C CE2 . TYR D  1  318 ? 4.929   -4.443  17.637  1.00 45.83  ?  318  TYR D CE2 1 
ATOM   8468  C CZ  . TYR D  1  318 ? 3.947   -3.469  17.651  1.00 44.82  ?  318  TYR D CZ  1 
ATOM   8469  O OH  . TYR D  1  318 ? 2.639   -3.789  17.368  1.00 43.22  ?  318  TYR D OH  1 
ATOM   8470  N N   . LEU D  1  319 ? 7.839   -0.215  20.643  1.00 49.34  ?  319  LEU D N   1 
ATOM   8471  C CA  . LEU D  1  319 ? 7.162   0.868   21.363  1.00 52.11  ?  319  LEU D CA  1 
ATOM   8472  C C   . LEU D  1  319 ? 7.348   0.736   22.877  1.00 53.24  ?  319  LEU D C   1 
ATOM   8473  O O   . LEU D  1  319 ? 6.394   0.579   23.646  1.00 53.42  ?  319  LEU D O   1 
ATOM   8474  C CB  . LEU D  1  319 ? 5.677   0.933   20.993  1.00 51.23  ?  319  LEU D CB  1 
ATOM   8475  C CG  . LEU D  1  319 ? 5.378   1.807   19.780  1.00 51.61  ?  319  LEU D CG  1 
ATOM   8476  C CD1 . LEU D  1  319 ? 3.971   1.579   19.295  1.00 48.97  ?  319  LEU D CD1 1 
ATOM   8477  C CD2 . LEU D  1  319 ? 5.587   3.259   20.127  1.00 56.30  ?  319  LEU D CD2 1 
ATOM   8478  N N   . ASN D  1  320 ? 8.612   0.805   23.289  1.00 57.90  ?  320  ASN D N   1 
ATOM   8479  C CA  . ASN D  1  320 ? 9.013   0.731   24.691  1.00 58.81  ?  320  ASN D CA  1 
ATOM   8480  C C   . ASN D  1  320 ? 10.179  1.694   24.889  1.00 60.81  ?  320  ASN D C   1 
ATOM   8481  O O   . ASN D  1  320 ? 10.453  2.547   24.038  1.00 61.86  ?  320  ASN D O   1 
ATOM   8482  C CB  . ASN D  1  320 ? 9.356   -0.712  25.084  1.00 56.45  ?  320  ASN D CB  1 
ATOM   8483  C CG  . ASN D  1  320 ? 8.172   -1.447  25.692  1.00 55.34  ?  320  ASN D CG  1 
ATOM   8484  O OD1 . ASN D  1  320 ? 7.794   -1.198  26.837  1.00 56.77  ?  320  ASN D OD1 1 
ATOM   8485  N ND2 . ASN D  1  320 ? 7.575   -2.352  24.922  1.00 52.78  ?  320  ASN D ND2 1 
ATOM   8486  N N   . GLN D  1  321 ? 10.853  1.585   26.030  1.00 62.28  ?  321  GLN D N   1 
ATOM   8487  C CA  . GLN D  1  321 ? 12.017  2.415   26.327  1.00 63.89  ?  321  GLN D CA  1 
ATOM   8488  C C   . GLN D  1  321 ? 13.228  1.549   26.661  1.00 62.87  ?  321  GLN D C   1 
ATOM   8489  O O   . GLN D  1  321 ? 14.050  1.895   27.516  1.00 63.98  ?  321  GLN D O   1 
ATOM   8490  C CB  . GLN D  1  321 ? 11.716  3.388   27.462  1.00 65.97  ?  321  GLN D CB  1 
ATOM   8491  C CG  . GLN D  1  321 ? 10.344  4.025   27.373  1.00 66.80  ?  321  GLN D CG  1 
ATOM   8492  C CD  . GLN D  1  321 ? 10.244  5.305   28.175  1.00 68.94  ?  321  GLN D CD  1 
ATOM   8493  O OE1 . GLN D  1  321 ? 9.240   5.556   28.851  1.00 69.58  ?  321  GLN D OE1 1 
ATOM   8494  N NE2 . GLN D  1  321 ? 11.289  6.124   28.110  1.00 70.02  ?  321  GLN D NE2 1 
ATOM   8495  N N   . LEU D  1  322 ? 13.346  0.402   25.998  1.00 61.47  ?  322  LEU D N   1 
ATOM   8496  C CA  . LEU D  1  322 ? 14.506  -0.461  26.181  1.00 60.50  ?  322  LEU D CA  1 
ATOM   8497  C C   . LEU D  1  322 ? 15.758  0.188   25.594  1.00 61.52  ?  322  LEU D C   1 
ATOM   8498  O O   . LEU D  1  322 ? 15.705  0.855   24.557  1.00 62.02  ?  322  LEU D O   1 
ATOM   8499  C CB  . LEU D  1  322 ? 14.260  -1.821  25.529  1.00 58.10  ?  322  LEU D CB  1 
ATOM   8500  C CG  . LEU D  1  322 ? 12.994  -2.577  25.936  1.00 56.93  ?  322  LEU D CG  1 
ATOM   8501  C CD1 . LEU D  1  322 ? 12.802  -3.807  25.061  1.00 55.16  ?  322  LEU D CD1 1 
ATOM   8502  C CD2 . LEU D  1  322 ? 13.050  -2.967  27.400  1.00 57.87  ?  322  LEU D CD2 1 
ATOM   8503  N N   . ASN D  1  323 ? 16.892  -0.017  26.258  1.00 67.57  ?  323  ASN D N   1 
ATOM   8504  C CA  . ASN D  1  323 ? 18.148  0.606   25.861  1.00 68.63  ?  323  ASN D CA  1 
ATOM   8505  C C   . ASN D  1  323 ? 19.248  -0.446  25.936  1.00 67.49  ?  323  ASN D C   1 
ATOM   8506  O O   . ASN D  1  323 ? 18.979  -1.644  26.072  1.00 65.83  ?  323  ASN D O   1 
ATOM   8507  C CB  . ASN D  1  323 ? 18.451  1.851   26.712  1.00 70.76  ?  323  ASN D CB  1 
ATOM   8508  C CG  . ASN D  1  323 ? 18.664  1.539   28.194  1.00 70.92  ?  323  ASN D CG  1 
ATOM   8509  O OD1 . ASN D  1  323 ? 18.394  0.434   28.671  1.00 69.52  ?  323  ASN D OD1 1 
ATOM   8510  N ND2 . ASN D  1  323 ? 19.156  2.539   28.929  1.00 72.60  ?  323  ASN D ND2 1 
ATOM   8511  N N   . GLY D  1  324 ? 20.499  0.003   25.816  1.00 63.16  ?  324  GLY D N   1 
ATOM   8512  C CA  . GLY D  1  324 ? 21.618  -0.913  25.749  1.00 64.24  ?  324  GLY D CA  1 
ATOM   8513  C C   . GLY D  1  324 ? 21.793  -1.464  24.346  1.00 62.92  ?  324  GLY D C   1 
ATOM   8514  O O   . GLY D  1  324 ? 21.244  -0.948  23.370  1.00 61.43  ?  324  GLY D O   1 
ATOM   8515  N N   . SER D  1  325 ? 22.576  -2.533  24.249  1.00 64.95  ?  325  SER D N   1 
ATOM   8516  C CA  . SER D  1  325 ? 22.904  -3.136  22.966  1.00 64.24  ?  325  SER D CA  1 
ATOM   8517  C C   . SER D  1  325 ? 22.159  -4.451  22.791  1.00 62.39  ?  325  SER D C   1 
ATOM   8518  O O   . SER D  1  325 ? 21.856  -5.147  23.765  1.00 61.57  ?  325  SER D O   1 
ATOM   8519  C CB  . SER D  1  325 ? 24.414  -3.371  22.841  1.00 64.69  ?  325  SER D CB  1 
ATOM   8520  O OG  . SER D  1  325 ? 25.130  -2.147  22.910  1.00 66.39  ?  325  SER D OG  1 
ATOM   8521  N N   . ILE D  1  326 ? 21.865  -4.784  21.536  1.00 58.68  ?  326  ILE D N   1 
ATOM   8522  C CA  . ILE D  1  326 ? 21.196  -6.037  21.198  1.00 57.63  ?  326  ILE D CA  1 
ATOM   8523  C C   . ILE D  1  326 ? 22.074  -7.201  21.637  1.00 59.24  ?  326  ILE D C   1 
ATOM   8524  O O   . ILE D  1  326 ? 23.219  -7.319  21.178  1.00 60.45  ?  326  ILE D O   1 
ATOM   8525  C CB  . ILE D  1  326 ? 20.893  -6.129  19.697  1.00 56.23  ?  326  ILE D CB  1 
ATOM   8526  C CG1 . ILE D  1  326 ? 19.948  -5.007  19.272  1.00 54.76  ?  326  ILE D CG1 1 
ATOM   8527  C CG2 . ILE D  1  326 ? 20.310  -7.490  19.368  1.00 55.50  ?  326  ILE D CG2 1 
ATOM   8528  C CD1 . ILE D  1  326 ? 19.756  -4.915  17.776  1.00 53.68  ?  326  ILE D CD1 1 
ATOM   8529  N N   . PRO D  1  327 ? 21.598  -8.069  22.523  1.00 61.15  ?  327  PRO D N   1 
ATOM   8530  C CA  . PRO D  1  327 ? 22.410  -9.212  22.952  1.00 61.09  ?  327  PRO D CA  1 
ATOM   8531  C C   . PRO D  1  327 ? 22.704  -10.135 21.784  1.00 60.86  ?  327  PRO D C   1 
ATOM   8532  O O   . PRO D  1  327 ? 21.789  -10.530 21.046  1.00 59.69  ?  327  PRO D O   1 
ATOM   8533  C CB  . PRO D  1  327 ? 21.526  -9.904  24.003  1.00 60.82  ?  327  PRO D CB  1 
ATOM   8534  C CG  . PRO D  1  327 ? 20.527  -8.860  24.422  1.00 60.04  ?  327  PRO D CG  1 
ATOM   8535  C CD  . PRO D  1  327 ? 20.294  -8.023  23.203  1.00 60.44  ?  327  PRO D CD  1 
ATOM   8536  N N   . PRO D  1  328 ? 23.973  -10.496 21.581  1.00 63.20  ?  328  PRO D N   1 
ATOM   8537  C CA  . PRO D  1  328 ? 24.305  -11.447 20.508  1.00 63.29  ?  328  PRO D CA  1 
ATOM   8538  C C   . PRO D  1  328 ? 23.609  -12.785 20.652  1.00 63.01  ?  328  PRO D C   1 
ATOM   8539  O O   . PRO D  1  328 ? 23.511  -13.523 19.664  1.00 62.63  ?  328  PRO D O   1 
ATOM   8540  C CB  . PRO D  1  328 ? 25.826  -11.601 20.632  1.00 65.69  ?  328  PRO D CB  1 
ATOM   8541  C CG  . PRO D  1  328 ? 26.272  -10.382 21.348  1.00 66.38  ?  328  PRO D CG  1 
ATOM   8542  C CD  . PRO D  1  328 ? 25.171  -10.032 22.296  1.00 65.36  ?  328  PRO D CD  1 
ATOM   8543  N N   . GLU D  1  329 ? 23.142  -13.131 21.855  1.00 62.30  ?  329  GLU D N   1 
ATOM   8544  C CA  . GLU D  1  329 ? 22.467  -14.401 22.079  1.00 62.18  ?  329  GLU D CA  1 
ATOM   8545  C C   . GLU D  1  329 ? 21.111  -14.471 21.394  1.00 59.84  ?  329  GLU D C   1 
ATOM   8546  O O   . GLU D  1  329 ? 20.571  -15.573 21.249  1.00 59.66  ?  329  GLU D O   1 
ATOM   8547  C CB  . GLU D  1  329 ? 22.313  -14.642 23.583  1.00 63.23  ?  329  GLU D CB  1 
ATOM   8548  C CG  . GLU D  1  329 ? 23.639  -14.708 24.342  1.00 65.90  ?  329  GLU D CG  1 
ATOM   8549  C CD  . GLU D  1  329 ? 24.134  -13.344 24.815  1.00 66.34  ?  329  GLU D CD  1 
ATOM   8550  O OE1 . GLU D  1  329 ? 23.743  -12.319 24.212  1.00 64.71  ?  329  GLU D OE1 1 
ATOM   8551  O OE2 . GLU D  1  329 ? 24.935  -13.299 25.778  1.00 68.49  -1 329  GLU D OE2 1 
ATOM   8552  N N   . LEU D  1  330 ? 20.560  -13.333 20.955  1.00 61.02  ?  330  LEU D N   1 
ATOM   8553  C CA  . LEU D  1  330 ? 19.274  -13.350 20.264  1.00 59.30  ?  330  LEU D CA  1 
ATOM   8554  C C   . LEU D  1  330 ? 19.346  -14.139 18.964  1.00 59.64  ?  330  LEU D C   1 
ATOM   8555  O O   . LEU D  1  330 ? 18.330  -14.683 18.514  1.00 59.14  ?  330  LEU D O   1 
ATOM   8556  C CB  . LEU D  1  330 ? 18.795  -11.923 19.986  1.00 59.62  ?  330  LEU D CB  1 
ATOM   8557  C CG  . LEU D  1  330 ? 18.330  -11.097 21.188  1.00 59.45  ?  330  LEU D CG  1 
ATOM   8558  C CD1 . LEU D  1  330 ? 17.408  -9.967  20.748  1.00 59.56  ?  330  LEU D CD1 1 
ATOM   8559  C CD2 . LEU D  1  330 ? 17.647  -11.981 22.220  1.00 58.44  ?  330  LEU D CD2 1 
ATOM   8560  N N   . GLY D  1  331 ? 20.530  -14.216 18.352  1.00 59.51  ?  331  GLY D N   1 
ATOM   8561  C CA  . GLY D  1  331 ? 20.722  -15.015 17.154  1.00 60.26  ?  331  GLY D CA  1 
ATOM   8562  C C   . GLY D  1  331 ? 20.552  -16.506 17.359  1.00 60.11  ?  331  GLY D C   1 
ATOM   8563  O O   . GLY D  1  331 ? 20.517  -17.251 16.374  1.00 60.53  ?  331  GLY D O   1 
ATOM   8564  N N   . GLU D  1  332 ? 20.436  -16.954 18.606  1.00 61.35  ?  332  GLU D N   1 
ATOM   8565  C CA  . GLU D  1  332 ? 20.198  -18.354 18.909  1.00 62.23  ?  332  GLU D CA  1 
ATOM   8566  C C   . GLU D  1  332 ? 18.715  -18.677 19.045  1.00 60.60  ?  332  GLU D C   1 
ATOM   8567  O O   . GLU D  1  332 ? 18.369  -19.789 19.455  1.00 61.24  ?  332  GLU D O   1 
ATOM   8568  C CB  . GLU D  1  332 ? 20.948  -18.743 20.183  1.00 64.19  ?  332  GLU D CB  1 
ATOM   8569  C CG  . GLU D  1  332 ? 22.342  -18.124 20.285  1.00 65.75  ?  332  GLU D CG  1 
ATOM   8570  C CD  . GLU D  1  332 ? 23.397  -18.826 19.421  1.00 67.41  ?  332  GLU D CD  1 
ATOM   8571  O OE1 . GLU D  1  332 ? 23.090  -19.866 18.796  1.00 67.56  ?  332  GLU D OE1 1 
ATOM   8572  O OE2 . GLU D  1  332 ? 24.545  -18.331 19.364  1.00 68.69  -1 332  GLU D OE2 1 
ATOM   8573  N N   . MET D  1  333 ? 17.831  -17.740 18.710  1.00 60.40  ?  333  MET D N   1 
ATOM   8574  C CA  . MET D  1  333 ? 16.396  -18.017 18.659  1.00 59.02  ?  333  MET D CA  1 
ATOM   8575  C C   . MET D  1  333 ? 16.095  -18.698 17.329  1.00 59.89  ?  333  MET D C   1 
ATOM   8576  O O   . MET D  1  333 ? 15.715  -18.054 16.351  1.00 60.67  ?  333  MET D O   1 
ATOM   8577  C CB  . MET D  1  333 ? 15.585  -16.739 18.835  1.00 58.37  ?  333  MET D CB  1 
ATOM   8578  C CG  . MET D  1  333 ? 15.726  -16.087 20.204  1.00 57.76  ?  333  MET D CG  1 
ATOM   8579  S SD  . MET D  1  333 ? 14.957  -14.451 20.312  1.00 57.50  ?  333  MET D SD  1 
ATOM   8580  C CE  . MET D  1  333 ? 15.074  -13.875 18.615  1.00 58.45  ?  333  MET D CE  1 
ATOM   8581  N N   . GLU D  1  334 ? 16.256  -20.026 17.301  1.00 60.04  ?  334  GLU D N   1 
ATOM   8582  C CA  . GLU D  1  334 ? 16.234  -20.761 16.038  1.00 61.39  ?  334  GLU D CA  1 
ATOM   8583  C C   . GLU D  1  334 ? 14.923  -20.575 15.288  1.00 61.87  ?  334  GLU D C   1 
ATOM   8584  O O   . GLU D  1  334 ? 14.918  -20.440 14.059  1.00 63.55  ?  334  GLU D O   1 
ATOM   8585  C CB  . GLU D  1  334 ? 16.474  -22.247 16.295  1.00 61.97  ?  334  GLU D CB  1 
ATOM   8586  C CG  . GLU D  1  334 ? 17.241  -22.552 17.571  1.00 63.36  ?  334  GLU D CG  1 
ATOM   8587  C CD  . GLU D  1  334 ? 17.659  -24.015 17.659  1.00 65.45  ?  334  GLU D CD  1 
ATOM   8588  O OE1 . GLU D  1  334 ? 16.807  -24.888 17.373  1.00 65.25  ?  334  GLU D OE1 1 
ATOM   8589  O OE2 . GLU D  1  334 ? 18.842  -24.289 17.982  1.00 67.42  -1 334  GLU D OE2 1 
ATOM   8590  N N   . SER D  1  335 ? 13.804  -20.563 16.005  1.00 55.30  ?  335  SER D N   1 
ATOM   8591  C CA  . SER D  1  335 ? 12.490  -20.539 15.376  1.00 55.72  ?  335  SER D CA  1 
ATOM   8592  C C   . SER D  1  335 ? 12.033  -19.140 14.983  1.00 55.72  ?  335  SER D C   1 
ATOM   8593  O O   . SER D  1  335 ? 10.933  -19.008 14.433  1.00 56.13  ?  335  SER D O   1 
ATOM   8594  C CB  . SER D  1  335 ? 11.448  -21.165 16.313  1.00 54.39  ?  335  SER D CB  1 
ATOM   8595  O OG  . SER D  1  335 ? 11.785  -22.495 16.668  1.00 54.52  ?  335  SER D OG  1 
ATOM   8596  N N   . MET D  1  336 ? 12.845  -18.109 15.230  1.00 54.77  ?  336  MET D N   1 
ATOM   8597  C CA  . MET D  1  336 ? 12.383  -16.732 15.099  1.00 54.31  ?  336  MET D CA  1 
ATOM   8598  C C   . MET D  1  336 ? 11.938  -16.433 13.674  1.00 55.95  ?  336  MET D C   1 
ATOM   8599  O O   . MET D  1  336 ? 12.668  -16.687 12.713  1.00 57.85  ?  336  MET D O   1 
ATOM   8600  C CB  . MET D  1  336 ? 13.489  -15.765 15.528  1.00 54.11  ?  336  MET D CB  1 
ATOM   8601  C CG  . MET D  1  336 ? 13.087  -14.293 15.494  1.00 53.62  ?  336  MET D CG  1 
ATOM   8602  S SD  . MET D  1  336 ? 11.518  -13.945 16.321  1.00 51.79  ?  336  MET D SD  1 
ATOM   8603  C CE  . MET D  1  336 ? 11.730  -14.751 17.920  1.00 50.77  ?  336  MET D CE  1 
ATOM   8604  N N   . ILE D  1  337 ? 10.729  -15.887 13.544  1.00 48.99  ?  337  ILE D N   1 
ATOM   8605  C CA  . ILE D  1  337 ? 10.115  -15.599 12.254  1.00 50.67  ?  337  ILE D CA  1 
ATOM   8606  C C   . ILE D  1  337 ? 9.779   -14.119 12.117  1.00 49.84  ?  337  ILE D C   1 
ATOM   8607  O O   . ILE D  1  337 ? 10.060  -13.495 11.087  1.00 51.40  ?  337  ILE D O   1 
ATOM   8608  C CB  . ILE D  1  337 ? 8.858   -16.468 12.026  1.00 51.20  ?  337  ILE D CB  1 
ATOM   8609  C CG1 . ILE D  1  337 ? 9.261   -17.862 11.557  1.00 53.13  ?  337  ILE D CG1 1 
ATOM   8610  C CG2 . ILE D  1  337 ? 7.930   -15.823 11.010  1.00 52.47  ?  337  ILE D CG2 1 
ATOM   8611  C CD1 . ILE D  1  337 ? 8.139   -18.865 11.619  1.00 53.43  ?  337  ILE D CD1 1 
ATOM   8612  N N   . ASP D  1  338 ? 9.161   -13.542 13.144  1.00 52.02  ?  338  ASP D N   1 
ATOM   8613  C CA  . ASP D  1  338 ? 8.798   -12.128 13.175  1.00 51.00  ?  338  ASP D CA  1 
ATOM   8614  C C   . ASP D  1  338 ? 9.493   -11.502 14.381  1.00 49.76  ?  338  ASP D C   1 
ATOM   8615  O O   . ASP D  1  338 ? 9.068   -11.706 15.524  1.00 48.43  ?  338  ASP D O   1 
ATOM   8616  C CB  . ASP D  1  338 ? 7.281   -11.957 13.244  1.00 49.86  ?  338  ASP D CB  1 
ATOM   8617  C CG  . ASP D  1  338 ? 6.860   -10.505 13.301  1.00 48.78  ?  338  ASP D CG  1 
ATOM   8618  O OD1 . ASP D  1  338 ? 7.651   -9.653  12.864  1.00 49.51  ?  338  ASP D OD1 1 
ATOM   8619  O OD2 . ASP D  1  338 ? 5.742   -10.212 13.776  1.00 47.35  -1 338  ASP D OD2 1 
ATOM   8620  N N   . LEU D  1  339 ? 10.557  -10.739 14.125  1.00 48.47  ?  339  LEU D N   1 
ATOM   8621  C CA  . LEU D  1  339 ? 11.347  -10.094 15.170  1.00 48.11  ?  339  LEU D CA  1 
ATOM   8622  C C   . LEU D  1  339 ? 11.171  -8.583  15.058  1.00 48.15  ?  339  LEU D C   1 
ATOM   8623  O O   . LEU D  1  339 ? 11.608  -7.974  14.076  1.00 49.27  ?  339  LEU D O   1 
ATOM   8624  C CB  . LEU D  1  339 ? 12.815  -10.486 15.045  1.00 49.38  ?  339  LEU D CB  1 
ATOM   8625  C CG  . LEU D  1  339 ? 13.783  -9.805  16.005  1.00 49.58  ?  339  LEU D CG  1 
ATOM   8626  C CD1 . LEU D  1  339 ? 13.338  -10.016 17.437  1.00 48.52  ?  339  LEU D CD1 1 
ATOM   8627  C CD2 . LEU D  1  339 ? 15.174  -10.343 15.792  1.00 50.74  ?  339  LEU D CD2 1 
ATOM   8628  N N   . GLU D  1  340 ? 10.529  -7.978  16.058  1.00 49.49  ?  340  GLU D N   1 
ATOM   8629  C CA  . GLU D  1  340 ? 10.221  -6.549  16.039  1.00 49.85  ?  340  GLU D CA  1 
ATOM   8630  C C   . GLU D  1  340 ? 10.649  -5.918  17.358  1.00 50.53  ?  340  GLU D C   1 
ATOM   8631  O O   . GLU D  1  340 ? 10.040  -6.178  18.402  1.00 49.89  ?  340  GLU D O   1 
ATOM   8632  C CB  . GLU D  1  340 ? 8.730   -6.310  15.789  1.00 48.68  ?  340  GLU D CB  1 
ATOM   8633  C CG  . GLU D  1  340 ? 8.085   -7.311  14.850  1.00 48.09  ?  340  GLU D CG  1 
ATOM   8634  C CD  . GLU D  1  340 ? 6.794   -6.801  14.240  1.00 47.41  ?  340  GLU D CD  1 
ATOM   8635  O OE1 . GLU D  1  340 ? 6.167   -5.893  14.820  1.00 46.89  ?  340  GLU D OE1 1 
ATOM   8636  O OE2 . GLU D  1  340 ? 6.405   -7.313  13.175  1.00 47.80  -1 340  GLU D OE2 1 
ATOM   8637  N N   . ILE D  1  341 ? 11.686  -5.085  17.314  1.00 46.08  ?  341  ILE D N   1 
ATOM   8638  C CA  . ILE D  1  341 ? 12.104  -4.320  18.486  1.00 47.42  ?  341  ILE D CA  1 
ATOM   8639  C C   . ILE D  1  341 ? 12.175  -2.833  18.149  1.00 49.18  ?  341  ILE D C   1 
ATOM   8640  O O   . ILE D  1  341 ? 12.965  -2.090  18.741  1.00 51.03  ?  341  ILE D O   1 
ATOM   8641  C CB  . ILE D  1  341 ? 13.435  -4.842  19.048  1.00 48.16  ?  341  ILE D CB  1 
ATOM   8642  C CG1 . ILE D  1  341 ? 14.410  -5.142  17.924  1.00 48.44  ?  341  ILE D CG1 1 
ATOM   8643  C CG2 . ILE D  1  341 ? 13.211  -6.103  19.844  1.00 47.72  ?  341  ILE D CG2 1 
ATOM   8644  C CD1 . ILE D  1  341 ? 15.829  -5.193  18.398  1.00 49.79  ?  341  ILE D CD1 1 
ATOM   8645  N N   . SER D  1  342 ? 11.349  -2.394  17.198  1.00 50.26  ?  342  SER D N   1 
ATOM   8646  C CA  . SER D  1  342 ? 11.352  -1.021  16.712  1.00 52.13  ?  342  SER D CA  1 
ATOM   8647  C C   . SER D  1  342 ? 10.963  -0.035  17.810  1.00 54.06  ?  342  SER D C   1 
ATOM   8648  O O   . SER D  1  342 ? 10.472  -0.402  18.875  1.00 53.66  ?  342  SER D O   1 
ATOM   8649  C CB  . SER D  1  342 ? 10.359  -0.856  15.566  1.00 51.04  ?  342  SER D CB  1 
ATOM   8650  O OG  . SER D  1  342 ? 10.555  -1.838  14.575  1.00 49.66  ?  342  SER D OG  1 
ATOM   8651  N N   . GLU D  1  343 ? 11.190  1.244   17.520  1.00 53.59  ?  343  GLU D N   1 
ATOM   8652  C CA  . GLU D  1  343 ? 10.695  2.357   18.330  1.00 56.19  ?  343  GLU D CA  1 
ATOM   8653  C C   . GLU D  1  343 ? 11.096  2.207   19.797  1.00 56.86  ?  343  GLU D C   1 
ATOM   8654  O O   . GLU D  1  343 ? 10.266  2.095   20.702  1.00 56.88  ?  343  GLU D O   1 
ATOM   8655  C CB  . GLU D  1  343 ? 9.182   2.506   18.166  1.00 55.64  ?  343  GLU D CB  1 
ATOM   8656  C CG  . GLU D  1  343 ? 8.807   3.007   16.784  1.00 55.25  ?  343  GLU D CG  1 
ATOM   8657  C CD  . GLU D  1  343 ? 7.374   2.713   16.406  1.00 52.65  ?  343  GLU D CD  1 
ATOM   8658  O OE1 . GLU D  1  343 ? 6.500   3.550   16.712  1.00 53.80  ?  343  GLU D OE1 1 
ATOM   8659  O OE2 . GLU D  1  343 ? 7.125   1.653   15.789  1.00 49.60  -1 343  GLU D OE2 1 
ATOM   8660  N N   . ASN D  1  344 ? 12.408  2.202   20.008  1.00 57.60  ?  344  ASN D N   1 
ATOM   8661  C CA  . ASN D  1  344 ? 13.015  2.032   21.321  1.00 58.01  ?  344  ASN D CA  1 
ATOM   8662  C C   . ASN D  1  344 ? 14.203  2.981   21.398  1.00 59.99  ?  344  ASN D C   1 
ATOM   8663  O O   . ASN D  1  344 ? 14.361  3.874   20.560  1.00 61.26  ?  344  ASN D O   1 
ATOM   8664  C CB  . ASN D  1  344 ? 13.421  0.570   21.552  1.00 55.68  ?  344  ASN D CB  1 
ATOM   8665  C CG  . ASN D  1  344 ? 12.353  -0.229  22.270  1.00 54.24  ?  344  ASN D CG  1 
ATOM   8666  O OD1 . ASN D  1  344 ? 12.163  -0.087  23.476  1.00 55.12  ?  344  ASN D OD1 1 
ATOM   8667  N ND2 . ASN D  1  344 ? 11.654  -1.084  21.531  1.00 52.00  ?  344  ASN D ND2 1 
ATOM   8668  N N   . LYS D  1  345 ? 15.041  2.799   22.411  1.00 61.40  ?  345  LYS D N   1 
ATOM   8669  C CA  . LYS D  1  345 ? 16.239  3.610   22.589  1.00 62.99  ?  345  LYS D CA  1 
ATOM   8670  C C   . LYS D  1  345 ? 17.492  2.738   22.619  1.00 62.05  ?  345  LYS D C   1 
ATOM   8671  O O   . LYS D  1  345 ? 18.413  2.961   23.409  1.00 62.86  ?  345  LYS D O   1 
ATOM   8672  C CB  . LYS D  1  345 ? 16.127  4.460   23.851  1.00 64.60  ?  345  LYS D CB  1 
ATOM   8673  C CG  . LYS D  1  345 ? 15.010  5.483   23.779  1.00 65.80  ?  345  LYS D CG  1 
ATOM   8674  C CD  . LYS D  1  345 ? 14.824  6.199   25.102  1.00 67.19  ?  345  LYS D CD  1 
ATOM   8675  C CE  . LYS D  1  345 ? 13.578  7.071   25.085  1.00 68.10  ?  345  LYS D CE  1 
ATOM   8676  N NZ  . LYS D  1  345 ? 13.239  7.549   26.456  1.00 69.20  ?  345  LYS D NZ  1 
ATOM   8677  N N   . LEU D  1  346 ? 17.540  1.740   21.738  1.00 62.21  ?  346  LEU D N   1 
ATOM   8678  C CA  . LEU D  1  346 ? 18.679  0.837   21.657  1.00 61.32  ?  346  LEU D CA  1 
ATOM   8679  C C   . LEU D  1  346 ? 19.873  1.520   20.990  1.00 62.65  ?  346  LEU D C   1 
ATOM   8680  O O   . LEU D  1  346 ? 19.732  2.471   20.217  1.00 63.81  ?  346  LEU D O   1 
ATOM   8681  C CB  . LEU D  1  346 ? 18.307  -0.430  20.884  1.00 59.17  ?  346  LEU D CB  1 
ATOM   8682  C CG  . LEU D  1  346 ? 17.155  -1.261  21.450  1.00 57.56  ?  346  LEU D CG  1 
ATOM   8683  C CD1 . LEU D  1  346 ? 16.880  -2.472  20.573  1.00 55.50  ?  346  LEU D CD1 1 
ATOM   8684  C CD2 . LEU D  1  346 ? 17.443  -1.683  22.887  1.00 57.56  ?  346  LEU D CD2 1 
ATOM   8685  N N   . THR D  1  347 ? 21.066  1.020   21.309  1.00 63.74  ?  347  THR D N   1 
ATOM   8686  C CA  . THR D  1  347 ? 22.318  1.569   20.808  1.00 64.95  ?  347  THR D CA  1 
ATOM   8687  C C   . THR D  1  347 ? 23.252  0.421   20.443  1.00 63.89  ?  347  THR D C   1 
ATOM   8688  O O   . THR D  1  347 ? 23.061  -0.721  20.870  1.00 62.41  ?  347  THR D O   1 
ATOM   8689  C CB  . THR D  1  347 ? 22.999  2.487   21.839  1.00 66.49  ?  347  THR D CB  1 
ATOM   8690  O OG1 . THR D  1  347 ? 23.302  1.738   23.022  1.00 65.76  ?  347  THR D OG1 1 
ATOM   8691  C CG2 . THR D  1  347 ? 22.103  3.663   22.205  1.00 67.76  ?  347  THR D CG2 1 
ATOM   8692  N N   . GLY D  1  348 ? 24.262  0.733   19.630  1.00 66.23  ?  348  GLY D N   1 
ATOM   8693  C CA  . GLY D  1  348 ? 25.272  -0.236  19.270  1.00 65.63  ?  348  GLY D CA  1 
ATOM   8694  C C   . GLY D  1  348 ? 24.949  -1.013  18.008  1.00 64.77  ?  348  GLY D C   1 
ATOM   8695  O O   . GLY D  1  348 ? 23.899  -0.830  17.386  1.00 64.47  ?  348  GLY D O   1 
ATOM   8696  N N   . PRO D  1  349 ? 25.849  -1.908  17.616  1.00 62.05  ?  349  PRO D N   1 
ATOM   8697  C CA  . PRO D  1  349 ? 25.706  -2.600  16.332  1.00 61.44  ?  349  PRO D CA  1 
ATOM   8698  C C   . PRO D  1  349 ? 24.805  -3.823  16.423  1.00 59.90  ?  349  PRO D C   1 
ATOM   8699  O O   . PRO D  1  349 ? 24.522  -4.354  17.499  1.00 59.31  ?  349  PRO D O   1 
ATOM   8700  C CB  . PRO D  1  349 ? 27.141  -3.016  16.011  1.00 62.43  ?  349  PRO D CB  1 
ATOM   8701  C CG  . PRO D  1  349 ? 27.722  -3.286  17.359  1.00 62.70  ?  349  PRO D CG  1 
ATOM   8702  C CD  . PRO D  1  349 ? 27.091  -2.291  18.307  1.00 62.85  ?  349  PRO D CD  1 
ATOM   8703  N N   . VAL D  1  350 ? 24.366  -4.272  15.255  1.00 60.98  ?  350  VAL D N   1 
ATOM   8704  C CA  . VAL D  1  350 ? 23.569  -5.497  15.164  1.00 59.53  ?  350  VAL D CA  1 
ATOM   8705  C C   . VAL D  1  350 ? 24.512  -6.697  15.209  1.00 59.44  ?  350  VAL D C   1 
ATOM   8706  O O   . VAL D  1  350 ? 25.522  -6.704  14.490  1.00 60.64  ?  350  VAL D O   1 
ATOM   8707  C CB  . VAL D  1  350 ? 22.739  -5.498  13.886  1.00 59.58  ?  350  VAL D CB  1 
ATOM   8708  C CG1 . VAL D  1  350 ? 22.055  -6.834  13.701  1.00 58.41  ?  350  VAL D CG1 1 
ATOM   8709  C CG2 . VAL D  1  350 ? 21.713  -4.375  13.923  1.00 59.45  ?  350  VAL D CG2 1 
ATOM   8710  N N   . PRO D  1  351 ? 24.231  -7.711  16.023  1.00 63.59  ?  351  PRO D N   1 
ATOM   8711  C CA  . PRO D  1  351 ? 25.158  -8.845  16.131  1.00 63.52  ?  351  PRO D CA  1 
ATOM   8712  C C   . PRO D  1  351 ? 25.245  -9.656  14.846  1.00 64.11  ?  351  PRO D C   1 
ATOM   8713  O O   . PRO D  1  351 ? 24.275  -9.787  14.097  1.00 64.02  ?  351  PRO D O   1 
ATOM   8714  C CB  . PRO D  1  351 ? 24.557  -9.686  17.266  1.00 61.96  ?  351  PRO D CB  1 
ATOM   8715  C CG  . PRO D  1  351 ? 23.676  -8.738  18.021  1.00 61.54  ?  351  PRO D CG  1 
ATOM   8716  C CD  . PRO D  1  351 ? 23.127  -7.807  16.989  1.00 62.22  ?  351  PRO D CD  1 
ATOM   8717  N N   . ASP D  1  352 ? 26.431  -10.232 14.616  1.00 71.03  ?  352  ASP D N   1 
ATOM   8718  C CA  . ASP D  1  352 ? 26.611  -11.196 13.534  1.00 71.79  ?  352  ASP D CA  1 
ATOM   8719  C C   . ASP D  1  352 ? 25.693  -12.398 13.688  1.00 70.68  ?  352  ASP D C   1 
ATOM   8720  O O   . ASP D  1  352 ? 25.446  -13.104 12.704  1.00 71.45  ?  352  ASP D O   1 
ATOM   8721  C CB  . ASP D  1  352 ? 28.060  -11.696 13.479  1.00 72.55  ?  352  ASP D CB  1 
ATOM   8722  C CG  . ASP D  1  352 ? 29.075  -10.569 13.497  1.00 73.58  ?  352  ASP D CG  1 
ATOM   8723  O OD1 . ASP D  1  352 ? 29.029  -9.745  14.437  1.00 72.99  -1 352  ASP D OD1 1 
ATOM   8724  O OD2 . ASP D  1  352 ? 29.920  -10.509 12.576  1.00 75.13  ?  352  ASP D OD2 1 
ATOM   8725  N N   . SER D  1  353 ? 25.201  -12.654 14.905  1.00 67.07  ?  353  SER D N   1 
ATOM   8726  C CA  . SER D  1  353 ? 24.370  -13.823 15.161  1.00 65.98  ?  353  SER D CA  1 
ATOM   8727  C C   . SER D  1  353 ? 23.091  -13.814 14.341  1.00 66.05  ?  353  SER D C   1 
ATOM   8728  O O   . SER D  1  353 ? 22.491  -14.876 14.143  1.00 65.74  ?  353  SER D O   1 
ATOM   8729  C CB  . SER D  1  353 ? 24.016  -13.911 16.645  1.00 64.57  ?  353  SER D CB  1 
ATOM   8730  O OG  . SER D  1  353 ? 25.040  -13.378 17.464  1.00 65.65  ?  353  SER D OG  1 
ATOM   8731  N N   . PHE D  1  354 ? 22.663  -12.648 13.854  1.00 59.94  ?  354  PHE D N   1 
ATOM   8732  C CA  . PHE D  1  354 ? 21.433  -12.586 13.076  1.00 60.02  ?  354  PHE D CA  1 
ATOM   8733  C C   . PHE D  1  354 ? 21.512  -13.443 11.818  1.00 61.61  ?  354  PHE D C   1 
ATOM   8734  O O   . PHE D  1  354 ? 20.471  -13.841 11.283  1.00 61.76  ?  354  PHE D O   1 
ATOM   8735  C CB  . PHE D  1  354 ? 21.112  -11.129 12.721  1.00 60.40  ?  354  PHE D CB  1 
ATOM   8736  C CG  . PHE D  1  354 ? 20.385  -10.385 13.811  1.00 58.87  ?  354  PHE D CG  1 
ATOM   8737  C CD1 . PHE D  1  354 ? 20.702  -10.593 15.146  1.00 57.87  ?  354  PHE D CD1 1 
ATOM   8738  C CD2 . PHE D  1  354 ? 19.377  -9.482  13.500  1.00 58.58  ?  354  PHE D CD2 1 
ATOM   8739  C CE1 . PHE D  1  354 ? 20.033  -9.915  16.149  1.00 56.89  ?  354  PHE D CE1 1 
ATOM   8740  C CE2 . PHE D  1  354 ? 18.703  -8.798  14.502  1.00 57.38  ?  354  PHE D CE2 1 
ATOM   8741  C CZ  . PHE D  1  354 ? 19.033  -9.016  15.826  1.00 56.68  ?  354  PHE D CZ  1 
ATOM   8742  N N   . GLY D  1  355 ? 22.722  -13.761 11.352  1.00 60.83  ?  355  GLY D N   1 
ATOM   8743  C CA  . GLY D  1  355 ? 22.872  -14.691 10.250  1.00 62.20  ?  355  GLY D CA  1 
ATOM   8744  C C   . GLY D  1  355 ? 22.415  -16.098 10.573  1.00 61.85  ?  355  GLY D C   1 
ATOM   8745  O O   . GLY D  1  355 ? 22.167  -16.884 9.653   1.00 62.91  ?  355  GLY D O   1 
ATOM   8746  N N   . LYS D  1  356 ? 22.304  -16.432 11.860  1.00 59.89  ?  356  LYS D N   1 
ATOM   8747  C CA  . LYS D  1  356 ? 21.817  -17.742 12.268  1.00 59.06  ?  356  LYS D CA  1 
ATOM   8748  C C   . LYS D  1  356 ? 20.301  -17.857 12.186  1.00 58.50  ?  356  LYS D C   1 
ATOM   8749  O O   . LYS D  1  356 ? 19.777  -18.975 12.231  1.00 58.26  ?  356  LYS D O   1 
ATOM   8750  C CB  . LYS D  1  356 ? 22.265  -18.046 13.695  1.00 57.59  ?  356  LYS D CB  1 
ATOM   8751  C CG  . LYS D  1  356 ? 23.760  -18.173 13.888  1.00 59.79  ?  356  LYS D CG  1 
ATOM   8752  C CD  . LYS D  1  356 ? 24.048  -18.508 15.339  1.00 60.92  ?  356  LYS D CD  1 
ATOM   8753  C CE  . LYS D  1  356 ? 25.426  -19.105 15.534  1.00 63.57  ?  356  LYS D CE  1 
ATOM   8754  N NZ  . LYS D  1  356 ? 25.582  -19.649 16.916  1.00 64.88  ?  356  LYS D NZ  1 
ATOM   8755  N N   . LEU D  1  357 ? 19.586  -16.739 12.067  1.00 55.58  ?  357  LEU D N   1 
ATOM   8756  C CA  . LEU D  1  357 ? 18.126  -16.763 11.988  1.00 55.05  ?  357  LEU D CA  1 
ATOM   8757  C C   . LEU D  1  357 ? 17.733  -17.200 10.580  1.00 57.31  ?  357  LEU D C   1 
ATOM   8758  O O   . LEU D  1  357 ? 17.444  -16.392 9.693   1.00 58.65  ?  357  LEU D O   1 
ATOM   8759  C CB  . LEU D  1  357 ? 17.541  -15.401 12.348  1.00 54.02  ?  357  LEU D CB  1 
ATOM   8760  C CG  . LEU D  1  357 ? 18.041  -14.761 13.648  1.00 52.45  ?  357  LEU D CG  1 
ATOM   8761  C CD1 . LEU D  1  357 ? 17.521  -13.336 13.780  1.00 51.90  ?  357  LEU D CD1 1 
ATOM   8762  C CD2 . LEU D  1  357 ? 17.664  -15.597 14.869  1.00 50.87  ?  357  LEU D CD2 1 
ATOM   8763  N N   . THR D  1  358 ? 17.721  -18.520 10.379  1.00 52.80  ?  358  THR D N   1 
ATOM   8764  C CA  . THR D  1  358 ? 17.476  -19.094 9.061   1.00 53.30  ?  358  THR D CA  1 
ATOM   8765  C C   . THR D  1  358 ? 16.015  -19.019 8.635   1.00 53.00  ?  358  THR D C   1 
ATOM   8766  O O   . THR D  1  358 ? 15.724  -19.245 7.455   1.00 55.59  ?  358  THR D O   1 
ATOM   8767  C CB  . THR D  1  358 ? 17.947  -20.553 9.025   1.00 55.10  ?  358  THR D CB  1 
ATOM   8768  O OG1 . THR D  1  358 ? 17.433  -21.262 10.159  1.00 55.10  ?  358  THR D OG1 1 
ATOM   8769  C CG2 . THR D  1  358 ? 19.453  -20.615 9.062   1.00 56.86  ?  358  THR D CG2 1 
ATOM   8770  N N   . ALA D  1  359 ? 15.095  -18.710 9.546   1.00 53.99  ?  359  ALA D N   1 
ATOM   8771  C CA  . ALA D  1  359 ? 13.681  -18.637 9.207   1.00 52.66  ?  359  ALA D CA  1 
ATOM   8772  C C   . ALA D  1  359 ? 13.123  -17.225 9.304   1.00 51.04  ?  359  ALA D C   1 
ATOM   8773  O O   . ALA D  1  359 ? 11.899  -17.057 9.267   1.00 49.89  ?  359  ALA D O   1 
ATOM   8774  C CB  . ALA D  1  359 ? 12.875  -19.580 10.099  1.00 52.56  ?  359  ALA D CB  1 
ATOM   8775  N N   . LEU D  1  360 ? 13.985  -16.211 9.411   1.00 49.94  ?  360  LEU D N   1 
ATOM   8776  C CA  . LEU D  1  360 ? 13.532  -14.841 9.626   1.00 48.61  ?  360  LEU D CA  1 
ATOM   8777  C C   . LEU D  1  360 ? 12.774  -14.327 8.407   1.00 47.90  ?  360  LEU D C   1 
ATOM   8778  O O   . LEU D  1  360 ? 13.218  -14.499 7.269   1.00 48.64  ?  360  LEU D O   1 
ATOM   8779  C CB  . LEU D  1  360 ? 14.727  -13.934 9.929   1.00 49.09  ?  360  LEU D CB  1 
ATOM   8780  C CG  . LEU D  1  360 ? 14.442  -12.534 10.479  1.00 48.06  ?  360  LEU D CG  1 
ATOM   8781  C CD1 . LEU D  1  360 ? 13.750  -12.639 11.807  1.00 47.47  ?  360  LEU D CD1 1 
ATOM   8782  C CD2 . LEU D  1  360 ? 15.707  -11.723 10.634  1.00 48.82  ?  360  LEU D CD2 1 
ATOM   8783  N N   . GLU D  1  361 ? 11.610  -13.723 8.646   1.00 48.93  ?  361  GLU D N   1 
ATOM   8784  C CA  . GLU D  1  361 ? 10.817  -13.105 7.589   1.00 50.67  ?  361  GLU D CA  1 
ATOM   8785  C C   . GLU D  1  361 ? 10.624  -11.609 7.795   1.00 48.82  ?  361  GLU D C   1 
ATOM   8786  O O   . GLU D  1  361 ? 10.819  -10.826 6.856   1.00 50.51  ?  361  GLU D O   1 
ATOM   8787  C CB  . GLU D  1  361 ? 9.457   -13.816 7.477   1.00 51.16  ?  361  GLU D CB  1 
ATOM   8788  C CG  . GLU D  1  361 ? 9.563   -15.274 7.037   1.00 53.66  ?  361  GLU D CG  1 
ATOM   8789  C CD  . GLU D  1  361 ? 8.211   -15.896 6.716   1.00 55.01  ?  361  GLU D CD  1 
ATOM   8790  O OE1 . GLU D  1  361 ? 7.259   -15.140 6.425   1.00 55.16  ?  361  GLU D OE1 1 
ATOM   8791  O OE2 . GLU D  1  361 ? 8.100   -17.144 6.761   1.00 55.88  -1 361  GLU D OE2 1 
ATOM   8792  N N   . TRP D  1  362 ? 10.246  -11.184 8.998   1.00 53.31  ?  362  TRP D N   1 
ATOM   8793  C CA  . TRP D  1  362 ? 10.128  -9.774  9.344   1.00 51.55  ?  362  TRP D CA  1 
ATOM   8794  C C   . TRP D  1  362 ? 11.216  -9.416  10.346  1.00 50.41  ?  362  TRP D C   1 
ATOM   8795  O O   . TRP D  1  362 ? 11.323  -10.051 11.400  1.00 49.16  ?  362  TRP D O   1 
ATOM   8796  C CB  . TRP D  1  362 ? 8.757   -9.462  9.947   1.00 49.33  ?  362  TRP D CB  1 
ATOM   8797  C CG  . TRP D  1  362 ? 7.592   -9.589  9.016   1.00 50.41  ?  362  TRP D CG  1 
ATOM   8798  C CD1 . TRP D  1  362 ? 7.065   -8.609  8.233   1.00 50.84  ?  362  TRP D CD1 1 
ATOM   8799  C CD2 . TRP D  1  362 ? 6.782   -10.754 8.800   1.00 51.50  ?  362  TRP D CD2 1 
ATOM   8800  N NE1 . TRP D  1  362 ? 5.988   -9.091  7.528   1.00 52.23  ?  362  TRP D NE1 1 
ATOM   8801  C CE2 . TRP D  1  362 ? 5.793   -10.405 7.858   1.00 52.85  ?  362  TRP D CE2 1 
ATOM   8802  C CE3 . TRP D  1  362 ? 6.801   -12.060 9.306   1.00 51.69  ?  362  TRP D CE3 1 
ATOM   8803  C CZ2 . TRP D  1  362 ? 4.835   -11.309 7.410   1.00 54.77  ?  362  TRP D CZ2 1 
ATOM   8804  C CZ3 . TRP D  1  362 ? 5.847   -12.959 8.857   1.00 53.38  ?  362  TRP D CZ3 1 
ATOM   8805  C CH2 . TRP D  1  362 ? 4.878   -12.578 7.919   1.00 55.09  ?  362  TRP D CH2 1 
ATOM   8806  N N   . LEU D  1  363 ? 12.015  -8.403  10.025  1.00 49.43  ?  363  LEU D N   1 
ATOM   8807  C CA  . LEU D  1  363 ? 12.983  -7.847  10.966  1.00 48.82  ?  363  LEU D CA  1 
ATOM   8808  C C   . LEU D  1  363 ? 12.725  -6.352  11.079  1.00 48.41  ?  363  LEU D C   1 
ATOM   8809  O O   . LEU D  1  363 ? 13.012  -5.600  10.141  1.00 49.76  ?  363  LEU D O   1 
ATOM   8810  C CB  . LEU D  1  363 ? 14.421  -8.121  10.529  1.00 50.67  ?  363  LEU D CB  1 
ATOM   8811  C CG  . LEU D  1  363 ? 15.487  -7.493  11.430  1.00 50.50  ?  363  LEU D CG  1 
ATOM   8812  C CD1 . LEU D  1  363 ? 15.382  -8.017  12.846  1.00 48.93  ?  363  LEU D CD1 1 
ATOM   8813  C CD2 . LEU D  1  363 ? 16.872  -7.739  10.875  1.00 52.34  ?  363  LEU D CD2 1 
ATOM   8814  N N   . PHE D  1  364 ? 12.171  -5.928  12.216  1.00 49.61  ?  364  PHE D N   1 
ATOM   8815  C CA  . PHE D  1  364 ? 11.802  -4.535  12.470  1.00 49.57  ?  364  PHE D CA  1 
ATOM   8816  C C   . PHE D  1  364 ? 12.798  -3.939  13.462  1.00 50.45  ?  364  PHE D C   1 
ATOM   8817  O O   . PHE D  1  364 ? 12.747  -4.243  14.659  1.00 49.82  ?  364  PHE D O   1 
ATOM   8818  C CB  . PHE D  1  364 ? 10.383  -4.453  13.014  1.00 47.92  ?  364  PHE D CB  1 
ATOM   8819  C CG  . PHE D  1  364 ? 9.339   -4.198  11.974  1.00 47.58  ?  364  PHE D CG  1 
ATOM   8820  C CD1 . PHE D  1  364 ? 8.919   -5.214  11.132  1.00 47.58  ?  364  PHE D CD1 1 
ATOM   8821  C CD2 . PHE D  1  364 ? 8.745   -2.950  11.865  1.00 47.66  ?  364  PHE D CD2 1 
ATOM   8822  C CE1 . PHE D  1  364 ? 7.942   -4.983  10.181  1.00 47.67  ?  364  PHE D CE1 1 
ATOM   8823  C CE2 . PHE D  1  364 ? 7.764   -2.712  10.918  1.00 47.30  ?  364  PHE D CE2 1 
ATOM   8824  C CZ  . PHE D  1  364 ? 7.363   -3.729  10.076  1.00 47.29  ?  364  PHE D CZ  1 
ATOM   8825  N N   . LEU D  1  365 ? 13.705  -3.095  12.958  1.00 48.99  ?  365  LEU D N   1 
ATOM   8826  C CA  . LEU D  1  365 ? 14.702  -2.414  13.776  1.00 50.37  ?  365  LEU D CA  1 
ATOM   8827  C C   . LEU D  1  365 ? 14.591  -0.896  13.721  1.00 52.00  ?  365  LEU D C   1 
ATOM   8828  O O   . LEU D  1  365 ? 15.381  -0.208  14.379  1.00 53.63  ?  365  LEU D O   1 
ATOM   8829  C CB  . LEU D  1  365 ? 16.118  -2.821  13.342  1.00 51.47  ?  365  LEU D CB  1 
ATOM   8830  C CG  . LEU D  1  365 ? 16.553  -4.275  13.504  1.00 50.64  ?  365  LEU D CG  1 
ATOM   8831  C CD1 . LEU D  1  365 ? 17.998  -4.450  13.061  1.00 52.13  ?  365  LEU D CD1 1 
ATOM   8832  C CD2 . LEU D  1  365 ? 16.388  -4.696  14.936  1.00 49.62  ?  365  LEU D CD2 1 
ATOM   8833  N N   . ARG D  1  366 ? 13.629  -0.359  12.975  1.00 52.86  ?  366  ARG D N   1 
ATOM   8834  C CA  . ARG D  1  366 ? 13.544  1.070   12.715  1.00 54.81  ?  366  ARG D CA  1 
ATOM   8835  C C   . ARG D  1  366 ? 13.377  1.862   14.009  1.00 56.23  ?  366  ARG D C   1 
ATOM   8836  O O   . ARG D  1  366 ? 13.054  1.319   15.068  1.00 55.27  ?  366  ARG D O   1 
ATOM   8837  C CB  . ARG D  1  366 ? 12.378  1.362   11.771  1.00 53.92  ?  366  ARG D CB  1 
ATOM   8838  C CG  . ARG D  1  366 ? 11.063  0.709   12.186  1.00 51.54  ?  366  ARG D CG  1 
ATOM   8839  C CD  . ARG D  1  366 ? 9.884   1.227   11.373  1.00 50.77  ?  366  ARG D CD  1 
ATOM   8840  N NE  . ARG D  1  366 ? 10.032  2.633   11.022  1.00 52.84  ?  366  ARG D NE  1 
ATOM   8841  C CZ  . ARG D  1  366 ? 9.789   3.641   11.850  1.00 54.50  ?  366  ARG D CZ  1 
ATOM   8842  N NH1 . ARG D  1  366 ? 9.374   3.434   13.090  1.00 54.45  ?  366  ARG D NH1 1 
ATOM   8843  N NH2 . ARG D  1  366 ? 9.972   4.888   11.425  1.00 56.67  ?  366  ARG D NH2 1 
ATOM   8844  N N   . ASP D  1  367 ? 13.628  3.169   13.910  1.00 54.77  ?  367  ASP D N   1 
ATOM   8845  C CA  . ASP D  1  367 ? 13.414  4.123   15.000  1.00 57.00  ?  367  ASP D CA  1 
ATOM   8846  C C   . ASP D  1  367 ? 14.165  3.712   16.268  1.00 56.84  ?  367  ASP D C   1 
ATOM   8847  O O   . ASP D  1  367 ? 13.580  3.432   17.315  1.00 56.30  ?  367  ASP D O   1 
ATOM   8848  C CB  . ASP D  1  367 ? 11.922  4.311   15.282  1.00 56.66  ?  367  ASP D CB  1 
ATOM   8849  C CG  . ASP D  1  367 ? 11.622  5.654   15.916  1.00 60.02  ?  367  ASP D CG  1 
ATOM   8850  O OD1 . ASP D  1  367 ? 12.540  6.239   16.531  1.00 61.33  ?  367  ASP D OD1 1 
ATOM   8851  O OD2 . ASP D  1  367 ? 10.474  6.129   15.797  1.00 60.76  -1 367  ASP D OD2 1 
ATOM   8852  N N   . ASN D  1  368 ? 15.485  3.669   16.150  1.00 60.82  ?  368  ASN D N   1 
ATOM   8853  C CA  . ASN D  1  368 ? 16.354  3.386   17.282  1.00 60.81  ?  368  ASN D CA  1 
ATOM   8854  C C   . ASN D  1  368 ? 17.601  4.251   17.143  1.00 62.67  ?  368  ASN D C   1 
ATOM   8855  O O   . ASN D  1  368 ? 17.652  5.180   16.330  1.00 64.13  ?  368  ASN D O   1 
ATOM   8856  C CB  . ASN D  1  368 ? 16.685  1.888   17.359  1.00 58.49  ?  368  ASN D CB  1 
ATOM   8857  C CG  . ASN D  1  368 ? 15.747  1.125   18.276  1.00 56.91  ?  368  ASN D CG  1 
ATOM   8858  O OD1 . ASN D  1  368 ? 15.851  1.204   19.498  1.00 57.39  ?  368  ASN D OD1 1 
ATOM   8859  N ND2 . ASN D  1  368 ? 14.830  0.374   17.685  1.00 54.98  ?  368  ASN D ND2 1 
ATOM   8860  N N   . GLN D  1  369 ? 18.614  3.951   17.948  1.00 66.53  ?  369  GLN D N   1 
ATOM   8861  C CA  . GLN D  1  369 ? 19.887  4.655   17.894  1.00 68.00  ?  369  GLN D CA  1 
ATOM   8862  C C   . GLN D  1  369 ? 21.032  3.685   17.626  1.00 67.12  ?  369  GLN D C   1 
ATOM   8863  O O   . GLN D  1  369 ? 22.150  3.882   18.106  1.00 67.82  ?  369  GLN D O   1 
ATOM   8864  C CB  . GLN D  1  369 ? 20.125  5.435   19.187  1.00 69.16  ?  369  GLN D CB  1 
ATOM   8865  C CG  . GLN D  1  369 ? 19.233  6.660   19.350  1.00 70.48  ?  369  GLN D CG  1 
ATOM   8866  C CD  . GLN D  1  369 ? 19.388  7.329   20.710  1.00 71.50  ?  369  GLN D CD  1 
ATOM   8867  O OE1 . GLN D  1  369 ? 20.118  6.846   21.580  1.00 71.23  ?  369  GLN D OE1 1 
ATOM   8868  N NE2 . GLN D  1  369 ? 18.707  8.455   20.892  1.00 72.69  ?  369  GLN D NE2 1 
ATOM   8869  N N   . LEU D  1  370 ? 20.759  2.633   16.857  1.00 63.98  ?  370  LEU D N   1 
ATOM   8870  C CA  . LEU D  1  370 ? 21.777  1.661   16.491  1.00 63.26  ?  370  LEU D CA  1 
ATOM   8871  C C   . LEU D  1  370 ? 22.794  2.289   15.538  1.00 64.78  ?  370  LEU D C   1 
ATOM   8872  O O   . LEU D  1  370 ? 22.524  3.294   14.874  1.00 66.03  ?  370  LEU D O   1 
ATOM   8873  C CB  . LEU D  1  370 ? 21.128  0.434   15.854  1.00 61.40  ?  370  LEU D CB  1 
ATOM   8874  C CG  . LEU D  1  370 ? 20.049  -0.237  16.708  1.00 59.74  ?  370  LEU D CG  1 
ATOM   8875  C CD1 . LEU D  1  370 ? 19.171  -1.145  15.858  1.00 58.07  ?  370  LEU D CD1 1 
ATOM   8876  C CD2 . LEU D  1  370 ? 20.681  -1.012  17.854  1.00 59.11  ?  370  LEU D CD2 1 
ATOM   8877  N N   . SER D  1  371 ? 23.978  1.681   15.471  1.00 62.62  ?  371  SER D N   1 
ATOM   8878  C CA  . SER D  1  371 ? 25.110  2.301   14.796  1.00 64.14  ?  371  SER D CA  1 
ATOM   8879  C C   . SER D  1  371 ? 26.015  1.236   14.190  1.00 63.72  ?  371  SER D C   1 
ATOM   8880  O O   . SER D  1  371 ? 25.824  0.032   14.387  1.00 62.29  ?  371  SER D O   1 
ATOM   8881  C CB  . SER D  1  371 ? 25.904  3.184   15.761  1.00 65.27  ?  371  SER D CB  1 
ATOM   8882  O OG  . SER D  1  371 ? 26.430  2.413   16.827  1.00 64.42  ?  371  SER D OG  1 
ATOM   8883  N N   . GLY D  1  372 ? 27.006  1.702   13.430  1.00 64.16  ?  372  GLY D N   1 
ATOM   8884  C CA  . GLY D  1  372 ? 28.004  0.838   12.846  1.00 64.21  ?  372  GLY D CA  1 
ATOM   8885  C C   . GLY D  1  372 ? 27.602  0.312   11.484  1.00 64.32  ?  372  GLY D C   1 
ATOM   8886  O O   . GLY D  1  372 ? 26.593  0.726   10.906  1.00 64.43  ?  372  GLY D O   1 
ATOM   8887  N N   . PRO D  1  373 ? 28.399  -0.604  10.939  1.00 61.11  ?  373  PRO D N   1 
ATOM   8888  C CA  . PRO D  1  373 ? 28.041  -1.245  9.670   1.00 61.48  ?  373  PRO D CA  1 
ATOM   8889  C C   . PRO D  1  373 ? 27.003  -2.345  9.852   1.00 59.89  ?  373  PRO D C   1 
ATOM   8890  O O   . PRO D  1  373 ? 26.891  -2.966  10.912  1.00 58.44  ?  373  PRO D O   1 
ATOM   8891  C CB  . PRO D  1  373 ? 29.375  -1.827  9.190   1.00 62.43  ?  373  PRO D CB  1 
ATOM   8892  C CG  . PRO D  1  373 ? 30.102  -2.141  10.461  1.00 61.49  ?  373  PRO D CG  1 
ATOM   8893  C CD  . PRO D  1  373 ? 29.703  -1.070  11.447  1.00 61.18  ?  373  PRO D CD  1 
ATOM   8894  N N   . ILE D  1  374 ? 26.238  -2.582  8.792   1.00 58.93  ?  374  ILE D N   1 
ATOM   8895  C CA  . ILE D  1  374 ? 25.233  -3.642  8.796   1.00 57.86  ?  374  ILE D CA  1 
ATOM   8896  C C   . ILE D  1  374 ? 25.941  -4.951  8.469   1.00 58.88  ?  374  ILE D C   1 
ATOM   8897  O O   . ILE D  1  374 ? 26.529  -5.078  7.386   1.00 59.51  ?  374  ILE D O   1 
ATOM   8898  C CB  . ILE D  1  374 ? 24.100  -3.347  7.797   1.00 56.44  ?  374  ILE D CB  1 
ATOM   8899  C CG1 . ILE D  1  374 ? 23.144  -2.311  8.373   1.00 55.39  ?  374  ILE D CG1 1 
ATOM   8900  C CG2 . ILE D  1  374 ? 23.328  -4.609  7.456   1.00 55.76  ?  374  ILE D CG2 1 
ATOM   8901  C CD1 . ILE D  1  374 ? 22.556  -2.734  9.669   1.00 54.95  ?  374  ILE D CD1 1 
ATOM   8902  N N   . PRO D  1  375 ? 25.918  -5.942  9.362   1.00 59.43  ?  375  PRO D N   1 
ATOM   8903  C CA  . PRO D  1  375 ? 26.605  -7.198  9.069   1.00 59.88  ?  375  PRO D CA  1 
ATOM   8904  C C   . PRO D  1  375 ? 25.907  -7.943  7.948   1.00 60.83  ?  375  PRO D C   1 
ATOM   8905  O O   . PRO D  1  375 ? 24.670  -7.906  7.838   1.00 60.17  ?  375  PRO D O   1 
ATOM   8906  C CB  . PRO D  1  375 ? 26.514  -7.973  10.397  1.00 57.97  ?  375  PRO D CB  1 
ATOM   8907  C CG  . PRO D  1  375 ? 26.030  -6.991  11.417  1.00 56.90  ?  375  PRO D CG  1 
ATOM   8908  C CD  . PRO D  1  375 ? 25.264  -5.953  10.679  1.00 57.43  ?  375  PRO D CD  1 
ATOM   8909  N N   . PRO D  1  376 ? 26.658  -8.647  7.092   1.00 61.21  ?  376  PRO D N   1 
ATOM   8910  C CA  . PRO D  1  376 ? 26.026  -9.371  5.976   1.00 62.72  ?  376  PRO D CA  1 
ATOM   8911  C C   . PRO D  1  376 ? 25.010  -10.411 6.413   1.00 61.34  ?  376  PRO D C   1 
ATOM   8912  O O   . PRO D  1  376 ? 24.276  -10.923 5.559   1.00 62.66  ?  376  PRO D O   1 
ATOM   8913  C CB  . PRO D  1  376 ? 27.213  -10.038 5.264   1.00 64.63  ?  376  PRO D CB  1 
ATOM   8914  C CG  . PRO D  1  376 ? 28.406  -9.270  5.696   1.00 64.45  ?  376  PRO D CG  1 
ATOM   8915  C CD  . PRO D  1  376 ? 28.120  -8.818  7.097   1.00 61.99  ?  376  PRO D CD  1 
ATOM   8916  N N   . GLY D  1  377 ? 24.942  -10.739 7.702   1.00 65.13  ?  377  GLY D N   1 
ATOM   8917  C CA  . GLY D  1  377 ? 24.010  -11.743 8.167   1.00 63.76  ?  377  GLY D CA  1 
ATOM   8918  C C   . GLY D  1  377 ? 22.582  -11.279 8.314   1.00 62.71  ?  377  GLY D C   1 
ATOM   8919  O O   . GLY D  1  377 ? 21.692  -12.120 8.455   1.00 62.00  ?  377  GLY D O   1 
ATOM   8920  N N   . ILE D  1  378 ? 22.337  -9.967  8.300   1.00 62.31  ?  378  ILE D N   1 
ATOM   8921  C CA  . ILE D  1  378 ? 20.982  -9.467  8.511   1.00 61.01  ?  378  ILE D CA  1 
ATOM   8922  C C   . ILE D  1  378 ? 20.048  -9.989  7.430   1.00 62.35  ?  378  ILE D C   1 
ATOM   8923  O O   . ILE D  1  378 ? 18.990  -10.567 7.719   1.00 61.24  ?  378  ILE D O   1 
ATOM   8924  C CB  . ILE D  1  378 ? 20.968  -7.931  8.559   1.00 60.91  ?  378  ILE D CB  1 
ATOM   8925  C CG1 . ILE D  1  378 ? 21.432  -7.439  9.925   1.00 59.41  ?  378  ILE D CG1 1 
ATOM   8926  C CG2 . ILE D  1  378 ? 19.562  -7.412  8.294   1.00 60.18  ?  378  ILE D CG2 1 
ATOM   8927  C CD1 . ILE D  1  378 ? 21.061  -5.994  10.201  1.00 59.11  ?  378  ILE D CD1 1 
ATOM   8928  N N   . ALA D  1  379 ? 20.418  -9.778  6.166   1.00 58.06  ?  379  ALA D N   1 
ATOM   8929  C CA  . ALA D  1  379 ? 19.606  -10.206 5.039   1.00 60.21  ?  379  ALA D CA  1 
ATOM   8930  C C   . ALA D  1  379 ? 19.935  -11.619 4.587   1.00 61.94  ?  379  ALA D C   1 
ATOM   8931  O O   . ALA D  1  379 ? 19.577  -11.999 3.467   1.00 64.82  ?  379  ALA D O   1 
ATOM   8932  C CB  . ALA D  1  379 ? 19.758  -9.224  3.878   1.00 62.73  ?  379  ALA D CB  1 
ATOM   8933  N N   . ASN D  1  380 ? 20.584  -12.410 5.445   1.00 63.80  ?  380  ASN D N   1 
ATOM   8934  C CA  . ASN D  1  380 ? 21.054  -13.741 5.077   1.00 65.13  ?  380  ASN D CA  1 
ATOM   8935  C C   . ASN D  1  380 ? 19.923  -14.748 4.900   1.00 65.43  ?  380  ASN D C   1 
ATOM   8936  O O   . ASN D  1  380 ? 20.100  -15.736 4.180   1.00 67.44  ?  380  ASN D O   1 
ATOM   8937  C CB  . ASN D  1  380 ? 22.032  -14.239 6.138   1.00 63.14  ?  380  ASN D CB  1 
ATOM   8938  C CG  . ASN D  1  380 ? 22.841  -15.432 5.681   1.00 64.48  ?  380  ASN D CG  1 
ATOM   8939  O OD1 . ASN D  1  380 ? 23.212  -15.540 4.512   1.00 67.21  ?  380  ASN D OD1 1 
ATOM   8940  N ND2 . ASN D  1  380 ? 23.125  -16.335 6.614   1.00 62.62  ?  380  ASN D ND2 1 
ATOM   8941  N N   . SER D  1  381 ? 18.777  -14.535 5.541   1.00 58.71  ?  381  SER D N   1 
ATOM   8942  C CA  . SER D  1  381 ? 17.669  -15.475 5.425   1.00 58.99  ?  381  SER D CA  1 
ATOM   8943  C C   . SER D  1  381 ? 17.103  -15.472 4.010   1.00 62.61  ?  381  SER D C   1 
ATOM   8944  O O   . SER D  1  381 ? 16.874  -14.411 3.422   1.00 63.88  ?  381  SER D O   1 
ATOM   8945  C CB  . SER D  1  381 ? 16.571  -15.129 6.430   1.00 56.14  ?  381  SER D CB  1 
ATOM   8946  O OG  . SER D  1  381 ? 15.389  -15.865 6.162   1.00 56.81  ?  381  SER D OG  1 
ATOM   8947  N N   . THR D  1  382 ? 16.888  -16.666 3.456   1.00 55.37  ?  382  THR D N   1 
ATOM   8948  C CA  . THR D  1  382 ? 16.221  -16.766 2.164   1.00 59.07  ?  382  THR D CA  1 
ATOM   8949  C C   . THR D  1  382 ? 14.739  -16.426 2.256   1.00 58.87  ?  382  THR D C   1 
ATOM   8950  O O   . THR D  1  382 ? 14.131  -16.069 1.239   1.00 62.09  ?  382  THR D O   1 
ATOM   8951  C CB  . THR D  1  382 ? 16.400  -18.171 1.587   1.00 60.75  ?  382  THR D CB  1 
ATOM   8952  O OG1 . THR D  1  382 ? 16.355  -19.137 2.645   1.00 57.74  ?  382  THR D OG1 1 
ATOM   8953  C CG2 . THR D  1  382 ? 17.740  -18.275 0.888   1.00 62.51  ?  382  THR D CG2 1 
ATOM   8954  N N   . GLU D  1  383 ? 14.153  -16.521 3.448   1.00 58.67  ?  383  GLU D N   1 
ATOM   8955  C CA  . GLU D  1  383 ? 12.750  -16.203 3.674   1.00 57.96  ?  383  GLU D CA  1 
ATOM   8956  C C   . GLU D  1  383 ? 12.520  -14.756 4.080   1.00 55.95  ?  383  GLU D C   1 
ATOM   8957  O O   . GLU D  1  383 ? 11.368  -14.380 4.324   1.00 54.87  ?  383  GLU D O   1 
ATOM   8958  C CB  . GLU D  1  383 ? 12.169  -17.120 4.752   1.00 55.18  ?  383  GLU D CB  1 
ATOM   8959  C CG  . GLU D  1  383 ? 12.516  -18.588 4.583   1.00 56.07  ?  383  GLU D CG  1 
ATOM   8960  C CD  . GLU D  1  383 ? 12.046  -19.155 3.254   1.00 59.98  ?  383  GLU D CD  1 
ATOM   8961  O OE1 . GLU D  1  383 ? 10.818  -19.294 3.060   1.00 60.82  ?  383  GLU D OE1 1 
ATOM   8962  O OE2 . GLU D  1  383 ? 12.906  -19.474 2.404   1.00 62.21  -1 383  GLU D OE2 1 
ATOM   8963  N N   . LEU D  1  384 ? 13.575  -13.945 4.178   1.00 52.30  ?  384  LEU D N   1 
ATOM   8964  C CA  . LEU D  1  384 ? 13.404  -12.555 4.580   1.00 50.11  ?  384  LEU D CA  1 
ATOM   8965  C C   . LEU D  1  384 ? 12.569  -11.809 3.548   1.00 52.37  ?  384  LEU D C   1 
ATOM   8966  O O   . LEU D  1  384 ? 12.814  -11.905 2.342   1.00 56.43  ?  384  LEU D O   1 
ATOM   8967  C CB  . LEU D  1  384 ? 14.762  -11.875 4.760   1.00 49.83  ?  384  LEU D CB  1 
ATOM   8968  C CG  . LEU D  1  384 ? 14.688  -10.527 5.484   1.00 48.40  ?  384  LEU D CG  1 
ATOM   8969  C CD1 . LEU D  1  384 ? 14.472  -10.737 6.974   1.00 47.91  ?  384  LEU D CD1 1 
ATOM   8970  C CD2 . LEU D  1  384 ? 15.923  -9.670  5.232   1.00 49.09  ?  384  LEU D CD2 1 
ATOM   8971  N N   . THR D  1  385 ? 11.577  -11.062 4.027   1.00 51.35  ?  385  THR D N   1 
ATOM   8972  C CA  . THR D  1  385 ? 10.649  -10.375 3.138   1.00 53.08  ?  385  THR D CA  1 
ATOM   8973  C C   . THR D  1  385 ? 10.542  -8.891  3.466   1.00 50.12  ?  385  THR D C   1 
ATOM   8974  O O   . THR D  1  385 ? 10.224  -8.081  2.590   1.00 51.61  ?  385  THR D O   1 
ATOM   8975  C CB  . THR D  1  385 ? 9.266   -11.016 3.211   1.00 53.26  ?  385  THR D CB  1 
ATOM   8976  O OG1 . THR D  1  385 ? 8.835   -11.067 4.578   1.00 49.07  ?  385  THR D OG1 1 
ATOM   8977  C CG2 . THR D  1  385 ? 9.316   -12.418 2.655   1.00 56.95  ?  385  THR D CG2 1 
ATOM   8978  N N   . VAL D  1  386 ? 10.756  -8.527  4.729   1.00 54.53  ?  386  VAL D N   1 
ATOM   8979  C CA  . VAL D  1  386 ? 10.624  -7.149  5.187   1.00 51.89  ?  386  VAL D CA  1 
ATOM   8980  C C   . VAL D  1  386 ? 11.834  -6.793  6.037   1.00 50.57  ?  386  VAL D C   1 
ATOM   8981  O O   . VAL D  1  386 ? 12.143  -7.494  7.006   1.00 49.23  ?  386  VAL D O   1 
ATOM   8982  C CB  . VAL D  1  386 ? 9.323   -6.938  5.984   1.00 48.88  ?  386  VAL D CB  1 
ATOM   8983  C CG1 . VAL D  1  386 ? 9.191   -5.479  6.428   1.00 46.73  ?  386  VAL D CG1 1 
ATOM   8984  C CG2 . VAL D  1  386 ? 8.118   -7.361  5.155   1.00 50.45  ?  386  VAL D CG2 1 
ATOM   8985  N N   . LEU D  1  387 ? 12.494  -5.688  5.698   1.00 50.81  ?  387  LEU D N   1 
ATOM   8986  C CA  . LEU D  1  387 ? 13.681  -5.221  6.414   1.00 50.28  ?  387  LEU D CA  1 
ATOM   8987  C C   . LEU D  1  387 ? 13.544  -3.718  6.658   1.00 49.40  ?  387  LEU D C   1 
ATOM   8988  O O   . LEU D  1  387 ? 13.851  -2.908  5.779   1.00 51.04  ?  387  LEU D O   1 
ATOM   8989  C CB  . LEU D  1  387 ? 14.953  -5.551  5.636   1.00 53.05  ?  387  LEU D CB  1 
ATOM   8990  C CG  . LEU D  1  387 ? 16.279  -5.145  6.284   1.00 52.92  ?  387  LEU D CG  1 
ATOM   8991  C CD1 . LEU D  1  387 ? 16.403  -5.766  7.666   1.00 50.81  ?  387  LEU D CD1 1 
ATOM   8992  C CD2 . LEU D  1  387 ? 17.460  -5.533  5.405   1.00 55.75  ?  387  LEU D CD2 1 
ATOM   8993  N N   . GLN D  1  388 ? 13.057  -3.349  7.844   1.00 53.62  ?  388  GLN D N   1 
ATOM   8994  C CA  . GLN D  1  388 ? 12.874  -1.953  8.233   1.00 53.31  ?  388  GLN D CA  1 
ATOM   8995  C C   . GLN D  1  388 ? 14.070  -1.502  9.062   1.00 54.12  ?  388  GLN D C   1 
ATOM   8996  O O   . GLN D  1  388 ? 14.307  -2.031  10.155  1.00 53.22  ?  388  GLN D O   1 
ATOM   8997  C CB  . GLN D  1  388 ? 11.579  -1.779  9.027   1.00 51.23  ?  388  GLN D CB  1 
ATOM   8998  C CG  . GLN D  1  388 ? 10.378  -2.463  8.407   1.00 50.29  ?  388  GLN D CG  1 
ATOM   8999  C CD  . GLN D  1  388 ? 9.634   -1.570  7.437   1.00 50.74  ?  388  GLN D CD  1 
ATOM   9000  O OE1 . GLN D  1  388 ? 9.594   -0.351  7.602   1.00 50.89  ?  388  GLN D OE1 1 
ATOM   9001  N NE2 . GLN D  1  388 ? 9.038   -2.173  6.417   1.00 51.40  ?  388  GLN D NE2 1 
ATOM   9002  N N   . LEU D  1  389 ? 14.817  -0.518  8.550   1.00 53.39  ?  389  LEU D N   1 
ATOM   9003  C CA  . LEU D  1  389 ? 16.035  -0.066  9.214   1.00 54.68  ?  389  LEU D CA  1 
ATOM   9004  C C   . LEU D  1  389 ? 16.141  1.452   9.323   1.00 56.38  ?  389  LEU D C   1 
ATOM   9005  O O   . LEU D  1  389 ? 17.177  1.952   9.778   1.00 57.95  ?  389  LEU D O   1 
ATOM   9006  C CB  . LEU D  1  389 ? 17.275  -0.618  8.494   1.00 56.12  ?  389  LEU D CB  1 
ATOM   9007  C CG  . LEU D  1  389 ? 17.430  -2.138  8.493   1.00 55.31  ?  389  LEU D CG  1 
ATOM   9008  C CD1 . LEU D  1  389 ? 18.606  -2.565  7.648   1.00 57.28  ?  389  LEU D CD1 1 
ATOM   9009  C CD2 . LEU D  1  389 ? 17.596  -2.634  9.908   1.00 53.87  ?  389  LEU D CD2 1 
ATOM   9010  N N   . ASP D  1  390 ? 15.099  2.193   8.946   1.00 57.37  ?  390  ASP D N   1 
ATOM   9011  C CA  . ASP D  1  390 ? 15.158  3.647   8.924   1.00 59.53  ?  390  ASP D CA  1 
ATOM   9012  C C   . ASP D  1  390 ? 15.277  4.217   10.337  1.00 60.62  ?  390  ASP D C   1 
ATOM   9013  O O   . ASP D  1  390 ? 15.055  3.532   11.337  1.00 59.18  ?  390  ASP D O   1 
ATOM   9014  C CB  . ASP D  1  390 ? 13.922  4.228   8.248   1.00 58.87  ?  390  ASP D CB  1 
ATOM   9015  C CG  . ASP D  1  390 ? 12.649  3.925   9.008   1.00 56.66  ?  390  ASP D CG  1 
ATOM   9016  O OD1 . ASP D  1  390 ? 12.177  2.770   8.947   1.00 54.43  ?  390  ASP D OD1 1 
ATOM   9017  O OD2 . ASP D  1  390 ? 12.135  4.838   9.687   1.00 57.54  -1 390  ASP D OD2 1 
ATOM   9018  N N   . THR D  1  391 ? 15.634  5.502   10.400  1.00 58.38  ?  391  THR D N   1 
ATOM   9019  C CA  . THR D  1  391 ? 15.716  6.263   11.651  1.00 60.09  ?  391  THR D CA  1 
ATOM   9020  C C   . THR D  1  391 ? 16.688  5.613   12.641  1.00 59.19  ?  391  THR D C   1 
ATOM   9021  O O   . THR D  1  391 ? 16.319  5.163   13.729  1.00 58.11  ?  391  THR D O   1 
ATOM   9022  C CB  . THR D  1  391 ? 14.328  6.454   12.269  1.00 59.80  ?  391  THR D CB  1 
ATOM   9023  O OG1 . THR D  1  391 ? 13.394  6.778   11.234  1.00 59.18  ?  391  THR D OG1 1 
ATOM   9024  C CG2 . THR D  1  391 ? 14.353  7.589   13.278  1.00 61.83  ?  391  THR D CG2 1 
ATOM   9025  N N   . ASN D  1  392 ? 17.950  5.562   12.225  1.00 63.45  ?  392  ASN D N   1 
ATOM   9026  C CA  . ASN D  1  392 ? 19.036  4.986   13.008  1.00 62.83  ?  392  ASN D CA  1 
ATOM   9027  C C   . ASN D  1  392 ? 20.303  5.760   12.669  1.00 64.57  ?  392  ASN D C   1 
ATOM   9028  O O   . ASN D  1  392 ? 20.243  6.853   12.099  1.00 66.18  ?  392  ASN D O   1 
ATOM   9029  C CB  . ASN D  1  392 ? 19.173  3.484   12.729  1.00 60.68  ?  392  ASN D CB  1 
ATOM   9030  C CG  . ASN D  1  392 ? 18.329  2.634   13.669  1.00 58.66  ?  392  ASN D CG  1 
ATOM   9031  O OD1 . ASN D  1  392 ? 18.618  2.531   14.862  1.00 58.55  ?  392  ASN D OD1 1 
ATOM   9032  N ND2 . ASN D  1  392 ? 17.282  2.019   13.131  1.00 57.02  ?  392  ASN D ND2 1 
ATOM   9033  N N   . ASN D  1  393 ? 21.455  5.213   13.043  1.00 65.57  ?  393  ASN D N   1 
ATOM   9034  C CA  . ASN D  1  393 ? 22.741  5.826   12.719  1.00 66.97  ?  393  ASN D CA  1 
ATOM   9035  C C   . ASN D  1  393 ? 23.690  4.795   12.113  1.00 66.41  ?  393  ASN D C   1 
ATOM   9036  O O   . ASN D  1  393 ? 24.866  4.704   12.470  1.00 66.71  ?  393  ASN D O   1 
ATOM   9037  C CB  . ASN D  1  393 ? 23.355  6.487   13.949  1.00 67.58  ?  393  ASN D CB  1 
ATOM   9038  C CG  . ASN D  1  393 ? 22.392  7.437   14.640  1.00 68.16  ?  393  ASN D CG  1 
ATOM   9039  O OD1 . ASN D  1  393 ? 22.407  8.649   14.402  1.00 69.49  ?  393  ASN D OD1 1 
ATOM   9040  N ND2 . ASN D  1  393 ? 21.543  6.888   15.502  1.00 67.08  ?  393  ASN D ND2 1 
ATOM   9041  N N   . PHE D  1  394 ? 23.183  3.997   11.177  1.00 65.82  ?  394  PHE D N   1 
ATOM   9042  C CA  . PHE D  1  394 ? 24.032  3.031   10.495  1.00 65.59  ?  394  PHE D CA  1 
ATOM   9043  C C   . PHE D  1  394 ? 24.968  3.733   9.510   1.00 67.49  ?  394  PHE D C   1 
ATOM   9044  O O   . PHE D  1  394 ? 24.730  4.864   9.078   1.00 68.80  ?  394  PHE D O   1 
ATOM   9045  C CB  . PHE D  1  394 ? 23.185  1.985   9.767   1.00 64.37  ?  394  PHE D CB  1 
ATOM   9046  C CG  . PHE D  1  394 ? 22.395  1.095   10.690  1.00 62.25  ?  394  PHE D CG  1 
ATOM   9047  C CD1 . PHE D  1  394 ? 23.014  0.435   11.742  1.00 61.42  ?  394  PHE D CD1 1 
ATOM   9048  C CD2 . PHE D  1  394 ? 21.033  0.922   10.505  1.00 61.10  ?  394  PHE D CD2 1 
ATOM   9049  C CE1 . PHE D  1  394 ? 22.286  -0.379  12.592  1.00 59.58  ?  394  PHE D CE1 1 
ATOM   9050  C CE2 . PHE D  1  394 ? 20.300  0.106   11.351  1.00 59.11  ?  394  PHE D CE2 1 
ATOM   9051  C CZ  . PHE D  1  394 ? 20.928  -0.545  12.396  1.00 58.43  ?  394  PHE D CZ  1 
ATOM   9052  N N   . THR D  1  395 ? 26.054  3.043   9.162   1.00 64.54  ?  395  THR D N   1 
ATOM   9053  C CA  . THR D  1  395 ? 27.075  3.577   8.271   1.00 66.25  ?  395  THR D CA  1 
ATOM   9054  C C   . THR D  1  395 ? 27.492  2.503   7.272   1.00 66.51  ?  395  THR D C   1 
ATOM   9055  O O   . THR D  1  395 ? 27.130  1.329   7.399   1.00 65.32  ?  395  THR D O   1 
ATOM   9056  C CB  . THR D  1  395 ? 28.303  4.062   9.051   1.00 66.70  ?  395  THR D CB  1 
ATOM   9057  O OG1 . THR D  1  395 ? 28.916  2.947   9.710   1.00 65.64  ?  395  THR D OG1 1 
ATOM   9058  C CG2 . THR D  1  395 ? 27.911  5.098   10.089  1.00 66.73  ?  395  THR D CG2 1 
ATOM   9059  N N   . GLY D  1  396 ? 28.251  2.916   6.262   1.00 63.92  ?  396  GLY D N   1 
ATOM   9060  C CA  . GLY D  1  396 ? 28.874  1.968   5.357   1.00 64.62  ?  396  GLY D CA  1 
ATOM   9061  C C   . GLY D  1  396 ? 27.974  1.517   4.220   1.00 65.16  ?  396  GLY D C   1 
ATOM   9062  O O   . GLY D  1  396 ? 27.008  2.180   3.832   1.00 65.46  ?  396  GLY D O   1 
ATOM   9063  N N   . PHE D  1  397 ? 28.307  0.345   3.686   1.00 66.00  ?  397  PHE D N   1 
ATOM   9064  C CA  . PHE D  1  397 ? 27.699  -0.186  2.475   1.00 67.37  ?  397  PHE D CA  1 
ATOM   9065  C C   . PHE D  1  397 ? 26.606  -1.198  2.807   1.00 65.96  ?  397  PHE D C   1 
ATOM   9066  O O   . PHE D  1  397 ? 26.586  -1.803  3.884   1.00 63.98  ?  397  PHE D O   1 
ATOM   9067  C CB  . PHE D  1  397 ? 28.754  -0.859  1.588   1.00 69.24  ?  397  PHE D CB  1 
ATOM   9068  C CG  . PHE D  1  397 ? 29.843  0.064   1.105   1.00 70.60  ?  397  PHE D CG  1 
ATOM   9069  C CD1 . PHE D  1  397 ? 30.766  0.603   1.987   1.00 69.68  ?  397  PHE D CD1 1 
ATOM   9070  C CD2 . PHE D  1  397 ? 29.964  0.363   -0.243  1.00 72.87  ?  397  PHE D CD2 1 
ATOM   9071  C CE1 . PHE D  1  397 ? 31.768  1.442   1.538   1.00 70.84  ?  397  PHE D CE1 1 
ATOM   9072  C CE2 . PHE D  1  397 ? 30.969  1.198   -0.699  1.00 73.86  ?  397  PHE D CE2 1 
ATOM   9073  C CZ  . PHE D  1  397 ? 31.870  1.738   0.192   1.00 72.80  ?  397  PHE D CZ  1 
ATOM   9074  N N   . LEU D  1  398 ? 25.683  -1.377  1.852   1.00 64.45  ?  398  LEU D N   1 
ATOM   9075  C CA  . LEU D  1  398 ? 24.716  -2.463  1.940   1.00 63.59  ?  398  LEU D CA  1 
ATOM   9076  C C   . LEU D  1  398 ? 25.394  -3.790  1.602   1.00 64.73  ?  398  LEU D C   1 
ATOM   9077  O O   . LEU D  1  398 ? 26.149  -3.869  0.630   1.00 67.25  ?  398  LEU D O   1 
ATOM   9078  C CB  . LEU D  1  398 ? 23.546  -2.228  0.987   1.00 64.86  ?  398  LEU D CB  1 
ATOM   9079  C CG  . LEU D  1  398 ? 22.603  -1.061  1.286   1.00 63.47  ?  398  LEU D CG  1 
ATOM   9080  C CD1 . LEU D  1  398 ? 21.380  -1.130  0.396   1.00 64.43  ?  398  LEU D CD1 1 
ATOM   9081  C CD2 . LEU D  1  398 ? 22.193  -1.056  2.743   1.00 60.23  ?  398  LEU D CD2 1 
ATOM   9082  N N   . PRO D  1  399 ? 25.148  -4.840  2.381   1.00 67.18  ?  399  PRO D N   1 
ATOM   9083  C CA  . PRO D  1  399 ? 25.747  -6.145  2.073   1.00 68.26  ?  399  PRO D CA  1 
ATOM   9084  C C   . PRO D  1  399 ? 25.164  -6.743  0.801   1.00 71.12  ?  399  PRO D C   1 
ATOM   9085  O O   . PRO D  1  399 ? 24.037  -6.446  0.397   1.00 71.69  ?  399  PRO D O   1 
ATOM   9086  C CB  . PRO D  1  399 ? 25.393  -7.000  3.296   1.00 65.49  ?  399  PRO D CB  1 
ATOM   9087  C CG  . PRO D  1  399 ? 25.056  -6.011  4.373   1.00 63.08  ?  399  PRO D CG  1 
ATOM   9088  C CD  . PRO D  1  399 ? 24.419  -4.861  3.658   1.00 64.10  ?  399  PRO D CD  1 
ATOM   9089  N N   . ASP D  1  400 ? 25.956  -7.611  0.171   1.00 72.65  ?  400  ASP D N   1 
ATOM   9090  C CA  . ASP D  1  400 ? 25.565  -8.239  -1.086  1.00 75.99  ?  400  ASP D CA  1 
ATOM   9091  C C   . ASP D  1  400 ? 24.554  -9.361  -0.903  1.00 75.68  ?  400  ASP D C   1 
ATOM   9092  O O   . ASP D  1  400 ? 24.112  -9.941  -1.900  1.00 78.68  ?  400  ASP D O   1 
ATOM   9093  C CB  . ASP D  1  400 ? 26.793  -8.780  -1.817  1.00 77.97  ?  400  ASP D CB  1 
ATOM   9094  C CG  . ASP D  1  400 ? 27.803  -7.696  -2.136  1.00 78.63  ?  400  ASP D CG  1 
ATOM   9095  O OD1 . ASP D  1  400 ? 28.632  -7.381  -1.253  1.00 76.54  -1 400  ASP D OD1 1 
ATOM   9096  O OD2 . ASP D  1  400 ? 27.776  -7.168  -3.271  1.00 81.26  ?  400  ASP D OD2 1 
ATOM   9097  N N   . THR D  1  401 ? 24.191  -9.687  0.333   1.00 70.13  ?  401  THR D N   1 
ATOM   9098  C CA  . THR D  1  401 ? 23.197  -10.707 0.633   1.00 69.35  ?  401  THR D CA  1 
ATOM   9099  C C   . THR D  1  401 ? 21.772  -10.164 0.646   1.00 68.91  ?  401  THR D C   1 
ATOM   9100  O O   . THR D  1  401 ? 20.866  -10.863 1.110   1.00 67.61  ?  401  THR D O   1 
ATOM   9101  C CB  . THR D  1  401 ? 23.514  -11.358 1.983   1.00 65.89  ?  401  THR D CB  1 
ATOM   9102  O OG1 . THR D  1  401 ? 23.469  -10.367 3.014   1.00 63.11  ?  401  THR D OG1 1 
ATOM   9103  C CG2 . THR D  1  401 ? 24.892  -11.964 1.962   1.00 66.31  ?  401  THR D CG2 1 
ATOM   9104  N N   . ILE D  1  402 ? 21.555  -8.950  0.128   1.00 68.04  ?  402  ILE D N   1 
ATOM   9105  C CA  . ILE D  1  402 ? 20.338  -8.198  0.431   1.00 66.38  ?  402  ILE D CA  1 
ATOM   9106  C C   . ILE D  1  402 ? 19.085  -8.965  0.009   1.00 67.75  ?  402  ILE D C   1 
ATOM   9107  O O   . ILE D  1  402 ? 18.118  -9.063  0.775   1.00 65.03  ?  402  ILE D O   1 
ATOM   9108  C CB  . ILE D  1  402 ? 20.409  -6.800  -0.215  1.00 67.58  ?  402  ILE D CB  1 
ATOM   9109  C CG1 . ILE D  1  402 ? 19.171  -5.970  0.136   1.00 65.34  ?  402  ILE D CG1 1 
ATOM   9110  C CG2 . ILE D  1  402 ? 20.616  -6.904  -1.719  1.00 72.54  ?  402  ILE D CG2 1 
ATOM   9111  C CD1 . ILE D  1  402 ? 18.933  -5.830  1.623   1.00 60.85  ?  402  ILE D CD1 1 
ATOM   9112  N N   . CYS D  1  403 ? 19.080  -9.542  -1.188  1.00 62.35  ?  403  CYS D N   1 
ATOM   9113  C CA  . CYS D  1  403 ? 17.907  -10.253 -1.695  1.00 64.54  ?  403  CYS D CA  1 
ATOM   9114  C C   . CYS D  1  403 ? 18.303  -11.659 -2.120  1.00 66.81  ?  403  CYS D C   1 
ATOM   9115  O O   . CYS D  1  403 ? 17.965  -12.136 -3.204  1.00 71.08  ?  403  CYS D O   1 
ATOM   9116  C CB  . CYS D  1  403 ? 17.229  -9.496  -2.836  1.00 68.31  ?  403  CYS D CB  1 
ATOM   9117  S SG  . CYS D  1  403 ? 15.555  -10.106 -3.213  1.00 70.22  ?  403  CYS D SG  1 
ATOM   9118  N N   . ARG D  1  404 ? 19.054  -12.332 -1.245  1.00 68.22  ?  404  ARG D N   1 
ATOM   9119  C CA  . ARG D  1  404 ? 19.620  -13.634 -1.576  1.00 69.45  ?  404  ARG D CA  1 
ATOM   9120  C C   . ARG D  1  404 ? 18.539  -14.652 -1.910  1.00 70.82  ?  404  ARG D C   1 
ATOM   9121  O O   . ARG D  1  404 ? 18.663  -15.402 -2.883  1.00 73.84  ?  404  ARG D O   1 
ATOM   9122  C CB  . ARG D  1  404 ? 20.468  -14.128 -0.409  1.00 65.59  ?  404  ARG D CB  1 
ATOM   9123  C CG  . ARG D  1  404 ? 21.197  -15.413 -0.684  1.00 66.25  ?  404  ARG D CG  1 
ATOM   9124  C CD  . ARG D  1  404 ? 22.350  -15.590 0.291   1.00 63.30  ?  404  ARG D CD  1 
ATOM   9125  N NE  . ARG D  1  404 ? 21.930  -16.161 1.564   1.00 59.84  ?  404  ARG D NE  1 
ATOM   9126  C CZ  . ARG D  1  404 ? 21.399  -17.368 1.708   1.00 59.31  ?  404  ARG D CZ  1 
ATOM   9127  N NH1 . ARG D  1  404 ? 21.215  -18.174 0.673   1.00 61.85  ?  404  ARG D NH1 1 
ATOM   9128  N NH2 . ARG D  1  404 ? 21.056  -17.783 2.924   1.00 56.20  ?  404  ARG D NH2 1 
ATOM   9129  N N   . GLY D  1  405 ? 17.476  -14.700 -1.118  1.00 60.25  ?  405  GLY D N   1 
ATOM   9130  C CA  . GLY D  1  405 ? 16.408  -15.645 -1.374  1.00 61.33  ?  405  GLY D CA  1 
ATOM   9131  C C   . GLY D  1  405 ? 15.413  -15.231 -2.435  1.00 65.28  ?  405  GLY D C   1 
ATOM   9132  O O   . GLY D  1  405 ? 14.514  -16.015 -2.756  1.00 66.41  ?  405  GLY D O   1 
ATOM   9133  N N   . GLY D  1  406 ? 15.534  -14.018 -2.970  1.00 58.95  ?  406  GLY D N   1 
ATOM   9134  C CA  . GLY D  1  406 ? 14.600  -13.563 -3.980  1.00 61.89  ?  406  GLY D CA  1 
ATOM   9135  C C   . GLY D  1  406 ? 13.182  -13.363 -3.496  1.00 60.23  ?  406  GLY D C   1 
ATOM   9136  O O   . GLY D  1  406 ? 12.248  -13.429 -4.303  1.00 62.23  ?  406  GLY D O   1 
ATOM   9137  N N   . LYS D  1  407 ? 12.994  -13.115 -2.196  1.00 63.06  ?  407  LYS D N   1 
ATOM   9138  C CA  . LYS D  1  407 ? 11.674  -12.926 -1.603  1.00 60.97  ?  407  LYS D CA  1 
ATOM   9139  C C   . LYS D  1  407 ? 11.527  -11.593 -0.881  1.00 57.21  ?  407  LYS D C   1 
ATOM   9140  O O   . LYS D  1  407 ? 10.520  -11.385 -0.199  1.00 54.35  ?  407  LYS D O   1 
ATOM   9141  C CB  . LYS D  1  407 ? 11.367  -14.062 -0.626  1.00 58.05  ?  407  LYS D CB  1 
ATOM   9142  C CG  . LYS D  1  407 ? 11.351  -15.443 -1.241  1.00 60.53  ?  407  LYS D CG  1 
ATOM   9143  C CD  . LYS D  1  407 ? 10.838  -16.456 -0.236  1.00 57.32  ?  407  LYS D CD  1 
ATOM   9144  C CE  . LYS D  1  407 ? 10.898  -17.871 -0.773  1.00 58.79  ?  407  LYS D CE  1 
ATOM   9145  N NZ  . LYS D  1  407 ? 10.276  -18.828 0.186   1.00 55.75  ?  407  LYS D NZ  1 
ATOM   9146  N N   . LEU D  1  408 ? 12.492  -10.686 -1.003  1.00 58.47  ?  408  LEU D N   1 
ATOM   9147  C CA  . LEU D  1  408 ? 12.431  -9.433  -0.261  1.00 54.00  ?  408  LEU D CA  1 
ATOM   9148  C C   . LEU D  1  408 ? 11.400  -8.509  -0.894  1.00 54.73  ?  408  LEU D C   1 
ATOM   9149  O O   . LEU D  1  408 ? 11.481  -8.200  -2.088  1.00 58.90  ?  408  LEU D O   1 
ATOM   9150  C CB  . LEU D  1  408 ? 13.801  -8.761  -0.219  1.00 53.35  ?  408  LEU D CB  1 
ATOM   9151  C CG  . LEU D  1  408 ? 13.919  -7.592  0.762   1.00 49.22  ?  408  LEU D CG  1 
ATOM   9152  C CD1 . LEU D  1  408 ? 13.970  -8.100  2.191   1.00 48.64  ?  408  LEU D CD1 1 
ATOM   9153  C CD2 . LEU D  1  408 ? 15.137  -6.736  0.447   1.00 49.89  ?  408  LEU D CD2 1 
ATOM   9154  N N   . GLU D  1  409 ? 10.423  -8.084  -0.090  1.00 57.52  ?  409  GLU D N   1 
ATOM   9155  C CA  . GLU D  1  409 ? 9.337   -7.220  -0.542  1.00 56.96  ?  409  GLU D CA  1 
ATOM   9156  C C   . GLU D  1  409 ? 9.570   -5.757  -0.179  1.00 53.15  ?  409  GLU D C   1 
ATOM   9157  O O   . GLU D  1  409 ? 9.558   -4.883  -1.051  1.00 54.41  ?  409  GLU D O   1 
ATOM   9158  C CB  . GLU D  1  409 ? 8.009   -7.699  0.057   1.00 54.93  ?  409  GLU D CB  1 
ATOM   9159  C CG  . GLU D  1  409 ? 7.355   -8.842  -0.690  1.00 59.86  ?  409  GLU D CG  1 
ATOM   9160  C CD  . GLU D  1  409 ? 6.089   -9.345  -0.008  1.00 57.76  ?  409  GLU D CD  1 
ATOM   9161  O OE1 . GLU D  1  409 ? 5.705   -8.801  1.056   1.00 52.33  ?  409  GLU D OE1 1 
ATOM   9162  O OE2 . GLU D  1  409 ? 5.467   -10.286 -0.548  1.00 61.96  -1 409  GLU D OE2 1 
ATOM   9163  N N   . ASN D  1  410 ? 9.783   -5.477  1.105   1.00 57.11  ?  410  ASN D N   1 
ATOM   9164  C CA  . ASN D  1  410 ? 9.810   -4.120  1.634   1.00 53.83  ?  410  ASN D CA  1 
ATOM   9165  C C   . ASN D  1  410 ? 11.145  -3.871  2.320   1.00 52.98  ?  410  ASN D C   1 
ATOM   9166  O O   . ASN D  1  410 ? 11.529  -4.617  3.228   1.00 51.76  ?  410  ASN D O   1 
ATOM   9167  C CB  . ASN D  1  410 ? 8.647   -3.900  2.611   1.00 50.06  ?  410  ASN D CB  1 
ATOM   9168  C CG  . ASN D  1  410 ? 7.294   -4.165  1.969   1.00 50.80  ?  410  ASN D CG  1 
ATOM   9169  O OD1 . ASN D  1  410 ? 7.122   -3.950  0.773   1.00 53.52  ?  410  ASN D OD1 1 
ATOM   9170  N ND2 . ASN D  1  410 ? 6.330   -4.630  2.754   1.00 48.58  ?  410  ASN D ND2 1 
ATOM   9171  N N   . LEU D  1  411 ? 11.842  -2.817  1.891   1.00 50.67  ?  411  LEU D N   1 
ATOM   9172  C CA  . LEU D  1  411 ? 13.161  -2.470  2.410   1.00 50.55  ?  411  LEU D CA  1 
ATOM   9173  C C   . LEU D  1  411 ? 13.180  -0.983  2.723   1.00 49.32  ?  411  LEU D C   1 
ATOM   9174  O O   . LEU D  1  411 ? 12.942  -0.159  1.834   1.00 50.43  ?  411  LEU D O   1 
ATOM   9175  C CB  . LEU D  1  411 ? 14.261  -2.820  1.403   1.00 54.25  ?  411  LEU D CB  1 
ATOM   9176  C CG  . LEU D  1  411 ? 15.685  -2.365  1.731   1.00 54.64  ?  411  LEU D CG  1 
ATOM   9177  C CD1 . LEU D  1  411 ? 16.196  -3.020  3.013   1.00 52.58  ?  411  LEU D CD1 1 
ATOM   9178  C CD2 . LEU D  1  411 ? 16.620  -2.643  0.560   1.00 58.60  ?  411  LEU D CD2 1 
ATOM   9179  N N   . THR D  1  412 ? 13.483  -0.644  3.976   1.00 56.11  ?  412  THR D N   1 
ATOM   9180  C CA  . THR D  1  412 ? 13.440  0.727   4.468   1.00 55.49  ?  412  THR D CA  1 
ATOM   9181  C C   . THR D  1  412 ? 14.800  1.119   5.030   1.00 56.63  ?  412  THR D C   1 
ATOM   9182  O O   . THR D  1  412 ? 15.304  0.470   5.954   1.00 55.89  ?  412  THR D O   1 
ATOM   9183  C CB  . THR D  1  412 ? 12.364  0.881   5.549   1.00 52.97  ?  412  THR D CB  1 
ATOM   9184  O OG1 . THR D  1  412 ? 11.107  0.439   5.032   1.00 51.94  ?  412  THR D OG1 1 
ATOM   9185  C CG2 . THR D  1  412 ? 12.213  2.323   5.942   1.00 53.22  ?  412  THR D CG2 1 
ATOM   9186  N N   . LEU D  1  413 ? 15.366  2.217   4.510   1.00 54.89  ?  413  LEU D N   1 
ATOM   9187  C CA  . LEU D  1  413 ? 16.698  2.654   4.917   1.00 56.53  ?  413  LEU D CA  1 
ATOM   9188  C C   . LEU D  1  413 ? 16.762  4.154   5.194   1.00 57.87  ?  413  LEU D C   1 
ATOM   9189  O O   . LEU D  1  413 ? 17.858  4.728   5.163   1.00 60.03  ?  413  LEU D O   1 
ATOM   9190  C CB  . LEU D  1  413 ? 17.743  2.295   3.850   1.00 58.73  ?  413  LEU D CB  1 
ATOM   9191  C CG  . LEU D  1  413 ? 17.793  0.827   3.424   1.00 58.64  ?  413  LEU D CG  1 
ATOM   9192  C CD1 . LEU D  1  413 ? 18.656  0.651   2.189   1.00 61.61  ?  413  LEU D CD1 1 
ATOM   9193  C CD2 . LEU D  1  413 ? 18.299  -0.040  4.566   1.00 57.22  ?  413  LEU D CD2 1 
ATOM   9194  N N   . ASP D  1  414 ? 15.627  4.796   5.477   1.00 60.37  ?  414  ASP D N   1 
ATOM   9195  C CA  . ASP D  1  414 ? 15.567  6.253   5.527   1.00 62.12  ?  414  ASP D CA  1 
ATOM   9196  C C   . ASP D  1  414 ? 16.463  6.815   6.625   1.00 64.35  ?  414  ASP D C   1 
ATOM   9197  O O   . ASP D  1  414 ? 16.679  6.189   7.666   1.00 63.53  ?  414  ASP D O   1 
ATOM   9198  C CB  . ASP D  1  414 ? 14.130  6.726   5.759   1.00 60.35  ?  414  ASP D CB  1 
ATOM   9199  C CG  . ASP D  1  414 ? 13.274  6.614   4.521   1.00 58.98  ?  414  ASP D CG  1 
ATOM   9200  O OD1 . ASP D  1  414 ? 13.577  5.724   3.706   1.00 59.07  ?  414  ASP D OD1 1 
ATOM   9201  O OD2 . ASP D  1  414 ? 12.305  7.398   4.365   1.00 58.12  -1 414  ASP D OD2 1 
ATOM   9202  N N   . ASP D  1  415 ? 17.014  8.003   6.360   1.00 65.45  ?  415  ASP D N   1 
ATOM   9203  C CA  . ASP D  1  415 ? 17.668  8.829   7.376   1.00 67.09  ?  415  ASP D CA  1 
ATOM   9204  C C   . ASP D  1  415 ? 18.773  8.061   8.106   1.00 66.42  ?  415  ASP D C   1 
ATOM   9205  O O   . ASP D  1  415 ? 18.725  7.834   9.317   1.00 65.46  ?  415  ASP D O   1 
ATOM   9206  C CB  . ASP D  1  415 ? 16.634  9.387   8.353   1.00 66.36  ?  415  ASP D CB  1 
ATOM   9207  C CG  . ASP D  1  415 ? 15.631  10.286  7.669   1.00 65.22  ?  415  ASP D CG  1 
ATOM   9208  O OD1 . ASP D  1  415 ? 16.040  11.013  6.736   1.00 65.62  -1 415  ASP D OD1 1 
ATOM   9209  O OD2 . ASP D  1  415 ? 14.441  10.267  8.060   1.00 63.56  ?  415  ASP D OD2 1 
ATOM   9210  N N   . ASN D  1  416 ? 19.774  7.658   7.332   1.00 67.31  ?  416  ASN D N   1 
ATOM   9211  C CA  . ASN D  1  416 ? 20.934  6.929   7.827   1.00 66.48  ?  416  ASN D CA  1 
ATOM   9212  C C   . ASN D  1  416 ? 22.166  7.543   7.175   1.00 67.98  ?  416  ASN D C   1 
ATOM   9213  O O   . ASN D  1  416 ? 22.095  8.614   6.564   1.00 69.28  ?  416  ASN D O   1 
ATOM   9214  C CB  . ASN D  1  416 ? 20.802  5.427   7.538   1.00 64.67  ?  416  ASN D CB  1 
ATOM   9215  C CG  . ASN D  1  416 ? 20.188  4.656   8.696   1.00 62.53  ?  416  ASN D CG  1 
ATOM   9216  O OD1 . ASN D  1  416 ? 20.322  5.034   9.857   1.00 62.52  ?  416  ASN D OD1 1 
ATOM   9217  N ND2 . ASN D  1  416 ? 19.497  3.573   8.376   1.00 60.71  ?  416  ASN D ND2 1 
ATOM   9218  N N   . HIS D  1  417 ? 23.311  6.884   7.331   1.00 67.67  ?  417  HIS D N   1 
ATOM   9219  C CA  . HIS D  1  417 ? 24.568  7.335   6.746   1.00 68.91  ?  417  HIS D CA  1 
ATOM   9220  C C   . HIS D  1  417 ? 25.168  6.264   5.843   1.00 68.99  ?  417  HIS D C   1 
ATOM   9221  O O   . HIS D  1  417 ? 26.370  5.996   5.882   1.00 69.24  ?  417  HIS D O   1 
ATOM   9222  C CB  . HIS D  1  417 ? 25.561  7.737   7.831   1.00 68.83  ?  417  HIS D CB  1 
ATOM   9223  C CG  . HIS D  1  417 ? 25.115  8.902   8.658   1.00 69.09  ?  417  HIS D CG  1 
ATOM   9224  N ND1 . HIS D  1  417 ? 25.083  8.866   10.036  1.00 68.57  ?  417  HIS D ND1 1 
ATOM   9225  C CD2 . HIS D  1  417 ? 24.683  10.135  8.302   1.00 69.81  ?  417  HIS D CD2 1 
ATOM   9226  C CE1 . HIS D  1  417 ? 24.652  10.028  10.493  1.00 69.08  ?  417  HIS D CE1 1 
ATOM   9227  N NE2 . HIS D  1  417 ? 24.401  10.816  9.462   1.00 69.73  ?  417  HIS D NE2 1 
ATOM   9228  N N   . PHE D  1  418 ? 24.335  5.630   5.024   1.00 65.87  ?  418  PHE D N   1 
ATOM   9229  C CA  . PHE D  1  418 ? 24.826  4.595   4.130   1.00 66.23  ?  418  PHE D CA  1 
ATOM   9230  C C   . PHE D  1  418 ? 25.629  5.213   2.985   1.00 68.30  ?  418  PHE D C   1 
ATOM   9231  O O   . PHE D  1  418 ? 25.479  6.391   2.647   1.00 69.26  ?  418  PHE D O   1 
ATOM   9232  C CB  . PHE D  1  418 ? 23.665  3.763   3.585   1.00 65.60  ?  418  PHE D CB  1 
ATOM   9233  C CG  . PHE D  1  418 ? 23.026  2.868   4.614   1.00 63.18  ?  418  PHE D CG  1 
ATOM   9234  C CD1 . PHE D  1  418 ? 23.768  1.902   5.275   1.00 62.22  ?  418  PHE D CD1 1 
ATOM   9235  C CD2 . PHE D  1  418 ? 21.679  2.992   4.922   1.00 61.83  ?  418  PHE D CD2 1 
ATOM   9236  C CE1 . PHE D  1  418 ? 23.179  1.078   6.223   1.00 60.06  ?  418  PHE D CE1 1 
ATOM   9237  C CE2 . PHE D  1  418 ? 21.086  2.168   5.869   1.00 59.53  ?  418  PHE D CE2 1 
ATOM   9238  C CZ  . PHE D  1  418 ? 21.840  1.211   6.519   1.00 58.70  ?  418  PHE D CZ  1 
ATOM   9239  N N   . GLU D  1  419 ? 26.506  4.399   2.398   1.00 69.99  ?  419  GLU D N   1 
ATOM   9240  C CA  . GLU D  1  419 ? 27.372  4.800   1.296   1.00 71.86  ?  419  GLU D CA  1 
ATOM   9241  C C   . GLU D  1  419 ? 27.329  3.742   0.201   1.00 73.06  ?  419  GLU D C   1 
ATOM   9242  O O   . GLU D  1  419 ? 26.689  2.695   0.333   1.00 72.44  ?  419  GLU D O   1 
ATOM   9243  C CB  . GLU D  1  419 ? 28.824  4.990   1.752   1.00 71.88  ?  419  GLU D CB  1 
ATOM   9244  C CG  . GLU D  1  419 ? 29.035  5.974   2.883   1.00 71.07  ?  419  GLU D CG  1 
ATOM   9245  C CD  . GLU D  1  419 ? 30.442  5.884   3.452   1.00 70.98  ?  419  GLU D CD  1 
ATOM   9246  O OE1 . GLU D  1  419 ? 31.358  6.544   2.906   1.00 72.00  ?  419  GLU D OE1 1 
ATOM   9247  O OE2 . GLU D  1  419 ? 30.634  5.139   4.440   1.00 69.85  -1 419  GLU D OE2 1 
ATOM   9248  N N   . GLY D  1  420 ? 28.037  4.022   -0.888  1.00 67.16  ?  420  GLY D N   1 
ATOM   9249  C CA  . GLY D  1  420 ? 28.315  3.028   -1.893  1.00 68.70  ?  420  GLY D CA  1 
ATOM   9250  C C   . GLY D  1  420 ? 27.183  2.800   -2.868  1.00 69.95  ?  420  GLY D C   1 
ATOM   9251  O O   . GLY D  1  420 ? 26.149  3.471   -2.831  1.00 69.53  ?  420  GLY D O   1 
ATOM   9252  N N   . PRO D  1  421 ? 27.372  1.844   -3.774  1.00 63.97  ?  421  PRO D N   1 
ATOM   9253  C CA  . PRO D  1  421 ? 26.358  1.584   -4.799  1.00 65.42  ?  421  PRO D CA  1 
ATOM   9254  C C   . PRO D  1  421 ? 25.291  0.608   -4.338  1.00 65.06  ?  421  PRO D C   1 
ATOM   9255  O O   . PRO D  1  421 ? 25.328  0.103   -3.210  1.00 63.33  ?  421  PRO D O   1 
ATOM   9256  C CB  . PRO D  1  421 ? 27.184  0.999   -5.947  1.00 67.42  ?  421  PRO D CB  1 
ATOM   9257  C CG  . PRO D  1  421 ? 28.258  0.248   -5.245  1.00 66.95  ?  421  PRO D CG  1 
ATOM   9258  C CD  . PRO D  1  421 ? 28.580  1.028   -3.985  1.00 64.75  ?  421  PRO D CD  1 
ATOM   9259  N N   . VAL D  1  422 ? 24.334  0.339   -5.218  1.00 62.77  ?  422  VAL D N   1 
ATOM   9260  C CA  . VAL D  1  422 ? 23.285  -0.641  -4.965  1.00 62.90  ?  422  VAL D CA  1 
ATOM   9261  C C   . VAL D  1  422 ? 23.803  -2.025  -5.337  1.00 64.55  ?  422  VAL D C   1 
ATOM   9262  O O   . VAL D  1  422 ? 24.201  -2.242  -6.490  1.00 66.40  ?  422  VAL D O   1 
ATOM   9263  C CB  . VAL D  1  422 ? 22.014  -0.295  -5.752  1.00 63.49  ?  422  VAL D CB  1 
ATOM   9264  C CG1 . VAL D  1  422 ? 20.840  -1.095  -5.233  1.00 63.03  ?  422  VAL D CG1 1 
ATOM   9265  C CG2 . VAL D  1  422 ? 21.739  1.193   -5.657  1.00 62.09  ?  422  VAL D CG2 1 
ATOM   9266  N N   . PRO D  1  423 ? 23.802  -2.986  -4.411  1.00 68.58  ?  423  PRO D N   1 
ATOM   9267  C CA  . PRO D  1  423 ? 24.316  -4.326  -4.722  1.00 70.05  ?  423  PRO D CA  1 
ATOM   9268  C C   . PRO D  1  423 ? 23.532  -4.997  -5.842  1.00 72.55  ?  423  PRO D C   1 
ATOM   9269  O O   . PRO D  1  423 ? 22.367  -4.687  -6.100  1.00 72.73  ?  423  PRO D O   1 
ATOM   9270  C CB  . PRO D  1  423 ? 24.149  -5.086  -3.401  1.00 67.47  ?  423  PRO D CB  1 
ATOM   9271  C CG  . PRO D  1  423 ? 24.112  -4.019  -2.358  1.00 64.16  ?  423  PRO D CG  1 
ATOM   9272  C CD  . PRO D  1  423 ? 23.404  -2.865  -3.000  1.00 65.17  ?  423  PRO D CD  1 
ATOM   9273  N N   . LYS D  1  424 ? 24.201  -5.935  -6.520  1.00 71.19  ?  424  LYS D N   1 
ATOM   9274  C CA  . LYS D  1  424 ? 23.587  -6.585  -7.675  1.00 73.24  ?  424  LYS D CA  1 
ATOM   9275  C C   . LYS D  1  424 ? 22.364  -7.401  -7.281  1.00 73.43  ?  424  LYS D C   1 
ATOM   9276  O O   . LYS D  1  424 ? 21.396  -7.474  -8.050  1.00 74.51  ?  424  LYS D O   1 
ATOM   9277  C CB  . LYS D  1  424 ? 24.608  -7.468  -8.389  1.00 74.48  ?  424  LYS D CB  1 
ATOM   9278  C CG  . LYS D  1  424 ? 25.651  -6.679  -9.152  1.00 74.77  ?  424  LYS D CG  1 
ATOM   9279  C CD  . LYS D  1  424 ? 26.449  -7.568  -10.097 1.00 76.11  ?  424  LYS D CD  1 
ATOM   9280  C CE  . LYS D  1  424 ? 27.746  -8.058  -9.455  1.00 75.28  ?  424  LYS D CE  1 
ATOM   9281  N NZ  . LYS D  1  424 ? 28.518  -8.974  -10.352 1.00 76.36  ?  424  LYS D NZ  1 
ATOM   9282  N N   . SER D  1  425 ? 22.383  -8.012  -6.093  1.00 73.44  ?  425  SER D N   1 
ATOM   9283  C CA  . SER D  1  425 ? 21.240  -8.800  -5.641  1.00 73.53  ?  425  SER D CA  1 
ATOM   9284  C C   . SER D  1  425 ? 19.983  -7.949  -5.536  1.00 72.90  ?  425  SER D C   1 
ATOM   9285  O O   . SER D  1  425 ? 18.874  -8.451  -5.749  1.00 73.54  ?  425  SER D O   1 
ATOM   9286  C CB  . SER D  1  425 ? 21.548  -9.447  -4.294  1.00 70.98  ?  425  SER D CB  1 
ATOM   9287  O OG  . SER D  1  425 ? 22.931  -9.727  -4.192  1.00 70.15  ?  425  SER D OG  1 
ATOM   9288  N N   . LEU D  1  426 ? 20.136  -6.668  -5.196  1.00 71.27  ?  426  LEU D N   1 
ATOM   9289  C CA  . LEU D  1  426 ? 19.002  -5.753  -5.163  1.00 70.12  ?  426  LEU D CA  1 
ATOM   9290  C C   . LEU D  1  426 ? 18.585  -5.319  -6.562  1.00 71.61  ?  426  LEU D C   1 
ATOM   9291  O O   . LEU D  1  426 ? 17.395  -5.079  -6.802  1.00 71.39  ?  426  LEU D O   1 
ATOM   9292  C CB  . LEU D  1  426 ? 19.343  -4.529  -4.311  1.00 67.16  ?  426  LEU D CB  1 
ATOM   9293  C CG  . LEU D  1  426 ? 18.184  -3.617  -3.910  1.00 64.22  ?  426  LEU D CG  1 
ATOM   9294  C CD1 . LEU D  1  426 ? 17.002  -4.423  -3.369  1.00 62.57  ?  426  LEU D CD1 1 
ATOM   9295  C CD2 . LEU D  1  426 ? 18.658  -2.613  -2.874  1.00 60.17  ?  426  LEU D CD2 1 
ATOM   9296  N N   . ARG D  1  427 ? 19.546  -5.202  -7.485  1.00 68.50  ?  427  ARG D N   1 
ATOM   9297  C CA  . ARG D  1  427 ? 19.220  -4.815  -8.853  1.00 69.93  ?  427  ARG D CA  1 
ATOM   9298  C C   . ARG D  1  427 ? 18.370  -5.876  -9.542  1.00 71.87  ?  427  ARG D C   1 
ATOM   9299  O O   . ARG D  1  427 ? 17.433  -5.547  -10.278 1.00 72.50  ?  427  ARG D O   1 
ATOM   9300  C CB  . ARG D  1  427 ? 20.503  -4.558  -9.638  1.00 70.86  ?  427  ARG D CB  1 
ATOM   9301  C CG  . ARG D  1  427 ? 20.302  -4.451  -11.140 1.00 72.75  ?  427  ARG D CG  1 
ATOM   9302  C CD  . ARG D  1  427 ? 21.626  -4.361  -11.869 1.00 73.64  ?  427  ARG D CD  1 
ATOM   9303  N NE  . ARG D  1  427 ? 22.069  -5.673  -12.323 1.00 75.24  ?  427  ARG D NE  1 
ATOM   9304  C CZ  . ARG D  1  427 ? 23.339  -6.018  -12.483 1.00 75.45  ?  427  ARG D CZ  1 
ATOM   9305  N NH1 . ARG D  1  427 ? 24.322  -5.161  -12.250 1.00 74.48  ?  427  ARG D NH1 1 
ATOM   9306  N NH2 . ARG D  1  427 ? 23.631  -7.251  -12.892 1.00 76.47  ?  427  ARG D NH2 1 
ATOM   9307  N N   . ASP D  1  428 ? 18.670  -7.150  -9.306  1.00 70.97  ?  428  ASP D N   1 
ATOM   9308  C CA  . ASP D  1  428 ? 17.944  -8.242  -9.938  1.00 72.74  ?  428  ASP D CA  1 
ATOM   9309  C C   . ASP D  1  428 ? 16.781  -8.753  -9.098  1.00 72.08  ?  428  ASP D C   1 
ATOM   9310  O O   . ASP D  1  428 ? 16.037  -9.618  -9.571  1.00 73.36  ?  428  ASP D O   1 
ATOM   9311  C CB  . ASP D  1  428 ? 18.902  -9.392  -10.254 1.00 73.64  ?  428  ASP D CB  1 
ATOM   9312  C CG  . ASP D  1  428 ? 20.203  -8.912  -10.878 1.00 73.89  ?  428  ASP D CG  1 
ATOM   9313  O OD1 . ASP D  1  428 ? 20.263  -7.747  -11.327 1.00 73.83  ?  428  ASP D OD1 1 
ATOM   9314  O OD2 . ASP D  1  428 ? 21.171  -9.700  -10.919 1.00 74.04  -1 428  ASP D OD2 1 
ATOM   9315  N N   . CYS D  1  429 ? 16.607  -8.241  -7.875  1.00 69.04  ?  429  CYS D N   1 
ATOM   9316  C CA  . CYS D  1  429 ? 15.540  -8.676  -6.973  1.00 67.99  ?  429  CYS D CA  1 
ATOM   9317  C C   . CYS D  1  429 ? 14.194  -8.183  -7.490  1.00 68.18  ?  429  CYS D C   1 
ATOM   9318  O O   . CYS D  1  429 ? 13.909  -6.985  -7.444  1.00 66.62  ?  429  CYS D O   1 
ATOM   9319  C CB  . CYS D  1  429 ? 15.811  -8.139  -5.569  1.00 65.23  ?  429  CYS D CB  1 
ATOM   9320  S SG  . CYS D  1  429 ? 14.637  -8.619  -4.272  1.00 62.84  ?  429  CYS D SG  1 
ATOM   9321  N N   . LYS D  1  430 ? 13.342  -9.100  -7.932  1.00 64.14  ?  430  LYS D N   1 
ATOM   9322  C CA  . LYS D  1  430 ? 12.102  -8.733  -8.605  1.00 64.53  ?  430  LYS D CA  1 
ATOM   9323  C C   . LYS D  1  430 ? 10.894  -8.666  -7.674  1.00 62.44  ?  430  LYS D C   1 
ATOM   9324  O O   . LYS D  1  430 ? 9.797   -8.318  -8.128  1.00 62.03  ?  430  LYS D O   1 
ATOM   9325  C CB  . LYS D  1  430 ? 11.811  -9.717  -9.741  1.00 66.63  ?  430  LYS D CB  1 
ATOM   9326  C CG  . LYS D  1  430 ? 12.744  -9.585  -10.915 1.00 67.78  ?  430  LYS D CG  1 
ATOM   9327  C CD  . LYS D  1  430 ? 12.567  -10.737 -11.882 1.00 68.74  ?  430  LYS D CD  1 
ATOM   9328  C CE  . LYS D  1  430 ? 13.339  -10.485 -13.167 1.00 69.50  ?  430  LYS D CE  1 
ATOM   9329  N NZ  . LYS D  1  430 ? 13.471  -9.028  -13.461 1.00 69.08  ?  430  LYS D NZ  1 
ATOM   9330  N N   . SER D  1  431 ? 11.058  -8.987  -6.394  1.00 65.33  ?  431  SER D N   1 
ATOM   9331  C CA  . SER D  1  431 ? 9.943   -9.033  -5.459  1.00 63.12  ?  431  SER D CA  1 
ATOM   9332  C C   . SER D  1  431 ? 9.705   -7.705  -4.745  1.00 59.64  ?  431  SER D C   1 
ATOM   9333  O O   . SER D  1  431 ? 8.892   -7.656  -3.816  1.00 56.62  ?  431  SER D O   1 
ATOM   9334  C CB  . SER D  1  431 ? 10.169  -10.140 -4.425  1.00 62.33  ?  431  SER D CB  1 
ATOM   9335  O OG  . SER D  1  431 ? 11.401  -9.974  -3.745  1.00 60.86  ?  431  SER D OG  1 
ATOM   9336  N N   . LEU D  1  432 ? 10.379  -6.632  -5.158  1.00 63.43  ?  432  LEU D N   1 
ATOM   9337  C CA  . LEU D  1  432 ? 10.281  -5.370  -4.437  1.00 58.74  ?  432  LEU D CA  1 
ATOM   9338  C C   . LEU D  1  432 ? 8.877   -4.785  -4.543  1.00 56.06  ?  432  LEU D C   1 
ATOM   9339  O O   . LEU D  1  432 ? 8.253   -4.814  -5.608  1.00 58.55  ?  432  LEU D O   1 
ATOM   9340  C CB  . LEU D  1  432 ? 11.303  -4.370  -4.978  1.00 59.32  ?  432  LEU D CB  1 
ATOM   9341  C CG  . LEU D  1  432 ? 12.762  -4.802  -4.856  1.00 61.15  ?  432  LEU D CG  1 
ATOM   9342  C CD1 . LEU D  1  432 ? 13.696  -3.631  -5.105  1.00 60.34  ?  432  LEU D CD1 1 
ATOM   9343  C CD2 . LEU D  1  432 ? 13.025  -5.426  -3.494  1.00 58.11  ?  432  LEU D CD2 1 
ATOM   9344  N N   . ILE D  1  433 ? 8.387   -4.251  -3.421  1.00 59.18  ?  433  ILE D N   1 
ATOM   9345  C CA  . ILE D  1  433 ? 7.083   -3.598  -3.352  1.00 55.98  ?  433  ILE D CA  1 
ATOM   9346  C C   . ILE D  1  433 ? 7.259   -2.157  -2.885  1.00 52.18  ?  433  ILE D C   1 
ATOM   9347  O O   . ILE D  1  433 ? 6.873   -1.215  -3.589  1.00 51.96  ?  433  ILE D O   1 
ATOM   9348  C CB  . ILE D  1  433 ? 6.127   -4.366  -2.422  1.00 53.73  ?  433  ILE D CB  1 
ATOM   9349  C CG1 . ILE D  1  433 ? 5.971   -5.809  -2.904  1.00 58.26  ?  433  ILE D CG1 1 
ATOM   9350  C CG2 . ILE D  1  433 ? 4.776   -3.669  -2.352  1.00 50.51  ?  433  ILE D CG2 1 
ATOM   9351  C CD1 . ILE D  1  433 ? 4.901   -6.577  -2.180  1.00 56.62  ?  433  ILE D CD1 1 
ATOM   9352  N N   . ARG D  1  434 ? 7.830   -1.978  -1.692  1.00 57.65  ?  434  ARG D N   1 
ATOM   9353  C CA  . ARG D  1  434 ? 8.188   -0.664  -1.170  1.00 55.02  ?  434  ARG D CA  1 
ATOM   9354  C C   . ARG D  1  434 ? 9.694   -0.586  -0.976  1.00 56.17  ?  434  ARG D C   1 
ATOM   9355  O O   . ARG D  1  434 ? 10.281  -1.436  -0.299  1.00 56.05  ?  434  ARG D O   1 
ATOM   9356  C CB  . ARG D  1  434 ? 7.483   -0.369  0.155   1.00 50.93  ?  434  ARG D CB  1 
ATOM   9357  C CG  . ARG D  1  434 ? 6.242   0.487   0.012   1.00 49.16  ?  434  ARG D CG  1 
ATOM   9358  C CD  . ARG D  1  434 ? 5.648   0.821   1.361   1.00 45.78  ?  434  ARG D CD  1 
ATOM   9359  N NE  . ARG D  1  434 ? 6.070   2.120   1.867   1.00 44.87  ?  434  ARG D NE  1 
ATOM   9360  C CZ  . ARG D  1  434 ? 5.454   3.261   1.584   1.00 44.38  ?  434  ARG D CZ  1 
ATOM   9361  N NH1 . ARG D  1  434 ? 4.424   3.302   0.752   1.00 44.45  ?  434  ARG D NH1 1 
ATOM   9362  N NH2 . ARG D  1  434 ? 5.878   4.387   2.151   1.00 44.08  ?  434  ARG D NH2 1 
ATOM   9363  N N   . VAL D  1  435 ? 10.307  0.447   -1.552  1.00 52.02  ?  435  VAL D N   1 
ATOM   9364  C CA  . VAL D  1  435 ? 11.738  0.699   -1.434  1.00 53.21  ?  435  VAL D CA  1 
ATOM   9365  C C   . VAL D  1  435 ? 11.917  2.142   -0.980  1.00 51.47  ?  435  VAL D C   1 
ATOM   9366  O O   . VAL D  1  435 ? 11.466  3.073   -1.660  1.00 51.72  ?  435  VAL D O   1 
ATOM   9367  C CB  . VAL D  1  435 ? 12.478  0.448   -2.758  1.00 57.56  ?  435  VAL D CB  1 
ATOM   9368  C CG1 . VAL D  1  435 ? 13.967  0.700   -2.597  1.00 58.71  ?  435  VAL D CG1 1 
ATOM   9369  C CG2 . VAL D  1  435 ? 12.227  -0.959  -3.243  1.00 60.31  ?  435  VAL D CG2 1 
ATOM   9370  N N   . ARG D  1  436 ? 12.564  2.328   0.168   1.00 58.34  ?  436  ARG D N   1 
ATOM   9371  C CA  . ARG D  1  436 ? 12.798  3.653   0.732   1.00 57.56  ?  436  ARG D CA  1 
ATOM   9372  C C   . ARG D  1  436 ? 14.291  3.822   0.986   1.00 59.22  ?  436  ARG D C   1 
ATOM   9373  O O   . ARG D  1  436 ? 14.828  3.246   1.940   1.00 58.54  ?  436  ARG D O   1 
ATOM   9374  C CB  . ARG D  1  436 ? 12.003  3.838   2.022   1.00 54.79  ?  436  ARG D CB  1 
ATOM   9375  C CG  . ARG D  1  436 ? 10.498  3.741   1.863   1.00 53.03  ?  436  ARG D CG  1 
ATOM   9376  C CD  . ARG D  1  436 ? 9.797   4.704   2.797   1.00 51.30  ?  436  ARG D CD  1 
ATOM   9377  N NE  . ARG D  1  436 ? 10.110  6.085   2.456   1.00 52.53  ?  436  ARG D NE  1 
ATOM   9378  C CZ  . ARG D  1  436 ? 9.294   7.105   2.673   1.00 51.72  ?  436  ARG D CZ  1 
ATOM   9379  N NH1 . ARG D  1  436 ? 8.121   6.933   3.261   1.00 49.71  ?  436  ARG D NH1 1 
ATOM   9380  N NH2 . ARG D  1  436 ? 9.657   8.325   2.279   1.00 53.01  ?  436  ARG D NH2 1 
ATOM   9381  N N   . PHE D  1  437 ? 14.951  4.627   0.147   1.00 53.08  ?  437  PHE D N   1 
ATOM   9382  C CA  . PHE D  1  437 ? 16.367  4.950   0.285   1.00 55.04  ?  437  PHE D CA  1 
ATOM   9383  C C   . PHE D  1  437 ? 16.603  6.373   0.773   1.00 55.38  ?  437  PHE D C   1 
ATOM   9384  O O   . PHE D  1  437 ? 17.760  6.779   0.908   1.00 57.35  ?  437  PHE D O   1 
ATOM   9385  C CB  . PHE D  1  437 ? 17.094  4.761   -1.056  1.00 57.99  ?  437  PHE D CB  1 
ATOM   9386  C CG  . PHE D  1  437 ? 17.578  3.361   -1.306  1.00 59.18  ?  437  PHE D CG  1 
ATOM   9387  C CD1 . PHE D  1  437 ? 16.829  2.269   -0.906  1.00 57.59  ?  437  PHE D CD1 1 
ATOM   9388  C CD2 . PHE D  1  437 ? 18.778  3.137   -1.960  1.00 62.12  ?  437  PHE D CD2 1 
ATOM   9389  C CE1 . PHE D  1  437 ? 17.273  0.982   -1.142  1.00 59.09  ?  437  PHE D CE1 1 
ATOM   9390  C CE2 . PHE D  1  437 ? 19.226  1.851   -2.201  1.00 63.58  ?  437  PHE D CE2 1 
ATOM   9391  C CZ  . PHE D  1  437 ? 18.473  0.774   -1.792  1.00 62.15  ?  437  PHE D CZ  1 
ATOM   9392  N N   . LYS D  1  438 ? 15.542  7.123   1.063   1.00 57.17  ?  438  LYS D N   1 
ATOM   9393  C CA  . LYS D  1  438 ? 15.644  8.561   1.282   1.00 57.86  ?  438  LYS D CA  1 
ATOM   9394  C C   . LYS D  1  438 ? 16.626  8.901   2.399   1.00 59.34  ?  438  LYS D C   1 
ATOM   9395  O O   . LYS D  1  438 ? 16.643  8.257   3.452   1.00 58.77  ?  438  LYS D O   1 
ATOM   9396  C CB  . LYS D  1  438 ? 14.264  9.134   1.616   1.00 55.69  ?  438  LYS D CB  1 
ATOM   9397  C CG  . LYS D  1  438 ? 14.147  10.639  1.434   1.00 56.12  ?  438  LYS D CG  1 
ATOM   9398  C CD  . LYS D  1  438 ? 13.101  11.223  2.367   1.00 54.47  ?  438  LYS D CD  1 
ATOM   9399  C CE  . LYS D  1  438 ? 12.540  12.536  1.843   1.00 54.10  ?  438  LYS D CE  1 
ATOM   9400  N NZ  . LYS D  1  438 ? 11.705  12.342  0.627   1.00 53.12  ?  438  LYS D NZ  1 
ATOM   9401  N N   . GLY D  1  439 ? 17.442  9.929   2.163   1.00 59.38  ?  439  GLY D N   1 
ATOM   9402  C CA  . GLY D  1  439 ? 18.340  10.451  3.177   1.00 60.74  ?  439  GLY D CA  1 
ATOM   9403  C C   . GLY D  1  439 ? 19.572  9.613   3.452   1.00 62.16  ?  439  GLY D C   1 
ATOM   9404  O O   . GLY D  1  439 ? 19.785  9.150   4.576   1.00 61.71  ?  439  GLY D O   1 
ATOM   9405  N N   . ASN D  1  440 ? 20.403  9.431   2.430   1.00 63.15  ?  440  ASN D N   1 
ATOM   9406  C CA  . ASN D  1  440 ? 21.639  8.673   2.548   1.00 63.60  ?  440  ASN D CA  1 
ATOM   9407  C C   . ASN D  1  440 ? 22.650  9.268   1.574   1.00 64.75  ?  440  ASN D C   1 
ATOM   9408  O O   . ASN D  1  440 ? 22.457  10.368  1.048   1.00 64.95  ?  440  ASN D O   1 
ATOM   9409  C CB  . ASN D  1  440 ? 21.386  7.181   2.295   1.00 63.17  ?  440  ASN D CB  1 
ATOM   9410  C CG  . ASN D  1  440 ? 20.783  6.478   3.500   1.00 60.86  ?  440  ASN D CG  1 
ATOM   9411  O OD1 . ASN D  1  440 ? 21.482  6.164   4.463   1.00 59.99  ?  440  ASN D OD1 1 
ATOM   9412  N ND2 . ASN D  1  440 ? 19.479  6.229   3.449   1.00 59.22  ?  440  ASN D ND2 1 
ATOM   9413  N N   . SER D  1  441 ? 23.739  8.542   1.342   1.00 63.27  ?  441  SER D N   1 
ATOM   9414  C CA  . SER D  1  441 ? 24.787  8.951   0.416   1.00 64.40  ?  441  SER D CA  1 
ATOM   9415  C C   . SER D  1  441 ? 25.037  7.874   -0.630  1.00 65.35  ?  441  SER D C   1 
ATOM   9416  O O   . SER D  1  441 ? 26.173  7.632   -1.044  1.00 66.07  ?  441  SER D O   1 
ATOM   9417  C CB  . SER D  1  441 ? 26.071  9.287   1.165   1.00 64.24  ?  441  SER D CB  1 
ATOM   9418  O OG  . SER D  1  441 ? 25.889  10.450  1.944   1.00 63.85  ?  441  SER D OG  1 
ATOM   9419  N N   . PHE D  1  442 ? 23.966  7.213   -1.067  1.00 65.74  ?  442  PHE D N   1 
ATOM   9420  C CA  . PHE D  1  442 ? 24.079  6.197   -2.103  1.00 66.95  ?  442  PHE D CA  1 
ATOM   9421  C C   . PHE D  1  442 ? 24.537  6.837   -3.408  1.00 68.29  ?  442  PHE D C   1 
ATOM   9422  O O   . PHE D  1  442 ? 24.229  7.995   -3.699  1.00 68.05  ?  442  PHE D O   1 
ATOM   9423  C CB  . PHE D  1  442 ? 22.738  5.489   -2.304  1.00 66.73  ?  442  PHE D CB  1 
ATOM   9424  C CG  . PHE D  1  442 ? 22.387  4.522   -1.207  1.00 65.25  ?  442  PHE D CG  1 
ATOM   9425  C CD1 . PHE D  1  442 ? 23.084  3.335   -1.061  1.00 65.12  ?  442  PHE D CD1 1 
ATOM   9426  C CD2 . PHE D  1  442 ? 21.349  4.797   -0.328  1.00 62.97  ?  442  PHE D CD2 1 
ATOM   9427  C CE1 . PHE D  1  442 ? 22.758  2.440   -0.055  1.00 62.75  ?  442  PHE D CE1 1 
ATOM   9428  C CE2 . PHE D  1  442 ? 21.019  3.907   0.679   1.00 60.48  ?  442  PHE D CE2 1 
ATOM   9429  C CZ  . PHE D  1  442 ? 21.726  2.727   0.815   1.00 60.37  ?  442  PHE D CZ  1 
ATOM   9430  N N   . SER D  1  443 ? 25.277  6.068   -4.205  1.00 65.61  ?  443  SER D N   1 
ATOM   9431  C CA  . SER D  1  443 ? 25.981  6.612   -5.355  1.00 65.75  ?  443  SER D CA  1 
ATOM   9432  C C   . SER D  1  443 ? 25.984  5.599   -6.490  1.00 66.08  ?  443  SER D C   1 
ATOM   9433  O O   . SER D  1  443 ? 25.562  4.450   -6.333  1.00 66.18  ?  443  SER D O   1 
ATOM   9434  C CB  . SER D  1  443 ? 27.415  7.001   -4.982  1.00 68.12  ?  443  SER D CB  1 
ATOM   9435  O OG  . SER D  1  443 ? 28.045  5.950   -4.268  1.00 71.15  ?  443  SER D OG  1 
ATOM   9436  N N   . GLY D  1  444 ? 26.471  6.042   -7.641  1.00 67.76  ?  444  GLY D N   1 
ATOM   9437  C CA  . GLY D  1  444 ? 26.556  5.221   -8.830  1.00 68.39  ?  444  GLY D CA  1 
ATOM   9438  C C   . GLY D  1  444 ? 25.665  5.741   -9.941  1.00 68.25  ?  444  GLY D C   1 
ATOM   9439  O O   . GLY D  1  444 ? 25.027  6.787   -9.832  1.00 67.57  ?  444  GLY D O   1 
ATOM   9440  N N   . ASP D  1  445 ? 25.648  4.986   -11.037 1.00 71.46  ?  445  ASP D N   1 
ATOM   9441  C CA  . ASP D  1  445 ? 24.789  5.313   -12.166 1.00 71.75  ?  445  ASP D CA  1 
ATOM   9442  C C   . ASP D  1  445 ? 23.387  4.775   -11.903 1.00 71.33  ?  445  ASP D C   1 
ATOM   9443  O O   . ASP D  1  445 ? 23.211  3.590   -11.599 1.00 71.35  ?  445  ASP D O   1 
ATOM   9444  C CB  . ASP D  1  445 ? 25.358  4.726   -13.459 1.00 72.91  ?  445  ASP D CB  1 
ATOM   9445  C CG  . ASP D  1  445 ? 24.620  5.205   -14.704 1.00 73.51  ?  445  ASP D CG  1 
ATOM   9446  O OD1 . ASP D  1  445 ? 23.383  5.368   -14.668 1.00 73.09  ?  445  ASP D OD1 1 
ATOM   9447  O OD2 . ASP D  1  445 ? 25.287  5.417   -15.736 1.00 74.48  -1 445  ASP D OD2 1 
ATOM   9448  N N   . ILE D  1  446 ? 22.386  5.645   -12.043 1.00 70.79  ?  446  ILE D N   1 
ATOM   9449  C CA  . ILE D  1  446 ? 21.025  5.243   -11.715 1.00 70.28  ?  446  ILE D CA  1 
ATOM   9450  C C   . ILE D  1  446 ? 20.520  4.189   -12.692 1.00 71.08  ?  446  ILE D C   1 
ATOM   9451  O O   . ILE D  1  446 ? 19.748  3.301   -12.310 1.00 70.52  ?  446  ILE D O   1 
ATOM   9452  C CB  . ILE D  1  446 ? 20.103  6.479   -11.669 1.00 69.69  ?  446  ILE D CB  1 
ATOM   9453  C CG1 . ILE D  1  446 ? 18.668  6.074   -11.340 1.00 69.08  ?  446  ILE D CG1 1 
ATOM   9454  C CG2 . ILE D  1  446 ? 20.155  7.250   -12.977 1.00 70.79  ?  446  ILE D CG2 1 
ATOM   9455  C CD1 . ILE D  1  446 ? 18.423  5.902   -9.868  1.00 67.69  ?  446  ILE D CD1 1 
ATOM   9456  N N   . SER D  1  447 ? 20.959  4.239   -13.950 1.00 71.95  ?  447  SER D N   1 
ATOM   9457  C CA  . SER D  1  447 ? 20.514  3.253   -14.926 1.00 72.44  ?  447  SER D CA  1 
ATOM   9458  C C   . SER D  1  447 ? 21.283  1.943   -14.831 1.00 72.56  ?  447  SER D C   1 
ATOM   9459  O O   . SER D  1  447 ? 20.901  0.970   -15.490 1.00 72.71  ?  447  SER D O   1 
ATOM   9460  C CB  . SER D  1  447 ? 20.620  3.817   -16.341 1.00 73.55  ?  447  SER D CB  1 
ATOM   9461  O OG  . SER D  1  447 ? 21.972  3.958   -16.719 1.00 74.22  ?  447  SER D OG  1 
ATOM   9462  N N   . GLU D  1  448 ? 22.370  1.908   -14.059 1.00 78.09  ?  448  GLU D N   1 
ATOM   9463  C CA  . GLU D  1  448 ? 23.082  0.672   -13.762 1.00 78.21  ?  448  GLU D CA  1 
ATOM   9464  C C   . GLU D  1  448 ? 22.635  0.054   -12.446 1.00 77.35  ?  448  GLU D C   1 
ATOM   9465  O O   . GLU D  1  448 ? 22.705  -1.170  -12.283 1.00 77.40  ?  448  GLU D O   1 
ATOM   9466  C CB  . GLU D  1  448 ? 24.591  0.931   -13.701 1.00 78.69  ?  448  GLU D CB  1 
ATOM   9467  C CG  . GLU D  1  448 ? 25.334  0.738   -15.016 1.00 79.70  ?  448  GLU D CG  1 
ATOM   9468  C CD  . GLU D  1  448 ? 26.759  1.271   -14.955 1.00 79.99  ?  448  GLU D CD  1 
ATOM   9469  O OE1 . GLU D  1  448 ? 27.262  1.456   -13.826 1.00 79.52  ?  448  GLU D OE1 1 
ATOM   9470  O OE2 . GLU D  1  448 ? 27.378  1.501   -16.024 1.00 80.68  -1 448  GLU D OE2 1 
ATOM   9471  N N   . ALA D  1  449 ? 22.181  0.884   -11.506 1.00 71.87  ?  449  ALA D N   1 
ATOM   9472  C CA  . ALA D  1  449 ? 21.910  0.409   -10.155 1.00 71.13  ?  449  ALA D CA  1 
ATOM   9473  C C   . ALA D  1  449 ? 20.650  -0.445  -10.091 1.00 70.61  ?  449  ALA D C   1 
ATOM   9474  O O   . ALA D  1  449 ? 20.617  -1.451  -9.374  1.00 70.48  ?  449  ALA D O   1 
ATOM   9475  C CB  . ALA D  1  449 ? 21.793  1.599   -9.203  1.00 70.41  ?  449  ALA D CB  1 
ATOM   9476  N N   . PHE D  1  450 ? 19.607  -0.068  -10.825 1.00 64.57  ?  450  PHE D N   1 
ATOM   9477  C CA  . PHE D  1  450 ? 18.291  -0.672  -10.672 1.00 63.80  ?  450  PHE D CA  1 
ATOM   9478  C C   . PHE D  1  450 ? 17.874  -1.382  -11.951 1.00 64.19  ?  450  PHE D C   1 
ATOM   9479  O O   . PHE D  1  450 ? 18.067  -0.860  -13.055 1.00 64.82  ?  450  PHE D O   1 
ATOM   9480  C CB  . PHE D  1  450 ? 17.249  0.385   -10.293 1.00 62.88  ?  450  PHE D CB  1 
ATOM   9481  C CG  . PHE D  1  450 ? 17.526  1.059   -8.982  1.00 62.42  ?  450  PHE D CG  1 
ATOM   9482  C CD1 . PHE D  1  450 ? 17.312  0.395   -7.786  1.00 61.99  ?  450  PHE D CD1 1 
ATOM   9483  C CD2 . PHE D  1  450 ? 18.024  2.350   -8.944  1.00 62.52  ?  450  PHE D CD2 1 
ATOM   9484  C CE1 . PHE D  1  450 ? 17.574  1.012   -6.574  1.00 61.73  ?  450  PHE D CE1 1 
ATOM   9485  C CE2 . PHE D  1  450 ? 18.289  2.972   -7.736  1.00 62.01  ?  450  PHE D CE2 1 
ATOM   9486  C CZ  . PHE D  1  450 ? 18.063  2.300   -6.549  1.00 61.69  ?  450  PHE D CZ  1 
ATOM   9487  N N   . GLY D  1  451 ? 17.306  -2.576  -11.791 1.00 59.47  ?  451  GLY D N   1 
ATOM   9488  C CA  . GLY D  1  451 ? 16.829  -3.359  -12.914 1.00 60.00  ?  451  GLY D CA  1 
ATOM   9489  C C   . GLY D  1  451 ? 15.363  -3.131  -13.220 1.00 59.14  ?  451  GLY D C   1 
ATOM   9490  O O   . GLY D  1  451 ? 14.928  -1.987  -13.378 1.00 58.67  ?  451  GLY D O   1 
ATOM   9491  N N   . VAL D  1  452 ? 14.588  -4.211  -13.294 1.00 60.62  ?  452  VAL D N   1 
ATOM   9492  C CA  . VAL D  1  452 ? 13.155  -4.141  -13.548 1.00 60.12  ?  452  VAL D CA  1 
ATOM   9493  C C   . VAL D  1  452 ? 12.426  -4.823  -12.401 1.00 59.43  ?  452  VAL D C   1 
ATOM   9494  O O   . VAL D  1  452 ? 12.873  -5.856  -11.891 1.00 59.79  ?  452  VAL D O   1 
ATOM   9495  C CB  . VAL D  1  452 ? 12.766  -4.785  -14.893 1.00 61.07  ?  452  VAL D CB  1 
ATOM   9496  C CG1 . VAL D  1  452 ? 13.199  -3.901  -16.046 1.00 61.62  ?  452  VAL D CG1 1 
ATOM   9497  C CG2 . VAL D  1  452 ? 13.378  -6.164  -15.007 1.00 61.79  ?  452  VAL D CG2 1 
ATOM   9498  N N   . TYR D  1  453 ? 11.300  -4.238  -12.001 1.00 59.90  ?  453  TYR D N   1 
ATOM   9499  C CA  . TYR D  1  453 ? 10.545  -4.698  -10.838 1.00 59.17  ?  453  TYR D CA  1 
ATOM   9500  C C   . TYR D  1  453 ? 9.059   -4.704  -11.170 1.00 58.71  ?  453  TYR D C   1 
ATOM   9501  O O   . TYR D  1  453 ? 8.383   -3.670  -11.043 1.00 57.63  ?  453  TYR D O   1 
ATOM   9502  C CB  . TYR D  1  453 ? 10.836  -3.817  -9.630  1.00 58.31  ?  453  TYR D CB  1 
ATOM   9503  C CG  . TYR D  1  453 ? 12.303  -3.528  -9.430  1.00 58.89  ?  453  TYR D CG  1 
ATOM   9504  C CD1 . TYR D  1  453 ? 13.137  -4.473  -8.855  1.00 59.59  ?  453  TYR D CD1 1 
ATOM   9505  C CD2 . TYR D  1  453 ? 12.851  -2.316  -9.813  1.00 58.85  ?  453  TYR D CD2 1 
ATOM   9506  C CE1 . TYR D  1  453 ? 14.471  -4.222  -8.660  1.00 60.17  ?  453  TYR D CE1 1 
ATOM   9507  C CE2 . TYR D  1  453 ? 14.189  -2.053  -9.623  1.00 59.54  ?  453  TYR D CE2 1 
ATOM   9508  C CZ  . TYR D  1  453 ? 14.994  -3.013  -9.045  1.00 60.17  ?  453  TYR D CZ  1 
ATOM   9509  O OH  . TYR D  1  453 ? 16.329  -2.768  -8.847  1.00 60.85  ?  453  TYR D OH  1 
ATOM   9510  N N   . PRO D  1  454 ? 8.513   -5.846  -11.592 1.00 60.03  ?  454  PRO D N   1 
ATOM   9511  C CA  . PRO D  1  454 ? 7.103   -5.869  -12.015 1.00 59.77  ?  454  PRO D CA  1 
ATOM   9512  C C   . PRO D  1  454 ? 6.128   -5.565  -10.892 1.00 58.43  ?  454  PRO D C   1 
ATOM   9513  O O   . PRO D  1  454 ? 5.018   -5.087  -11.159 1.00 57.74  ?  454  PRO D O   1 
ATOM   9514  C CB  . PRO D  1  454 ? 6.916   -7.299  -12.547 1.00 61.30  ?  454  PRO D CB  1 
ATOM   9515  C CG  . PRO D  1  454 ? 8.300   -7.895  -12.638 1.00 62.17  ?  454  PRO D CG  1 
ATOM   9516  C CD  . PRO D  1  454 ? 9.122   -7.184  -11.618 1.00 61.16  ?  454  PRO D CD  1 
ATOM   9517  N N   . THR D  1  455 ? 6.500   -5.846  -9.645  1.00 59.21  ?  455  THR D N   1 
ATOM   9518  C CA  . THR D  1  455 ? 5.614   -5.677  -8.502  1.00 58.51  ?  455  THR D CA  1 
ATOM   9519  C C   . THR D  1  455 ? 5.931   -4.428  -7.692  1.00 57.68  ?  455  THR D C   1 
ATOM   9520  O O   . THR D  1  455 ? 5.422   -4.286  -6.575  1.00 57.55  ?  455  THR D O   1 
ATOM   9521  C CB  . THR D  1  455 ? 5.670   -6.907  -7.588  1.00 59.29  ?  455  THR D CB  1 
ATOM   9522  O OG1 . THR D  1  455 ? 7.016   -7.119  -7.142  1.00 59.75  ?  455  THR D OG1 1 
ATOM   9523  C CG2 . THR D  1  455 ? 5.183   -8.143  -8.326  1.00 60.24  ?  455  THR D CG2 1 
ATOM   9524  N N   . LEU D  1  456 ? 6.770   -3.535  -8.212  1.00 56.01  ?  456  LEU D N   1 
ATOM   9525  C CA  . LEU D  1  456 ? 7.135   -2.338  -7.465  1.00 55.49  ?  456  LEU D CA  1 
ATOM   9526  C C   . LEU D  1  456 ? 5.936   -1.407  -7.341  1.00 54.64  ?  456  LEU D C   1 
ATOM   9527  O O   . LEU D  1  456 ? 5.229   -1.152  -8.322  1.00 54.18  ?  456  LEU D O   1 
ATOM   9528  C CB  . LEU D  1  456 ? 8.295   -1.618  -8.150  1.00 55.61  ?  456  LEU D CB  1 
ATOM   9529  C CG  . LEU D  1  456 ? 9.034   -0.577  -7.317  1.00 55.59  ?  456  LEU D CG  1 
ATOM   9530  C CD1 . LEU D  1  456 ? 9.691   -1.246  -6.125  1.00 56.41  ?  456  LEU D CD1 1 
ATOM   9531  C CD2 . LEU D  1  456 ? 10.064  0.151   -8.169  1.00 55.87  ?  456  LEU D CD2 1 
ATOM   9532  N N   . ASN D  1  457 ? 5.720   -0.889  -6.130  1.00 53.02  ?  457  ASN D N   1 
ATOM   9533  C CA  . ASN D  1  457 ? 4.606   -0.002  -5.818  1.00 52.63  ?  457  ASN D CA  1 
ATOM   9534  C C   . ASN D  1  457 ? 5.050   1.414   -5.479  1.00 52.57  ?  457  ASN D C   1 
ATOM   9535  O O   . ASN D  1  457 ? 4.528   2.381   -6.050  1.00 51.95  ?  457  ASN D O   1 
ATOM   9536  C CB  . ASN D  1  457 ? 3.789   -0.581  -4.651  1.00 53.40  ?  457  ASN D CB  1 
ATOM   9537  C CG  . ASN D  1  457 ? 2.693   0.363   -4.175  1.00 53.52  ?  457  ASN D CG  1 
ATOM   9538  O OD1 . ASN D  1  457 ? 2.890   1.158   -3.251  1.00 54.18  ?  457  ASN D OD1 1 
ATOM   9539  N ND2 . ASN D  1  457 ? 1.528   0.274   -4.804  1.00 53.20  ?  457  ASN D ND2 1 
ATOM   9540  N N   . PHE D  1  458 ? 6.007   1.564   -4.562  1.00 51.25  ?  458  PHE D N   1 
ATOM   9541  C CA  . PHE D  1  458 ? 6.437   2.866   -4.064  1.00 51.70  ?  458  PHE D CA  1 
ATOM   9542  C C   . PHE D  1  458 ? 7.951   2.853   -3.942  1.00 52.21  ?  458  PHE D C   1 
ATOM   9543  O O   . PHE D  1  458 ? 8.515   1.891   -3.413  1.00 52.81  ?  458  PHE D O   1 
ATOM   9544  C CB  . PHE D  1  458 ? 5.778   3.160   -2.707  1.00 52.94  ?  458  PHE D CB  1 
ATOM   9545  C CG  . PHE D  1  458 ? 6.069   4.529   -2.146  1.00 53.95  ?  458  PHE D CG  1 
ATOM   9546  C CD1 . PHE D  1  458 ? 7.284   4.811   -1.535  1.00 54.96  ?  458  PHE D CD1 1 
ATOM   9547  C CD2 . PHE D  1  458 ? 5.101   5.516   -2.181  1.00 54.19  ?  458  PHE D CD2 1 
ATOM   9548  C CE1 . PHE D  1  458 ? 7.535   6.063   -0.999  1.00 56.28  ?  458  PHE D CE1 1 
ATOM   9549  C CE2 . PHE D  1  458 ? 5.344   6.766   -1.651  1.00 55.61  ?  458  PHE D CE2 1 
ATOM   9550  C CZ  . PHE D  1  458 ? 6.563   7.042   -1.058  1.00 56.76  ?  458  PHE D CZ  1 
ATOM   9551  N N   . ILE D  1  459 ? 8.607   3.904   -4.433  1.00 54.96  ?  459  ILE D N   1 
ATOM   9552  C CA  . ILE D  1  459 ? 10.061  4.017   -4.336  1.00 55.59  ?  459  ILE D CA  1 
ATOM   9553  C C   . ILE D  1  459 ? 10.438  5.480   -4.130  1.00 56.01  ?  459  ILE D C   1 
ATOM   9554  O O   . ILE D  1  459 ? 9.943   6.367   -4.836  1.00 55.52  ?  459  ILE D O   1 
ATOM   9555  C CB  . ILE D  1  459 ? 10.775  3.424   -5.572  1.00 55.26  ?  459  ILE D CB  1 
ATOM   9556  C CG1 . ILE D  1  459 ? 12.290  3.505   -5.409  1.00 56.08  ?  459  ILE D CG1 1 
ATOM   9557  C CG2 . ILE D  1  459 ? 10.336  4.097   -6.866  1.00 54.53  ?  459  ILE D CG2 1 
ATOM   9558  C CD1 . ILE D  1  459 ? 12.994  2.250   -5.824  1.00 56.54  ?  459  ILE D CD1 1 
ATOM   9559  N N   . ASP D  1  460 ? 11.323  5.731   -3.164  1.00 55.06  ?  460  ASP D N   1 
ATOM   9560  C CA  . ASP D  1  460 ? 11.721  7.091   -2.797  1.00 55.73  ?  460  ASP D CA  1 
ATOM   9561  C C   . ASP D  1  460 ? 13.236  7.106   -2.609  1.00 55.97  ?  460  ASP D C   1 
ATOM   9562  O O   . ASP D  1  460 ? 13.738  6.706   -1.553  1.00 56.90  ?  460  ASP D O   1 
ATOM   9563  C CB  . ASP D  1  460 ? 10.997  7.549   -1.536  1.00 57.29  ?  460  ASP D CB  1 
ATOM   9564  C CG  . ASP D  1  460 ? 11.170  9.034   -1.264  1.00 58.38  ?  460  ASP D CG  1 
ATOM   9565  O OD1 . ASP D  1  460 ? 11.805  9.723   -2.088  1.00 57.47  ?  460  ASP D OD1 1 
ATOM   9566  O OD2 . ASP D  1  460 ? 10.671  9.512   -0.224  1.00 60.25  -1 460  ASP D OD2 1 
ATOM   9567  N N   . LEU D  1  461 ? 13.958  7.564   -3.634  1.00 55.60  ?  461  LEU D N   1 
ATOM   9568  C CA  . LEU D  1  461 ? 15.414  7.641   -3.608  1.00 55.82  ?  461  LEU D CA  1 
ATOM   9569  C C   . LEU D  1  461 ? 15.922  9.043   -3.288  1.00 56.00  ?  461  LEU D C   1 
ATOM   9570  O O   . LEU D  1  461 ? 17.101  9.328   -3.517  1.00 56.02  ?  461  LEU D O   1 
ATOM   9571  C CB  . LEU D  1  461 ? 15.993  7.184   -4.947  1.00 55.48  ?  461  LEU D CB  1 
ATOM   9572  C CG  . LEU D  1  461 ? 15.537  5.843   -5.509  1.00 55.56  ?  461  LEU D CG  1 
ATOM   9573  C CD1 . LEU D  1  461 ? 16.045  5.676   -6.938  1.00 55.98  ?  461  LEU D CD1 1 
ATOM   9574  C CD2 . LEU D  1  461 ? 16.027  4.723   -4.613  1.00 56.09  ?  461  LEU D CD2 1 
ATOM   9575  N N   . SER D  1  462 ? 15.066  9.910   -2.745  1.00 58.24  ?  462  SER D N   1 
ATOM   9576  C CA  . SER D  1  462 ? 15.373  11.330  -2.634  1.00 58.42  ?  462  SER D CA  1 
ATOM   9577  C C   . SER D  1  462 ? 16.525  11.583  -1.667  1.00 59.39  ?  462  SER D C   1 
ATOM   9578  O O   . SER D  1  462 ? 16.823  10.779  -0.779  1.00 60.25  ?  462  SER D O   1 
ATOM   9579  C CB  . SER D  1  462 ? 14.144  12.112  -2.173  1.00 59.34  ?  462  SER D CB  1 
ATOM   9580  O OG  . SER D  1  462 ? 12.974  11.641  -2.813  1.00 58.84  ?  462  SER D OG  1 
ATOM   9581  N N   . ASN D  1  463 ? 17.180  12.729  -1.864  1.00 60.20  ?  463  ASN D N   1 
ATOM   9582  C CA  . ASN D  1  463 ? 18.312  13.170  -1.049  1.00 61.13  ?  463  ASN D CA  1 
ATOM   9583  C C   . ASN D  1  463 ? 19.428  12.123  -1.047  1.00 61.16  ?  463  ASN D C   1 
ATOM   9584  O O   . ASN D  1  463 ? 19.846  11.617  -0.002  1.00 62.21  ?  463  ASN D O   1 
ATOM   9585  C CB  . ASN D  1  463 ? 17.869  13.506  0.378   1.00 62.79  ?  463  ASN D CB  1 
ATOM   9586  C CG  . ASN D  1  463 ? 16.752  14.524  0.414   1.00 63.26  ?  463  ASN D CG  1 
ATOM   9587  O OD1 . ASN D  1  463 ? 16.674  15.404  -0.443  1.00 62.39  ?  463  ASN D OD1 1 
ATOM   9588  N ND2 . ASN D  1  463 ? 15.881  14.413  1.412   1.00 64.85  ?  463  ASN D ND2 1 
ATOM   9589  N N   . ASN D  1  464 ? 19.913  11.814  -2.248  1.00 63.45  ?  464  ASN D N   1 
ATOM   9590  C CA  . ASN D  1  464 ? 21.001  10.861  -2.436  1.00 63.71  ?  464  ASN D CA  1 
ATOM   9591  C C   . ASN D  1  464 ? 21.961  11.432  -3.475  1.00 63.48  ?  464  ASN D C   1 
ATOM   9592  O O   . ASN D  1  464 ? 21.859  12.597  -3.872  1.00 63.16  ?  464  ASN D O   1 
ATOM   9593  C CB  . ASN D  1  464 ? 20.460  9.479   -2.827  1.00 63.41  ?  464  ASN D CB  1 
ATOM   9594  C CG  . ASN D  1  464 ? 20.068  8.648   -1.620  1.00 64.14  ?  464  ASN D CG  1 
ATOM   9595  O OD1 . ASN D  1  464 ? 20.923  8.126   -0.902  1.00 64.99  ?  464  ASN D OD1 1 
ATOM   9596  N ND2 . ASN D  1  464 ? 18.765  8.530   -1.386  1.00 63.97  ?  464  ASN D ND2 1 
ATOM   9597  N N   . ASN D  1  465 ? 22.907  10.604  -3.915  1.00 69.23  ?  465  ASN D N   1 
ATOM   9598  C CA  . ASN D  1  465 ? 23.981  11.038  -4.799  1.00 69.48  ?  465  ASN D CA  1 
ATOM   9599  C C   . ASN D  1  465 ? 24.021  10.237  -6.094  1.00 69.48  ?  465  ASN D C   1 
ATOM   9600  O O   . ASN D  1  465 ? 25.096  10.005  -6.649  1.00 70.16  ?  465  ASN D O   1 
ATOM   9601  C CB  . ASN D  1  465 ? 25.325  10.942  -4.083  1.00 70.49  ?  465  ASN D CB  1 
ATOM   9602  C CG  . ASN D  1  465 ? 25.789  12.269  -3.556  1.00 70.83  ?  465  ASN D CG  1 
ATOM   9603  O OD1 . ASN D  1  465 ? 26.334  13.084  -4.298  1.00 70.96  ?  465  ASN D OD1 1 
ATOM   9604  N ND2 . ASN D  1  465 ? 25.565  12.506  -2.268  1.00 71.19  ?  465  ASN D ND2 1 
ATOM   9605  N N   . PHE D  1  466 ? 22.864  9.803   -6.586  1.00 64.98  ?  466  PHE D N   1 
ATOM   9606  C CA  . PHE D  1  466 ? 22.828  9.079   -7.848  1.00 65.41  ?  466  PHE D CA  1 
ATOM   9607  C C   . PHE D  1  466 ? 23.072  10.031  -9.011  1.00 65.56  ?  466  PHE D C   1 
ATOM   9608  O O   . PHE D  1  466 ? 22.583  11.164  -9.015  1.00 64.87  ?  466  PHE D O   1 
ATOM   9609  C CB  . PHE D  1  466 ? 21.484  8.377   -8.030  1.00 65.07  ?  466  PHE D CB  1 
ATOM   9610  C CG  . PHE D  1  466 ? 21.240  7.274   -7.049  1.00 65.09  ?  466  PHE D CG  1 
ATOM   9611  C CD1 . PHE D  1  466 ? 22.034  6.140   -7.052  1.00 65.87  ?  466  PHE D CD1 1 
ATOM   9612  C CD2 . PHE D  1  466 ? 20.213  7.366   -6.125  1.00 64.41  ?  466  PHE D CD2 1 
ATOM   9613  C CE1 . PHE D  1  466 ? 21.811  5.121   -6.148  1.00 65.93  ?  466  PHE D CE1 1 
ATOM   9614  C CE2 . PHE D  1  466 ? 19.989  6.350   -5.220  1.00 64.62  ?  466  PHE D CE2 1 
ATOM   9615  C CZ  . PHE D  1  466 ? 20.788  5.226   -5.232  1.00 65.33  ?  466  PHE D CZ  1 
ATOM   9616  N N   . HIS D  1  467 ? 23.830  9.564   -9.999  1.00 68.54  ?  467  HIS D N   1 
ATOM   9617  C CA  . HIS D  1  467 ? 24.080  10.289  -11.239 1.00 69.04  ?  467  HIS D CA  1 
ATOM   9618  C C   . HIS D  1  467 ? 23.649  9.428   -12.424 1.00 70.09  ?  467  HIS D C   1 
ATOM   9619  O O   . HIS D  1  467 ? 23.166  8.307   -12.265 1.00 70.37  ?  467  HIS D O   1 
ATOM   9620  C CB  . HIS D  1  467 ? 25.554  10.694  -11.351 1.00 69.60  ?  467  HIS D CB  1 
ATOM   9621  C CG  . HIS D  1  467 ? 26.476  9.562   -11.689 1.00 70.61  ?  467  HIS D CG  1 
ATOM   9622  N ND1 . HIS D  1  467 ? 27.023  8.735   -10.731 1.00 70.70  ?  467  HIS D ND1 1 
ATOM   9623  C CD2 . HIS D  1  467 ? 26.958  9.128   -12.879 1.00 71.61  ?  467  HIS D CD2 1 
ATOM   9624  C CE1 . HIS D  1  467 ? 27.799  7.839   -11.316 1.00 71.61  ?  467  HIS D CE1 1 
ATOM   9625  N NE2 . HIS D  1  467 ? 27.776  8.055   -12.619 1.00 72.16  ?  467  HIS D NE2 1 
ATOM   9626  N N   . GLY D  1  468 ? 23.838  9.960   -13.624 1.00 68.35  ?  468  GLY D N   1 
ATOM   9627  C CA  . GLY D  1  468 ? 23.429  9.272   -14.832 1.00 69.67  ?  468  GLY D CA  1 
ATOM   9628  C C   . GLY D  1  468 ? 22.061  9.716   -15.305 1.00 69.80  ?  468  GLY D C   1 
ATOM   9629  O O   . GLY D  1  468 ? 21.500  10.720  -14.856 1.00 68.64  ?  468  GLY D O   1 
ATOM   9630  N N   . GLN D  1  469 ? 21.516  8.937   -16.235 1.00 68.60  ?  469  GLN D N   1 
ATOM   9631  C CA  . GLN D  1  469 ? 20.226  9.226   -16.843 1.00 69.35  ?  469  GLN D CA  1 
ATOM   9632  C C   . GLN D  1  469 ? 19.220  8.150   -16.466 1.00 69.41  ?  469  GLN D C   1 
ATOM   9633  O O   . GLN D  1  469 ? 19.588  7.011   -16.162 1.00 69.07  ?  469  GLN D O   1 
ATOM   9634  C CB  . GLN D  1  469 ? 20.333  9.304   -18.366 1.00 70.84  ?  469  GLN D CB  1 
ATOM   9635  C CG  . GLN D  1  469 ? 21.717  9.643   -18.871 1.00 70.80  ?  469  GLN D CG  1 
ATOM   9636  C CD  . GLN D  1  469 ? 21.685  10.331  -20.219 1.00 71.60  ?  469  GLN D CD  1 
ATOM   9637  O OE1 . GLN D  1  469 ? 20.704  10.224  -20.961 1.00 72.55  ?  469  GLN D OE1 1 
ATOM   9638  N NE2 . GLN D  1  469 ? 22.759  11.047  -20.545 1.00 71.21  ?  469  GLN D NE2 1 
ATOM   9639  N N   . LEU D  1  470 ? 17.943  8.524   -16.492 1.00 66.28  ?  470  LEU D N   1 
ATOM   9640  C CA  . LEU D  1  470 ? 16.878  7.597   -16.131 1.00 64.70  ?  470  LEU D CA  1 
ATOM   9641  C C   . LEU D  1  470 ? 16.753  6.510   -17.192 1.00 64.87  ?  470  LEU D C   1 
ATOM   9642  O O   . LEU D  1  470 ? 16.572  6.805   -18.377 1.00 65.70  ?  470  LEU D O   1 
ATOM   9643  C CB  . LEU D  1  470 ? 15.558  8.346   -15.973 1.00 62.99  ?  470  LEU D CB  1 
ATOM   9644  C CG  . LEU D  1  470 ? 15.420  9.276   -14.768 1.00 62.02  ?  470  LEU D CG  1 
ATOM   9645  C CD1 . LEU D  1  470 ? 13.959  9.456   -14.434 1.00 59.09  ?  470  LEU D CD1 1 
ATOM   9646  C CD2 . LEU D  1  470 ? 16.180  8.735   -13.567 1.00 62.15  ?  470  LEU D CD2 1 
ATOM   9647  N N   . SER D  1  471 ? 16.844  5.255   -16.764 1.00 66.98  ?  471  SER D N   1 
ATOM   9648  C CA  . SER D  1  471 ? 16.643  4.134   -17.669 1.00 67.13  ?  471  SER D CA  1 
ATOM   9649  C C   . SER D  1  471 ? 15.168  3.996   -18.023 1.00 66.14  ?  471  SER D C   1 
ATOM   9650  O O   . SER D  1  471 ? 14.285  4.330   -17.231 1.00 64.78  ?  471  SER D O   1 
ATOM   9651  C CB  . SER D  1  471 ? 17.147  2.840   -17.031 1.00 66.80  ?  471  SER D CB  1 
ATOM   9652  O OG  . SER D  1  471 ? 16.775  1.713   -17.803 1.00 66.88  ?  471  SER D OG  1 
ATOM   9653  N N   . ALA D  1  472 ? 14.900  3.500   -19.228 1.00 63.92  ?  472  ALA D N   1 
ATOM   9654  C CA  . ALA D  1  472 ? 13.529  3.153   -19.584 1.00 63.30  ?  472  ALA D CA  1 
ATOM   9655  C C   . ALA D  1  472 ? 13.060  1.863   -18.918 1.00 62.50  ?  472  ALA D C   1 
ATOM   9656  O O   . ALA D  1  472 ? 11.926  1.432   -19.161 1.00 62.16  ?  472  ALA D O   1 
ATOM   9657  C CB  . ALA D  1  472 ? 13.387  3.040   -21.104 1.00 64.56  ?  472  ALA D CB  1 
ATOM   9658  N N   . ASN D  1  473 ? 13.897  1.250   -18.076 1.00 69.46  ?  473  ASN D N   1 
ATOM   9659  C CA  . ASN D  1  473 ? 13.504  0.034   -17.371 1.00 68.87  ?  473  ASN D CA  1 
ATOM   9660  C C   . ASN D  1  473 ? 12.277  0.258   -16.501 1.00 67.66  ?  473  ASN D C   1 
ATOM   9661  O O   . ASN D  1  473 ? 11.534  -0.691  -16.224 1.00 67.43  ?  473  ASN D O   1 
ATOM   9662  C CB  . ASN D  1  473 ? 14.658  -0.472  -16.504 1.00 68.90  ?  473  ASN D CB  1 
ATOM   9663  C CG  . ASN D  1  473 ? 15.725  -1.181  -17.304 1.00 70.05  ?  473  ASN D CG  1 
ATOM   9664  O OD1 . ASN D  1  473 ? 15.542  -1.464  -18.489 1.00 70.71  ?  473  ASN D OD1 1 
ATOM   9665  N ND2 . ASN D  1  473 ? 16.855  -1.467  -16.662 1.00 70.28  ?  473  ASN D ND2 1 
ATOM   9666  N N   . TRP D  1  474 ? 12.060  1.494   -16.042 1.00 65.36  ?  474  TRP D N   1 
ATOM   9667  C CA  . TRP D  1  474 ? 10.976  1.762   -15.105 1.00 63.79  ?  474  TRP D CA  1 
ATOM   9668  C C   . TRP D  1  474 ? 9.603   1.521   -15.717 1.00 63.84  ?  474  TRP D C   1 
ATOM   9669  O O   . TRP D  1  474 ? 8.655   1.235   -14.978 1.00 62.26  ?  474  TRP D O   1 
ATOM   9670  C CB  . TRP D  1  474 ? 11.074  3.196   -14.573 1.00 62.75  ?  474  TRP D CB  1 
ATOM   9671  C CG  . TRP D  1  474 ? 12.376  3.503   -13.880 1.00 63.09  ?  474  TRP D CG  1 
ATOM   9672  C CD1 . TRP D  1  474 ? 13.393  4.272   -14.362 1.00 64.28  ?  474  TRP D CD1 1 
ATOM   9673  C CD2 . TRP D  1  474 ? 12.800  3.048   -12.581 1.00 62.69  ?  474  TRP D CD2 1 
ATOM   9674  N NE1 . TRP D  1  474 ? 14.420  4.325   -13.452 1.00 64.76  ?  474  TRP D NE1 1 
ATOM   9675  C CE2 . TRP D  1  474 ? 14.082  3.583   -12.350 1.00 63.79  ?  474  TRP D CE2 1 
ATOM   9676  C CE3 . TRP D  1  474 ? 12.219  2.243   -11.595 1.00 61.80  ?  474  TRP D CE3 1 
ATOM   9677  C CZ2 . TRP D  1  474 ? 14.795  3.339   -11.174 1.00 63.94  ?  474  TRP D CZ2 1 
ATOM   9678  C CZ3 . TRP D  1  474 ? 12.931  2.002   -10.426 1.00 62.03  ?  474  TRP D CZ3 1 
ATOM   9679  C CH2 . TRP D  1  474 ? 14.205  2.549   -10.229 1.00 63.04  ?  474  TRP D CH2 1 
ATOM   9680  N N   . GLU D  1  475 ? 9.477   1.608   -17.043 1.00 68.17  ?  475  GLU D N   1 
ATOM   9681  C CA  . GLU D  1  475 ? 8.179   1.396   -17.671 1.00 67.74  ?  475  GLU D CA  1 
ATOM   9682  C C   . GLU D  1  475 ? 7.666   -0.020  -17.435 1.00 67.62  ?  475  GLU D C   1 
ATOM   9683  O O   . GLU D  1  475 ? 6.451   -0.240  -17.386 1.00 66.88  ?  475  GLU D O   1 
ATOM   9684  C CB  . GLU D  1  475 ? 8.271   1.693   -19.164 1.00 69.11  ?  475  GLU D CB  1 
ATOM   9685  C CG  . GLU D  1  475 ? 6.973   1.477   -19.909 1.00 69.24  ?  475  GLU D CG  1 
ATOM   9686  C CD  . GLU D  1  475 ? 7.186   1.240   -21.389 1.00 70.92  ?  475  GLU D CD  1 
ATOM   9687  O OE1 . GLU D  1  475 ? 8.282   0.769   -21.779 1.00 71.66  ?  475  GLU D OE1 1 
ATOM   9688  O OE2 . GLU D  1  475 ? 6.249   1.526   -22.166 1.00 71.53  -1 475  GLU D OE2 1 
ATOM   9689  N N   . GLN D  1  476 ? 8.572   -0.987  -17.270 1.00 68.29  ?  476  GLN D N   1 
ATOM   9690  C CA  . GLN D  1  476 ? 8.161   -2.360  -17.000 1.00 68.38  ?  476  GLN D CA  1 
ATOM   9691  C C   . GLN D  1  476 ? 7.534   -2.509  -15.622 1.00 67.08  ?  476  GLN D C   1 
ATOM   9692  O O   . GLN D  1  476 ? 6.801   -3.477  -15.390 1.00 66.98  ?  476  GLN D O   1 
ATOM   9693  C CB  . GLN D  1  476 ? 9.355   -3.307  -17.144 1.00 69.55  ?  476  GLN D CB  1 
ATOM   9694  C CG  . GLN D  1  476 ? 10.077  -3.186  -18.479 1.00 70.49  ?  476  GLN D CG  1 
ATOM   9695  C CD  . GLN D  1  476 ? 10.597  -4.515  -18.983 1.00 71.33  ?  476  GLN D CD  1 
ATOM   9696  O OE1 . GLN D  1  476 ? 10.715  -5.475  -18.221 1.00 71.29  ?  476  GLN D OE1 1 
ATOM   9697  N NE2 . GLN D  1  476 ? 10.902  -4.582  -20.275 1.00 72.13  ?  476  GLN D NE2 1 
ATOM   9698  N N   . SER D  1  477 ? 7.801   -1.574  -14.709 1.00 65.29  ?  477  SER D N   1 
ATOM   9699  C CA  . SER D  1  477 ? 7.164   -1.546  -13.392 1.00 63.66  ?  477  SER D CA  1 
ATOM   9700  C C   . SER D  1  477 ? 5.752   -0.959  -13.500 1.00 62.57  ?  477  SER D C   1 
ATOM   9701  O O   . SER D  1  477 ? 5.420   0.067   -12.908 1.00 61.39  ?  477  SER D O   1 
ATOM   9702  C CB  . SER D  1  477 ? 8.021   -0.755  -12.412 1.00 62.94  ?  477  SER D CB  1 
ATOM   9703  O OG  . SER D  1  477 ? 9.287   -1.363  -12.233 1.00 63.95  ?  477  SER D OG  1 
ATOM   9704  N N   . GLN D  1  478 ? 4.912   -1.652  -14.275 1.00 66.29  ?  478  GLN D N   1 
ATOM   9705  C CA  . GLN D  1  478 ? 3.613   -1.117  -14.673 1.00 65.78  ?  478  GLN D CA  1 
ATOM   9706  C C   . GLN D  1  478 ? 2.687   -0.839  -13.492 1.00 64.54  ?  478  GLN D C   1 
ATOM   9707  O O   . GLN D  1  478 ? 1.690   -0.125  -13.657 1.00 64.14  ?  478  GLN D O   1 
ATOM   9708  C CB  . GLN D  1  478 ? 2.932   -2.076  -15.654 1.00 66.86  ?  478  GLN D CB  1 
ATOM   9709  C CG  . GLN D  1  478 ? 3.362   -1.877  -17.102 1.00 68.11  ?  478  GLN D CG  1 
ATOM   9710  C CD  . GLN D  1  478 ? 2.827   -0.578  -17.708 1.00 67.79  ?  478  GLN D CD  1 
ATOM   9711  O OE1 . GLN D  1  478 ? 1.742   -0.107  -17.352 1.00 66.93  ?  478  GLN D OE1 1 
ATOM   9712  N NE2 . GLN D  1  478 ? 3.599   0.011   -18.621 1.00 68.72  ?  478  GLN D NE2 1 
ATOM   9713  N N   . LYS D  1  479 ? 2.984   -1.370  -12.311 1.00 62.18  ?  479  LYS D N   1 
ATOM   9714  C CA  . LYS D  1  479 ? 2.157   -1.141  -11.136 1.00 61.46  ?  479  LYS D CA  1 
ATOM   9715  C C   . LYS D  1  479 ? 2.687   -0.015  -10.249 1.00 60.71  ?  479  LYS D C   1 
ATOM   9716  O O   . LYS D  1  479 ? 2.179   0.178   -9.140  1.00 60.56  ?  479  LYS D O   1 
ATOM   9717  C CB  . LYS D  1  479 ? 2.015   -2.440  -10.343 1.00 62.01  ?  479  LYS D CB  1 
ATOM   9718  C CG  . LYS D  1  479 ? 1.402   -3.562  -11.165 1.00 62.89  ?  479  LYS D CG  1 
ATOM   9719  C CD  . LYS D  1  479 ? 0.904   -4.700  -10.300 1.00 63.42  ?  479  LYS D CD  1 
ATOM   9720  C CE  . LYS D  1  479 ? 0.216   -5.751  -11.155 1.00 64.39  ?  479  LYS D CE  1 
ATOM   9721  N NZ  . LYS D  1  479 ? -0.392  -6.853  -10.349 1.00 65.03  ?  479  LYS D NZ  1 
ATOM   9722  N N   . LEU D  1  480 ? 3.682   0.738   -10.717 1.00 57.77  ?  480  LEU D N   1 
ATOM   9723  C CA  . LEU D  1  480 ? 4.249   1.828   -9.932  1.00 57.25  ?  480  LEU D CA  1 
ATOM   9724  C C   . LEU D  1  480 ? 3.275   2.997   -9.862  1.00 56.71  ?  480  LEU D C   1 
ATOM   9725  O O   . LEU D  1  480 ? 2.702   3.400   -10.877 1.00 56.68  ?  480  LEU D O   1 
ATOM   9726  C CB  . LEU D  1  480 ? 5.569   2.284   -10.556 1.00 57.49  ?  480  LEU D CB  1 
ATOM   9727  C CG  . LEU D  1  480 ? 6.526   3.113   -9.703  1.00 57.43  ?  480  LEU D CG  1 
ATOM   9728  C CD1 . LEU D  1  480 ? 7.093   2.266   -8.585  1.00 58.11  ?  480  LEU D CD1 1 
ATOM   9729  C CD2 . LEU D  1  480 ? 7.645   3.669   -10.569 1.00 57.89  ?  480  LEU D CD2 1 
ATOM   9730  N N   . VAL D  1  481 ? 3.097   3.549   -8.663  1.00 55.66  ?  481  VAL D N   1 
ATOM   9731  C CA  . VAL D  1  481 ? 2.230   4.706   -8.475  1.00 55.64  ?  481  VAL D CA  1 
ATOM   9732  C C   . VAL D  1  481 ? 2.954   5.910   -7.886  1.00 55.81  ?  481  VAL D C   1 
ATOM   9733  O O   . VAL D  1  481 ? 2.431   7.035   -7.983  1.00 55.98  ?  481  VAL D O   1 
ATOM   9734  C CB  . VAL D  1  481 ? 1.004   4.353   -7.606  1.00 56.35  ?  481  VAL D CB  1 
ATOM   9735  C CG1 . VAL D  1  481 ? 0.107   3.380   -8.335  1.00 56.28  ?  481  VAL D CG1 1 
ATOM   9736  C CG2 . VAL D  1  481 ? 1.442   3.786   -6.273  1.00 57.14  ?  481  VAL D CG2 1 
ATOM   9737  N N   . ALA D  1  482 ? 4.131   5.735   -7.286  1.00 53.80  ?  482  ALA D N   1 
ATOM   9738  C CA  . ALA D  1  482 ? 4.896   6.847   -6.731  1.00 54.41  ?  482  ALA D CA  1 
ATOM   9739  C C   . ALA D  1  482 ? 6.364   6.667   -7.100  1.00 54.40  ?  482  ALA D C   1 
ATOM   9740  O O   . ALA D  1  482 ? 7.015   5.735   -6.615  1.00 55.04  ?  482  ALA D O   1 
ATOM   9741  C CB  . ALA D  1  482 ? 4.717   6.929   -5.218  1.00 56.03  ?  482  ALA D CB  1 
ATOM   9742  N N   . PHE D  1  483 ? 6.886   7.562   -7.945  1.00 54.37  ?  483  PHE D N   1 
ATOM   9743  C CA  . PHE D  1  483 ? 8.290   7.551   -8.356  1.00 54.93  ?  483  PHE D CA  1 
ATOM   9744  C C   . PHE D  1  483 ? 8.919   8.861   -7.905  1.00 55.57  ?  483  PHE D C   1 
ATOM   9745  O O   . PHE D  1  483 ? 8.688   9.905   -8.523  1.00 54.58  ?  483  PHE D O   1 
ATOM   9746  C CB  . PHE D  1  483 ? 8.412   7.377   -9.871  1.00 54.35  ?  483  PHE D CB  1 
ATOM   9747  C CG  . PHE D  1  483 ? 9.811   7.099   -10.345 1.00 55.65  ?  483  PHE D CG  1 
ATOM   9748  C CD1 . PHE D  1  483 ? 10.735  6.497   -9.511  1.00 56.94  ?  483  PHE D CD1 1 
ATOM   9749  C CD2 . PHE D  1  483 ? 10.198  7.426   -11.635 1.00 56.11  ?  483  PHE D CD2 1 
ATOM   9750  C CE1 . PHE D  1  483 ? 12.028  6.235   -9.949  1.00 58.44  ?  483  PHE D CE1 1 
ATOM   9751  C CE2 . PHE D  1  483 ? 11.489  7.167   -12.078 1.00 57.88  ?  483  PHE D CE2 1 
ATOM   9752  C CZ  . PHE D  1  483 ? 12.404  6.571   -11.232 1.00 59.02  ?  483  PHE D CZ  1 
ATOM   9753  N N   . ILE D  1  484 ? 9.743   8.805   -6.858  1.00 53.13  ?  484  ILE D N   1 
ATOM   9754  C CA  . ILE D  1  484 ? 10.252  10.001  -6.187  1.00 53.57  ?  484  ILE D CA  1 
ATOM   9755  C C   . ILE D  1  484 ? 11.773  9.914   -6.135  1.00 53.63  ?  484  ILE D C   1 
ATOM   9756  O O   . ILE D  1  484 ? 12.326  9.070   -5.418  1.00 54.36  ?  484  ILE D O   1 
ATOM   9757  C CB  . ILE D  1  484 ? 9.661   10.162  -4.778  1.00 55.44  ?  484  ILE D CB  1 
ATOM   9758  C CG1 . ILE D  1  484 ? 8.137   10.073  -4.835  1.00 55.18  ?  484  ILE D CG1 1 
ATOM   9759  C CG2 . ILE D  1  484 ? 10.067  11.486  -4.171  1.00 56.65  ?  484  ILE D CG2 1 
ATOM   9760  C CD1 . ILE D  1  484 ? 7.472   10.150  -3.492  1.00 57.03  ?  484  ILE D CD1 1 
ATOM   9761  N N   . LEU D  1  485 ? 12.448  10.803  -6.875  1.00 59.41  ?  485  LEU D N   1 
ATOM   9762  C CA  . LEU D  1  485 ? 13.900  10.776  -7.074  1.00 59.77  ?  485  LEU D CA  1 
ATOM   9763  C C   . LEU D  1  485 ? 14.500  12.180  -6.951  1.00 59.57  ?  485  LEU D C   1 
ATOM   9764  O O   . LEU D  1  485 ? 15.335  12.588  -7.766  1.00 59.55  ?  485  LEU D O   1 
ATOM   9765  C CB  . LEU D  1  485 ? 14.246  10.159  -8.431  1.00 60.18  ?  485  LEU D CB  1 
ATOM   9766  C CG  . LEU D  1  485 ? 15.499  9.285   -8.530  1.00 61.43  ?  485  LEU D CG  1 
ATOM   9767  C CD1 . LEU D  1  485 ? 15.486  8.525   -9.850  1.00 62.91  ?  485  LEU D CD1 1 
ATOM   9768  C CD2 . LEU D  1  485 ? 16.802  10.075  -8.372  1.00 61.50  ?  485  LEU D CD2 1 
ATOM   9769  N N   . SER D  1  486 ? 14.081  12.951  -5.951  1.00 60.90  ?  486  SER D N   1 
ATOM   9770  C CA  . SER D  1  486 ? 14.475  14.354  -5.913  1.00 61.01  ?  486  SER D CA  1 
ATOM   9771  C C   . SER D  1  486 ? 15.823  14.548  -5.221  1.00 61.84  ?  486  SER D C   1 
ATOM   9772  O O   . SER D  1  486 ? 16.304  13.689  -4.478  1.00 62.50  ?  486  SER D O   1 
ATOM   9773  C CB  . SER D  1  486 ? 13.414  15.203  -5.210  1.00 61.86  ?  486  SER D CB  1 
ATOM   9774  O OG  . SER D  1  486 ? 13.166  14.735  -3.895  1.00 63.61  ?  486  SER D OG  1 
ATOM   9775  N N   . ASN D  1  487 ? 16.415  15.718  -5.471  1.00 64.28  ?  487  ASN D N   1 
ATOM   9776  C CA  . ASN D  1  487 ? 17.706  16.131  -4.915  1.00 65.09  ?  487  ASN D CA  1 
ATOM   9777  C C   . ASN D  1  487 ? 18.790  15.070  -5.122  1.00 65.18  ?  487  ASN D C   1 
ATOM   9778  O O   . ASN D  1  487 ? 19.451  14.621  -4.183  1.00 66.00  ?  487  ASN D O   1 
ATOM   9779  C CB  . ASN D  1  487 ? 17.579  16.505  -3.437  1.00 66.44  ?  487  ASN D CB  1 
ATOM   9780  C CG  . ASN D  1  487 ? 18.790  17.266  -2.936  1.00 67.26  ?  487  ASN D CG  1 
ATOM   9781  O OD1 . ASN D  1  487 ? 19.478  17.912  -3.721  1.00 66.91  ?  487  ASN D OD1 1 
ATOM   9782  N ND2 . ASN D  1  487 ? 19.063  17.191  -1.636  1.00 68.55  ?  487  ASN D ND2 1 
ATOM   9783  N N   . ASN D  1  488 ? 18.977  14.672  -6.374  1.00 63.43  ?  488  ASN D N   1 
ATOM   9784  C CA  . ASN D  1  488 ? 20.073  13.801  -6.782  1.00 63.94  ?  488  ASN D CA  1 
ATOM   9785  C C   . ASN D  1  488 ? 20.931  14.548  -7.804  1.00 64.23  ?  488  ASN D C   1 
ATOM   9786  O O   . ASN D  1  488 ? 20.740  15.742  -8.047  1.00 63.99  ?  488  ASN D O   1 
ATOM   9787  C CB  . ASN D  1  488 ? 19.545  12.472  -7.328  1.00 63.86  ?  488  ASN D CB  1 
ATOM   9788  C CG  . ASN D  1  488 ? 19.303  11.450  -6.234  1.00 64.10  ?  488  ASN D CG  1 
ATOM   9789  O OD1 . ASN D  1  488 ? 20.138  10.585  -5.975  1.00 64.77  ?  488  ASN D OD1 1 
ATOM   9790  N ND2 . ASN D  1  488 ? 18.152  11.544  -5.589  1.00 63.72  ?  488  ASN D ND2 1 
ATOM   9791  N N   . SER D  1  489 ? 21.907  13.850  -8.384  1.00 64.16  ?  489  SER D N   1 
ATOM   9792  C CA  . SER D  1  489 ? 22.698  14.399  -9.479  1.00 64.71  ?  489  SER D CA  1 
ATOM   9793  C C   . SER D  1  489 ? 22.236  13.872  -10.834 1.00 65.06  ?  489  SER D C   1 
ATOM   9794  O O   . SER D  1  489 ? 23.055  13.685  -11.740 1.00 66.04  ?  489  SER D O   1 
ATOM   9795  C CB  . SER D  1  489 ? 24.182  14.096  -9.270  1.00 65.64  ?  489  SER D CB  1 
ATOM   9796  O OG  . SER D  1  489 ? 24.633  14.578  -8.015  1.00 65.71  ?  489  SER D OG  1 
ATOM   9797  N N   . ILE D  1  490 ? 20.936  13.613  -10.980 1.00 63.00  ?  490  ILE D N   1 
ATOM   9798  C CA  . ILE D  1  490 ? 20.412  13.017  -12.203 1.00 63.83  ?  490  ILE D CA  1 
ATOM   9799  C C   . ILE D  1  490 ? 20.559  13.999  -13.357 1.00 64.26  ?  490  ILE D C   1 
ATOM   9800  O O   . ILE D  1  490 ? 20.219  15.183  -13.237 1.00 63.34  ?  490  ILE D O   1 
ATOM   9801  C CB  . ILE D  1  490 ? 18.946  12.600  -12.014 1.00 63.21  ?  490  ILE D CB  1 
ATOM   9802  C CG1 . ILE D  1  490 ? 18.823  11.598  -10.865 1.00 62.88  ?  490  ILE D CG1 1 
ATOM   9803  C CG2 . ILE D  1  490 ? 18.387  12.017  -13.301 1.00 64.68  ?  490  ILE D CG2 1 
ATOM   9804  C CD1 . ILE D  1  490 ? 19.755  10.415  -10.989 1.00 64.17  ?  490  ILE D CD1 1 
ATOM   9805  N N   . THR D  1  491 ? 21.065  13.507  -14.482 1.00 62.89  ?  491  THR D N   1 
ATOM   9806  C CA  . THR D  1  491 ? 21.268  14.282  -15.699 1.00 63.58  ?  491  THR D CA  1 
ATOM   9807  C C   . THR D  1  491 ? 20.512  13.624  -16.853 1.00 65.04  ?  491  THR D C   1 
ATOM   9808  O O   . THR D  1  491 ? 19.798  12.633  -16.676 1.00 65.63  ?  491  THR D O   1 
ATOM   9809  C CB  . THR D  1  491 ? 22.761  14.409  -16.025 1.00 64.28  ?  491  THR D CB  1 
ATOM   9810  O OG1 . THR D  1  491 ? 23.291  13.122  -16.368 1.00 65.53  ?  491  THR D OG1 1 
ATOM   9811  C CG2 . THR D  1  491 ? 23.527  14.959  -14.833 1.00 63.34  ?  491  THR D CG2 1 
ATOM   9812  N N   . GLY D  1  492 ? 20.667  14.194  -18.046 1.00 61.90  ?  492  GLY D N   1 
ATOM   9813  C CA  . GLY D  1  492 ? 20.032  13.642  -19.224 1.00 63.60  ?  492  GLY D CA  1 
ATOM   9814  C C   . GLY D  1  492 ? 18.602  14.122  -19.398 1.00 63.07  ?  492  GLY D C   1 
ATOM   9815  O O   . GLY D  1  492 ? 18.153  15.088  -18.777 1.00 61.18  ?  492  GLY D O   1 
ATOM   9816  N N   . ALA D  1  493 ? 17.876  13.418  -20.265 1.00 61.45  ?  493  ALA D N   1 
ATOM   9817  C CA  . ALA D  1  493 ? 16.492  13.742  -20.582 1.00 60.87  ?  493  ALA D CA  1 
ATOM   9818  C C   . ALA D  1  493 ? 15.547  12.704  -19.991 1.00 60.54  ?  493  ALA D C   1 
ATOM   9819  O O   . ALA D  1  493 ? 15.949  11.596  -19.625 1.00 61.60  ?  493  ALA D O   1 
ATOM   9820  C CB  . ALA D  1  493 ? 16.277  13.835  -22.095 1.00 62.61  ?  493  ALA D CB  1 
ATOM   9821  N N   . ILE D  1  494 ? 14.279  13.089  -19.882 1.00 59.72  ?  494  ILE D N   1 
ATOM   9822  C CA  . ILE D  1  494 ? 13.232  12.193  -19.398 1.00 58.54  ?  494  ILE D CA  1 
ATOM   9823  C C   . ILE D  1  494 ? 12.854  11.231  -20.519 1.00 60.27  ?  494  ILE D C   1 
ATOM   9824  O O   . ILE D  1  494 ? 12.352  11.667  -21.565 1.00 61.46  ?  494  ILE D O   1 
ATOM   9825  C CB  . ILE D  1  494 ? 12.008  12.980  -18.899 1.00 56.44  ?  494  ILE D CB  1 
ATOM   9826  C CG1 . ILE D  1  494 ? 12.402  13.958  -17.794 1.00 54.72  ?  494  ILE D CG1 1 
ATOM   9827  C CG2 . ILE D  1  494 ? 10.932  12.043  -18.376 1.00 55.50  ?  494  ILE D CG2 1 
ATOM   9828  C CD1 . ILE D  1  494 ? 11.219  14.675  -17.183 1.00 52.98  ?  494  ILE D CD1 1 
ATOM   9829  N N   . PRO D  1  495 ? 13.058  9.928   -20.344 1.00 61.99  ?  495  PRO D N   1 
ATOM   9830  C CA  . PRO D  1  495 ? 12.706  8.967   -21.397 1.00 63.26  ?  495  PRO D CA  1 
ATOM   9831  C C   . PRO D  1  495 ? 11.230  9.059   -21.736 1.00 62.86  ?  495  PRO D C   1 
ATOM   9832  O O   . PRO D  1  495 ? 10.390  9.218   -20.837 1.00 61.00  ?  495  PRO D O   1 
ATOM   9833  C CB  . PRO D  1  495 ? 13.045  7.607   -20.767 1.00 62.48  ?  495  PRO D CB  1 
ATOM   9834  C CG  . PRO D  1  495 ? 13.974  7.918   -19.643 1.00 61.97  ?  495  PRO D CG  1 
ATOM   9835  C CD  . PRO D  1  495 ? 13.596  9.270   -19.143 1.00 60.98  ?  495  PRO D CD  1 
ATOM   9836  N N   . PRO D  1  496 ? 10.876  8.977   -23.021 1.00 61.68  ?  496  PRO D N   1 
ATOM   9837  C CA  . PRO D  1  496 ? 9.459   9.094   -23.405 1.00 62.08  ?  496  PRO D CA  1 
ATOM   9838  C C   . PRO D  1  496 ? 8.565   8.017   -22.812 1.00 60.48  ?  496  PRO D C   1 
ATOM   9839  O O   . PRO D  1  496 ? 7.361   8.249   -22.647 1.00 60.23  ?  496  PRO D O   1 
ATOM   9840  C CB  . PRO D  1  496 ? 9.505   9.001   -24.937 1.00 64.65  ?  496  PRO D CB  1 
ATOM   9841  C CG  . PRO D  1  496 ? 10.893  9.359   -25.297 1.00 65.64  ?  496  PRO D CG  1 
ATOM   9842  C CD  . PRO D  1  496 ? 11.747  8.824   -24.192 1.00 63.89  ?  496  PRO D CD  1 
ATOM   9843  N N   . GLU D  1  497 ? 9.113   6.839   -22.504 1.00 68.35  ?  497  GLU D N   1 
ATOM   9844  C CA  . GLU D  1  497 ? 8.304   5.745   -21.979 1.00 67.04  ?  497  GLU D CA  1 
ATOM   9845  C C   . GLU D  1  497 ? 7.786   6.016   -20.572 1.00 64.91  ?  497  GLU D C   1 
ATOM   9846  O O   . GLU D  1  497 ? 6.850   5.339   -20.131 1.00 63.89  ?  497  GLU D O   1 
ATOM   9847  C CB  . GLU D  1  497 ? 9.114   4.449   -21.992 1.00 67.03  ?  497  GLU D CB  1 
ATOM   9848  C CG  . GLU D  1  497 ? 9.348   3.889   -23.380 1.00 68.65  ?  497  GLU D CG  1 
ATOM   9849  C CD  . GLU D  1  497 ? 10.563  4.496   -24.059 1.00 70.03  ?  497  GLU D CD  1 
ATOM   9850  O OE1 . GLU D  1  497 ? 11.424  5.072   -23.358 1.00 69.61  ?  497  GLU D OE1 1 
ATOM   9851  O OE2 . GLU D  1  497 ? 10.652  4.400   -25.300 1.00 71.49  -1 497  GLU D OE2 1 
ATOM   9852  N N   . ILE D  1  498 ? 8.368   6.985   -19.861 1.00 62.19  ?  498  ILE D N   1 
ATOM   9853  C CA  . ILE D  1  498 ? 7.891   7.318   -18.522 1.00 60.03  ?  498  ILE D CA  1 
ATOM   9854  C C   . ILE D  1  498 ? 6.426   7.732   -18.568 1.00 59.61  ?  498  ILE D C   1 
ATOM   9855  O O   . ILE D  1  498 ? 5.633   7.370   -17.691 1.00 58.02  ?  498  ILE D O   1 
ATOM   9856  C CB  . ILE D  1  498 ? 8.769   8.421   -17.904 1.00 59.57  ?  498  ILE D CB  1 
ATOM   9857  C CG1 . ILE D  1  498 ? 10.210  7.936   -17.749 1.00 60.49  ?  498  ILE D CG1 1 
ATOM   9858  C CG2 . ILE D  1  498 ? 8.210   8.850   -16.560 1.00 57.10  ?  498  ILE D CG2 1 
ATOM   9859  C CD1 . ILE D  1  498 ? 10.418  7.023   -16.575 1.00 59.37  ?  498  ILE D CD1 1 
ATOM   9860  N N   . TRP D  1  499 ? 6.044   8.503   -19.586 1.00 60.47  ?  499  TRP D N   1 
ATOM   9861  C CA  . TRP D  1  499 ? 4.658   8.935   -19.683 1.00 61.00  ?  499  TRP D CA  1 
ATOM   9862  C C   . TRP D  1  499 ? 3.712   7.784   -19.997 1.00 60.99  ?  499  TRP D C   1 
ATOM   9863  O O   . TRP D  1  499 ? 2.509   7.905   -19.745 1.00 60.46  ?  499  TRP D O   1 
ATOM   9864  C CB  . TRP D  1  499 ? 4.528   10.036  -20.733 1.00 63.75  ?  499  TRP D CB  1 
ATOM   9865  C CG  . TRP D  1  499 ? 5.627   11.035  -20.645 1.00 63.23  ?  499  TRP D CG  1 
ATOM   9866  C CD1 . TRP D  1  499 ? 6.535   11.331  -21.613 1.00 64.86  ?  499  TRP D CD1 1 
ATOM   9867  C CD2 . TRP D  1  499 ? 5.950   11.868  -19.520 1.00 60.61  ?  499  TRP D CD2 1 
ATOM   9868  N NE1 . TRP D  1  499 ? 7.402   12.298  -21.167 1.00 63.28  ?  499  TRP D NE1 1 
ATOM   9869  C CE2 . TRP D  1  499 ? 7.065   12.646  -19.886 1.00 60.77  ?  499  TRP D CE2 1 
ATOM   9870  C CE3 . TRP D  1  499 ? 5.403   12.034  -18.243 1.00 58.42  ?  499  TRP D CE3 1 
ATOM   9871  C CZ2 . TRP D  1  499 ? 7.645   13.574  -19.024 1.00 59.01  ?  499  TRP D CZ2 1 
ATOM   9872  C CZ3 . TRP D  1  499 ? 5.982   12.957  -17.386 1.00 56.61  ?  499  TRP D CZ3 1 
ATOM   9873  C CH2 . TRP D  1  499 ? 7.092   13.716  -17.783 1.00 57.02  ?  499  TRP D CH2 1 
ATOM   9874  N N   . ASN D  1  500 ? 4.219   6.669   -20.518 1.00 70.19  ?  500  ASN D N   1 
ATOM   9875  C CA  . ASN D  1  500 ? 3.367   5.505   -20.725 1.00 69.82  ?  500  ASN D CA  1 
ATOM   9876  C C   . ASN D  1  500 ? 3.165   4.690   -19.449 1.00 67.72  ?  500  ASN D C   1 
ATOM   9877  O O   . ASN D  1  500 ? 2.497   3.650   -19.496 1.00 67.46  ?  500  ASN D O   1 
ATOM   9878  C CB  . ASN D  1  500 ? 3.938   4.624   -21.844 1.00 71.21  ?  500  ASN D CB  1 
ATOM   9879  C CG  . ASN D  1  500 ? 3.303   4.919   -23.200 1.00 72.87  ?  500  ASN D CG  1 
ATOM   9880  O OD1 . ASN D  1  500 ? 2.345   5.685   -23.289 1.00 72.95  ?  500  ASN D OD1 1 
ATOM   9881  N ND2 . ASN D  1  500 ? 3.841   4.313   -24.263 1.00 74.07  ?  500  ASN D ND2 1 
ATOM   9882  N N   . MET D  1  501 ? 3.718   5.136   -18.315 1.00 63.48  ?  501  MET D N   1 
ATOM   9883  C CA  . MET D  1  501 ? 3.455   4.527   -17.007 1.00 61.61  ?  501  MET D CA  1 
ATOM   9884  C C   . MET D  1  501 ? 2.154   5.101   -16.444 1.00 60.76  ?  501  MET D C   1 
ATOM   9885  O O   . MET D  1  501 ? 2.134   5.863   -15.475 1.00 59.65  ?  501  MET D O   1 
ATOM   9886  C CB  . MET D  1  501 ? 4.616   4.767   -16.052 1.00 60.60  ?  501  MET D CB  1 
ATOM   9887  C CG  . MET D  1  501 ? 5.977   4.413   -16.605 1.00 61.81  ?  501  MET D CG  1 
ATOM   9888  S SD  . MET D  1  501 ? 7.294   4.451   -15.364 1.00 60.99  ?  501  MET D SD  1 
ATOM   9889  C CE  . MET D  1  501 ? 6.471   5.163   -13.955 1.00 58.81  ?  501  MET D CE  1 
ATOM   9890  N N   . THR D  1  502 ? 1.046   4.691   -17.068 1.00 64.14  ?  502  THR D N   1 
ATOM   9891  C CA  . THR D  1  502 ? -0.246  5.336   -16.844 1.00 63.89  ?  502  THR D CA  1 
ATOM   9892  C C   . THR D  1  502 ? -0.723  5.264   -15.396 1.00 62.43  ?  502  THR D C   1 
ATOM   9893  O O   . THR D  1  502 ? -1.522  6.111   -14.981 1.00 62.29  ?  502  THR D O   1 
ATOM   9894  C CB  . THR D  1  502 ? -1.299  4.711   -17.752 1.00 64.77  ?  502  THR D CB  1 
ATOM   9895  O OG1 . THR D  1  502 ? -1.509  3.350   -17.361 1.00 64.29  ?  502  THR D OG1 1 
ATOM   9896  C CG2 . THR D  1  502 ? -0.835  4.748   -19.193 1.00 66.46  ?  502  THR D CG2 1 
ATOM   9897  N N   . GLN D  1  503 ? -0.246  4.300   -14.611 1.00 63.84  ?  503  GLN D N   1 
ATOM   9898  C CA  . GLN D  1  503 ? -0.717  4.139   -13.240 1.00 62.99  ?  503  GLN D CA  1 
ATOM   9899  C C   . GLN D  1  503 ? -0.098  5.139   -12.273 1.00 62.32  ?  503  GLN D C   1 
ATOM   9900  O O   . GLN D  1  503 ? -0.449  5.122   -11.087 1.00 62.11  ?  503  GLN D O   1 
ATOM   9901  C CB  . GLN D  1  503 ? -0.429  2.719   -12.749 1.00 62.87  ?  503  GLN D CB  1 
ATOM   9902  C CG  . GLN D  1  503 ? -1.413  1.699   -13.257 1.00 63.55  ?  503  GLN D CG  1 
ATOM   9903  C CD  . GLN D  1  503 ? -2.750  1.808   -12.568 1.00 63.55  ?  503  GLN D CD  1 
ATOM   9904  O OE1 . GLN D  1  503 ? -3.734  2.249   -13.166 1.00 64.01  ?  503  GLN D OE1 1 
ATOM   9905  N NE2 . GLN D  1  503 ? -2.800  1.397   -11.304 1.00 63.32  ?  503  GLN D NE2 1 
ATOM   9906  N N   . LEU D  1  504 ? 0.820   5.987   -12.733 1.00 60.23  ?  504  LEU D N   1 
ATOM   9907  C CA  . LEU D  1  504 ? 1.501   6.918   -11.840 1.00 59.68  ?  504  LEU D CA  1 
ATOM   9908  C C   . LEU D  1  504 ? 0.513   7.932   -11.265 1.00 60.12  ?  504  LEU D C   1 
ATOM   9909  O O   . LEU D  1  504 ? -0.302  8.506   -11.994 1.00 60.91  ?  504  LEU D O   1 
ATOM   9910  C CB  . LEU D  1  504 ? 2.628   7.635   -12.590 1.00 59.82  ?  504  LEU D CB  1 
ATOM   9911  C CG  . LEU D  1  504 ? 4.077   7.269   -12.266 1.00 59.36  ?  504  LEU D CG  1 
ATOM   9912  C CD1 . LEU D  1  504 ? 5.010   8.257   -12.933 1.00 59.61  ?  504  LEU D CD1 1 
ATOM   9913  C CD2 . LEU D  1  504 ? 4.314   7.250   -10.772 1.00 58.88  ?  504  LEU D CD2 1 
ATOM   9914  N N   . SER D  1  505 ? 0.572   8.136   -9.949  1.00 57.22  ?  505  SER D N   1 
ATOM   9915  C CA  . SER D  1  505 ? -0.215  9.164   -9.278  1.00 58.39  ?  505  SER D CA  1 
ATOM   9916  C C   . SER D  1  505 ? 0.629   10.273  -8.665  1.00 58.95  ?  505  SER D C   1 
ATOM   9917  O O   . SER D  1  505 ? 0.103   11.355  -8.394  1.00 60.46  ?  505  SER D O   1 
ATOM   9918  C CB  . SER D  1  505 ? -1.106  8.539   -8.196  1.00 59.15  ?  505  SER D CB  1 
ATOM   9919  O OG  . SER D  1  505 ? -2.057  9.475   -7.708  1.00 60.72  ?  505  SER D OG  1 
ATOM   9920  N N   . GLN D  1  506 ? 1.898   10.005  -8.363  1.00 54.13  ?  506  GLN D N   1 
ATOM   9921  C CA  . GLN D  1  506 ? 2.823   11.029  -7.898  1.00 54.60  ?  506  GLN D CA  1 
ATOM   9922  C C   . GLN D  1  506 ? 4.175   10.842  -8.571  1.00 53.20  ?  506  GLN D C   1 
ATOM   9923  O O   . GLN D  1  506 ? 4.747   9.750   -8.515  1.00 52.66  ?  506  GLN D O   1 
ATOM   9924  C CB  . GLN D  1  506 ? 2.977   10.978  -6.378  1.00 56.18  ?  506  GLN D CB  1 
ATOM   9925  C CG  . GLN D  1  506 ? 4.150   11.775  -5.867  1.00 57.03  ?  506  GLN D CG  1 
ATOM   9926  C CD  . GLN D  1  506 ? 4.030   12.103  -4.399  1.00 59.78  ?  506  GLN D CD  1 
ATOM   9927  O OE1 . GLN D  1  506 ? 3.261   11.475  -3.674  1.00 60.58  ?  506  GLN D OE1 1 
ATOM   9928  N NE2 . GLN D  1  506 ? 4.791   13.094  -3.950  1.00 61.61  ?  506  GLN D NE2 1 
ATOM   9929  N N   . LEU D  1  507 ? 4.698   11.904  -9.182  1.00 52.82  ?  507  LEU D N   1 
ATOM   9930  C CA  . LEU D  1  507 ? 6.005   11.874  -9.827  1.00 52.01  ?  507  LEU D CA  1 
ATOM   9931  C C   . LEU D  1  507 ? 6.799   13.090  -9.379  1.00 52.51  ?  507  LEU D C   1 
ATOM   9932  O O   . LEU D  1  507 ? 6.323   14.222  -9.497  1.00 53.12  ?  507  LEU D O   1 
ATOM   9933  C CB  . LEU D  1  507 ? 5.880   11.856  -11.357 1.00 51.91  ?  507  LEU D CB  1 
ATOM   9934  C CG  . LEU D  1  507 ? 7.164   11.964  -12.192 1.00 52.12  ?  507  LEU D CG  1 
ATOM   9935  C CD1 . LEU D  1  507 ? 8.079   10.782  -11.935 1.00 52.25  ?  507  LEU D CD1 1 
ATOM   9936  C CD2 . LEU D  1  507 ? 6.834   12.068  -13.675 1.00 53.20  ?  507  LEU D CD2 1 
ATOM   9937  N N   . ASP D  1  508 ? 7.999   12.857  -8.852  1.00 53.50  ?  508  ASP D N   1 
ATOM   9938  C CA  . ASP D  1  508 ? 8.820   13.931  -8.294  1.00 54.31  ?  508  ASP D CA  1 
ATOM   9939  C C   . ASP D  1  508 ? 10.269  13.698  -8.712  1.00 54.05  ?  508  ASP D C   1 
ATOM   9940  O O   . ASP D  1  508 ? 10.961  12.865  -8.119  1.00 54.65  ?  508  ASP D O   1 
ATOM   9941  C CB  . ASP D  1  508 ? 8.683   13.989  -6.776  1.00 56.43  ?  508  ASP D CB  1 
ATOM   9942  C CG  . ASP D  1  508 ? 9.468   15.138  -6.156  1.00 57.73  ?  508  ASP D CG  1 
ATOM   9943  O OD1 . ASP D  1  508 ? 10.013  15.969  -6.917  1.00 56.66  ?  508  ASP D OD1 1 
ATOM   9944  O OD2 . ASP D  1  508 ? 9.529   15.218  -4.904  1.00 60.22  -1 508  ASP D OD2 1 
ATOM   9945  N N   . LEU D  1  509 ? 10.728  14.459  -9.710  1.00 53.63  ?  509  LEU D N   1 
ATOM   9946  C CA  . LEU D  1  509 ? 12.118  14.440  -10.155 1.00 54.15  ?  509  LEU D CA  1 
ATOM   9947  C C   . LEU D  1  509 ? 12.799  15.780  -9.892  1.00 54.50  ?  509  LEU D C   1 
ATOM   9948  O O   . LEU D  1  509 ? 13.758  16.146  -10.572 1.00 54.97  ?  509  LEU D O   1 
ATOM   9949  C CB  . LEU D  1  509 ? 12.205  14.077  -11.637 1.00 54.63  ?  509  LEU D CB  1 
ATOM   9950  C CG  . LEU D  1  509 ? 11.461  12.818  -12.066 1.00 54.70  ?  509  LEU D CG  1 
ATOM   9951  C CD1 . LEU D  1  509 ? 11.717  12.528  -13.526 1.00 56.14  ?  509  LEU D CD1 1 
ATOM   9952  C CD2 . LEU D  1  509 ? 11.897  11.648  -11.207 1.00 55.19  ?  509  LEU D CD2 1 
ATOM   9953  N N   . SER D  1  510 ? 12.320  16.513  -8.892  1.00 58.20  ?  510  SER D N   1 
ATOM   9954  C CA  . SER D  1  510 ? 12.783  17.870  -8.650  1.00 58.89  ?  510  SER D CA  1 
ATOM   9955  C C   . SER D  1  510 ? 14.243  17.892  -8.197  1.00 59.46  ?  510  SER D C   1 
ATOM   9956  O O   . SER D  1  510 ? 14.812  16.880  -7.781  1.00 59.56  ?  510  SER D O   1 
ATOM   9957  C CB  . SER D  1  510 ? 11.917  18.547  -7.593  1.00 60.00  ?  510  SER D CB  1 
ATOM   9958  O OG  . SER D  1  510 ? 12.097  17.908  -6.346  1.00 61.03  ?  510  SER D OG  1 
ATOM   9959  N N   . SER D  1  511 ? 14.844  19.081  -8.291  1.00 61.02  ?  511  SER D N   1 
ATOM   9960  C CA  . SER D  1  511 ? 16.192  19.346  -7.782  1.00 61.77  ?  511  SER D CA  1 
ATOM   9961  C C   . SER D  1  511 ? 17.228  18.433  -8.428  1.00 61.60  ?  511  SER D C   1 
ATOM   9962  O O   . SER D  1  511 ? 18.100  17.879  -7.756  1.00 62.10  ?  511  SER D O   1 
ATOM   9963  C CB  . SER D  1  511 ? 16.248  19.224  -6.258  1.00 62.70  ?  511  SER D CB  1 
ATOM   9964  O OG  . SER D  1  511 ? 15.320  20.097  -5.640  1.00 63.50  ?  511  SER D OG  1 
ATOM   9965  N N   . ASN D  1  512 ? 17.133  18.280  -9.747  1.00 62.22  ?  512  ASN D N   1 
ATOM   9966  C CA  . ASN D  1  512 ? 18.144  17.569  -10.519 1.00 62.77  ?  512  ASN D CA  1 
ATOM   9967  C C   . ASN D  1  512 ? 18.608  18.461  -11.663 1.00 63.28  ?  512  ASN D C   1 
ATOM   9968  O O   . ASN D  1  512 ? 18.253  19.644  -11.715 1.00 63.14  ?  512  ASN D O   1 
ATOM   9969  C CB  . ASN D  1  512 ? 17.599  16.236  -11.040 1.00 62.69  ?  512  ASN D CB  1 
ATOM   9970  C CG  . ASN D  1  512 ? 17.494  15.181  -9.948  1.00 62.53  ?  512  ASN D CG  1 
ATOM   9971  O OD1 . ASN D  1  512 ? 18.486  14.571  -9.561  1.00 63.19  ?  512  ASN D OD1 1 
ATOM   9972  N ND2 . ASN D  1  512 ? 16.285  14.967  -9.447  1.00 61.76  ?  512  ASN D ND2 1 
ATOM   9973  N N   . ARG D  1  513 ? 19.410  17.923  -12.572 1.00 70.30  ?  513  ARG D N   1 
ATOM   9974  C CA  . ARG D  1  513 ? 19.872  18.664  -13.739 1.00 71.01  ?  513  ARG D CA  1 
ATOM   9975  C C   . ARG D  1  513 ? 19.357  18.024  -15.021 1.00 71.66  ?  513  ARG D C   1 
ATOM   9976  O O   . ARG D  1  513 ? 20.074  17.910  -16.015 1.00 72.82  ?  513  ARG D O   1 
ATOM   9977  C CB  . ARG D  1  513 ? 21.395  18.771  -13.753 1.00 71.89  ?  513  ARG D CB  1 
ATOM   9978  C CG  . ARG D  1  513 ? 21.936  19.789  -12.768 1.00 71.78  ?  513  ARG D CG  1 
ATOM   9979  C CD  . ARG D  1  513 ? 22.364  19.112  -11.476 1.00 71.63  ?  513  ARG D CD  1 
ATOM   9980  N NE  . ARG D  1  513 ? 23.710  18.555  -11.572 1.00 72.60  ?  513  ARG D NE  1 
ATOM   9981  C CZ  . ARG D  1  513 ? 24.541  18.413  -10.546 1.00 72.98  ?  513  ARG D CZ  1 
ATOM   9982  N NH1 . ARG D  1  513 ? 24.179  18.739  -9.311  1.00 72.61  ?  513  ARG D NH1 1 
ATOM   9983  N NH2 . ARG D  1  513 ? 25.766  17.933  -10.763 1.00 73.94  ?  513  ARG D NH2 1 
ATOM   9984  N N   . ILE D  1  514 ? 18.092  17.603  -15.006 1.00 60.71  ?  514  ILE D N   1 
ATOM   9985  C CA  . ILE D  1  514 ? 17.484  16.970  -16.170 1.00 61.69  ?  514  ILE D CA  1 
ATOM   9986  C C   . ILE D  1  514 ? 17.186  18.025  -17.229 1.00 61.93  ?  514  ILE D C   1 
ATOM   9987  O O   . ILE D  1  514 ? 16.716  19.131  -16.923 1.00 60.91  ?  514  ILE D O   1 
ATOM   9988  C CB  . ILE D  1  514 ? 16.212  16.208  -15.758 1.00 61.02  ?  514  ILE D CB  1 
ATOM   9989  C CG1 . ILE D  1  514 ? 16.562  15.054  -14.814 1.00 61.03  ?  514  ILE D CG1 1 
ATOM   9990  C CG2 . ILE D  1  514 ? 15.462  15.694  -16.981 1.00 62.22  ?  514  ILE D CG2 1 
ATOM   9991  C CD1 . ILE D  1  514 ? 15.458  14.708  -13.838 1.00 59.54  ?  514  ILE D CD1 1 
ATOM   9992  N N   . THR D  1  515 ? 17.473  17.689  -18.484 1.00 60.88  ?  515  THR D N   1 
ATOM   9993  C CA  . THR D  1  515 ? 17.338  18.578  -19.632 1.00 61.36  ?  515  THR D CA  1 
ATOM   9994  C C   . THR D  1  515 ? 16.317  17.994  -20.613 1.00 62.37  ?  515  THR D C   1 
ATOM   9995  O O   . THR D  1  515 ? 15.666  16.981  -20.338 1.00 62.60  ?  515  THR D O   1 
ATOM   9996  C CB  . THR D  1  515 ? 18.697  18.800  -20.305 1.00 62.40  ?  515  THR D CB  1 
ATOM   9997  O OG1 . THR D  1  515 ? 19.212  17.546  -20.770 1.00 63.93  ?  515  THR D OG1 1 
ATOM   9998  C CG2 . THR D  1  515 ? 19.691  19.416  -19.329 1.00 61.57  ?  515  THR D CG2 1 
ATOM   9999  N N   . GLY D  1  516 ? 16.181  18.643  -21.768 1.00 60.70  ?  516  GLY D N   1 
ATOM   10000 C CA  . GLY D  1  516 ? 15.146  18.281  -22.716 1.00 61.66  ?  516  GLY D CA  1 
ATOM   10001 C C   . GLY D  1  516 ? 13.864  19.044  -22.464 1.00 60.37  ?  516  GLY D C   1 
ATOM   10002 O O   . GLY D  1  516 ? 13.793  19.947  -21.627 1.00 58.83  ?  516  GLY D O   1 
ATOM   10003 N N   . GLU D  1  517 ? 12.827  18.680  -23.215 1.00 64.61  ?  517  GLU D N   1 
ATOM   10004 C CA  . GLU D  1  517 ? 11.552  19.376  -23.121 1.00 63.72  ?  517  GLU D CA  1 
ATOM   10005 C C   . GLU D  1  517 ? 10.396  18.394  -22.959 1.00 64.04  ?  517  GLU D C   1 
ATOM   10006 O O   . GLU D  1  517 ? 10.454  17.253  -23.420 1.00 65.52  ?  517  GLU D O   1 
ATOM   10007 C CB  . GLU D  1  517 ? 11.318  20.272  -24.344 1.00 64.44  ?  517  GLU D CB  1 
ATOM   10008 C CG  . GLU D  1  517 ? 11.680  19.674  -25.677 1.00 66.38  ?  517  GLU D CG  1 
ATOM   10009 C CD  . GLU D  1  517 ? 11.310  20.608  -26.812 1.00 66.77  ?  517  GLU D CD  1 
ATOM   10010 O OE1 . GLU D  1  517 ? 10.119  20.621  -27.188 1.00 66.86  ?  517  GLU D OE1 1 
ATOM   10011 O OE2 . GLU D  1  517 ? 12.196  21.330  -27.326 1.00 67.00  -1 517  GLU D OE2 1 
ATOM   10012 N N   . LEU D  1  518 ? 9.342   18.859  -22.293 1.00 60.46  ?  518  LEU D N   1 
ATOM   10013 C CA  . LEU D  1  518 ? 8.197   18.001  -21.999 1.00 60.62  ?  518  LEU D CA  1 
ATOM   10014 C C   . LEU D  1  518 ? 7.357   17.779  -23.253 1.00 62.36  ?  518  LEU D C   1 
ATOM   10015 O O   . LEU D  1  518 ? 6.967   18.751  -23.913 1.00 62.51  ?  518  LEU D O   1 
ATOM   10016 C CB  . LEU D  1  518 ? 7.338   18.624  -20.905 1.00 59.10  ?  518  LEU D CB  1 
ATOM   10017 C CG  . LEU D  1  518 ? 8.011   18.809  -19.549 1.00 57.48  ?  518  LEU D CG  1 
ATOM   10018 C CD1 . LEU D  1  518 ? 7.041   19.451  -18.579 1.00 56.60  ?  518  LEU D CD1 1 
ATOM   10019 C CD2 . LEU D  1  518 ? 8.515   17.482  -19.015 1.00 57.30  ?  518  LEU D CD2 1 
ATOM   10020 N N   . PRO D  1  519 ? 7.042   16.535  -23.601 1.00 60.83  ?  519  PRO D N   1 
ATOM   10021 C CA  . PRO D  1  519 ? 6.230   16.271  -24.792 1.00 62.45  ?  519  PRO D CA  1 
ATOM   10022 C C   . PRO D  1  519 ? 4.753   16.551  -24.547 1.00 61.78  ?  519  PRO D C   1 
ATOM   10023 O O   . PRO D  1  519 ? 4.297   16.718  -23.417 1.00 60.40  ?  519  PRO D O   1 
ATOM   10024 C CB  . PRO D  1  519 ? 6.465   14.780  -25.042 1.00 64.20  ?  519  PRO D CB  1 
ATOM   10025 C CG  . PRO D  1  519 ? 6.684   14.222  -23.683 1.00 63.11  ?  519  PRO D CG  1 
ATOM   10026 C CD  . PRO D  1  519 ? 7.426   15.289  -22.912 1.00 60.92  ?  519  PRO D CD  1 
ATOM   10027 N N   . GLU D  1  520 ? 3.998   16.597  -25.648 1.00 67.26  ?  520  GLU D N   1 
ATOM   10028 C CA  . GLU D  1  520 ? 2.545   16.570  -25.539 1.00 66.90  ?  520  GLU D CA  1 
ATOM   10029 C C   . GLU D  1  520 ? 2.032   15.202  -25.113 1.00 67.03  ?  520  GLU D C   1 
ATOM   10030 O O   . GLU D  1  520 ? 0.860   15.080  -24.745 1.00 66.34  ?  520  GLU D O   1 
ATOM   10031 C CB  . GLU D  1  520 ? 1.892   16.977  -26.863 1.00 67.77  ?  520  GLU D CB  1 
ATOM   10032 C CG  . GLU D  1  520 ? 2.230   18.393  -27.324 1.00 67.66  ?  520  GLU D CG  1 
ATOM   10033 C CD  . GLU D  1  520 ? 1.438   19.465  -26.589 1.00 66.73  ?  520  GLU D CD  1 
ATOM   10034 O OE1 . GLU D  1  520 ? 0.463   19.113  -25.885 1.00 66.27  ?  520  GLU D OE1 1 
ATOM   10035 O OE2 . GLU D  1  520 ? 1.786   20.661  -26.729 1.00 66.54  -1 520  GLU D OE2 1 
ATOM   10036 N N   . SER D  1  521 ? 2.881   14.178  -25.152 1.00 63.10  ?  521  SER D N   1 
ATOM   10037 C CA  . SER D  1  521 ? 2.519   12.854  -24.671 1.00 63.19  ?  521  SER D CA  1 
ATOM   10038 C C   . SER D  1  521 ? 2.388   12.791  -23.154 1.00 61.79  ?  521  SER D C   1 
ATOM   10039 O O   . SER D  1  521 ? 1.930   11.766  -22.635 1.00 61.36  ?  521  SER D O   1 
ATOM   10040 C CB  . SER D  1  521 ? 3.560   11.844  -25.140 1.00 64.75  ?  521  SER D CB  1 
ATOM   10041 O OG  . SER D  1  521 ? 3.209   10.532  -24.753 1.00 64.43  ?  521  SER D OG  1 
ATOM   10042 N N   . ILE D  1  522 ? 2.816   13.839  -22.437 1.00 62.67  ?  522  ILE D N   1 
ATOM   10043 C CA  . ILE D  1  522 ? 2.746   13.925  -20.979 1.00 60.88  ?  522  ILE D CA  1 
ATOM   10044 C C   . ILE D  1  522 ? 1.307   13.722  -20.546 1.00 59.99  ?  522  ILE D C   1 
ATOM   10045 O O   . ILE D  1  522 ? 1.030   13.353  -19.399 1.00 58.77  ?  522  ILE D O   1 
ATOM   10046 C CB  . ILE D  1  522 ? 3.300   15.270  -20.462 1.00 59.42  ?  522  ILE D CB  1 
ATOM   10047 C CG1 . ILE D  1  522 ? 3.604   15.190  -18.963 1.00 57.48  ?  522  ILE D CG1 1 
ATOM   10048 C CG2 . ILE D  1  522 ? 2.343   16.414  -20.766 1.00 59.23  ?  522  ILE D CG2 1 
ATOM   10049 C CD1 . ILE D  1  522 ? 4.251   16.431  -18.399 1.00 56.19  ?  522  ILE D CD1 1 
ATOM   10050 N N   . SER D  1  523 ? 0.385   13.945  -21.482 1.00 61.69  ?  523  SER D N   1 
ATOM   10051 C CA  . SER D  1  523 ? -1.035  13.797  -21.222 1.00 60.91  ?  523  SER D CA  1 
ATOM   10052 C C   . SER D  1  523 ? -1.424  12.371  -20.864 1.00 60.48  ?  523  SER D C   1 
ATOM   10053 O O   . SER D  1  523 ? -2.524  12.163  -20.345 1.00 59.56  ?  523  SER D O   1 
ATOM   10054 C CB  . SER D  1  523 ? -1.831  14.249  -22.439 1.00 61.81  ?  523  SER D CB  1 
ATOM   10055 O OG  . SER D  1  523 ? -3.202  14.302  -22.121 1.00 61.22  ?  523  SER D OG  1 
ATOM   10056 N N   . ASN D  1  524 ? -0.552  11.392  -21.115 1.00 63.32  ?  524  ASN D N   1 
ATOM   10057 C CA  . ASN D  1  524 ? -0.921  9.991   -20.931 1.00 62.74  ?  524  ASN D CA  1 
ATOM   10058 C C   . ASN D  1  524 ? -1.068  9.605   -19.464 1.00 60.93  ?  524  ASN D C   1 
ATOM   10059 O O   . ASN D  1  524 ? -1.798  8.656   -19.153 1.00 60.04  ?  524  ASN D O   1 
ATOM   10060 C CB  . ASN D  1  524 ? 0.113   9.086   -21.593 1.00 63.91  ?  524  ASN D CB  1 
ATOM   10061 C CG  . ASN D  1  524 ? -0.159  8.878   -23.056 1.00 65.27  ?  524  ASN D CG  1 
ATOM   10062 O OD1 . ASN D  1  524 ? -1.202  9.291   -23.574 1.00 65.25  ?  524  ASN D OD1 1 
ATOM   10063 N ND2 . ASN D  1  524 ? 0.785   8.249   -23.744 1.00 66.40  ?  524  ASN D ND2 1 
ATOM   10064 N N   . ILE D  1  525 ? -0.370  10.281  -18.557 1.00 61.97  ?  525  ILE D N   1 
ATOM   10065 C CA  . ILE D  1  525 ? -0.491  9.973   -17.122 1.00 60.14  ?  525  ILE D CA  1 
ATOM   10066 C C   . ILE D  1  525 ? -1.622  10.847  -16.591 1.00 59.66  ?  525  ILE D C   1 
ATOM   10067 O O   . ILE D  1  525 ? -1.421  11.918  -16.015 1.00 59.52  ?  525  ILE D O   1 
ATOM   10068 C CB  . ILE D  1  525 ? 0.832   10.182  -16.377 1.00 59.60  ?  525  ILE D CB  1 
ATOM   10069 C CG1 . ILE D  1  525 ? 1.449   11.538  -16.720 1.00 61.00  ?  525  ILE D CG1 1 
ATOM   10070 C CG2 . ILE D  1  525 ? 1.810   9.100   -16.738 1.00 59.52  ?  525  ILE D CG2 1 
ATOM   10071 C CD1 . ILE D  1  525 ? 2.636   11.883  -15.866 1.00 59.75  ?  525  ILE D CD1 1 
ATOM   10072 N N   . ASN D  1  526 ? -2.851  10.357  -16.748 1.00 64.09  ?  526  ASN D N   1 
ATOM   10073 C CA  . ASN D  1  526 ? -3.986  11.160  -16.308 1.00 64.05  ?  526  ASN D CA  1 
ATOM   10074 C C   . ASN D  1  526 ? -4.312  10.962  -14.832 1.00 63.23  ?  526  ASN D C   1 
ATOM   10075 O O   . ASN D  1  526 ? -5.012  11.796  -14.248 1.00 63.55  ?  526  ASN D O   1 
ATOM   10076 C CB  . ASN D  1  526 ? -5.213  10.877  -17.176 1.00 64.66  ?  526  ASN D CB  1 
ATOM   10077 C CG  . ASN D  1  526 ? -5.600  9.425   -17.175 1.00 64.32  ?  526  ASN D CG  1 
ATOM   10078 O OD1 . ASN D  1  526 ? -4.986  8.605   -16.494 1.00 63.53  ?  526  ASN D OD1 1 
ATOM   10079 N ND2 . ASN D  1  526 ? -6.635  9.093   -17.936 1.00 64.94  ?  526  ASN D ND2 1 
ATOM   10080 N N   . ARG D  1  527 ? -3.813  9.891   -14.218 1.00 66.01  ?  527  ARG D N   1 
ATOM   10081 C CA  . ARG D  1  527 ? -4.030  9.624   -12.802 1.00 65.55  ?  527  ARG D CA  1 
ATOM   10082 C C   . ARG D  1  527 ? -3.152  10.475  -11.889 1.00 65.58  ?  527  ARG D C   1 
ATOM   10083 O O   . ARG D  1  527 ? -3.293  10.378  -10.664 1.00 65.77  ?  527  ARG D O   1 
ATOM   10084 C CB  . ARG D  1  527 ? -3.786  8.142   -12.514 1.00 64.78  ?  527  ARG D CB  1 
ATOM   10085 C CG  . ARG D  1  527 ? -4.892  7.221   -12.996 1.00 65.05  ?  527  ARG D CG  1 
ATOM   10086 C CD  . ARG D  1  527 ? -4.848  5.888   -12.266 1.00 64.56  ?  527  ARG D CD  1 
ATOM   10087 N NE  . ARG D  1  527 ? -6.107  5.166   -12.401 1.00 65.06  ?  527  ARG D NE  1 
ATOM   10088 C CZ  . ARG D  1  527 ? -7.065  5.158   -11.483 1.00 65.41  ?  527  ARG D CZ  1 
ATOM   10089 N NH1 . ARG D  1  527 ? -6.935  5.819   -10.342 1.00 65.52  ?  527  ARG D NH1 1 
ATOM   10090 N NH2 . ARG D  1  527 ? -8.185  4.476   -11.718 1.00 65.93  ?  527  ARG D NH2 1 
ATOM   10091 N N   . ILE D  1  528 ? -2.267  11.304  -12.454 1.00 60.89  ?  528  ILE D N   1 
ATOM   10092 C CA  . ILE D  1  528 ? -1.309  12.081  -11.671 1.00 61.03  ?  528  ILE D CA  1 
ATOM   10093 C C   . ILE D  1  528 ? -2.057  13.070  -10.782 1.00 62.18  ?  528  ILE D C   1 
ATOM   10094 O O   . ILE D  1  528 ? -3.081  13.641  -11.182 1.00 62.71  ?  528  ILE D O   1 
ATOM   10095 C CB  . ILE D  1  528 ? -0.335  12.800  -12.634 1.00 61.27  ?  528  ILE D CB  1 
ATOM   10096 C CG1 . ILE D  1  528 ? 0.835   13.483  -11.922 1.00 61.20  ?  528  ILE D CG1 1 
ATOM   10097 C CG2 . ILE D  1  528 ? -1.038  13.810  -13.500 1.00 62.05  ?  528  ILE D CG2 1 
ATOM   10098 C CD1 . ILE D  1  528 ? 1.594   12.569  -11.033 1.00 59.92  ?  528  ILE D CD1 1 
ATOM   10099 N N   . SER D  1  529 ? -1.560  13.265  -9.555  1.00 57.67  ?  529  SER D N   1 
ATOM   10100 C CA  . SER D  1  529 ? -2.121  14.284  -8.671  1.00 59.40  ?  529  SER D CA  1 
ATOM   10101 C C   . SER D  1  529 ? -1.039  15.194  -8.091  1.00 60.23  ?  529  SER D C   1 
ATOM   10102 O O   . SER D  1  529 ? -1.327  16.339  -7.727  1.00 61.38  ?  529  SER D O   1 
ATOM   10103 C CB  . SER D  1  529 ? -2.940  13.643  -7.545  1.00 60.44  ?  529  SER D CB  1 
ATOM   10104 O OG  . SER D  1  529 ? -2.177  12.703  -6.815  1.00 60.21  ?  529  SER D OG  1 
ATOM   10105 N N   . LYS D  1  530 ? 0.200   14.706  -7.990  1.00 59.88  ?  530  LYS D N   1 
ATOM   10106 C CA  . LYS D  1  530 ? 1.348   15.538  -7.632  1.00 59.65  ?  530  LYS D CA  1 
ATOM   10107 C C   . LYS D  1  530 ? 2.403   15.432  -8.723  1.00 57.59  ?  530  LYS D C   1 
ATOM   10108 O O   . LYS D  1  530 ? 2.963   14.352  -8.943  1.00 56.21  ?  530  LYS D O   1 
ATOM   10109 C CB  . LYS D  1  530 ? 1.954   15.116  -6.295  1.00 60.52  ?  530  LYS D CB  1 
ATOM   10110 C CG  . LYS D  1  530 ? 1.133   15.481  -5.087  1.00 63.22  ?  530  LYS D CG  1 
ATOM   10111 C CD  . LYS D  1  530 ? 1.976   15.432  -3.814  1.00 65.05  ?  530  LYS D CD  1 
ATOM   10112 C CE  . LYS D  1  530 ? 1.103   15.538  -2.558  1.00 67.64  ?  530  LYS D CE  1 
ATOM   10113 N NZ  . LYS D  1  530 ? 1.719   14.866  -1.368  1.00 68.90  ?  530  LYS D NZ  1 
ATOM   10114 N N   . LEU D  1  531 ? 2.738   16.562  -9.343  1.00 54.15  ?  531  LEU D N   1 
ATOM   10115 C CA  . LEU D  1  531 ? 3.712   16.595  -10.431 1.00 52.72  ?  531  LEU D CA  1 
ATOM   10116 C C   . LEU D  1  531 ? 4.768   17.627  -10.069 1.00 52.83  ?  531  LEU D C   1 
ATOM   10117 O O   . LEU D  1  531 ? 4.506   18.832  -10.123 1.00 53.76  ?  531  LEU D O   1 
ATOM   10118 C CB  . LEU D  1  531 ? 3.047   16.936  -11.765 1.00 52.97  ?  531  LEU D CB  1 
ATOM   10119 C CG  . LEU D  1  531 ? 3.653   16.323  -13.026 1.00 52.41  ?  531  LEU D CG  1 
ATOM   10120 C CD1 . LEU D  1  531 ? 2.660   16.357  -14.161 1.00 53.51  ?  531  LEU D CD1 1 
ATOM   10121 C CD2 . LEU D  1  531 ? 4.871   17.084  -13.410 1.00 52.01  ?  531  LEU D CD2 1 
ATOM   10122 N N   . GLN D  1  532 ? 5.956   17.161  -9.701  1.00 51.54  ?  532  GLN D N   1 
ATOM   10123 C CA  . GLN D  1  532 ? 7.030   18.040  -9.248  1.00 51.98  ?  532  GLN D CA  1 
ATOM   10124 C C   . GLN D  1  532 ? 8.258   17.824  -10.124 1.00 50.68  ?  532  GLN D C   1 
ATOM   10125 O O   . GLN D  1  532 ? 9.044   16.902  -9.883  1.00 50.13  ?  532  GLN D O   1 
ATOM   10126 C CB  . GLN D  1  532 ? 7.354   17.789  -7.782  1.00 53.41  ?  532  GLN D CB  1 
ATOM   10127 C CG  . GLN D  1  532 ? 6.172   17.925  -6.849  1.00 55.78  ?  532  GLN D CG  1 
ATOM   10128 C CD  . GLN D  1  532 ? 6.414   17.248  -5.514  1.00 57.81  ?  532  GLN D CD  1 
ATOM   10129 O OE1 . GLN D  1  532 ? 5.805   16.225  -5.208  1.00 58.06  ?  532  GLN D OE1 1 
ATOM   10130 N NE2 . GLN D  1  532 ? 7.309   17.817  -4.712  1.00 59.30  ?  532  GLN D NE2 1 
ATOM   10131 N N   . LEU D  1  533 ? 8.428   18.685  -11.129 1.00 51.97  ?  533  LEU D N   1 
ATOM   10132 C CA  . LEU D  1  533 ? 9.612   18.686  -11.979 1.00 51.74  ?  533  LEU D CA  1 
ATOM   10133 C C   . LEU D  1  533 ? 10.461  19.940  -11.793 1.00 52.31  ?  533  LEU D C   1 
ATOM   10134 O O   . LEU D  1  533 ? 11.370  20.186  -12.590 1.00 52.49  ?  533  LEU D O   1 
ATOM   10135 C CB  . LEU D  1  533 ? 9.209   18.540  -13.448 1.00 52.07  ?  533  LEU D CB  1 
ATOM   10136 C CG  . LEU D  1  533 ? 8.352   17.322  -13.784 1.00 51.92  ?  533  LEU D CG  1 
ATOM   10137 C CD1 . LEU D  1  533 ? 8.127   17.204  -15.275 1.00 53.18  ?  533  LEU D CD1 1 
ATOM   10138 C CD2 . LEU D  1  533 ? 8.987   16.064  -13.243 1.00 51.30  ?  533  LEU D CD2 1 
ATOM   10139 N N   . ASN D  1  534 ? 10.198  20.720  -10.750 1.00 56.38  ?  534  ASN D N   1 
ATOM   10140 C CA  . ASN D  1  534 ? 10.849  22.004  -10.536 1.00 57.19  ?  534  ASN D CA  1 
ATOM   10141 C C   . ASN D  1  534 ? 12.336  21.837  -10.233 1.00 57.23  ?  534  ASN D C   1 
ATOM   10142 O O   . ASN D  1  534 ? 12.798  20.774  -9.815  1.00 56.84  ?  534  ASN D O   1 
ATOM   10143 C CB  . ASN D  1  534 ? 10.181  22.746  -9.381  1.00 58.53  ?  534  ASN D CB  1 
ATOM   10144 C CG  . ASN D  1  534 ? 10.233  21.962  -8.088  1.00 59.12  ?  534  ASN D CG  1 
ATOM   10145 O OD1 . ASN D  1  534 ? 9.627   20.896  -7.974  1.00 58.75  ?  534  ASN D OD1 1 
ATOM   10146 N ND2 . ASN D  1  534 ? 10.967  22.479  -7.109  1.00 60.16  ?  534  ASN D ND2 1 
ATOM   10147 N N   . GLY D  1  535 ? 13.086  22.917  -10.440 1.00 59.00  ?  535  GLY D N   1 
ATOM   10148 C CA  . GLY D  1  535 ? 14.502  22.921  -10.120 1.00 59.37  ?  535  GLY D CA  1 
ATOM   10149 C C   . GLY D  1  535 ? 15.311  22.026  -11.034 1.00 58.81  ?  535  GLY D C   1 
ATOM   10150 O O   . GLY D  1  535 ? 16.045  21.144  -10.577 1.00 58.77  ?  535  GLY D O   1 
ATOM   10151 N N   . ASN D  1  536 ? 15.176  22.254  -12.337 1.00 59.39  ?  536  ASN D N   1 
ATOM   10152 C CA  . ASN D  1  536 ? 15.798  21.434  -13.364 1.00 59.52  ?  536  ASN D CA  1 
ATOM   10153 C C   . ASN D  1  536 ? 16.223  22.352  -14.500 1.00 60.14  ?  536  ASN D C   1 
ATOM   10154 O O   . ASN D  1  536 ? 16.265  23.577  -14.347 1.00 60.34  ?  536  ASN D O   1 
ATOM   10155 C CB  . ASN D  1  536 ? 14.845  20.324  -13.817 1.00 59.09  ?  536  ASN D CB  1 
ATOM   10156 C CG  . ASN D  1  536 ? 15.085  19.038  -13.078 1.00 58.83  ?  536  ASN D CG  1 
ATOM   10157 O OD1 . ASN D  1  536 ? 16.071  18.351  -13.321 1.00 59.48  ?  536  ASN D OD1 1 
ATOM   10158 N ND2 . ASN D  1  536 ? 14.201  18.715  -12.148 1.00 58.10  ?  536  ASN D ND2 1 
ATOM   10159 N N   . ARG D  1  537 ? 16.560  21.752  -15.644 1.00 65.19  ?  537  ARG D N   1 
ATOM   10160 C CA  . ARG D  1  537 ? 16.954  22.494  -16.836 1.00 65.94  ?  537  ARG D CA  1 
ATOM   10161 C C   . ARG D  1  537 ? 16.047  22.174  -18.024 1.00 66.28  ?  537  ARG D C   1 
ATOM   10162 O O   . ARG D  1  537 ? 16.483  22.221  -19.176 1.00 67.26  ?  537  ARG D O   1 
ATOM   10163 C CB  . ARG D  1  537 ? 18.414  22.209  -17.189 1.00 66.88  ?  537  ARG D CB  1 
ATOM   10164 C CG  . ARG D  1  537 ? 19.333  22.137  -15.987 1.00 66.72  ?  537  ARG D CG  1 
ATOM   10165 C CD  . ARG D  1  537 ? 20.629  22.886  -16.239 1.00 67.56  ?  537  ARG D CD  1 
ATOM   10166 N NE  . ARG D  1  537 ? 21.470  22.194  -17.209 1.00 68.40  ?  537  ARG D NE  1 
ATOM   10167 C CZ  . ARG D  1  537 ? 22.191  22.796  -18.147 1.00 69.22  ?  537  ARG D CZ  1 
ATOM   10168 N NH1 . ARG D  1  537 ? 22.222  24.115  -18.255 1.00 69.33  ?  537  ARG D NH1 1 
ATOM   10169 N NH2 . ARG D  1  537 ? 22.902  22.056  -18.996 1.00 70.05  ?  537  ARG D NH2 1 
ATOM   10170 N N   . LEU D  1  538 ? 14.779  21.865  -17.757 1.00 61.45  ?  538  LEU D N   1 
ATOM   10171 C CA  . LEU D  1  538 ? 13.824  21.612  -18.829 1.00 61.96  ?  538  LEU D CA  1 
ATOM   10172 C C   . LEU D  1  538 ? 13.525  22.894  -19.595 1.00 62.17  ?  538  LEU D C   1 
ATOM   10173 O O   . LEU D  1  538 ? 13.312  23.956  -19.003 1.00 61.53  ?  538  LEU D O   1 
ATOM   10174 C CB  . LEU D  1  538 ? 12.527  21.029  -18.266 1.00 61.28  ?  538  LEU D CB  1 
ATOM   10175 C CG  . LEU D  1  538 ? 12.689  19.844  -17.319 1.00 60.83  ?  538  LEU D CG  1 
ATOM   10176 C CD1 . LEU D  1  538 ? 11.592  19.849  -16.265 1.00 59.75  ?  538  LEU D CD1 1 
ATOM   10177 C CD2 . LEU D  1  538 ? 12.693  18.541  -18.100 1.00 61.95  ?  538  LEU D CD2 1 
ATOM   10178 N N   . SER D  1  539 ? 13.484  22.781  -20.923 1.00 62.80  ?  539  SER D N   1 
ATOM   10179 C CA  . SER D  1  539 ? 13.357  23.933  -21.807 1.00 63.16  ?  539  SER D CA  1 
ATOM   10180 C C   . SER D  1  539 ? 12.188  23.736  -22.762 1.00 63.85  ?  539  SER D C   1 
ATOM   10181 O O   . SER D  1  539 ? 11.379  22.824  -22.574 1.00 63.92  ?  539  SER D O   1 
ATOM   10182 C CB  . SER D  1  539 ? 14.660  24.180  -22.574 1.00 64.03  ?  539  SER D CB  1 
ATOM   10183 O OG  . SER D  1  539 ? 15.039  23.058  -23.352 1.00 65.21  ?  539  SER D OG  1 
ATOM   10184 N N   . GLY D  1  540 ? 12.061  24.614  -23.755 1.00 65.13  ?  540  GLY D N   1 
ATOM   10185 C CA  . GLY D  1  540 ? 10.958  24.549  -24.692 1.00 65.92  ?  540  GLY D CA  1 
ATOM   10186 C C   . GLY D  1  540 ? 9.672   25.057  -24.061 1.00 65.21  ?  540  GLY D C   1 
ATOM   10187 O O   . GLY D  1  540 ? 9.658   25.601  -22.959 1.00 64.13  ?  540  GLY D O   1 
ATOM   10188 N N   . LYS D  1  541 ? 8.573   24.868  -24.784 1.00 64.96  ?  541  LYS D N   1 
ATOM   10189 C CA  . LYS D  1  541 ? 7.291   25.360  -24.302 1.00 64.64  ?  541  LYS D CA  1 
ATOM   10190 C C   . LYS D  1  541 ? 6.604   24.314  -23.429 1.00 64.35  ?  541  LYS D C   1 
ATOM   10191 O O   . LYS D  1  541 ? 6.880   23.114  -23.514 1.00 64.72  ?  541  LYS D O   1 
ATOM   10192 C CB  . LYS D  1  541 ? 6.375   25.754  -25.463 1.00 65.78  ?  541  LYS D CB  1 
ATOM   10193 C CG  . LYS D  1  541 ? 5.793   24.585  -26.245 1.00 66.96  ?  541  LYS D CG  1 
ATOM   10194 C CD  . LYS D  1  541 ? 4.783   25.066  -27.279 1.00 68.03  ?  541  LYS D CD  1 
ATOM   10195 C CE  . LYS D  1  541 ? 4.565   24.034  -28.381 1.00 69.34  ?  541  LYS D CE  1 
ATOM   10196 N NZ  . LYS D  1  541 ? 5.698   23.979  -29.358 1.00 69.91  ?  541  LYS D NZ  1 
ATOM   10197 N N   . ILE D  1  542 ? 5.702   24.796  -22.578 1.00 61.58  ?  542  ILE D N   1 
ATOM   10198 C CA  . ILE D  1  542 ? 4.903   23.941  -21.704 1.00 61.41  ?  542  ILE D CA  1 
ATOM   10199 C C   . ILE D  1  542 ? 3.813   23.300  -22.554 1.00 62.69  ?  542  ILE D C   1 
ATOM   10200 O O   . ILE D  1  542 ? 3.007   24.018  -23.164 1.00 63.43  ?  542  ILE D O   1 
ATOM   10201 C CB  . ILE D  1  542 ? 4.305   24.738  -20.534 1.00 60.74  ?  542  ILE D CB  1 
ATOM   10202 C CG1 . ILE D  1  542 ? 5.415   25.262  -19.626 1.00 59.52  ?  542  ILE D CG1 1 
ATOM   10203 C CG2 . ILE D  1  542 ? 3.342   23.883  -19.746 1.00 60.92  ?  542  ILE D CG2 1 
ATOM   10204 C CD1 . ILE D  1  542 ? 4.924   25.743  -18.283 1.00 58.98  ?  542  ILE D CD1 1 
ATOM   10205 N N   . PRO D  1  543 ? 3.750   21.971  -22.633 1.00 61.73  ?  543  PRO D N   1 
ATOM   10206 C CA  . PRO D  1  543 ? 2.784   21.338  -23.537 1.00 62.93  ?  543  PRO D CA  1 
ATOM   10207 C C   . PRO D  1  543 ? 1.357   21.587  -23.085 1.00 63.02  ?  543  PRO D C   1 
ATOM   10208 O O   . PRO D  1  543 ? 1.053   21.593  -21.890 1.00 62.23  ?  543  PRO D O   1 
ATOM   10209 C CB  . PRO D  1  543 ? 3.142   19.850  -23.454 1.00 63.11  ?  543  PRO D CB  1 
ATOM   10210 C CG  . PRO D  1  543 ? 3.774   19.698  -22.113 1.00 61.79  ?  543  PRO D CG  1 
ATOM   10211 C CD  . PRO D  1  543 ? 4.515   20.981  -21.856 1.00 61.02  ?  543  PRO D CD  1 
ATOM   10212 N N   . SER D  1  544 ? 0.471   21.782  -24.058 1.00 64.62  ?  544  SER D N   1 
ATOM   10213 C CA  . SER D  1  544 ? -0.933  21.959  -23.723 1.00 64.90  ?  544  SER D CA  1 
ATOM   10214 C C   . SER D  1  544 ? -1.593  20.660  -23.285 1.00 64.51  ?  544  SER D C   1 
ATOM   10215 O O   . SER D  1  544 ? -2.731  20.699  -22.810 1.00 64.43  ?  544  SER D O   1 
ATOM   10216 C CB  . SER D  1  544 ? -1.685  22.554  -24.909 1.00 66.20  ?  544  SER D CB  1 
ATOM   10217 O OG  . SER D  1  544 ? -1.835  21.597  -25.936 1.00 66.85  ?  544  SER D OG  1 
ATOM   10218 N N   . GLY D  1  545 ? -0.913  19.520  -23.426 1.00 65.26  ?  545  GLY D N   1 
ATOM   10219 C CA  . GLY D  1  545 ? -1.453  18.260  -22.946 1.00 64.84  ?  545  GLY D CA  1 
ATOM   10220 C C   . GLY D  1  545 ? -1.617  18.190  -21.441 1.00 63.53  ?  545  GLY D C   1 
ATOM   10221 O O   . GLY D  1  545 ? -2.292  17.281  -20.943 1.00 63.07  ?  545  GLY D O   1 
ATOM   10222 N N   . ILE D  1  546 ? -0.995  19.116  -20.703 1.00 62.43  ?  546  ILE D N   1 
ATOM   10223 C CA  . ILE D  1  546 ? -1.219  19.208  -19.267 1.00 61.36  ?  546  ILE D CA  1 
ATOM   10224 C C   . ILE D  1  546 ? -2.670  19.557  -18.956 1.00 61.58  ?  546  ILE D C   1 
ATOM   10225 O O   . ILE D  1  546 ? -3.160  19.259  -17.860 1.00 60.93  ?  546  ILE D O   1 
ATOM   10226 C CB  . ILE D  1  546 ? -0.234  20.233  -18.663 1.00 60.91  ?  546  ILE D CB  1 
ATOM   10227 C CG1 . ILE D  1  546 ? 1.200   19.854  -19.027 1.00 60.69  ?  546  ILE D CG1 1 
ATOM   10228 C CG2 . ILE D  1  546 ? -0.364  20.308  -17.157 1.00 60.00  ?  546  ILE D CG2 1 
ATOM   10229 C CD1 . ILE D  1  546 ? 2.247   20.586  -18.219 1.00 59.88  ?  546  ILE D CD1 1 
ATOM   10230 N N   . ARG D  1  547 ? -3.388  20.149  -19.918 1.00 66.01  ?  547  ARG D N   1 
ATOM   10231 C CA  . ARG D  1  547 ? -4.799  20.471  -19.714 1.00 66.38  ?  547  ARG D CA  1 
ATOM   10232 C C   . ARG D  1  547 ? -5.613  19.243  -19.325 1.00 65.88  ?  547  ARG D C   1 
ATOM   10233 O O   . ARG D  1  547 ? -6.624  19.369  -18.624 1.00 65.85  ?  547  ARG D O   1 
ATOM   10234 C CB  . ARG D  1  547 ? -5.387  21.109  -20.974 1.00 67.73  ?  547  ARG D CB  1 
ATOM   10235 C CG  . ARG D  1  547 ? -5.579  20.129  -22.119 1.00 68.14  ?  547  ARG D CG  1 
ATOM   10236 C CD  . ARG D  1  547 ? -6.200  20.783  -23.341 1.00 69.59  ?  547  ARG D CD  1 
ATOM   10237 N NE  . ARG D  1  547 ? -6.943  19.816  -24.142 1.00 70.19  ?  547  ARG D NE  1 
ATOM   10238 C CZ  . ARG D  1  547 ? -6.417  19.088  -25.119 1.00 70.52  ?  547  ARG D CZ  1 
ATOM   10239 N NH1 . ARG D  1  547 ? -5.142  19.207  -25.462 1.00 70.35  ?  547  ARG D NH1 1 
ATOM   10240 N NH2 . ARG D  1  547 ? -7.187  18.217  -25.766 1.00 71.12  ?  547  ARG D NH2 1 
ATOM   10241 N N   . LEU D  1  548 ? -5.198  18.057  -19.765 1.00 59.94  ?  548  LEU D N   1 
ATOM   10242 C CA  . LEU D  1  548 ? -5.975  16.841  -19.567 1.00 59.59  ?  548  LEU D CA  1 
ATOM   10243 C C   . LEU D  1  548 ? -5.625  16.104  -18.278 1.00 58.47  ?  548  LEU D C   1 
ATOM   10244 O O   . LEU D  1  548 ? -6.241  15.072  -17.987 1.00 58.12  ?  548  LEU D O   1 
ATOM   10245 C CB  . LEU D  1  548 ? -5.794  15.903  -20.765 1.00 60.77  ?  548  LEU D CB  1 
ATOM   10246 C CG  . LEU D  1  548 ? -6.207  16.463  -22.126 1.00 63.80  ?  548  LEU D CG  1 
ATOM   10247 C CD1 . LEU D  1  548 ? -6.122  15.391  -23.195 1.00 65.47  ?  548  LEU D CD1 1 
ATOM   10248 C CD2 . LEU D  1  548 ? -7.606  17.038  -22.059 1.00 66.83  ?  548  LEU D CD2 1 
ATOM   10249 N N   . LEU D  1  549 ? -4.667  16.604  -17.499 1.00 62.13  ?  549  LEU D N   1 
ATOM   10250 C CA  . LEU D  1  549 ? -4.330  15.998  -16.209 1.00 61.26  ?  549  LEU D CA  1 
ATOM   10251 C C   . LEU D  1  549 ? -5.240  16.587  -15.128 1.00 61.42  ?  549  LEU D C   1 
ATOM   10252 O O   . LEU D  1  549 ? -4.824  17.352  -14.255 1.00 61.46  ?  549  LEU D O   1 
ATOM   10253 C CB  . LEU D  1  549 ? -2.854  16.215  -15.894 1.00 60.84  ?  549  LEU D CB  1 
ATOM   10254 C CG  . LEU D  1  549 ? -1.888  16.031  -17.070 1.00 61.24  ?  549  LEU D CG  1 
ATOM   10255 C CD1 . LEU D  1  549 ? -0.456  16.347  -16.671 1.00 60.79  ?  549  LEU D CD1 1 
ATOM   10256 C CD2 . LEU D  1  549 ? -1.986  14.625  -17.630 1.00 61.44  ?  549  LEU D CD2 1 
ATOM   10257 N N   . THR D  1  550 ? -6.518  16.199  -15.199 1.00 63.60  ?  550  THR D N   1 
ATOM   10258 C CA  . THR D  1  550 ? -7.548  16.864  -14.402 1.00 64.17  ?  550  THR D CA  1 
ATOM   10259 C C   . THR D  1  550 ? -7.469  16.501  -12.923 1.00 64.06  ?  550  THR D C   1 
ATOM   10260 O O   . THR D  1  550 ? -7.889  17.298  -12.074 1.00 64.77  ?  550  THR D O   1 
ATOM   10261 C CB  . THR D  1  550 ? -8.933  16.525  -14.946 1.00 64.63  ?  550  THR D CB  1 
ATOM   10262 O OG1 . THR D  1  550 ? -9.222  15.146  -14.684 1.00 64.11  ?  550  THR D OG1 1 
ATOM   10263 C CG2 . THR D  1  550 ? -8.984  16.772  -16.440 1.00 65.07  ?  550  THR D CG2 1 
ATOM   10264 N N   . ASN D  1  551 ? -6.950  15.314  -12.596 1.00 65.87  ?  551  ASN D N   1 
ATOM   10265 C CA  . ASN D  1  551 ? -6.786  14.897  -11.206 1.00 66.02  ?  551  ASN D CA  1 
ATOM   10266 C C   . ASN D  1  551 ? -5.646  15.616  -10.496 1.00 66.36  ?  551  ASN D C   1 
ATOM   10267 O O   . ASN D  1  551 ? -5.396  15.326  -9.320  1.00 66.94  ?  551  ASN D O   1 
ATOM   10268 C CB  . ASN D  1  551 ? -6.564  13.385  -11.134 1.00 65.16  ?  551  ASN D CB  1 
ATOM   10269 C CG  . ASN D  1  551 ? -7.837  12.628  -10.828 1.00 65.35  ?  551  ASN D CG  1 
ATOM   10270 O OD1 . ASN D  1  551 ? -8.593  12.269  -11.733 1.00 65.21  ?  551  ASN D OD1 1 
ATOM   10271 N ND2 . ASN D  1  551 ? -8.093  12.395  -9.544  1.00 65.92  ?  551  ASN D ND2 1 
ATOM   10272 N N   . LEU D  1  552 ? -4.977  16.554  -11.165 1.00 61.68  ?  552  LEU D N   1 
ATOM   10273 C CA  . LEU D  1  552 ? -3.814  17.229  -10.603 1.00 61.90  ?  552  LEU D CA  1 
ATOM   10274 C C   . LEU D  1  552 ? -4.232  18.128  -9.445  1.00 63.30  ?  552  LEU D C   1 
ATOM   10275 O O   . LEU D  1  552 ? -5.100  18.993  -9.603  1.00 63.81  ?  552  LEU D O   1 
ATOM   10276 C CB  . LEU D  1  552 ? -3.120  18.047  -11.691 1.00 61.39  ?  552  LEU D CB  1 
ATOM   10277 C CG  . LEU D  1  552 ? -1.706  17.659  -12.123 1.00 60.47  ?  552  LEU D CG  1 
ATOM   10278 C CD1 . LEU D  1  552 ? -1.186  18.624  -13.184 1.00 60.39  ?  552  LEU D CD1 1 
ATOM   10279 C CD2 . LEU D  1  552 ? -0.772  17.612  -10.922 1.00 60.47  ?  552  LEU D CD2 1 
ATOM   10280 N N   . GLU D  1  553 ? -3.615  17.920  -8.280  1.00 61.98  ?  553  GLU D N   1 
ATOM   10281 C CA  . GLU D  1  553 ? -3.808  18.786  -7.122  1.00 63.72  ?  553  GLU D CA  1 
ATOM   10282 C C   . GLU D  1  553 ? -2.668  19.770  -6.909  1.00 63.96  ?  553  GLU D C   1 
ATOM   10283 O O   . GLU D  1  553 ? -2.903  20.878  -6.418  1.00 64.93  ?  553  GLU D O   1 
ATOM   10284 C CB  . GLU D  1  553 ? -3.956  17.951  -5.845  1.00 65.22  ?  553  GLU D CB  1 
ATOM   10285 C CG  . GLU D  1  553 ? -5.084  16.952  -5.866  1.00 64.81  ?  553  GLU D CG  1 
ATOM   10286 C CD  . GLU D  1  553 ? -5.004  15.985  -4.707  1.00 65.86  ?  553  GLU D CD  1 
ATOM   10287 O OE1 . GLU D  1  553 ? -4.195  16.233  -3.786  1.00 67.41  ?  553  GLU D OE1 1 
ATOM   10288 O OE2 . GLU D  1  553 ? -5.751  14.983  -4.716  1.00 65.10  -1 553  GLU D OE2 1 
ATOM   10289 N N   . TYR D  1  554 ? -1.446  19.391  -7.272  1.00 59.54  ?  554  TYR D N   1 
ATOM   10290 C CA  . TYR D  1  554 ? -0.248  20.147  -6.932  1.00 59.69  ?  554  TYR D CA  1 
ATOM   10291 C C   . TYR D  1  554 ? 0.694   20.098  -8.126  1.00 57.65  ?  554  TYR D C   1 
ATOM   10292 O O   . TYR D  1  554 ? 1.145   19.013  -8.510  1.00 56.45  ?  554  TYR D O   1 
ATOM   10293 C CB  . TYR D  1  554 ? 0.406   19.554  -5.680  1.00 61.09  ?  554  TYR D CB  1 
ATOM   10294 C CG  . TYR D  1  554 ? 1.628   20.278  -5.164  1.00 61.72  ?  554  TYR D CG  1 
ATOM   10295 C CD1 . TYR D  1  554 ? 2.879   20.060  -5.730  1.00 60.19  ?  554  TYR D CD1 1 
ATOM   10296 C CD2 . TYR D  1  554 ? 1.540   21.147  -4.082  1.00 63.93  ?  554  TYR D CD2 1 
ATOM   10297 C CE1 . TYR D  1  554 ? 3.999   20.705  -5.253  1.00 60.76  ?  554  TYR D CE1 1 
ATOM   10298 C CE2 . TYR D  1  554 ? 2.657   21.794  -3.596  1.00 64.45  ?  554  TYR D CE2 1 
ATOM   10299 C CZ  . TYR D  1  554 ? 3.883   21.569  -4.186  1.00 62.84  ?  554  TYR D CZ  1 
ATOM   10300 O OH  . TYR D  1  554 ? 5.002   22.208  -3.714  1.00 63.05  ?  554  TYR D OH  1 
ATOM   10301 N N   . LEU D  1  555 ? 0.988   21.260  -8.716  1.00 59.83  ?  555  LEU D N   1 
ATOM   10302 C CA  . LEU D  1  555 ? 1.802   21.341  -9.927  1.00 58.32  ?  555  LEU D CA  1 
ATOM   10303 C C   . LEU D  1  555 ? 2.956   22.304  -9.706  1.00 58.27  ?  555  LEU D C   1 
ATOM   10304 O O   . LEU D  1  555 ? 2.740   23.468  -9.358  1.00 59.00  ?  555  LEU D O   1 
ATOM   10305 C CB  . LEU D  1  555 ? 0.967   21.795  -11.130 1.00 58.12  ?  555  LEU D CB  1 
ATOM   10306 C CG  . LEU D  1  555 ? 1.685   21.789  -12.476 1.00 57.22  ?  555  LEU D CG  1 
ATOM   10307 C CD1 . LEU D  1  555 ? 2.256   20.409  -12.743 1.00 56.31  ?  555  LEU D CD1 1 
ATOM   10308 C CD2 . LEU D  1  555 ? 0.744   22.207  -13.595 1.00 57.72  ?  555  LEU D CD2 1 
ATOM   10309 N N   . ASP D  1  556 ? 4.177   21.828  -9.927  1.00 58.29  ?  556  ASP D N   1 
ATOM   10310 C CA  . ASP D  1  556 ? 5.377   22.631  -9.715  1.00 58.16  ?  556  ASP D CA  1 
ATOM   10311 C C   . ASP D  1  556 ? 6.306   22.433  -10.904 1.00 56.76  ?  556  ASP D C   1 
ATOM   10312 O O   . ASP D  1  556 ? 6.873   21.350  -11.077 1.00 55.91  ?  556  ASP D O   1 
ATOM   10313 C CB  . ASP D  1  556 ? 6.067   22.236  -8.410  1.00 59.01  ?  556  ASP D CB  1 
ATOM   10314 C CG  . ASP D  1  556 ? 7.038   23.288  -7.921  1.00 59.42  ?  556  ASP D CG  1 
ATOM   10315 O OD1 . ASP D  1  556 ? 7.380   24.197  -8.707  1.00 58.70  ?  556  ASP D OD1 1 
ATOM   10316 O OD2 . ASP D  1  556 ? 7.461   23.208  -6.747  1.00 60.60  -1 556  ASP D OD2 1 
ATOM   10317 N N   . LEU D  1  557 ? 6.460   23.474  -11.726 1.00 56.89  ?  557  LEU D N   1 
ATOM   10318 C CA  . LEU D  1  557 ? 7.377   23.446  -12.862 1.00 56.20  ?  557  LEU D CA  1 
ATOM   10319 C C   . LEU D  1  557 ? 8.420   24.548  -12.802 1.00 56.25  ?  557  LEU D C   1 
ATOM   10320 O O   . LEU D  1  557 ? 9.127   24.785  -13.788 1.00 56.04  ?  557  LEU D O   1 
ATOM   10321 C CB  . LEU D  1  557 ? 6.604   23.578  -14.169 1.00 56.40  ?  557  LEU D CB  1 
ATOM   10322 C CG  . LEU D  1  557 ? 5.538   22.538  -14.469 1.00 56.73  ?  557  LEU D CG  1 
ATOM   10323 C CD1 . LEU D  1  557 ? 4.844   22.848  -15.781 1.00 57.51  ?  557  LEU D CD1 1 
ATOM   10324 C CD2 . LEU D  1  557 ? 6.167   21.167  -14.520 1.00 56.13  ?  557  LEU D CD2 1 
ATOM   10325 N N   . SER D  1  558 ? 8.537   25.215  -11.674 1.00 60.55  ?  558  SER D N   1 
ATOM   10326 C CA  . SER D  1  558 ? 9.365   26.394  -11.549 1.00 60.90  ?  558  SER D CA  1 
ATOM   10327 C C   . SER D  1  558 ? 10.858  26.050  -11.478 1.00 60.84  ?  558  SER D C   1 
ATOM   10328 O O   . SER D  1  558 ? 11.262  24.886  -11.437 1.00 60.46  ?  558  SER D O   1 
ATOM   10329 C CB  . SER D  1  558 ? 8.859   27.183  -10.356 1.00 61.90  ?  558  SER D CB  1 
ATOM   10330 O OG  . SER D  1  558 ? 9.079   26.469  -9.181  1.00 62.56  ?  558  SER D OG  1 
ATOM   10331 N N   . SER D  1  559 ? 11.682  27.103  -11.489 1.00 63.17  ?  559  SER D N   1 
ATOM   10332 C CA  . SER D  1  559 ? 13.145  27.010  -11.560 1.00 63.45  ?  559  SER D CA  1 
ATOM   10333 C C   . SER D  1  559 ? 13.585  26.082  -12.697 1.00 62.69  ?  559  SER D C   1 
ATOM   10334 O O   . SER D  1  559 ? 14.277  25.079  -12.507 1.00 62.53  ?  559  SER D O   1 
ATOM   10335 C CB  . SER D  1  559 ? 13.736  26.575  -10.215 1.00 64.28  ?  559  SER D CB  1 
ATOM   10336 O OG  . SER D  1  559 ? 13.791  27.677  -9.326  1.00 65.52  ?  559  SER D OG  1 
ATOM   10337 N N   . ASN D  1  560 ? 13.165  26.453  -13.904 1.00 62.21  ?  560  ASN D N   1 
ATOM   10338 C CA  . ASN D  1  560 ? 13.407  25.672  -15.106 1.00 61.99  ?  560  ASN D CA  1 
ATOM   10339 C C   . ASN D  1  560 ? 13.714  26.648  -16.234 1.00 62.46  ?  560  ASN D C   1 
ATOM   10340 O O   . ASN D  1  560 ? 13.978  27.831  -15.997 1.00 62.82  ?  560  ASN D O   1 
ATOM   10341 C CB  . ASN D  1  560 ? 12.212  24.757  -15.404 1.00 61.53  ?  560  ASN D CB  1 
ATOM   10342 C CG  . ASN D  1  560 ? 12.505  23.304  -15.087 1.00 61.25  ?  560  ASN D CG  1 
ATOM   10343 O OD1 . ASN D  1  560 ? 13.340  22.674  -15.730 1.00 61.58  ?  560  ASN D OD1 1 
ATOM   10344 N ND2 . ASN D  1  560 ? 11.817  22.765  -14.091 1.00 60.82  ?  560  ASN D ND2 1 
ATOM   10345 N N   . ARG D  1  561 ? 13.708  26.153  -17.473 1.00 64.45  ?  561  ARG D N   1 
ATOM   10346 C CA  . ARG D  1  561 ? 14.017  26.975  -18.638 1.00 65.08  ?  561  ARG D CA  1 
ATOM   10347 C C   . ARG D  1  561 ? 12.877  26.979  -19.656 1.00 65.25  ?  561  ARG D C   1 
ATOM   10348 O O   . ARG D  1  561 ? 13.109  27.174  -20.851 1.00 65.97  ?  561  ARG D O   1 
ATOM   10349 C CB  . ARG D  1  561 ? 15.319  26.507  -19.290 1.00 65.77  ?  561  ARG D CB  1 
ATOM   10350 C CG  . ARG D  1  561 ? 16.500  26.459  -18.331 1.00 65.82  ?  561  ARG D CG  1 
ATOM   10351 C CD  . ARG D  1  561 ? 17.828  26.488  -19.069 1.00 66.74  ?  561  ARG D CD  1 
ATOM   10352 N NE  . ARG D  1  561 ? 18.015  25.310  -19.911 1.00 67.26  ?  561  ARG D NE  1 
ATOM   10353 C CZ  . ARG D  1  561 ? 19.186  24.900  -20.385 1.00 68.12  ?  561  ARG D CZ  1 
ATOM   10354 N NH1 . ARG D  1  561 ? 20.304  25.564  -20.132 1.00 68.47  ?  561  ARG D NH1 1 
ATOM   10355 N NH2 . ARG D  1  561 ? 19.233  23.807  -21.145 1.00 68.83  ?  561  ARG D NH2 1 
ATOM   10356 N N   . PHE D  1  562 ? 11.640  26.774  -19.195 1.00 62.47  ?  562  PHE D N   1 
ATOM   10357 C CA  . PHE D  1  562 ? 10.476  26.886  -20.071 1.00 62.86  ?  562  PHE D CA  1 
ATOM   10358 C C   . PHE D  1  562 ? 10.398  28.299  -20.636 1.00 63.21  ?  562  PHE D C   1 
ATOM   10359 O O   . PHE D  1  562 ? 10.562  29.276  -19.904 1.00 62.94  ?  562  PHE D O   1 
ATOM   10360 C CB  . PHE D  1  562 ? 9.196   26.540  -19.306 1.00 62.49  ?  562  PHE D CB  1 
ATOM   10361 C CG  . PHE D  1  562 ? 9.120   25.101  -18.862 1.00 62.25  ?  562  PHE D CG  1 
ATOM   10362 C CD1 . PHE D  1  562 ? 8.974   24.081  -19.793 1.00 62.95  ?  562  PHE D CD1 1 
ATOM   10363 C CD2 . PHE D  1  562 ? 9.192   24.768  -17.515 1.00 61.52  ?  562  PHE D CD2 1 
ATOM   10364 C CE1 . PHE D  1  562 ? 8.902   22.752  -19.389 1.00 62.85  ?  562  PHE D CE1 1 
ATOM   10365 C CE2 . PHE D  1  562 ? 9.123   23.445  -17.106 1.00 61.29  ?  562  PHE D CE2 1 
ATOM   10366 C CZ  . PHE D  1  562 ? 8.978   22.435  -18.045 1.00 61.91  ?  562  PHE D CZ  1 
ATOM   10367 N N   . SER D  1  563 ? 10.165  28.418  -21.945 1.00 69.32  ?  563  SER D N   1 
ATOM   10368 C CA  . SER D  1  563 ? 10.519  29.656  -22.624 1.00 69.74  ?  563  SER D CA  1 
ATOM   10369 C C   . SER D  1  563 ? 9.441   30.283  -23.505 1.00 70.36  ?  563  SER D C   1 
ATOM   10370 O O   . SER D  1  563 ? 9.681   31.368  -24.053 1.00 70.71  ?  563  SER D O   1 
ATOM   10371 C CB  . SER D  1  563 ? 11.788  29.446  -23.473 1.00 70.34  ?  563  SER D CB  1 
ATOM   10372 O OG  . SER D  1  563 ? 11.519  28.696  -24.649 1.00 71.16  ?  563  SER D OG  1 
ATOM   10373 N N   . PHE D  1  564 ? 8.275   29.671  -23.656 1.00 71.77  ?  564  PHE D N   1 
ATOM   10374 C CA  . PHE D  1  564 ? 7.270   30.248  -24.545 1.00 72.60  ?  564  PHE D CA  1 
ATOM   10375 C C   . PHE D  1  564 ? 6.000   30.600  -23.765 1.00 72.46  ?  564  PHE D C   1 
ATOM   10376 O O   . PHE D  1  564 ? 5.959   30.528  -22.535 1.00 71.68  ?  564  PHE D O   1 
ATOM   10377 C CB  . PHE D  1  564 ? 7.005   29.306  -25.718 1.00 73.62  ?  564  PHE D CB  1 
ATOM   10378 C CG  . PHE D  1  564 ? 8.014   29.433  -26.825 1.00 74.23  ?  564  PHE D CG  1 
ATOM   10379 C CD1 . PHE D  1  564 ? 7.916   30.457  -27.749 1.00 74.87  ?  564  PHE D CD1 1 
ATOM   10380 C CD2 . PHE D  1  564 ? 9.064   28.537  -26.934 1.00 74.27  ?  564  PHE D CD2 1 
ATOM   10381 C CE1 . PHE D  1  564 ? 8.842   30.583  -28.770 1.00 75.48  ?  564  PHE D CE1 1 
ATOM   10382 C CE2 . PHE D  1  564 ? 9.991   28.656  -27.950 1.00 74.97  ?  564  PHE D CE2 1 
ATOM   10383 C CZ  . PHE D  1  564 ? 9.880   29.681  -28.870 1.00 75.54  ?  564  PHE D CZ  1 
ATOM   10384 N N   . GLU D  1  565 ? 4.967   31.016  -24.493 1.00 74.74  ?  565  GLU D N   1 
ATOM   10385 C CA  . GLU D  1  565 ? 3.752   31.531  -23.873 1.00 74.89  ?  565  GLU D CA  1 
ATOM   10386 C C   . GLU D  1  565 ? 2.957   30.424  -23.181 1.00 74.88  ?  565  GLU D C   1 
ATOM   10387 O O   . GLU D  1  565 ? 2.955   29.266  -23.609 1.00 75.23  ?  565  GLU D O   1 
ATOM   10388 C CB  . GLU D  1  565 ? 2.879   32.224  -24.918 1.00 76.11  ?  565  GLU D CB  1 
ATOM   10389 C CG  . GLU D  1  565 ? 3.002   31.634  -26.315 1.00 77.11  ?  565  GLU D CG  1 
ATOM   10390 C CD  . GLU D  1  565 ? 4.019   32.366  -27.191 1.00 77.20  ?  565  GLU D CD  1 
ATOM   10391 O OE1 . GLU D  1  565 ? 4.996   32.933  -26.651 1.00 76.31  ?  565  GLU D OE1 1 
ATOM   10392 O OE2 . GLU D  1  565 ? 3.837   32.381  -28.427 1.00 78.29  -1 565  GLU D OE2 1 
ATOM   10393 N N   . ILE D  1  566 ? 2.277   30.799  -22.098 1.00 68.68  ?  566  ILE D N   1 
ATOM   10394 C CA  . ILE D  1  566 ? 1.518   29.847  -21.274 1.00 68.69  ?  566  ILE D CA  1 
ATOM   10395 C C   . ILE D  1  566 ? 0.350   29.295  -22.084 1.00 70.09  ?  566  ILE D C   1 
ATOM   10396 O O   . ILE D  1  566 ? -0.369  30.075  -22.737 1.00 71.05  ?  566  ILE D O   1 
ATOM   10397 C CB  . ILE D  1  566 ? 1.016   30.532  -19.999 1.00 68.31  ?  566  ILE D CB  1 
ATOM   10398 C CG1 . ILE D  1  566 ? 2.185   30.927  -19.098 1.00 67.19  ?  566  ILE D CG1 1 
ATOM   10399 C CG2 . ILE D  1  566 ? 0.038   29.628  -19.257 1.00 68.58  ?  566  ILE D CG2 1 
ATOM   10400 C CD1 . ILE D  1  566 ? 1.850   30.995  -17.618 1.00 66.78  ?  566  ILE D CD1 1 
ATOM   10401 N N   . PRO D  1  567 ? 0.103   27.986  -22.058 1.00 69.85  ?  567  PRO D N   1 
ATOM   10402 C CA  . PRO D  1  567 ? -1.020  27.421  -22.816 1.00 71.41  ?  567  PRO D CA  1 
ATOM   10403 C C   . PRO D  1  567 ? -2.331  28.069  -22.412 1.00 72.21  ?  567  PRO D C   1 
ATOM   10404 O O   . PRO D  1  567 ? -2.686  28.090  -21.224 1.00 71.51  ?  567  PRO D O   1 
ATOM   10405 C CB  . PRO D  1  567 ? -0.993  25.933  -22.435 1.00 71.30  ?  567  PRO D CB  1 
ATOM   10406 C CG  . PRO D  1  567 ? 0.421   25.675  -22.033 1.00 69.86  ?  567  PRO D CG  1 
ATOM   10407 C CD  . PRO D  1  567 ? 0.886   26.941  -21.372 1.00 68.90  ?  567  PRO D CD  1 
ATOM   10408 N N   . PRO D  1  568 ? -3.082  28.611  -23.375 1.00 73.73  ?  568  PRO D N   1 
ATOM   10409 C CA  . PRO D  1  568 ? -4.367  29.238  -23.038 1.00 74.48  ?  568  PRO D CA  1 
ATOM   10410 C C   . PRO D  1  568 ? -5.443  28.237  -22.676 1.00 75.01  ?  568  PRO D C   1 
ATOM   10411 O O   . PRO D  1  568 ? -6.480  28.637  -22.135 1.00 75.02  ?  568  PRO D O   1 
ATOM   10412 C CB  . PRO D  1  568 ? -4.736  30.002  -24.318 1.00 75.93  ?  568  PRO D CB  1 
ATOM   10413 C CG  . PRO D  1  568 ? -3.779  29.504  -25.392 1.00 75.92  ?  568  PRO D CG  1 
ATOM   10414 C CD  . PRO D  1  568 ? -2.946  28.400  -24.821 1.00 74.70  ?  568  PRO D CD  1 
ATOM   10415 N N   . THR D  1  569 ? -5.223  26.956  -22.946 1.00 77.13  ?  569  THR D N   1 
ATOM   10416 C CA  . THR D  1  569 ? -6.200  25.905  -22.717 1.00 76.73  ?  569  THR D CA  1 
ATOM   10417 C C   . THR D  1  569 ? -6.075  25.273  -21.336 1.00 75.07  ?  569  THR D C   1 
ATOM   10418 O O   . THR D  1  569 ? -6.755  24.279  -21.060 1.00 74.58  ?  569  THR D O   1 
ATOM   10419 C CB  . THR D  1  569 ? -6.067  24.832  -23.799 1.00 77.01  ?  569  THR D CB  1 
ATOM   10420 O OG1 . THR D  1  569 ? -4.821  24.140  -23.639 1.00 75.95  ?  569  THR D OG1 1 
ATOM   10421 C CG2 . THR D  1  569 ? -6.105  25.479  -25.177 1.00 78.58  ?  569  THR D CG2 1 
ATOM   10422 N N   . LEU D  1  570 ? -5.204  25.802  -20.477 1.00 74.93  ?  570  LEU D N   1 
ATOM   10423 C CA  . LEU D  1  570 ? -5.066  25.290  -19.115 1.00 73.59  ?  570  LEU D CA  1 
ATOM   10424 C C   . LEU D  1  570 ? -6.122  25.965  -18.242 1.00 73.65  ?  570  LEU D C   1 
ATOM   10425 O O   . LEU D  1  570 ? -5.856  26.907  -17.490 1.00 73.34  ?  570  LEU D O   1 
ATOM   10426 C CB  . LEU D  1  570 ? -3.653  25.524  -18.590 1.00 72.69  ?  570  LEU D CB  1 
ATOM   10427 C CG  . LEU D  1  570 ? -2.672  24.348  -18.650 1.00 72.06  ?  570  LEU D CG  1 
ATOM   10428 C CD1 . LEU D  1  570 ? -2.909  23.389  -17.496 1.00 71.08  ?  570  LEU D CD1 1 
ATOM   10429 C CD2 . LEU D  1  570 ? -2.766  23.614  -19.982 1.00 72.85  ?  570  LEU D CD2 1 
ATOM   10430 N N   . ASN D  1  571 ? -7.359  25.467  -18.353 1.00 74.66  ?  571  ASN D N   1 
ATOM   10431 C CA  . ASN D  1  571 ? -8.459  26.027  -17.576 1.00 74.94  ?  571  ASN D CA  1 
ATOM   10432 C C   . ASN D  1  571 ? -9.382  24.964  -16.980 1.00 74.70  ?  571  ASN D C   1 
ATOM   10433 O O   . ASN D  1  571 ? -10.506 25.294  -16.585 1.00 75.23  ?  571  ASN D O   1 
ATOM   10434 C CB  . ASN D  1  571 ? -9.273  26.998  -18.432 1.00 76.16  ?  571  ASN D CB  1 
ATOM   10435 C CG  . ASN D  1  571 ? -9.931  26.323  -19.620 1.00 77.01  ?  571  ASN D CG  1 
ATOM   10436 O OD1 . ASN D  1  571 ? -10.520 25.249  -19.502 1.00 76.76  ?  571  ASN D OD1 1 
ATOM   10437 N ND2 . ASN D  1  571 ? -9.841  26.963  -20.779 1.00 78.12  ?  571  ASN D ND2 1 
ATOM   10438 N N   . ASN D  1  572 ? -8.955  23.705  -16.908 1.00 72.04  ?  572  ASN D N   1 
ATOM   10439 C CA  . ASN D  1  572 ? -9.845  22.589  -16.581 1.00 71.85  ?  572  ASN D CA  1 
ATOM   10440 C C   . ASN D  1  572 ? -9.224  21.661  -15.537 1.00 70.90  ?  572  ASN D C   1 
ATOM   10441 O O   . ASN D  1  572 ? -9.192  20.440  -15.705 1.00 70.38  ?  572  ASN D O   1 
ATOM   10442 C CB  . ASN D  1  572 ? -10.231 21.807  -17.832 1.00 72.14  ?  572  ASN D CB  1 
ATOM   10443 C CG  . ASN D  1  572 ? -11.465 20.946  -17.619 1.00 72.23  ?  572  ASN D CG  1 
ATOM   10444 O OD1 . ASN D  1  572 ? -12.409 21.354  -16.943 1.00 72.64  ?  572  ASN D OD1 1 
ATOM   10445 N ND2 . ASN D  1  572 ? -11.464 19.754  -18.200 1.00 71.93  ?  572  ASN D ND2 1 
ATOM   10446 N N   . LEU D  1  573 ? -8.693  22.222  -14.447 1.00 67.41  ?  573  LEU D N   1 
ATOM   10447 C CA  . LEU D  1  573 ? -8.079  21.437  -13.373 1.00 66.84  ?  573  LEU D CA  1 
ATOM   10448 C C   . LEU D  1  573 ? -8.894  21.614  -12.092 1.00 67.47  ?  573  LEU D C   1 
ATOM   10449 O O   . LEU D  1  573 ? -8.517  22.393  -11.201 1.00 67.87  ?  573  LEU D O   1 
ATOM   10450 C CB  . LEU D  1  573 ? -6.620  21.837  -13.163 1.00 66.40  ?  573  LEU D CB  1 
ATOM   10451 C CG  . LEU D  1  573 ? -5.764  21.940  -14.427 1.00 66.04  ?  573  LEU D CG  1 
ATOM   10452 C CD1 . LEU D  1  573 ? -4.378  22.421  -14.072 1.00 65.61  ?  573  LEU D CD1 1 
ATOM   10453 C CD2 . LEU D  1  573 ? -5.698  20.610  -15.162 1.00 65.56  ?  573  LEU D CD2 1 
ATOM   10454 N N   . PRO D  1  574 ? -10.003 20.876  -11.948 1.00 70.52  ?  574  PRO D N   1 
ATOM   10455 C CA  . PRO D  1  574 ? -10.941 21.127  -10.840 1.00 71.32  ?  574  PRO D CA  1 
ATOM   10456 C C   . PRO D  1  574 ? -10.432 20.735  -9.463  1.00 71.59  ?  574  PRO D C   1 
ATOM   10457 O O   . PRO D  1  574 ? -11.186 20.868  -8.493  1.00 72.39  ?  574  PRO D O   1 
ATOM   10458 C CB  . PRO D  1  574 ? -12.164 20.268  -11.216 1.00 71.35  ?  574  PRO D CB  1 
ATOM   10459 C CG  . PRO D  1  574 ? -12.004 19.967  -12.665 1.00 70.85  ?  574  PRO D CG  1 
ATOM   10460 C CD  . PRO D  1  574 ? -10.525 19.855  -12.870 1.00 70.12  ?  574  PRO D CD  1 
ATOM   10461 N N   . ARG D  1  575 ? -9.195  20.267  -9.326  1.00 71.87  ?  575  ARG D N   1 
ATOM   10462 C CA  . ARG D  1  575 ? -8.657  19.903  -8.025  1.00 72.49  ?  575  ARG D CA  1 
ATOM   10463 C C   . ARG D  1  575 ? -7.366  20.629  -7.697  1.00 72.74  ?  575  ARG D C   1 
ATOM   10464 O O   . ARG D  1  575 ? -6.792  20.387  -6.630  1.00 73.58  ?  575  ARG D O   1 
ATOM   10465 C CB  . ARG D  1  575 ? -8.402  18.394  -7.946  1.00 71.91  ?  575  ARG D CB  1 
ATOM   10466 C CG  . ARG D  1  575 ? -9.637  17.535  -8.009  1.00 71.73  ?  575  ARG D CG  1 
ATOM   10467 C CD  . ARG D  1  575 ? -9.253  16.076  -8.205  1.00 70.79  ?  575  ARG D CD  1 
ATOM   10468 N NE  . ARG D  1  575 ? -10.420 15.241  -8.463  1.00 70.49  ?  575  ARG D NE  1 
ATOM   10469 C CZ  . ARG D  1  575 ? -11.102 15.237  -9.600  1.00 70.08  ?  575  ARG D CZ  1 
ATOM   10470 N NH1 . ARG D  1  575 ? -10.744 15.994  -10.625 1.00 69.86  ?  575  ARG D NH1 1 
ATOM   10471 N NH2 . ARG D  1  575 ? -12.177 14.459  -9.708  1.00 70.07  ?  575  ARG D NH2 1 
ATOM   10472 N N   . LEU D  1  576 ? -6.888  21.497  -8.578  1.00 68.55  ?  576  LEU D N   1 
ATOM   10473 C CA  . LEU D  1  576 ? -5.575  22.103  -8.411  1.00 68.49  ?  576  LEU D CA  1 
ATOM   10474 C C   . LEU D  1  576 ? -5.640  23.247  -7.405  1.00 69.64  ?  576  LEU D C   1 
ATOM   10475 O O   . LEU D  1  576 ? -6.352  24.233  -7.626  1.00 69.81  ?  576  LEU D O   1 
ATOM   10476 C CB  . LEU D  1  576 ? -5.063  22.595  -9.758  1.00 67.42  ?  576  LEU D CB  1 
ATOM   10477 C CG  . LEU D  1  576 ? -3.610  23.039  -9.802  1.00 66.95  ?  576  LEU D CG  1 
ATOM   10478 C CD1 . LEU D  1  576 ? -2.682  21.841  -9.941  1.00 66.14  ?  576  LEU D CD1 1 
ATOM   10479 C CD2 . LEU D  1  576 ? -3.458  23.987  -10.962 1.00 66.46  ?  576  LEU D CD2 1 
ATOM   10480 N N   . TYR D  1  577 ? -4.892  23.122  -6.308  1.00 64.40  ?  577  TYR D N   1 
ATOM   10481 C CA  . TYR D  1  577 ? -4.777  24.186  -5.319  1.00 65.53  ?  577  TYR D CA  1 
ATOM   10482 C C   . TYR D  1  577 ? -3.393  24.825  -5.278  1.00 65.32  ?  577  TYR D C   1 
ATOM   10483 O O   . TYR D  1  577 ? -3.153  25.683  -4.421  1.00 66.19  ?  577  TYR D O   1 
ATOM   10484 C CB  . TYR D  1  577 ? -5.151  23.661  -3.920  1.00 67.15  ?  577  TYR D CB  1 
ATOM   10485 C CG  . TYR D  1  577 ? -4.194  22.638  -3.330  1.00 67.92  ?  577  TYR D CG  1 
ATOM   10486 C CD1 . TYR D  1  577 ? -3.081  23.031  -2.593  1.00 68.87  ?  577  TYR D CD1 1 
ATOM   10487 C CD2 . TYR D  1  577 ? -4.413  21.277  -3.499  1.00 67.74  ?  577  TYR D CD2 1 
ATOM   10488 C CE1 . TYR D  1  577 ? -2.204  22.093  -2.051  1.00 69.90  ?  577  TYR D CE1 1 
ATOM   10489 C CE2 . TYR D  1  577 ? -3.542  20.330  -2.960  1.00 68.62  ?  577  TYR D CE2 1 
ATOM   10490 C CZ  . TYR D  1  577 ? -2.440  20.743  -2.236  1.00 69.88  ?  577  TYR D CZ  1 
ATOM   10491 O OH  . TYR D  1  577 ? -1.580  19.806  -1.698  1.00 71.04  ?  577  TYR D OH  1 
ATOM   10492 N N   . TYR D  1  578 ? -2.482  24.441  -6.174  1.00 62.64  ?  578  TYR D N   1 
ATOM   10493 C CA  . TYR D  1  578 ? -1.110  24.938  -6.141  1.00 62.26  ?  578  TYR D CA  1 
ATOM   10494 C C   . TYR D  1  578 ? -0.542  24.985  -7.551  1.00 60.47  ?  578  TYR D C   1 
ATOM   10495 O O   . TYR D  1  578 ? -0.678  24.017  -8.302  1.00 59.64  ?  578  TYR D O   1 
ATOM   10496 C CB  . TYR D  1  578 ? -0.239  24.049  -5.255  1.00 63.13  ?  578  TYR D CB  1 
ATOM   10497 C CG  . TYR D  1  578 ? 1.192   24.504  -5.110  1.00 62.81  ?  578  TYR D CG  1 
ATOM   10498 C CD1 . TYR D  1  578 ? 2.158   24.153  -6.050  1.00 61.12  ?  578  TYR D CD1 1 
ATOM   10499 C CD2 . TYR D  1  578 ? 1.586   25.257  -4.018  1.00 64.09  ?  578  TYR D CD2 1 
ATOM   10500 C CE1 . TYR D  1  578 ? 3.476   24.557  -5.908  1.00 60.74  ?  578  TYR D CE1 1 
ATOM   10501 C CE2 . TYR D  1  578 ? 2.893   25.662  -3.865  1.00 63.72  ?  578  TYR D CE2 1 
ATOM   10502 C CZ  . TYR D  1  578 ? 3.835   25.311  -4.810  1.00 62.06  ?  578  TYR D CZ  1 
ATOM   10503 O OH  . TYR D  1  578 ? 5.136   25.722  -4.645  1.00 61.64  ?  578  TYR D OH  1 
ATOM   10504 N N   . MET D  1  579 ? 0.100   26.099  -7.900  1.00 64.17  ?  579  MET D N   1 
ATOM   10505 C CA  . MET D  1  579 ? 0.755   26.236  -9.200  1.00 62.75  ?  579  MET D CA  1 
ATOM   10506 C C   . MET D  1  579 ? 1.953   27.162  -9.032  1.00 62.46  ?  579  MET D C   1 
ATOM   10507 O O   . MET D  1  579 ? 1.777   28.359  -8.789  1.00 62.88  ?  579  MET D O   1 
ATOM   10508 C CB  . MET D  1  579 ? -0.225  26.771  -10.245 1.00 62.55  ?  579  MET D CB  1 
ATOM   10509 C CG  . MET D  1  579 ? 0.416   27.368  -11.490 1.00 61.72  ?  579  MET D CG  1 
ATOM   10510 S SD  . MET D  1  579 ? -0.625  27.342  -12.970 1.00 61.80  ?  579  MET D SD  1 
ATOM   10511 C CE  . MET D  1  579 ? -1.198  25.652  -12.943 1.00 61.59  ?  579  MET D CE  1 
ATOM   10512 N N   . ASN D  1  580 ? 3.164   26.610  -9.149  1.00 60.66  ?  580  ASN D N   1 
ATOM   10513 C CA  . ASN D  1  580 ? 4.409   27.373  -9.069  1.00 60.32  ?  580  ASN D CA  1 
ATOM   10514 C C   . ASN D  1  580 ? 5.107   27.311  -10.422 1.00 59.02  ?  580  ASN D C   1 
ATOM   10515 O O   . ASN D  1  580 ? 5.598   26.249  -10.821 1.00 58.33  ?  580  ASN D O   1 
ATOM   10516 C CB  . ASN D  1  580 ? 5.313   26.804  -7.979  1.00 60.86  ?  580  ASN D CB  1 
ATOM   10517 C CG  . ASN D  1  580 ? 6.292   27.819  -7.422  1.00 61.23  ?  580  ASN D CG  1 
ATOM   10518 O OD1 . ASN D  1  580 ? 6.515   28.881  -7.997  1.00 60.83  ?  580  ASN D OD1 1 
ATOM   10519 N ND2 . ASN D  1  580 ? 6.905   27.464  -6.294  1.00 62.15  ?  580  ASN D ND2 1 
ATOM   10520 N N   . LEU D  1  581 ? 5.203   28.457  -11.103 1.00 60.07  ?  581  LEU D N   1 
ATOM   10521 C CA  . LEU D  1  581 ? 5.865   28.522  -12.403 1.00 59.25  ?  581  LEU D CA  1 
ATOM   10522 C C   . LEU D  1  581 ? 6.974   29.571  -12.416 1.00 59.27  ?  581  LEU D C   1 
ATOM   10523 O O   . LEU D  1  581 ? 7.341   30.065  -13.486 1.00 59.00  ?  581  LEU D O   1 
ATOM   10524 C CB  . LEU D  1  581 ? 4.854   28.803  -13.522 1.00 59.34  ?  581  LEU D CB  1 
ATOM   10525 C CG  . LEU D  1  581 ? 3.581   27.964  -13.741 1.00 59.69  ?  581  LEU D CG  1 
ATOM   10526 C CD1 . LEU D  1  581 ? 3.110   28.108  -15.161 1.00 59.84  ?  581  LEU D CD1 1 
ATOM   10527 C CD2 . LEU D  1  581 ? 3.774   26.481  -13.466 1.00 59.36  ?  581  LEU D CD2 1 
ATOM   10528 N N   . SER D  1  582 ? 7.510   29.920  -11.249 1.00 64.72  ?  582  SER D N   1 
ATOM   10529 C CA  . SER D  1  582 ? 8.488   30.991  -11.142 1.00 65.06  ?  582  SER D CA  1 
ATOM   10530 C C   . SER D  1  582 ? 9.848   30.561  -11.704 1.00 64.64  ?  582  SER D C   1 
ATOM   10531 O O   . SER D  1  582 ? 10.102  29.387  -11.982 1.00 64.07  ?  582  SER D O   1 
ATOM   10532 C CB  . SER D  1  582 ? 8.625   31.444  -9.685  1.00 66.11  ?  582  SER D CB  1 
ATOM   10533 O OG  . SER D  1  582 ? 9.055   30.389  -8.840  1.00 66.35  ?  582  SER D OG  1 
ATOM   10534 N N   . ARG D  1  583 ? 10.723  31.551  -11.894 1.00 67.86  ?  583  ARG D N   1 
ATOM   10535 C CA  . ARG D  1  583 ? 12.117  31.315  -12.273 1.00 67.92  ?  583  ARG D CA  1 
ATOM   10536 C C   . ARG D  1  583 ? 12.220  30.509  -13.573 1.00 67.11  ?  583  ARG D C   1 
ATOM   10537 O O   . ARG D  1  583 ? 12.751  29.398  -13.620 1.00 66.78  ?  583  ARG D O   1 
ATOM   10538 C CB  . ARG D  1  583 ? 12.876  30.650  -11.121 1.00 68.48  ?  583  ARG D CB  1 
ATOM   10539 C CG  . ARG D  1  583 ? 12.964  31.548  -9.897  1.00 69.70  ?  583  ARG D CG  1 
ATOM   10540 C CD  . ARG D  1  583 ? 13.191  30.761  -8.626  1.00 70.35  ?  583  ARG D CD  1 
ATOM   10541 N NE  . ARG D  1  583 ? 12.255  31.150  -7.577  1.00 70.93  ?  583  ARG D NE  1 
ATOM   10542 C CZ  . ARG D  1  583 ? 12.295  32.294  -6.908  1.00 71.92  ?  583  ARG D CZ  1 
ATOM   10543 N NH1 . ARG D  1  583 ? 13.235  33.199  -7.135  1.00 72.55  ?  583  ARG D NH1 1 
ATOM   10544 N NH2 . ARG D  1  583 ? 11.369  32.536  -5.983  1.00 72.48  ?  583  ARG D NH2 1 
ATOM   10545 N N   . ASN D  1  584 ? 11.700  31.108  -14.637 1.00 67.58  ?  584  ASN D N   1 
ATOM   10546 C CA  . ASN D  1  584 ? 11.618  30.489  -15.954 1.00 67.20  ?  584  ASN D CA  1 
ATOM   10547 C C   . ASN D  1  584 ? 11.752  31.602  -16.991 1.00 67.61  ?  584  ASN D C   1 
ATOM   10548 O O   . ASN D  1  584 ? 12.217  32.702  -16.676 1.00 68.12  ?  584  ASN D O   1 
ATOM   10549 C CB  . ASN D  1  584 ? 10.319  29.683  -16.084 1.00 66.77  ?  584  ASN D CB  1 
ATOM   10550 C CG  . ASN D  1  584 ? 10.467  28.247  -15.629 1.00 66.34  ?  584  ASN D CG  1 
ATOM   10551 O OD1 . ASN D  1  584 ? 10.853  27.374  -16.404 1.00 66.23  ?  584  ASN D OD1 1 
ATOM   10552 N ND2 . ASN D  1  584 ? 10.143  27.991  -14.368 1.00 66.30  ?  584  ASN D ND2 1 
ATOM   10553 N N   . ASP D  1  585 ? 11.391  31.315  -18.242 1.00 73.83  ?  585  ASP D N   1 
ATOM   10554 C CA  . ASP D  1  585 ? 11.511  32.311  -19.301 1.00 74.37  ?  585  ASP D CA  1 
ATOM   10555 C C   . ASP D  1  585 ? 10.228  32.445  -20.117 1.00 74.51  ?  585  ASP D C   1 
ATOM   10556 O O   . ASP D  1  585 ? 10.287  32.717  -21.321 1.00 75.02  ?  585  ASP D O   1 
ATOM   10557 C CB  . ASP D  1  585 ? 12.686  31.984  -20.221 1.00 74.75  ?  585  ASP D CB  1 
ATOM   10558 C CG  . ASP D  1  585 ? 14.009  32.490  -19.680 1.00 75.09  ?  585  ASP D CG  1 
ATOM   10559 O OD1 . ASP D  1  585 ? 14.142  33.718  -19.468 1.00 75.60  ?  585  ASP D OD1 1 
ATOM   10560 O OD2 . ASP D  1  585 ? 14.918  31.658  -19.467 1.00 74.98  -1 585  ASP D OD2 1 
ATOM   10561 N N   . LEU D  1  586 ? 9.066   32.267  -19.484 1.00 69.94  ?  586  LEU D N   1 
ATOM   10562 C CA  . LEU D  1  586 ? 7.797   32.431  -20.187 1.00 70.35  ?  586  LEU D CA  1 
ATOM   10563 C C   . LEU D  1  586 ? 7.535   33.897  -20.504 1.00 70.83  ?  586  LEU D C   1 
ATOM   10564 O O   . LEU D  1  586 ? 7.737   34.779  -19.667 1.00 70.77  ?  586  LEU D O   1 
ATOM   10565 C CB  . LEU D  1  586 ? 6.629   31.874  -19.370 1.00 70.19  ?  586  LEU D CB  1 
ATOM   10566 C CG  . LEU D  1  586 ? 6.712   30.474  -18.763 1.00 69.72  ?  586  LEU D CG  1 
ATOM   10567 C CD1 . LEU D  1  586 ? 7.465   30.498  -17.483 1.00 69.23  ?  586  LEU D CD1 1 
ATOM   10568 C CD2 . LEU D  1  586 ? 5.345   29.914  -18.507 1.00 70.00  ?  586  LEU D CD2 1 
ATOM   10569 N N   . ASP D  1  587 ? 7.064   34.150  -21.718 1.00 76.06  ?  587  ASP D N   1 
ATOM   10570 C CA  . ASP D  1  587 ? 6.842   35.495  -22.223 1.00 76.62  ?  587  ASP D CA  1 
ATOM   10571 C C   . ASP D  1  587 ? 5.360   35.706  -22.516 1.00 77.21  ?  587  ASP D C   1 
ATOM   10572 O O   . ASP D  1  587 ? 4.526   34.823  -22.300 1.00 77.25  ?  587  ASP D O   1 
ATOM   10573 C CB  . ASP D  1  587 ? 7.702   35.760  -23.467 1.00 77.11  ?  587  ASP D CB  1 
ATOM   10574 C CG  . ASP D  1  587 ? 7.252   34.963  -24.691 1.00 77.73  ?  587  ASP D CG  1 
ATOM   10575 O OD1 . ASP D  1  587 ? 6.399   34.062  -24.561 1.00 77.63  ?  587  ASP D OD1 1 
ATOM   10576 O OD2 . ASP D  1  587 ? 7.759   35.243  -25.798 1.00 78.47  -1 587  ASP D OD2 1 
ATOM   10577 N N   . GLN D  1  588 ? 5.050   36.905  -23.011 1.00 81.00  ?  588  GLN D N   1 
ATOM   10578 C CA  . GLN D  1  588 ? 3.704   37.290  -23.426 1.00 81.82  ?  588  GLN D CA  1 
ATOM   10579 C C   . GLN D  1  588 ? 2.725   37.331  -22.252 1.00 81.69  ?  588  GLN D C   1 
ATOM   10580 O O   . GLN D  1  588 ? 3.125   37.212  -21.088 1.00 80.98  ?  588  GLN D O   1 
ATOM   10581 C CB  . GLN D  1  588 ? 3.210   36.362  -24.543 1.00 82.52  ?  588  GLN D CB  1 
ATOM   10582 C CG  . GLN D  1  588 ? 4.182   36.291  -25.723 1.00 82.80  ?  588  GLN D CG  1 
ATOM   10583 C CD  . GLN D  1  588 ? 3.505   35.965  -27.044 1.00 84.02  ?  588  GLN D CD  1 
ATOM   10584 O OE1 . GLN D  1  588 ? 2.283   35.845  -27.116 1.00 84.78  ?  588  GLN D OE1 1 
ATOM   10585 N NE2 . GLN D  1  588 ? 4.302   35.821  -28.099 1.00 84.60  ?  588  GLN D NE2 1 
ATOM   10586 N N   . THR D  1  589 ? 1.441   37.517  -22.549 1.00 79.84  ?  589  THR D N   1 
ATOM   10587 C CA  . THR D  1  589 ? 0.460   37.861  -21.532 1.00 79.98  ?  589  THR D CA  1 
ATOM   10588 C C   . THR D  1  589 ? -0.013  36.628  -20.765 1.00 79.68  ?  589  THR D C   1 
ATOM   10589 O O   . THR D  1  589 ? 0.058   35.496  -21.248 1.00 79.69  ?  589  THR D O   1 
ATOM   10590 C CB  . THR D  1  589 ? -0.738  38.560  -22.171 1.00 81.31  ?  589  THR D CB  1 
ATOM   10591 O OG1 . THR D  1  589 ? -1.819  38.597  -21.232 1.00 81.49  ?  589  THR D OG1 1 
ATOM   10592 C CG2 . THR D  1  589 ? -1.186  37.811  -23.414 1.00 82.11  ?  589  THR D CG2 1 
ATOM   10593 N N   . ILE D  1  590 ? -0.504  36.869  -19.553 1.00 75.78  ?  590  ILE D N   1 
ATOM   10594 C CA  . ILE D  1  590 ? -1.129  35.809  -18.750 1.00 73.48  ?  590  ILE D CA  1 
ATOM   10595 C C   . ILE D  1  590 ? -2.451  35.408  -19.396 1.00 74.83  ?  590  ILE D C   1 
ATOM   10596 O O   . ILE D  1  590 ? -3.299  36.280  -19.649 1.00 78.07  ?  590  ILE D O   1 
ATOM   10597 C CB  . ILE D  1  590 ? -1.342  36.285  -17.310 1.00 73.72  ?  590  ILE D CB  1 
ATOM   10598 C CG1 . ILE D  1  590 ? -0.011  36.665  -16.677 1.00 72.85  ?  590  ILE D CG1 1 
ATOM   10599 C CG2 . ILE D  1  590 ? -2.014  35.211  -16.468 1.00 71.97  ?  590  ILE D CG2 1 
ATOM   10600 C CD1 . ILE D  1  590 ? 0.195   38.126  -16.612 1.00 76.00  ?  590  ILE D CD1 1 
ATOM   10601 N N   . PRO D  1  591 ? -2.683  34.127  -19.671 1.00 76.26  ?  591  PRO D N   1 
ATOM   10602 C CA  . PRO D  1  591 ? -3.918  33.738  -20.360 1.00 77.54  ?  591  PRO D CA  1 
ATOM   10603 C C   . PRO D  1  591 ? -5.147  33.898  -19.477 1.00 78.75  ?  591  PRO D C   1 
ATOM   10604 O O   . PRO D  1  591 ? -5.083  33.795  -18.249 1.00 77.34  ?  591  PRO D O   1 
ATOM   10605 C CB  . PRO D  1  591 ? -3.677  32.266  -20.709 1.00 77.53  ?  591  PRO D CB  1 
ATOM   10606 C CG  . PRO D  1  591 ? -2.722  31.795  -19.667 1.00 76.15  ?  591  PRO D CG  1 
ATOM   10607 C CD  . PRO D  1  591 ? -1.825  32.966  -19.372 1.00 75.41  ?  591  PRO D CD  1 
ATOM   10608 N N   . GLU D  1  592 ? -6.284  34.159  -20.130 1.00 90.55  ?  592  GLU D N   1 
ATOM   10609 C CA  . GLU D  1  592 ? -7.542  34.325  -19.406 1.00 91.06  ?  592  GLU D CA  1 
ATOM   10610 C C   . GLU D  1  592 ? -8.034  33.016  -18.801 1.00 90.86  ?  592  GLU D C   1 
ATOM   10611 O O   . GLU D  1  592 ? -8.782  33.036  -17.817 1.00 90.84  ?  592  GLU D O   1 
ATOM   10612 C CB  . GLU D  1  592 ? -8.610  34.899  -20.336 1.00 92.56  ?  592  GLU D CB  1 
ATOM   10613 C CG  . GLU D  1  592 ? -8.806  36.390  -20.192 1.00 93.76  ?  592  GLU D CG  1 
ATOM   10614 C CD  . GLU D  1  592 ? -9.873  36.733  -19.178 1.00 95.31  ?  592  GLU D CD  1 
ATOM   10615 O OE1 . GLU D  1  592 ? -11.012 36.242  -19.327 1.00 97.18  ?  592  GLU D OE1 1 
ATOM   10616 O OE2 . GLU D  1  592 ? -9.572  37.491  -18.230 1.00 95.27  -1 592  GLU D OE2 1 
ATOM   10617 N N   . GLY D  1  593 ? -7.640  31.877  -19.374 1.00 83.38  ?  593  GLY D N   1 
ATOM   10618 C CA  . GLY D  1  593 ? -8.100  30.592  -18.877 1.00 83.15  ?  593  GLY D CA  1 
ATOM   10619 C C   . GLY D  1  593 ? -7.660  30.273  -17.462 1.00 81.99  ?  593  GLY D C   1 
ATOM   10620 O O   . GLY D  1  593 ? -8.301  29.456  -16.793 1.00 81.88  ?  593  GLY D O   1 
ATOM   10621 N N   . LEU D  1  594 ? -6.573  30.892  -16.990 1.00 81.79  ?  594  LEU D N   1 
ATOM   10622 C CA  . LEU D  1  594 ? -6.100  30.631  -15.633 1.00 81.02  ?  594  LEU D CA  1 
ATOM   10623 C C   . LEU D  1  594 ? -7.120  31.060  -14.583 1.00 81.50  ?  594  LEU D C   1 
ATOM   10624 O O   . LEU D  1  594 ? -7.218  30.435  -13.520 1.00 81.35  ?  594  LEU D O   1 
ATOM   10625 C CB  . LEU D  1  594 ? -4.765  31.339  -15.399 1.00 80.28  ?  594  LEU D CB  1 
ATOM   10626 C CG  . LEU D  1  594 ? -3.519  30.455  -15.326 1.00 79.39  ?  594  LEU D CG  1 
ATOM   10627 C CD1 . LEU D  1  594 ? -3.404  29.605  -16.578 1.00 79.52  ?  594  LEU D CD1 1 
ATOM   10628 C CD2 . LEU D  1  594 ? -2.273  31.304  -15.138 1.00 78.74  ?  594  LEU D CD2 1 
ATOM   10629 N N   . THR D  1  595 ? -7.881  32.123  -14.856 1.00 86.38  ?  595  THR D N   1 
ATOM   10630 C CA  . THR D  1  595 ? -8.894  32.606  -13.923 1.00 86.95  ?  595  THR D CA  1 
ATOM   10631 C C   . THR D  1  595 ? -10.039 31.620  -13.717 1.00 87.37  ?  595  THR D C   1 
ATOM   10632 O O   . THR D  1  595 ? -10.915 31.882  -12.887 1.00 87.89  ?  595  THR D O   1 
ATOM   10633 C CB  . THR D  1  595 ? -9.458  33.947  -14.401 1.00 87.62  ?  595  THR D CB  1 
ATOM   10634 O OG1 . THR D  1  595 ? -10.369 33.729  -15.485 1.00 88.41  ?  595  THR D OG1 1 
ATOM   10635 C CG2 . THR D  1  595 ? -8.342  34.847  -14.876 1.00 87.19  ?  595  THR D CG2 1 
ATOM   10636 N N   . LYS D  1  596 ? -10.089 30.529  -14.472 1.00 82.21  ?  596  LYS D N   1 
ATOM   10637 C CA  . LYS D  1  596 ? -11.123 29.521  -14.292 1.00 82.49  ?  596  LYS D CA  1 
ATOM   10638 C C   . LYS D  1  596 ? -10.679 28.363  -13.405 1.00 81.82  ?  596  LYS D C   1 
ATOM   10639 O O   . LYS D  1  596 ? -11.447 27.416  -13.216 1.00 81.92  ?  596  LYS D O   1 
ATOM   10640 C CB  . LYS D  1  596 ? -11.592 29.011  -15.657 1.00 82.93  ?  596  LYS D CB  1 
ATOM   10641 C CG  . LYS D  1  596 ? -12.074 30.136  -16.567 1.00 83.90  ?  596  LYS D CG  1 
ATOM   10642 C CD  . LYS D  1  596 ? -12.089 29.726  -18.028 1.00 84.49  ?  596  LYS D CD  1 
ATOM   10643 C CE  . LYS D  1  596 ? -12.201 30.946  -18.935 1.00 85.52  ?  596  LYS D CE  1 
ATOM   10644 N NZ  . LYS D  1  596 ? -11.907 30.629  -20.363 1.00 86.29  ?  596  LYS D NZ  1 
ATOM   10645 N N   . LEU D  1  597 ? -9.465  28.421  -12.851 1.00 79.96  ?  597  LEU D N   1 
ATOM   10646 C CA  . LEU D  1  597 ? -8.968  27.395  -11.930 1.00 79.54  ?  597  LEU D CA  1 
ATOM   10647 C C   . LEU D  1  597 ? -9.458  27.736  -10.525 1.00 80.16  ?  597  LEU D C   1 
ATOM   10648 O O   . LEU D  1  597 ? -8.736  28.292  -9.695  1.00 80.26  ?  597  LEU D O   1 
ATOM   10649 C CB  . LEU D  1  597 ? -7.446  27.308  -11.993 1.00 78.80  ?  597  LEU D CB  1 
ATOM   10650 C CG  . LEU D  1  597 ? -6.758  27.165  -13.356 1.00 78.27  ?  597  LEU D CG  1 
ATOM   10651 C CD1 . LEU D  1  597 ? -5.401  26.489  -13.218 1.00 77.43  ?  597  LEU D CD1 1 
ATOM   10652 C CD2 . LEU D  1  597 ? -7.627  26.366  -14.296 1.00 78.56  ?  597  LEU D CD2 1 
ATOM   10653 N N   . SER D  1  598 ? -10.714 27.367  -10.255 1.00 80.75  ?  598  SER D N   1 
ATOM   10654 C CA  . SER D  1  598 ? -11.429 27.904  -9.098  1.00 81.54  ?  598  SER D CA  1 
ATOM   10655 C C   . SER D  1  598 ? -10.801 27.478  -7.775  1.00 81.76  ?  598  SER D C   1 
ATOM   10656 O O   . SER D  1  598 ? -10.778 28.256  -6.815  1.00 82.37  ?  598  SER D O   1 
ATOM   10657 C CB  . SER D  1  598 ? -12.887 27.460  -9.145  1.00 81.99  ?  598  SER D CB  1 
ATOM   10658 O OG  . SER D  1  598 ? -12.965 26.051  -9.254  1.00 81.61  ?  598  SER D OG  1 
ATOM   10659 N N   . GLN D  1  599 ? -10.284 26.258  -7.698  1.00 82.83  ?  599  GLN D N   1 
ATOM   10660 C CA  . GLN D  1  599 ? -9.798  25.747  -6.424  1.00 83.38  ?  599  GLN D CA  1 
ATOM   10661 C C   . GLN D  1  599 ? -8.395  26.226  -6.079  1.00 83.37  ?  599  GLN D C   1 
ATOM   10662 O O   . GLN D  1  599 ? -7.875  25.841  -5.027  1.00 84.07  ?  599  GLN D O   1 
ATOM   10663 C CB  . GLN D  1  599 ? -9.834  24.217  -6.427  1.00 83.12  ?  599  GLN D CB  1 
ATOM   10664 C CG  . GLN D  1  599 ? -11.205 23.619  -6.726  1.00 83.09  ?  599  GLN D CG  1 
ATOM   10665 C CD  . GLN D  1  599 ? -12.321 24.214  -5.876  1.00 83.99  ?  599  GLN D CD  1 
ATOM   10666 O OE1 . GLN D  1  599 ? -12.110 24.596  -4.720  1.00 84.54  ?  599  GLN D OE1 1 
ATOM   10667 N NE2 . GLN D  1  599 ? -13.521 24.291  -6.448  1.00 84.24  ?  599  GLN D NE2 1 
ATOM   10668 N N   . LEU D  1  600 ? -7.774  27.045  -6.928  1.00 78.11  ?  600  LEU D N   1 
ATOM   10669 C CA  . LEU D  1  600 ? -6.392  27.459  -6.710  1.00 77.92  ?  600  LEU D CA  1 
ATOM   10670 C C   . LEU D  1  600 ? -6.243  28.220  -5.395  1.00 78.93  ?  600  LEU D C   1 
ATOM   10671 O O   . LEU D  1  600 ? -7.014  29.138  -5.102  1.00 79.36  ?  600  LEU D O   1 
ATOM   10672 C CB  . LEU D  1  600 ? -5.920  28.324  -7.879  1.00 77.02  ?  600  LEU D CB  1 
ATOM   10673 C CG  . LEU D  1  600 ? -4.559  28.018  -8.504  1.00 76.05  ?  600  LEU D CG  1 
ATOM   10674 C CD1 . LEU D  1  600 ? -4.319  26.520  -8.573  1.00 75.74  ?  600  LEU D CD1 1 
ATOM   10675 C CD2 . LEU D  1  600 ? -4.480  28.647  -9.887  1.00 75.28  ?  600  LEU D CD2 1 
ATOM   10676 N N   . GLN D  1  601 ? -5.252  27.824  -4.597  1.00 76.13  ?  601  GLN D N   1 
ATOM   10677 C CA  . GLN D  1  601 ? -4.908  28.505  -3.354  1.00 77.14  ?  601  GLN D CA  1 
ATOM   10678 C C   . GLN D  1  601 ? -3.634  29.327  -3.454  1.00 76.70  ?  601  GLN D C   1 
ATOM   10679 O O   . GLN D  1  601 ? -3.581  30.444  -2.933  1.00 77.01  ?  601  GLN D O   1 
ATOM   10680 C CB  . GLN D  1  601 ? -4.763  27.490  -2.213  1.00 78.33  ?  601  GLN D CB  1 
ATOM   10681 C CG  . GLN D  1  601 ? -4.491  28.123  -0.850  1.00 79.45  ?  601  GLN D CG  1 
ATOM   10682 C CD  . GLN D  1  601 ? -4.291  27.100  0.261   1.00 80.71  ?  601  GLN D CD  1 
ATOM   10683 O OE1 . GLN D  1  601 ? -4.890  26.020  0.255   1.00 80.97  ?  601  GLN D OE1 1 
ATOM   10684 N NE2 . GLN D  1  601 ? -3.436  27.439  1.220   1.00 81.43  ?  601  GLN D NE2 1 
ATOM   10685 N N   . MET D  1  602 ? -2.608  28.803  -4.120  1.00 75.28  ?  602  MET D N   1 
ATOM   10686 C CA  . MET D  1  602 ? -1.338  29.495  -4.294  1.00 74.68  ?  602  MET D CA  1 
ATOM   10687 C C   . MET D  1  602 ? -1.004  29.533  -5.777  1.00 73.16  ?  602  MET D C   1 
ATOM   10688 O O   . MET D  1  602 ? -1.141  28.520  -6.473  1.00 72.58  ?  602  MET D O   1 
ATOM   10689 C CB  . MET D  1  602 ? -0.220  28.800  -3.503  1.00 75.28  ?  602  MET D CB  1 
ATOM   10690 C CG  . MET D  1  602 ? -0.121  29.217  -2.034  1.00 76.78  ?  602  MET D CG  1 
ATOM   10691 S SD  . MET D  1  602 ? 0.518   27.907  -0.961  1.00 78.07  ?  602  MET D SD  1 
ATOM   10692 C CE  . MET D  1  602 ? 2.003   28.656  -0.284  1.00 78.24  ?  602  MET D CE  1 
ATOM   10693 N N   . LEU D  1  603 ? -0.578  30.701  -6.258  1.00 69.83  ?  603  LEU D N   1 
ATOM   10694 C CA  . LEU D  1  603 ? -0.238  30.900  -7.665  1.00 68.56  ?  603  LEU D CA  1 
ATOM   10695 C C   . LEU D  1  603 ? 0.982   31.805  -7.743  1.00 68.11  ?  603  LEU D C   1 
ATOM   10696 O O   . LEU D  1  603 ? 0.892   32.997  -7.431  1.00 68.49  ?  603  LEU D O   1 
ATOM   10697 C CB  . LEU D  1  603 ? -1.407  31.509  -8.438  1.00 68.53  ?  603  LEU D CB  1 
ATOM   10698 C CG  . LEU D  1  603 ? -1.070  32.033  -9.832  1.00 67.62  ?  603  LEU D CG  1 
ATOM   10699 C CD1 . LEU D  1  603 ? -0.584  30.896  -10.715 1.00 66.80  ?  603  LEU D CD1 1 
ATOM   10700 C CD2 . LEU D  1  603 ? -2.278  32.718  -10.443 1.00 67.99  ?  603  LEU D CD2 1 
ATOM   10701 N N   . ASP D  1  604 ? 2.114   31.253  -8.169  1.00 65.84  ?  604  ASP D N   1 
ATOM   10702 C CA  . ASP D  1  604 ? 3.347   32.017  -8.292  1.00 65.44  ?  604  ASP D CA  1 
ATOM   10703 C C   . ASP D  1  604 ? 3.768   32.050  -9.756  1.00 64.31  ?  604  ASP D C   1 
ATOM   10704 O O   . ASP D  1  604 ? 4.027   30.999  -10.352 1.00 63.62  ?  604  ASP D O   1 
ATOM   10705 C CB  . ASP D  1  604 ? 4.445   31.414  -7.413  1.00 65.71  ?  604  ASP D CB  1 
ATOM   10706 C CG  . ASP D  1  604 ? 5.658   32.312  -7.296  1.00 65.69  ?  604  ASP D CG  1 
ATOM   10707 O OD1 . ASP D  1  604 ? 5.644   33.417  -7.883  1.00 65.48  ?  604  ASP D OD1 1 
ATOM   10708 O OD2 . ASP D  1  604 ? 6.624   31.921  -6.609  1.00 66.03  -1 604  ASP D OD2 1 
ATOM   10709 N N   . LEU D  1  605 ? 3.831   33.255  -10.331 1.00 62.00  ?  605  LEU D N   1 
ATOM   10710 C CA  . LEU D  1  605 ? 4.309   33.457  -11.695 1.00 61.90  ?  605  LEU D CA  1 
ATOM   10711 C C   . LEU D  1  605 ? 5.534   34.364  -11.738 1.00 63.61  ?  605  LEU D C   1 
ATOM   10712 O O   . LEU D  1  605 ? 5.814   34.976  -12.775 1.00 64.77  ?  605  LEU D O   1 
ATOM   10713 C CB  . LEU D  1  605 ? 3.198   34.028  -12.580 1.00 63.31  ?  605  LEU D CB  1 
ATOM   10714 C CG  . LEU D  1  605 ? 1.913   33.208  -12.694 1.00 62.31  ?  605  LEU D CG  1 
ATOM   10715 C CD1 . LEU D  1  605 ? 0.932   33.871  -13.647 1.00 64.35  ?  605  LEU D CD1 1 
ATOM   10716 C CD2 . LEU D  1  605 ? 2.215   31.788  -13.140 1.00 59.43  ?  605  LEU D CD2 1 
ATOM   10717 N N   . SER D  1  606 ? 6.270   34.458  -10.634 1.00 69.55  ?  606  SER D N   1 
ATOM   10718 C CA  . SER D  1  606 ? 7.330   35.444  -10.500 1.00 69.92  ?  606  SER D CA  1 
ATOM   10719 C C   . SER D  1  606 ? 8.541   35.067  -11.354 1.00 69.37  ?  606  SER D C   1 
ATOM   10720 O O   . SER D  1  606 ? 8.672   33.941  -11.837 1.00 68.68  ?  606  SER D O   1 
ATOM   10721 C CB  . SER D  1  606 ? 7.738   35.592  -9.034  1.00 70.86  ?  606  SER D CB  1 
ATOM   10722 O OG  . SER D  1  606 ? 8.152   34.353  -8.485  1.00 70.78  ?  606  SER D OG  1 
ATOM   10723 N N   . TYR D  1  607 ? 9.433   36.044  -11.543 1.00 73.13  ?  607  TYR D N   1 
ATOM   10724 C CA  . TYR D  1  607 ? 10.714  35.834  -12.219 1.00 73.00  ?  607  TYR D CA  1 
ATOM   10725 C C   . TYR D  1  607 ? 10.510  35.232  -13.609 1.00 72.12  ?  607  TYR D C   1 
ATOM   10726 O O   . TYR D  1  607 ? 10.917  34.106  -13.899 1.00 71.59  ?  607  TYR D O   1 
ATOM   10727 C CB  . TYR D  1  607 ? 11.647  34.969  -11.365 1.00 73.27  ?  607  TYR D CB  1 
ATOM   10728 C CG  . TYR D  1  607 ? 12.138  35.684  -10.131 1.00 74.53  ?  607  TYR D CG  1 
ATOM   10729 C CD1 . TYR D  1  607 ? 11.342  35.785  -8.999  1.00 75.00  ?  607  TYR D CD1 1 
ATOM   10730 C CD2 . TYR D  1  607 ? 13.386  36.282  -10.106 1.00 75.46  ?  607  TYR D CD2 1 
ATOM   10731 C CE1 . TYR D  1  607 ? 11.783  36.450  -7.869  1.00 76.27  ?  607  TYR D CE1 1 
ATOM   10732 C CE2 . TYR D  1  607 ? 13.836  36.950  -8.982  1.00 76.85  ?  607  TYR D CE2 1 
ATOM   10733 C CZ  . TYR D  1  607 ? 13.032  37.030  -7.868  1.00 77.18  ?  607  TYR D CZ  1 
ATOM   10734 O OH  . TYR D  1  607 ? 13.482  37.693  -6.751  1.00 78.61  ?  607  TYR D OH  1 
ATOM   10735 N N   . ASN D  1  608 ? 9.829   35.997  -14.458 1.00 73.69  ?  608  ASN D N   1 
ATOM   10736 C CA  . ASN D  1  608 ? 9.554   35.585  -15.826 1.00 73.21  ?  608  ASN D CA  1 
ATOM   10737 C C   . ASN D  1  608 ? 9.608   36.818  -16.721 1.00 73.67  ?  608  ASN D C   1 
ATOM   10738 O O   . ASN D  1  608 ? 9.993   37.909  -16.291 1.00 74.27  ?  608  ASN D O   1 
ATOM   10739 C CB  . ASN D  1  608 ? 8.204   34.863  -15.907 1.00 72.86  ?  608  ASN D CB  1 
ATOM   10740 C CG  . ASN D  1  608 ? 8.347   33.360  -15.826 1.00 72.29  ?  608  ASN D CG  1 
ATOM   10741 O OD1 . ASN D  1  608 ? 9.231   32.782  -16.446 1.00 72.07  ?  608  ASN D OD1 1 
ATOM   10742 N ND2 . ASN D  1  608 ? 7.480   32.720  -15.054 1.00 72.19  ?  608  ASN D ND2 1 
ATOM   10743 N N   . GLN D  1  609 ? 9.242   36.638  -17.987 1.00 81.68  ?  609  GLN D N   1 
ATOM   10744 C CA  . GLN D  1  609 ? 9.215   37.724  -18.957 1.00 82.18  ?  609  GLN D CA  1 
ATOM   10745 C C   . GLN D  1  609 ? 7.790   38.073  -19.373 1.00 82.37  ?  609  GLN D C   1 
ATOM   10746 O O   . GLN D  1  609 ? 7.564   38.573  -20.478 1.00 82.78  ?  609  GLN D O   1 
ATOM   10747 C CB  . GLN D  1  609 ? 10.058  37.369  -20.181 1.00 82.26  ?  609  GLN D CB  1 
ATOM   10748 C CG  . GLN D  1  609 ? 11.460  37.969  -20.173 1.00 82.81  ?  609  GLN D CG  1 
ATOM   10749 C CD  . GLN D  1  609 ? 12.338  37.413  -21.285 1.00 82.90  ?  609  GLN D CD  1 
ATOM   10750 O OE1 . GLN D  1  609 ? 12.004  37.511  -22.469 1.00 83.45  ?  609  GLN D OE1 1 
ATOM   10751 N NE2 . GLN D  1  609 ? 13.463  36.813  -20.906 1.00 82.92  ?  609  GLN D NE2 1 
ATOM   10752 N N   . LEU D  1  610 ? 6.822   37.814  -18.497 1.00 79.88  ?  610  LEU D N   1 
ATOM   10753 C CA  . LEU D  1  610 ? 5.429   38.085  -18.819 1.00 80.25  ?  610  LEU D CA  1 
ATOM   10754 C C   . LEU D  1  610 ? 5.195   39.583  -18.948 1.00 80.93  ?  610  LEU D C   1 
ATOM   10755 O O   . LEU D  1  610 ? 5.749   40.382  -18.187 1.00 81.46  ?  610  LEU D O   1 
ATOM   10756 C CB  . LEU D  1  610 ? 4.507   37.505  -17.747 1.00 80.12  ?  610  LEU D CB  1 
ATOM   10757 C CG  . LEU D  1  610 ? 4.617   36.007  -17.462 1.00 79.56  ?  610  LEU D CG  1 
ATOM   10758 C CD1 . LEU D  1  610 ? 4.580   35.736  -15.968 1.00 79.45  ?  610  LEU D CD1 1 
ATOM   10759 C CD2 . LEU D  1  610 ? 3.509   35.254  -18.176 1.00 79.79  ?  610  LEU D CD2 1 
ATOM   10760 N N   . ASP D  1  611 ? 4.374   39.963  -19.926 1.00 88.07  ?  611  ASP D N   1 
ATOM   10761 C CA  . ASP D  1  611 ? 3.996   41.363  -20.089 1.00 90.58  ?  611  ASP D CA  1 
ATOM   10762 C C   . ASP D  1  611 ? 2.483   41.490  -20.237 1.00 91.58  ?  611  ASP D C   1 
ATOM   10763 O O   . ASP D  1  611 ? 1.756   40.503  -20.082 1.00 89.88  ?  611  ASP D O   1 
ATOM   10764 C CB  . ASP D  1  611 ? 4.726   41.995  -21.284 1.00 92.96  ?  611  ASP D CB  1 
ATOM   10765 C CG  . ASP D  1  611 ? 4.298   41.411  -22.621 1.00 92.99  ?  611  ASP D CG  1 
ATOM   10766 O OD1 . ASP D  1  611 ? 3.619   40.364  -22.644 1.00 90.86  ?  611  ASP D OD1 1 
ATOM   10767 O OD2 . ASP D  1  611 ? 4.649   42.008  -23.661 1.00 95.72  -1 611  ASP D OD2 1 
ATOM   10768 N N   . GLY D  1  612 ? 2.001   42.690  -20.537 1.00 92.21  ?  612  GLY D N   1 
ATOM   10769 C CA  . GLY D  1  612 ? 0.573   42.930  -20.565 1.00 93.89  ?  612  GLY D CA  1 
ATOM   10770 C C   . GLY D  1  612 ? 0.040   43.355  -19.212 1.00 94.41  ?  612  GLY D C   1 
ATOM   10771 O O   . GLY D  1  612 ? 0.780   43.665  -18.275 1.00 94.10  ?  612  GLY D O   1 
ATOM   10772 N N   . GLU D  1  613 ? -1.285  43.366  -19.114 1.00 95.32  ?  613  GLU D N   1 
ATOM   10773 C CA  . GLU D  1  613 ? -1.972  43.858  -17.930 1.00 96.73  ?  613  GLU D CA  1 
ATOM   10774 C C   . GLU D  1  613 ? -2.535  42.707  -17.104 1.00 93.71  ?  613  GLU D C   1 
ATOM   10775 O O   . GLU D  1  613 ? -2.909  41.658  -17.637 1.00 91.64  ?  613  GLU D O   1 
ATOM   10776 C CB  . GLU D  1  613 ? -3.093  44.823  -18.321 1.00 101.17 ?  613  GLU D CB  1 
ATOM   10777 C CG  . GLU D  1  613 ? -2.587  46.048  -19.064 1.00 104.70 ?  613  GLU D CG  1 
ATOM   10778 C CD  . GLU D  1  613 ? -3.647  47.110  -19.228 1.00 109.54 ?  613  GLU D CD  1 
ATOM   10779 O OE1 . GLU D  1  613 ? -4.637  46.854  -19.945 1.00 110.74 ?  613  GLU D OE1 1 
ATOM   10780 O OE2 . GLU D  1  613 ? -3.491  48.201  -18.640 1.00 112.47 -1 613  GLU D OE2 1 
ATOM   10781 N N   . ILE D  1  614 ? -2.590  42.921  -15.790 1.00 94.12  ?  614  ILE D N   1 
ATOM   10782 C CA  . ILE D  1  614 ? -3.168  41.936  -14.882 1.00 91.92  ?  614  ILE D CA  1 
ATOM   10783 C C   . ILE D  1  614 ? -4.679  41.942  -15.058 1.00 94.13  ?  614  ILE D C   1 
ATOM   10784 O O   . ILE D  1  614 ? -5.341  42.957  -14.813 1.00 97.96  ?  614  ILE D O   1 
ATOM   10785 C CB  . ILE D  1  614 ? -2.781  42.230  -13.428 1.00 92.13  ?  614  ILE D CB  1 
ATOM   10786 C CG1 . ILE D  1  614 ? -1.264  42.349  -13.294 1.00 90.83  ?  614  ILE D CG1 1 
ATOM   10787 C CG2 . ILE D  1  614 ? -3.319  41.143  -12.509 1.00 90.12  ?  614  ILE D CG2 1 
ATOM   10788 C CD1 . ILE D  1  614 ? -0.818  43.010  -12.021 1.00 92.44  ?  614  ILE D CD1 1 
ATOM   10789 N N   . SER D  1  615 ? -5.228  40.812  -15.495 1.00 98.44  ?  615  SER D N   1 
ATOM   10790 C CA  . SER D  1  615 ? -6.651  40.740  -15.791 1.00 100.79 ?  615  SER D CA  1 
ATOM   10791 C C   . SER D  1  615 ? -7.483  40.931  -14.530 1.00 102.54 ?  615  SER D C   1 
ATOM   10792 O O   . SER D  1  615 ? -7.238  40.288  -13.505 1.00 100.27 ?  615  SER D O   1 
ATOM   10793 C CB  . SER D  1  615 ? -6.989  39.399  -16.439 1.00 98.51  ?  615  SER D CB  1 
ATOM   10794 O OG  . SER D  1  615 ? -8.381  39.306  -16.682 1.00 101.07 ?  615  SER D OG  1 
ATOM   10795 N N   . SER D  1  616 ? -8.479  41.816  -14.616 1.00 101.02 ?  616  SER D N   1 
ATOM   10796 C CA  . SER D  1  616 ? -9.453  41.964  -13.543 1.00 103.46 ?  616  SER D CA  1 
ATOM   10797 C C   . SER D  1  616 ? -10.297 40.714  -13.358 1.00 102.10 ?  616  SER D C   1 
ATOM   10798 O O   . SER D  1  616 ? -10.963 40.583  -12.325 1.00 103.43 ?  616  SER D O   1 
ATOM   10799 C CB  . SER D  1  616 ? -10.362 43.162  -13.815 1.00 108.95 ?  616  SER D CB  1 
ATOM   10800 O OG  . SER D  1  616 ? -11.099 42.976  -15.010 1.00 110.47 ?  616  SER D OG  1 
ATOM   10801 N N   . GLN D  1  617 ? -10.279 39.798  -14.330 1.00 106.42 ?  617  GLN D N   1 
ATOM   10802 C CA  . GLN D  1  617 ? -10.981 38.527  -14.226 1.00 105.07 ?  617  GLN D CA  1 
ATOM   10803 C C   . GLN D  1  617 ? -10.422 37.636  -13.127 1.00 101.44 ?  617  GLN D C   1 
ATOM   10804 O O   . GLN D  1  617 ? -11.029 36.601  -12.828 1.00 100.74 ?  617  GLN D O   1 
ATOM   10805 C CB  . GLN D  1  617 ? -10.932 37.789  -15.567 1.00 103.66 ?  617  GLN D CB  1 
ATOM   10806 C CG  . GLN D  1  617 ? -12.131 36.894  -15.828 1.00 105.00 ?  617  GLN D CG  1 
ATOM   10807 C CD  . GLN D  1  617 ? -13.428 37.673  -15.858 1.00 110.45 ?  617  GLN D CD  1 
ATOM   10808 O OE1 . GLN D  1  617 ? -13.591 38.594  -16.658 1.00 113.46 ?  617  GLN D OE1 1 
ATOM   10809 N NE2 . GLN D  1  617 ? -14.357 37.316  -14.975 1.00 112.10 ?  617  GLN D NE2 1 
ATOM   10810 N N   . PHE D  1  618 ? -9.288  38.008  -12.521 1.00 103.98 ?  618  PHE D N   1 
ATOM   10811 C CA  . PHE D  1  618 ? -8.746  37.243  -11.402 1.00 101.75 ?  618  PHE D CA  1 
ATOM   10812 C C   . PHE D  1  618 ? -9.728  37.164  -10.241 1.00 103.53 ?  618  PHE D C   1 
ATOM   10813 O O   . PHE D  1  618 ? -9.597  36.276  -9.391  1.00 102.22 ?  618  PHE D O   1 
ATOM   10814 C CB  . PHE D  1  618 ? -7.424  37.857  -10.928 1.00 100.90 ?  618  PHE D CB  1 
ATOM   10815 C CG  . PHE D  1  618 ? -6.210  37.321  -11.641 1.00 99.51  ?  618  PHE D CG  1 
ATOM   10816 C CD1 . PHE D  1  618 ? -6.319  36.765  -12.903 1.00 99.26  ?  618  PHE D CD1 1 
ATOM   10817 C CD2 . PHE D  1  618 ? -4.959  37.369  -11.045 1.00 99.08  ?  618  PHE D CD2 1 
ATOM   10818 C CE1 . PHE D  1  618 ? -5.207  36.268  -13.561 1.00 98.51  ?  618  PHE D CE1 1 
ATOM   10819 C CE2 . PHE D  1  618 ? -3.841  36.874  -11.699 1.00 98.30  ?  618  PHE D CE2 1 
ATOM   10820 C CZ  . PHE D  1  618 ? -3.968  36.323  -12.958 1.00 97.97  ?  618  PHE D CZ  1 
ATOM   10821 N N   . ARG D  1  619 ? -10.718 38.064  -10.206 1.00 101.34 ?  619  ARG D N   1 
ATOM   10822 C CA  . ARG D  1  619 ? -11.737 38.092  -9.162  1.00 104.44 ?  619  ARG D CA  1 
ATOM   10823 C C   . ARG D  1  619 ? -12.429 36.750  -8.966  1.00 103.26 ?  619  ARG D C   1 
ATOM   10824 O O   . ARG D  1  619 ? -12.994 36.506  -7.894  1.00 104.86 ?  619  ARG D O   1 
ATOM   10825 C CB  . ARG D  1  619 ? -12.773 39.166  -9.504  1.00 109.72 ?  619  ARG D CB  1 
ATOM   10826 C CG  . ARG D  1  619 ? -13.663 39.590  -8.352  1.00 113.93 ?  619  ARG D CG  1 
ATOM   10827 C CD  . ARG D  1  619 ? -14.964 40.172  -8.871  1.00 119.05 ?  619  ARG D CD  1 
ATOM   10828 N NE  . ARG D  1  619 ? -15.679 40.918  -7.842  1.00 123.88 ?  619  ARG D NE  1 
ATOM   10829 C CZ  . ARG D  1  619 ? -16.992 40.871  -7.659  1.00 128.22 ?  619  ARG D CZ  1 
ATOM   10830 N NH1 . ARG D  1  619 ? -17.769 40.112  -8.414  1.00 128.47 ?  619  ARG D NH1 1 
ATOM   10831 N NH2 . ARG D  1  619 ? -17.540 41.606  -6.693  1.00 132.82 ?  619  ARG D NH2 1 
ATOM   10832 N N   . SER D  1  620 ? -12.377 35.865  -9.963  1.00 101.59 ?  620  SER D N   1 
ATOM   10833 C CA  . SER D  1  620 ? -13.080 34.590  -9.881  1.00 100.96 ?  620  SER D CA  1 
ATOM   10834 C C   . SER D  1  620 ? -12.457 33.640  -8.866  1.00 98.22  ?  620  SER D C   1 
ATOM   10835 O O   . SER D  1  620 ? -13.151 32.750  -8.361  1.00 98.64  ?  620  SER D O   1 
ATOM   10836 C CB  . SER D  1  620 ? -13.105 33.921  -11.257 1.00 99.61  ?  620  SER D CB  1 
ATOM   10837 O OG  . SER D  1  620 ? -13.534 34.824  -12.263 1.00 102.41 ?  620  SER D OG  1 
ATOM   10838 N N   . LEU D  1  621 ? -11.169 33.803  -8.560  1.00 94.63  ?  621  LEU D N   1 
ATOM   10839 C CA  . LEU D  1  621 ? -10.421 32.837  -7.751  1.00 94.25  ?  621  LEU D CA  1 
ATOM   10840 C C   . LEU D  1  621 ? -10.797 33.020  -6.281  1.00 95.03  ?  621  LEU D C   1 
ATOM   10841 O O   . LEU D  1  621 ? -10.089 33.651  -5.492  1.00 95.20  ?  621  LEU D O   1 
ATOM   10842 C CB  . LEU D  1  621 ? -8.921  32.989  -7.994  1.00 93.54  ?  621  LEU D CB  1 
ATOM   10843 C CG  . LEU D  1  621 ? -8.335  32.266  -9.219  1.00 92.58  ?  621  LEU D CG  1 
ATOM   10844 C CD1 . LEU D  1  621 ? -9.295  32.252  -10.369 1.00 93.05  ?  621  LEU D CD1 1 
ATOM   10845 C CD2 . LEU D  1  621 ? -7.037  32.887  -9.696  1.00 91.92  ?  621  LEU D CD2 1 
ATOM   10846 N N   . GLN D  1  622 ? -11.943 32.434  -5.913  1.00 90.59  ?  622  GLN D N   1 
ATOM   10847 C CA  . GLN D  1  622 ? -12.530 32.650  -4.592  1.00 92.54  ?  622  GLN D CA  1 
ATOM   10848 C C   . GLN D  1  622 ? -11.653 32.138  -3.458  1.00 91.69  ?  622  GLN D C   1 
ATOM   10849 O O   . GLN D  1  622 ? -11.777 32.621  -2.329  1.00 93.29  ?  622  GLN D O   1 
ATOM   10850 C CB  . GLN D  1  622 ? -13.903 31.979  -4.512  1.00 94.80  ?  622  GLN D CB  1 
ATOM   10851 C CG  . GLN D  1  622 ? -14.968 32.622  -5.383  1.00 98.31  ?  622  GLN D CG  1 
ATOM   10852 C CD  . GLN D  1  622 ? -15.661 33.778  -4.694  1.00 103.43 ?  622  GLN D CD  1 
ATOM   10853 O OE1 . GLN D  1  622 ? -15.059 34.827  -4.463  1.00 103.92 ?  622  GLN D OE1 1 
ATOM   10854 N NE2 . GLN D  1  622 ? -16.933 33.592  -4.357  1.00 107.63 ?  622  GLN D NE2 1 
ATOM   10855 N N   . ASN D  1  623 ? -10.769 31.183  -3.727  1.00 89.86  ?  623  ASN D N   1 
ATOM   10856 C CA  . ASN D  1  623 ? -9.969  30.555  -2.686  1.00 90.31  ?  623  ASN D CA  1 
ATOM   10857 C C   . ASN D  1  623 ? -8.521  31.024  -2.673  1.00 90.05  ?  623  ASN D C   1 
ATOM   10858 O O   . ASN D  1  623 ? -7.731  30.521  -1.867  1.00 90.53  ?  623  ASN D O   1 
ATOM   10859 C CB  . ASN D  1  623 ? -10.016 29.029  -2.841  1.00 90.17  ?  623  ASN D CB  1 
ATOM   10860 C CG  . ASN D  1  623 ? -11.346 28.439  -2.413  1.00 90.67  ?  623  ASN D CG  1 
ATOM   10861 O OD1 . ASN D  1  623 ? -11.683 28.441  -1.230  1.00 91.50  ?  623  ASN D OD1 1 
ATOM   10862 N ND2 . ASN D  1  623 ? -12.109 27.932  -3.374  1.00 90.15  ?  623  ASN D ND2 1 
ATOM   10863 N N   . LEU D  1  624 ? -8.151  31.974  -3.531  1.00 87.87  ?  624  LEU D N   1 
ATOM   10864 C CA  . LEU D  1  624 ? -6.751  32.360  -3.666  1.00 87.43  ?  624  LEU D CA  1 
ATOM   10865 C C   . LEU D  1  624 ? -6.269  33.078  -2.411  1.00 88.21  ?  624  LEU D C   1 
ATOM   10866 O O   . LEU D  1  624 ? -6.780  34.145  -2.058  1.00 88.54  ?  624  LEU D O   1 
ATOM   10867 C CB  . LEU D  1  624 ? -6.559  33.246  -4.894  1.00 86.57  ?  624  LEU D CB  1 
ATOM   10868 C CG  . LEU D  1  624 ? -5.199  33.113  -5.588  1.00 85.67  ?  624  LEU D CG  1 
ATOM   10869 C CD1 . LEU D  1  624 ? -5.244  33.675  -6.980  1.00 85.08  ?  624  LEU D CD1 1 
ATOM   10870 C CD2 . LEU D  1  624 ? -4.130  33.830  -4.802  1.00 85.84  ?  624  LEU D CD2 1 
ATOM   10871 N N   . GLU D  1  625 ? -5.266  32.500  -1.752  1.00 86.18  ?  625  GLU D N   1 
ATOM   10872 C CA  . GLU D  1  625 ? -4.667  33.088  -0.561  1.00 86.94  ?  625  GLU D CA  1 
ATOM   10873 C C   . GLU D  1  625 ? -3.322  33.751  -0.820  1.00 86.45  ?  625  GLU D C   1 
ATOM   10874 O O   . GLU D  1  625 ? -2.992  34.729  -0.141  1.00 86.84  ?  625  GLU D O   1 
ATOM   10875 C CB  . GLU D  1  625 ? -4.489  32.022  0.526   1.00 87.92  ?  625  GLU D CB  1 
ATOM   10876 C CG  . GLU D  1  625 ? -5.772  31.333  0.943   1.00 88.48  ?  625  GLU D CG  1 
ATOM   10877 C CD  . GLU D  1  625 ? -5.591  30.468  2.172   1.00 89.55  ?  625  GLU D CD  1 
ATOM   10878 O OE1 . GLU D  1  625 ? -4.888  30.902  3.109   1.00 90.15  ?  625  GLU D OE1 1 
ATOM   10879 O OE2 . GLU D  1  625 ? -6.157  29.355  2.202   1.00 89.79  -1 625  GLU D OE2 1 
ATOM   10880 N N   . ARG D  1  626 ? -2.537  33.253  -1.780  1.00 86.45  ?  626  ARG D N   1 
ATOM   10881 C CA  . ARG D  1  626 ? -1.182  33.741  -2.016  1.00 85.94  ?  626  ARG D CA  1 
ATOM   10882 C C   . ARG D  1  626 ? -0.952  34.000  -3.495  1.00 84.64  ?  626  ARG D C   1 
ATOM   10883 O O   . ARG D  1  626 ? -1.178  33.114  -4.325  1.00 84.00  ?  626  ARG D O   1 
ATOM   10884 C CB  . ARG D  1  626 ? -0.137  32.751  -1.511  1.00 86.27  ?  626  ARG D CB  1 
ATOM   10885 C CG  . ARG D  1  626 ? 0.204   32.946  -0.063  1.00 87.50  ?  626  ARG D CG  1 
ATOM   10886 C CD  . ARG D  1  626 ? 0.658   31.649  0.558   1.00 88.18  ?  626  ARG D CD  1 
ATOM   10887 N NE  . ARG D  1  626 ? 1.352   31.854  1.823   1.00 89.12  ?  626  ARG D NE  1 
ATOM   10888 C CZ  . ARG D  1  626 ? 2.558   32.391  1.944   1.00 89.00  ?  626  ARG D CZ  1 
ATOM   10889 N NH1 . ARG D  1  626 ? 3.249   32.790  0.886   1.00 87.98  ?  626  ARG D NH1 1 
ATOM   10890 N NH2 . ARG D  1  626 ? 3.087   32.530  3.158   1.00 89.92  ?  626  ARG D NH2 1 
ATOM   10891 N N   . LEU D  1  627 ? -0.448  35.196  -3.809  1.00 81.28  ?  627  LEU D N   1 
ATOM   10892 C CA  . LEU D  1  627 ? -0.259  35.625  -5.188  1.00 80.22  ?  627  LEU D CA  1 
ATOM   10893 C C   . LEU D  1  627 ? 1.106   36.289  -5.307  1.00 79.88  ?  627  LEU D C   1 
ATOM   10894 O O   . LEU D  1  627 ? 1.482   37.095  -4.449  1.00 80.56  ?  627  LEU D O   1 
ATOM   10895 C CB  . LEU D  1  627 ? -1.349  36.613  -5.621  1.00 80.31  ?  627  LEU D CB  1 
ATOM   10896 C CG  . LEU D  1  627 ? -1.363  36.924  -7.118  1.00 79.38  ?  627  LEU D CG  1 
ATOM   10897 C CD1 . LEU D  1  627 ? -1.012  35.652  -7.895  1.00 78.58  ?  627  LEU D CD1 1 
ATOM   10898 C CD2 . LEU D  1  627 ? -2.696  37.493  -7.577  1.00 79.63  ?  627  LEU D CD2 1 
ATOM   10899 N N   . ASP D  1  628 ? 1.847   35.943  -6.362  1.00 76.28  ?  628  ASP D N   1 
ATOM   10900 C CA  . ASP D  1  628 ? 3.145   36.555  -6.642  1.00 75.94  ?  628  ASP D CA  1 
ATOM   10901 C C   . ASP D  1  628 ? 3.262   36.793  -8.143  1.00 74.97  ?  628  ASP D C   1 
ATOM   10902 O O   . ASP D  1  628 ? 3.375   35.836  -8.916  1.00 74.21  ?  628  ASP D O   1 
ATOM   10903 C CB  . ASP D  1  628 ? 4.291   35.676  -6.138  1.00 75.95  ?  628  ASP D CB  1 
ATOM   10904 C CG  . ASP D  1  628 ? 5.614   36.417  -6.085  1.00 76.05  ?  628  ASP D CG  1 
ATOM   10905 O OD1 . ASP D  1  628 ? 5.668   37.578  -6.543  1.00 76.05  ?  628  ASP D OD1 1 
ATOM   10906 O OD2 . ASP D  1  628 ? 6.601   35.842  -5.579  1.00 76.25  -1 628  ASP D OD2 1 
ATOM   10907 N N   . LEU D  1  629 ? 3.247   38.065  -8.551  1.00 74.19  ?  629  LEU D N   1 
ATOM   10908 C CA  . LEU D  1  629 ? 3.482   38.473  -9.935  1.00 74.31  ?  629  LEU D CA  1 
ATOM   10909 C C   . LEU D  1  629 ? 4.766   39.274  -10.088 1.00 76.05  ?  629  LEU D C   1 
ATOM   10910 O O   . LEU D  1  629 ? 4.956   39.944  -11.108 1.00 77.36  ?  629  LEU D O   1 
ATOM   10911 C CB  . LEU D  1  629 ? 2.315   39.300  -10.484 1.00 76.64  ?  629  LEU D CB  1 
ATOM   10912 C CG  . LEU D  1  629 ? 1.059   38.670  -11.087 1.00 75.52  ?  629  LEU D CG  1 
ATOM   10913 C CD1 . LEU D  1  629 ? 0.688   37.388  -10.379 1.00 72.87  ?  629  LEU D CD1 1 
ATOM   10914 C CD2 . LEU D  1  629 ? -0.100  39.645  -11.036 1.00 78.94  ?  629  LEU D CD2 1 
ATOM   10915 N N   . SER D  1  630 ? 5.648   39.216  -9.098  1.00 80.44  ?  630  SER D N   1 
ATOM   10916 C CA  . SER D  1  630 ? 6.818   40.074  -9.084  1.00 80.87  ?  630  SER D CA  1 
ATOM   10917 C C   . SER D  1  630 ? 7.800   39.674  -10.180 1.00 80.20  ?  630  SER D C   1 
ATOM   10918 O O   . SER D  1  630 ? 7.763   38.561  -10.714 1.00 79.39  ?  630  SER D O   1 
ATOM   10919 C CB  . SER D  1  630 ? 7.500   40.020  -7.719  1.00 81.77  ?  630  SER D CB  1 
ATOM   10920 O OG  . SER D  1  630 ? 8.006   38.723  -7.463  1.00 81.45  ?  630  SER D OG  1 
ATOM   10921 N N   . HIS D  1  631 ? 8.692   40.612  -10.504 1.00 82.49  ?  631  HIS D N   1 
ATOM   10922 C CA  . HIS D  1  631 ? 9.789   40.376  -11.439 1.00 82.18  ?  631  HIS D CA  1 
ATOM   10923 C C   . HIS D  1  631 ? 9.266   39.931  -12.808 1.00 81.20  ?  631  HIS D C   1 
ATOM   10924 O O   . HIS D  1  631 ? 9.503   38.812  -13.268 1.00 80.49  ?  631  HIS D O   1 
ATOM   10925 C CB  . HIS D  1  631 ? 10.786  39.373  -10.849 1.00 82.25  ?  631  HIS D CB  1 
ATOM   10926 C CG  . HIS D  1  631 ? 11.515  39.898  -9.648  1.00 83.53  ?  631  HIS D CG  1 
ATOM   10927 N ND1 . HIS D  1  631 ? 12.692  40.609  -9.744  1.00 84.97  ?  631  HIS D ND1 1 
ATOM   10928 C CD2 . HIS D  1  631 ? 11.222  39.835  -8.327  1.00 84.19  ?  631  HIS D CD2 1 
ATOM   10929 C CE1 . HIS D  1  631 ? 13.098  40.953  -8.535  1.00 86.71  ?  631  HIS D CE1 1 
ATOM   10930 N NE2 . HIS D  1  631 ? 12.224  40.496  -7.657  1.00 85.81  ?  631  HIS D NE2 1 
ATOM   10931 N N   . ASN D  1  632 ? 8.514   40.836  -13.434 1.00 82.26  ?  632  ASN D N   1 
ATOM   10932 C CA  . ASN D  1  632 ? 7.963   40.647  -14.773 1.00 81.64  ?  632  ASN D CA  1 
ATOM   10933 C C   . ASN D  1  632 ? 7.889   42.015  -15.452 1.00 84.01  ?  632  ASN D C   1 
ATOM   10934 O O   . ASN D  1  632 ? 8.486   42.987  -14.982 1.00 86.75  ?  632  ASN D O   1 
ATOM   10935 C CB  . ASN D  1  632 ? 6.598   39.949  -14.698 1.00 81.19  ?  632  ASN D CB  1 
ATOM   10936 C CG  . ASN D  1  632 ? 6.720   38.446  -14.495 1.00 80.55  ?  632  ASN D CG  1 
ATOM   10937 O OD1 . ASN D  1  632 ? 6.920   37.700  -15.451 1.00 80.05  ?  632  ASN D OD1 1 
ATOM   10938 N ND2 . ASN D  1  632 ? 6.591   37.998  -13.250 1.00 80.71  ?  632  ASN D ND2 1 
ATOM   10939 N N   . ASN D  1  633 ? 7.166   42.093  -16.574 1.00 91.53  ?  633  ASN D N   1 
ATOM   10940 C CA  . ASN D  1  633 ? 7.006   43.339  -17.324 1.00 95.07  ?  633  ASN D CA  1 
ATOM   10941 C C   . ASN D  1  633 ? 5.543   43.763  -17.394 1.00 96.19  ?  633  ASN D C   1 
ATOM   10942 O O   . ASN D  1  633 ? 5.127   44.416  -18.355 1.00 98.61  ?  633  ASN D O   1 
ATOM   10943 C CB  . ASN D  1  633 ? 7.574   43.203  -18.739 1.00 95.51  ?  633  ASN D CB  1 
ATOM   10944 C CG  . ASN D  1  633 ? 8.156   44.515  -19.295 1.00 99.91  ?  633  ASN D CG  1 
ATOM   10945 O OD1 . ASN D  1  633 ? 8.483   45.445  -18.555 1.00 102.46 ?  633  ASN D OD1 1 
ATOM   10946 N ND2 . ASN D  1  633 ? 8.280   44.572  -20.628 1.00 101.10 ?  633  ASN D ND2 1 
ATOM   10947 N N   . LEU D  1  634 ? 4.749   43.391  -16.393 1.00 91.60  ?  634  LEU D N   1 
ATOM   10948 C CA  . LEU D  1  634 ? 3.341   43.764  -16.394 1.00 93.02  ?  634  LEU D CA  1 
ATOM   10949 C C   . LEU D  1  634 ? 3.185   45.281  -16.370 1.00 97.64  ?  634  LEU D C   1 
ATOM   10950 O O   . LEU D  1  634 ? 3.939   45.988  -15.698 1.00 99.50  ?  634  LEU D O   1 
ATOM   10951 C CB  . LEU D  1  634 ? 2.625   43.138  -15.198 1.00 91.24  ?  634  LEU D CB  1 
ATOM   10952 C CG  . LEU D  1  634 ? 2.643   41.612  -15.135 1.00 87.48  ?  634  LEU D CG  1 
ATOM   10953 C CD1 . LEU D  1  634 ? 3.137   41.095  -13.790 1.00 86.57  ?  634  LEU D CD1 1 
ATOM   10954 C CD2 . LEU D  1  634 ? 1.255   41.122  -15.418 1.00 87.34  ?  634  LEU D CD2 1 
ATOM   10955 N N   . SER D  1  635 ? 2.189   45.779  -17.100 1.00 96.42  ?  635  SER D N   1 
ATOM   10956 C CA  . SER D  1  635 ? 1.925   47.208  -17.198 1.00 101.15 ?  635  SER D CA  1 
ATOM   10957 C C   . SER D  1  635 ? 0.463   47.473  -16.854 1.00 102.84 ?  635  SER D C   1 
ATOM   10958 O O   . SER D  1  635 ? -0.311  46.552  -16.574 1.00 100.40 ?  635  SER D O   1 
ATOM   10959 C CB  . SER D  1  635 ? 2.260   47.741  -18.595 1.00 103.37 ?  635  SER D CB  1 
ATOM   10960 O OG  . SER D  1  635 ? 1.272   47.342  -19.528 1.00 103.22 ?  635  SER D OG  1 
ATOM   10961 N N   . GLY D  1  636 ? 0.083   48.747  -16.882 1.00 104.15 ?  636  GLY D N   1 
ATOM   10962 C CA  . GLY D  1  636 ? -1.253  49.136  -16.494 1.00 106.57 ?  636  GLY D CA  1 
ATOM   10963 C C   . GLY D  1  636 ? -1.407  49.235  -14.988 1.00 106.83 ?  636  GLY D C   1 
ATOM   10964 O O   . GLY D  1  636 ? -0.443  49.187  -14.220 1.00 105.77 ?  636  GLY D O   1 
ATOM   10965 N N   . GLN D  1  637 ? -2.658  49.367  -14.564 1.00 108.67 ?  637  GLN D N   1 
ATOM   10966 C CA  . GLN D  1  637 ? -2.984  49.532  -13.157 1.00 109.78 ?  637  GLN D CA  1 
ATOM   10967 C C   . GLN D  1  637 ? -3.468  48.218  -12.560 1.00 105.97 ?  637  GLN D C   1 
ATOM   10968 O O   . GLN D  1  637 ? -4.094  47.401  -13.241 1.00 103.95 ?  637  GLN D O   1 
ATOM   10969 C CB  . GLN D  1  637 ? -4.047  50.615  -12.971 1.00 115.09 ?  637  GLN D CB  1 
ATOM   10970 C CG  . GLN D  1  637 ? -3.724  51.917  -13.685 1.00 119.33 ?  637  GLN D CG  1 
ATOM   10971 C CD  . GLN D  1  637 ? -4.362  53.116  -13.017 1.00 124.93 ?  637  GLN D CD  1 
ATOM   10972 O OE1 . GLN D  1  637 ? -5.102  52.975  -12.043 1.00 125.79 ?  637  GLN D OE1 1 
ATOM   10973 N NE2 . GLN D  1  637 ? -4.082  54.306  -13.538 1.00 129.11 ?  637  GLN D NE2 1 
ATOM   10974 N N   . ILE D  1  638 ? -3.158  48.014  -11.282 1.00 109.47 ?  638  ILE D N   1 
ATOM   10975 C CA  . ILE D  1  638 ? -3.662  46.849  -10.560 1.00 106.55 ?  638  ILE D CA  1 
ATOM   10976 C C   . ILE D  1  638 ? -5.182  46.953  -10.565 1.00 109.07 ?  638  ILE D C   1 
ATOM   10977 O O   . ILE D  1  638 ? -5.732  47.959  -10.092 1.00 113.58 ?  638  ILE D O   1 
ATOM   10978 C CB  . ILE D  1  638 ? -3.107  46.766  -9.130  1.00 106.43 ?  638  ILE D CB  1 
ATOM   10979 C CG1 . ILE D  1  638 ? -1.593  46.963  -9.122  1.00 105.43 ?  638  ILE D CG1 1 
ATOM   10980 C CG2 . ILE D  1  638 ? -3.448  45.421  -8.516  1.00 102.92 ?  638  ILE D CG2 1 
ATOM   10981 C CD1 . ILE D  1  638 ? -1.021  47.218  -7.745  1.00 106.89 ?  638  ILE D CD1 1 
ATOM   10982 N N   . PRO D  1  639 ? -5.886  45.961  -11.103 1.00 108.60 ?  639  PRO D N   1 
ATOM   10983 C CA  . PRO D  1  639 ? -7.342  46.073  -11.280 1.00 111.49 ?  639  PRO D CA  1 
ATOM   10984 C C   . PRO D  1  639 ? -8.050  46.304  -9.958  1.00 114.21 ?  639  PRO D C   1 
ATOM   10985 O O   . PRO D  1  639 ? -7.920  45.500  -9.022  1.00 111.93 ?  639  PRO D O   1 
ATOM   10986 C CB  . PRO D  1  639 ? -7.730  44.717  -11.893 1.00 107.83 ?  639  PRO D CB  1 
ATOM   10987 C CG  . PRO D  1  639 ? -6.576  43.816  -11.608 1.00 103.03 ?  639  PRO D CG  1 
ATOM   10988 C CD  . PRO D  1  639 ? -5.366  44.687  -11.620 1.00 103.59 ?  639  PRO D CD  1 
ATOM   10989 N N   . PRO D  1  640 ? -8.801  47.405  -9.839  1.00 113.34 ?  640  PRO D N   1 
ATOM   10990 C CA  . PRO D  1  640 ? -9.498  47.695  -8.575  1.00 116.64 ?  640  PRO D CA  1 
ATOM   10991 C C   . PRO D  1  640 ? -10.508 46.643  -8.143  1.00 115.78 ?  640  PRO D C   1 
ATOM   10992 O O   . PRO D  1  640 ? -11.037 46.755  -7.033  1.00 118.37 ?  640  PRO D O   1 
ATOM   10993 C CB  . PRO D  1  640 ? -10.184 49.039  -8.853  1.00 122.62 ?  640  PRO D CB  1 
ATOM   10994 C CG  . PRO D  1  640 ? -9.308  49.683  -9.860  1.00 122.27 ?  640  PRO D CG  1 
ATOM   10995 C CD  . PRO D  1  640 ? -8.831  48.562  -10.751 1.00 116.86 ?  640  PRO D CD  1 
ATOM   10996 N N   . SER D  1  641 ? -10.796 45.630  -8.960  1.00 121.01 ?  641  SER D N   1 
ATOM   10997 C CA  . SER D  1  641 ? -11.693 44.568  -8.518  1.00 120.24 ?  641  SER D CA  1 
ATOM   10998 C C   . SER D  1  641 ? -11.118 43.745  -7.368  1.00 117.16 ?  641  SER D C   1 
ATOM   10999 O O   . SER D  1  641 ? -11.860 42.968  -6.757  1.00 117.27 ?  641  SER D O   1 
ATOM   11000 C CB  . SER D  1  641 ? -12.036 43.648  -9.692  1.00 117.69 ?  641  SER D CB  1 
ATOM   11001 O OG  . SER D  1  641 ? -13.024 42.700  -9.324  1.00 117.83 ?  641  SER D OG  1 
ATOM   11002 N N   . PHE D  1  642 ? -9.831  43.909  -7.051  1.00 119.14 ?  642  PHE D N   1 
ATOM   11003 C CA  . PHE D  1  642 ? -9.157  43.057  -6.077  1.00 116.02 ?  642  PHE D CA  1 
ATOM   11004 C C   . PHE D  1  642 ? -9.538  43.369  -4.632  1.00 119.40 ?  642  PHE D C   1 
ATOM   11005 O O   . PHE D  1  642 ? -9.121  42.630  -3.732  1.00 117.43 ?  642  PHE D O   1 
ATOM   11006 C CB  . PHE D  1  642 ? -7.636  43.158  -6.258  1.00 113.03 ?  642  PHE D CB  1 
ATOM   11007 C CG  . PHE D  1  642 ? -7.108  42.391  -7.448  1.00 108.69 ?  642  PHE D CG  1 
ATOM   11008 C CD1 . PHE D  1  642 ? -7.977  41.824  -8.371  1.00 108.05 ?  642  PHE D CD1 1 
ATOM   11009 C CD2 . PHE D  1  642 ? -5.744  42.231  -7.639  1.00 105.70 ?  642  PHE D CD2 1 
ATOM   11010 C CE1 . PHE D  1  642 ? -7.495  41.120  -9.464  1.00 104.50 ?  642  PHE D CE1 1 
ATOM   11011 C CE2 . PHE D  1  642 ? -5.257  41.526  -8.730  1.00 102.12 ?  642  PHE D CE2 1 
ATOM   11012 C CZ  . PHE D  1  642 ? -6.133  40.970  -9.641  1.00 101.51 ?  642  PHE D CZ  1 
ATOM   11013 N N   . LYS D  1  643 ? -10.310 44.433  -4.377  1.00 113.20 ?  643  LYS D N   1 
ATOM   11014 C CA  . LYS D  1  643 ? -10.758 44.701  -3.012  1.00 116.97 ?  643  LYS D CA  1 
ATOM   11015 C C   . LYS D  1  643 ? -11.636 43.587  -2.461  1.00 116.45 ?  643  LYS D C   1 
ATOM   11016 O O   . LYS D  1  643 ? -11.768 43.460  -1.238  1.00 118.35 ?  643  LYS D O   1 
ATOM   11017 C CB  . LYS D  1  643 ? -11.581 45.988  -2.935  1.00 123.24 ?  643  LYS D CB  1 
ATOM   11018 C CG  . LYS D  1  643 ? -10.860 47.309  -2.905  1.00 125.98 ?  643  LYS D CG  1 
ATOM   11019 C CD  . LYS D  1  643 ? -10.759 47.890  -4.283  1.00 125.78 ?  643  LYS D CD  1 
ATOM   11020 C CE  . LYS D  1  643 ? -9.489  48.678  -4.392  1.00 125.53 ?  643  LYS D CE  1 
ATOM   11021 N NZ  . LYS D  1  643 ? -8.888  48.706  -5.748  1.00 122.65 ?  643  LYS D NZ  1 
ATOM   11022 N N   . ASP D  1  644 ? -12.248 42.793  -3.334  1.00 122.04 ?  644  ASP D N   1 
ATOM   11023 C CA  . ASP D  1  644 ? -13.205 41.766  -2.949  1.00 122.16 ?  644  ASP D CA  1 
ATOM   11024 C C   . ASP D  1  644 ? -12.551 40.430  -2.614  1.00 117.10 ?  644  ASP D C   1 
ATOM   11025 O O   . ASP D  1  644 ? -13.262 39.474  -2.288  1.00 116.95 ?  644  ASP D O   1 
ATOM   11026 C CB  . ASP D  1  644 ? -14.237 41.580  -4.065  1.00 123.12 ?  644  ASP D CB  1 
ATOM   11027 C CG  . ASP D  1  644 ? -14.831 42.899  -4.535  1.00 128.12 ?  644  ASP D CG  1 
ATOM   11028 O OD1 . ASP D  1  644 ? -14.895 43.853  -3.727  1.00 132.17 ?  644  ASP D OD1 1 
ATOM   11029 O OD2 . ASP D  1  644 ? -15.234 42.983  -5.713  1.00 128.32 -1 644  ASP D OD2 1 
ATOM   11030 N N   . MET D  1  645 ? -11.223 40.342  -2.675  1.00 114.55 ?  645  MET D N   1 
ATOM   11031 C CA  . MET D  1  645 ? -10.511 39.092  -2.412  1.00 109.83 ?  645  MET D CA  1 
ATOM   11032 C C   . MET D  1  645 ? -10.311 38.952  -0.909  1.00 111.34 ?  645  MET D C   1 
ATOM   11033 O O   . MET D  1  645 ? -9.278  39.335  -0.359  1.00 110.98 ?  645  MET D O   1 
ATOM   11034 C CB  . MET D  1  645 ? -9.178  39.079  -3.142  1.00 105.74 ?  645  MET D CB  1 
ATOM   11035 C CG  . MET D  1  645 ? -9.272  39.406  -4.615  1.00 104.96 ?  645  MET D CG  1 
ATOM   11036 S SD  . MET D  1  645 ? -8.122  38.419  -5.586  1.00 98.99  ?  645  MET D SD  1 
ATOM   11037 C CE  . MET D  1  645 ? -8.975  38.384  -7.145  1.00 99.26  ?  645  MET D CE  1 
ATOM   11038 N N   . LEU D  1  646 ? -11.314 38.377  -0.236  1.00 102.19 ?  646  LEU D N   1 
ATOM   11039 C CA  . LEU D  1  646 ? -11.269 38.235  1.216   1.00 104.38 ?  646  LEU D CA  1 
ATOM   11040 C C   . LEU D  1  646 ? -10.284 37.164  1.669   1.00 100.18 ?  646  LEU D C   1 
ATOM   11041 O O   . LEU D  1  646 ? -9.820  37.210  2.814   1.00 101.63 ?  646  LEU D O   1 
ATOM   11042 C CB  . LEU D  1  646 ? -12.665 37.913  1.754   1.00 108.20 ?  646  LEU D CB  1 
ATOM   11043 C CG  . LEU D  1  646 ? -13.787 38.881  1.370   1.00 113.06 ?  646  LEU D CG  1 
ATOM   11044 C CD1 . LEU D  1  646 ? -14.776 38.214  0.428   1.00 112.45 ?  646  LEU D CD1 1 
ATOM   11045 C CD2 . LEU D  1  646 ? -14.496 39.396  2.611   1.00 119.02 ?  646  LEU D CD2 1 
ATOM   11046 N N   . ALA D  1  647 ? -9.958  36.204  0.802   1.00 101.11 ?  647  ALA D N   1 
ATOM   11047 C CA  . ALA D  1  647 ? -9.028  35.141  1.160   1.00 97.25  ?  647  ALA D CA  1 
ATOM   11048 C C   . ALA D  1  647 ? -7.569  35.568  1.054   1.00 95.33  ?  647  ALA D C   1 
ATOM   11049 O O   . ALA D  1  647 ? -6.704  34.919  1.651   1.00 94.22  ?  647  ALA D O   1 
ATOM   11050 C CB  . ALA D  1  647 ? -9.270  33.914  0.276   1.00 94.22  ?  647  ALA D CB  1 
ATOM   11051 N N   . LEU D  1  648 ? -7.283  36.644  0.324   1.00 97.50  ?  648  LEU D N   1 
ATOM   11052 C CA  . LEU D  1  648 ? -5.907  37.010  0.017   1.00 95.66  ?  648  LEU D CA  1 
ATOM   11053 C C   . LEU D  1  648 ? -5.166  37.430  1.283   1.00 97.73  ?  648  LEU D C   1 
ATOM   11054 O O   . LEU D  1  648 ? -5.657  38.255  2.059   1.00 102.16 ?  648  LEU D O   1 
ATOM   11055 C CB  . LEU D  1  648 ? -5.891  38.147  -1.005  1.00 96.54  ?  648  LEU D CB  1 
ATOM   11056 C CG  . LEU D  1  648 ? -4.744  38.221  -2.019  1.00 93.62  ?  648  LEU D CG  1 
ATOM   11057 C CD1 . LEU D  1  648 ? -4.906  39.439  -2.921  1.00 95.67  ?  648  LEU D CD1 1 
ATOM   11058 C CD2 . LEU D  1  648 ? -3.384  38.208  -1.357  1.00 93.11  ?  648  LEU D CD2 1 
ATOM   11059 N N   . THR D  1  649 ? -3.974  36.863  1.486   1.00 92.44  ?  649  THR D N   1 
ATOM   11060 C CA  . THR D  1  649 ? -3.118  37.234  2.603   1.00 94.28  ?  649  THR D CA  1 
ATOM   11061 C C   . THR D  1  649 ? -1.722  37.702  2.200   1.00 93.22  ?  649  THR D C   1 
ATOM   11062 O O   . THR D  1  649 ? -1.096  38.432  2.977   1.00 96.04  ?  649  THR D O   1 
ATOM   11063 C CB  . THR D  1  649 ? -2.981  36.057  3.586   1.00 93.76  ?  649  THR D CB  1 
ATOM   11064 O OG1 . THR D  1  649 ? -2.356  34.948  2.927   1.00 92.96  ?  649  THR D OG1 1 
ATOM   11065 C CG2 . THR D  1  649 ? -4.344  35.625  4.093   1.00 95.23  ?  649  THR D CG2 1 
ATOM   11066 N N   . HIS D  1  650 ? -1.219  37.317  1.024   1.00 91.22  ?  650  HIS D N   1 
ATOM   11067 C CA  . HIS D  1  650 ? 0.142   37.651  0.606   1.00 90.72  ?  650  HIS D CA  1 
ATOM   11068 C C   . HIS D  1  650 ? 0.140   38.084  -0.854  1.00 89.61  ?  650  HIS D C   1 
ATOM   11069 O O   . HIS D  1  650 ? -0.287  37.319  -1.724  1.00 88.94  ?  650  HIS D O   1 
ATOM   11070 C CB  . HIS D  1  650 ? 1.092   36.460  0.793   1.00 90.76  ?  650  HIS D CB  1 
ATOM   11071 C CG  . HIS D  1  650 ? 1.331   36.084  2.222   1.00 91.92  ?  650  HIS D CG  1 
ATOM   11072 N ND1 . HIS D  1  650 ? 0.318   35.697  3.071   1.00 92.84  ?  650  HIS D ND1 1 
ATOM   11073 C CD2 . HIS D  1  650 ? 2.472   36.031  2.950   1.00 92.33  ?  650  HIS D CD2 1 
ATOM   11074 C CE1 . HIS D  1  650 ? 0.823   35.428  4.262   1.00 93.75  ?  650  HIS D CE1 1 
ATOM   11075 N NE2 . HIS D  1  650 ? 2.128   35.621  4.215   1.00 93.49  ?  650  HIS D NE2 1 
ATOM   11076 N N   . VAL D  1  651 ? 0.637   39.295  -1.124  1.00 88.85  ?  651  VAL D N   1 
ATOM   11077 C CA  . VAL D  1  651 ? 0.827   39.783  -2.485  1.00 87.90  ?  651  VAL D CA  1 
ATOM   11078 C C   . VAL D  1  651 ? 2.264   40.251  -2.645  1.00 87.97  ?  651  VAL D C   1 
ATOM   11079 O O   . VAL D  1  651 ? 2.883   40.757  -1.703  1.00 90.34  ?  651  VAL D O   1 
ATOM   11080 C CB  . VAL D  1  651 ? -0.121  40.946  -2.860  1.00 90.53  ?  651  VAL D CB  1 
ATOM   11081 C CG1 . VAL D  1  651 ? -0.289  41.024  -4.369  1.00 88.85  ?  651  VAL D CG1 1 
ATOM   11082 C CG2 . VAL D  1  651 ? -1.449  40.813  -2.182  1.00 92.24  ?  651  VAL D CG2 1 
ATOM   11083 N N   . ASP D  1  652 ? 2.793   40.079  -3.856  1.00 87.76  ?  652  ASP D N   1 
ATOM   11084 C CA  . ASP D  1  652 ? 4.051   40.703  -4.249  1.00 87.89  ?  652  ASP D CA  1 
ATOM   11085 C C   . ASP D  1  652 ? 3.958   41.065  -5.721  1.00 87.09  ?  652  ASP D C   1 
ATOM   11086 O O   . ASP D  1  652 ? 3.775   40.180  -6.562  1.00 85.88  ?  652  ASP D O   1 
ATOM   11087 C CB  . ASP D  1  652 ? 5.239   39.778  -3.999  1.00 87.55  ?  652  ASP D CB  1 
ATOM   11088 C CG  . ASP D  1  652 ? 6.545   40.534  -3.890  1.00 88.14  ?  652  ASP D CG  1 
ATOM   11089 O OD1 . ASP D  1  652 ? 6.675   41.598  -4.533  1.00 89.74  ?  652  ASP D OD1 1 
ATOM   11090 O OD2 . ASP D  1  652 ? 7.443   40.065  -3.160  1.00 88.54  -1 652  ASP D OD2 1 
ATOM   11091 N N   . VAL D  1  653 ? 4.073   42.359  -6.028  1.00 87.13  ?  653  VAL D N   1 
ATOM   11092 C CA  . VAL D  1  653 ? 4.020   42.845  -7.404  1.00 87.13  ?  653  VAL D CA  1 
ATOM   11093 C C   . VAL D  1  653 ? 5.255   43.701  -7.664  1.00 89.37  ?  653  VAL D C   1 
ATOM   11094 O O   . VAL D  1  653 ? 5.305   44.480  -8.625  1.00 90.98  ?  653  VAL D O   1 
ATOM   11095 C CB  . VAL D  1  653 ? 2.720   43.627  -7.676  1.00 89.54  ?  653  VAL D CB  1 
ATOM   11096 C CG1 . VAL D  1  653 ? 2.445   43.683  -9.157  1.00 88.61  ?  653  VAL D CG1 1 
ATOM   11097 C CG2 . VAL D  1  653 ? 1.550   42.979  -6.973  1.00 88.74  ?  653  VAL D CG2 1 
ATOM   11098 N N   . SER D  1  654 ? 6.262   43.555  -6.808  1.00 93.33  ?  654  SER D N   1 
ATOM   11099 C CA  . SER D  1  654 ? 7.479   44.345  -6.918  1.00 96.07  ?  654  SER D CA  1 
ATOM   11100 C C   . SER D  1  654 ? 8.178   44.092  -8.252  1.00 94.25  ?  654  SER D C   1 
ATOM   11101 O O   . SER D  1  654 ? 8.014   43.043  -8.882  1.00 90.48  ?  654  SER D O   1 
ATOM   11102 C CB  . SER D  1  654 ? 8.428   44.020  -5.764  1.00 96.80  ?  654  SER D CB  1 
ATOM   11103 O OG  . SER D  1  654 ? 8.807   42.653  -5.785  1.00 92.75  ?  654  SER D OG  1 
ATOM   11104 N N   . HIS D  1  655 ? 8.967   45.082  -8.679  1.00 96.53  ?  655  HIS D N   1 
ATOM   11105 C CA  . HIS D  1  655 ? 9.803   44.983  -9.876  1.00 95.83  ?  655  HIS D CA  1 
ATOM   11106 C C   . HIS D  1  655 ? 8.968   44.677  -11.121 1.00 93.56  ?  655  HIS D C   1 
ATOM   11107 O O   . HIS D  1  655 ? 9.108   43.637  -11.767 1.00 90.11  ?  655  HIS D O   1 
ATOM   11108 C CB  . HIS D  1  655 ? 10.913  43.947  -9.675  1.00 93.55  ?  655  HIS D CB  1 
ATOM   11109 C CG  . HIS D  1  655 ? 11.887  44.323  -8.604  1.00 96.54  ?  655  HIS D CG  1 
ATOM   11110 N ND1 . HIS D  1  655 ? 13.011  45.079  -8.854  1.00 100.05 ?  655  HIS D ND1 1 
ATOM   11111 C CD2 . HIS D  1  655 ? 11.892  44.069  -7.274  1.00 97.03  ?  655  HIS D CD2 1 
ATOM   11112 C CE1 . HIS D  1  655 ? 13.674  45.265  -7.727  1.00 102.59 ?  655  HIS D CE1 1 
ATOM   11113 N NE2 . HIS D  1  655 ? 13.015  44.663  -6.753  1.00 100.81 ?  655  HIS D NE2 1 
ATOM   11114 N N   . ASN D  1  656 ? 8.077   45.611  -11.437 1.00 95.97  ?  656  ASN D N   1 
ATOM   11115 C CA  . ASN D  1  656 ? 7.201   45.503  -12.593 1.00 94.84  ?  656  ASN D CA  1 
ATOM   11116 C C   . ASN D  1  656 ? 7.091   46.884  -13.232 1.00 99.17  ?  656  ASN D C   1 
ATOM   11117 O O   . ASN D  1  656 ? 7.876   47.790  -12.938 1.00 102.60 ?  656  ASN D O   1 
ATOM   11118 C CB  . ASN D  1  656 ? 5.842   44.918  -12.194 1.00 92.84  ?  656  ASN D CB  1 
ATOM   11119 C CG  . ASN D  1  656 ? 5.685   43.479  -12.638 1.00 88.32  ?  656  ASN D CG  1 
ATOM   11120 O OD1 . ASN D  1  656 ? 5.365   43.218  -13.795 1.00 87.38  ?  656  ASN D OD1 1 
ATOM   11121 N ND2 . ASN D  1  656 ? 5.902   42.537  -11.722 1.00 86.03  ?  656  ASN D ND2 1 
ATOM   11122 N N   . ASN D  1  657 ? 6.130   47.036  -14.145 1.00 98.66  ?  657  ASN D N   1 
ATOM   11123 C CA  . ASN D  1  657 ? 5.931   48.274  -14.893 1.00 102.78 ?  657  ASN D CA  1 
ATOM   11124 C C   . ASN D  1  657 ? 4.518   48.820  -14.685 1.00 104.67 ?  657  ASN D C   1 
ATOM   11125 O O   . ASN D  1  657 ? 3.960   49.487  -15.561 1.00 107.10 ?  657  ASN D O   1 
ATOM   11126 C CB  . ASN D  1  657 ? 6.222   48.049  -16.379 1.00 102.18 ?  657  ASN D CB  1 
ATOM   11127 C CG  . ASN D  1  657 ? 6.347   49.345  -17.163 1.00 106.85 ?  657  ASN D CG  1 
ATOM   11128 O OD1 . ASN D  1  657 ? 6.913   50.329  -16.683 1.00 110.37 ?  657  ASN D OD1 1 
ATOM   11129 N ND2 . ASN D  1  657 ? 5.808   49.351  -18.376 1.00 107.26 ?  657  ASN D ND2 1 
ATOM   11130 N N   . LEU D  1  658 ? 3.931   48.551  -13.521 1.00 103.84 ?  658  LEU D N   1 
ATOM   11131 C CA  . LEU D  1  658 ? 2.556   48.941  -13.256 1.00 105.63 ?  658  LEU D CA  1 
ATOM   11132 C C   . LEU D  1  658 ? 2.479   50.402  -12.820 1.00 111.01 ?  658  LEU D C   1 
ATOM   11133 O O   . LEU D  1  658 ? 3.488   51.099  -12.673 1.00 113.34 ?  658  LEU D O   1 
ATOM   11134 C CB  . LEU D  1  658 ? 1.938   48.050  -12.183 1.00 103.12 ?  658  LEU D CB  1 
ATOM   11135 C CG  . LEU D  1  658 ? 1.832   46.550  -12.428 1.00 98.06  ?  658  LEU D CG  1 
ATOM   11136 C CD1 . LEU D  1  658 ? 1.010   45.948  -11.327 1.00 96.96  ?  658  LEU D CD1 1 
ATOM   11137 C CD2 . LEU D  1  658 ? 1.185   46.274  -13.757 1.00 97.26  ?  658  LEU D CD2 1 
ATOM   11138 N N   . GLN D  1  659 ? 1.248   50.866  -12.616 1.00 107.30 ?  659  GLN D N   1 
ATOM   11139 C CA  . GLN D  1  659 ? 0.991   52.219  -12.148 1.00 112.75 ?  659  GLN D CA  1 
ATOM   11140 C C   . GLN D  1  659 ? -0.361  52.242  -11.449 1.00 114.10 ?  659  GLN D C   1 
ATOM   11141 O O   . GLN D  1  659 ? -1.123  51.276  -11.506 1.00 111.05 ?  659  GLN D O   1 
ATOM   11142 C CB  . GLN D  1  659 ? 1.039   53.231  -13.296 1.00 116.27 ?  659  GLN D CB  1 
ATOM   11143 C CG  . GLN D  1  659 ? -0.036  53.041  -14.347 1.00 116.05 ?  659  GLN D CG  1 
ATOM   11144 C CD  . GLN D  1  659 ? 0.288   53.772  -15.632 1.00 118.63 ?  659  GLN D CD  1 
ATOM   11145 O OE1 . GLN D  1  659 ? 1.404   53.683  -16.143 1.00 117.61 ?  659  GLN D OE1 1 
ATOM   11146 N NE2 . GLN D  1  659 ? -0.686  54.502  -16.162 1.00 122.35 ?  659  GLN D NE2 1 
ATOM   11147 N N   . GLY D  1  660 ? -0.643  53.349  -10.764 1.00 119.15 ?  660  GLY D N   1 
ATOM   11148 C CA  . GLY D  1  660 ? -1.949  53.560  -10.181 1.00 121.57 ?  660  GLY D CA  1 
ATOM   11149 C C   . GLY D  1  660 ? -2.040  53.183  -8.714  1.00 121.32 ?  660  GLY D C   1 
ATOM   11150 O O   . GLY D  1  660 ? -1.148  52.531  -8.159  1.00 118.40 ?  660  GLY D O   1 
ATOM   11151 N N   . PRO D  1  661 ? -3.130  53.591  -8.058  1.00 122.70 ?  661  PRO D N   1 
ATOM   11152 C CA  . PRO D  1  661 ? -3.298  53.285  -6.630  1.00 123.20 ?  661  PRO D CA  1 
ATOM   11153 C C   . PRO D  1  661 ? -3.567  51.807  -6.385  1.00 117.97 ?  661  PRO D C   1 
ATOM   11154 O O   . PRO D  1  661 ? -4.269  51.144  -7.152  1.00 115.49 ?  661  PRO D O   1 
ATOM   11155 C CB  . PRO D  1  661 ? -4.504  54.140  -6.226  1.00 128.70 ?  661  PRO D CB  1 
ATOM   11156 C CG  . PRO D  1  661 ? -5.271  54.321  -7.499  1.00 129.08 ?  661  PRO D CG  1 
ATOM   11157 C CD  . PRO D  1  661 ? -4.235  54.411  -8.583  1.00 126.92 ?  661  PRO D CD  1 
ATOM   11158 N N   . ILE D  1  662 ? -3.011  51.298  -5.290  1.00 120.47 ?  662  ILE D N   1 
ATOM   11159 C CA  . ILE D  1  662 ? -3.127  49.882  -4.948  1.00 115.70 ?  662  ILE D CA  1 
ATOM   11160 C C   . ILE D  1  662 ? -4.564  49.554  -4.556  1.00 116.87 ?  662  ILE D C   1 
ATOM   11161 O O   . ILE D  1  662 ? -5.329  50.458  -4.194  1.00 121.86 ?  662  ILE D O   1 
ATOM   11162 C CB  . ILE D  1  662 ? -2.115  49.504  -3.851  1.00 114.77 ?  662  ILE D CB  1 
ATOM   11163 C CG1 . ILE D  1  662 ? -2.276  50.348  -2.569  1.00 120.16 ?  662  ILE D CG1 1 
ATOM   11164 C CG2 . ILE D  1  662 ? -0.688  49.609  -4.382  1.00 113.10 ?  662  ILE D CG2 1 
ATOM   11165 C CD1 . ILE D  1  662 ? -3.436  49.982  -1.652  1.00 121.66 ?  662  ILE D CD1 1 
ATOM   11166 N N   . PRO D  1  663 ? -4.980  48.294  -4.632  1.00 119.30 ?  663  PRO D N   1 
ATOM   11167 C CA  . PRO D  1  663 ? -6.295  47.921  -4.097  1.00 120.79 ?  663  PRO D CA  1 
ATOM   11168 C C   . PRO D  1  663 ? -6.300  47.823  -2.578  1.00 122.74 ?  663  PRO D C   1 
ATOM   11169 O O   . PRO D  1  663 ? -5.315  47.421  -1.959  1.00 120.81 ?  663  PRO D O   1 
ATOM   11170 C CB  . PRO D  1  663 ? -6.569  46.552  -4.736  1.00 115.69 ?  663  PRO D CB  1 
ATOM   11171 C CG  . PRO D  1  663 ? -5.682  46.493  -5.932  1.00 112.56 ?  663  PRO D CG  1 
ATOM   11172 C CD  . PRO D  1  663 ? -4.472  47.315  -5.607  1.00 113.92 ?  663  PRO D CD  1 
ATOM   11173 N N   . ASP D  1  664 ? -7.425  48.200  -1.974  1.00 119.22 ?  664  ASP D N   1 
ATOM   11174 C CA  . ASP D  1  664 ? -7.596  48.123  -0.525  1.00 121.86 ?  664  ASP D CA  1 
ATOM   11175 C C   . ASP D  1  664 ? -8.115  46.739  -0.143  1.00 118.71 ?  664  ASP D C   1 
ATOM   11176 O O   . ASP D  1  664 ? -9.287  46.423  -0.369  1.00 119.55 ?  664  ASP D O   1 
ATOM   11177 C CB  . ASP D  1  664 ? -8.547  49.218  -0.045  1.00 128.58 ?  664  ASP D CB  1 
ATOM   11178 C CG  . ASP D  1  664 ? -8.765  49.193  1.460   1.00 132.05 ?  664  ASP D CG  1 
ATOM   11179 O OD1 . ASP D  1  664 ? -7.990  48.529  2.184   1.00 129.73 ?  664  ASP D OD1 1 
ATOM   11180 O OD2 . ASP D  1  664 ? -9.726  49.843  1.918   1.00 137.47 -1 664  ASP D OD2 1 
ATOM   11181 N N   . ASN D  1  665 ? -7.247  45.916  0.443   1.00 123.27 ?  665  ASN D N   1 
ATOM   11182 C CA  . ASN D  1  665 ? -7.665  44.675  1.084   1.00 121.21 ?  665  ASN D CA  1 
ATOM   11183 C C   . ASN D  1  665 ? -6.707  44.384  2.233   1.00 121.03 ?  665  ASN D C   1 
ATOM   11184 O O   . ASN D  1  665 ? -5.734  45.110  2.454   1.00 122.35 ?  665  ASN D O   1 
ATOM   11185 C CB  . ASN D  1  665 ? -7.735  43.518  0.082   1.00 115.65 ?  665  ASN D CB  1 
ATOM   11186 C CG  . ASN D  1  665 ? -6.434  43.303  -0.654  1.00 111.28 ?  665  ASN D CG  1 
ATOM   11187 O OD1 . ASN D  1  665 ? -5.351  43.483  -0.100  1.00 111.15 ?  665  ASN D OD1 1 
ATOM   11188 N ND2 . ASN D  1  665 ? -6.534  42.914  -1.918  1.00 108.10 ?  665  ASN D ND2 1 
ATOM   11189 N N   . ALA D  1  666 ? -6.987  43.303  2.966   1.00 119.84 ?  666  ALA D N   1 
ATOM   11190 C CA  . ALA D  1  666 ? -6.153  42.955  4.113   1.00 120.08 ?  666  ALA D CA  1 
ATOM   11191 C C   . ALA D  1  666 ? -4.709  42.688  3.705   1.00 116.08 ?  666  ALA D C   1 
ATOM   11192 O O   . ALA D  1  666 ? -3.785  42.981  4.474   1.00 117.69 ?  666  ALA D O   1 
ATOM   11193 C CB  . ALA D  1  666 ? -6.734  41.738  4.834   1.00 119.08 ?  666  ALA D CB  1 
ATOM   11194 N N   . ALA D  1  667 ? -4.493  42.142  2.504   1.00 112.57 ?  667  ALA D N   1 
ATOM   11195 C CA  . ALA D  1  667 ? -3.146  41.788  2.066   1.00 108.83 ?  667  ALA D CA  1 
ATOM   11196 C C   . ALA D  1  667 ? -2.360  43.004  1.591   1.00 110.68 ?  667  ALA D C   1 
ATOM   11197 O O   . ALA D  1  667 ? -1.173  43.139  1.908   1.00 110.68 ?  667  ALA D O   1 
ATOM   11198 C CB  . ALA D  1  667 ? -3.216  40.736  0.960   1.00 103.48 ?  667  ALA D CB  1 
ATOM   11199 N N   . PHE D  1  668 ? -2.996  43.892  0.822   1.00 109.36 ?  668  PHE D N   1 
ATOM   11200 C CA  . PHE D  1  668 ? -2.316  45.106  0.385   1.00 111.71 ?  668  PHE D CA  1 
ATOM   11201 C C   . PHE D  1  668 ? -2.063  46.055  1.549   1.00 117.14 ?  668  PHE D C   1 
ATOM   11202 O O   . PHE D  1  668 ? -1.044  46.756  1.565   1.00 118.72 ?  668  PHE D O   1 
ATOM   11203 C CB  . PHE D  1  668 ? -3.132  45.812  -0.695  1.00 112.87 ?  668  PHE D CB  1 
ATOM   11204 C CG  . PHE D  1  668 ? -2.939  45.254  -2.080  1.00 108.32 ?  668  PHE D CG  1 
ATOM   11205 C CD1 . PHE D  1  668 ? -1.705  45.319  -2.707  1.00 106.19 ?  668  PHE D CD1 1 
ATOM   11206 C CD2 . PHE D  1  668 ? -3.999  44.679  -2.763  1.00 106.65 ?  668  PHE D CD2 1 
ATOM   11207 C CE1 . PHE D  1  668 ? -1.530  44.810  -3.983  1.00 102.42 ?  668  PHE D CE1 1 
ATOM   11208 C CE2 . PHE D  1  668 ? -3.830  44.168  -4.038  1.00 102.92 ?  668  PHE D CE2 1 
ATOM   11209 C CZ  . PHE D  1  668 ? -2.594  44.235  -4.649  1.00 100.79 ?  668  PHE D CZ  1 
ATOM   11210 N N   . ARG D  1  669 ? -2.983  46.106  2.516   1.00 114.30 ?  669  ARG D N   1 
ATOM   11211 C CA  . ARG D  1  669 ? -2.794  46.965  3.681   1.00 119.95 ?  669  ARG D CA  1 
ATOM   11212 C C   . ARG D  1  669 ? -1.572  46.535  4.484   1.00 119.30 ?  669  ARG D C   1 
ATOM   11213 O O   . ARG D  1  669 ? -0.726  47.363  4.844   1.00 122.57 ?  669  ARG D O   1 
ATOM   11214 C CB  . ARG D  1  669 ? -4.050  46.948  4.555   1.00 123.59 ?  669  ARG D CB  1 
ATOM   11215 C CG  . ARG D  1  669 ? -5.188  47.835  4.053   1.00 127.02 ?  669  ARG D CG  1 
ATOM   11216 C CD  . ARG D  1  669 ? -6.253  48.044  5.129   1.00 132.21 ?  669  ARG D CD  1 
ATOM   11217 N NE  . ARG D  1  669 ? -7.012  46.828  5.405   1.00 129.80 ?  669  ARG D NE  1 
ATOM   11218 C CZ  . ARG D  1  669 ? -6.784  46.018  6.431   1.00 129.41 ?  669  ARG D CZ  1 
ATOM   11219 N NH1 . ARG D  1  669 ? -5.820  46.262  7.303   1.00 131.30 ?  669  ARG D NH1 1 
ATOM   11220 N NH2 . ARG D  1  669 ? -7.543  44.936  6.584   1.00 127.43 ?  669  ARG D NH2 1 
ATOM   11221 N N   . ASN D  1  670 ? -1.461  45.240  4.768   1.00 119.23 ?  670  ASN D N   1 
ATOM   11222 C CA  . ASN D  1  670 ? -0.357  44.697  5.547   1.00 118.62 ?  670  ASN D CA  1 
ATOM   11223 C C   . ASN D  1  670 ? 0.858   44.344  4.697   1.00 114.41 ?  670  ASN D C   1 
ATOM   11224 O O   . ASN D  1  670 ? 1.826   43.789  5.227   1.00 113.55 ?  670  ASN D O   1 
ATOM   11225 C CB  . ASN D  1  670 ? -0.823  43.457  6.321   1.00 116.97 ?  670  ASN D CB  1 
ATOM   11226 C CG  . ASN D  1  670 ? -1.353  43.796  7.700   1.00 122.59 ?  670  ASN D CG  1 
ATOM   11227 O OD1 . ASN D  1  670 ? -2.560  43.762  7.939   1.00 124.31 ?  670  ASN D OD1 1 
ATOM   11228 N ND2 . ASN D  1  670 ? -0.450  44.127  8.617   1.00 125.87 ?  670  ASN D ND2 1 
ATOM   11229 N N   . ALA D  1  671 ? 0.831   44.646  3.402   1.00 113.31 ?  671  ALA D N   1 
ATOM   11230 C CA  . ALA D  1  671 ? 1.969   44.344  2.546   1.00 109.71 ?  671  ALA D CA  1 
ATOM   11231 C C   . ALA D  1  671 ? 3.170   45.201  2.939   1.00 113.24 ?  671  ALA D C   1 
ATOM   11232 O O   . ALA D  1  671 ? 3.027   46.406  3.173   1.00 118.06 ?  671  ALA D O   1 
ATOM   11233 C CB  . ALA D  1  671 ? 1.617   44.579  1.080   1.00 107.33 ?  671  ALA D CB  1 
ATOM   11234 N N   . PRO D  1  672 ? 4.360   44.613  3.028   1.00 112.09 ?  672  PRO D N   1 
ATOM   11235 C CA  . PRO D  1  672 ? 5.553   45.391  3.380   1.00 115.75 ?  672  PRO D CA  1 
ATOM   11236 C C   . PRO D  1  672 ? 5.983   46.278  2.225   1.00 116.14 ?  672  PRO D C   1 
ATOM   11237 O O   . PRO D  1  672 ? 5.567   46.057  1.077   1.00 112.65 ?  672  PRO D O   1 
ATOM   11238 C CB  . PRO D  1  672 ? 6.601   44.308  3.681   1.00 113.10 ?  672  PRO D CB  1 
ATOM   11239 C CG  . PRO D  1  672 ? 6.150   43.125  2.894   1.00 107.10 ?  672  PRO D CG  1 
ATOM   11240 C CD  . PRO D  1  672 ? 4.650   43.176  2.883   1.00 107.00 ?  672  PRO D CD  1 
ATOM   11241 N N   . PRO D  1  673 ? 6.813   47.295  2.487   1.00 112.76 ?  673  PRO D N   1 
ATOM   11242 C CA  . PRO D  1  673 ? 7.176   48.239  1.414   1.00 113.86 ?  673  PRO D CA  1 
ATOM   11243 C C   . PRO D  1  673 ? 7.892   47.603  0.232   1.00 109.22 ?  673  PRO D C   1 
ATOM   11244 O O   . PRO D  1  673 ? 7.735   48.080  -0.899  1.00 108.55 ?  673  PRO D O   1 
ATOM   11245 C CB  . PRO D  1  673 ? 8.076   49.253  2.134   1.00 119.91 ?  673  PRO D CB  1 
ATOM   11246 C CG  . PRO D  1  673 ? 7.670   49.167  3.566   1.00 122.98 ?  673  PRO D CG  1 
ATOM   11247 C CD  . PRO D  1  673 ? 7.338   47.724  3.795   1.00 117.91 ?  673  PRO D CD  1 
ATOM   11248 N N   . ASP D  1  674 ? 8.674   46.543  0.451   1.00 115.76 ?  674  ASP D N   1 
ATOM   11249 C CA  . ASP D  1  674 ? 9.415   45.940  -0.652  1.00 111.87 ?  674  ASP D CA  1 
ATOM   11250 C C   . ASP D  1  674 ? 8.506   45.237  -1.653  1.00 106.93 ?  674  ASP D C   1 
ATOM   11251 O O   . ASP D  1  674 ? 8.913   45.039  -2.802  1.00 104.50 ?  674  ASP D O   1 
ATOM   11252 C CB  . ASP D  1  674 ? 10.464  44.962  -0.124  1.00 110.45 ?  674  ASP D CB  1 
ATOM   11253 C CG  . ASP D  1  674 ? 10.001  44.226  1.107   1.00 110.19 ?  674  ASP D CG  1 
ATOM   11254 O OD1 . ASP D  1  674 ? 8.772   44.124  1.304   1.00 109.35 ?  674  ASP D OD1 1 
ATOM   11255 O OD2 . ASP D  1  674 ? 10.861  43.749  1.877   1.00 111.15 -1 674  ASP D OD2 1 
ATOM   11256 N N   . ALA D  1  675 ? 7.297   44.842  -1.246  1.00 103.88 ?  675  ALA D N   1 
ATOM   11257 C CA  . ALA D  1  675 ? 6.374   44.152  -2.144  1.00 99.68  ?  675  ALA D CA  1 
ATOM   11258 C C   . ALA D  1  675 ? 5.789   45.062  -3.221  1.00 100.76 ?  675  ALA D C   1 
ATOM   11259 O O   . ALA D  1  675 ? 5.044   44.572  -4.079  1.00 97.77  ?  675  ALA D O   1 
ATOM   11260 C CB  . ALA D  1  675 ? 5.246   43.506  -1.337  1.00 98.83  ?  675  ALA D CB  1 
ATOM   11261 N N   . PHE D  1  676 ? 6.100   46.359  -3.200  1.00 97.05  ?  676  PHE D N   1 
ATOM   11262 C CA  . PHE D  1  676 ? 5.684   47.288  -4.245  1.00 98.60  ?  676  PHE D CA  1 
ATOM   11263 C C   . PHE D  1  676 ? 6.872   47.925  -4.955  1.00 100.15 ?  676  PHE D C   1 
ATOM   11264 O O   . PHE D  1  676 ? 6.693   48.901  -5.694  1.00 102.64 ?  676  PHE D O   1 
ATOM   11265 C CB  . PHE D  1  676 ? 4.782   48.377  -3.660  1.00 103.33 ?  676  PHE D CB  1 
ATOM   11266 C CG  . PHE D  1  676 ? 3.548   47.849  -2.984  1.00 102.58 ?  676  PHE D CG  1 
ATOM   11267 C CD1 . PHE D  1  676 ? 2.435   47.483  -3.724  1.00 100.35 ?  676  PHE D CD1 1 
ATOM   11268 C CD2 . PHE D  1  676 ? 3.496   47.730  -1.605  1.00 104.57 ?  676  PHE D CD2 1 
ATOM   11269 C CE1 . PHE D  1  676 ? 1.298   47.005  -3.100  1.00 100.12 ?  676  PHE D CE1 1 
ATOM   11270 C CE2 . PHE D  1  676 ? 2.363   47.254  -0.978  1.00 104.30 ?  676  PHE D CE2 1 
ATOM   11271 C CZ  . PHE D  1  676 ? 1.263   46.890  -1.726  1.00 102.07 ?  676  PHE D CZ  1 
ATOM   11272 N N   . GLU D  1  677 ? 8.074   47.391  -4.757  1.00 104.92 ?  677  GLU D N   1 
ATOM   11273 C CA  . GLU D  1  677 ? 9.296   48.015  -5.243  1.00 107.22 ?  677  GLU D CA  1 
ATOM   11274 C C   . GLU D  1  677 ? 9.350   48.058  -6.766  1.00 105.46 ?  677  GLU D C   1 
ATOM   11275 O O   . GLU D  1  677 ? 8.763   47.223  -7.459  1.00 101.35 ?  677  GLU D O   1 
ATOM   11276 C CB  . GLU D  1  677 ? 10.517  47.251  -4.731  1.00 106.19 ?  677  GLU D CB  1 
ATOM   11277 C CG  . GLU D  1  677 ? 11.061  47.727  -3.403  1.00 110.49 ?  677  GLU D CG  1 
ATOM   11278 C CD  . GLU D  1  677 ? 12.289  46.944  -2.981  1.00 109.71 ?  677  GLU D CD  1 
ATOM   11279 O OE1 . GLU D  1  677 ? 12.857  46.222  -3.831  1.00 106.45 ?  677  GLU D OE1 1 
ATOM   11280 O OE2 . GLU D  1  677 ? 12.682  47.048  -1.800  1.00 112.70 -1 677  GLU D OE2 1 
ATOM   11281 N N   . GLY D  1  678 ? 10.077  49.049  -7.276  1.00 105.32 ?  678  GLY D N   1 
ATOM   11282 C CA  . GLY D  1  678 ? 10.519  49.053  -8.662  1.00 104.26 ?  678  GLY D CA  1 
ATOM   11283 C C   . GLY D  1  678 ? 9.432   49.003  -9.712  1.00 102.31 ?  678  GLY D C   1 
ATOM   11284 O O   . GLY D  1  678 ? 9.598   48.331  -10.738 1.00 99.27  ?  678  GLY D O   1 
ATOM   11285 N N   . ASN D  1  679 ? 8.314   49.682  -9.476  1.00 105.76 ?  679  ASN D N   1 
ATOM   11286 C CA  . ASN D  1  679 ? 7.297   49.861  -10.499 1.00 105.20 ?  679  ASN D CA  1 
ATOM   11287 C C   . ASN D  1  679 ? 7.430   51.262  -11.095 1.00 110.15 ?  679  ASN D C   1 
ATOM   11288 O O   . ASN D  1  679 ? 8.279   52.058  -10.686 1.00 113.90 ?  679  ASN D O   1 
ATOM   11289 C CB  . ASN D  1  679 ? 5.903   49.603  -9.924  1.00 104.28 ?  679  ASN D CB  1 
ATOM   11290 C CG  . ASN D  1  679 ? 5.559   48.123  -9.880  1.00 98.93  ?  679  ASN D CG  1 
ATOM   11291 O OD1 . ASN D  1  679 ? 4.708   47.649  -10.632 1.00 96.77  ?  679  ASN D OD1 1 
ATOM   11292 N ND2 . ASN D  1  679 ? 6.223   47.386  -8.996  1.00 97.13  ?  679  ASN D ND2 1 
ATOM   11293 N N   . LYS D  1  680 ? 6.600   51.562  -12.097 1.00 107.33 ?  680  LYS D N   1 
ATOM   11294 C CA  . LYS D  1  680 ? 6.740   52.846  -12.774 1.00 112.08 ?  680  LYS D CA  1 
ATOM   11295 C C   . LYS D  1  680 ? 6.150   53.981  -11.943 1.00 116.88 ?  680  LYS D C   1 
ATOM   11296 O O   . LYS D  1  680 ? 6.868   54.897  -11.528 1.00 121.09 ?  680  LYS D O   1 
ATOM   11297 C CB  . LYS D  1  680 ? 6.077   52.786  -14.155 1.00 111.28 ?  680  LYS D CB  1 
ATOM   11298 C CG  . LYS D  1  680 ? 6.111   54.092  -14.953 1.00 116.36 ?  680  LYS D CG  1 
ATOM   11299 C CD  . LYS D  1  680 ? 7.416   54.868  -14.777 1.00 119.93 ?  680  LYS D CD  1 
ATOM   11300 C CE  . LYS D  1  680 ? 8.478   54.427  -15.766 1.00 118.52 ?  680  LYS D CE  1 
ATOM   11301 N NZ  . LYS D  1  680 ? 9.845   54.526  -15.182 1.00 119.85 ?  680  LYS D NZ  1 
ATOM   11302 N N   . ASP D  1  681 ? 4.846   53.932  -11.669 1.00 116.22 ?  681  ASP D N   1 
ATOM   11303 C CA  . ASP D  1  681 ? 4.257   54.963  -10.814 1.00 121.01 ?  681  ASP D CA  1 
ATOM   11304 C C   . ASP D  1  681 ? 3.078   54.361  -10.042 1.00 119.25 ?  681  ASP D C   1 
ATOM   11305 O O   . ASP D  1  681 ? 1.936   54.429  -10.495 1.00 119.56 ?  681  ASP D O   1 
ATOM   11306 C CB  . ASP D  1  681 ? 3.828   56.148  -11.666 1.00 125.52 ?  681  ASP D CB  1 
ATOM   11307 C CG  . ASP D  1  681 ? 3.257   57.270  -10.852 1.00 131.00 ?  681  ASP D CG  1 
ATOM   11308 O OD1 . ASP D  1  681 ? 3.928   57.701  -9.892  1.00 133.58 ?  681  ASP D OD1 1 
ATOM   11309 O OD2 . ASP D  1  681 ? 2.138   57.718  -11.173 1.00 133.07 ?  681  ASP D OD2 1 
ATOM   11310 N N   . LEU D  1  682 ? 3.344   53.882  -8.829  1.00 120.05 ?  682  LEU D N   1 
ATOM   11311 C CA  . LEU D  1  682 ? 2.275   53.342  -8.001  1.00 118.95 ?  682  LEU D CA  1 
ATOM   11312 C C   . LEU D  1  682 ? 1.712   54.453  -7.113  1.00 124.71 ?  682  LEU D C   1 
ATOM   11313 O O   . LEU D  1  682 ? 2.074   55.625  -7.252  1.00 129.36 ?  682  LEU D O   1 
ATOM   11314 C CB  . LEU D  1  682 ? 2.772   52.134  -7.206  1.00 114.82 ?  682  LEU D CB  1 
ATOM   11315 C CG  . LEU D  1  682 ? 2.289   50.768  -7.718  1.00 109.13 ?  682  LEU D CG  1 
ATOM   11316 C CD1 . LEU D  1  682 ? 2.485   50.643  -9.221  1.00 107.20 ?  682  LEU D CD1 1 
ATOM   11317 C CD2 . LEU D  1  682 ? 2.982   49.622  -6.994  1.00 105.39 ?  682  LEU D CD2 1 
ATOM   11318 N N   . CYS D  1  683 ? 0.816   54.096  -6.194  1.00 123.00 ?  683  CYS D N   1 
ATOM   11319 C CA  . CYS D  1  683 ? 0.187   55.059  -5.288  1.00 128.64 ?  683  CYS D CA  1 
ATOM   11320 C C   . CYS D  1  683 ? -0.481  56.206  -6.050  1.00 132.97 ?  683  CYS D C   1 
ATOM   11321 O O   . CYS D  1  683 ? -1.500  56.015  -6.715  1.00 132.12 ?  683  CYS D O   1 
ATOM   11322 C CB  . CYS D  1  683 ? 1.215   55.612  -4.293  1.00 131.95 ?  683  CYS D CB  1 
ATOM   11323 S SG  . CYS D  1  683 ? 2.395   54.376  -3.670  1.00 127.24 ?  683  CYS D SG  1 
ATOM   11324 N N   . ASN E  2  26  ? -0.078  5.484   13.147  1.00 62.84  ?  26   ASN E N   1 
ATOM   11325 C CA  . ASN E  2  26  ? -0.209  6.180   14.420  1.00 65.73  ?  26   ASN E CA  1 
ATOM   11326 C C   . ASN E  2  26  ? -1.649  6.626   14.639  1.00 66.42  ?  26   ASN E C   1 
ATOM   11327 O O   . ASN E  2  26  ? -2.560  6.181   13.935  1.00 65.38  ?  26   ASN E O   1 
ATOM   11328 C CB  . ASN E  2  26  ? 0.737   7.384   14.481  1.00 66.55  ?  26   ASN E CB  1 
ATOM   11329 C CG  . ASN E  2  26  ? 0.423   8.426   13.428  1.00 64.89  ?  26   ASN E CG  1 
ATOM   11330 O OD1 . ASN E  2  26  ? -0.279  8.149   12.456  1.00 62.51  ?  26   ASN E OD1 1 
ATOM   11331 N ND2 . ASN E  2  26  ? 0.943   9.634   13.615  1.00 64.27  ?  26   ASN E ND2 1 
ATOM   11332 N N   . ALA E  2  27  ? -1.846  7.517   15.613  1.00 67.63  ?  27   ALA E N   1 
ATOM   11333 C CA  . ALA E  2  27  ? -3.198  7.937   15.957  1.00 67.95  ?  27   ALA E CA  1 
ATOM   11334 C C   . ALA E  2  27  ? -3.871  8.639   14.787  1.00 66.75  ?  27   ALA E C   1 
ATOM   11335 O O   . ALA E  2  27  ? -5.035  8.360   14.474  1.00 66.47  ?  27   ALA E O   1 
ATOM   11336 C CB  . ALA E  2  27  ? -3.166  8.843   17.185  1.00 69.65  ?  27   ALA E CB  1 
ATOM   11337 N N   . GLU E  2  28  ? -3.152  9.547   14.123  1.00 71.18  ?  28   GLU E N   1 
ATOM   11338 C CA  . GLU E  2  28  ? -3.728  10.263  12.989  1.00 70.03  ?  28   GLU E CA  1 
ATOM   11339 C C   . GLU E  2  28  ? -4.074  9.311   11.851  1.00 68.09  ?  28   GLU E C   1 
ATOM   11340 O O   . GLU E  2  28  ? -5.107  9.470   11.189  1.00 67.88  ?  28   GLU E O   1 
ATOM   11341 C CB  . GLU E  2  28  ? -2.765  11.348  12.511  1.00 68.87  ?  28   GLU E CB  1 
ATOM   11342 C CG  . GLU E  2  28  ? -2.527  12.460  13.521  1.00 69.44  ?  28   GLU E CG  1 
ATOM   11343 C CD  . GLU E  2  28  ? -1.835  13.653  12.904  1.00 66.65  ?  28   GLU E CD  1 
ATOM   11344 O OE1 . GLU E  2  28  ? -1.046  13.439  11.962  1.00 63.38  ?  28   GLU E OE1 1 
ATOM   11345 O OE2 . GLU E  2  28  ? -2.083  14.797  13.346  1.00 67.61  -1 28   GLU E OE2 1 
ATOM   11346 N N   . GLY E  2  29  ? -3.218  8.318   11.604  1.00 67.91  ?  29   GLY E N   1 
ATOM   11347 C CA  . GLY E  2  29  ? -3.506  7.357   10.554  1.00 66.37  ?  29   GLY E CA  1 
ATOM   11348 C C   . GLY E  2  29  ? -4.705  6.484   10.870  1.00 67.97  ?  29   GLY E C   1 
ATOM   11349 O O   . GLY E  2  29  ? -5.491  6.153   9.978   1.00 68.19  ?  29   GLY E O   1 
ATOM   11350 N N   . ASP E  2  30  ? -4.863  6.099   12.140  1.00 66.81  ?  30   ASP E N   1 
ATOM   11351 C CA  . ASP E  2  30  ? -6.027  5.309   12.528  1.00 68.32  ?  30   ASP E CA  1 
ATOM   11352 C C   . ASP E  2  30  ? -7.323  6.093   12.373  1.00 69.46  ?  30   ASP E C   1 
ATOM   11353 O O   . ASP E  2  30  ? -8.363  5.508   12.051  1.00 70.43  ?  30   ASP E O   1 
ATOM   11354 C CB  . ASP E  2  30  ? -5.882  4.820   13.967  1.00 69.51  ?  30   ASP E CB  1 
ATOM   11355 C CG  . ASP E  2  30  ? -4.851  3.727   14.105  1.00 69.10  ?  30   ASP E CG  1 
ATOM   11356 O OD1 . ASP E  2  30  ? -5.089  2.617   13.586  1.00 68.91  ?  30   ASP E OD1 1 
ATOM   11357 O OD2 . ASP E  2  30  ? -3.808  3.974   14.743  1.00 69.34  -1 30   ASP E OD2 1 
ATOM   11358 N N   . ALA E  2  31  ? -7.284  7.407   12.602  1.00 67.11  ?  31   ALA E N   1 
ATOM   11359 C CA  . ALA E  2  31  ? -8.470  8.228   12.394  1.00 68.16  ?  31   ALA E CA  1 
ATOM   11360 C C   . ALA E  2  31  ? -8.835  8.291   10.917  1.00 67.77  ?  31   ALA E C   1 
ATOM   11361 O O   . ALA E  2  31  ? -9.999  8.108   10.545  1.00 69.02  ?  31   ALA E O   1 
ATOM   11362 C CB  . ALA E  2  31  ? -8.239  9.628   12.959  1.00 68.22  ?  31   ALA E CB  1 
ATOM   11363 N N   . LEU E  2  32  ? -7.847  8.542   10.056  1.00 72.39  ?  32   LEU E N   1 
ATOM   11364 C CA  . LEU E  2  32  ? -8.124  8.592   8.624   1.00 71.59  ?  32   LEU E CA  1 
ATOM   11365 C C   . LEU E  2  32  ? -8.471  7.214   8.069   1.00 71.72  ?  32   LEU E C   1 
ATOM   11366 O O   . LEU E  2  32  ? -9.185  7.114   7.063   1.00 70.33  ?  32   LEU E O   1 
ATOM   11367 C CB  . LEU E  2  32  ? -6.932  9.197   7.881   1.00 69.71  ?  32   LEU E CB  1 
ATOM   11368 C CG  . LEU E  2  32  ? -6.671  10.683  8.141   1.00 68.77  ?  32   LEU E CG  1 
ATOM   11369 C CD1 . LEU E  2  32  ? -5.502  11.173  7.291   1.00 66.46  ?  32   LEU E CD1 1 
ATOM   11370 C CD2 . LEU E  2  32  ? -7.921  11.510  7.879   1.00 68.76  ?  32   LEU E CD2 1 
ATOM   11371 N N   . SER E  2  33  ? -7.972  6.143   8.696   1.00 71.08  ?  33   SER E N   1 
ATOM   11372 C CA  . SER E  2  33  ? -8.408  4.802   8.316   1.00 69.83  ?  33   SER E CA  1 
ATOM   11373 C C   . SER E  2  33  ? -9.855  4.553   8.718   1.00 71.09  ?  33   SER E C   1 
ATOM   11374 O O   . SER E  2  33  ? -10.580 3.841   8.014   1.00 70.03  ?  33   SER E O   1 
ATOM   11375 C CB  . SER E  2  33  ? -7.505  3.745   8.951   1.00 69.54  ?  33   SER E CB  1 
ATOM   11376 O OG  . SER E  2  33  ? -6.184  3.831   8.456   1.00 67.47  ?  33   SER E OG  1 
ATOM   11377 N N   . ALA E  2  34  ? -10.291 5.130   9.841   1.00 71.99  ?  34   ALA E N   1 
ATOM   11378 C CA  . ALA E  2  34  ? -11.678 4.974   10.260  1.00 73.19  ?  34   ALA E CA  1 
ATOM   11379 C C   . ALA E  2  34  ? -12.621 5.627   9.260   1.00 72.69  ?  34   ALA E C   1 
ATOM   11380 O O   . ALA E  2  34  ? -13.658 5.053   8.908   1.00 74.97  ?  34   ALA E O   1 
ATOM   11381 C CB  . ALA E  2  34  ? -11.873 5.565   11.656  1.00 74.73  ?  34   ALA E CB  1 
ATOM   11382 N N   . LEU E  2  35  ? -12.270 6.829   8.786   1.00 78.91  ?  35   LEU E N   1 
ATOM   11383 C CA  . LEU E  2  35  ? -13.034 7.471   7.717   1.00 77.90  ?  35   LEU E CA  1 
ATOM   11384 C C   . LEU E  2  35  ? -13.098 6.581   6.486   1.00 76.42  ?  35   LEU E C   1 
ATOM   11385 O O   . LEU E  2  35  ? -14.160 6.432   5.869   1.00 76.64  ?  35   LEU E O   1 
ATOM   11386 C CB  . LEU E  2  35  ? -12.414 8.835   7.372   1.00 77.10  ?  35   LEU E CB  1 
ATOM   11387 C CG  . LEU E  2  35  ? -13.068 9.814   6.372   1.00 76.44  ?  35   LEU E CG  1 
ATOM   11388 C CD1 . LEU E  2  35  ? -12.451 11.188  6.483   1.00 75.76  ?  35   LEU E CD1 1 
ATOM   11389 C CD2 . LEU E  2  35  ? -12.922 9.372   4.926   1.00 75.54  ?  35   LEU E CD2 1 
ATOM   11390 N N   . LYS E  2  36  ? -11.962 5.995   6.107   1.00 76.37  ?  36   LYS E N   1 
ATOM   11391 C CA  . LYS E  2  36  ? -11.899 5.161   4.913   1.00 74.57  ?  36   LYS E CA  1 
ATOM   11392 C C   . LYS E  2  36  ? -12.893 4.005   4.972   1.00 75.20  ?  36   LYS E C   1 
ATOM   11393 O O   . LYS E  2  36  ? -13.405 3.575   3.932   1.00 74.62  ?  36   LYS E O   1 
ATOM   11394 C CB  . LYS E  2  36  ? -10.467 4.649   4.728   1.00 72.66  ?  36   LYS E CB  1 
ATOM   11395 C CG  . LYS E  2  36  ? -10.249 3.689   3.569   1.00 70.29  ?  36   LYS E CG  1 
ATOM   11396 C CD  . LYS E  2  36  ? -8.789  3.261   3.515   1.00 67.93  ?  36   LYS E CD  1 
ATOM   11397 C CE  . LYS E  2  36  ? -8.643  1.766   3.328   1.00 66.36  ?  36   LYS E CE  1 
ATOM   11398 N NZ  . LYS E  2  36  ? -7.992  1.474   2.030   1.00 63.58  ?  36   LYS E NZ  1 
ATOM   11399 N N   . ASN E  2  37  ? -13.190 3.497   6.171   1.00 79.27  ?  37   ASN E N   1 
ATOM   11400 C CA  . ASN E  2  37  ? -14.108 2.370   6.290   1.00 80.31  ?  37   ASN E CA  1 
ATOM   11401 C C   . ASN E  2  37  ? -15.572 2.789   6.281   1.00 82.08  ?  37   ASN E C   1 
ATOM   11402 O O   . ASN E  2  37  ? -16.445 1.932   6.108   1.00 83.11  ?  37   ASN E O   1 
ATOM   11403 C CB  . ASN E  2  37  ? -13.813 1.580   7.567   1.00 81.82  ?  37   ASN E CB  1 
ATOM   11404 C CG  . ASN E  2  37  ? -12.450 0.920   7.537   1.00 80.31  ?  37   ASN E CG  1 
ATOM   11405 O OD1 . ASN E  2  37  ? -12.304 -0.224  7.103   1.00 79.50  ?  37   ASN E OD1 1 
ATOM   11406 N ND2 . ASN E  2  37  ? -11.438 1.650   7.985   1.00 80.06  ?  37   ASN E ND2 1 
ATOM   11407 N N   . SER E  2  38  ? -15.865 4.073   6.475   1.00 86.52  ?  38   SER E N   1 
ATOM   11408 C CA  . SER E  2  38  ? -17.236 4.561   6.465   1.00 88.19  ?  38   SER E CA  1 
ATOM   11409 C C   . SER E  2  38  ? -17.645 5.154   5.123   1.00 87.64  ?  38   SER E C   1 
ATOM   11410 O O   . SER E  2  38  ? -18.798 5.569   4.972   1.00 89.21  ?  38   SER E O   1 
ATOM   11411 C CB  . SER E  2  38  ? -17.435 5.596   7.574   1.00 89.41  ?  38   SER E CB  1 
ATOM   11412 O OG  . SER E  2  38  ? -18.384 6.582   7.206   1.00 90.03  ?  38   SER E OG  1 
ATOM   11413 N N   . LEU E  2  39  ? -16.739 5.214   4.152   1.00 84.72  ?  39   LEU E N   1 
ATOM   11414 C CA  . LEU E  2  39  ? -17.043 5.750   2.834   1.00 84.83  ?  39   LEU E CA  1 
ATOM   11415 C C   . LEU E  2  39  ? -16.991 4.650   1.786   1.00 84.44  ?  39   LEU E C   1 
ATOM   11416 O O   . LEU E  2  39  ? -16.087 3.809   1.794   1.00 82.73  ?  39   LEU E O   1 
ATOM   11417 C CB  . LEU E  2  39  ? -16.081 6.873   2.427   1.00 83.78  ?  39   LEU E CB  1 
ATOM   11418 C CG  . LEU E  2  39  ? -16.368 8.325   2.823   1.00 84.50  ?  39   LEU E CG  1 
ATOM   11419 C CD1 . LEU E  2  39  ? -16.803 8.441   4.271   1.00 85.40  ?  39   LEU E CD1 1 
ATOM   11420 C CD2 . LEU E  2  39  ? -15.180 9.225   2.527   1.00 82.90  ?  39   LEU E CD2 1 
ATOM   11421 N N   . ALA E  2  40  ? -17.985 4.647   0.904   1.00 83.80  ?  40   ALA E N   1 
ATOM   11422 C CA  . ALA E  2  40  ? -17.937 3.826   -0.295  1.00 85.61  ?  40   ALA E CA  1 
ATOM   11423 C C   . ALA E  2  40  ? -17.127 4.569   -1.345  1.00 83.13  ?  40   ALA E C   1 
ATOM   11424 O O   . ALA E  2  40  ? -17.461 5.704   -1.706  1.00 84.09  ?  40   ALA E O   1 
ATOM   11425 C CB  . ALA E  2  40  ? -19.342 3.522   -0.810  1.00 92.37  ?  40   ALA E CB  1 
ATOM   11426 N N   . ASP E  2  41  ? -16.056 3.939   -1.814  1.00 82.94  ?  41   ASP E N   1 
ATOM   11427 C CA  . ASP E  2  41  ? -15.127 4.556   -2.750  1.00 82.38  ?  41   ASP E CA  1 
ATOM   11428 C C   . ASP E  2  41  ? -15.175 3.816   -4.080  1.00 82.82  ?  41   ASP E C   1 
ATOM   11429 O O   . ASP E  2  41  ? -14.320 2.960   -4.346  1.00 81.12  ?  41   ASP E O   1 
ATOM   11430 C CB  . ASP E  2  41  ? -13.707 4.536   -2.181  1.00 79.83  ?  41   ASP E CB  1 
ATOM   11431 C CG  . ASP E  2  41  ? -12.703 5.253   -3.066  1.00 79.66  ?  41   ASP E CG  1 
ATOM   11432 O OD1 . ASP E  2  41  ? -13.025 5.580   -4.229  1.00 81.47  ?  41   ASP E OD1 1 
ATOM   11433 O OD2 . ASP E  2  41  ? -11.574 5.485   -2.585  1.00 77.91  -1 41   ASP E OD2 1 
ATOM   11434 N N   . PRO E  2  42  ? -16.136 4.134   -4.951  1.00 79.27  ?  42   PRO E N   1 
ATOM   11435 C CA  . PRO E  2  42  ? -16.191 3.451   -6.251  1.00 83.00  ?  42   PRO E CA  1 
ATOM   11436 C C   . PRO E  2  42  ? -15.029 3.803   -7.167  1.00 80.38  ?  42   PRO E C   1 
ATOM   11437 O O   . PRO E  2  42  ? -14.682 2.992   -8.035  1.00 82.56  ?  42   PRO E O   1 
ATOM   11438 C CB  . PRO E  2  42  ? -17.529 3.920   -6.836  1.00 88.48  ?  42   PRO E CB  1 
ATOM   11439 C CG  . PRO E  2  42  ? -17.770 5.248   -6.191  1.00 86.17  ?  42   PRO E CG  1 
ATOM   11440 C CD  . PRO E  2  42  ? -17.186 5.158   -4.809  1.00 81.45  ?  42   PRO E CD  1 
ATOM   11441 N N   . ASN E  2  43  ? -14.408 4.968   -6.989  1.00 82.28  ?  43   ASN E N   1 
ATOM   11442 C CA  . ASN E  2  43  ? -13.335 5.436   -7.859  1.00 83.03  ?  43   ASN E CA  1 
ATOM   11443 C C   . ASN E  2  43  ? -11.945 5.063   -7.364  1.00 81.64  ?  43   ASN E C   1 
ATOM   11444 O O   . ASN E  2  43  ? -10.961 5.371   -8.046  1.00 82.87  ?  43   ASN E O   1 
ATOM   11445 C CB  . ASN E  2  43  ? -13.419 6.954   -8.024  1.00 83.43  ?  43   ASN E CB  1 
ATOM   11446 C CG  . ASN E  2  43  ? -14.460 7.365   -9.030  1.00 85.36  ?  43   ASN E CG  1 
ATOM   11447 O OD1 . ASN E  2  43  ? -15.310 8.204   -8.751  1.00 84.98  ?  43   ASN E OD1 1 
ATOM   11448 N ND2 . ASN E  2  43  ? -14.406 6.767   -10.213 1.00 87.57  ?  43   ASN E ND2 1 
ATOM   11449 N N   . LYS E  2  44  ? -11.844 4.426   -6.199  1.00 83.02  ?  44   LYS E N   1 
ATOM   11450 C CA  . LYS E  2  44  ? -10.564 4.001   -5.626  1.00 81.03  ?  44   LYS E CA  1 
ATOM   11451 C C   . LYS E  2  44  ? -9.668  5.202   -5.332  1.00 81.06  ?  44   LYS E C   1 
ATOM   11452 O O   . LYS E  2  44  ? -8.455  5.160   -5.535  1.00 80.98  ?  44   LYS E O   1 
ATOM   11453 C CB  . LYS E  2  44  ? -9.848  2.987   -6.525  1.00 80.98  ?  44   LYS E CB  1 
ATOM   11454 C CG  . LYS E  2  44  ? -10.569 1.640   -6.702  1.00 80.21  ?  44   LYS E CG  1 
ATOM   11455 C CD  . LYS E  2  44  ? -11.642 1.395   -5.634  1.00 79.01  ?  44   LYS E CD  1 
ATOM   11456 C CE  . LYS E  2  44  ? -11.714 -0.063  -5.197  1.00 76.66  ?  44   LYS E CE  1 
ATOM   11457 N NZ  . LYS E  2  44  ? -12.448 -0.201  -3.899  1.00 75.53  ?  44   LYS E NZ  1 
ATOM   11458 N N   . VAL E  2  45  ? -10.279 6.288   -4.853  1.00 74.89  ?  45   VAL E N   1 
ATOM   11459 C CA  . VAL E  2  45  ? -9.513  7.458   -4.436  1.00 74.21  ?  45   VAL E CA  1 
ATOM   11460 C C   . VAL E  2  45  ? -8.713  7.151   -3.174  1.00 71.39  ?  45   VAL E C   1 
ATOM   11461 O O   . VAL E  2  45  ? -7.539  7.528   -3.058  1.00 71.06  ?  45   VAL E O   1 
ATOM   11462 C CB  . VAL E  2  45  ? -10.452 8.662   -4.236  1.00 74.10  ?  45   VAL E CB  1 
ATOM   11463 C CG1 . VAL E  2  45  ? -9.780  9.728   -3.393  1.00 72.71  ?  45   VAL E CG1 1 
ATOM   11464 C CG2 . VAL E  2  45  ? -10.878 9.226   -5.577  1.00 76.38  ?  45   VAL E CG2 1 
ATOM   11465 N N   . LEU E  2  46  ? -9.330  6.461   -2.212  1.00 73.35  ?  46   LEU E N   1 
ATOM   11466 C CA  . LEU E  2  46  ? -8.683  6.087   -0.958  1.00 70.75  ?  46   LEU E CA  1 
ATOM   11467 C C   . LEU E  2  46  ? -7.767  4.874   -1.096  1.00 68.69  ?  46   LEU E C   1 
ATOM   11468 O O   . LEU E  2  46  ? -7.289  4.361   -0.077  1.00 66.42  ?  46   LEU E O   1 
ATOM   11469 C CB  . LEU E  2  46  ? -9.742  5.812   0.113   1.00 70.54  ?  46   LEU E CB  1 
ATOM   11470 C CG  . LEU E  2  46  ? -10.726 6.955   0.353   1.00 72.18  ?  46   LEU E CG  1 
ATOM   11471 C CD1 . LEU E  2  46  ? -11.852 6.518   1.280   1.00 72.80  ?  46   LEU E CD1 1 
ATOM   11472 C CD2 . LEU E  2  46  ? -10.000 8.177   0.904   1.00 72.24  ?  46   LEU E CD2 1 
ATOM   11473 N N   . GLN E  2  47  ? -7.520  4.417   -2.327  1.00 67.28  ?  47   GLN E N   1 
ATOM   11474 C CA  . GLN E  2  47  ? -6.671  3.252   -2.558  1.00 65.03  ?  47   GLN E CA  1 
ATOM   11475 C C   . GLN E  2  47  ? -5.326  3.381   -1.853  1.00 62.16  ?  47   GLN E C   1 
ATOM   11476 O O   . GLN E  2  47  ? -4.809  2.410   -1.290  1.00 58.94  ?  47   GLN E O   1 
ATOM   11477 C CB  . GLN E  2  47  ? -6.475  3.067   -4.063  1.00 67.94  ?  47   GLN E CB  1 
ATOM   11478 C CG  . GLN E  2  47  ? -5.383  2.098   -4.445  1.00 65.90  ?  47   GLN E CG  1 
ATOM   11479 C CD  . GLN E  2  47  ? -5.824  0.662   -4.329  1.00 63.68  ?  47   GLN E CD  1 
ATOM   11480 O OE1 . GLN E  2  47  ? -7.018  0.366   -4.342  1.00 64.75  ?  47   GLN E OE1 1 
ATOM   11481 N NE2 . GLN E  2  47  ? -4.861  -0.246  -4.206  1.00 60.81  ?  47   GLN E NE2 1 
ATOM   11482 N N   . SER E  2  48  ? -4.757  4.584   -1.860  1.00 62.14  ?  48   SER E N   1 
ATOM   11483 C CA  . SER E  2  48  ? -3.415  4.796   -1.340  1.00 59.83  ?  48   SER E CA  1 
ATOM   11484 C C   . SER E  2  48  ? -3.332  4.638   0.175   1.00 57.41  ?  48   SER E C   1 
ATOM   11485 O O   . SER E  2  48  ? -2.232  4.460   0.706   1.00 54.91  ?  48   SER E O   1 
ATOM   11486 C CB  . SER E  2  48  ? -2.946  6.187   -1.770  1.00 63.09  ?  48   SER E CB  1 
ATOM   11487 O OG  . SER E  2  48  ? -2.106  6.782   -0.805  1.00 61.46  ?  48   SER E OG  1 
ATOM   11488 N N   . TRP E  2  49  ? -4.463  4.680   0.876   1.00 58.43  ?  49   TRP E N   1 
ATOM   11489 C CA  . TRP E  2  49  ? -4.481  4.803   2.336   1.00 58.90  ?  49   TRP E CA  1 
ATOM   11490 C C   . TRP E  2  49  ? -4.194  3.440   2.964   1.00 56.82  ?  49   TRP E C   1 
ATOM   11491 O O   . TRP E  2  49  ? -5.102  2.672   3.295   1.00 57.49  ?  49   TRP E O   1 
ATOM   11492 C CB  . TRP E  2  49  ? -5.813  5.381   2.806   1.00 61.91  ?  49   TRP E CB  1 
ATOM   11493 C CG  . TRP E  2  49  ? -5.998  6.844   2.458   1.00 64.04  ?  49   TRP E CG  1 
ATOM   11494 C CD1 . TRP E  2  49  ? -5.355  7.540   1.475   1.00 64.20  ?  49   TRP E CD1 1 
ATOM   11495 C CD2 . TRP E  2  49  ? -6.874  7.784   3.103   1.00 66.43  ?  49   TRP E CD2 1 
ATOM   11496 N NE1 . TRP E  2  49  ? -5.778  8.848   1.461   1.00 66.07  ?  49   TRP E NE1 1 
ATOM   11497 C CE2 . TRP E  2  49  ? -6.708  9.025   2.450   1.00 66.98  ?  49   TRP E CE2 1 
ATOM   11498 C CE3 . TRP E  2  49  ? -7.780  7.698   4.166   1.00 68.30  ?  49   TRP E CE3 1 
ATOM   11499 C CZ2 . TRP E  2  49  ? -7.415  10.168  2.823   1.00 68.26  ?  49   TRP E CZ2 1 
ATOM   11500 C CZ3 . TRP E  2  49  ? -8.482  8.837   4.535   1.00 70.24  ?  49   TRP E CZ3 1 
ATOM   11501 C CH2 . TRP E  2  49  ? -8.294  10.054  3.864   1.00 69.78  ?  49   TRP E CH2 1 
ATOM   11502 N N   . ASP E  2  50  ? -2.905  3.148   3.136   1.00 57.58  ?  50   ASP E N   1 
ATOM   11503 C CA  . ASP E  2  50  ? -2.445  1.895   3.723   1.00 56.02  ?  50   ASP E CA  1 
ATOM   11504 C C   . ASP E  2  50  ? -2.341  2.049   5.236   1.00 59.22  ?  50   ASP E C   1 
ATOM   11505 O O   . ASP E  2  50  ? -1.497  2.802   5.733   1.00 60.22  ?  50   ASP E O   1 
ATOM   11506 C CB  . ASP E  2  50  ? -1.096  1.497   3.128   1.00 52.49  ?  50   ASP E CB  1 
ATOM   11507 C CG  . ASP E  2  50  ? -0.467  0.308   3.830   1.00 51.70  ?  50   ASP E CG  1 
ATOM   11508 O OD1 . ASP E  2  50  ? -1.193  -0.465  4.488   1.00 53.61  ?  50   ASP E OD1 1 
ATOM   11509 O OD2 . ASP E  2  50  ? 0.767   0.144   3.713   1.00 49.66  -1 50   ASP E OD2 1 
ATOM   11510 N N   . ALA E  2  51  ? -3.157  1.281   5.960   1.00 54.62  ?  51   ALA E N   1 
ATOM   11511 C CA  . ALA E  2  51  ? -3.272  1.417   7.407   1.00 59.15  ?  51   ALA E CA  1 
ATOM   11512 C C   . ALA E  2  51  ? -2.022  0.971   8.153   1.00 59.45  ?  51   ALA E C   1 
ATOM   11513 O O   . ALA E  2  51  ? -1.813  1.401   9.293   1.00 62.90  ?  51   ALA E O   1 
ATOM   11514 C CB  . ALA E  2  51  ? -4.473  0.614   7.905   1.00 61.10  ?  51   ALA E CB  1 
ATOM   11515 N N   . THR E  2  52  ? -1.196  0.121   7.547   1.00 57.13  ?  52   THR E N   1 
ATOM   11516 C CA  . THR E  2  52  ? -0.081  -0.510  8.239   1.00 57.86  ?  52   THR E CA  1 
ATOM   11517 C C   . THR E  2  52  ? 1.193   0.328   8.220   1.00 57.33  ?  52   THR E C   1 
ATOM   11518 O O   . THR E  2  52  ? 2.234   -0.144  8.688   1.00 58.07  ?  52   THR E O   1 
ATOM   11519 C CB  . THR E  2  52  ? 0.195   -1.892  7.635   1.00 56.25  ?  52   THR E CB  1 
ATOM   11520 O OG1 . THR E  2  52  ? 0.714   -1.742  6.308   1.00 53.92  ?  52   THR E OG1 1 
ATOM   11521 C CG2 . THR E  2  52  ? -1.083  -2.709  7.572   1.00 59.13  ?  52   THR E CG2 1 
ATOM   11522 N N   . LEU E  2  53  ? 1.147   1.545   7.689   1.00 53.44  ?  53   LEU E N   1 
ATOM   11523 C CA  . LEU E  2  53  ? 2.298   2.430   7.774   1.00 53.43  ?  53   LEU E CA  1 
ATOM   11524 C C   . LEU E  2  53  ? 2.313   3.146   9.123   1.00 58.56  ?  53   LEU E C   1 
ATOM   11525 O O   . LEU E  2  53  ? 1.299   3.230   9.820   1.00 61.32  ?  53   LEU E O   1 
ATOM   11526 C CB  . LEU E  2  53  ? 2.285   3.450   6.633   1.00 49.93  ?  53   LEU E CB  1 
ATOM   11527 C CG  . LEU E  2  53  ? 2.173   2.871   5.219   1.00 47.16  ?  53   LEU E CG  1 
ATOM   11528 C CD1 . LEU E  2  53  ? 2.232   3.970   4.186   1.00 44.92  ?  53   LEU E CD1 1 
ATOM   11529 C CD2 . LEU E  2  53  ? 3.259   1.843   4.957   1.00 48.60  ?  53   LEU E CD2 1 
ATOM   11530 N N   . VAL E  2  54  ? 3.488   3.669   9.487   1.00 53.67  ?  54   VAL E N   1 
ATOM   11531 C CA  . VAL E  2  54  ? 3.620   4.391   10.752  1.00 58.22  ?  54   VAL E CA  1 
ATOM   11532 C C   . VAL E  2  54  ? 2.736   5.632   10.755  1.00 59.78  ?  54   VAL E C   1 
ATOM   11533 O O   . VAL E  2  54  ? 1.953   5.854   11.685  1.00 63.01  ?  54   VAL E O   1 
ATOM   11534 C CB  . VAL E  2  54  ? 5.091   4.757   11.021  1.00 59.28  ?  54   VAL E CB  1 
ATOM   11535 C CG1 . VAL E  2  54  ? 5.276   5.158   12.473  1.00 63.78  ?  54   VAL E CG1 1 
ATOM   11536 C CG2 . VAL E  2  54  ? 6.002   3.605   10.674  1.00 57.34  ?  54   VAL E CG2 1 
ATOM   11537 N N   . THR E  2  55  ? 2.859   6.466   9.730   1.00 58.77  ?  55   THR E N   1 
ATOM   11538 C CA  . THR E  2  55  ? 2.065   7.675   9.591   1.00 60.41  ?  55   THR E CA  1 
ATOM   11539 C C   . THR E  2  55  ? 1.440   7.704   8.206   1.00 55.89  ?  55   THR E C   1 
ATOM   11540 O O   . THR E  2  55  ? 1.942   7.063   7.274   1.00 51.55  ?  55   THR E O   1 
ATOM   11541 C CB  . THR E  2  55  ? 2.902   8.946   9.818   1.00 63.18  ?  55   THR E CB  1 
ATOM   11542 O OG1 . THR E  2  55  ? 3.583   9.302   8.611   1.00 58.02  ?  55   THR E OG1 1 
ATOM   11543 C CG2 . THR E  2  55  ? 3.912   8.736   10.927  1.00 66.77  ?  55   THR E CG2 1 
ATOM   11544 N N   . PRO E  2  56  ? 0.325   8.420   8.042   1.00 59.39  ?  56   PRO E N   1 
ATOM   11545 C CA  . PRO E  2  56  ? -0.338  8.502   6.735   1.00 56.69  ?  56   PRO E CA  1 
ATOM   11546 C C   . PRO E  2  56  ? 0.256   9.529   5.782   1.00 54.64  ?  56   PRO E C   1 
ATOM   11547 O O   . PRO E  2  56  ? -0.380  9.850   4.774   1.00 54.24  ?  56   PRO E O   1 
ATOM   11548 C CB  . PRO E  2  56  ? -1.775  8.888   7.121   1.00 60.10  ?  56   PRO E CB  1 
ATOM   11549 C CG  . PRO E  2  56  ? -1.614  9.682   8.363   1.00 64.13  ?  56   PRO E CG  1 
ATOM   11550 C CD  . PRO E  2  56  ? -0.491  9.026   9.112   1.00 64.44  ?  56   PRO E CD  1 
ATOM   11551 N N   . CYS E  2  57  ? 1.452   10.048  6.067   1.00 60.16  ?  57   CYS E N   1 
ATOM   11552 C CA  . CYS E  2  57  ? 1.992   11.164  5.302   1.00 58.19  ?  57   CYS E CA  1 
ATOM   11553 C C   . CYS E  2  57  ? 2.360   10.791  3.871   1.00 54.09  ?  57   CYS E C   1 
ATOM   11554 O O   . CYS E  2  57  ? 2.416   11.682  3.019   1.00 53.81  ?  57   CYS E O   1 
ATOM   11555 C CB  . CYS E  2  57  ? 3.208   11.739  6.021   1.00 58.46  ?  57   CYS E CB  1 
ATOM   11556 S SG  . CYS E  2  57  ? 2.820   12.433  7.652   1.00 66.24  ?  57   CYS E SG  1 
ATOM   11557 N N   . THR E  2  58  ? 2.612   9.512   3.581   1.00 57.75  ?  58   THR E N   1 
ATOM   11558 C CA  . THR E  2  58  ? 2.902   9.086   2.215   1.00 55.19  ?  58   THR E CA  1 
ATOM   11559 C C   . THR E  2  58  ? 1.644   8.721   1.434   1.00 57.98  ?  58   THR E C   1 
ATOM   11560 O O   . THR E  2  58  ? 1.750   8.284   0.282   1.00 57.89  ?  58   THR E O   1 
ATOM   11561 C CB  . THR E  2  58  ? 3.873   7.892   2.203   1.00 51.17  ?  58   THR E CB  1 
ATOM   11562 O OG1 . THR E  2  58  ? 3.293   6.780   2.894   1.00 51.48  ?  58   THR E OG1 1 
ATOM   11563 C CG2 . THR E  2  58  ? 5.182   8.256   2.873   1.00 49.50  ?  58   THR E CG2 1 
ATOM   11564 N N   . TRP E  2  59  ? 0.465   8.880   2.032   1.00 52.47  ?  59   TRP E N   1 
ATOM   11565 C CA  . TRP E  2  59  ? -0.779  8.635   1.321   1.00 55.67  ?  59   TRP E CA  1 
ATOM   11566 C C   . TRP E  2  59  ? -1.072  9.773   0.356   1.00 59.12  ?  59   TRP E C   1 
ATOM   11567 O O   . TRP E  2  59  ? -0.638  10.909  0.555   1.00 58.77  ?  59   TRP E O   1 
ATOM   11568 C CB  . TRP E  2  59  ? -1.950  8.501   2.293   1.00 58.15  ?  59   TRP E CB  1 
ATOM   11569 C CG  . TRP E  2  59  ? -1.823  7.427   3.333   1.00 56.18  ?  59   TRP E CG  1 
ATOM   11570 C CD1 . TRP E  2  59  ? -0.811  6.524   3.474   1.00 52.18  ?  59   TRP E CD1 1 
ATOM   11571 C CD2 . TRP E  2  59  ? -2.761  7.143   4.375   1.00 58.78  ?  59   TRP E CD2 1 
ATOM   11572 N NE1 . TRP E  2  59  ? -1.059  5.702   4.546   1.00 53.00  ?  59   TRP E NE1 1 
ATOM   11573 C CE2 . TRP E  2  59  ? -2.253  6.062   5.113   1.00 57.31  ?  59   TRP E CE2 1 
ATOM   11574 C CE3 . TRP E  2  59  ? -3.980  7.708   4.758   1.00 61.90  ?  59   TRP E CE3 1 
ATOM   11575 C CZ2 . TRP E  2  59  ? -2.922  5.532   6.208   1.00 60.38  ?  59   TRP E CZ2 1 
ATOM   11576 C CZ3 . TRP E  2  59  ? -4.643  7.179   5.841   1.00 63.94  ?  59   TRP E CZ3 1 
ATOM   11577 C CH2 . TRP E  2  59  ? -4.114  6.103   6.556   1.00 63.56  ?  59   TRP E CH2 1 
ATOM   11578 N N   . PHE E  2  60  ? -1.833  9.467   -0.690  1.00 56.47  ?  60   PHE E N   1 
ATOM   11579 C CA  . PHE E  2  60  ? -2.254  10.518  -1.600  1.00 59.20  ?  60   PHE E CA  1 
ATOM   11580 C C   . PHE E  2  60  ? -3.425  11.293  -1.001  1.00 58.44  ?  60   PHE E C   1 
ATOM   11581 O O   . PHE E  2  60  ? -4.155  10.797  -0.139  1.00 57.42  ?  60   PHE E O   1 
ATOM   11582 C CB  . PHE E  2  60  ? -2.642  9.947   -2.966  1.00 62.36  ?  60   PHE E CB  1 
ATOM   11583 C CG  . PHE E  2  60  ? -1.556  9.142   -3.624  1.00 63.38  ?  60   PHE E CG  1 
ATOM   11584 C CD1 . PHE E  2  60  ? -0.221  9.460   -3.437  1.00 61.60  ?  60   PHE E CD1 1 
ATOM   11585 C CD2 . PHE E  2  60  ? -1.874  8.067   -4.433  1.00 64.56  ?  60   PHE E CD2 1 
ATOM   11586 C CE1 . PHE E  2  60  ? 0.773   8.717   -4.039  1.00 60.73  ?  60   PHE E CE1 1 
ATOM   11587 C CE2 . PHE E  2  60  ? -0.884  7.318   -5.034  1.00 64.84  ?  60   PHE E CE2 1 
ATOM   11588 C CZ  . PHE E  2  60  ? 0.441   7.646   -4.840  1.00 63.05  ?  60   PHE E CZ  1 
ATOM   11589 N N   . HIS E  2  61  ? -3.589  12.532  -1.465  1.00 61.44  ?  61   HIS E N   1 
ATOM   11590 C CA  . HIS E  2  61  ? -4.634  13.452  -1.023  1.00 60.50  ?  61   HIS E CA  1 
ATOM   11591 C C   . HIS E  2  61  ? -4.488  13.851  0.442   1.00 58.99  ?  61   HIS E C   1 
ATOM   11592 O O   . HIS E  2  61  ? -5.386  14.490  1.000   1.00 59.13  ?  61   HIS E O   1 
ATOM   11593 C CB  . HIS E  2  61  ? -6.029  12.871  -1.285  1.00 61.34  ?  61   HIS E CB  1 
ATOM   11594 C CG  . HIS E  2  61  ? -6.134  12.136  -2.586  1.00 63.50  ?  61   HIS E CG  1 
ATOM   11595 N ND1 . HIS E  2  61  ? -5.976  12.759  -3.806  1.00 65.55  ?  61   HIS E ND1 1 
ATOM   11596 C CD2 . HIS E  2  61  ? -6.370  10.831  -2.858  1.00 64.18  ?  61   HIS E CD2 1 
ATOM   11597 C CE1 . HIS E  2  61  ? -6.119  11.870  -4.774  1.00 68.16  ?  61   HIS E CE1 1 
ATOM   11598 N NE2 . HIS E  2  61  ? -6.358  10.693  -4.226  1.00 67.11  ?  61   HIS E NE2 1 
ATOM   11599 N N   . VAL E  2  62  ? -3.360  13.520  1.066   1.00 63.02  ?  62   VAL E N   1 
ATOM   11600 C CA  . VAL E  2  62  ? -3.045  13.895  2.438   1.00 62.80  ?  62   VAL E CA  1 
ATOM   11601 C C   . VAL E  2  62  ? -1.664  14.538  2.434   1.00 61.37  ?  62   VAL E C   1 
ATOM   11602 O O   . VAL E  2  62  ? -0.718  13.970  1.878   1.00 59.92  ?  62   VAL E O   1 
ATOM   11603 C CB  . VAL E  2  62  ? -3.073  12.675  3.381   1.00 63.46  ?  62   VAL E CB  1 
ATOM   11604 C CG1 . VAL E  2  62  ? -2.344  12.980  4.678   1.00 64.51  ?  62   VAL E CG1 1 
ATOM   11605 C CG2 . VAL E  2  62  ? -4.504  12.246  3.653   1.00 64.94  ?  62   VAL E CG2 1 
ATOM   11606 N N   . THR E  2  63  ? -1.546  15.720  3.036   1.00 65.34  ?  63   THR E N   1 
ATOM   11607 C CA  . THR E  2  63  ? -0.261  16.395  3.162   1.00 64.04  ?  63   THR E CA  1 
ATOM   11608 C C   . THR E  2  63  ? 0.027   16.654  4.639   1.00 66.44  ?  63   THR E C   1 
ATOM   11609 O O   . THR E  2  63  ? -0.876  17.009  5.404   1.00 69.67  ?  63   THR E O   1 
ATOM   11610 C CB  . THR E  2  63  ? -0.222  17.717  2.352   1.00 63.33  ?  63   THR E CB  1 
ATOM   11611 O OG1 . THR E  2  63  ? -0.787  18.783  3.119   1.00 65.06  ?  63   THR E OG1 1 
ATOM   11612 C CG2 . THR E  2  63  ? -0.998  17.588  1.040   1.00 63.50  ?  63   THR E CG2 1 
ATOM   11613 N N   . CYS E  2  64  ? 1.281   16.448  5.039   1.00 64.38  ?  64   CYS E N   1 
ATOM   11614 C CA  . CYS E  2  64  ? 1.740   16.623  6.412   1.00 67.77  ?  64   CYS E CA  1 
ATOM   11615 C C   . CYS E  2  64  ? 2.665   17.827  6.512   1.00 66.80  ?  64   CYS E C   1 
ATOM   11616 O O   . CYS E  2  64  ? 3.144   18.358  5.508   1.00 63.12  ?  64   CYS E O   1 
ATOM   11617 C CB  . CYS E  2  64  ? 2.478   15.380  6.923   1.00 67.66  ?  64   CYS E CB  1 
ATOM   11618 S SG  . CYS E  2  64  ? 1.464   13.938  7.316   1.00 70.29  ?  64   CYS E SG  1 
ATOM   11619 N N   . ASN E  2  65  ? 2.909   18.260  7.747   1.00 67.21  ?  65   ASN E N   1 
ATOM   11620 C CA  . ASN E  2  65  ? 3.916   19.276  8.012   1.00 66.34  ?  65   ASN E CA  1 
ATOM   11621 C C   . ASN E  2  65  ? 5.244   18.583  8.330   1.00 64.71  ?  65   ASN E C   1 
ATOM   11622 O O   . ASN E  2  65  ? 5.377   17.364  8.193   1.00 63.66  ?  65   ASN E O   1 
ATOM   11623 C CB  . ASN E  2  65  ? 3.446   20.232  9.116   1.00 71.42  ?  65   ASN E CB  1 
ATOM   11624 C CG  . ASN E  2  65  ? 3.219   19.546  10.461  1.00 77.26  ?  65   ASN E CG  1 
ATOM   11625 O OD1 . ASN E  2  65  ? 3.563   18.381  10.661  1.00 77.82  ?  65   ASN E OD1 1 
ATOM   11626 N ND2 . ASN E  2  65  ? 2.632   20.285  11.396  1.00 81.81  ?  65   ASN E ND2 1 
ATOM   11627 N N   . SER E  2  66  ? 6.249   19.352  8.754   1.00 68.12  ?  66   SER E N   1 
ATOM   11628 C CA  . SER E  2  66  ? 7.562   18.777  9.030   1.00 66.51  ?  66   SER E CA  1 
ATOM   11629 C C   . SER E  2  66  ? 7.574   17.890  10.270  1.00 71.38  ?  66   SER E C   1 
ATOM   11630 O O   . SER E  2  66  ? 8.550   17.158  10.472  1.00 70.37  ?  66   SER E O   1 
ATOM   11631 C CB  . SER E  2  66  ? 8.605   19.885  9.179   1.00 65.48  ?  66   SER E CB  1 
ATOM   11632 O OG  . SER E  2  66  ? 8.181   20.866  10.106  1.00 69.74  ?  66   SER E OG  1 
ATOM   11633 N N   . ASP E  2  67  ? 6.538   17.950  11.107  1.00 66.23  ?  67   ASP E N   1 
ATOM   11634 C CA  . ASP E  2  67  ? 6.405   17.074  12.265  1.00 72.17  ?  67   ASP E CA  1 
ATOM   11635 C C   . ASP E  2  67  ? 5.645   15.792  11.950  1.00 73.48  ?  67   ASP E C   1 
ATOM   11636 O O   . ASP E  2  67  ? 5.421   14.983  12.858  1.00 79.25  ?  67   ASP E O   1 
ATOM   11637 C CB  . ASP E  2  67  ? 5.709   17.817  13.410  1.00 78.22  ?  67   ASP E CB  1 
ATOM   11638 C CG  . ASP E  2  67  ? 6.456   19.068  13.831  1.00 77.29  ?  67   ASP E CG  1 
ATOM   11639 O OD1 . ASP E  2  67  ? 7.687   19.121  13.619  1.00 73.86  ?  67   ASP E OD1 1 
ATOM   11640 O OD2 . ASP E  2  67  ? 5.819   19.993  14.378  1.00 80.05  -1 67   ASP E OD2 1 
ATOM   11641 N N   . ASN E  2  68  ? 5.258   15.593  10.685  1.00 69.51  ?  68   ASN E N   1 
ATOM   11642 C CA  . ASN E  2  68  ? 4.476   14.438  10.237  1.00 69.42  ?  68   ASN E CA  1 
ATOM   11643 C C   . ASN E  2  68  ? 3.077   14.429  10.846  1.00 76.07  ?  68   ASN E C   1 
ATOM   11644 O O   . ASN E  2  68  ? 2.529   13.372  11.153  1.00 79.01  ?  68   ASN E O   1 
ATOM   11645 C CB  . ASN E  2  68  ? 5.198   13.122  10.528  1.00 69.63  ?  68   ASN E CB  1 
ATOM   11646 C CG  . ASN E  2  68  ? 6.616   13.120  10.018  1.00 63.30  ?  68   ASN E CG  1 
ATOM   11647 O OD1 . ASN E  2  68  ? 6.865   12.806  8.857   1.00 56.53  ?  68   ASN E OD1 1 
ATOM   11648 N ND2 . ASN E  2  68  ? 7.557   13.479  10.883  1.00 65.63  ?  68   ASN E ND2 1 
ATOM   11649 N N   . SER E  2  69  ? 2.496   15.611  11.022  1.00 73.12  ?  69   SER E N   1 
ATOM   11650 C CA  . SER E  2  69  ? 1.118   15.755  11.469  1.00 77.87  ?  69   SER E CA  1 
ATOM   11651 C C   . SER E  2  69  ? 0.265   16.205  10.292  1.00 72.79  ?  69   SER E C   1 
ATOM   11652 O O   . SER E  2  69  ? 0.652   17.117  9.555   1.00 68.57  ?  69   SER E O   1 
ATOM   11653 C CB  . SER E  2  69  ? 1.010   16.756  12.622  1.00 82.43  ?  69   SER E CB  1 
ATOM   11654 O OG  . SER E  2  69  ? -0.066  16.429  13.488  1.00 87.99  ?  69   SER E OG  1 
ATOM   11655 N N   . VAL E  2  70  ? -0.897  15.573  10.125  1.00 77.69  ?  70   VAL E N   1 
ATOM   11656 C CA  . VAL E  2  70  ? -1.743  15.849  8.970   1.00 72.82  ?  70   VAL E CA  1 
ATOM   11657 C C   . VAL E  2  70  ? -2.239  17.288  9.032   1.00 73.08  ?  70   VAL E C   1 
ATOM   11658 O O   . VAL E  2  70  ? -2.710  17.758  10.078  1.00 77.35  ?  70   VAL E O   1 
ATOM   11659 C CB  . VAL E  2  70  ? -2.915  14.857  8.916   1.00 72.71  ?  70   VAL E CB  1 
ATOM   11660 C CG1 . VAL E  2  70  ? -3.941  15.281  7.868   1.00 68.92  ?  70   VAL E CG1 1 
ATOM   11661 C CG2 . VAL E  2  70  ? -2.406  13.451  8.641   1.00 70.26  ?  70   VAL E CG2 1 
ATOM   11662 N N   . THR E  2  71  ? -2.130  17.998  7.905   1.00 75.85  ?  71   THR E N   1 
ATOM   11663 C CA  . THR E  2  71  ? -2.624  19.366  7.795   1.00 75.50  ?  71   THR E CA  1 
ATOM   11664 C C   . THR E  2  71  ? -3.601  19.592  6.646   1.00 72.31  ?  71   THR E C   1 
ATOM   11665 O O   . THR E  2  71  ? -4.276  20.629  6.638   1.00 72.71  ?  71   THR E O   1 
ATOM   11666 C CB  . THR E  2  71  ? -1.456  20.356  7.647   1.00 74.20  ?  71   THR E CB  1 
ATOM   11667 O OG1 . THR E  2  71  ? -0.696  20.033  6.477   1.00 69.72  ?  71   THR E OG1 1 
ATOM   11668 C CG2 . THR E  2  71  ? -0.544  20.307  8.869   1.00 77.93  ?  71   THR E CG2 1 
ATOM   11669 N N   . ARG E  2  72  ? -3.700  18.677  5.681   1.00 72.97  ?  72   ARG E N   1 
ATOM   11670 C CA  . ARG E  2  72  ? -4.634  18.811  4.571   1.00 70.95  ?  72   ARG E CA  1 
ATOM   11671 C C   . ARG E  2  72  ? -5.236  17.452  4.246   1.00 70.49  ?  72   ARG E C   1 
ATOM   11672 O O   . ARG E  2  72  ? -4.560  16.423  4.349   1.00 70.13  ?  72   ARG E O   1 
ATOM   11673 C CB  . ARG E  2  72  ? -3.954  19.378  3.307   1.00 68.29  ?  72   ARG E CB  1 
ATOM   11674 C CG  . ARG E  2  72  ? -3.574  20.856  3.367   1.00 68.44  ?  72   ARG E CG  1 
ATOM   11675 C CD  . ARG E  2  72  ? -3.244  21.413  1.977   1.00 66.58  ?  72   ARG E CD  1 
ATOM   11676 N NE  . ARG E  2  72  ? -4.406  21.405  1.097   1.00 66.75  ?  72   ARG E NE  1 
ATOM   11677 C CZ  . ARG E  2  72  ? -5.039  22.494  0.679   1.00 67.27  ?  72   ARG E CZ  1 
ATOM   11678 N NH1 . ARG E  2  72  ? -4.626  23.705  1.016   1.00 67.63  ?  72   ARG E NH1 1 
ATOM   11679 N NH2 . ARG E  2  72  ? -6.123  22.363  -0.081  1.00 67.66  ?  72   ARG E NH2 1 
ATOM   11680 N N   . VAL E  2  73  ? -6.509  17.458  3.856   1.00 70.35  ?  73   VAL E N   1 
ATOM   11681 C CA  . VAL E  2  73  ? -7.196  16.290  3.302   1.00 69.82  ?  73   VAL E CA  1 
ATOM   11682 C C   . VAL E  2  73  ? -7.964  16.812  2.092   1.00 69.02  ?  73   VAL E C   1 
ATOM   11683 O O   . VAL E  2  73  ? -9.023  17.433  2.241   1.00 69.86  ?  73   VAL E O   1 
ATOM   11684 C CB  . VAL E  2  73  ? -8.134  15.610  4.312   1.00 71.88  ?  73   VAL E CB  1 
ATOM   11685 C CG1 . VAL E  2  73  ? -8.806  14.396  3.691   1.00 71.20  ?  73   VAL E CG1 1 
ATOM   11686 C CG2 . VAL E  2  73  ? -7.376  15.206  5.558   1.00 73.92  ?  73   VAL E CG2 1 
ATOM   11687 N N   . ASP E  2  74  ? -7.430  16.588  0.895   1.00 69.01  ?  74   ASP E N   1 
ATOM   11688 C CA  . ASP E  2  74  ? -7.995  17.150  -0.333  1.00 69.15  ?  74   ASP E CA  1 
ATOM   11689 C C   . ASP E  2  74  ? -8.760  16.041  -1.050  1.00 69.94  ?  74   ASP E C   1 
ATOM   11690 O O   . ASP E  2  74  ? -8.222  15.352  -1.915  1.00 70.51  ?  74   ASP E O   1 
ATOM   11691 C CB  . ASP E  2  74  ? -6.895  17.738  -1.210  1.00 68.76  ?  74   ASP E CB  1 
ATOM   11692 C CG  . ASP E  2  74  ? -6.177  18.910  -0.554  1.00 68.00  ?  74   ASP E CG  1 
ATOM   11693 O OD1 . ASP E  2  74  ? -5.180  18.669  0.163   1.00 67.41  -1 74   ASP E OD1 1 
ATOM   11694 O OD2 . ASP E  2  74  ? -6.611  20.069  -0.747  1.00 68.24  ?  74   ASP E OD2 1 
ATOM   11695 N N   . LEU E  2  75  ? -10.036 15.875  -0.689  1.00 70.75  ?  75   LEU E N   1 
ATOM   11696 C CA  . LEU E  2  75  ? -10.878 14.813  -1.234  1.00 71.55  ?  75   LEU E CA  1 
ATOM   11697 C C   . LEU E  2  75  ? -12.094 15.365  -1.977  1.00 72.45  ?  75   LEU E C   1 
ATOM   11698 O O   . LEU E  2  75  ? -13.137 14.711  -2.044  1.00 73.23  ?  75   LEU E O   1 
ATOM   11699 C CB  . LEU E  2  75  ? -11.326 13.861  -0.124  1.00 71.63  ?  75   LEU E CB  1 
ATOM   11700 C CG  . LEU E  2  75  ? -10.278 12.912  0.458   1.00 71.08  ?  75   LEU E CG  1 
ATOM   11701 C CD1 . LEU E  2  75  ? -10.829 12.144  1.650   1.00 71.64  ?  75   LEU E CD1 1 
ATOM   11702 C CD2 . LEU E  2  75  ? -9.794  11.959  -0.606  1.00 71.16  ?  75   LEU E CD2 1 
ATOM   11703 N N   . GLY E  2  76  ? -11.980 16.564  -2.542  1.00 76.62  ?  76   GLY E N   1 
ATOM   11704 C CA  . GLY E  2  76  ? -13.082 17.119  -3.311  1.00 77.67  ?  76   GLY E CA  1 
ATOM   11705 C C   . GLY E  2  76  ? -13.236 16.430  -4.657  1.00 79.04  ?  76   GLY E C   1 
ATOM   11706 O O   . GLY E  2  76  ? -12.255 16.059  -5.307  1.00 79.42  ?  76   GLY E O   1 
ATOM   11707 N N   . ASN E  2  77  ? -14.494 16.263  -5.079  1.00 79.37  ?  77   ASN E N   1 
ATOM   11708 C CA  . ASN E  2  77  ? -14.835 15.669  -6.377  1.00 81.17  ?  77   ASN E CA  1 
ATOM   11709 C C   . ASN E  2  77  ? -14.235 14.274  -6.527  1.00 81.59  ?  77   ASN E C   1 
ATOM   11710 O O   . ASN E  2  77  ? -13.570 13.960  -7.519  1.00 82.96  ?  77   ASN E O   1 
ATOM   11711 C CB  . ASN E  2  77  ? -14.391 16.563  -7.537  1.00 82.08  ?  77   ASN E CB  1 
ATOM   11712 C CG  . ASN E  2  77  ? -14.869 17.984  -7.397  1.00 81.80  ?  77   ASN E CG  1 
ATOM   11713 O OD1 . ASN E  2  77  ? -16.024 18.291  -7.684  1.00 86.00  ?  77   ASN E OD1 1 
ATOM   11714 N ND2 . ASN E  2  77  ? -13.976 18.868  -6.968  1.00 80.41  ?  77   ASN E ND2 1 
ATOM   11715 N N   . ALA E  2  78  ? -14.469 13.429  -5.526  1.00 84.16  ?  78   ALA E N   1 
ATOM   11716 C CA  . ALA E  2  78  ? -13.937 12.074  -5.531  1.00 84.39  ?  78   ALA E CA  1 
ATOM   11717 C C   . ALA E  2  78  ? -15.036 11.022  -5.552  1.00 85.25  ?  78   ALA E C   1 
ATOM   11718 O O   . ALA E  2  78  ? -14.739 9.825   -5.450  1.00 85.29  ?  78   ALA E O   1 
ATOM   11719 C CB  . ALA E  2  78  ? -13.016 11.875  -4.325  1.00 82.54  ?  78   ALA E CB  1 
ATOM   11720 N N   . ASN E  2  79  ? -16.296 11.443  -5.697  1.00 90.52  ?  79   ASN E N   1 
ATOM   11721 C CA  . ASN E  2  79  ? -17.438 10.537  -5.845  1.00 91.91  ?  79   ASN E CA  1 
ATOM   11722 C C   . ASN E  2  79  ? -17.539 9.564   -4.673  1.00 91.08  ?  79   ASN E C   1 
ATOM   11723 O O   . ASN E  2  79  ? -17.919 8.402   -4.837  1.00 92.07  ?  79   ASN E O   1 
ATOM   11724 C CB  . ASN E  2  79  ? -17.389 9.790   -7.177  1.00 93.80  ?  79   ASN E CB  1 
ATOM   11725 C CG  . ASN E  2  79  ? -17.003 10.692  -8.332  1.00 94.78  ?  79   ASN E CG  1 
ATOM   11726 O OD1 . ASN E  2  79  ? -16.964 11.915  -8.189  1.00 94.05  ?  79   ASN E OD1 1 
ATOM   11727 N ND2 . ASN E  2  79  ? -16.716 10.095  -9.485  1.00 96.64  ?  79   ASN E ND2 1 
ATOM   11728 N N   . LEU E  2  80  ? -17.195 10.047  -3.481  1.00 87.94  ?  80   LEU E N   1 
ATOM   11729 C CA  . LEU E  2  80  ? -17.322 9.256   -2.266  1.00 89.37  ?  80   LEU E CA  1 
ATOM   11730 C C   . LEU E  2  80  ? -18.739 9.344   -1.715  1.00 92.27  ?  80   LEU E C   1 
ATOM   11731 O O   . LEU E  2  80  ? -19.335 10.424  -1.646  1.00 92.45  ?  80   LEU E O   1 
ATOM   11732 C CB  . LEU E  2  80  ? -16.333 9.734   -1.200  1.00 87.53  ?  80   LEU E CB  1 
ATOM   11733 C CG  . LEU E  2  80  ? -14.919 9.145   -1.135  1.00 85.44  ?  80   LEU E CG  1 
ATOM   11734 C CD1 . LEU E  2  80  ? -14.958 7.657   -0.844  1.00 87.91  ?  80   LEU E CD1 1 
ATOM   11735 C CD2 . LEU E  2  80  ? -14.157 9.392   -2.397  1.00 83.10  ?  80   LEU E CD2 1 
ATOM   11736 N N   . SER E  2  81  ? -19.278 8.195   -1.320  1.00 88.78  ?  81   SER E N   1 
ATOM   11737 C CA  . SER E  2  81  ? -20.567 8.130   -0.653  1.00 91.79  ?  81   SER E CA  1 
ATOM   11738 C C   . SER E  2  81  ? -20.394 7.370   0.654   1.00 93.90  ?  81   SER E C   1 
ATOM   11739 O O   . SER E  2  81  ? -19.563 6.465   0.760   1.00 93.80  ?  81   SER E O   1 
ATOM   11740 C CB  . SER E  2  81  ? -21.642 7.463   -1.538  1.00 94.69  ?  81   SER E CB  1 
ATOM   11741 O OG  . SER E  2  81  ? -21.249 6.169   -1.965  1.00 95.20  ?  81   SER E OG  1 
ATOM   11742 N N   . GLY E  2  82  ? -21.164 7.762   1.649   1.00 95.34  ?  82   GLY E N   1 
ATOM   11743 C CA  . GLY E  2  82  ? -21.029 7.222   2.986   1.00 97.46  ?  82   GLY E CA  1 
ATOM   11744 C C   . GLY E  2  82  ? -21.318 8.303   4.014   1.00 98.34  ?  82   GLY E C   1 
ATOM   11745 O O   . GLY E  2  82  ? -22.019 9.271   3.724   1.00 98.05  ?  82   GLY E O   1 
ATOM   11746 N N   . GLN E  2  83  ? -20.756 8.119   5.209   1.00 93.49  ?  83   GLN E N   1 
ATOM   11747 C CA  . GLN E  2  83  ? -20.998 9.002   6.342   1.00 94.90  ?  83   GLN E CA  1 
ATOM   11748 C C   . GLN E  2  83  ? -19.674 9.442   6.950   1.00 94.25  ?  83   GLN E C   1 
ATOM   11749 O O   . GLN E  2  83  ? -18.696 8.693   6.945   1.00 93.81  ?  83   GLN E O   1 
ATOM   11750 C CB  . GLN E  2  83  ? -21.847 8.299   7.396   1.00 97.75  ?  83   GLN E CB  1 
ATOM   11751 C CG  . GLN E  2  83  ? -22.932 7.419   6.805   1.00 98.68  ?  83   GLN E CG  1 
ATOM   11752 C CD  . GLN E  2  83  ? -24.323 7.889   7.164   1.00 101.75 ?  83   GLN E CD  1 
ATOM   11753 O OE1 . GLN E  2  83  ? -24.492 8.734   8.041   1.00 102.48 ?  83   GLN E OE1 1 
ATOM   11754 N NE2 . GLN E  2  83  ? -25.332 7.328   6.504   1.00 104.23 ?  83   GLN E NE2 1 
ATOM   11755 N N   . LEU E  2  84  ? -19.645 10.667  7.473   1.00 89.14  ?  84   LEU E N   1 
ATOM   11756 C CA  . LEU E  2  84  ? -18.473 11.130  8.203   1.00 89.19  ?  84   LEU E CA  1 
ATOM   11757 C C   . LEU E  2  84  ? -18.317 10.331  9.495   1.00 91.76  ?  84   LEU E C   1 
ATOM   11758 O O   . LEU E  2  84  ? -19.227 9.627   9.939   1.00 93.20  ?  84   LEU E O   1 
ATOM   11759 C CB  . LEU E  2  84  ? -18.575 12.625  8.522   1.00 89.00  ?  84   LEU E CB  1 
ATOM   11760 C CG  . LEU E  2  84  ? -18.108 13.687  7.521   1.00 85.36  ?  84   LEU E CG  1 
ATOM   11761 C CD1 . LEU E  2  84  ? -18.879 13.594  6.225   1.00 83.60  ?  84   LEU E CD1 1 
ATOM   11762 C CD2 . LEU E  2  84  ? -18.256 15.079  8.122   1.00 86.07  ?  84   LEU E CD2 1 
ATOM   11763 N N   . VAL E  2  85  ? -17.135 10.431  10.092  1.00 84.15  ?  85   VAL E N   1 
ATOM   11764 C CA  . VAL E  2  85  ? -16.787 9.670   11.284  1.00 85.08  ?  85   VAL E CA  1 
ATOM   11765 C C   . VAL E  2  85  ? -16.358 10.638  12.377  1.00 86.21  ?  85   VAL E C   1 
ATOM   11766 O O   . VAL E  2  85  ? -15.737 11.668  12.096  1.00 86.02  ?  85   VAL E O   1 
ATOM   11767 C CB  . VAL E  2  85  ? -15.676 8.645   10.973  1.00 82.91  ?  85   VAL E CB  1 
ATOM   11768 C CG1 . VAL E  2  85  ? -15.139 8.031   12.232  1.00 82.34  ?  85   VAL E CG1 1 
ATOM   11769 C CG2 . VAL E  2  85  ? -16.208 7.563   10.076  1.00 82.56  ?  85   VAL E CG2 1 
ATOM   11770 N N   . MET E  2  86  ? -16.695 10.308  13.627  1.00 94.93  ?  86   MET E N   1 
ATOM   11771 C CA  . MET E  2  86  ? -16.267 11.127  14.756  1.00 96.10  ?  86   MET E CA  1 
ATOM   11772 C C   . MET E  2  86  ? -14.749 11.194  14.887  1.00 94.69  ?  86   MET E C   1 
ATOM   11773 O O   . MET E  2  86  ? -14.231 12.130  15.508  1.00 95.77  ?  86   MET E O   1 
ATOM   11774 C CB  . MET E  2  86  ? -16.896 10.598  16.055  1.00 97.36  ?  86   MET E CB  1 
ATOM   11775 C CG  . MET E  2  86  ? -16.292 9.296   16.598  1.00 95.70  ?  86   MET E CG  1 
ATOM   11776 S SD  . MET E  2  86  ? -14.743 9.486   17.525  1.00 93.90  ?  86   MET E SD  1 
ATOM   11777 C CE  . MET E  2  86  ? -14.719 8.009   18.544  1.00 92.62  ?  86   MET E CE  1 
ATOM   11778 N N   . GLN E  2  87  ? -14.024 10.230  14.318  1.00 89.41  ?  87   GLN E N   1 
ATOM   11779 C CA  . GLN E  2  87  ? -12.572 10.180  14.448  1.00 86.95  ?  87   GLN E CA  1 
ATOM   11780 C C   . GLN E  2  87  ? -11.874 11.359  13.779  1.00 87.42  ?  87   GLN E C   1 
ATOM   11781 O O   . GLN E  2  87  ? -10.684 11.576  14.031  1.00 85.80  ?  87   GLN E O   1 
ATOM   11782 C CB  . GLN E  2  87  ? -12.042 8.867   13.867  1.00 83.05  ?  87   GLN E CB  1 
ATOM   11783 C CG  . GLN E  2  87  ? -11.868 7.751   14.888  1.00 81.67  ?  87   GLN E CG  1 
ATOM   11784 C CD  . GLN E  2  87  ? -13.114 6.901   15.057  1.00 83.55  ?  87   GLN E CD  1 
ATOM   11785 O OE1 . GLN E  2  87  ? -14.229 7.413   15.082  1.00 86.50  ?  87   GLN E OE1 1 
ATOM   11786 N NE2 . GLN E  2  87  ? -12.925 5.592   15.187  1.00 81.81  ?  87   GLN E NE2 1 
ATOM   11787 N N   . LEU E  2  88  ? -12.584 12.125  12.947  1.00 86.79  ?  88   LEU E N   1 
ATOM   11788 C CA  . LEU E  2  88  ? -12.013 13.286  12.274  1.00 87.30  ?  88   LEU E CA  1 
ATOM   11789 C C   . LEU E  2  88  ? -11.561 14.379  13.232  1.00 89.20  ?  88   LEU E C   1 
ATOM   11790 O O   . LEU E  2  88  ? -10.932 15.344  12.782  1.00 87.50  ?  88   LEU E O   1 
ATOM   11791 C CB  . LEU E  2  88  ? -13.032 13.867  11.300  1.00 85.51  ?  88   LEU E CB  1 
ATOM   11792 C CG  . LEU E  2  88  ? -13.340 13.011  10.089  1.00 82.33  ?  88   LEU E CG  1 
ATOM   11793 C CD1 . LEU E  2  88  ? -14.322 13.725  9.166   1.00 79.94  ?  88   LEU E CD1 1 
ATOM   11794 C CD2 . LEU E  2  88  ? -12.017 12.768  9.424   1.00 76.56  ?  88   LEU E CD2 1 
ATOM   11795 N N   . GLY E  2  89  ? -11.885 14.274  14.523  1.00 88.25  ?  89   GLY E N   1 
ATOM   11796 C CA  . GLY E  2  89  ? -11.375 15.186  15.525  1.00 89.75  ?  89   GLY E CA  1 
ATOM   11797 C C   . GLY E  2  89  ? -10.017 14.827  16.087  1.00 89.12  ?  89   GLY E C   1 
ATOM   11798 O O   . GLY E  2  89  ? -9.536  15.499  17.003  1.00 90.37  ?  89   GLY E O   1 
ATOM   11799 N N   . GLN E  2  90  ? -9.379  13.786  15.554  1.00 90.34  ?  90   GLN E N   1 
ATOM   11800 C CA  . GLN E  2  90  ? -8.066  13.341  16.000  1.00 87.48  ?  90   GLN E CA  1 
ATOM   11801 C C   . GLN E  2  90  ? -6.923  13.954  15.195  1.00 86.74  ?  90   GLN E C   1 
ATOM   11802 O O   . GLN E  2  90  ? -5.787  13.479  15.295  1.00 82.76  ?  90   GLN E O   1 
ATOM   11803 C CB  . GLN E  2  90  ? -7.978  11.814  15.934  1.00 82.23  ?  90   GLN E CB  1 
ATOM   11804 C CG  . GLN E  2  90  ? -8.323  11.117  17.233  1.00 82.53  ?  90   GLN E CG  1 
ATOM   11805 C CD  . GLN E  2  90  ? -9.809  10.853  17.367  1.00 84.86  ?  90   GLN E CD  1 
ATOM   11806 O OE1 . GLN E  2  90  ? -10.325 9.873   16.835  1.00 83.12  ?  90   GLN E OE1 1 
ATOM   11807 N NE2 . GLN E  2  90  ? -10.506 11.731  18.082  1.00 88.72  ?  90   GLN E NE2 1 
ATOM   11808 N N   . LEU E  2  91  ? -7.196  14.979  14.395  1.00 89.92  ?  91   LEU E N   1 
ATOM   11809 C CA  . LEU E  2  91  ? -6.150  15.636  13.627  1.00 86.32  ?  91   LEU E CA  1 
ATOM   11810 C C   . LEU E  2  91  ? -5.961  17.057  14.142  1.00 89.88  ?  91   LEU E C   1 
ATOM   11811 O O   . LEU E  2  91  ? -6.488  18.009  13.553  1.00 87.54  ?  91   LEU E O   1 
ATOM   11812 C CB  . LEU E  2  91  ? -6.496  15.613  12.138  1.00 79.51  ?  91   LEU E CB  1 
ATOM   11813 C CG  . LEU E  2  91  ? -7.019  14.243  11.685  1.00 75.76  ?  91   LEU E CG  1 
ATOM   11814 C CD1 . LEU E  2  91  ? -7.722  14.323  10.344  1.00 71.76  ?  91   LEU E CD1 1 
ATOM   11815 C CD2 . LEU E  2  91  ? -5.895  13.213  11.638  1.00 70.43  ?  91   LEU E CD2 1 
ATOM   11816 N N   . PRO E  2  92  ? -5.217  17.237  15.237  1.00 85.00  ?  92   PRO E N   1 
ATOM   11817 C CA  . PRO E  2  92  ? -5.150  18.565  15.870  1.00 85.66  ?  92   PRO E CA  1 
ATOM   11818 C C   . PRO E  2  92  ? -4.545  19.641  14.988  1.00 82.66  ?  92   PRO E C   1 
ATOM   11819 O O   . PRO E  2  92  ? -4.901  20.819  15.132  1.00 82.82  ?  92   PRO E O   1 
ATOM   11820 C CB  . PRO E  2  92  ? -4.294  18.311  17.119  1.00 87.21  ?  92   PRO E CB  1 
ATOM   11821 C CG  . PRO E  2  92  ? -3.489  17.106  16.788  1.00 85.86  ?  92   PRO E CG  1 
ATOM   11822 C CD  . PRO E  2  92  ? -4.364  16.252  15.923  1.00 84.85  ?  92   PRO E CD  1 
ATOM   11823 N N   . ASN E  2  93  ? -3.645  19.279  14.078  1.00 85.86  ?  93   ASN E N   1 
ATOM   11824 C CA  . ASN E  2  93  ? -2.991  20.243  13.208  1.00 82.43  ?  93   ASN E CA  1 
ATOM   11825 C C   . ASN E  2  93  ? -3.654  20.347  11.843  1.00 77.99  ?  93   ASN E C   1 
ATOM   11826 O O   . ASN E  2  93  ? -3.129  21.035  10.963  1.00 75.21  ?  93   ASN E O   1 
ATOM   11827 C CB  . ASN E  2  93  ? -1.515  19.890  13.054  1.00 81.06  ?  93   ASN E CB  1 
ATOM   11828 C CG  . ASN E  2  93  ? -0.710  20.245  14.284  1.00 84.69  ?  93   ASN E CG  1 
ATOM   11829 O OD1 . ASN E  2  93  ? -0.038  19.395  14.868  1.00 86.11  ?  93   ASN E OD1 1 
ATOM   11830 N ND2 . ASN E  2  93  ? -0.772  21.510  14.685  1.00 85.77  ?  93   ASN E ND2 1 
ATOM   11831 N N   . LEU E  2  94  ? -4.796  19.688  11.652  1.00 86.17  ?  94   LEU E N   1 
ATOM   11832 C CA  . LEU E  2  94  ? -5.510  19.736  10.383  1.00 81.86  ?  94   LEU E CA  1 
ATOM   11833 C C   . LEU E  2  94  ? -6.010  21.147  10.100  1.00 82.19  ?  94   LEU E C   1 
ATOM   11834 O O   . LEU E  2  94  ? -6.900  21.646  10.793  1.00 85.32  ?  94   LEU E O   1 
ATOM   11835 C CB  . LEU E  2  94  ? -6.683  18.754  10.399  1.00 82.17  ?  94   LEU E CB  1 
ATOM   11836 C CG  . LEU E  2  94  ? -7.514  18.634  9.123   1.00 78.02  ?  94   LEU E CG  1 
ATOM   11837 C CD1 . LEU E  2  94  ? -6.627  18.355  7.915   1.00 72.53  ?  94   LEU E CD1 1 
ATOM   11838 C CD2 . LEU E  2  94  ? -8.582  17.567  9.277   1.00 79.23  ?  94   LEU E CD2 1 
ATOM   11839 N N   . GLN E  2  95  ? -5.447  21.792  9.081   1.00 82.61  ?  95   GLN E N   1 
ATOM   11840 C CA  . GLN E  2  95  ? -5.811  23.158  8.725   1.00 82.99  ?  95   GLN E CA  1 
ATOM   11841 C C   . GLN E  2  95  ? -6.856  23.245  7.623   1.00 80.12  ?  95   GLN E C   1 
ATOM   11842 O O   . GLN E  2  95  ? -7.638  24.200  7.603   1.00 81.29  ?  95   GLN E O   1 
ATOM   11843 C CB  . GLN E  2  95  ? -4.564  23.936  8.296   1.00 82.40  ?  95   GLN E CB  1 
ATOM   11844 C CG  . GLN E  2  95  ? -3.503  24.029  9.375   1.00 85.57  ?  95   GLN E CG  1 
ATOM   11845 C CD  . GLN E  2  95  ? -2.285  24.799  8.921   1.00 85.34  ?  95   GLN E CD  1 
ATOM   11846 O OE1 . GLN E  2  95  ? -2.193  25.205  7.764   1.00 82.77  ?  95   GLN E OE1 1 
ATOM   11847 N NE2 . GLN E  2  95  ? -1.339  25.005  9.829   1.00 87.74  ?  95   GLN E NE2 1 
ATOM   11848 N N   . TYR E  2  96  ? -6.882  22.288  6.698   1.00 80.64  ?  96   TYR E N   1 
ATOM   11849 C CA  . TYR E  2  96  ? -7.821  22.299  5.582   1.00 78.07  ?  96   TYR E CA  1 
ATOM   11850 C C   . TYR E  2  96  ? -8.484  20.933  5.487   1.00 76.98  ?  96   TYR E C   1 
ATOM   11851 O O   . TYR E  2  96  ? -7.795  19.917  5.338   1.00 75.03  ?  96   TYR E O   1 
ATOM   11852 C CB  . TYR E  2  96  ? -7.107  22.645  4.269   1.00 75.24  ?  96   TYR E CB  1 
ATOM   11853 C CG  . TYR E  2  96  ? -6.520  24.038  4.236   1.00 77.07  ?  96   TYR E CG  1 
ATOM   11854 C CD1 . TYR E  2  96  ? -5.290  24.314  4.822   1.00 77.59  ?  96   TYR E CD1 1 
ATOM   11855 C CD2 . TYR E  2  96  ? -7.198  25.078  3.618   1.00 79.14  ?  96   TYR E CD2 1 
ATOM   11856 C CE1 . TYR E  2  96  ? -4.756  25.589  4.794   1.00 79.37  ?  96   TYR E CE1 1 
ATOM   11857 C CE2 . TYR E  2  96  ? -6.674  26.352  3.585   1.00 81.24  ?  96   TYR E CE2 1 
ATOM   11858 C CZ  . TYR E  2  96  ? -5.454  26.604  4.173   1.00 81.06  ?  96   TYR E CZ  1 
ATOM   11859 O OH  . TYR E  2  96  ? -4.940  27.881  4.135   1.00 83.44  ?  96   TYR E OH  1 
ATOM   11860 N N   . LEU E  2  97  ? -9.814  20.911  5.559   1.00 77.63  ?  97   LEU E N   1 
ATOM   11861 C CA  . LEU E  2  97  ? -10.607 19.687  5.432   1.00 77.43  ?  97   LEU E CA  1 
ATOM   11862 C C   . LEU E  2  97  ? -11.514 19.867  4.222   1.00 75.67  ?  97   LEU E C   1 
ATOM   11863 O O   . LEU E  2  97  ? -12.539 20.549  4.303   1.00 77.76  ?  97   LEU E O   1 
ATOM   11864 C CB  . LEU E  2  97  ? -11.411 19.402  6.702   1.00 82.00  ?  97   LEU E CB  1 
ATOM   11865 C CG  . LEU E  2  97  ? -12.040 18.010  6.848   1.00 83.08  ?  97   LEU E CG  1 
ATOM   11866 C CD1 . LEU E  2  97  ? -10.987 16.930  6.763   1.00 80.87  ?  97   LEU E CD1 1 
ATOM   11867 C CD2 . LEU E  2  97  ? -12.798 17.885  8.153   1.00 88.41  ?  97   LEU E CD2 1 
ATOM   11868 N N   . GLU E  2  98  ? -11.141 19.265  3.100   1.00 79.31  ?  98   GLU E N   1 
ATOM   11869 C CA  . GLU E  2  98  ? -11.827 19.481  1.830   1.00 80.31  ?  98   GLU E CA  1 
ATOM   11870 C C   . GLU E  2  98  ? -12.528 18.190  1.414   1.00 79.87  ?  98   GLU E C   1 
ATOM   11871 O O   . GLU E  2  98  ? -11.948 17.344  0.732   1.00 78.22  ?  98   GLU E O   1 
ATOM   11872 C CB  . GLU E  2  98  ? -10.839 19.946  0.771   1.00 79.63  ?  98   GLU E CB  1 
ATOM   11873 C CG  . GLU E  2  98  ? -9.904  21.053  1.242   1.00 79.89  ?  98   GLU E CG  1 
ATOM   11874 C CD  . GLU E  2  98  ? -10.573 22.419  1.302   1.00 82.81  ?  98   GLU E CD  1 
ATOM   11875 O OE1 . GLU E  2  98  ? -11.805 22.499  1.126   1.00 84.61  ?  98   GLU E OE1 1 
ATOM   11876 O OE2 . GLU E  2  98  ? -9.861  23.423  1.522   1.00 83.65  -1 98   GLU E OE2 1 
ATOM   11877 N N   . LEU E  2  99  ? -13.791 18.048  1.825   1.00 79.06  ?  99   LEU E N   1 
ATOM   11878 C CA  . LEU E  2  99  ? -14.629 16.924  1.422   1.00 79.45  ?  99   LEU E CA  1 
ATOM   11879 C C   . LEU E  2  99  ? -15.811 17.366  0.569   1.00 82.21  ?  99   LEU E C   1 
ATOM   11880 O O   . LEU E  2  99  ? -16.802 16.638  0.460   1.00 83.60  ?  99   LEU E O   1 
ATOM   11881 C CB  . LEU E  2  99  ? -15.123 16.157  2.648   1.00 81.57  ?  99   LEU E CB  1 
ATOM   11882 C CG  . LEU E  2  99  ? -14.139 15.165  3.260   1.00 81.21  ?  99   LEU E CG  1 
ATOM   11883 C CD1 . LEU E  2  99  ? -13.416 15.810  4.413   1.00 82.18  ?  99   LEU E CD1 1 
ATOM   11884 C CD2 . LEU E  2  99  ? -14.863 13.922  3.719   1.00 84.51  ?  99   LEU E CD2 1 
ATOM   11885 N N   . TYR E  2  100 ? -15.717 18.540  -0.046  1.00 84.88  ?  100  TYR E N   1 
ATOM   11886 C CA  . TYR E  2  100 ? -16.819 19.111  -0.803  1.00 88.05  ?  100  TYR E CA  1 
ATOM   11887 C C   . TYR E  2  100 ? -17.088 18.314  -2.079  1.00 88.54  ?  100  TYR E C   1 
ATOM   11888 O O   . TYR E  2  100 ? -16.251 17.538  -2.550  1.00 86.46  ?  100  TYR E O   1 
ATOM   11889 C CB  . TYR E  2  100 ? -16.524 20.571  -1.147  1.00 89.43  ?  100  TYR E CB  1 
ATOM   11890 C CG  . TYR E  2  100 ? -15.262 20.804  -1.968  1.00 87.86  ?  100  TYR E CG  1 
ATOM   11891 C CD1 . TYR E  2  100 ? -15.281 20.717  -3.356  1.00 89.48  ?  100  TYR E CD1 1 
ATOM   11892 C CD2 . TYR E  2  100 ? -14.059 21.134  -1.353  1.00 85.32  ?  100  TYR E CD2 1 
ATOM   11893 C CE1 . TYR E  2  100 ? -14.137 20.938  -4.108  1.00 88.68  ?  100  TYR E CE1 1 
ATOM   11894 C CE2 . TYR E  2  100 ? -12.907 21.355  -2.098  1.00 84.37  ?  100  TYR E CE2 1 
ATOM   11895 C CZ  . TYR E  2  100 ? -12.952 21.256  -3.475  1.00 86.10  ?  100  TYR E CZ  1 
ATOM   11896 O OH  . TYR E  2  100 ? -11.814 21.473  -4.225  1.00 85.79  ?  100  TYR E OH  1 
ATOM   11897 N N   . SER E  2  101 ? -18.290 18.510  -2.627  1.00 88.26  ?  101  SER E N   1 
ATOM   11898 C CA  . SER E  2  101 ? -18.703 17.928  -3.906  1.00 90.65  ?  101  SER E CA  1 
ATOM   11899 C C   . SER E  2  101 ? -18.587 16.401  -3.894  1.00 88.10  ?  101  SER E C   1 
ATOM   11900 O O   . SER E  2  101 ? -17.844 15.791  -4.665  1.00 86.29  ?  101  SER E O   1 
ATOM   11901 C CB  . SER E  2  101 ? -17.914 18.540  -5.066  1.00 91.21  ?  101  SER E CB  1 
ATOM   11902 O OG  . SER E  2  101 ? -18.216 19.917  -5.209  1.00 94.94  ?  101  SER E OG  1 
ATOM   11903 N N   . ASN E  2  102 ? -19.350 15.789  -2.993  1.00 95.37  ?  102  ASN E N   1 
ATOM   11904 C CA  . ASN E  2  102 ? -19.446 14.341  -2.890  1.00 94.53  ?  102  ASN E CA  1 
ATOM   11905 C C   . ASN E  2  102 ? -20.888 13.980  -2.546  1.00 98.19  ?  102  ASN E C   1 
ATOM   11906 O O   . ASN E  2  102 ? -21.769 14.844  -2.466  1.00 102.16 ?  102  ASN E O   1 
ATOM   11907 C CB  . ASN E  2  102 ? -18.465 13.787  -1.847  1.00 91.00  ?  102  ASN E CB  1 
ATOM   11908 C CG  . ASN E  2  102 ? -17.034 13.715  -2.360  1.00 88.19  ?  102  ASN E CG  1 
ATOM   11909 O OD1 . ASN E  2  102 ? -16.715 12.924  -3.251  1.00 87.98  ?  102  ASN E OD1 1 
ATOM   11910 N ND2 . ASN E  2  102 ? -16.162 14.539  -1.791  1.00 86.43  ?  102  ASN E ND2 1 
ATOM   11911 N N   . ASN E  2  103 ? -21.133 12.688  -2.349  1.00 95.22  ?  103  ASN E N   1 
ATOM   11912 C CA  . ASN E  2  103 ? -22.452 12.181  -1.989  1.00 99.68  ?  103  ASN E CA  1 
ATOM   11913 C C   . ASN E  2  103 ? -22.462 11.659  -0.557  1.00 98.07  ?  103  ASN E C   1 
ATOM   11914 O O   . ASN E  2  103 ? -23.110 10.657  -0.246  1.00 100.52 ?  103  ASN E O   1 
ATOM   11915 C CB  . ASN E  2  103 ? -22.904 11.094  -2.960  1.00 102.41 ?  103  ASN E CB  1 
ATOM   11916 C CG  . ASN E  2  103 ? -24.389 10.802  -2.857  1.00 108.52 ?  103  ASN E CG  1 
ATOM   11917 O OD1 . ASN E  2  103 ? -25.199 11.713  -2.691  1.00 112.12 ?  103  ASN E OD1 1 
ATOM   11918 N ND2 . ASN E  2  103 ? -24.752 9.528   -2.946  1.00 110.21 ?  103  ASN E ND2 1 
ATOM   11919 N N   . ILE E  2  104 ? -21.741 12.334  0.330   1.00 100.01 ?  104  ILE E N   1 
ATOM   11920 C CA  . ILE E  2  104 ? -21.629 11.881  1.709   1.00 101.34 ?  104  ILE E CA  1 
ATOM   11921 C C   . ILE E  2  104 ? -22.894 12.264  2.463   1.00 104.59 ?  104  ILE E C   1 
ATOM   11922 O O   . ILE E  2  104 ? -23.425 13.372  2.304   1.00 105.72 ?  104  ILE E O   1 
ATOM   11923 C CB  . ILE E  2  104 ? -20.376 12.475  2.373   1.00 99.65  ?  104  ILE E CB  1 
ATOM   11924 C CG1 . ILE E  2  104 ? -19.221 12.521  1.370   1.00 95.92  ?  104  ILE E CG1 1 
ATOM   11925 C CG2 . ILE E  2  104 ? -19.984 11.650  3.578   1.00 101.87 ?  104  ILE E CG2 1 
ATOM   11926 C CD1 . ILE E  2  104 ? -17.983 13.224  1.888   1.00 93.82  ?  104  ILE E CD1 1 
ATOM   11927 N N   . THR E  2  105 ? -23.382 11.347  3.290   1.00 100.17 ?  105  THR E N   1 
ATOM   11928 C CA  . THR E  2  105 ? -24.646 11.510  3.998   1.00 104.34 ?  105  THR E CA  1 
ATOM   11929 C C   . THR E  2  105 ? -24.412 11.439  5.510   1.00 105.49 ?  105  THR E C   1 
ATOM   11930 O O   . THR E  2  105 ? -23.283 11.257  5.976   1.00 103.78 ?  105  THR E O   1 
ATOM   11931 C CB  . THR E  2  105 ? -25.658 10.458  3.529   1.00 107.81 ?  105  THR E CB  1 
ATOM   11932 O OG1 . THR E  2  105 ? -26.906 10.657  4.202   1.00 113.37 ?  105  THR E OG1 1 
ATOM   11933 C CG2 . THR E  2  105 ? -25.153 9.054   3.796   1.00 107.64 ?  105  THR E CG2 1 
ATOM   11934 N N   . GLY E  2  106 ? -25.491 11.579  6.287   1.00 107.75 ?  106  GLY E N   1 
ATOM   11935 C CA  . GLY E  2  106 ? -25.384 11.592  7.740   1.00 109.25 ?  106  GLY E CA  1 
ATOM   11936 C C   . GLY E  2  106 ? -25.210 12.979  8.314   1.00 108.96 ?  106  GLY E C   1 
ATOM   11937 O O   . GLY E  2  106 ? -25.535 13.998  7.711   1.00 108.68 ?  106  GLY E O   1 
ATOM   11938 N N   . THR E  2  107 ? -24.726 12.991  9.550   1.00 106.53 ?  107  THR E N   1 
ATOM   11939 C CA  . THR E  2  107 ? -24.535 14.192  10.358  1.00 107.05 ?  107  THR E CA  1 
ATOM   11940 C C   . THR E  2  107 ? -23.077 14.590  10.465  1.00 105.11 ?  107  THR E C   1 
ATOM   11941 O O   . THR E  2  107 ? -22.134 13.851  10.084  1.00 103.63 ?  107  THR E O   1 
ATOM   11942 C CB  . THR E  2  107 ? -25.158 14.003  11.760  1.00 110.93 ?  107  THR E CB  1 
ATOM   11943 O OG1 . THR E  2  107 ? -25.332 15.279  12.411  1.00 113.16 ?  107  THR E OG1 1 
ATOM   11944 C CG2 . THR E  2  107 ? -24.289 13.102  12.614  1.00 110.27 ?  107  THR E CG2 1 
ATOM   11945 N N   . ILE E  2  108 ? -22.928 15.818  10.958  1.00 104.44 ?  108  ILE E N   1 
ATOM   11946 C CA  . ILE E  2  108 ? -21.607 16.468  11.099  1.00 103.17 ?  108  ILE E CA  1 
ATOM   11947 C C   . ILE E  2  108 ? -21.178 16.268  12.553  1.00 105.62 ?  108  ILE E C   1 
ATOM   11948 O O   . ILE E  2  108 ? -21.941 16.604  13.456  1.00 108.00 ?  108  ILE E O   1 
ATOM   11949 C CB  . ILE E  2  108 ? -21.779 17.996  10.744  1.00 102.36 ?  108  ILE E CB  1 
ATOM   11950 C CG1 . ILE E  2  108 ? -21.788 18.290  9.239   1.00 99.06  ?  108  ILE E CG1 1 
ATOM   11951 C CG2 . ILE E  2  108 ? -20.640 18.900  11.352  1.00 102.34 ?  108  ILE E CG2 1 
ATOM   11952 C CD1 . ILE E  2  108 ? -22.752 17.424  8.428   1.00 98.90  ?  108  ILE E CD1 1 
ATOM   11953 N N   . PRO E  2  109 ? -20.009 15.657  12.796  1.00 99.82  ?  109  PRO E N   1 
ATOM   11954 C CA  . PRO E  2  109 ? -19.566 15.376  14.155  1.00 101.87 ?  109  PRO E CA  1 
ATOM   11955 C C   . PRO E  2  109 ? -19.402 16.610  15.027  1.00 103.42 ?  109  PRO E C   1 
ATOM   11956 O O   . PRO E  2  109 ? -18.597 17.519  14.763  1.00 102.48 ?  109  PRO E O   1 
ATOM   11957 C CB  . PRO E  2  109 ? -18.221 14.720  13.896  1.00 100.45 ?  109  PRO E CB  1 
ATOM   11958 C CG  . PRO E  2  109 ? -17.961 14.853  12.276  1.00 97.53  ?  109  PRO E CG  1 
ATOM   11959 C CD  . PRO E  2  109 ? -18.841 15.846  11.914  1.00 97.16  ?  109  PRO E CD  1 
ATOM   11960 N N   . GLU E  2  110 ? -20.119 16.592  16.171  1.00 104.87 ?  110  GLU E N   1 
ATOM   11961 C CA  . GLU E  2  110 ? -19.767 17.661  17.127  1.00 106.49 ?  110  GLU E CA  1 
ATOM   11962 C C   . GLU E  2  110 ? -18.329 17.524  17.591  1.00 106.11 ?  110  GLU E C   1 
ATOM   11963 O O   . GLU E  2  110 ? -17.784 18.497  18.099  1.00 106.92 ?  110  GLU E O   1 
ATOM   11964 C CB  . GLU E  2  110 ? -20.736 17.666  18.301  1.00 112.57 ?  110  GLU E CB  1 
ATOM   11965 C CG  . GLU E  2  110 ? -20.617 16.569  19.220  1.00 114.08 ?  110  GLU E CG  1 
ATOM   11966 C CD  . GLU E  2  110 ? -21.534 16.743  20.357  1.00 121.95 ?  110  GLU E CD  1 
ATOM   11967 O OE1 . GLU E  2  110 ? -22.553 17.432  20.169  1.00 126.01 ?  110  GLU E OE1 1 
ATOM   11968 O OE2 . GLU E  2  110 ? -21.241 16.190  21.431  1.00 124.53 -1 110  GLU E OE2 1 
ATOM   11969 N N   . GLN E  2  111 ? -17.666 16.387  17.300  1.00 103.31 ?  111  GLN E N   1 
ATOM   11970 C CA  . GLN E  2  111 ? -16.239 16.215  17.568  1.00 102.68 ?  111  GLN E CA  1 
ATOM   11971 C C   . GLN E  2  111 ? -15.341 16.974  16.608  1.00 101.15 ?  111  GLN E C   1 
ATOM   11972 O O   . GLN E  2  111 ? -14.151 17.095  16.898  1.00 101.05 ?  111  GLN E O   1 
ATOM   11973 C CB  . GLN E  2  111 ? -15.888 14.733  17.534  1.00 101.52 ?  111  GLN E CB  1 
ATOM   11974 C CG  . GLN E  2  111 ? -16.293 13.979  18.780  1.00 102.46 ?  111  GLN E CG  1 
ATOM   11975 C CD  . GLN E  2  111 ? -16.337 14.855  20.020  1.00 104.61 ?  111  GLN E CD  1 
ATOM   11976 O OE1 . GLN E  2  111 ? -17.390 15.018  20.639  1.00 106.84 ?  111  GLN E OE1 1 
ATOM   11977 N NE2 . GLN E  2  111 ? -15.186 15.395  20.410  1.00 104.24 ?  111  GLN E NE2 1 
ATOM   11978 N N   . LEU E  2  112 ? -15.861 17.468  15.476  1.00 98.18  ?  112  LEU E N   1 
ATOM   11979 C CA  . LEU E  2  112 ? -15.065 18.349  14.621  1.00 94.95  ?  112  LEU E CA  1 
ATOM   11980 C C   . LEU E  2  112 ? -14.695 19.648  15.314  1.00 97.81  ?  112  LEU E C   1 
ATOM   11981 O O   . LEU E  2  112 ? -13.829 20.376  14.816  1.00 95.61  ?  112  LEU E O   1 
ATOM   11982 C CB  . LEU E  2  112 ? -15.794 18.643  13.304  1.00 94.33  ?  112  LEU E CB  1 
ATOM   11983 C CG  . LEU E  2  112 ? -15.125 18.073  12.054  1.00 89.05  ?  112  LEU E CG  1 
ATOM   11984 C CD1 . LEU E  2  112 ? -14.665 16.685  12.343  1.00 86.52  ?  112  LEU E CD1 1 
ATOM   11985 C CD2 . LEU E  2  112 ? -16.045 18.087  10.834  1.00 89.48  ?  112  LEU E CD2 1 
ATOM   11986 N N   . GLY E  2  113 ? -15.351 19.971  16.428  1.00 101.45 ?  113  GLY E N   1 
ATOM   11987 C CA  . GLY E  2  113 ? -14.981 21.127  17.218  1.00 102.98 ?  113  GLY E CA  1 
ATOM   11988 C C   . GLY E  2  113 ? -13.634 21.015  17.897  1.00 103.52 ?  113  GLY E C   1 
ATOM   11989 O O   . GLY E  2  113 ? -13.175 21.999  18.488  1.00 104.65 ?  113  GLY E O   1 
ATOM   11990 N N   . ASN E  2  114 ? -12.998 19.847  17.834  1.00 104.46 ?  114  ASN E N   1 
ATOM   11991 C CA  . ASN E  2  114 ? -11.695 19.641  18.447  1.00 104.79 ?  114  ASN E CA  1 
ATOM   11992 C C   . ASN E  2  114 ? -10.533 19.932  17.504  1.00 102.82 ?  114  ASN E C   1 
ATOM   11993 O O   . ASN E  2  114 ? -9.380  19.890  17.944  1.00 103.06 ?  114  ASN E O   1 
ATOM   11994 C CB  . ASN E  2  114 ? -11.575 18.202  18.967  1.00 104.85 ?  114  ASN E CB  1 
ATOM   11995 C CG  . ASN E  2  114 ? -12.448 17.936  20.184  1.00 106.52 ?  114  ASN E CG  1 
ATOM   11996 O OD1 . ASN E  2  114 ? -12.240 16.956  20.902  1.00 105.96 ?  114  ASN E OD1 1 
ATOM   11997 N ND2 . ASN E  2  114 ? -13.431 18.799  20.418  1.00 108.34 ?  114  ASN E ND2 1 
ATOM   11998 N N   . LEU E  2  115 ? -10.803 20.224  16.228  1.00 97.63  ?  115  LEU E N   1 
ATOM   11999 C CA  . LEU E  2  115 ? -9.761  20.575  15.259  1.00 95.67  ?  115  LEU E CA  1 
ATOM   12000 C C   . LEU E  2  115 ? -9.342  22.020  15.519  1.00 94.67  ?  115  LEU E C   1 
ATOM   12001 O O   . LEU E  2  115 ? -9.820  22.968  14.891  1.00 93.14  ?  115  LEU E O   1 
ATOM   12002 C CB  . LEU E  2  115 ? -10.255 20.371  13.832  1.00 93.58  ?  115  LEU E CB  1 
ATOM   12003 C CG  . LEU E  2  115 ? -10.711 18.949  13.499  1.00 93.60  ?  115  LEU E CG  1 
ATOM   12004 C CD1 . LEU E  2  115 ? -11.136 18.828  12.044  1.00 90.92  ?  115  LEU E CD1 1 
ATOM   12005 C CD2 . LEU E  2  115 ? -9.607  17.971  13.818  1.00 93.11  ?  115  LEU E CD2 1 
ATOM   12006 N N   . THR E  2  116 ? -8.434  22.181  16.486  1.00 98.54  ?  116  THR E N   1 
ATOM   12007 C CA  . THR E  2  116 ? -8.092  23.512  16.985  1.00 98.08  ?  116  THR E CA  1 
ATOM   12008 C C   . THR E  2  116 ? -7.463  24.380  15.899  1.00 95.75  ?  116  THR E C   1 
ATOM   12009 O O   . THR E  2  116 ? -7.711  25.591  15.843  1.00 95.28  ?  116  THR E O   1 
ATOM   12010 C CB  . THR E  2  116 ? -7.157  23.390  18.193  1.00 99.40  ?  116  THR E CB  1 
ATOM   12011 O OG1 . THR E  2  116 ? -7.859  22.784  19.288  1.00 101.61 ?  116  THR E OG1 1 
ATOM   12012 C CG2 . THR E  2  116 ? -6.645  24.757  18.631  1.00 98.99  ?  116  THR E CG2 1 
ATOM   12013 N N   . GLU E  2  117 ? -6.669  23.779  15.011  1.00 96.82  ?  117  GLU E N   1 
ATOM   12014 C CA  . GLU E  2  117 ? -5.953  24.523  13.982  1.00 95.35  ?  117  GLU E CA  1 
ATOM   12015 C C   . GLU E  2  117 ? -6.714  24.610  12.664  1.00 94.26  ?  117  GLU E C   1 
ATOM   12016 O O   . GLU E  2  117 ? -6.153  25.090  11.674  1.00 93.65  ?  117  GLU E O   1 
ATOM   12017 C CB  . GLU E  2  117 ? -4.575  23.900  13.742  1.00 94.82  ?  117  GLU E CB  1 
ATOM   12018 C CG  . GLU E  2  117 ? -3.443  24.917  13.689  1.00 94.65  ?  117  GLU E CG  1 
ATOM   12019 C CD  . GLU E  2  117 ? -3.194  25.584  15.033  1.00 95.40  ?  117  GLU E CD  1 
ATOM   12020 O OE1 . GLU E  2  117 ? -3.841  25.186  16.027  1.00 96.02  ?  117  GLU E OE1 1 
ATOM   12021 O OE2 . GLU E  2  117 ? -2.353  26.508  15.098  1.00 95.63  -1 117  GLU E OE2 1 
ATOM   12022 N N   . LEU E  2  118 ? -7.974  24.181  12.638  1.00 92.11  ?  118  LEU E N   1 
ATOM   12023 C CA  . LEU E  2  118 ? -8.742  24.154  11.399  1.00 90.88  ?  118  LEU E CA  1 
ATOM   12024 C C   . LEU E  2  118 ? -8.964  25.565  10.868  1.00 90.28  ?  118  LEU E C   1 
ATOM   12025 O O   . LEU E  2  118 ? -9.365  26.465  11.610  1.00 90.83  ?  118  LEU E O   1 
ATOM   12026 C CB  . LEU E  2  118 ? -10.081 23.451  11.633  1.00 91.41  ?  118  LEU E CB  1 
ATOM   12027 C CG  . LEU E  2  118 ? -10.917 23.108  10.399  1.00 90.29  ?  118  LEU E CG  1 
ATOM   12028 C CD1 . LEU E  2  118 ? -10.084 22.343  9.380   1.00 89.41  ?  118  LEU E CD1 1 
ATOM   12029 C CD2 . LEU E  2  118 ? -12.144 22.303  10.795  1.00 91.41  ?  118  LEU E CD2 1 
ATOM   12030 N N   . VAL E  2  119 ? -8.691  25.758  9.579   1.00 89.61  ?  119  VAL E N   1 
ATOM   12031 C CA  . VAL E  2  119 ? -8.802  27.058  8.925   1.00 89.48  ?  119  VAL E CA  1 
ATOM   12032 C C   . VAL E  2  119 ? -9.928  27.068  7.891   1.00 88.91  ?  119  VAL E C   1 
ATOM   12033 O O   . VAL E  2  119 ? -10.734 27.998  7.847   1.00 88.96  ?  119  VAL E O   1 
ATOM   12034 C CB  . VAL E  2  119 ? -7.453  27.466  8.285   1.00 89.93  ?  119  VAL E CB  1 
ATOM   12035 C CG1 . VAL E  2  119 ? -7.648  28.523  7.202   1.00 90.03  ?  119  VAL E CG1 1 
ATOM   12036 C CG2 . VAL E  2  119 ? -6.487  27.966  9.353   1.00 90.91  ?  119  VAL E CG2 1 
ATOM   12037 N N   . SER E  2  120 ? -10.005 26.029  7.062   1.00 89.56  ?  120  SER E N   1 
ATOM   12038 C CA  . SER E  2  120 ? -11.030 25.899  6.034   1.00 89.24  ?  120  SER E CA  1 
ATOM   12039 C C   . SER E  2  120 ? -11.818 24.620  6.268   1.00 88.83  ?  120  SER E C   1 
ATOM   12040 O O   . SER E  2  120 ? -11.230 23.556  6.492   1.00 88.78  ?  120  SER E O   1 
ATOM   12041 C CB  . SER E  2  120 ? -10.411 25.891  4.634   1.00 89.63  ?  120  SER E CB  1 
ATOM   12042 O OG  . SER E  2  120 ? -11.397 25.713  3.631   1.00 89.21  ?  120  SER E OG  1 
ATOM   12043 N N   . LEU E  2  121 ? -13.145 24.724  6.209   1.00 86.67  ?  121  LEU E N   1 
ATOM   12044 C CA  . LEU E  2  121 ? -14.044 23.588  6.413   1.00 86.58  ?  121  LEU E CA  1 
ATOM   12045 C C   . LEU E  2  121 ? -15.054 23.580  5.267   1.00 86.81  ?  121  LEU E C   1 
ATOM   12046 O O   . LEU E  2  121 ? -16.032 24.332  5.291   1.00 88.28  ?  121  LEU E O   1 
ATOM   12047 C CB  . LEU E  2  121 ? -14.721 23.679  7.776   1.00 87.95  ?  121  LEU E CB  1 
ATOM   12048 C CG  . LEU E  2  121 ? -15.426 22.433  8.306   1.00 88.96  ?  121  LEU E CG  1 
ATOM   12049 C CD1 . LEU E  2  121 ? -16.879 22.366  7.829   1.00 90.07  ?  121  LEU E CD1 1 
ATOM   12050 C CD2 . LEU E  2  121 ? -14.640 21.192  7.899   1.00 87.97  ?  121  LEU E CD2 1 
ATOM   12051 N N   . ASP E  2  122 ? -14.815 22.739  4.261   1.00 90.28  ?  122  ASP E N   1 
ATOM   12052 C CA  . ASP E  2  122 ? -15.616 22.716  3.037   1.00 90.41  ?  122  ASP E CA  1 
ATOM   12053 C C   . ASP E  2  122 ? -16.352 21.384  2.947   1.00 91.25  ?  122  ASP E C   1 
ATOM   12054 O O   . ASP E  2  122 ? -15.799 20.389  2.469   1.00 90.61  ?  122  ASP E O   1 
ATOM   12055 C CB  . ASP E  2  122 ? -14.740 22.928  1.805   1.00 89.49  ?  122  ASP E CB  1 
ATOM   12056 C CG  . ASP E  2  122 ? -14.194 24.338  1.708   1.00 89.67  ?  122  ASP E CG  1 
ATOM   12057 O OD1 . ASP E  2  122 ? -14.350 25.105  2.679   1.00 90.14  ?  122  ASP E OD1 1 
ATOM   12058 O OD2 . ASP E  2  122 ? -13.590 24.673  0.666   1.00 89.64  -1 122  ASP E OD2 1 
ATOM   12059 N N   . LEU E  2  123 ? -17.611 21.379  3.392   1.00 91.01  ?  123  LEU E N   1 
ATOM   12060 C CA  . LEU E  2  123 ? -18.516 20.245  3.233   1.00 93.12  ?  123  LEU E CA  1 
ATOM   12061 C C   . LEU E  2  123 ? -19.616 20.532  2.219   1.00 94.30  ?  123  LEU E C   1 
ATOM   12062 O O   . LEU E  2  123 ? -20.599 19.788  2.145   1.00 96.30  ?  123  LEU E O   1 
ATOM   12063 C CB  . LEU E  2  123 ? -19.137 19.838  4.572   1.00 94.49  ?  123  LEU E CB  1 
ATOM   12064 C CG  . LEU E  2  123 ? -18.345 19.023  5.601   1.00 94.17  ?  123  LEU E CG  1 
ATOM   12065 C CD1 . LEU E  2  123 ? -16.897 19.460  5.685   1.00 92.39  ?  123  LEU E CD1 1 
ATOM   12066 C CD2 . LEU E  2  123 ? -19.005 19.117  6.975   1.00 94.59  ?  123  LEU E CD2 1 
ATOM   12067 N N   . TYR E  2  124 ? -19.449 21.580  1.417   1.00 97.87  ?  124  TYR E N   1 
ATOM   12068 C CA  . TYR E  2  124 ? -20.483 22.035  0.503   1.00 99.28  ?  124  TYR E CA  1 
ATOM   12069 C C   . TYR E  2  124 ? -20.745 21.008  -0.605  1.00 100.40 ?  124  TYR E C   1 
ATOM   12070 O O   . TYR E  2  124 ? -19.919 20.138  -0.895  1.00 99.51  ?  124  TYR E O   1 
ATOM   12071 C CB  . TYR E  2  124 ? -20.094 23.407  -0.067  1.00 98.03  ?  124  TYR E CB  1 
ATOM   12072 C CG  . TYR E  2  124 ? -18.883 23.478  -1.004  1.00 96.21  ?  124  TYR E CG  1 
ATOM   12073 C CD1 . TYR E  2  124 ? -18.866 22.811  -2.218  1.00 96.95  ?  124  TYR E CD1 1 
ATOM   12074 C CD2 . TYR E  2  124 ? -17.770 24.259  -0.682  1.00 94.09  ?  124  TYR E CD2 1 
ATOM   12075 C CE1 . TYR E  2  124 ? -17.788 22.898  -3.082  1.00 95.54  ?  124  TYR E CE1 1 
ATOM   12076 C CE2 . TYR E  2  124 ? -16.675 24.352  -1.539  1.00 92.86  ?  124  TYR E CE2 1 
ATOM   12077 C CZ  . TYR E  2  124 ? -16.692 23.662  -2.743  1.00 93.51  ?  124  TYR E CZ  1 
ATOM   12078 O OH  . TYR E  2  124 ? -15.638 23.714  -3.634  1.00 92.62  ?  124  TYR E OH  1 
ATOM   12079 N N   . LEU E  2  125 ? -21.926 21.118  -1.219  1.00 97.97  ?  125  LEU E N   1 
ATOM   12080 C CA  . LEU E  2  125 ? -22.355 20.220  -2.296  1.00 99.94  ?  125  LEU E CA  1 
ATOM   12081 C C   . LEU E  2  125 ? -22.285 18.751  -1.860  1.00 100.13 ?  125  LEU E C   1 
ATOM   12082 O O   . LEU E  2  125 ? -21.560 17.933  -2.429  1.00 99.45  ?  125  LEU E O   1 
ATOM   12083 C CB  . LEU E  2  125 ? -21.565 20.463  -3.595  1.00 99.49  ?  125  LEU E CB  1 
ATOM   12084 C CG  . LEU E  2  125 ? -21.902 21.722  -4.420  1.00 101.21 ?  125  LEU E CG  1 
ATOM   12085 C CD1 . LEU E  2  125 ? -20.718 22.626  -4.743  1.00 98.89  ?  125  LEU E CD1 1 
ATOM   12086 C CD2 . LEU E  2  125 ? -22.619 21.332  -5.707  1.00 104.83 ?  125  LEU E CD2 1 
ATOM   12087 N N   . ASN E  2  126 ? -23.074 18.429  -0.835  1.00 103.24 ?  126  ASN E N   1 
ATOM   12088 C CA  . ASN E  2  126 ? -23.155 17.076  -0.291  1.00 104.05 ?  126  ASN E CA  1 
ATOM   12089 C C   . ASN E  2  126 ? -24.613 16.774  0.050   1.00 106.74 ?  126  ASN E C   1 
ATOM   12090 O O   . ASN E  2  126 ? -25.524 17.543  -0.276  1.00 108.22 ?  126  ASN E O   1 
ATOM   12091 C CB  . ASN E  2  126 ? -22.253 16.927  0.942   1.00 102.48 ?  126  ASN E CB  1 
ATOM   12092 C CG  . ASN E  2  126 ? -20.805 16.686  0.581   1.00 100.48 ?  126  ASN E CG  1 
ATOM   12093 O OD1 . ASN E  2  126 ? -20.455 15.641  0.032   1.00 100.65 ?  126  ASN E OD1 1 
ATOM   12094 N ND2 . ASN E  2  126 ? -19.951 17.656  0.887   1.00 98.55  ?  126  ASN E ND2 1 
ATOM   12095 N N   . ASN E  2  127 ? -24.833 15.639  0.719   1.00 107.96 ?  127  ASN E N   1 
ATOM   12096 C CA  . ASN E  2  127 ? -26.158 15.224  1.170   1.00 110.54 ?  127  ASN E CA  1 
ATOM   12097 C C   . ASN E  2  127 ? -26.197 15.042  2.683   1.00 110.18 ?  127  ASN E C   1 
ATOM   12098 O O   . ASN E  2  127 ? -26.921 14.187  3.200   1.00 111.77 ?  127  ASN E O   1 
ATOM   12099 C CB  . ASN E  2  127 ? -26.598 13.941  0.467   1.00 112.53 ?  127  ASN E CB  1 
ATOM   12100 C CG  . ASN E  2  127 ? -28.106 13.806  0.399   1.00 116.61 ?  127  ASN E CG  1 
ATOM   12101 O OD1 . ASN E  2  127 ? -28.662 12.758  0.725   1.00 118.40 ?  127  ASN E OD1 1 
ATOM   12102 N ND2 . ASN E  2  127 ? -28.777 14.872  -0.021  1.00 118.34 ?  127  ASN E ND2 1 
ATOM   12103 N N   . LEU E  2  128 ? -25.418 15.844  3.400   1.00 113.89 ?  128  LEU E N   1 
ATOM   12104 C CA  . LEU E  2  128 ? -25.389 15.785  4.851   1.00 113.37 ?  128  LEU E CA  1 
ATOM   12105 C C   . LEU E  2  128 ? -26.708 16.292  5.433   1.00 115.36 ?  128  LEU E C   1 
ATOM   12106 O O   . LEU E  2  128 ? -27.434 17.070  4.809   1.00 116.71 ?  128  LEU E O   1 
ATOM   12107 C CB  . LEU E  2  128 ? -24.211 16.600  5.379   1.00 110.86 ?  128  LEU E CB  1 
ATOM   12108 C CG  . LEU E  2  128 ? -22.840 16.158  4.858   1.00 109.16 ?  128  LEU E CG  1 
ATOM   12109 C CD1 . LEU E  2  128 ? -21.819 17.281  4.970   1.00 107.23 ?  128  LEU E CD1 1 
ATOM   12110 C CD2 . LEU E  2  128 ? -22.354 14.912  5.594   1.00 108.68 ?  128  LEU E CD2 1 
ATOM   12111 N N   . SER E  2  129 ? -27.019 15.835  6.644   1.00 115.19 ?  129  SER E N   1 
ATOM   12112 C CA  . SER E  2  129 ? -28.282 16.168  7.289   1.00 117.57 ?  129  SER E CA  1 
ATOM   12113 C C   . SER E  2  129 ? -28.041 16.457  8.766   1.00 116.47 ?  129  SER E C   1 
ATOM   12114 O O   . SER E  2  129 ? -26.904 16.460  9.249   1.00 113.74 ?  129  SER E O   1 
ATOM   12115 C CB  . SER E  2  129 ? -29.308 15.043  7.111   1.00 120.73 ?  129  SER E CB  1 
ATOM   12116 O OG  . SER E  2  129 ? -28.987 13.926  7.923   1.00 120.01 ?  129  SER E OG  1 
ATOM   12117 N N   . GLY E  2  130 ? -29.133 16.709  9.486   1.00 120.77 ?  130  GLY E N   1 
ATOM   12118 C CA  . GLY E  2  130 ? -29.070 17.007  10.896  1.00 120.33 ?  130  GLY E CA  1 
ATOM   12119 C C   . GLY E  2  130 ? -28.805 18.476  11.158  1.00 119.32 ?  130  GLY E C   1 
ATOM   12120 O O   . GLY E  2  130 ? -28.974 19.327  10.278  1.00 119.65 ?  130  GLY E O   1 
ATOM   12121 N N   . PRO E  2  131 ? -28.377 18.802  12.384  1.00 118.31 ?  131  PRO E N   1 
ATOM   12122 C CA  . PRO E  2  131 ? -28.095 20.204  12.717  1.00 117.99 ?  131  PRO E CA  1 
ATOM   12123 C C   . PRO E  2  131 ? -26.692 20.637  12.316  1.00 111.88 ?  131  PRO E C   1 
ATOM   12124 O O   . PRO E  2  131 ? -25.929 19.861  11.730  1.00 110.15 ?  131  PRO E O   1 
ATOM   12125 C CB  . PRO E  2  131 ? -28.272 20.238  14.240  1.00 121.86 ?  131  PRO E CB  1 
ATOM   12126 C CG  . PRO E  2  131 ? -28.004 18.814  14.698  1.00 121.22 ?  131  PRO E CG  1 
ATOM   12127 C CD  . PRO E  2  131 ? -28.037 17.896  13.495  1.00 118.67 ?  131  PRO E CD  1 
ATOM   12128 N N   . ILE E  2  132 ? -26.360 21.891  12.607  1.00 116.66 ?  132  ILE E N   1 
ATOM   12129 C CA  . ILE E  2  132 ? -24.987 22.384  12.525  1.00 113.75 ?  132  ILE E CA  1 
ATOM   12130 C C   . ILE E  2  132 ? -24.477 22.416  13.961  1.00 113.18 ?  132  ILE E C   1 
ATOM   12131 O O   . ILE E  2  132 ? -24.873 23.308  14.727  1.00 114.36 ?  132  ILE E O   1 
ATOM   12132 C CB  . ILE E  2  132 ? -24.893 23.771  11.862  1.00 113.35 ?  132  ILE E CB  1 
ATOM   12133 C CG1 . ILE E  2  132 ? -25.150 23.727  10.348  1.00 113.76 ?  132  ILE E CG1 1 
ATOM   12134 C CG2 . ILE E  2  132 ? -23.536 24.401  12.124  1.00 111.11 ?  132  ILE E CG2 1 
ATOM   12135 C CD1 . ILE E  2  132 ? -26.521 23.259  9.932   1.00 116.59 ?  132  ILE E CD1 1 
ATOM   12136 N N   . PRO E  2  133 ? -23.676 21.437  14.385  1.00 111.03 ?  133  PRO E N   1 
ATOM   12137 C CA  . PRO E  2  133 ? -23.252 21.356  15.792  1.00 110.71 ?  133  PRO E CA  1 
ATOM   12138 C C   . PRO E  2  133 ? -22.793 22.699  16.346  1.00 110.37 ?  133  PRO E C   1 
ATOM   12139 O O   . PRO E  2  133 ? -22.147 23.488  15.658  1.00 109.38 ?  133  PRO E O   1 
ATOM   12140 C CB  . PRO E  2  133 ? -22.112 20.332  15.757  1.00 109.15 ?  133  PRO E CB  1 
ATOM   12141 C CG  . PRO E  2  133 ? -22.316 19.543  14.478  1.00 109.26 ?  133  PRO E CG  1 
ATOM   12142 C CD  . PRO E  2  133 ? -23.407 20.184  13.663  1.00 110.68 ?  133  PRO E CD  1 
ATOM   12143 N N   . SER E  2  134 ? -23.221 23.012  17.568  1.00 115.09 ?  134  SER E N   1 
ATOM   12144 C CA  . SER E  2  134 ? -22.765 24.260  18.169  1.00 114.94 ?  134  SER E CA  1 
ATOM   12145 C C   . SER E  2  134 ? -21.274 24.242  18.487  1.00 113.54 ?  134  SER E C   1 
ATOM   12146 O O   . SER E  2  134 ? -20.694 25.307  18.725  1.00 113.27 ?  134  SER E O   1 
ATOM   12147 C CB  . SER E  2  134 ? -23.566 24.565  19.430  1.00 117.26 ?  134  SER E CB  1 
ATOM   12148 O OG  . SER E  2  134 ? -23.305 23.591  20.422  1.00 118.77 ?  134  SER E OG  1 
ATOM   12149 N N   . THR E  2  135 ? -20.643 23.064  18.500  1.00 110.54 ?  135  THR E N   1 
ATOM   12150 C CA  . THR E  2  135 ? -19.219 22.966  18.794  1.00 109.67 ?  135  THR E CA  1 
ATOM   12151 C C   . THR E  2  135 ? -18.334 23.532  17.690  1.00 108.62 ?  135  THR E C   1 
ATOM   12152 O O   . THR E  2  135 ? -17.131 23.701  17.924  1.00 108.26 ?  135  THR E O   1 
ATOM   12153 C CB  . THR E  2  135 ? -18.827 21.513  19.051  1.00 109.29 ?  135  THR E CB  1 
ATOM   12154 O OG1 . THR E  2  135 ? -19.457 20.677  18.073  1.00 109.05 ?  135  THR E OG1 1 
ATOM   12155 C CG2 . THR E  2  135 ? -19.269 21.086  20.447  1.00 110.12 ?  135  THR E CG2 1 
ATOM   12156 N N   . LEU E  2  136 ? -18.882 23.830  16.505  1.00 107.95 ?  136  LEU E N   1 
ATOM   12157 C CA  . LEU E  2  136 ? -18.062 24.415  15.446  1.00 105.21 ?  136  LEU E CA  1 
ATOM   12158 C C   . LEU E  2  136 ? -17.540 25.795  15.820  1.00 105.43 ?  136  LEU E C   1 
ATOM   12159 O O   . LEU E  2  136 ? -16.610 26.285  15.173  1.00 103.58 ?  136  LEU E O   1 
ATOM   12160 C CB  . LEU E  2  136 ? -18.817 24.478  14.106  1.00 104.83 ?  136  LEU E CB  1 
ATOM   12161 C CG  . LEU E  2  136 ? -19.046 23.183  13.305  1.00 104.63 ?  136  LEU E CG  1 
ATOM   12162 C CD1 . LEU E  2  136 ? -20.337 22.473  13.619  1.00 106.25 ?  136  LEU E CD1 1 
ATOM   12163 C CD2 . LEU E  2  136 ? -18.991 23.469  11.816  1.00 104.23 ?  136  LEU E CD2 1 
ATOM   12164 N N   . GLY E  2  137 ? -18.114 26.432  16.839  1.00 105.13 ?  137  GLY E N   1 
ATOM   12165 C CA  . GLY E  2  137 ? -17.591 27.695  17.324  1.00 107.15 ?  137  GLY E CA  1 
ATOM   12166 C C   . GLY E  2  137 ? -16.270 27.592  18.062  1.00 106.29 ?  137  GLY E C   1 
ATOM   12167 O O   . GLY E  2  137 ? -15.666 28.631  18.352  1.00 107.79 ?  137  GLY E O   1 
ATOM   12168 N N   . ARG E  2  138 ? -15.805 26.377  18.366  1.00 110.83 ?  138  ARG E N   1 
ATOM   12169 C CA  . ARG E  2  138 ? -14.508 26.211  19.011  1.00 110.83 ?  138  ARG E CA  1 
ATOM   12170 C C   . ARG E  2  138 ? -13.341 26.427  18.056  1.00 109.28 ?  138  ARG E C   1 
ATOM   12171 O O   . ARG E  2  138 ? -12.206 26.593  18.516  1.00 109.00 ?  138  ARG E O   1 
ATOM   12172 C CB  . ARG E  2  138 ? -14.395 24.816  19.630  1.00 111.82 ?  138  ARG E CB  1 
ATOM   12173 C CG  . ARG E  2  138 ? -15.472 24.484  20.642  1.00 112.93 ?  138  ARG E CG  1 
ATOM   12174 C CD  . ARG E  2  138 ? -14.897 23.665  21.786  1.00 113.75 ?  138  ARG E CD  1 
ATOM   12175 N NE  . ARG E  2  138 ? -15.816 22.629  22.244  1.00 113.83 ?  138  ARG E NE  1 
ATOM   12176 C CZ  . ARG E  2  138 ? -15.483 21.356  22.414  1.00 113.33 ?  138  ARG E CZ  1 
ATOM   12177 N NH1 . ARG E  2  138 ? -14.258 20.923  22.156  1.00 113.01 ?  138  ARG E NH1 1 
ATOM   12178 N NH2 . ARG E  2  138 ? -16.400 20.498  22.855  1.00 113.12 ?  138  ARG E NH2 1 
ATOM   12179 N N   . LEU E  2  139 ? -13.589 26.424  16.745  1.00 108.04 ?  139  LEU E N   1 
ATOM   12180 C CA  . LEU E  2  139 ? -12.533 26.599  15.746  1.00 106.40 ?  139  LEU E CA  1 
ATOM   12181 C C   . LEU E  2  139 ? -12.239 28.093  15.620  1.00 105.52 ?  139  LEU E C   1 
ATOM   12182 O O   . LEU E  2  139 ? -12.756 28.798  14.748  1.00 104.92 ?  139  LEU E O   1 
ATOM   12183 C CB  . LEU E  2  139 ? -12.947 25.981  14.414  1.00 105.79 ?  139  LEU E CB  1 
ATOM   12184 C CG  . LEU E  2  139 ? -13.873 24.760  14.481  1.00 107.18 ?  139  LEU E CG  1 
ATOM   12185 C CD1 . LEU E  2  139 ? -14.297 24.299  13.094  1.00 106.62 ?  139  LEU E CD1 1 
ATOM   12186 C CD2 . LEU E  2  139 ? -13.213 23.618  15.234  1.00 108.24 ?  139  LEU E CD2 1 
ATOM   12187 N N   . LYS E  2  140 ? -11.400 28.589  16.536  1.00 107.26 ?  140  LYS E N   1 
ATOM   12188 C CA  . LYS E  2  140 ? -11.070 30.010  16.562  1.00 106.96 ?  140  LYS E CA  1 
ATOM   12189 C C   . LYS E  2  140 ? -10.216 30.440  15.376  1.00 105.84 ?  140  LYS E C   1 
ATOM   12190 O O   . LYS E  2  140 ? -10.188 31.631  15.048  1.00 105.93 ?  140  LYS E O   1 
ATOM   12191 C CB  . LYS E  2  140 ? -10.351 30.356  17.867  1.00 107.77 ?  140  LYS E CB  1 
ATOM   12192 C CG  . LYS E  2  140 ? -11.155 30.043  19.118  1.00 109.26 ?  140  LYS E CG  1 
ATOM   12193 C CD  . LYS E  2  140 ? -12.586 30.543  18.998  1.00 109.82 ?  140  LYS E CD  1 
ATOM   12194 C CE  . LYS E  2  140 ? -13.413 30.184  20.228  1.00 111.54 ?  140  LYS E CE  1 
ATOM   12195 N NZ  . LYS E  2  140 ? -12.987 30.932  21.446  1.00 113.35 ?  140  LYS E NZ  1 
ATOM   12196 N N   . LYS E  2  141 ? -9.516  29.513  14.731  1.00 100.62 ?  141  LYS E N   1 
ATOM   12197 C CA  . LYS E  2  141 ? -8.712  29.839  13.562  1.00 100.01 ?  141  LYS E CA  1 
ATOM   12198 C C   . LYS E  2  141 ? -9.494  29.727  12.259  1.00 99.54  ?  141  LYS E C   1 
ATOM   12199 O O   . LYS E  2  141 ? -8.919  29.956  11.188  1.00 99.40  ?  141  LYS E O   1 
ATOM   12200 C CB  . LYS E  2  141 ? -7.473  28.937  13.505  1.00 99.73  ?  141  LYS E CB  1 
ATOM   12201 C CG  . LYS E  2  141 ? -6.477  29.155  14.640  1.00 100.19 ?  141  LYS E CG  1 
ATOM   12202 C CD  . LYS E  2  141 ? -5.403  30.164  14.259  1.00 100.78 ?  141  LYS E CD  1 
ATOM   12203 C CE  . LYS E  2  141 ? -4.556  29.667  13.094  1.00 100.67 ?  141  LYS E CE  1 
ATOM   12204 N NZ  . LYS E  2  141 ? -3.091  29.728  13.373  1.00 101.02 ?  141  LYS E NZ  1 
ATOM   12205 N N   . LEU E  2  142 ? -10.780 29.381  12.325  1.00 96.53  ?  142  LEU E N   1 
ATOM   12206 C CA  . LEU E  2  142 ? -11.560 29.129  11.121  1.00 95.44  ?  142  LEU E CA  1 
ATOM   12207 C C   . LEU E  2  142 ? -11.793 30.420  10.345  1.00 96.34  ?  142  LEU E C   1 
ATOM   12208 O O   . LEU E  2  142 ? -12.266 31.416  10.899  1.00 98.71  ?  142  LEU E O   1 
ATOM   12209 C CB  . LEU E  2  142 ? -12.895 28.482  11.482  1.00 95.72  ?  142  LEU E CB  1 
ATOM   12210 C CG  . LEU E  2  142 ? -13.762 28.022  10.310  1.00 95.04  ?  142  LEU E CG  1 
ATOM   12211 C CD1 . LEU E  2  142 ? -13.332 26.644  9.845   1.00 93.55  ?  142  LEU E CD1 1 
ATOM   12212 C CD2 . LEU E  2  142 ? -15.223 28.014  10.699  1.00 96.50  ?  142  LEU E CD2 1 
ATOM   12213 N N   . ARG E  2  143 ? -11.450 30.400  9.059   1.00 98.16  ?  143  ARG E N   1 
ATOM   12214 C CA  . ARG E  2  143 ? -11.659 31.524  8.153   1.00 98.83  ?  143  ARG E CA  1 
ATOM   12215 C C   . ARG E  2  143 ? -12.784 31.293  7.159   1.00 99.18  ?  143  ARG E C   1 
ATOM   12216 O O   . ARG E  2  143 ? -13.583 32.200  6.914   1.00 99.80  ?  143  ARG E O   1 
ATOM   12217 C CB  . ARG E  2  143 ? -10.370 31.830  7.379   1.00 99.34  ?  143  ARG E CB  1 
ATOM   12218 C CG  . ARG E  2  143 ? -9.491  32.908  7.996   1.00 99.82  ?  143  ARG E CG  1 
ATOM   12219 C CD  . ARG E  2  143 ? -8.424  33.382  7.017   1.00 100.87 ?  143  ARG E CD  1 
ATOM   12220 N NE  . ARG E  2  143 ? -7.370  32.390  6.853   1.00 100.60 ?  143  ARG E NE  1 
ATOM   12221 C CZ  . ARG E  2  143 ? -6.524  32.352  5.831   1.00 101.47 ?  143  ARG E CZ  1 
ATOM   12222 N NH1 . ARG E  2  143 ? -6.574  33.251  4.860   1.00 102.82 ?  143  ARG E NH1 1 
ATOM   12223 N NH2 . ARG E  2  143 ? -5.609  31.385  5.780   1.00 101.12 ?  143  ARG E NH2 1 
ATOM   12224 N N   . PHE E  2  144 ? -12.861 30.099  6.576   1.00 94.92  ?  144  PHE E N   1 
ATOM   12225 C CA  . PHE E  2  144 ? -13.816 29.782  5.524   1.00 95.37  ?  144  PHE E CA  1 
ATOM   12226 C C   . PHE E  2  144 ? -14.694 28.622  5.966   1.00 95.21  ?  144  PHE E C   1 
ATOM   12227 O O   . PHE E  2  144 ? -14.183 27.577  6.381   1.00 94.81  ?  144  PHE E O   1 
ATOM   12228 C CB  . PHE E  2  144 ? -13.101 29.416  4.217   1.00 95.73  ?  144  PHE E CB  1 
ATOM   12229 C CG  . PHE E  2  144 ? -11.875 30.243  3.930   1.00 96.42  ?  144  PHE E CG  1 
ATOM   12230 C CD1 . PHE E  2  144 ? -10.645 29.908  4.474   1.00 95.68  ?  144  PHE E CD1 1 
ATOM   12231 C CD2 . PHE E  2  144 ? -11.956 31.356  3.112   1.00 98.01  ?  144  PHE E CD2 1 
ATOM   12232 C CE1 . PHE E  2  144 ? -9.526  30.670  4.207   1.00 96.61  ?  144  PHE E CE1 1 
ATOM   12233 C CE2 . PHE E  2  144 ? -10.843 32.119  2.840   1.00 99.00  ?  144  PHE E CE2 1 
ATOM   12234 C CZ  . PHE E  2  144 ? -9.626  31.779  3.387   1.00 98.35  ?  144  PHE E CZ  1 
ATOM   12235 N N   . LEU E  2  145 ? -16.011 28.799  5.856   1.00 96.90  ?  145  LEU E N   1 
ATOM   12236 C CA  . LEU E  2  145 ? -16.972 27.744  6.173   1.00 97.53  ?  145  LEU E CA  1 
ATOM   12237 C C   . LEU E  2  145 ? -18.020 27.705  5.069   1.00 98.63  ?  145  LEU E C   1 
ATOM   12238 O O   . LEU E  2  145 ? -18.852 28.612  4.970   1.00 99.61  ?  145  LEU E O   1 
ATOM   12239 C CB  . LEU E  2  145 ? -17.626 27.972  7.538   1.00 98.19  ?  145  LEU E CB  1 
ATOM   12240 C CG  . LEU E  2  145 ? -18.488 26.821  8.058   1.00 99.36  ?  145  LEU E CG  1 
ATOM   12241 C CD1 . LEU E  2  145 ? -18.250 26.594  9.530   1.00 99.42  ?  145  LEU E CD1 1 
ATOM   12242 C CD2 . LEU E  2  145 ? -19.947 27.102  7.813   1.00 101.09 ?  145  LEU E CD2 1 
ATOM   12243 N N   . ARG E  2  146 ? -17.986 26.656  4.247   1.00 96.60  ?  146  ARG E N   1 
ATOM   12244 C CA  . ARG E  2  146 ? -18.931 26.479  3.147   1.00 97.84  ?  146  ARG E CA  1 
ATOM   12245 C C   . ARG E  2  146 ? -19.711 25.191  3.372   1.00 99.15  ?  146  ARG E C   1 
ATOM   12246 O O   . ARG E  2  146 ? -19.153 24.094  3.256   1.00 98.74  ?  146  ARG E O   1 
ATOM   12247 C CB  . ARG E  2  146 ? -18.212 26.435  1.803   1.00 97.07  ?  146  ARG E CB  1 
ATOM   12248 C CG  . ARG E  2  146 ? -17.588 27.736  1.362   1.00 96.63  ?  146  ARG E CG  1 
ATOM   12249 C CD  . ARG E  2  146 ? -16.217 27.472  0.783   1.00 95.52  ?  146  ARG E CD  1 
ATOM   12250 N NE  . ARG E  2  146 ? -15.395 28.673  0.745   1.00 95.58  ?  146  ARG E NE  1 
ATOM   12251 C CZ  . ARG E  2  146 ? -14.098 28.702  1.020   1.00 95.22  ?  146  ARG E CZ  1 
ATOM   12252 N NH1 . ARG E  2  146 ? -13.445 27.613  1.393   1.00 94.47  ?  146  ARG E NH1 1 
ATOM   12253 N NH2 . ARG E  2  146 ? -13.439 29.850  0.914   1.00 96.02  ?  146  ARG E NH2 1 
ATOM   12254 N N   . LEU E  2  147 ? -21.005 25.326  3.672   1.00 110.52 ?  147  LEU E N   1 
ATOM   12255 C CA  . LEU E  2  147 ? -21.893 24.186  3.877   1.00 110.93 ?  147  LEU E CA  1 
ATOM   12256 C C   . LEU E  2  147 ? -23.083 24.223  2.923   1.00 114.61 ?  147  LEU E C   1 
ATOM   12257 O O   . LEU E  2  147 ? -24.081 23.533  3.155   1.00 116.48 ?  147  LEU E O   1 
ATOM   12258 C CB  . LEU E  2  147 ? -22.387 24.122  5.327   1.00 112.00 ?  147  LEU E CB  1 
ATOM   12259 C CG  . LEU E  2  147 ? -21.456 24.244  6.546   1.00 110.00 ?  147  LEU E CG  1 
ATOM   12260 C CD1 . LEU E  2  147 ? -22.068 23.550  7.756   1.00 111.31 ?  147  LEU E CD1 1 
ATOM   12261 C CD2 . LEU E  2  147 ? -20.050 23.703  6.304   1.00 105.87 ?  147  LEU E CD2 1 
ATOM   12262 N N   . ASN E  2  148 ? -22.995 25.006  1.849   1.00 116.27 ?  148  ASN E N   1 
ATOM   12263 C CA  . ASN E  2  148 ? -24.136 25.222  0.974   1.00 120.77 ?  148  ASN E CA  1 
ATOM   12264 C C   . ASN E  2  148 ? -24.461 23.960  0.171   1.00 120.62 ?  148  ASN E C   1 
ATOM   12265 O O   . ASN E  2  148 ? -23.682 23.005  0.109   1.00 116.86 ?  148  ASN E O   1 
ATOM   12266 C CB  . ASN E  2  148 ? -23.878 26.407  0.039   1.00 123.22 ?  148  ASN E CB  1 
ATOM   12267 C CG  . ASN E  2  148 ? -22.589 26.266  -0.753  1.00 120.34 ?  148  ASN E CG  1 
ATOM   12268 O OD1 . ASN E  2  148 ? -22.360 25.258  -1.421  1.00 118.73 ?  148  ASN E OD1 1 
ATOM   12269 N ND2 . ASN E  2  148 ? -21.738 27.283  -0.682  1.00 120.08 ?  148  ASN E ND2 1 
ATOM   12270 N N   . ASN E  2  149 ? -25.643 23.974  -0.445  1.00 125.26 ?  149  ASN E N   1 
ATOM   12271 C CA  . ASN E  2  149 ? -26.165 22.853  -1.227  1.00 126.50 ?  149  ASN E CA  1 
ATOM   12272 C C   . ASN E  2  149 ? -26.097 21.549  -0.427  1.00 123.56 ?  149  ASN E C   1 
ATOM   12273 O O   . ASN E  2  149 ? -25.428 20.583  -0.799  1.00 120.59 ?  149  ASN E O   1 
ATOM   12274 C CB  . ASN E  2  149 ? -25.430 22.735  -2.566  1.00 125.88 ?  149  ASN E CB  1 
ATOM   12275 C CG  . ASN E  2  149 ? -26.263 23.241  -3.733  1.00 131.75 ?  149  ASN E CG  1 
ATOM   12276 O OD1 . ASN E  2  149 ? -26.912 22.463  -4.432  1.00 134.38 ?  149  ASN E OD1 1 
ATOM   12277 N ND2 . ASN E  2  149 ? -26.258 24.554  -3.937  1.00 134.37 ?  149  ASN E ND2 1 
ATOM   12278 N N   . ASN E  2  150 ? -26.809 21.546  0.701   1.00 124.92 ?  150  ASN E N   1 
ATOM   12279 C CA  . ASN E  2  150 ? -26.872 20.395  1.591   1.00 123.35 ?  150  ASN E CA  1 
ATOM   12280 C C   . ASN E  2  150 ? -28.301 20.233  2.090   1.00 128.33 ?  150  ASN E C   1 
ATOM   12281 O O   . ASN E  2  150 ? -29.194 21.013  1.747   1.00 132.70 ?  150  ASN E O   1 
ATOM   12282 C CB  . ASN E  2  150 ? -25.896 20.548  2.762   1.00 119.37 ?  150  ASN E CB  1 
ATOM   12283 C CG  . ASN E  2  150 ? -24.595 19.814  2.530   1.00 114.48 ?  150  ASN E CG  1 
ATOM   12284 O OD1 . ASN E  2  150 ? -24.500 18.607  2.749   1.00 113.27 ?  150  ASN E OD1 1 
ATOM   12285 N ND2 . ASN E  2  150 ? -23.585 20.541  2.068   1.00 112.08 ?  150  ASN E ND2 1 
ATOM   12286 N N   . SER E  2  151 ? -28.517 19.200  2.906   1.00 128.17 ?  151  SER E N   1 
ATOM   12287 C CA  . SER E  2  151 ? -29.805 18.945  3.540   1.00 133.12 ?  151  SER E CA  1 
ATOM   12288 C C   . SER E  2  151 ? -29.772 19.268  5.033   1.00 133.01 ?  151  SER E C   1 
ATOM   12289 O O   . SER E  2  151 ? -30.476 18.641  5.830   1.00 135.95 ?  151  SER E O   1 
ATOM   12290 C CB  . SER E  2  151 ? -30.234 17.497  3.311   1.00 134.58 ?  151  SER E CB  1 
ATOM   12291 O OG  . SER E  2  151 ? -31.589 17.304  3.673   1.00 140.50 ?  151  SER E OG  1 
ATOM   12292 N N   . LEU E  2  152 ? -28.951 20.243  5.418   1.00 130.16 ?  152  LEU E N   1 
ATOM   12293 C CA  . LEU E  2  152 ? -28.809 20.622  6.819   1.00 130.21 ?  152  LEU E CA  1 
ATOM   12294 C C   . LEU E  2  152 ? -30.065 21.340  7.308   1.00 135.75 ?  152  LEU E C   1 
ATOM   12295 O O   . LEU E  2  152 ? -30.657 22.146  6.585   1.00 138.36 ?  152  LEU E O   1 
ATOM   12296 C CB  . LEU E  2  152 ? -27.579 21.517  6.989   1.00 126.18 ?  152  LEU E CB  1 
ATOM   12297 C CG  . LEU E  2  152 ? -26.204 20.883  7.246   1.00 121.10 ?  152  LEU E CG  1 
ATOM   12298 C CD1 . LEU E  2  152 ? -26.015 19.583  6.487   1.00 119.36 ?  152  LEU E CD1 1 
ATOM   12299 C CD2 . LEU E  2  152 ? -25.104 21.860  6.874   1.00 117.96 ?  152  LEU E CD2 1 
ATOM   12300 N N   . SER E  2  153 ? -30.470 21.050  8.546   1.00 138.04 ?  153  SER E N   1 
ATOM   12301 C CA  . SER E  2  153 ? -31.703 21.599  9.101   1.00 143.83 ?  153  SER E CA  1 
ATOM   12302 C C   . SER E  2  153 ? -31.517 21.958  10.570  1.00 144.62 ?  153  SER E C   1 
ATOM   12303 O O   . SER E  2  153 ? -30.934 21.184  11.336  1.00 142.96 ?  153  SER E O   1 
ATOM   12304 C CB  . SER E  2  153 ? -32.873 20.616  8.946   1.00 148.56 ?  153  SER E CB  1 
ATOM   12305 O OG  . SER E  2  153 ? -32.653 19.429  9.687   1.00 148.17 ?  153  SER E OG  1 
ATOM   12306 N N   . GLY E  2  154 ? -32.012 23.127  10.955  1.00 147.61 ?  154  GLY E N   1 
ATOM   12307 C CA  . GLY E  2  154 ? -31.905 23.617  12.322  1.00 149.15 ?  154  GLY E CA  1 
ATOM   12308 C C   . GLY E  2  154 ? -31.874 25.141  12.352  1.00 149.95 ?  154  GLY E C   1 
ATOM   12309 O O   . GLY E  2  154 ? -32.550 25.799  11.565  1.00 152.26 ?  154  GLY E O   1 
ATOM   12310 N N   . GLU E  2  155 ? -31.093 25.672  13.296  1.00 148.57 ?  155  GLU E N   1 
ATOM   12311 C CA  . GLU E  2  155 ? -30.856 27.103  13.445  1.00 149.10 ?  155  GLU E CA  1 
ATOM   12312 C C   . GLU E  2  155 ? -29.357 27.350  13.566  1.00 144.03 ?  155  GLU E C   1 
ATOM   12313 O O   . GLU E  2  155 ? -28.611 26.471  14.005  1.00 141.30 ?  155  GLU E O   1 
ATOM   12314 C CB  . GLU E  2  155 ? -31.592 27.660  14.675  1.00 154.42 ?  155  GLU E CB  1 
ATOM   12315 C CG  . GLU E  2  155 ? -31.639 29.181  14.770  1.00 156.34 ?  155  GLU E CG  1 
ATOM   12316 C CD  . GLU E  2  155 ? -32.753 29.671  15.684  1.00 162.80 ?  155  GLU E CD  1 
ATOM   12317 O OE1 . GLU E  2  155 ? -32.904 29.113  16.791  1.00 164.97 ?  155  GLU E OE1 1 
ATOM   12318 O OE2 . GLU E  2  155 ? -33.479 30.612  15.299  1.00 166.16 -1 155  GLU E OE2 1 
ATOM   12319 N N   . ILE E  2  156 ? -28.911 28.540  13.163  1.00 143.25 ?  156  ILE E N   1 
ATOM   12320 C CA  . ILE E  2  156 ? -27.479 28.857  13.182  1.00 138.98 ?  156  ILE E CA  1 
ATOM   12321 C C   . ILE E  2  156 ? -26.999 28.964  14.627  1.00 139.92 ?  156  ILE E C   1 
ATOM   12322 O O   . ILE E  2  156 ? -27.575 29.733  15.415  1.00 144.12 ?  156  ILE E O   1 
ATOM   12323 C CB  . ILE E  2  156 ? -27.153 30.162  12.428  1.00 138.92 ?  156  ILE E CB  1 
ATOM   12324 C CG1 . ILE E  2  156 ? -27.183 29.991  10.913  1.00 137.20 ?  156  ILE E CG1 1 
ATOM   12325 C CG2 . ILE E  2  156 ? -25.791 30.707  12.822  1.00 136.29 ?  156  ILE E CG2 1 
ATOM   12326 C CD1 . ILE E  2  156 ? -28.492 30.327  10.331  1.00 141.56 ?  156  ILE E CD1 1 
ATOM   12327 N N   . PRO E  2  157 ? -25.973 28.207  15.025  1.00 136.65 ?  157  PRO E N   1 
ATOM   12328 C CA  . PRO E  2  157 ? -25.407 28.382  16.369  1.00 138.03 ?  157  PRO E CA  1 
ATOM   12329 C C   . PRO E  2  157 ? -24.845 29.785  16.557  1.00 138.74 ?  157  PRO E C   1 
ATOM   12330 O O   . PRO E  2  157 ? -24.195 30.340  15.667  1.00 136.06 ?  157  PRO E O   1 
ATOM   12331 C CB  . PRO E  2  157 ? -24.297 27.325  16.444  1.00 134.04 ?  157  PRO E CB  1 
ATOM   12332 C CG  . PRO E  2  157 ? -24.392 26.506  15.206  1.00 130.72 ?  157  PRO E CG  1 
ATOM   12333 C CD  . PRO E  2  157 ? -25.549 26.951  14.385  1.00 132.79 ?  157  PRO E CD  1 
ATOM   12334 N N   . ARG E  2  158 ? -25.090 30.351  17.742  1.00 129.72 ?  158  ARG E N   1 
ATOM   12335 C CA  . ARG E  2  158 ? -24.531 31.655  18.082  1.00 129.36 ?  158  ARG E CA  1 
ATOM   12336 C C   . ARG E  2  158 ? -23.011 31.630  18.180  1.00 125.33 ?  158  ARG E C   1 
ATOM   12337 O O   . ARG E  2  158 ? -22.380 32.689  18.073  1.00 123.79 ?  158  ARG E O   1 
ATOM   12338 C CB  . ARG E  2  158 ? -25.121 32.155  19.400  1.00 135.89 ?  158  ARG E CB  1 
ATOM   12339 C CG  . ARG E  2  158 ? -24.372 31.671  20.635  1.00 138.18 ?  158  ARG E CG  1 
ATOM   12340 C CD  . ARG E  2  158 ? -23.536 32.775  21.268  1.00 138.53 ?  158  ARG E CD  1 
ATOM   12341 N NE  . ARG E  2  158 ? -22.603 32.248  22.256  1.00 139.91 ?  158  ARG E NE  1 
ATOM   12342 C CZ  . ARG E  2  158 ? -21.531 32.894  22.693  1.00 139.25 ?  158  ARG E CZ  1 
ATOM   12343 N NH1 . ARG E  2  158 ? -21.220 34.100  22.245  1.00 137.24 ?  158  ARG E NH1 1 
ATOM   12344 N NH2 . ARG E  2  158 ? -20.754 32.318  23.607  1.00 141.25 ?  158  ARG E NH2 1 
ATOM   12345 N N   . SER E  2  159 ? -22.412 30.451  18.383  1.00 124.66 ?  159  SER E N   1 
ATOM   12346 C CA  . SER E  2  159 ? -20.966 30.374  18.565  1.00 121.83 ?  159  SER E CA  1 
ATOM   12347 C C   . SER E  2  159 ? -20.217 30.845  17.326  1.00 120.26 ?  159  SER E C   1 
ATOM   12348 O O   . SER E  2  159 ? -19.126 31.414  17.443  1.00 118.04 ?  159  SER E O   1 
ATOM   12349 C CB  . SER E  2  159 ? -20.559 28.943  18.927  1.00 121.27 ?  159  SER E CB  1 
ATOM   12350 O OG  . SER E  2  159 ? -21.040 28.010  17.974  1.00 122.27 ?  159  SER E OG  1 
ATOM   12351 N N   . LEU E  2  160 ? -20.797 30.645  16.140  1.00 123.05 ?  160  LEU E N   1 
ATOM   12352 C CA  . LEU E  2  160 ? -20.161 31.061  14.895  1.00 121.63 ?  160  LEU E CA  1 
ATOM   12353 C C   . LEU E  2  160 ? -19.978 32.569  14.802  1.00 120.33 ?  160  LEU E C   1 
ATOM   12354 O O   . LEU E  2  160 ? -19.234 33.031  13.927  1.00 118.31 ?  160  LEU E O   1 
ATOM   12355 C CB  . LEU E  2  160 ? -20.967 30.560  13.693  1.00 123.66 ?  160  LEU E CB  1 
ATOM   12356 C CG  . LEU E  2  160 ? -21.143 29.043  13.567  1.00 125.10 ?  160  LEU E CG  1 
ATOM   12357 C CD1 . LEU E  2  160 ? -22.071 28.698  12.413  1.00 127.81 ?  160  LEU E CD1 1 
ATOM   12358 C CD2 . LEU E  2  160 ? -19.799 28.356  13.393  1.00 122.56 ?  160  LEU E CD2 1 
ATOM   12359 N N   . THR E  2  161 ? -20.651 33.344  15.656  1.00 119.75 ?  161  THR E N   1 
ATOM   12360 C CA  . THR E  2  161 ? -20.497 34.793  15.657  1.00 118.60 ?  161  THR E CA  1 
ATOM   12361 C C   . THR E  2  161 ? -19.307 35.269  16.484  1.00 116.72 ?  161  THR E C   1 
ATOM   12362 O O   . THR E  2  161 ? -18.925 36.439  16.368  1.00 116.61 ?  161  THR E O   1 
ATOM   12363 C CB  . THR E  2  161 ? -21.776 35.466  16.172  1.00 121.00 ?  161  THR E CB  1 
ATOM   12364 O OG1 . THR E  2  161 ? -22.168 34.874  17.416  1.00 123.39 ?  161  THR E OG1 1 
ATOM   12365 C CG2 . THR E  2  161 ? -22.910 35.309  15.168  1.00 123.00 ?  161  THR E CG2 1 
ATOM   12366 N N   . ALA E  2  162 ? -18.707 34.405  17.303  1.00 114.67 ?  162  ALA E N   1 
ATOM   12367 C CA  . ALA E  2  162 ? -17.601 34.795  18.169  1.00 115.90 ?  162  ALA E CA  1 
ATOM   12368 C C   . ALA E  2  162 ? -16.236 34.391  17.626  1.00 111.57 ?  162  ALA E C   1 
ATOM   12369 O O   . ALA E  2  162 ? -15.218 34.717  18.246  1.00 112.60 ?  162  ALA E O   1 
ATOM   12370 C CB  . ALA E  2  162 ? -17.793 34.199  19.567  1.00 120.29 ?  162  ALA E CB  1 
ATOM   12371 N N   . VAL E  2  163 ? -16.189 33.698  16.486  1.00 116.01 ?  163  VAL E N   1 
ATOM   12372 C CA  . VAL E  2  163 ? -14.926 33.176  15.968  1.00 113.57 ?  163  VAL E CA  1 
ATOM   12373 C C   . VAL E  2  163 ? -13.965 34.312  15.633  1.00 110.80 ?  163  VAL E C   1 
ATOM   12374 O O   . VAL E  2  163 ? -12.747 34.185  15.813  1.00 108.78 ?  163  VAL E O   1 
ATOM   12375 C CB  . VAL E  2  163 ? -15.193 32.279  14.744  1.00 114.41 ?  163  VAL E CB  1 
ATOM   12376 C CG1 . VAL E  2  163 ? -16.144 32.976  13.786  1.00 115.37 ?  163  VAL E CG1 1 
ATOM   12377 C CG2 . VAL E  2  163 ? -13.891 31.901  14.049  1.00 111.68 ?  163  VAL E CG2 1 
ATOM   12378 N N   . LEU E  2  164 ? -14.491 35.407  15.080  1.00 116.05 ?  164  LEU E N   1 
ATOM   12379 C CA  . LEU E  2  164 ? -13.811 36.655  14.732  1.00 115.20 ?  164  LEU E CA  1 
ATOM   12380 C C   . LEU E  2  164 ? -12.815 36.475  13.594  1.00 111.92 ?  164  LEU E C   1 
ATOM   12381 O O   . LEU E  2  164 ? -12.186 37.457  13.179  1.00 111.34 ?  164  LEU E O   1 
ATOM   12382 C CB  . LEU E  2  164 ? -13.111 37.322  15.933  1.00 116.40 ?  164  LEU E CB  1 
ATOM   12383 C CG  . LEU E  2  164 ? -11.722 36.902  16.439  1.00 114.89 ?  164  LEU E CG  1 
ATOM   12384 C CD1 . LEU E  2  164 ? -10.594 37.770  15.873  1.00 113.54 ?  164  LEU E CD1 1 
ATOM   12385 C CD2 . LEU E  2  164 ? -11.696 36.903  17.969  1.00 118.18 ?  164  LEU E CD2 1 
ATOM   12386 N N   . THR E  2  165 ? -12.665 35.264  13.059  1.00 106.92 ?  165  THR E N   1 
ATOM   12387 C CA  . THR E  2  165 ? -11.806 35.017  11.912  1.00 104.56 ?  165  THR E CA  1 
ATOM   12388 C C   . THR E  2  165 ? -12.588 34.690  10.647  1.00 105.66 ?  165  THR E C   1 
ATOM   12389 O O   . THR E  2  165 ? -11.991 34.637  9.565   1.00 103.75 ?  165  THR E O   1 
ATOM   12390 C CB  . THR E  2  165 ? -10.822 33.876  12.217  1.00 103.02 ?  165  THR E CB  1 
ATOM   12391 O OG1 . THR E  2  165 ? -10.443 33.920  13.596  1.00 103.84 ?  165  THR E OG1 1 
ATOM   12392 C CG2 . THR E  2  165 ? -9.572  34.016  11.379  1.00 99.73  ?  165  THR E CG2 1 
ATOM   12393 N N   . LEU E  2  166 ? -13.901 34.478  10.754  1.00 103.93 ?  166  LEU E N   1 
ATOM   12394 C CA  . LEU E  2  166 ? -14.727 34.152  9.599   1.00 105.03 ?  166  LEU E CA  1 
ATOM   12395 C C   . LEU E  2  166 ? -14.741 35.292  8.592   1.00 103.29 ?  166  LEU E C   1 
ATOM   12396 O O   . LEU E  2  166 ? -15.287 36.366  8.865   1.00 104.00 ?  166  LEU E O   1 
ATOM   12397 C CB  . LEU E  2  166 ? -16.158 33.824  10.035  1.00 108.79 ?  166  LEU E CB  1 
ATOM   12398 C CG  . LEU E  2  166 ? -16.536 32.344  10.094  1.00 111.28 ?  166  LEU E CG  1 
ATOM   12399 C CD1 . LEU E  2  166 ? -16.836 31.808  8.705   1.00 111.22 ?  166  LEU E CD1 1 
ATOM   12400 C CD2 . LEU E  2  166 ? -15.422 31.547  10.729  1.00 110.18 ?  166  LEU E CD2 1 
ATOM   12401 N N   . GLN E  2  167 ? -14.143 35.064  7.425   1.00 106.82 ?  167  GLN E N   1 
ATOM   12402 C CA  . GLN E  2  167 ? -14.218 36.009  6.321   1.00 105.54 ?  167  GLN E CA  1 
ATOM   12403 C C   . GLN E  2  167 ? -15.197 35.566  5.246   1.00 106.13 ?  167  GLN E C   1 
ATOM   12404 O O   . GLN E  2  167 ? -15.890 36.404  4.661   1.00 106.60 ?  167  GLN E O   1 
ATOM   12405 C CB  . GLN E  2  167 ? -12.832 36.208  5.696   1.00 102.85 ?  167  GLN E CB  1 
ATOM   12406 C CG  . GLN E  2  167 ? -11.763 36.719  6.655   1.00 102.09 ?  167  GLN E CG  1 
ATOM   12407 C CD  . GLN E  2  167 ? -11.248 38.104  6.280   1.00 102.04 ?  167  GLN E CD  1 
ATOM   12408 O OE1 . GLN E  2  167 ? -11.996 38.943  5.774   1.00 103.93 ?  167  GLN E OE1 1 
ATOM   12409 N NE2 . GLN E  2  167 ? -9.962  38.345  6.522   1.00 100.96 ?  167  GLN E NE2 1 
ATOM   12410 N N   . VAL E  2  168 ? -15.289 34.263  4.995   1.00 100.73 ?  168  VAL E N   1 
ATOM   12411 C CA  . VAL E  2  168 ? -16.149 33.706  3.959   1.00 101.25 ?  168  VAL E CA  1 
ATOM   12412 C C   . VAL E  2  168 ? -17.093 32.709  4.612   1.00 104.70 ?  168  VAL E C   1 
ATOM   12413 O O   . VAL E  2  168 ? -16.645 31.755  5.261   1.00 105.05 ?  168  VAL E O   1 
ATOM   12414 C CB  . VAL E  2  168 ? -15.338 33.034  2.840   1.00 98.35  ?  168  VAL E CB  1 
ATOM   12415 C CG1 . VAL E  2  168 ? -16.256 32.605  1.707   1.00 99.37  ?  168  VAL E CG1 1 
ATOM   12416 C CG2 . VAL E  2  168 ? -14.256 33.974  2.328   1.00 96.01  ?  168  VAL E CG2 1 
ATOM   12417 N N   . LEU E  2  169 ? -18.395 32.931  4.440   1.00 102.04 ?  169  LEU E N   1 
ATOM   12418 C CA  . LEU E  2  169 ? -19.433 32.030  4.920   1.00 106.30 ?  169  LEU E CA  1 
ATOM   12419 C C   . LEU E  2  169 ? -20.457 31.841  3.812   1.00 107.65 ?  169  LEU E C   1 
ATOM   12420 O O   . LEU E  2  169 ? -20.855 32.806  3.155   1.00 106.91 ?  169  LEU E O   1 
ATOM   12421 C CB  . LEU E  2  169 ? -20.111 32.578  6.196   1.00 109.36 ?  169  LEU E CB  1 
ATOM   12422 C CG  . LEU E  2  169 ? -21.237 31.835  6.939   1.00 114.07 ?  169  LEU E CG  1 
ATOM   12423 C CD1 . LEU E  2  169 ? -22.573 31.791  6.196   1.00 116.31 ?  169  LEU E CD1 1 
ATOM   12424 C CD2 . LEU E  2  169 ? -20.787 30.434  7.283   1.00 115.28 ?  169  LEU E CD2 1 
ATOM   12425 N N   . ASP E  2  170 ? -20.863 30.592  3.593   1.00 108.55 ?  170  ASP E N   1 
ATOM   12426 C CA  . ASP E  2  170 ? -21.980 30.306  2.696   1.00 110.68 ?  170  ASP E CA  1 
ATOM   12427 C C   . ASP E  2  170 ? -22.674 29.047  3.194   1.00 114.82 ?  170  ASP E C   1 
ATOM   12428 O O   . ASP E  2  170 ? -22.089 27.960  3.161   1.00 114.65 ?  170  ASP E O   1 
ATOM   12429 C CB  . ASP E  2  170 ? -21.507 30.142  1.252   1.00 107.70 ?  170  ASP E CB  1 
ATOM   12430 C CG  . ASP E  2  170 ? -22.660 30.095  0.260   1.00 109.65 ?  170  ASP E CG  1 
ATOM   12431 O OD1 . ASP E  2  170 ? -23.772 30.538  0.619   1.00 112.59 ?  170  ASP E OD1 1 
ATOM   12432 O OD2 . ASP E  2  170 ? -22.455 29.620  -0.878  1.00 108.20 -1 170  ASP E OD2 1 
ATOM   12433 N N   . LEU E  2  171 ? -23.918 29.195  3.643   1.00 113.56 ?  171  LEU E N   1 
ATOM   12434 C CA  . LEU E  2  171 ? -24.773 28.078  4.030   1.00 115.33 ?  171  LEU E CA  1 
ATOM   12435 C C   . LEU E  2  171 ? -26.087 28.132  3.267   1.00 115.35 ?  171  LEU E C   1 
ATOM   12436 O O   . LEU E  2  171 ? -27.158 27.868  3.813   1.00 117.44 ?  171  LEU E O   1 
ATOM   12437 C CB  . LEU E  2  171 ? -25.012 28.054  5.541   1.00 118.27 ?  171  LEU E CB  1 
ATOM   12438 C CG  . LEU E  2  171 ? -25.302 29.343  6.321   1.00 119.45 ?  171  LEU E CG  1 
ATOM   12439 C CD1 . LEU E  2  171 ? -26.735 29.826  6.144   1.00 120.24 ?  171  LEU E CD1 1 
ATOM   12440 C CD2 . LEU E  2  171 ? -24.996 29.144  7.799   1.00 121.35 ?  171  LEU E CD2 1 
ATOM   12441 N N   . SER E  2  172 ? -26.025 28.497  1.992   1.00 117.55 ?  172  SER E N   1 
ATOM   12442 C CA  . SER E  2  172 ? -27.224 28.601  1.181   1.00 118.15 ?  172  SER E CA  1 
ATOM   12443 C C   . SER E  2  172 ? -27.742 27.219  0.788   1.00 118.29 ?  172  SER E C   1 
ATOM   12444 O O   . SER E  2  172 ? -27.045 26.209  0.902   1.00 117.15 ?  172  SER E O   1 
ATOM   12445 C CB  . SER E  2  172 ? -26.948 29.435  -0.071  1.00 116.09 ?  172  SER E CB  1 
ATOM   12446 O OG  . SER E  2  172 ? -26.591 30.762  0.275   1.00 115.88 ?  172  SER E OG  1 
ATOM   12447 N N   . ASN E  2  173 ? -28.992 27.189  0.323   1.00 126.82 ?  173  ASN E N   1 
ATOM   12448 C CA  . ASN E  2  173 ? -29.585 26.000  -0.299  1.00 125.89 ?  173  ASN E CA  1 
ATOM   12449 C C   . ASN E  2  173 ? -29.690 24.818  0.668   1.00 125.97 ?  173  ASN E C   1 
ATOM   12450 O O   . ASN E  2  173 ? -29.432 23.670  0.297   1.00 123.86 ?  173  ASN E O   1 
ATOM   12451 C CB  . ASN E  2  173 ? -28.812 25.598  -1.560  1.00 123.10 ?  173  ASN E CB  1 
ATOM   12452 C CG  . ASN E  2  173 ? -28.836 26.675  -2.631  1.00 122.76 ?  173  ASN E CG  1 
ATOM   12453 O OD1 . ASN E  2  173 ? -29.813 26.809  -3.367  1.00 121.50 ?  173  ASN E OD1 1 
ATOM   12454 N ND2 . ASN E  2  173 ? -27.755 27.442  -2.729  1.00 121.28 ?  173  ASN E ND2 1 
ATOM   12455 N N   . ASN E  2  174 ? -30.050 25.095  1.927   1.00 125.60 ?  174  ASN E N   1 
ATOM   12456 C CA  . ASN E  2  174 ? -30.402 24.022  2.866   1.00 126.54 ?  174  ASN E CA  1 
ATOM   12457 C C   . ASN E  2  174 ? -31.472 24.512  3.834   1.00 129.11 ?  174  ASN E C   1 
ATOM   12458 O O   . ASN E  2  174 ? -31.404 25.660  4.294   1.00 130.41 ?  174  ASN E O   1 
ATOM   12459 C CB  . ASN E  2  174 ? -29.199 23.480  3.653   1.00 126.78 ?  174  ASN E CB  1 
ATOM   12460 C CG  . ASN E  2  174 ? -28.207 24.551  4.030   1.00 127.07 ?  174  ASN E CG  1 
ATOM   12461 O OD1 . ASN E  2  174 ? -27.986 25.493  3.280   1.00 125.84 ?  174  ASN E OD1 1 
ATOM   12462 N ND2 . ASN E  2  174 ? -27.593 24.405  5.199   1.00 128.59 ?  174  ASN E ND2 1 
ATOM   12463 N N   . PRO E  2  175 ? -32.458 23.668  4.162   1.00 128.03 ?  175  PRO E N   1 
ATOM   12464 C CA  . PRO E  2  175 ? -33.628 24.131  4.929   1.00 130.20 ?  175  PRO E CA  1 
ATOM   12465 C C   . PRO E  2  175 ? -33.373 24.384  6.412   1.00 132.36 ?  175  PRO E C   1 
ATOM   12466 O O   . PRO E  2  175 ? -33.692 23.541  7.258   1.00 133.31 ?  175  PRO E O   1 
ATOM   12467 C CB  . PRO E  2  175 ? -34.633 22.988  4.730   1.00 132.77 ?  175  PRO E CB  1 
ATOM   12468 C CG  . PRO E  2  175 ? -33.766 21.786  4.505   1.00 130.74 ?  175  PRO E CG  1 
ATOM   12469 C CD  . PRO E  2  175 ? -32.657 22.305  3.641   1.00 126.49 ?  175  PRO E CD  1 
ATOM   12470 N N   . LEU E  2  176 ? -32.803 25.543  6.738   1.00 133.94 ?  176  LEU E N   1 
ATOM   12471 C CA  . LEU E  2  176 ? -32.562 25.924  8.121   1.00 135.44 ?  176  LEU E CA  1 
ATOM   12472 C C   . LEU E  2  176 ? -33.733 26.773  8.627   1.00 137.03 ?  176  LEU E C   1 
ATOM   12473 O O   . LEU E  2  176 ? -34.674 27.073  7.888   1.00 137.11 ?  176  LEU E O   1 
ATOM   12474 C CB  . LEU E  2  176 ? -31.223 26.652  8.225   1.00 134.70 ?  176  LEU E CB  1 
ATOM   12475 C CG  . LEU E  2  176 ? -30.284 26.251  9.360   1.00 135.03 ?  176  LEU E CG  1 
ATOM   12476 C CD1 . LEU E  2  176 ? -29.933 24.788  9.289   1.00 134.83 ?  176  LEU E CD1 1 
ATOM   12477 C CD2 . LEU E  2  176 ? -29.020 27.049  9.224   1.00 133.70 ?  176  LEU E CD2 1 
ATOM   12478 N N   . THR E  2  177 ? -33.693 27.156  9.909   1.00 137.68 ?  177  THR E N   1 
ATOM   12479 C CA  . THR E  2  177 ? -34.781 27.900  10.541  1.00 139.30 ?  177  THR E CA  1 
ATOM   12480 C C   . THR E  2  177 ? -34.212 28.965  11.469  1.00 139.75 ?  177  THR E C   1 
ATOM   12481 O O   . THR E  2  177 ? -33.091 28.839  11.965  1.00 138.99 ?  177  THR E O   1 
ATOM   12482 C CB  . THR E  2  177 ? -35.717 26.989  11.356  1.00 140.80 ?  177  THR E CB  1 
ATOM   12483 O OG1 . THR E  2  177 ? -35.023 26.499  12.511  1.00 140.69 ?  177  THR E OG1 1 
ATOM   12484 C CG2 . THR E  2  177 ? -36.206 25.811  10.525  1.00 143.33 ?  177  THR E CG2 1 
ATOM   12485 N N   . GLY E  2  178 ? -34.994 30.019  11.698  1.00 140.64 ?  178  GLY E N   1 
ATOM   12486 C CA  . GLY E  2  178 ? -34.611 31.094  12.595  1.00 141.06 ?  178  GLY E CA  1 
ATOM   12487 C C   . GLY E  2  178 ? -34.233 32.362  11.845  1.00 140.50 ?  178  GLY E C   1 
ATOM   12488 O O   . GLY E  2  178 ? -34.268 32.434  10.616  1.00 139.80 ?  178  GLY E O   1 
ATOM   12489 N N   . ASP E  2  179 ? -33.884 33.381  12.629  1.00 139.17 ?  179  ASP E N   1 
ATOM   12490 C CA  . ASP E  2  179 ? -33.420 34.659  12.105  1.00 138.54 ?  179  ASP E CA  1 
ATOM   12491 C C   . ASP E  2  179 ? -31.894 34.690  12.011  1.00 136.63 ?  179  ASP E C   1 
ATOM   12492 O O   . ASP E  2  179 ? -31.190 34.044  12.792  1.00 136.32 ?  179  ASP E O   1 
ATOM   12493 C CB  . ASP E  2  179 ? -33.915 35.812  12.980  1.00 140.08 ?  179  ASP E CB  1 
ATOM   12494 C CG  . ASP E  2  179 ? -35.302 36.289  12.584  1.00 141.82 ?  179  ASP E CG  1 
ATOM   12495 O OD1 . ASP E  2  179 ? -36.118 35.453  12.140  1.00 142.44 ?  179  ASP E OD1 1 
ATOM   12496 O OD2 . ASP E  2  179 ? -35.581 37.499  12.722  1.00 142.74 -1 179  ASP E OD2 1 
ATOM   12497 N N   . ILE E  2  180 ? -31.392 35.446  11.038  1.00 135.03 ?  180  ILE E N   1 
ATOM   12498 C CA  . ILE E  2  180 ? -29.957 35.526  10.760  1.00 133.16 ?  180  ILE E CA  1 
ATOM   12499 C C   . ILE E  2  180 ? -29.270 36.413  11.794  1.00 133.50 ?  180  ILE E C   1 
ATOM   12500 O O   . ILE E  2  180 ? -29.624 37.592  11.936  1.00 134.15 ?  180  ILE E O   1 
ATOM   12501 C CB  . ILE E  2  180 ? -29.694 36.049  9.338   1.00 131.56 ?  180  ILE E CB  1 
ATOM   12502 C CG1 . ILE E  2  180 ? -30.622 37.221  9.011   1.00 132.47 ?  180  ILE E CG1 1 
ATOM   12503 C CG2 . ILE E  2  180 ? -29.894 34.949  8.327   1.00 130.74 ?  180  ILE E CG2 1 
ATOM   12504 C CD1 . ILE E  2  180 ? -30.564 37.671  7.566   1.00 131.01 ?  180  ILE E CD1 1 
ATOM   12505 N N   . PRO E  2  181 ? -28.295 35.897  12.538  1.00 130.92 ?  181  PRO E N   1 
ATOM   12506 C CA  . PRO E  2  181 ? -27.582 36.745  13.499  1.00 131.48 ?  181  PRO E CA  1 
ATOM   12507 C C   . PRO E  2  181 ? -26.686 37.754  12.801  1.00 130.26 ?  181  PRO E C   1 
ATOM   12508 O O   . PRO E  2  181 ? -26.204 37.528  11.690  1.00 128.62 ?  181  PRO E O   1 
ATOM   12509 C CB  . PRO E  2  181 ? -26.753 35.741  14.312  1.00 131.58 ?  181  PRO E CB  1 
ATOM   12510 C CG  . PRO E  2  181 ? -27.413 34.411  14.076  1.00 131.40 ?  181  PRO E CG  1 
ATOM   12511 C CD  . PRO E  2  181 ? -27.927 34.480  12.673  1.00 130.53 ?  181  PRO E CD  1 
ATOM   12512 N N   . VAL E  2  182 ? -26.497 38.899  13.459  1.00 127.90 ?  182  VAL E N   1 
ATOM   12513 C CA  . VAL E  2  182 ? -25.529 39.908  13.038  1.00 126.94 ?  182  VAL E CA  1 
ATOM   12514 C C   . VAL E  2  182 ? -24.663 40.251  14.253  1.00 128.29 ?  182  VAL E C   1 
ATOM   12515 O O   . VAL E  2  182 ? -24.043 41.319  14.318  1.00 128.33 ?  182  VAL E O   1 
ATOM   12516 C CB  . VAL E  2  182 ? -26.258 41.140  12.452  1.00 126.85 ?  182  VAL E CB  1 
ATOM   12517 C CG1 . VAL E  2  182 ? -25.295 42.184  11.890  1.00 125.59 ?  182  VAL E CG1 1 
ATOM   12518 C CG2 . VAL E  2  182 ? -27.238 40.714  11.367  1.00 126.17 ?  182  VAL E CG2 1 
ATOM   12519 N N   . ASN E  2  183 ? -24.607 39.338  15.227  1.00 127.48 ?  183  ASN E N   1 
ATOM   12520 C CA  . ASN E  2  183 ? -24.120 39.694  16.559  1.00 129.47 ?  183  ASN E CA  1 
ATOM   12521 C C   . ASN E  2  183 ? -22.664 40.156  16.627  1.00 129.55 ?  183  ASN E C   1 
ATOM   12522 O O   . ASN E  2  183 ? -22.406 41.325  16.934  1.00 130.33 ?  183  ASN E O   1 
ATOM   12523 C CB  . ASN E  2  183 ? -24.309 38.500  17.503  1.00 130.53 ?  183  ASN E CB  1 
ATOM   12524 C CG  . ASN E  2  183 ? -24.178 38.880  18.967  1.00 132.92 ?  183  ASN E CG  1 
ATOM   12525 O OD1 . ASN E  2  183 ? -23.990 40.048  19.305  1.00 134.00 ?  183  ASN E OD1 1 
ATOM   12526 N ND2 . ASN E  2  183 ? -24.267 37.887  19.844  1.00 133.74 ?  183  ASN E ND2 1 
ATOM   12527 N N   . GLY E  2  184 ? -21.704 39.275  16.339  1.00 125.00 ?  184  GLY E N   1 
ATOM   12528 C CA  . GLY E  2  184 ? -20.317 39.694  16.455  1.00 125.39 ?  184  GLY E CA  1 
ATOM   12529 C C   . GLY E  2  184 ? -19.443 39.619  15.221  1.00 123.25 ?  184  GLY E C   1 
ATOM   12530 O O   . GLY E  2  184 ? -18.513 40.416  15.063  1.00 122.96 ?  184  GLY E O   1 
ATOM   12531 N N   . SER E  2  185 ? -19.735 38.669  14.335  1.00 124.80 ?  185  SER E N   1 
ATOM   12532 C CA  . SER E  2  185 ? -18.921 38.435  13.148  1.00 122.73 ?  185  SER E CA  1 
ATOM   12533 C C   . SER E  2  185 ? -19.723 38.411  11.863  1.00 120.45 ?  185  SER E C   1 
ATOM   12534 O O   . SER E  2  185 ? -19.127 38.509  10.783  1.00 118.40 ?  185  SER E O   1 
ATOM   12535 C CB  . SER E  2  185 ? -18.150 37.111  13.276  1.00 123.35 ?  185  SER E CB  1 
ATOM   12536 O OG  . SER E  2  185 ? -18.039 36.455  12.026  1.00 121.23 ?  185  SER E OG  1 
ATOM   12537 N N   . PHE E  2  186 ? -21.044 38.285  11.940  1.00 122.96 ?  186  PHE E N   1 
ATOM   12538 C CA  . PHE E  2  186 ? -21.914 38.311  10.776  1.00 121.37 ?  186  PHE E CA  1 
ATOM   12539 C C   . PHE E  2  186 ? -22.249 39.731  10.345  1.00 120.73 ?  186  PHE E C   1 
ATOM   12540 O O   . PHE E  2  186 ? -23.065 39.908  9.434   1.00 119.79 ?  186  PHE E O   1 
ATOM   12541 C CB  . PHE E  2  186 ? -23.212 37.547  11.064  1.00 122.36 ?  186  PHE E CB  1 
ATOM   12542 C CG  . PHE E  2  186 ? -23.058 36.041  11.132  1.00 122.49 ?  186  PHE E CG  1 
ATOM   12543 C CD1 . PHE E  2  186 ? -21.928 35.452  11.682  1.00 122.97 ?  186  PHE E CD1 1 
ATOM   12544 C CD2 . PHE E  2  186 ? -24.068 35.214  10.663  1.00 122.36 ?  186  PHE E CD2 1 
ATOM   12545 C CE1 . PHE E  2  186 ? -21.805 34.074  11.747  1.00 123.01 ?  186  PHE E CE1 1 
ATOM   12546 C CE2 . PHE E  2  186 ? -23.949 33.835  10.726  1.00 122.45 ?  186  PHE E CE2 1 
ATOM   12547 C CZ  . PHE E  2  186 ? -22.817 33.266  11.269  1.00 122.62 ?  186  PHE E CZ  1 
ATOM   12548 N N   . SER E  2  187 ? -21.652 40.737  10.994  1.00 124.65 ?  187  SER E N   1 
ATOM   12549 C CA  . SER E  2  187 ? -21.939 42.130  10.663  1.00 124.30 ?  187  SER E CA  1 
ATOM   12550 C C   . SER E  2  187 ? -21.528 42.467  9.237   1.00 121.87 ?  187  SER E C   1 
ATOM   12551 O O   . SER E  2  187 ? -22.180 43.286  8.579   1.00 121.39 ?  187  SER E O   1 
ATOM   12552 C CB  . SER E  2  187 ? -21.226 43.058  11.647  1.00 125.61 ?  187  SER E CB  1 
ATOM   12553 O OG  . SER E  2  187 ? -19.849 42.731  11.750  1.00 125.21 ?  187  SER E OG  1 
ATOM   12554 N N   . LEU E  2  188 ? -20.457 41.849  8.745   1.00 120.41 ?  188  LEU E N   1 
ATOM   12555 C CA  . LEU E  2  188 ? -19.988 42.084  7.389   1.00 117.97 ?  188  LEU E CA  1 
ATOM   12556 C C   . LEU E  2  188 ? -20.670 41.190  6.365   1.00 116.59 ?  188  LEU E C   1 
ATOM   12557 O O   . LEU E  2  188 ? -20.498 41.414  5.161   1.00 114.56 ?  188  LEU E O   1 
ATOM   12558 C CB  . LEU E  2  188 ? -18.470 41.877  7.303   1.00 117.01 ?  188  LEU E CB  1 
ATOM   12559 C CG  . LEU E  2  188 ? -17.538 42.609  8.273   1.00 118.22 ?  188  LEU E CG  1 
ATOM   12560 C CD1 . LEU E  2  188 ? -17.446 41.896  9.617   1.00 120.20 ?  188  LEU E CD1 1 
ATOM   12561 C CD2 . LEU E  2  188 ? -16.158 42.761  7.650   1.00 116.72 ?  188  LEU E CD2 1 
ATOM   12562 N N   . PHE E  2  189 ? -21.445 40.202  6.805   1.00 115.72 ?  189  PHE E N   1 
ATOM   12563 C CA  . PHE E  2  189 ? -22.028 39.233  5.889   1.00 114.60 ?  189  PHE E CA  1 
ATOM   12564 C C   . PHE E  2  189 ? -23.282 39.794  5.225   1.00 114.68 ?  189  PHE E C   1 
ATOM   12565 O O   . PHE E  2  189 ? -24.016 40.600  5.805   1.00 116.33 ?  189  PHE E O   1 
ATOM   12566 C CB  . PHE E  2  189 ? -22.351 37.933  6.624   1.00 116.12 ?  189  PHE E CB  1 
ATOM   12567 C CG  . PHE E  2  189 ? -21.131 37.157  7.043   1.00 116.09 ?  189  PHE E CG  1 
ATOM   12568 C CD1 . PHE E  2  189 ? -19.865 37.549  6.631   1.00 114.46 ?  189  PHE E CD1 1 
ATOM   12569 C CD2 . PHE E  2  189 ? -21.247 36.038  7.851   1.00 117.88 ?  189  PHE E CD2 1 
ATOM   12570 C CE1 . PHE E  2  189 ? -18.742 36.841  7.016   1.00 114.69 ?  189  PHE E CE1 1 
ATOM   12571 C CE2 . PHE E  2  189 ? -20.126 35.328  8.241   1.00 118.29 ?  189  PHE E CE2 1 
ATOM   12572 C CZ  . PHE E  2  189 ? -18.873 35.729  7.821   1.00 116.75 ?  189  PHE E CZ  1 
ATOM   12573 N N   . THR E  2  190 ? -23.515 39.357  3.988   1.00 116.94 ?  190  THR E N   1 
ATOM   12574 C CA  . THR E  2  190 ? -24.602 39.851  3.151   1.00 117.05 ?  190  THR E CA  1 
ATOM   12575 C C   . THR E  2  190 ? -25.561 38.702  2.844   1.00 117.64 ?  190  THR E C   1 
ATOM   12576 O O   . THR E  2  190 ? -25.223 37.539  3.101   1.00 117.46 ?  190  THR E O   1 
ATOM   12577 C CB  . THR E  2  190 ? -24.041 40.482  1.870   1.00 114.86 ?  190  THR E CB  1 
ATOM   12578 O OG1 . THR E  2  190 ? -23.895 39.479  0.859   1.00 113.20 ?  190  THR E OG1 1 
ATOM   12579 C CG2 . THR E  2  190 ? -22.688 41.137  2.134   1.00 113.84 ?  190  THR E CG2 1 
ATOM   12580 N N   . PRO E  2  191 ? -26.761 38.973  2.312   1.00 116.54 ?  191  PRO E N   1 
ATOM   12581 C CA  . PRO E  2  191 ? -27.749 37.892  2.128   1.00 117.65 ?  191  PRO E CA  1 
ATOM   12582 C C   . PRO E  2  191 ? -27.316 36.754  1.203   1.00 115.79 ?  191  PRO E C   1 
ATOM   12583 O O   . PRO E  2  191 ? -27.997 35.719  1.191   1.00 116.83 ?  191  PRO E O   1 
ATOM   12584 C CB  . PRO E  2  191 ? -28.970 38.630  1.561   1.00 119.02 ?  191  PRO E CB  1 
ATOM   12585 C CG  . PRO E  2  191 ? -28.856 40.000  2.121   1.00 119.65 ?  191  PRO E CG  1 
ATOM   12586 C CD  . PRO E  2  191 ? -27.380 40.301  2.128   1.00 117.45 ?  191  PRO E CD  1 
ATOM   12587 N N   . ILE E  2  192 ? -26.235 36.896  0.429   1.00 117.28 ?  192  ILE E N   1 
ATOM   12588 C CA  . ILE E  2  192 ? -25.805 35.781  -0.415  1.00 115.52 ?  192  ILE E CA  1 
ATOM   12589 C C   . ILE E  2  192 ? -25.322 34.615  0.445   1.00 115.82 ?  192  ILE E C   1 
ATOM   12590 O O   . ILE E  2  192 ? -25.484 33.447  0.070   1.00 115.56 ?  192  ILE E O   1 
ATOM   12591 C CB  . ILE E  2  192 ? -24.723 36.239  -1.416  1.00 112.90 ?  192  ILE E CB  1 
ATOM   12592 C CG1 . ILE E  2  192 ? -24.274 35.090  -2.336  1.00 111.09 ?  192  ILE E CG1 1 
ATOM   12593 C CG2 . ILE E  2  192 ? -23.522 36.827  -0.692  1.00 112.23 ?  192  ILE E CG2 1 
ATOM   12594 C CD1 . ILE E  2  192 ? -25.405 34.268  -2.946  1.00 111.81 ?  192  ILE E CD1 1 
ATOM   12595 N N   . SER E  2  193 ? -24.752 34.900  1.618   1.00 111.37 ?  193  SER E N   1 
ATOM   12596 C CA  . SER E  2  193 ? -24.309 33.829  2.502   1.00 111.76 ?  193  SER E CA  1 
ATOM   12597 C C   . SER E  2  193 ? -25.469 32.985  3.021   1.00 114.11 ?  193  SER E C   1 
ATOM   12598 O O   . SER E  2  193 ? -25.243 31.853  3.464   1.00 114.67 ?  193  SER E O   1 
ATOM   12599 C CB  . SER E  2  193 ? -23.533 34.419  3.679   1.00 112.72 ?  193  SER E CB  1 
ATOM   12600 O OG  . SER E  2  193 ? -22.468 35.234  3.229   1.00 110.74 ?  193  SER E OG  1 
ATOM   12601 N N   . PHE E  2  194 ? -26.708 33.503  2.965   1.00 114.14 ?  194  PHE E N   1 
ATOM   12602 C CA  . PHE E  2  194 ? -27.870 32.847  3.559   1.00 116.65 ?  194  PHE E CA  1 
ATOM   12603 C C   . PHE E  2  194 ? -29.012 32.670  2.563   1.00 117.20 ?  194  PHE E C   1 
ATOM   12604 O O   . PHE E  2  194 ? -30.169 32.548  2.979   1.00 119.62 ?  194  PHE E O   1 
ATOM   12605 C CB  . PHE E  2  194 ? -28.391 33.625  4.776   1.00 118.85 ?  194  PHE E CB  1 
ATOM   12606 C CG  . PHE E  2  194 ? -27.320 34.079  5.729   1.00 118.67 ?  194  PHE E CG  1 
ATOM   12607 C CD1 . PHE E  2  194 ? -26.544 35.194  5.452   1.00 117.43 ?  194  PHE E CD1 1 
ATOM   12608 C CD2 . PHE E  2  194 ? -27.099 33.395  6.913   1.00 119.89 ?  194  PHE E CD2 1 
ATOM   12609 C CE1 . PHE E  2  194 ? -25.562 35.612  6.331   1.00 117.60 ?  194  PHE E CE1 1 
ATOM   12610 C CE2 . PHE E  2  194 ? -26.120 33.809  7.798   1.00 120.07 ?  194  PHE E CE2 1 
ATOM   12611 C CZ  . PHE E  2  194 ? -25.350 34.919  7.505   1.00 119.02 ?  194  PHE E CZ  1 
ATOM   12612 N N   . ALA E  2  195 ? -28.721 32.662  1.264   1.00 121.33 ?  195  ALA E N   1 
ATOM   12613 C CA  . ALA E  2  195 ? -29.773 32.540  0.263   1.00 122.11 ?  195  ALA E CA  1 
ATOM   12614 C C   . ALA E  2  195 ? -30.455 31.180  0.361   1.00 123.77 ?  195  ALA E C   1 
ATOM   12615 O O   . ALA E  2  195 ? -29.861 30.192  0.796   1.00 123.09 ?  195  ALA E O   1 
ATOM   12616 C CB  . ALA E  2  195 ? -29.201 32.742  -1.141  1.00 119.20 ?  195  ALA E CB  1 
ATOM   12617 N N   . ASN E  2  196 ? -31.731 31.143  -0.023  1.00 129.58 ?  196  ASN E N   1 
ATOM   12618 C CA  . ASN E  2  196 ? -32.528 29.918  -0.041  1.00 130.42 ?  196  ASN E CA  1 
ATOM   12619 C C   . ASN E  2  196 ? -32.669 29.287  1.346   1.00 131.11 ?  196  ASN E C   1 
ATOM   12620 O O   . ASN E  2  196 ? -32.959 28.091  1.458   1.00 130.14 ?  196  ASN E O   1 
ATOM   12621 C CB  . ASN E  2  196 ? -31.946 28.901  -1.036  1.00 127.39 ?  196  ASN E CB  1 
ATOM   12622 C CG  . ASN E  2  196 ? -32.981 27.913  -1.544  1.00 126.81 ?  196  ASN E CG  1 
ATOM   12623 O OD1 . ASN E  2  196 ? -32.986 26.747  -1.148  1.00 126.20 ?  196  ASN E OD1 1 
ATOM   12624 N ND2 . ASN E  2  196 ? -33.860 28.375  -2.427  1.00 129.78 ?  196  ASN E ND2 1 
ATOM   12625 N N   . THR E  2  197 ? -32.467 30.063  2.416   1.00 131.51 ?  197  THR E N   1 
ATOM   12626 C CA  . THR E  2  197 ? -32.590 29.562  3.784   1.00 132.44 ?  197  THR E CA  1 
ATOM   12627 C C   . THR E  2  197 ? -33.254 30.609  4.669   1.00 134.48 ?  197  THR E C   1 
ATOM   12628 O O   . THR E  2  197 ? -32.866 31.780  4.649   1.00 134.36 ?  197  THR E O   1 
ATOM   12629 C CB  . THR E  2  197 ? -31.222 29.195  4.392   1.00 131.17 ?  197  THR E CB  1 
ATOM   12630 O OG1 . THR E  2  197 ? -30.547 30.388  4.817   1.00 130.92 ?  197  THR E OG1 1 
ATOM   12631 C CG2 . THR E  2  197 ? -30.335 28.443  3.397   1.00 128.82 ?  197  THR E CG2 1 
ATOM   12632 N N   . LYS E  2  198 ? -34.240 30.174  5.447   1.00 134.42 ?  198  LYS E N   1 
ATOM   12633 C CA  . LYS E  2  198 ? -34.816 30.910  6.591   1.00 136.31 ?  198  LYS E CA  1 
ATOM   12634 C C   . LYS E  2  198 ? -35.356 32.251  6.089   1.00 137.27 ?  198  LYS E C   1 
ATOM   12635 O O   . LYS E  2  198 ? -35.862 32.334  4.959   1.00 137.21 ?  198  LYS E O   1 
ATOM   12636 C CB  . LYS E  2  198 ? -33.791 31.054  7.681   1.00 136.05 ?  198  LYS E CB  1 
ATOM   12637 C CG  . LYS E  2  198 ? -32.897 29.868  7.918   1.00 134.90 ?  198  LYS E CG  1 
ATOM   12638 C CD  . LYS E  2  198 ? -32.127 30.076  9.203   1.00 135.20 ?  198  LYS E CD  1 
ATOM   12639 C CE  . LYS E  2  198 ? -31.473 31.455  9.333   1.00 134.73 ?  198  LYS E CE  1 
ATOM   12640 N NZ  . LYS E  2  198 ? -30.975 32.049  8.058   1.00 133.06 ?  198  LYS E NZ  1 
ATOM   12641 N N   . LEU E  2  199 ? -35.231 33.306  6.895   1.00 130.90 ?  199  LEU E N   1 
ATOM   12642 C CA  . LEU E  2  199 ? -35.744 34.636  6.593   1.00 133.21 ?  199  LEU E CA  1 
ATOM   12643 C C   . LEU E  2  199 ? -35.141 35.673  7.545   1.00 130.97 ?  199  LEU E C   1 
ATOM   12644 O O   . LEU E  2  199 ? -35.273 36.882  7.339   1.00 132.02 ?  199  LEU E O   1 
ATOM   12645 C CB  . LEU E  2  199 ? -37.267 34.651  6.694   1.00 140.25 ?  199  LEU E CB  1 
ATOM   12646 C CG  . LEU E  2  199 ? -37.970 35.731  5.877   1.00 143.85 ?  199  LEU E CG  1 
ATOM   12647 C CD1 . LEU E  2  199 ? -37.805 35.452  4.390   1.00 143.52 ?  199  LEU E CD1 1 
ATOM   12648 C CD2 . LEU E  2  199 ? -39.442 35.818  6.259   1.00 151.09 ?  199  LEU E CD2 1 
ATOM   12649 N N   . PRO F  3  1   ? -17.447 -17.246 18.817  1.00 73.50  ?  1    PRO F N   1 
ATOM   12650 C CA  . PRO F  3  1   ? -16.530 -18.211 19.432  1.00 73.53  ?  1    PRO F CA  1 
ATOM   12651 C C   . PRO F  3  1   ? -15.366 -17.526 20.143  1.00 71.78  ?  1    PRO F C   1 
ATOM   12652 O O   . PRO F  3  1   ? -14.769 -16.600 19.591  1.00 70.83  ?  1    PRO F O   1 
ATOM   12653 C CB  . PRO F  3  1   ? -16.033 -19.043 18.239  1.00 75.21  ?  1    PRO F CB  1 
ATOM   12654 C CG  . PRO F  3  1   ? -16.843 -18.586 17.031  1.00 76.18  ?  1    PRO F CG  1 
ATOM   12655 C CD  . PRO F  3  1   ? -17.961 -17.727 17.527  1.00 75.51  ?  1    PRO F CD  1 
ATOM   12656 N N   . VAL F  3  2   ? -15.049 -17.989 21.353  1.00 71.66  ?  2    VAL F N   1 
ATOM   12657 C CA  . VAL F  3  2   ? -13.997 -17.370 22.151  1.00 70.49  ?  2    VAL F CA  1 
ATOM   12658 C C   . VAL F  3  2   ? -12.648 -17.631 21.497  1.00 70.83  ?  2    VAL F C   1 
ATOM   12659 O O   . VAL F  3  2   ? -12.302 -18.780 21.195  1.00 72.45  ?  2    VAL F O   1 
ATOM   12660 C CB  . VAL F  3  2   ? -14.035 -17.905 23.591  1.00 70.91  ?  2    VAL F CB  1 
ATOM   12661 C CG1 . VAL F  3  2   ? -12.714 -17.655 24.297  1.00 70.67  ?  2    VAL F CG1 1 
ATOM   12662 C CG2 . VAL F  3  2   ? -15.177 -17.270 24.363  1.00 70.37  ?  2    VAL F CG2 1 
ATOM   12663 N N   . ARG F  3  3   ? -11.881 -16.563 21.268  1.00 69.58  ?  3    ARG F N   1 
ATOM   12664 C CA  . ARG F  3  3   ? -10.561 -16.647 20.652  1.00 69.90  ?  3    ARG F CA  1 
ATOM   12665 C C   . ARG F  3  3   ? -9.535  -15.944 21.532  1.00 69.10  ?  3    ARG F C   1 
ATOM   12666 O O   . ARG F  3  3   ? -9.875  -15.234 22.479  1.00 68.21  ?  3    ARG F O   1 
ATOM   12667 C CB  . ARG F  3  3   ? -10.546 -16.024 19.247  1.00 69.53  ?  3    ARG F CB  1 
ATOM   12668 C CG  . ARG F  3  3   ? -11.825 -16.202 18.453  1.00 70.17  ?  3    ARG F CG  1 
ATOM   12669 C CD  . ARG F  3  3   ? -11.775 -15.446 17.128  1.00 70.06  ?  3    ARG F CD  1 
ATOM   12670 N NE  . ARG F  3  3   ? -13.082 -15.400 16.476  1.00 70.93  ?  3    ARG F NE  1 
ATOM   12671 C CZ  . ARG F  3  3   ? -14.106 -14.655 16.879  1.00 70.36  ?  3    ARG F CZ  1 
ATOM   12672 N NH1 . ARG F  3  3   ? -14.003 -13.841 17.920  1.00 68.85  ?  3    ARG F NH1 1 
ATOM   12673 N NH2 . ARG F  3  3   ? -15.263 -14.728 16.221  1.00 71.73  ?  3    ARG F NH2 1 
ATOM   12674 N N   . SER F  3  4   ? -8.264  -16.142 21.203  1.00 69.76  ?  4    SER F N   1 
ATOM   12675 C CA  . SER F  3  4   ? -7.162  -15.465 21.868  1.00 69.40  ?  4    SER F CA  1 
ATOM   12676 C C   . SER F  3  4   ? -6.763  -14.217 21.088  1.00 67.97  ?  4    SER F C   1 
ATOM   12677 O O   . SER F  3  4   ? -6.859  -14.174 19.859  1.00 67.87  ?  4    SER F O   1 
ATOM   12678 C CB  . SER F  3  4   ? -5.958  -16.393 22.001  1.00 71.43  ?  4    SER F CB  1 
ATOM   12679 O OG  . SER F  3  4   ? -5.650  -16.971 20.747  1.00 72.42  ?  4    SER F OG  1 
ATOM   12680 N N   . SER F  3  5   ? -6.317  -13.196 21.816  1.00 67.13  ?  5    SER F N   1 
ATOM   12681 C CA  . SER F  3  5   ? -5.917  -11.951 21.178  1.00 65.91  ?  5    SER F CA  1 
ATOM   12682 C C   . SER F  3  5   ? -4.669  -12.158 20.324  1.00 66.58  ?  5    SER F C   1 
ATOM   12683 O O   . SER F  3  5   ? -3.837  -13.029 20.593  1.00 68.14  ?  5    SER F O   1 
ATOM   12684 C CB  . SER F  3  5   ? -5.671  -10.864 22.226  1.00 65.34  ?  5    SER F CB  1 
ATOM   12685 O OG  . SER F  3  5   ? -4.923  -11.362 23.320  1.00 66.63  ?  5    SER F OG  1 
ATOM   12686 N N   . GLN F  3  6   ? -4.555  -11.353 19.270  1.00 65.70  ?  6    GLN F N   1 
ATOM   12687 C CA  . GLN F  3  6   ? -3.456  -11.451 18.321  1.00 66.35  ?  6    GLN F CA  1 
ATOM   12688 C C   . GLN F  3  6   ? -2.643  -10.165 18.344  1.00 65.43  ?  6    GLN F C   1 
ATOM   12689 O O   . GLN F  3  6   ? -3.198  -9.073  18.191  1.00 64.14  ?  6    GLN F O   1 
ATOM   12690 C CB  . GLN F  3  6   ? -3.984  -11.726 16.909  1.00 66.60  ?  6    GLN F CB  1 
ATOM   12691 C CG  . GLN F  3  6   ? -4.317  -13.190 16.646  1.00 68.34  ?  6    GLN F CG  1 
ATOM   12692 C CD  . GLN F  3  6   ? -3.225  -13.892 15.854  1.00 70.19  ?  6    GLN F CD  1 
ATOM   12693 O OE1 . GLN F  3  6   ? -2.457  -13.249 15.131  1.00 69.99  ?  6    GLN F OE1 1 
ATOM   12694 N NE2 . GLN F  3  6   ? -3.142  -15.216 15.994  1.00 72.27  ?  6    GLN F NE2 1 
ATOM   12695 N N   . SER F  3  7   ? -1.329  -10.298 18.514  1.00 66.43  ?  7    SER F N   1 
ATOM   12696 C CA  . SER F  3  7   ? -0.455  -9.133  18.493  1.00 65.86  ?  7    SER F CA  1 
ATOM   12697 C C   . SER F  3  7   ? -0.336  -8.582  17.078  1.00 65.24  ?  7    SER F C   1 
ATOM   12698 O O   . SER F  3  7   ? -0.024  -9.317  16.134  1.00 66.25  ?  7    SER F O   1 
ATOM   12699 C CB  . SER F  3  7   ? 0.929   -9.487  19.036  1.00 67.57  ?  7    SER F CB  1 
ATOM   12700 O OG  . SER F  3  7   ? 1.646   -8.318  19.409  1.00 67.17  ?  7    SER F OG  1 
ATOM   12701 N N   . SER F  3  8   ? -0.562  -7.282  16.936  1.00 63.92  ?  8    SER F N   1 
ATOM   12702 C CA  . SER F  3  8   ? -0.449  -6.637  15.640  1.00 63.48  ?  8    SER F CA  1 
ATOM   12703 C C   . SER F  3  8   ? 1.010   -6.330  15.313  1.00 64.07  ?  8    SER F C   1 
ATOM   12704 O O   . SER F  3  8   ? 1.839   -6.119  16.202  1.00 64.49  ?  8    SER F O   1 
ATOM   12705 C CB  . SER F  3  8   ? -1.276  -5.357  15.613  1.00 62.28  ?  8    SER F CB  1 
ATOM   12706 O OG  . SER F  3  8   ? -1.891  -5.196  14.350  1.00 62.26  ?  8    SER F OG  1 
ATOM   12707 N N   . GLN F  3  9   ? 1.326   -6.339  14.021  1.00 64.43  ?  9    GLN F N   1 
ATOM   12708 C CA  . GLN F  3  9   ? 2.676   -6.008  13.593  1.00 65.10  ?  9    GLN F CA  1 
ATOM   12709 C C   . GLN F  3  9   ? 2.947   -4.514  13.784  1.00 63.98  ?  9    GLN F C   1 
ATOM   12710 O O   . GLN F  3  9   ? 2.032   -3.684  13.843  1.00 62.85  ?  9    GLN F O   1 
ATOM   12711 C CB  . GLN F  3  9   ? 2.888   -6.409  12.132  1.00 66.04  ?  9    GLN F CB  1 
ATOM   12712 C CG  . GLN F  3  9   ? 3.998   -7.430  11.918  1.00 68.16  ?  9    GLN F CG  1 
ATOM   12713 C CD  . GLN F  3  9   ? 3.912   -8.139  10.573  1.00 69.61  ?  9    GLN F CD  1 
ATOM   12714 O OE1 . GLN F  3  9   ? 3.549   -7.528  9.566   1.00 69.13  ?  9    GLN F OE1 1 
ATOM   12715 N NE2 . GLN F  3  9   ? 4.275   -9.423  10.544  1.00 71.80  ?  9    GLN F NE2 1 
ATOM   12716 N N   . ALA F  3  10  ? 4.229   -4.178  13.898  1.00 64.66  ?  10   ALA F N   1 
ATOM   12717 C CA  . ALA F  3  10  ? 4.621   -2.782  14.016  1.00 63.96  ?  10   ALA F CA  1 
ATOM   12718 C C   . ALA F  3  10  ? 4.424   -2.054  12.690  1.00 63.39  ?  10   ALA F C   1 
ATOM   12719 O O   . ALA F  3  10  ? 4.523   -2.640  11.604  1.00 64.02  ?  10   ALA F O   1 
ATOM   12720 C CB  . ALA F  3  10  ? 6.076   -2.671  14.469  1.00 65.20  ?  10   ALA F CB  1 
ATOM   12721 N N   . GLY F  3  11  ? 4.149   -0.757  12.789  1.00 62.57  ?  11   GLY F N   1 
ATOM   12722 C CA  . GLY F  3  11  ? 3.991   0.050   11.593  1.00 62.34  ?  11   GLY F CA  1 
ATOM   12723 C C   . GLY F  3  11  ? 5.313   0.221   10.866  1.00 63.06  ?  11   GLY F C   1 
ATOM   12724 O O   . GLY F  3  11  ? 6.369   0.390   11.480  1.00 63.54  ?  11   GLY F O   1 
ATOM   12725 N N   . GLY F  3  12  ? 5.247   0.174   9.537   1.00 63.45  ?  12   GLY F N   1 
ATOM   12726 C CA  . GLY F  3  12  ? 6.437   0.305   8.718   1.00 64.34  ?  12   GLY F CA  1 
ATOM   12727 C C   . GLY F  3  12  ? 6.500   1.620   7.971   1.00 64.10  ?  12   GLY F C   1 
ATOM   12728 O O   . GLY F  3  12  ? 5.480   2.296   7.801   1.00 63.56  ?  12   GLY F O   1 
ATOM   12729 N N   . ARG F  3  13  ? 7.689   1.999   7.521   1.00 64.76  ?  13   ARG F N   1 
ATOM   12730 C CA  . ARG F  3  13  ? 7.845   3.240   6.776   1.00 64.75  ?  13   ARG F CA  1 
ATOM   12731 C C   . ARG F  3  13  ? 7.798   2.987   5.267   1.00 65.74  ?  13   ARG F C   1 
ATOM   12732 O O   . ARG F  3  13  ? 6.960   3.548   4.554   1.00 65.81  ?  13   ARG F O   1 
ATOM   12733 C CB  . ARG F  3  13  ? 9.154   3.932   7.161   1.00 65.07  ?  13   ARG F CB  1 
ATOM   12734 C CG  . ARG F  3  13  ? 9.133   5.441   6.970   1.00 64.82  ?  13   ARG F CG  1 
ATOM   12735 C CD  . ARG F  3  13  ? 10.383  6.083   7.537   1.00 65.30  ?  13   ARG F CD  1 
ATOM   12736 N NE  . ARG F  3  13  ? 10.121  7.397   8.110   1.00 65.04  ?  13   ARG F NE  1 
ATOM   12737 C CZ  . ARG F  3  13  ? 10.732  8.514   7.737   1.00 65.58  ?  13   ARG F CZ  1 
ATOM   12738 N NH1 . ARG F  3  13  ? 11.649  8.516   6.782   1.00 66.26  ?  13   ARG F NH1 1 
ATOM   12739 N NH2 . ARG F  3  13  ? 10.419  9.657   8.343   1.00 65.69  ?  13   ARG F NH2 1 
HETATM 12740 C C1  . NAG G  4  .   ? -42.090 17.579  69.172  1.00 52.35  ?  1    NAG G C1  1 
HETATM 12741 C C2  . NAG G  4  .   ? -42.275 18.279  70.516  1.00 67.33  ?  1    NAG G C2  1 
HETATM 12742 C C3  . NAG G  4  .   ? -40.952 18.322  71.262  1.00 79.23  ?  1    NAG G C3  1 
HETATM 12743 C C4  . NAG G  4  .   ? -40.504 16.921  71.657  1.00 61.21  ?  1    NAG G C4  1 
HETATM 12744 C C5  . NAG G  4  .   ? -40.897 15.871  70.614  1.00 53.94  ?  1    NAG G C5  1 
HETATM 12745 C C6  . NAG G  4  .   ? -42.107 15.040  70.989  1.00 58.96  ?  1    NAG G C6  1 
HETATM 12746 C C7  . NAG G  4  .   ? -43.884 20.091  70.940  1.00 74.80  ?  1    NAG G C7  1 
HETATM 12747 C C8  . NAG G  4  .   ? -44.590 19.132  71.859  1.00 63.87  ?  1    NAG G C8  1 
HETATM 12748 N N2  . NAG G  4  .   ? -42.792 19.625  70.327  1.00 61.51  ?  1    NAG G N2  1 
HETATM 12749 O O3  . NAG G  4  .   ? -41.094 19.125  72.428  1.00 90.29  ?  1    NAG G O3  1 
HETATM 12750 O O4  . NAG G  4  .   ? -39.084 16.918  71.755  1.00 59.46  ?  1    NAG G O4  1 
HETATM 12751 O O5  . NAG G  4  .   ? -41.146 16.445  69.316  1.00 56.45  ?  1    NAG G O5  1 
HETATM 12752 O O6  . NAG G  4  .   ? -41.752 13.961  71.842  1.00 67.07  ?  1    NAG G O6  1 
HETATM 12753 O O7  . NAG G  4  .   ? -44.290 21.235  70.757  1.00 103.68 ?  1    NAG G O7  1 
HETATM 12754 C C1  . NAG G  4  .   ? -38.688 16.659  73.108  1.00 68.58  ?  2    NAG G C1  1 
HETATM 12755 C C2  . NAG G  4  .   ? -37.187 16.818  73.189  1.00 67.49  ?  2    NAG G C2  1 
HETATM 12756 C C3  . NAG G  4  .   ? -36.712 16.509  74.589  1.00 62.80  ?  2    NAG G C3  1 
HETATM 12757 C C4  . NAG G  4  .   ? -37.482 17.384  75.541  1.00 74.25  ?  2    NAG G C4  1 
HETATM 12758 C C5  . NAG G  4  .   ? -38.946 17.091  75.370  1.00 70.25  ?  2    NAG G C5  1 
HETATM 12759 C C6  . NAG G  4  .   ? -39.732 17.852  76.411  1.00 75.86  ?  2    NAG G C6  1 
HETATM 12760 C C7  . NAG G  4  .   ? -36.269 16.376  71.028  1.00 64.92  ?  2    NAG G C7  1 
HETATM 12761 C C8  . NAG G  4  .   ? -35.278 15.567  70.269  1.00 53.25  ?  2    NAG G C8  1 
HETATM 12762 N N2  . NAG G  4  .   ? -36.569 15.933  72.235  1.00 68.63  ?  2    NAG G N2  1 
HETATM 12763 O O3  . NAG G  4  .   ? -35.325 16.800  74.727  1.00 67.94  ?  2    NAG G O3  1 
HETATM 12764 O O5  . NAG G  4  .   ? -39.285 17.517  74.068  1.00 72.01  ?  2    NAG G O5  1 
HETATM 12765 O O6  . NAG G  4  .   ? -39.193 19.168  76.494  1.00 85.10  ?  2    NAG G O6  1 
HETATM 12766 O O7  . NAG G  4  .   ? -36.761 17.382  70.569  1.00 69.40  ?  2    NAG G O7  1 
HETATM 12767 C C1  . NAG H  5  .   ? -54.788 12.706  111.058 1.00 74.61  ?  1    NAG H C1  1 
HETATM 12768 C C2  . NAG H  5  .   ? -55.779 11.794  111.759 1.00 80.34  ?  1    NAG H C2  1 
HETATM 12769 C C3  . NAG H  5  .   ? -55.430 11.732  113.246 1.00 97.33  ?  1    NAG H C3  1 
HETATM 12770 C C4  . NAG H  5  .   ? -54.002 11.230  113.428 1.00 98.89  ?  1    NAG H C4  1 
HETATM 12771 C C5  . NAG H  5  .   ? -53.048 12.129  112.632 1.00 90.06  ?  1    NAG H C5  1 
HETATM 12772 C C6  . NAG H  5  .   ? -51.615 11.648  112.618 1.00 101.26 ?  1    NAG H C6  1 
HETATM 12773 C C7  . NAG H  5  .   ? -57.975 11.743  110.658 1.00 78.57  ?  1    NAG H C7  1 
HETATM 12774 C C8  . NAG H  5  .   ? -57.438 10.601  109.846 1.00 84.01  ?  1    NAG H C8  1 
HETATM 12775 N N2  . NAG H  5  .   ? -57.139 12.269  111.560 1.00 80.91  ?  1    NAG H N2  1 
HETATM 12776 O O3  . NAG H  5  .   ? -56.357 11.027  114.072 1.00 95.63  ?  1    NAG H O3  1 
HETATM 12777 O O4  . NAG H  5  .   ? -53.691 11.281  114.818 1.00 109.55 ?  1    NAG H O4  1 
HETATM 12778 O O5  . NAG H  5  .   ? -53.459 12.210  111.256 1.00 79.20  ?  1    NAG H O5  1 
HETATM 12779 O O6  . NAG H  5  .   ? -51.539 10.239  112.452 1.00 103.41 ?  1    NAG H O6  1 
HETATM 12780 O O7  . NAG H  5  .   ? -59.118 12.165  110.509 1.00 71.45  ?  1    NAG H O7  1 
HETATM 12781 C C1  . FUC H  5  .   ? -57.029 9.886   113.519 1.00 97.47  ?  2    FUC H C1  1 
HETATM 12782 C C2  . FUC H  5  .   ? -56.799 8.708   114.502 1.00 97.47  ?  2    FUC H C2  1 
HETATM 12783 C C3  . FUC H  5  .   ? -57.754 7.497   114.256 1.00 97.47  ?  2    FUC H C3  1 
HETATM 12784 C C4  . FUC H  5  .   ? -59.108 7.922   113.622 1.00 97.47  ?  2    FUC H C4  1 
HETATM 12785 C C5  . FUC H  5  .   ? -59.388 9.393   113.930 1.00 97.47  ?  2    FUC H C5  1 
HETATM 12786 C C6  . FUC H  5  .   ? -60.732 9.886   113.399 1.00 97.47  ?  2    FUC H C6  1 
HETATM 12787 O O2  . FUC H  5  .   ? -56.827 9.127   115.872 1.00 97.47  ?  2    FUC H O2  1 
HETATM 12788 O O3  . FUC H  5  .   ? -57.124 6.518   113.408 1.00 97.47  ?  2    FUC H O3  1 
HETATM 12789 O O4  . FUC H  5  .   ? -59.085 7.725   112.211 1.00 97.47  ?  2    FUC H O4  1 
HETATM 12790 O O5  . FUC H  5  .   ? -58.389 10.234  113.332 1.00 97.47  ?  2    FUC H O5  1 
HETATM 12791 C C1  . NAG H  5  .   ? -52.877 10.184  115.320 1.00 102.84 ?  3    NAG H C1  1 
HETATM 12792 C C2  . NAG H  5  .   ? -52.485 10.533  116.757 1.00 103.79 ?  3    NAG H C2  1 
HETATM 12793 C C3  . NAG H  5  .   ? -51.579 9.443   117.323 1.00 105.88 ?  3    NAG H C3  1 
HETATM 12794 C C4  . NAG H  5  .   ? -52.253 8.081   117.205 1.00 107.83 ?  3    NAG H C4  1 
HETATM 12795 C C5  . NAG H  5  .   ? -52.705 7.819   115.767 1.00 109.57 ?  3    NAG H C5  1 
HETATM 12796 C C6  . NAG H  5  .   ? -53.508 6.544   115.627 1.00 112.62 ?  3    NAG H C6  1 
HETATM 12797 C C7  . NAG H  5  .   ? -52.507 12.989  116.922 1.00 102.92 ?  3    NAG H C7  1 
HETATM 12798 C C8  . NAG H  5  .   ? -51.671 14.234  116.987 1.00 80.18  ?  3    NAG H C8  1 
HETATM 12799 N N2  . NAG H  5  .   ? -51.835 11.834  116.827 1.00 106.21 ?  3    NAG H N2  1 
HETATM 12800 O O3  . NAG H  5  .   ? -51.280 9.717   118.687 1.00 100.39 ?  3    NAG H O3  1 
HETATM 12801 O O4  . NAG H  5  .   ? -51.348 7.061   117.612 1.00 106.72 ?  3    NAG H O4  1 
HETATM 12802 O O5  . NAG H  5  .   ? -53.539 8.892   115.299 1.00 107.03 ?  3    NAG H O5  1 
HETATM 12803 O O6  . NAG H  5  .   ? -54.358 6.572   114.488 1.00 112.91 ?  3    NAG H O6  1 
HETATM 12804 O O7  . NAG H  5  .   ? -53.734 13.029  116.949 1.00 107.60 ?  3    NAG H O7  1 
HETATM 12805 C C1  . FUC H  5  .   ? -50.214 9.887   111.994 1.00 101.54 ?  4    FUC H C1  1 
HETATM 12806 C C2  . FUC H  5  .   ? -50.356 8.727   110.971 1.00 101.54 ?  4    FUC H C2  1 
HETATM 12807 C C3  . FUC H  5  .   ? -49.556 9.020   109.706 1.00 101.54 ?  4    FUC H C3  1 
HETATM 12808 C C4  . FUC H  5  .   ? -48.139 9.507   110.068 1.00 101.54 ?  4    FUC H C4  1 
HETATM 12809 C C5  . FUC H  5  .   ? -48.229 10.809  110.879 1.00 101.54 ?  4    FUC H C5  1 
HETATM 12810 C C6  . FUC H  5  .   ? -47.251 10.874  112.054 1.00 101.54 ?  4    FUC H C6  1 
HETATM 12811 O O2  . FUC H  5  .   ? -51.712 8.422   110.656 1.00 101.54 ?  4    FUC H O2  1 
HETATM 12812 O O3  . FUC H  5  .   ? -49.429 7.833   108.933 1.00 101.54 ?  4    FUC H O3  1 
HETATM 12813 O O4  . FUC H  5  .   ? -47.448 8.513   110.812 1.00 101.54 ?  4    FUC H O4  1 
HETATM 12814 O O5  . FUC H  5  .   ? -49.557 11.022  111.420 1.00 101.54 ?  4    FUC H O5  1 
HETATM 12815 C C1  . NAG I  4  .   ? -36.446 -15.885 62.537  1.00 74.66  ?  1    NAG I C1  1 
HETATM 12816 C C2  . NAG I  4  .   ? -37.444 -16.396 63.573  1.00 76.84  ?  1    NAG I C2  1 
HETATM 12817 C C3  . NAG I  4  .   ? -38.443 -17.359 62.920  1.00 78.82  ?  1    NAG I C3  1 
HETATM 12818 C C4  . NAG I  4  .   ? -39.054 -16.752 61.660  1.00 79.22  ?  1    NAG I C4  1 
HETATM 12819 C C5  . NAG I  4  .   ? -37.963 -16.181 60.755  1.00 80.23  ?  1    NAG I C5  1 
HETATM 12820 C C6  . NAG I  4  .   ? -38.506 -15.420 59.570  1.00 81.56  ?  1    NAG I C6  1 
HETATM 12821 C C7  . NAG I  4  .   ? -36.872 -16.634 65.952  1.00 76.31  ?  1    NAG I C7  1 
HETATM 12822 C C8  . NAG I  4  .   ? -36.083 -17.412 66.966  1.00 64.74  ?  1    NAG I C8  1 
HETATM 12823 N N2  . NAG I  4  .   ? -36.754 -17.038 64.681  1.00 74.64  ?  1    NAG I N2  1 
HETATM 12824 O O3  . NAG I  4  .   ? -39.474 -17.679 63.849  1.00 83.71  ?  1    NAG I O3  1 
HETATM 12825 O O4  . NAG I  4  .   ? -39.731 -17.762 60.918  1.00 90.10  ?  1    NAG I O4  1 
HETATM 12826 O O5  . NAG I  4  .   ? -37.137 -15.265 61.483  1.00 74.81  ?  1    NAG I O5  1 
HETATM 12827 O O6  . NAG I  4  .   ? -37.454 -14.985 58.721  1.00 83.55  ?  1    NAG I O6  1 
HETATM 12828 O O7  . NAG I  4  .   ? -37.584 -15.684 66.271  1.00 77.45  ?  1    NAG I O7  1 
HETATM 12829 C C1  . NAG I  4  .   ? -41.132 -17.903 61.221  1.00 83.13  ?  2    NAG I C1  1 
HETATM 12830 C C2  . NAG I  4  .   ? -41.934 -17.818 59.926  1.00 84.49  ?  2    NAG I C2  1 
HETATM 12831 C C3  . NAG I  4  .   ? -43.416 -18.028 60.210  1.00 86.48  ?  2    NAG I C3  1 
HETATM 12832 C C4  . NAG I  4  .   ? -43.631 -19.348 60.937  1.00 98.89  ?  2    NAG I C4  1 
HETATM 12833 C C5  . NAG I  4  .   ? -42.763 -19.412 62.192  1.00 94.16  ?  2    NAG I C5  1 
HETATM 12834 C C6  . NAG I  4  .   ? -42.810 -20.764 62.865  1.00 101.36 ?  2    NAG I C6  1 
HETATM 12835 C C7  . NAG I  4  .   ? -41.344 -16.476 57.961  1.00 84.28  ?  2    NAG I C7  1 
HETATM 12836 C C8  . NAG I  4  .   ? -41.189 -15.093 57.402  1.00 78.51  ?  2    NAG I C8  1 
HETATM 12837 N N2  . NAG I  4  .   ? -41.722 -16.553 59.242  1.00 85.66  ?  2    NAG I N2  1 
HETATM 12838 O O3  . NAG I  4  .   ? -44.130 -18.022 58.980  1.00 83.74  ?  2    NAG I O3  1 
HETATM 12839 O O4  . NAG I  4  .   ? -44.999 -19.492 61.303  1.00 99.61  ?  2    NAG I O4  1 
HETATM 12840 O O5  . NAG I  4  .   ? -41.385 -19.163 61.864  1.00 82.24  ?  2    NAG I O5  1 
HETATM 12841 O O6  . NAG I  4  .   ? -43.511 -21.715 62.075  1.00 102.06 ?  2    NAG I O6  1 
HETATM 12842 O O7  . NAG I  4  .   ? -41.130 -17.478 57.286  1.00 91.19  ?  2    NAG I O7  1 
HETATM 12843 C C1  . NAG J  4  .   ? -49.962 46.445  120.990 1.00 63.73  ?  1    NAG J C1  1 
HETATM 12844 C C2  . NAG J  4  .   ? -50.749 47.646  120.479 1.00 67.75  ?  1    NAG J C2  1 
HETATM 12845 C C3  . NAG J  4  .   ? -51.239 48.488  121.649 1.00 76.77  ?  1    NAG J C3  1 
HETATM 12846 C C4  . NAG J  4  .   ? -52.018 47.621  122.630 1.00 74.60  ?  1    NAG J C4  1 
HETATM 12847 C C5  . NAG J  4  .   ? -51.185 46.412  123.046 1.00 75.11  ?  1    NAG J C5  1 
HETATM 12848 C C6  . NAG J  4  .   ? -51.947 45.439  123.913 1.00 71.39  ?  1    NAG J C6  1 
HETATM 12849 C C7  . NAG J  4  .   ? -50.193 48.511  118.257 1.00 70.22  ?  1    NAG J C7  1 
HETATM 12850 C C8  . NAG J  4  .   ? -49.273 49.383  117.461 1.00 65.52  ?  1    NAG J C8  1 
HETATM 12851 N N2  . NAG J  4  .   ? -49.948 48.447  119.569 1.00 69.09  ?  1    NAG J N2  1 
HETATM 12852 O O3  . NAG J  4  .   ? -52.065 49.535  121.151 1.00 82.81  ?  1    NAG J O3  1 
HETATM 12853 O O4  . NAG J  4  .   ? -52.387 48.368  123.784 1.00 74.43  ?  1    NAG J O4  1 
HETATM 12854 O O5  . NAG J  4  .   ? -50.773 45.686  121.880 1.00 68.54  ?  1    NAG J O5  1 
HETATM 12855 O O6  . NAG J  4  .   ? -53.160 45.046  123.286 1.00 51.34  ?  1    NAG J O6  1 
HETATM 12856 O O7  . NAG J  4  .   ? -51.118 47.893  117.738 1.00 77.95  ?  1    NAG J O7  1 
HETATM 12857 C C1  . NAG J  4  .   ? -53.827 48.472  123.732 1.00 94.84  ?  2    NAG J C1  1 
HETATM 12858 C C2  . NAG J  4  .   ? -54.384 48.972  125.064 1.00 100.66 ?  2    NAG J C2  1 
HETATM 12859 C C3  . NAG J  4  .   ? -55.902 49.101  124.971 1.00 84.62  ?  2    NAG J C3  1 
HETATM 12860 C C4  . NAG J  4  .   ? -56.293 49.972  123.781 1.00 80.72  ?  2    NAG J C4  1 
HETATM 12861 C C5  . NAG J  4  .   ? -55.634 49.464  122.499 1.00 83.83  ?  2    NAG J C5  1 
HETATM 12862 C C6  . NAG J  4  .   ? -55.870 50.365  121.303 1.00 76.23  ?  2    NAG J C6  1 
HETATM 12863 C C7  . NAG J  4  .   ? -52.854 48.202  126.825 1.00 92.53  ?  2    NAG J C7  1 
HETATM 12864 C C8  . NAG J  4  .   ? -52.629 47.205  127.923 1.00 86.03  ?  2    NAG J C8  1 
HETATM 12865 N N2  . NAG J  4  .   ? -54.008 48.089  126.157 1.00 103.64 ?  2    NAG J N2  1 
HETATM 12866 O O3  . NAG J  4  .   ? -56.412 49.647  126.183 1.00 78.07  ?  2    NAG J O3  1 
HETATM 12867 O O4  . NAG J  4  .   ? -57.704 49.947  123.603 1.00 86.05  ?  2    NAG J O4  1 
HETATM 12868 O O5  . NAG J  4  .   ? -54.212 49.376  122.679 1.00 90.47  ?  2    NAG J O5  1 
HETATM 12869 O O6  . NAG J  4  .   ? -55.125 49.954  120.162 1.00 67.33  ?  2    NAG J O6  1 
HETATM 12870 O O7  . NAG J  4  .   ? -52.029 49.068  126.555 1.00 89.10  ?  2    NAG J O7  1 
HETATM 12871 C C1  . NAG K  4  .   ? -39.811 38.202  104.655 1.00 76.21  ?  1    NAG K C1  1 
HETATM 12872 C C2  . NAG K  4  .   ? -40.018 39.427  103.782 1.00 85.49  ?  1    NAG K C2  1 
HETATM 12873 C C3  . NAG K  4  .   ? -39.818 39.061  102.317 1.00 96.67  ?  1    NAG K C3  1 
HETATM 12874 C C4  . NAG K  4  .   ? -38.452 38.415  102.109 1.00 96.48  ?  1    NAG K C4  1 
HETATM 12875 C C5  . NAG K  4  .   ? -38.223 37.273  103.103 1.00 83.38  ?  1    NAG K C5  1 
HETATM 12876 C C6  . NAG K  4  .   ? -36.798 36.773  103.101 1.00 88.41  ?  1    NAG K C6  1 
HETATM 12877 C C7  . NAG K  4  .   ? -41.536 41.033  104.849 1.00 78.63  ?  1    NAG K C7  1 
HETATM 12878 C C8  . NAG K  4  .   ? -42.940 41.555  104.922 1.00 71.11  ?  1    NAG K C8  1 
HETATM 12879 N N2  . NAG K  4  .   ? -41.326 40.030  103.988 1.00 83.54  ?  1    NAG K N2  1 
HETATM 12880 O O3  . NAG K  4  .   ? -39.936 40.243  101.533 1.00 97.06  ?  1    NAG K O3  1 
HETATM 12881 O O4  . NAG K  4  .   ? -38.381 37.863  100.798 1.00 105.05 ?  1    NAG K O4  1 
HETATM 12882 O O5  . NAG K  4  .   ? -38.497 37.691  104.449 1.00 78.70  ?  1    NAG K O5  1 
HETATM 12883 O O6  . NAG K  4  .   ? -36.286 36.703  104.425 1.00 84.04  ?  1    NAG K O6  1 
HETATM 12884 O O7  . NAG K  4  .   ? -40.632 41.493  105.544 1.00 70.04  ?  1    NAG K O7  1 
HETATM 12885 C C1  . NAG K  4  .   ? -37.798 38.790  99.855  1.00 103.94 ?  2    NAG K C1  1 
HETATM 12886 C C2  . NAG K  4  .   ? -37.253 37.985  98.704  1.00 106.23 ?  2    NAG K C2  1 
HETATM 12887 C C3  . NAG K  4  .   ? -36.560 38.916  97.728  1.00 110.16 ?  2    NAG K C3  1 
HETATM 12888 C C4  . NAG K  4  .   ? -37.549 39.965  97.233  1.00 113.85 ?  2    NAG K C4  1 
HETATM 12889 C C5  . NAG K  4  .   ? -38.298 40.651  98.385  1.00 110.77 ?  2    NAG K C5  1 
HETATM 12890 C C6  . NAG K  4  .   ? -39.523 41.391  97.901  1.00 107.30 ?  2    NAG K C6  1 
HETATM 12891 C C7  . NAG K  4  .   ? -36.709 35.643  99.162  1.00 115.93 ?  2    NAG K C7  1 
HETATM 12892 C C8  . NAG K  4  .   ? -38.086 35.332  98.652  1.00 104.93 ?  2    NAG K C8  1 
HETATM 12893 N N2  . NAG K  4  .   ? -36.358 36.934  99.159  1.00 116.13 ?  2    NAG K N2  1 
HETATM 12894 O O3  . NAG K  4  .   ? -36.053 38.167  96.629  1.00 94.66  ?  2    NAG K O3  1 
HETATM 12895 O O4  . NAG K  4  .   ? -36.861 40.960  96.482  1.00 109.54 ?  2    NAG K O4  1 
HETATM 12896 O O5  . NAG K  4  .   ? -38.771 39.709  99.366  1.00 109.59 ?  2    NAG K O5  1 
HETATM 12897 O O6  . NAG K  4  .   ? -40.530 40.481  97.478  1.00 107.31 ?  2    NAG K O6  1 
HETATM 12898 O O7  . NAG K  4  .   ? -35.949 34.765  99.555  1.00 111.22 ?  2    NAG K O7  1 
HETATM 12899 C C1  . NAG L  4  .   ? -57.295 29.051  55.485  1.00 94.95  ?  1    NAG L C1  1 
HETATM 12900 C C2  . NAG L  4  .   ? -58.764 29.432  55.699  1.00 99.28  ?  1    NAG L C2  1 
HETATM 12901 C C3  . NAG L  4  .   ? -59.216 30.475  54.680  1.00 102.65 ?  1    NAG L C3  1 
HETATM 12902 C C4  . NAG L  4  .   ? -58.467 31.783  54.890  1.00 101.95 ?  1    NAG L C4  1 
HETATM 12903 C C5  . NAG L  4  .   ? -56.989 31.543  55.226  1.00 100.77 ?  1    NAG L C5  1 
HETATM 12904 C C6  . NAG L  4  .   ? -56.624 31.842  56.666  1.00 90.19  ?  1    NAG L C6  1 
HETATM 12905 C C7  . NAG L  4  .   ? -59.908 27.353  54.788  1.00 97.08  ?  1    NAG L C7  1 
HETATM 12906 C C8  . NAG L  4  .   ? -59.199 27.497  53.464  1.00 89.96  ?  1    NAG L C8  1 
HETATM 12907 N N2  . NAG L  4  .   ? -59.662 28.277  55.743  1.00 99.85  ?  1    NAG L N2  1 
HETATM 12908 O O3  . NAG L  4  .   ? -60.617 30.696  54.806  1.00 101.39 ?  1    NAG L O3  1 
HETATM 12909 O O4  . NAG L  4  .   ? -58.551 32.526  53.673  1.00 110.30 ?  1    NAG L O4  1 
HETATM 12910 O O5  . NAG L  4  .   ? -56.552 30.199  54.933  1.00 104.05 ?  1    NAG L O5  1 
HETATM 12911 O O6  . NAG L  4  .   ? -55.451 32.640  56.746  1.00 82.76  ?  1    NAG L O6  1 
HETATM 12912 O O7  . NAG L  4  .   ? -60.692 26.430  54.990  1.00 105.30 ?  1    NAG L O7  1 
HETATM 12913 C C1  . NAG L  4  .   ? -58.518 33.983  53.744  1.00 108.98 ?  2    NAG L C1  1 
HETATM 12914 C C2  . NAG L  4  .   ? -59.800 34.522  54.392  1.00 107.18 ?  2    NAG L C2  1 
HETATM 12915 C C3  . NAG L  4  .   ? -59.761 36.049  54.440  1.00 107.24 ?  2    NAG L C3  1 
HETATM 12916 C C4  . NAG L  4  .   ? -58.478 36.536  55.103  1.00 112.01 ?  2    NAG L C4  1 
HETATM 12917 C C5  . NAG L  4  .   ? -57.253 35.912  54.435  1.00 111.88 ?  2    NAG L C5  1 
HETATM 12918 C C6  . NAG L  4  .   ? -55.953 36.266  55.121  1.00 104.13 ?  2    NAG L C6  1 
HETATM 12919 C C7  . NAG L  4  .   ? -62.205 34.026  54.221  1.00 117.18 ?  2    NAG L C7  1 
HETATM 12920 C C8  . NAG L  4  .   ? -63.302 33.518  53.333  1.00 109.97 ?  2    NAG L C8  1 
HETATM 12921 N N2  . NAG L  4  .   ? -60.982 34.060  53.680  1.00 112.39 ?  2    NAG L N2  1 
HETATM 12922 O O3  . NAG L  4  .   ? -60.892 36.544  55.146  1.00 106.13 ?  2    NAG L O3  1 
HETATM 12923 O O4  . NAG L  4  .   ? -58.391 37.954  55.006  1.00 110.27 ?  2    NAG L O4  1 
HETATM 12924 O O5  . NAG L  4  .   ? -57.358 34.481  54.459  1.00 112.18 ?  2    NAG L O5  1 
HETATM 12925 O O6  . NAG L  4  .   ? -55.603 37.627  54.911  1.00 94.70  ?  2    NAG L O6  1 
HETATM 12926 O O7  . NAG L  4  .   ? -62.418 34.391  55.374  1.00 120.73 ?  2    NAG L O7  1 
HETATM 12927 C C1  . NAG M  6  .   ? -18.572 8.665   54.497  1.00 99.58  ?  1    NAG M C1  1 
HETATM 12928 C C2  . NAG M  6  .   ? -18.368 8.872   52.992  1.00 102.85 ?  1    NAG M C2  1 
HETATM 12929 C C3  . NAG M  6  .   ? -16.883 8.770   52.635  1.00 114.15 ?  1    NAG M C3  1 
HETATM 12930 C C4  . NAG M  6  .   ? -16.029 9.672   53.521  1.00 112.16 ?  1    NAG M C4  1 
HETATM 12931 C C5  . NAG M  6  .   ? -16.359 9.438   54.999  1.00 106.78 ?  1    NAG M C5  1 
HETATM 12932 C C6  . NAG M  6  .   ? -15.662 10.401  55.938  1.00 101.21 ?  1    NAG M C6  1 
HETATM 12933 C C7  . NAG M  6  .   ? -20.178 8.235   51.451  1.00 103.62 ?  1    NAG M C7  1 
HETATM 12934 C C8  . NAG M  6  .   ? -20.846 7.104   50.731  1.00 82.82  ?  1    NAG M C8  1 
HETATM 12935 N N2  . NAG M  6  .   ? -19.139 7.905   52.225  1.00 108.27 ?  1    NAG M N2  1 
HETATM 12936 O O3  . NAG M  6  .   ? -16.697 9.117   51.266  1.00 129.42 ?  1    NAG M O3  1 
HETATM 12937 O O4  . NAG M  6  .   ? -14.660 9.358   53.275  1.00 107.67 ?  1    NAG M O4  1 
HETATM 12938 O O5  . NAG M  6  .   ? -17.769 9.595   55.221  1.00 99.22  ?  1    NAG M O5  1 
HETATM 12939 O O6  . NAG M  6  .   ? -16.571 11.061  56.809  1.00 77.06  ?  1    NAG M O6  1 
HETATM 12940 O O7  . NAG M  6  .   ? -20.564 9.393   51.340  1.00 100.85 ?  1    NAG M O7  1 
HETATM 12941 C C1  . NAG M  6  .   ? -13.776 10.508  53.168  1.00 116.86 ?  2    NAG M C1  1 
HETATM 12942 C C2  . NAG M  6  .   ? -12.351 9.984   52.965  1.00 116.86 ?  2    NAG M C2  1 
HETATM 12943 C C3  . NAG M  6  .   ? -11.371 11.151  52.880  1.00 116.86 ?  2    NAG M C3  1 
HETATM 12944 C C4  . NAG M  6  .   ? -11.805 12.122  51.788  1.00 116.86 ?  2    NAG M C4  1 
HETATM 12945 C C5  . NAG M  6  .   ? -13.261 12.551  51.990  1.00 116.86 ?  2    NAG M C5  1 
HETATM 12946 C C6  . NAG M  6  .   ? -13.788 13.390  50.847  1.00 116.86 ?  2    NAG M C6  1 
HETATM 12947 C C7  . NAG M  6  .   ? -11.858 9.343   55.306  1.00 116.86 ?  2    NAG M C7  1 
HETATM 12948 C C8  . NAG M  6  .   ? -11.435 8.219   56.204  1.00 116.86 ?  2    NAG M C8  1 
HETATM 12949 N N2  . NAG M  6  .   ? -11.960 9.042   54.005  1.00 116.86 ?  2    NAG M N2  1 
HETATM 12950 O O3  . NAG M  6  .   ? -10.060 10.667  52.609  1.00 116.86 ?  2    NAG M O3  1 
HETATM 12951 O O4  . NAG M  6  .   ? -10.961 13.268  51.795  1.00 116.86 ?  2    NAG M O4  1 
HETATM 12952 O O5  . NAG M  6  .   ? -14.120 11.402  52.086  1.00 116.86 ?  2    NAG M O5  1 
HETATM 12953 O O6  . NAG M  6  .   ? -14.448 14.558  51.316  1.00 116.86 ?  2    NAG M O6  1 
HETATM 12954 O O7  . NAG M  6  .   ? -12.095 10.467  55.742  1.00 116.86 ?  2    NAG M O7  1 
HETATM 12955 C C1  . FUC M  6  .   ? -16.714 12.457  56.441  1.00 100.59 ?  3    FUC M C1  1 
HETATM 12956 C C2  . FUC M  6  .   ? -16.584 13.299  57.739  1.00 100.59 ?  3    FUC M C2  1 
HETATM 12957 C C3  . FUC M  6  .   ? -16.204 14.773  57.444  1.00 100.59 ?  3    FUC M C3  1 
HETATM 12958 C C4  . FUC M  6  .   ? -16.553 15.196  55.991  1.00 100.59 ?  3    FUC M C4  1 
HETATM 12959 C C5  . FUC M  6  .   ? -15.877 14.244  54.967  1.00 100.59 ?  3    FUC M C5  1 
HETATM 12960 C C6  . FUC M  6  .   ? -16.600 14.171  53.625  1.00 100.59 ?  3    FUC M C6  1 
HETATM 12961 O O2  . FUC M  6  .   ? -15.667 12.712  58.659  1.00 100.59 ?  3    FUC M O2  1 
HETATM 12962 O O3  . FUC M  6  .   ? -16.896 15.653  58.334  1.00 100.59 ?  3    FUC M O3  1 
HETATM 12963 O O4  . FUC M  6  .   ? -17.969 15.243  55.798  1.00 100.59 ?  3    FUC M O4  1 
HETATM 12964 O O5  . FUC M  6  .   ? -15.749 12.873  55.461  1.00 100.59 ?  3    FUC M O5  1 
HETATM 12965 C C1  . NAG N  7  .   ? 5.011   -4.916  2.241   1.00 55.19  ?  1    NAG N C1  1 
HETATM 12966 C C2  . NAG N  7  .   ? 4.031   -5.648  3.129   1.00 57.53  ?  1    NAG N C2  1 
HETATM 12967 C C3  . NAG N  7  .   ? 2.666   -5.623  2.491   1.00 58.72  ?  1    NAG N C3  1 
HETATM 12968 C C4  . NAG N  7  .   ? 2.138   -4.221  2.300   1.00 58.36  ?  1    NAG N C4  1 
HETATM 12969 C C5  . NAG N  7  .   ? 3.251   -3.218  2.034   1.00 53.80  ?  1    NAG N C5  1 
HETATM 12970 C C6  . NAG N  7  .   ? 3.630   -2.454  3.294   1.00 53.64  ?  1    NAG N C6  1 
HETATM 12971 C C7  . NAG N  7  .   ? 4.698   -7.572  4.416   1.00 54.38  ?  1    NAG N C7  1 
HETATM 12972 C C8  . NAG N  7  .   ? 4.617   -6.668  5.603   1.00 52.86  ?  1    NAG N C8  1 
HETATM 12973 N N2  . NAG N  7  .   ? 4.415   -7.028  3.251   1.00 53.26  ?  1    NAG N N2  1 
HETATM 12974 O O3  . NAG N  7  .   ? 1.770   -6.309  3.358   1.00 73.26  ?  1    NAG N O3  1 
HETATM 12975 O O4  . NAG N  7  .   ? 1.292   -4.272  1.161   1.00 56.36  ?  1    NAG N O4  1 
HETATM 12976 O O5  . NAG N  7  .   ? 4.415   -3.857  1.505   1.00 55.78  ?  1    NAG N O5  1 
HETATM 12977 O O6  . NAG N  7  .   ? 2.557   -1.579  3.630   1.00 53.89  ?  1    NAG N O6  1 
HETATM 12978 O O7  . NAG N  7  .   ? 4.997   -8.738  4.508   1.00 54.80  ?  1    NAG N O7  1 
HETATM 12979 C C1  . NAG N  7  .   ? -0.059  -3.886  1.465   1.00 59.42  ?  2    NAG N C1  1 
HETATM 12980 C C2  . NAG N  7  .   ? -0.964  -4.455  0.393   1.00 61.32  ?  2    NAG N C2  1 
HETATM 12981 C C3  . NAG N  7  .   ? -2.318  -3.807  0.566   1.00 56.26  ?  2    NAG N C3  1 
HETATM 12982 C C4  . NAG N  7  .   ? -2.824  -4.399  1.850   1.00 65.34  ?  2    NAG N C4  1 
HETATM 12983 C C5  . NAG N  7  .   ? -1.894  -3.982  2.966   1.00 61.77  ?  2    NAG N C5  1 
HETATM 12984 C C6  . NAG N  7  .   ? -2.340  -4.652  4.240   1.00 64.80  ?  2    NAG N C6  1 
HETATM 12985 C C7  . NAG N  7  .   ? 0.075   -3.210  -1.468  1.00 63.69  ?  2    NAG N C7  1 
HETATM 12986 C C8  . NAG N  7  .   ? 0.955   -3.456  -2.648  1.00 51.77  ?  2    NAG N C8  1 
HETATM 12987 N N2  . NAG N  7  .   ? -0.431  -4.305  -0.949  1.00 64.72  ?  2    NAG N N2  1 
HETATM 12988 O O3  . NAG N  7  .   ? -3.200  -4.142  -0.490  1.00 62.81  ?  2    NAG N O3  1 
HETATM 12989 O O4  . NAG N  7  .   ? -4.155  -3.959  2.101   1.00 76.12  ?  2    NAG N O4  1 
HETATM 12990 O O5  . NAG N  7  .   ? -0.574  -4.413  2.680   1.00 61.27  ?  2    NAG N O5  1 
HETATM 12991 O O6  . NAG N  7  .   ? -2.467  -6.039  3.951   1.00 73.81  ?  2    NAG N O6  1 
HETATM 12992 O O7  . NAG N  7  .   ? -0.169  -2.103  -1.038  1.00 66.46  ?  2    NAG N O7  1 
HETATM 12993 C C1  . BMA N  7  .   ? -4.938  -5.147  2.267   1.00 79.03  ?  3    BMA N C1  1 
HETATM 12994 C C2  . BMA N  7  .   ? -6.082  -4.871  3.208   1.00 79.03  ?  3    BMA N C2  1 
HETATM 12995 C C3  . BMA N  7  .   ? -7.183  -4.300  2.379   1.00 79.03  ?  3    BMA N C3  1 
HETATM 12996 C C4  . BMA N  7  .   ? -7.764  -5.418  1.548   1.00 79.03  ?  3    BMA N C4  1 
HETATM 12997 C C5  . BMA N  7  .   ? -6.648  -6.369  1.173   1.00 79.03  ?  3    BMA N C5  1 
HETATM 12998 C C6  . BMA N  7  .   ? -6.958  -7.053  -0.142  1.00 79.03  ?  3    BMA N C6  1 
HETATM 12999 O O2  . BMA N  7  .   ? -5.690  -3.885  4.144   1.00 79.03  ?  3    BMA N O2  1 
HETATM 13000 O O3  . BMA N  7  .   ? -6.589  -3.310  1.544   1.00 79.03  ?  3    BMA N O3  1 
HETATM 13001 O O4  . BMA N  7  .   ? -8.745  -6.103  2.322   1.00 79.03  ?  3    BMA N O4  1 
HETATM 13002 O O5  . BMA N  7  .   ? -5.449  -5.625  1.027   1.00 79.03  ?  3    BMA N O5  1 
HETATM 13003 O O6  . BMA N  7  .   ? -7.286  -6.053  -1.107  1.00 79.03  ?  3    BMA N O6  1 
HETATM 13004 C C1  . NAG O  6  .   ? -21.392 0.046   36.972  1.00 68.54  ?  1    NAG O C1  1 
HETATM 13005 C C2  . NAG O  6  .   ? -21.217 1.403   37.642  1.00 70.16  ?  1    NAG O C2  1 
HETATM 13006 C C3  . NAG O  6  .   ? -22.487 1.796   38.399  1.00 80.28  ?  1    NAG O C3  1 
HETATM 13007 C C4  . NAG O  6  .   ? -23.686 1.774   37.457  1.00 85.26  ?  1    NAG O C4  1 
HETATM 13008 C C5  . NAG O  6  .   ? -23.767 0.440   36.697  1.00 81.27  ?  1    NAG O C5  1 
HETATM 13009 C C6  . NAG O  6  .   ? -24.787 0.450   35.578  1.00 82.53  ?  1    NAG O C6  1 
HETATM 13010 C C7  . NAG O  6  .   ? -19.672 0.780   39.561  1.00 72.30  ?  1    NAG O C7  1 
HETATM 13011 C C8  . NAG O  6  .   ? -20.652 -0.250  40.064  1.00 74.40  ?  1    NAG O C8  1 
HETATM 13012 N N2  . NAG O  6  .   ? -20.013 1.497   38.469  1.00 67.34  ?  1    NAG O N2  1 
HETATM 13013 O O3  . NAG O  6  .   ? -22.352 3.079   39.004  1.00 81.15  ?  1    NAG O O3  1 
HETATM 13014 O O4  . NAG O  6  .   ? -24.862 1.945   38.243  1.00 100.63 ?  1    NAG O O4  1 
HETATM 13015 O O5  . NAG O  6  .   ? -22.511 0.094   36.087  1.00 64.37  ?  1    NAG O O5  1 
HETATM 13016 O O6  . NAG O  6  .   ? -24.183 0.478   34.291  1.00 82.18  ?  1    NAG O O6  1 
HETATM 13017 O O7  . NAG O  6  .   ? -18.605 0.972   40.134  1.00 71.67  ?  1    NAG O O7  1 
HETATM 13018 C C1  . NAG O  6  .   ? -25.836 2.865   37.691  1.00 94.74  ?  2    NAG O C1  1 
HETATM 13019 C C2  . NAG O  6  .   ? -27.210 2.299   38.029  1.00 96.69  ?  2    NAG O C2  1 
HETATM 13020 C C3  . NAG O  6  .   ? -28.301 3.203   37.466  1.00 109.05 ?  2    NAG O C3  1 
HETATM 13021 C C4  . NAG O  6  .   ? -28.112 4.635   37.954  1.00 111.44 ?  2    NAG O C4  1 
HETATM 13022 C C5  . NAG O  6  .   ? -26.688 5.117   37.662  1.00 103.31 ?  2    NAG O C5  1 
HETATM 13023 C C6  . NAG O  6  .   ? -26.384 6.472   38.260  1.00 104.25 ?  2    NAG O C6  1 
HETATM 13024 C C7  . NAG O  6  .   ? -27.335 -0.140  38.329  1.00 102.55 ?  2    NAG O C7  1 
HETATM 13025 C C8  . NAG O  6  .   ? -27.152 0.124   39.795  1.00 101.82 ?  2    NAG O C8  1 
HETATM 13026 N N2  . NAG O  6  .   ? -27.358 0.939   37.535  1.00 95.87  ?  2    NAG O N2  1 
HETATM 13027 O O3  . NAG O  6  .   ? -29.569 2.706   37.877  1.00 102.95 ?  2    NAG O O3  1 
HETATM 13028 O O5  . NAG O  6  .   ? -25.725 4.201   38.210  1.00 99.62  ?  2    NAG O O5  1 
HETATM 13029 O O6  . NAG O  6  .   ? -25.128 6.482   38.926  1.00 100.56 ?  2    NAG O O6  1 
HETATM 13030 O O7  . NAG O  6  .   ? -27.460 -1.278  37.886  1.00 86.85  ?  2    NAG O O7  1 
HETATM 13031 C C1  . FUC O  6  .   ? -23.974 1.850   33.863  1.00 88.60  ?  3    FUC O C1  1 
HETATM 13032 C C2  . FUC O  6  .   ? -23.736 1.890   32.316  1.00 88.60  ?  3    FUC O C2  1 
HETATM 13033 C C3  . FUC O  6  .   ? -24.516 3.039   31.664  1.00 88.60  ?  3    FUC O C3  1 
HETATM 13034 C C4  . FUC O  6  .   ? -24.409 4.323   32.502  1.00 88.60  ?  3    FUC O C4  1 
HETATM 13035 C C5  . FUC O  6  .   ? -24.944 4.070   33.919  1.00 88.60  ?  3    FUC O C5  1 
HETATM 13036 C C6  . FUC O  6  .   ? -24.053 4.664   35.012  1.00 88.60  ?  3    FUC O C6  1 
HETATM 13037 O O2  . FUC O  6  .   ? -24.022 0.654   31.671  1.00 88.60  ?  3    FUC O O2  1 
HETATM 13038 O O3  . FUC O  6  .   ? -23.972 3.314   30.382  1.00 88.60  ?  3    FUC O O3  1 
HETATM 13039 O O4  . FUC O  6  .   ? -23.061 4.765   32.569  1.00 88.60  ?  3    FUC O O4  1 
HETATM 13040 O O5  . FUC O  6  .   ? -25.082 2.656   34.214  1.00 88.60  ?  3    FUC O O5  1 
HETATM 13041 C C1  . BMA P  8  .   ? -30.145 6.377   38.607  1.00 120.09 ?  1    BMA P C1  1 
HETATM 13042 C C2  . BMA P  8  .   ? -30.032 7.887   38.385  1.00 120.09 ?  1    BMA P C2  1 
HETATM 13043 C C3  . BMA P  8  .   ? -30.863 8.612   39.449  1.00 120.09 ?  1    BMA P C3  1 
HETATM 13044 C C4  . BMA P  8  .   ? -32.289 8.053   39.419  1.00 120.09 ?  1    BMA P C4  1 
HETATM 13045 C C5  . BMA P  8  .   ? -32.232 6.531   39.564  1.00 120.09 ?  1    BMA P C5  1 
HETATM 13046 C C6  . BMA P  8  .   ? -33.654 5.967   39.571  1.00 120.09 ?  1    BMA P C6  1 
HETATM 13047 O O1  . BMA P  8  .   ? -29.347 5.694   37.638  1.00 120.09 ?  1    BMA P O1  1 
HETATM 13048 O O2  . BMA P  8  .   ? -30.521 8.217   37.086  1.00 120.09 ?  1    BMA P O2  1 
HETATM 13049 O O3  . BMA P  8  .   ? -30.886 10.012  39.167  1.00 120.09 ?  1    BMA P O3  1 
HETATM 13050 O O4  . BMA P  8  .   ? -33.043 8.609   40.498  1.00 120.09 ?  1    BMA P O4  1 
HETATM 13051 O O5  . BMA P  8  .   ? -31.504 5.969   38.474  1.00 120.09 ?  1    BMA P O5  1 
HETATM 13052 O O6  . BMA P  8  .   ? -33.602 4.546   39.711  1.00 120.09 ?  1    BMA P O6  1 
HETATM 13053 C C1  . MAN P  8  .   ? -29.685 10.814  39.332  1.00 128.11 ?  2    MAN P C1  1 
HETATM 13054 C C2  . MAN P  8  .   ? -30.073 12.282  39.204  1.00 128.11 ?  2    MAN P C2  1 
HETATM 13055 C C3  . MAN P  8  .   ? -28.826 13.122  38.961  1.00 128.11 ?  2    MAN P C3  1 
HETATM 13056 C C4  . MAN P  8  .   ? -27.587 12.364  39.419  1.00 128.11 ?  2    MAN P C4  1 
HETATM 13057 C C5  . MAN P  8  .   ? -27.442 11.067  38.634  1.00 128.11 ?  2    MAN P C5  1 
HETATM 13058 C C6  . MAN P  8  .   ? -26.710 10.004  39.440  1.00 128.11 ?  2    MAN P C6  1 
HETATM 13059 O O2  . MAN P  8  .   ? -30.736 12.727  40.392  1.00 128.11 ?  2    MAN P O2  1 
HETATM 13060 O O3  . MAN P  8  .   ? -28.929 14.361  39.669  1.00 128.11 ?  2    MAN P O3  1 
HETATM 13061 O O4  . MAN P  8  .   ? -26.422 13.175  39.231  1.00 128.11 ?  2    MAN P O4  1 
HETATM 13062 O O5  . MAN P  8  .   ? -28.735 10.581  38.292  1.00 128.11 ?  2    MAN P O5  1 
HETATM 13063 O O6  . MAN P  8  .   ? -25.600 9.526   38.673  1.00 128.11 ?  2    MAN P O6  1 
HETATM 13064 C C1  . NAG Q  4  .   ? 7.865   28.172  -5.448  1.00 65.76  ?  1    NAG Q C1  1 
HETATM 13065 C C2  . NAG Q  4  .   ? 9.327   28.361  -5.893  1.00 59.30  ?  1    NAG Q C2  1 
HETATM 13066 C C3  . NAG Q  4  .   ? 10.162  28.912  -4.739  1.00 63.12  ?  1    NAG Q C3  1 
HETATM 13067 C C4  . NAG Q  4  .   ? 9.526   30.125  -4.074  1.00 71.17  ?  1    NAG Q C4  1 
HETATM 13068 C C5  . NAG Q  4  .   ? 8.057   29.860  -3.745  1.00 69.30  ?  1    NAG Q C5  1 
HETATM 13069 C C6  . NAG Q  4  .   ? 7.345   31.087  -3.219  1.00 82.27  ?  1    NAG Q C6  1 
HETATM 13070 C C7  . NAG Q  4  .   ? 11.077  27.057  -6.995  1.00 83.92  ?  1    NAG Q C7  1 
HETATM 13071 C C8  . NAG Q  4  .   ? 11.612  25.687  -7.291  1.00 67.54  ?  1    NAG Q C8  1 
HETATM 13072 N N2  . NAG Q  4  .   ? 9.919   27.107  -6.327  1.00 72.28  ?  1    NAG Q N2  1 
HETATM 13073 O O3  . NAG Q  4  .   ? 11.465  29.217  -5.228  1.00 61.07  ?  1    NAG Q O3  1 
HETATM 13074 O O4  . NAG Q  4  .   ? 10.176  30.342  -2.823  1.00 74.66  ?  1    NAG Q O4  1 
HETATM 13075 O O5  . NAG Q  4  .   ? 7.350   29.423  -4.917  1.00 69.95  ?  1    NAG Q O5  1 
HETATM 13076 O O6  . NAG Q  4  .   ? 7.633   31.320  -1.846  1.00 79.94  ?  1    NAG Q O6  1 
HETATM 13077 O O7  . NAG Q  4  .   ? 11.658  28.080  -7.361  1.00 84.43  ?  1    NAG Q O7  1 
HETATM 13078 C C1  . NAG Q  4  .   ? 11.515  30.889  -2.823  1.00 73.37  ?  2    NAG Q C1  1 
HETATM 13079 C C2  . NAG Q  4  .   ? 11.767  31.558  -1.460  1.00 80.48  ?  2    NAG Q C2  1 
HETATM 13080 C C3  . NAG Q  4  .   ? 13.224  32.017  -1.325  1.00 79.82  ?  2    NAG Q C3  1 
HETATM 13081 C C4  . NAG Q  4  .   ? 14.185  30.888  -1.666  1.00 80.31  ?  2    NAG Q C4  1 
HETATM 13082 C C5  . NAG Q  4  .   ? 13.851  30.348  -3.049  1.00 73.16  ?  2    NAG Q C5  1 
HETATM 13083 C C6  . NAG Q  4  .   ? 14.718  29.183  -3.463  1.00 68.76  ?  2    NAG Q C6  1 
HETATM 13084 C C7  . NAG Q  4  .   ? 10.805  33.769  -2.019  1.00 81.75  ?  2    NAG Q C7  1 
HETATM 13085 C C8  . NAG Q  4  .   ? 9.796   34.803  -1.619  1.00 75.49  ?  2    NAG Q C8  1 
HETATM 13086 N N2  . NAG Q  4  .   ? 10.857  32.674  -1.246  1.00 83.74  ?  2    NAG Q N2  1 
HETATM 13087 O O3  . NAG Q  4  .   ? 13.463  32.471  0.002   1.00 76.33  ?  2    NAG Q O3  1 
HETATM 13088 O O4  . NAG Q  4  .   ? 15.525  31.367  -1.654  1.00 88.05  ?  2    NAG Q O4  1 
HETATM 13089 O O5  . NAG Q  4  .   ? 12.497  29.878  -3.057  1.00 63.83  ?  2    NAG Q O5  1 
HETATM 13090 O O6  . NAG Q  4  .   ? 14.760  29.058  -4.877  1.00 62.95  ?  2    NAG Q O6  1 
HETATM 13091 O O7  . NAG Q  4  .   ? 11.534  33.921  -2.995  1.00 105.53 ?  2    NAG Q O7  1 
HETATM 13092 C C1  . NAG R  4  .   ? -25.255 -25.524 20.609  1.00 69.84  ?  1    NAG R C1  1 
HETATM 13093 C C2  . NAG R  4  .   ? -24.549 -26.854 20.391  1.00 79.48  ?  1    NAG R C2  1 
HETATM 13094 C C3  . NAG R  4  .   ? -23.414 -26.693 19.384  1.00 86.77  ?  1    NAG R C3  1 
HETATM 13095 C C4  . NAG R  4  .   ? -23.913 -26.034 18.103  1.00 85.28  ?  1    NAG R C4  1 
HETATM 13096 C C5  . NAG R  4  .   ? -24.696 -24.761 18.417  1.00 73.15  ?  1    NAG R C5  1 
HETATM 13097 C C6  . NAG R  4  .   ? -25.374 -24.174 17.203  1.00 78.55  ?  1    NAG R C6  1 
HETATM 13098 C C7  . NAG R  4  .   ? -24.660 -28.360 22.335  1.00 70.59  ?  1    NAG R C7  1 
HETATM 13099 C C8  . NAG R  4  .   ? -25.917 -28.913 21.724  1.00 66.04  ?  1    NAG R C8  1 
HETATM 13100 N N2  . NAG R  4  .   ? -24.049 -27.386 21.650  1.00 78.55  ?  1    NAG R N2  1 
HETATM 13101 O O3  . NAG R  4  .   ? -22.878 -27.977 19.089  1.00 89.47  ?  1    NAG R O3  1 
HETATM 13102 O O4  . NAG R  4  .   ? -22.800 -25.673 17.291  1.00 95.17  ?  1    NAG R O4  1 
HETATM 13103 O O5  . NAG R  4  .   ? -25.735 -25.034 19.369  1.00 68.59  ?  1    NAG R O5  1 
HETATM 13104 O O6  . NAG R  4  .   ? -26.783 -24.351 17.275  1.00 84.28  ?  1    NAG R O6  1 
HETATM 13105 O O7  . NAG R  4  .   ? -24.215 -28.781 23.401  1.00 63.95  ?  1    NAG R O7  1 
HETATM 13106 C C1  . NAG R  4  .   ? -22.715 -26.430 16.069  1.00 99.50  ?  2    NAG R C1  1 
HETATM 13107 C C2  . NAG R  4  .   ? -22.135 -25.509 14.996  1.00 98.36  ?  2    NAG R C2  1 
HETATM 13108 C C3  . NAG R  4  .   ? -21.953 -26.266 13.686  1.00 105.35 ?  2    NAG R C3  1 
HETATM 13109 C C4  . NAG R  4  .   ? -21.101 -27.509 13.913  1.00 107.68 ?  2    NAG R C4  1 
HETATM 13110 C C5  . NAG R  4  .   ? -21.727 -28.369 15.007  1.00 106.48 ?  2    NAG R C5  1 
HETATM 13111 C C6  . NAG R  4  .   ? -20.888 -29.574 15.368  1.00 106.18 ?  2    NAG R C6  1 
HETATM 13112 C C7  . NAG R  4  .   ? -22.591 -23.104 15.143  1.00 93.11  ?  2    NAG R C7  1 
HETATM 13113 C C8  . NAG R  4  .   ? -23.578 -22.009 14.871  1.00 90.41  ?  2    NAG R C8  1 
HETATM 13114 N N2  . NAG R  4  .   ? -22.974 -24.337 14.799  1.00 94.52  ?  2    NAG R N2  1 
HETATM 13115 O O3  . NAG R  4  .   ? -21.338 -25.411 12.728  1.00 103.06 ?  2    NAG R O3  1 
HETATM 13116 O O4  . NAG R  4  .   ? -20.995 -28.265 12.711  1.00 106.31 ?  2    NAG R O4  1 
HETATM 13117 O O5  . NAG R  4  .   ? -21.884 -27.595 16.208  1.00 104.99 ?  2    NAG R O5  1 
HETATM 13118 O O6  . NAG R  4  .   ? -19.829 -29.233 16.254  1.00 105.17 ?  2    NAG R O6  1 
HETATM 13119 O O7  . NAG R  4  .   ? -21.495 -22.881 15.653  1.00 84.53  ?  2    NAG R O7  1 
HETATM 13120 C C1  . NAG S  4  .   ? 8.837   45.626  -21.461 1.00 117.84 ?  1    NAG S C1  1 
HETATM 13121 C C2  . NAG S  4  .   ? 8.089   46.955  -21.670 1.00 121.91 ?  1    NAG S C2  1 
HETATM 13122 C C3  . NAG S  4  .   ? 9.081   48.128  -21.688 1.00 125.54 ?  1    NAG S C3  1 
HETATM 13123 C C4  . NAG S  4  .   ? 10.316  47.816  -22.530 1.00 130.80 ?  1    NAG S C4  1 
HETATM 13124 C C5  . NAG S  4  .   ? 10.922  46.468  -22.145 1.00 129.25 ?  1    NAG S C5  1 
HETATM 13125 C C6  . NAG S  4  .   ? 12.357  46.561  -21.678 1.00 130.67 ?  1    NAG S C6  1 
HETATM 13126 C C7  . NAG S  4  .   ? 6.186   47.609  -23.112 1.00 115.29 ?  1    NAG S C7  1 
HETATM 13127 C C8  . NAG S  4  .   ? 5.688   48.435  -21.963 1.00 111.67 ?  1    NAG S C8  1 
HETATM 13128 N N2  . NAG S  4  .   ? 7.322   46.926  -22.908 1.00 123.22 ?  1    NAG S N2  1 
HETATM 13129 O O3  . NAG S  4  .   ? 9.468   48.439  -20.354 1.00 124.94 ?  1    NAG S O3  1 
HETATM 13130 O O4  . NAG S  4  .   ? 9.982   47.768  -23.914 1.00 136.16 ?  1    NAG S O4  1 
HETATM 13131 O O5  . NAG S  4  .   ? 10.172  45.890  -21.071 1.00 125.08 ?  1    NAG S O5  1 
HETATM 13132 O O6  . NAG S  4  .   ? 12.916  45.272  -21.464 1.00 123.02 ?  1    NAG S O6  1 
HETATM 13133 O O7  . NAG S  4  .   ? 5.580   47.554  -24.180 1.00 101.62 ?  1    NAG S O7  1 
HETATM 13134 C C1  . NAG S  4  .   ? 10.255  48.991  -24.642 1.00 138.96 ?  2    NAG S C1  1 
HETATM 13135 C C2  . NAG S  4  .   ? 11.602  48.937  -25.352 1.00 142.92 ?  2    NAG S C2  1 
HETATM 13136 C C3  . NAG S  4  .   ? 11.917  50.291  -25.983 1.00 141.24 ?  2    NAG S C3  1 
HETATM 13137 C C4  . NAG S  4  .   ? 10.652  51.061  -26.361 1.00 139.76 ?  2    NAG S C4  1 
HETATM 13138 C C5  . NAG S  4  .   ? 9.429   50.171  -26.629 1.00 141.14 ?  2    NAG S C5  1 
HETATM 13139 C C6  . NAG S  4  .   ? 9.490   49.450  -27.960 1.00 133.61 ?  2    NAG S C6  1 
HETATM 13140 C C7  . NAG S  4  .   ? 13.640  47.674  -24.791 1.00 132.32 ?  2    NAG S C7  1 
HETATM 13141 C C8  . NAG S  4  .   ? 13.569  47.112  -26.181 1.00 125.06 ?  2    NAG S C8  1 
HETATM 13142 N N2  . NAG S  4  .   ? 12.673  48.535  -24.451 1.00 137.22 ?  2    NAG S N2  1 
HETATM 13143 O O3  . NAG S  4  .   ? 12.727  50.092  -27.137 1.00 143.18 ?  2    NAG S O3  1 
HETATM 13144 O O4  . NAG S  4  .   ? 10.334  52.027  -25.364 1.00 136.93 ?  2    NAG S O4  1 
HETATM 13145 O O5  . NAG S  4  .   ? 9.215   49.176  -25.608 1.00 141.29 ?  2    NAG S O5  1 
HETATM 13146 O O6  . NAG S  4  .   ? 8.347   48.631  -28.167 1.00 129.43 ?  2    NAG S O6  1 
HETATM 13147 O O7  . NAG S  4  .   ? 14.532  47.360  -24.009 1.00 134.59 ?  2    NAG S O7  1 
HETATM 13148 C C1  . NAG T  7  .   ? 23.883  -17.550 6.429   1.00 72.65  ?  1    NAG T C1  1 
HETATM 13149 C C2  . NAG T  7  .   ? 24.831  -17.849 7.586   1.00 80.76  ?  1    NAG T C2  1 
HETATM 13150 C C3  . NAG T  7  .   ? 25.648  -19.092 7.283   1.00 79.17  ?  1    NAG T C3  1 
HETATM 13151 C C4  . NAG T  7  .   ? 24.738  -20.254 6.939   1.00 72.07  ?  1    NAG T C4  1 
HETATM 13152 C C5  . NAG T  7  .   ? 23.715  -19.850 5.889   1.00 72.24  ?  1    NAG T C5  1 
HETATM 13153 C C6  . NAG T  7  .   ? 22.695  -20.958 5.678   1.00 66.25  ?  1    NAG T C6  1 
HETATM 13154 C C7  . NAG T  7  .   ? 26.097  -15.808 7.035   1.00 81.33  ?  1    NAG T C7  1 
HETATM 13155 C C8  . NAG T  7  .   ? 26.968  -16.210 5.883   1.00 83.76  ?  1    NAG T C8  1 
HETATM 13156 N N2  . NAG T  7  .   ? 25.750  -16.763 7.884   1.00 79.98  ?  1    NAG T N2  1 
HETATM 13157 O O3  . NAG T  7  .   ? 26.434  -19.416 8.431   1.00 80.31  ?  1    NAG T O3  1 
HETATM 13158 O O4  . NAG T  7  .   ? 25.541  -21.314 6.424   1.00 75.12  ?  1    NAG T O4  1 
HETATM 13159 O O5  . NAG T  7  .   ? 23.022  -18.672 6.288   1.00 82.15  ?  1    NAG T O5  1 
HETATM 13160 O O6  . NAG T  7  .   ? 21.995  -20.719 4.453   1.00 61.82  ?  1    NAG T O6  1 
HETATM 13161 O O7  . NAG T  7  .   ? 25.737  -14.660 7.200   1.00 88.57  ?  1    NAG T O7  1 
HETATM 13162 C C1  . NAG T  7  .   ? 25.736  -22.309 7.444   1.00 79.03  ?  2    NAG T C1  1 
HETATM 13163 C C2  . NAG T  7  .   ? 26.086  -23.647 6.826   1.00 82.01  ?  2    NAG T C2  1 
HETATM 13164 C C3  . NAG T  7  .   ? 26.260  -24.685 7.909   1.00 81.10  ?  2    NAG T C3  1 
HETATM 13165 C C4  . NAG T  7  .   ? 27.274  -24.200 8.922   1.00 88.84  ?  2    NAG T C4  1 
HETATM 13166 C C5  . NAG T  7  .   ? 26.846  -22.845 9.425   1.00 88.96  ?  2    NAG T C5  1 
HETATM 13167 C C6  . NAG T  7  .   ? 27.867  -22.342 10.420  1.00 98.37  ?  2    NAG T C6  1 
HETATM 13168 C C7  . NAG T  7  .   ? 25.151  -23.922 4.636   1.00 81.72  ?  2    NAG T C7  1 
HETATM 13169 C C8  . NAG T  7  .   ? 24.193  -24.706 3.800   1.00 69.36  ?  2    NAG T C8  1 
HETATM 13170 N N2  . NAG T  7  .   ? 25.044  -24.098 5.938   1.00 85.30  ?  2    NAG T N2  1 
HETATM 13171 O O3  . NAG T  7  .   ? 26.705  -25.879 7.272   1.00 86.43  ?  2    NAG T O3  1 
HETATM 13172 O O4  . NAG T  7  .   ? 27.342  -25.067 10.053  1.00 99.22  ?  2    NAG T O4  1 
HETATM 13173 O O5  . NAG T  7  .   ? 26.785  -21.955 8.328   1.00 85.34  ?  2    NAG T O5  1 
HETATM 13174 O O6  . NAG T  7  .   ? 29.132  -22.328 9.758   1.00 100.06 ?  2    NAG T O6  1 
HETATM 13175 O O7  . NAG T  7  .   ? 25.979  -23.174 4.159   1.00 91.27  ?  2    NAG T O7  1 
HETATM 13176 C C1  . BMA T  7  .   ? 28.138  -26.208 9.724   1.00 103.57 ?  3    BMA T C1  1 
HETATM 13177 C C2  . BMA T  7  .   ? 29.051  -26.572 10.869  1.00 103.57 ?  3    BMA T C2  1 
HETATM 13178 C C3  . BMA T  7  .   ? 29.915  -27.743 10.450  1.00 103.57 ?  3    BMA T C3  1 
HETATM 13179 C C4  . BMA T  7  .   ? 29.046  -28.886 9.948   1.00 103.57 ?  3    BMA T C4  1 
HETATM 13180 C C5  . BMA T  7  .   ? 28.049  -28.400 8.911   1.00 103.57 ?  3    BMA T C5  1 
HETATM 13181 C C6  . BMA T  7  .   ? 27.061  -29.486 8.509   1.00 103.57 ?  3    BMA T C6  1 
HETATM 13182 O O2  . BMA T  7  .   ? 28.250  -26.949 11.983  1.00 103.57 ?  3    BMA T O2  1 
HETATM 13183 O O3  . BMA T  7  .   ? 30.687  -28.181 11.573  1.00 103.57 ?  3    BMA T O3  1 
HETATM 13184 O O4  . BMA T  7  .   ? 29.879  -29.883 9.354   1.00 103.57 ?  3    BMA T O4  1 
HETATM 13185 O O5  . BMA T  7  .   ? 27.312  -27.326 9.467   1.00 103.57 ?  3    BMA T O5  1 
HETATM 13186 O O6  . BMA T  7  .   ? 27.721  -30.504 7.752   1.00 103.57 ?  3    BMA T O6  1 
HETATM 13187 C C1  . NAG U  9  .   ? 16.165  -20.767 35.002  1.00 91.14  ?  1    NAG U C1  1 
HETATM 13188 C C2  . NAG U  9  .   ? 16.781  -19.690 35.875  1.00 89.93  ?  1    NAG U C2  1 
HETATM 13189 C C3  . NAG U  9  .   ? 18.103  -20.182 36.438  1.00 94.34  ?  1    NAG U C3  1 
HETATM 13190 C C4  . NAG U  9  .   ? 17.870  -21.454 37.244  1.00 100.60 ?  1    NAG U C4  1 
HETATM 13191 C C5  . NAG U  9  .   ? 17.095  -22.507 36.441  1.00 98.59  ?  1    NAG U C5  1 
HETATM 13192 C C6  . NAG U  9  .   ? 16.577  -23.619 37.325  1.00 96.34  ?  1    NAG U C6  1 
HETATM 13193 C C7  . NAG U  9  .   ? 17.665  -18.249 34.067  1.00 106.93 ?  1    NAG U C7  1 
HETATM 13194 C C8  . NAG U  9  .   ? 17.688  -16.856 33.519  1.00 95.23  ?  1    NAG U C8  1 
HETATM 13195 N N2  . NAG U  9  .   ? 16.938  -18.422 35.176  1.00 100.79 ?  1    NAG U N2  1 
HETATM 13196 O O3  . NAG U  9  .   ? 18.676  -19.173 37.262  1.00 92.14  ?  1    NAG U O3  1 
HETATM 13197 O O4  . NAG U  9  .   ? 19.115  -22.012 37.653  1.00 104.61 ?  1    NAG U O4  1 
HETATM 13198 O O5  . NAG U  9  .   ? 15.936  -21.947 35.792  1.00 92.92  ?  1    NAG U O5  1 
HETATM 13199 O O6  . NAG U  9  .   ? 15.467  -23.161 38.088  1.00 77.65  ?  1    NAG U O6  1 
HETATM 13200 O O7  . NAG U  9  .   ? 18.278  -19.169 33.530  1.00 110.66 ?  1    NAG U O7  1 
HETATM 13201 C C1  . FUC U  9  .   ? 15.371  -23.820 39.369  1.00 94.62  ?  2    FUC U C1  1 
HETATM 13202 C C2  . FUC U  9  .   ? 14.778  -22.833 40.410  1.00 94.62  ?  2    FUC U C2  1 
HETATM 13203 C C3  . FUC U  9  .   ? 13.370  -22.416 39.997  1.00 94.62  ?  2    FUC U C3  1 
HETATM 13204 C C4  . FUC U  9  .   ? 12.481  -23.658 39.793  1.00 94.62  ?  2    FUC U C4  1 
HETATM 13205 C C5  . FUC U  9  .   ? 13.177  -24.683 38.868  1.00 94.62  ?  2    FUC U C5  1 
HETATM 13206 C C6  . FUC U  9  .   ? 12.473  -26.029 38.840  1.00 94.62  ?  2    FUC U C6  1 
HETATM 13207 O O2  . FUC U  9  .   ? 15.589  -21.685 40.638  1.00 94.62  ?  2    FUC U O2  1 
HETATM 13208 O O3  . FUC U  9  .   ? 12.784  -21.612 41.018  1.00 94.62  ?  2    FUC U O3  1 
HETATM 13209 O O4  . FUC U  9  .   ? 12.194  -24.261 41.041  1.00 94.62  ?  2    FUC U O4  1 
HETATM 13210 O O5  . FUC U  9  .   ? 14.548  -24.950 39.264  1.00 94.62  ?  2    FUC U O5  1 
HETATM 13211 C C1  . NAG V  9  .   ? 3.321   4.517   -25.598 1.00 89.71  ?  1    NAG V C1  1 
HETATM 13212 C C2  . NAG V  9  .   ? 4.362   4.176   -26.678 1.00 89.71  ?  1    NAG V C2  1 
HETATM 13213 C C3  . NAG V  9  .   ? 3.750   4.300   -28.077 1.00 89.71  ?  1    NAG V C3  1 
HETATM 13214 C C4  . NAG V  9  .   ? 2.464   3.489   -28.178 1.00 89.71  ?  1    NAG V C4  1 
HETATM 13215 C C5  . NAG V  9  .   ? 1.503   3.907   -27.069 1.00 89.71  ?  1    NAG V C5  1 
HETATM 13216 C C6  . NAG V  9  .   ? 0.221   3.103   -27.051 1.00 89.71  ?  1    NAG V C6  1 
HETATM 13217 C C7  . NAG V  9  .   ? 6.707   4.612   -26.076 1.00 89.71  ?  1    NAG V C7  1 
HETATM 13218 C C8  . NAG V  9  .   ? 7.802   5.634   -26.037 1.00 89.71  ?  1    NAG V C8  1 
HETATM 13219 N N2  . NAG V  9  .   ? 5.533   5.031   -26.561 1.00 89.71  ?  1    NAG V N2  1 
HETATM 13220 O O3  . NAG V  9  .   ? 4.688   3.860   -29.055 1.00 89.71  ?  1    NAG V O3  1 
HETATM 13221 O O4  . NAG V  9  .   ? 1.848   3.685   -29.447 1.00 89.71  ?  1    NAG V O4  1 
HETATM 13222 O O5  . NAG V  9  .   ? 2.136   3.721   -25.795 1.00 89.71  ?  1    NAG V O5  1 
HETATM 13223 O O6  . NAG V  9  .   ? 0.399   1.815   -26.477 1.00 89.71  ?  1    NAG V O6  1 
HETATM 13224 O O7  . NAG V  9  .   ? 6.877   3.462   -25.684 1.00 89.71  ?  1    NAG V O7  1 
HETATM 13225 C C1  . FUC V  9  .   ? -0.384  0.852   -27.223 1.00 100.66 ?  2    FUC V C1  1 
HETATM 13226 C C2  . FUC V  9  .   ? 0.578   -0.257  -27.783 1.00 100.66 ?  2    FUC V C2  1 
HETATM 13227 C C3  . FUC V  9  .   ? 0.535   -1.566  -26.959 1.00 100.66 ?  2    FUC V C3  1 
HETATM 13228 C C4  . FUC V  9  .   ? 0.251   -1.330  -25.447 1.00 100.66 ?  2    FUC V C4  1 
HETATM 13229 C C5  . FUC V  9  .   ? -0.958  -0.380  -25.214 1.00 100.66 ?  2    FUC V C5  1 
HETATM 13230 C C6  . FUC V  9  .   ? -2.176  -1.091  -24.632 1.00 100.66 ?  2    FUC V C6  1 
HETATM 13231 O O2  . FUC V  9  .   ? 1.927   0.191   -27.941 1.00 100.66 ?  2    FUC V O2  1 
HETATM 13232 O O3  . FUC V  9  .   ? -0.462  -2.454  -27.482 1.00 100.66 ?  2    FUC V O3  1 
HETATM 13233 O O4  . FUC V  9  .   ? 0.008   -2.576  -24.807 1.00 100.66 ?  2    FUC V O4  1 
HETATM 13234 O O5  . FUC V  9  .   ? -1.405  0.283   -26.416 1.00 100.66 ?  2    FUC V O5  1 
HETATM 13235 C C1  . NAG W  4  .   ? -6.304  2.831   30.543  1.00 92.01  ?  1    NAG W C1  1 
HETATM 13236 C C2  . NAG W  4  .   ? -6.669  4.213   31.076  1.00 92.01  ?  1    NAG W C2  1 
HETATM 13237 C C3  . NAG W  4  .   ? -6.908  5.179   29.912  1.00 92.01  ?  1    NAG W C3  1 
HETATM 13238 C C4  . NAG W  4  .   ? -5.776  5.130   28.888  1.00 92.01  ?  1    NAG W C4  1 
HETATM 13239 C C5  . NAG W  4  .   ? -5.385  3.693   28.537  1.00 92.01  ?  1    NAG W C5  1 
HETATM 13240 C C6  . NAG W  4  .   ? -4.123  3.603   27.711  1.00 92.01  ?  1    NAG W C6  1 
HETATM 13241 C C7  . NAG W  4  .   ? -7.858  4.597   33.187  1.00 92.01  ?  1    NAG W C7  1 
HETATM 13242 C C8  . NAG W  4  .   ? -9.156  4.450   33.926  1.00 92.01  ?  1    NAG W C8  1 
HETATM 13243 N N2  . NAG W  4  .   ? -7.845  4.146   31.930  1.00 92.01  ?  1    NAG W N2  1 
HETATM 13244 O O3  . NAG W  4  .   ? -7.041  6.504   30.418  1.00 92.01  ?  1    NAG W O3  1 
HETATM 13245 O O4  . NAG W  4  .   ? -6.241  5.736   27.687  1.00 92.01  ?  1    NAG W O4  1 
HETATM 13246 O O5  . NAG W  4  .   ? -5.150  2.930   29.727  1.00 92.01  ?  1    NAG W O5  1 
HETATM 13247 O O6  . NAG W  4  .   ? -4.158  2.488   26.832  1.00 92.01  ?  1    NAG W O6  1 
HETATM 13248 O O7  . NAG W  4  .   ? -6.865  5.100   33.707  1.00 92.01  ?  1    NAG W O7  1 
HETATM 13249 C C1  . NAG W  4  .   ? -5.395  6.816   27.228  1.00 103.06 ?  2    NAG W C1  1 
HETATM 13250 C C2  . NAG W  4  .   ? -5.202  6.616   25.732  1.00 103.06 ?  2    NAG W C2  1 
HETATM 13251 C C3  . NAG W  4  .   ? -6.525  6.779   25.002  1.00 103.06 ?  2    NAG W C3  1 
HETATM 13252 C C4  . NAG W  4  .   ? -7.131  8.150   25.281  1.00 103.06 ?  2    NAG W C4  1 
HETATM 13253 C C5  . NAG W  4  .   ? -7.161  8.506   26.775  1.00 103.06 ?  2    NAG W C5  1 
HETATM 13254 C C6  . NAG W  4  .   ? -8.329  7.895   27.521  1.00 103.06 ?  2    NAG W C6  1 
HETATM 13255 C C7  . NAG W  4  .   ? -2.981  7.182   24.851  1.00 103.06 ?  2    NAG W C7  1 
HETATM 13256 C C8  . NAG W  4  .   ? -2.649  5.728   25.017  1.00 103.06 ?  2    NAG W C8  1 
HETATM 13257 N N2  . NAG W  4  .   ? -4.215  7.547   25.211  1.00 103.06 ?  2    NAG W N2  1 
HETATM 13258 O O3  . NAG W  4  .   ? -7.425  5.743   25.380  1.00 103.06 ?  2    NAG W O3  1 
HETATM 13259 O O4  . NAG W  4  .   ? -6.395  9.145   24.578  1.00 103.06 ?  2    NAG W O4  1 
HETATM 13260 O O5  . NAG W  4  .   ? -5.958  8.136   27.475  1.00 103.06 ?  2    NAG W O5  1 
HETATM 13261 O O6  . NAG W  4  .   ? -8.505  8.493   28.799  1.00 103.06 ?  2    NAG W O6  1 
HETATM 13262 O O7  . NAG W  4  .   ? -2.169  7.989   24.412  1.00 103.06 ?  2    NAG W O7  1 
HETATM 13263 C C1  . NAG X  10 .   ? -48.210 -5.093  55.853  1.00 86.11  ?  1601 NAG A C1  1 
HETATM 13264 C C2  . NAG X  10 .   ? -48.445 -6.004  54.639  1.00 94.34  ?  1601 NAG A C2  1 
HETATM 13265 C C3  . NAG X  10 .   ? -48.807 -7.420  55.093  1.00 105.25 ?  1601 NAG A C3  1 
HETATM 13266 C C4  . NAG X  10 .   ? -50.036 -7.411  55.996  1.00 104.51 ?  1601 NAG A C4  1 
HETATM 13267 C C5  . NAG X  10 .   ? -49.959 -6.260  56.994  1.00 99.45  ?  1601 NAG A C5  1 
HETATM 13268 C C6  . NAG X  10 .   ? -50.311 -6.676  58.402  1.00 105.79 ?  1601 NAG A C6  1 
HETATM 13269 C C7  . NAG X  10 .   ? -49.305 -4.436  52.949  1.00 99.42  ?  1601 NAG A C7  1 
HETATM 13270 C C8  . NAG X  10 .   ? -50.501 -4.019  52.147  1.00 103.93 ?  1601 NAG A C8  1 
HETATM 13271 N N2  . NAG X  10 .   ? -49.490 -5.466  53.782  1.00 96.41  ?  1601 NAG A N2  1 
HETATM 13272 O O3  . NAG X  10 .   ? -47.703 -7.990  55.788  1.00 103.64 ?  1601 NAG A O3  1 
HETATM 13273 O O4  . NAG X  10 .   ? -51.215 -7.270  55.210  1.00 110.83 ?  1601 NAG A O4  1 
HETATM 13274 O O5  . NAG X  10 .   ? -48.615 -5.768  57.046  1.00 88.52  ?  1601 NAG A O5  1 
HETATM 13275 O O6  . NAG X  10 .   ? -49.175 -6.594  59.252  1.00 96.77  ?  1601 NAG A O6  1 
HETATM 13276 O O7  . NAG X  10 .   ? -48.220 -3.865  52.847  1.00 92.51  ?  1601 NAG A O7  1 
HETATM 13277 C C1  . NAG Y  10 .   ? -64.482 41.645  88.338  1.00 91.80  ?  1602 NAG A C1  1 
HETATM 13278 C C2  . NAG Y  10 .   ? -65.885 42.066  88.805  1.00 91.48  ?  1602 NAG A C2  1 
HETATM 13279 C C3  . NAG Y  10 .   ? -65.953 43.584  89.006  1.00 104.18 ?  1602 NAG A C3  1 
HETATM 13280 C C4  . NAG Y  10 .   ? -64.835 44.052  89.928  1.00 106.60 ?  1602 NAG A C4  1 
HETATM 13281 C C5  . NAG Y  10 .   ? -63.486 43.592  89.383  1.00 105.32 ?  1602 NAG A C5  1 
HETATM 13282 C C6  . NAG Y  10 .   ? -62.328 43.934  90.293  1.00 99.69  ?  1602 NAG A C6  1 
HETATM 13283 C C7  . NAG Y  10 .   ? -68.070 41.088  88.229  1.00 90.73  ?  1602 NAG A C7  1 
HETATM 13284 C C8  . NAG Y  10 .   ? -68.301 40.955  89.705  1.00 92.58  ?  1602 NAG A C8  1 
HETATM 13285 N N2  . NAG Y  10 .   ? -66.901 41.627  87.860  1.00 89.91  ?  1602 NAG A N2  1 
HETATM 13286 O O3  . NAG Y  10 .   ? -67.211 43.941  89.567  1.00 106.24 ?  1602 NAG A O3  1 
HETATM 13287 O O4  . NAG Y  10 .   ? -64.855 45.470  90.049  1.00 103.24 ?  1602 NAG A O4  1 
HETATM 13288 O O5  . NAG Y  10 .   ? -63.489 42.163  89.246  1.00 101.35 ?  1602 NAG A O5  1 
HETATM 13289 O O6  . NAG Y  10 .   ? -62.010 45.319  90.246  1.00 98.17  ?  1602 NAG A O6  1 
HETATM 13290 O O7  . NAG Y  10 .   ? -68.907 40.725  87.406  1.00 87.39  ?  1602 NAG A O7  1 
HETATM 13291 C C1  . NAG Z  10 .   ? -75.273 31.615  79.337  1.00 103.04 ?  1603 NAG A C1  1 
HETATM 13292 C C2  . NAG Z  10 .   ? -76.144 32.827  78.988  1.00 106.53 ?  1603 NAG A C2  1 
HETATM 13293 C C3  . NAG Z  10 .   ? -77.583 32.375  78.727  1.00 107.84 ?  1603 NAG A C3  1 
HETATM 13294 C C4  . NAG Z  10 .   ? -77.615 31.263  77.684  1.00 111.14 ?  1603 NAG A C4  1 
HETATM 13295 C C5  . NAG Z  10 .   ? -76.660 30.132  78.068  1.00 109.51 ?  1603 NAG A C5  1 
HETATM 13296 C C6  . NAG Z  10 .   ? -76.555 29.054  77.014  1.00 113.91 ?  1603 NAG A C6  1 
HETATM 13297 C C7  . NAG Z  10 .   ? -76.437 35.103  79.865  1.00 109.18 ?  1603 NAG A C7  1 
HETATM 13298 C C8  . NAG Z  10 .   ? -76.332 35.989  81.071  1.00 110.38 ?  1603 NAG A C8  1 
HETATM 13299 N N2  . NAG Z  10 .   ? -76.101 33.822  80.048  1.00 106.54 ?  1603 NAG A N2  1 
HETATM 13300 O O3  . NAG Z  10 .   ? -78.371 33.475  78.285  1.00 104.29 ?  1603 NAG A O3  1 
HETATM 13301 O O4  . NAG Z  10 .   ? -78.937 30.746  77.567  1.00 106.14 ?  1603 NAG A O4  1 
HETATM 13302 O O5  . NAG Z  10 .   ? -75.335 30.651  78.266  1.00 98.83  ?  1603 NAG A O5  1 
HETATM 13303 O O6  . NAG Z  10 .   ? -76.578 27.756  77.592  1.00 130.90 ?  1603 NAG A O6  1 
HETATM 13304 O O7  . NAG Z  10 .   ? -76.815 35.527  78.777  1.00 112.24 ?  1603 NAG A O7  1 
HETATM 13305 C C1  . BMA AA 11 .   ? -36.530 17.506  77.599  1.00 82.62  ?  301  BMA B C1  1 
HETATM 13306 C C2  . BMA AA 11 .   ? -36.824 16.870  78.933  1.00 82.62  ?  301  BMA B C2  1 
HETATM 13307 C C3  . BMA AA 11 .   ? -36.553 17.853  80.042  1.00 82.62  ?  301  BMA B C3  1 
HETATM 13308 C C4  . BMA AA 11 .   ? -35.118 18.316  79.920  1.00 82.62  ?  301  BMA B C4  1 
HETATM 13309 C C5  . BMA AA 11 .   ? -34.829 18.857  78.537  1.00 82.62  ?  301  BMA B C5  1 
HETATM 13310 C C6  . BMA AA 11 .   ? -33.345 19.113  78.396  1.00 82.62  ?  301  BMA B C6  1 
HETATM 13311 O O1  . BMA AA 11 .   ? -36.717 16.521  76.588  1.00 82.62  ?  301  BMA B O1  1 
HETATM 13312 O O2  . BMA AA 11 .   ? -35.958 15.750  79.095  1.00 82.62  ?  301  BMA B O2  1 
HETATM 13313 O O3  . BMA AA 11 .   ? -36.769 17.209  81.300  1.00 82.62  ?  301  BMA B O3  1 
HETATM 13314 O O4  . BMA AA 11 .   ? -34.898 19.375  80.846  1.00 82.62  ?  301  BMA B O4  1 
HETATM 13315 O O5  . BMA AA 11 .   ? -35.178 17.913  77.547  1.00 82.62  ?  301  BMA B O5  1 
HETATM 13316 O O6  . BMA AA 11 .   ? -33.067 19.383  77.023  1.00 82.62  ?  301  BMA B O6  1 
HETATM 13317 C C1  . NAG BA 10 .   ? -32.845 -33.679 38.873  1.00 58.19  ?  1401 NAG D C1  1 
HETATM 13318 C C2  . NAG BA 10 .   ? -32.036 -34.957 39.059  1.00 58.85  ?  1401 NAG D C2  1 
HETATM 13319 C C3  . NAG BA 10 .   ? -32.650 -35.817 40.156  1.00 65.24  ?  1401 NAG D C3  1 
HETATM 13320 C C4  . NAG BA 10 .   ? -32.810 -35.012 41.440  1.00 66.94  ?  1401 NAG D C4  1 
HETATM 13321 C C5  . NAG BA 10 .   ? -33.577 -33.719 41.165  1.00 62.52  ?  1401 NAG D C5  1 
HETATM 13322 C C6  . NAG BA 10 .   ? -33.643 -32.802 42.363  1.00 70.68  ?  1401 NAG D C6  1 
HETATM 13323 C C7  . NAG BA 10 .   ? -30.882 -35.652 37.012  1.00 53.63  ?  1401 NAG D C7  1 
HETATM 13324 C C8  . NAG BA 10 .   ? -30.958 -36.485 35.770  1.00 52.21  ?  1401 NAG D C8  1 
HETATM 13325 N N2  . NAG BA 10 .   ? -31.947 -35.703 37.816  1.00 53.68  ?  1401 NAG D N2  1 
HETATM 13326 O O3  . NAG BA 10 .   ? -31.796 -36.934 40.373  1.00 81.52  ?  1401 NAG D O3  1 
HETATM 13327 O O4  . NAG BA 10 .   ? -33.497 -35.773 42.430  1.00 74.72  ?  1401 NAG D O4  1 
HETATM 13328 O O5  . NAG BA 10 .   ? -32.931 -32.977 40.119  1.00 63.36  ?  1401 NAG D O5  1 
HETATM 13329 O O6  . NAG BA 10 .   ? -32.362 -32.627 42.953  1.00 102.31 ?  1401 NAG D O6  1 
HETATM 13330 O O7  . NAG BA 10 .   ? -29.900 -34.965 37.276  1.00 51.46  ?  1401 NAG D O7  1 
HETATM 13331 C C1  . NAG CA 10 .   ? 2.772   -29.238 31.676  1.00 85.28  ?  1402 NAG D C1  1 
HETATM 13332 C C2  . NAG CA 10 .   ? 2.683   -29.444 33.193  1.00 86.49  ?  1402 NAG D C2  1 
HETATM 13333 C C3  . NAG CA 10 .   ? 1.501   -30.352 33.557  1.00 95.07  ?  1402 NAG D C3  1 
HETATM 13334 C C4  . NAG CA 10 .   ? 1.555   -31.677 32.803  1.00 102.04 ?  1402 NAG D C4  1 
HETATM 13335 C C5  . NAG CA 10 .   ? 1.951   -31.457 31.346  1.00 93.20  ?  1402 NAG D C5  1 
HETATM 13336 C C6  . NAG CA 10 .   ? 1.061   -32.206 30.380  1.00 84.61  ?  1402 NAG D C6  1 
HETATM 13337 C C7  . NAG CA 10 .   ? 4.818   -29.236 34.395  1.00 107.99 ?  1402 NAG D C7  1 
HETATM 13338 C C8  . NAG CA 10 .   ? 4.473   -27.786 34.574  1.00 92.58  ?  1402 NAG D C8  1 
HETATM 13339 N N2  . NAG CA 10 .   ? 3.926   -29.977 33.727  1.00 97.76  ?  1402 NAG D N2  1 
HETATM 13340 O O3  . NAG CA 10 .   ? 0.285   -29.678 33.251  1.00 89.04  ?  1402 NAG D O3  1 
HETATM 13341 O O4  . NAG CA 10 .   ? 2.473   -32.567 33.430  1.00 109.18 ?  1402 NAG D O4  1 
HETATM 13342 O O5  . NAG CA 10 .   ? 1.818   -30.066 31.022  1.00 87.46  ?  1402 NAG D O5  1 
HETATM 13343 O O6  . NAG CA 10 .   ? -0.249  -31.654 30.354  1.00 76.25  ?  1402 NAG D O6  1 
HETATM 13344 O O7  . NAG CA 10 .   ? 5.858   -29.715 34.836  1.00 127.25 ?  1402 NAG D O7  1 
HETATM 13345 C C1  . NAG DA 10 .   ? -37.239 -3.511  20.380  1.00 83.72  ?  1403 NAG D C1  1 
HETATM 13346 C C2  . NAG DA 10 .   ? -37.427 -2.563  19.184  1.00 89.72  ?  1403 NAG D C2  1 
HETATM 13347 C C3  . NAG DA 10 .   ? -38.171 -1.293  19.617  1.00 94.77  ?  1403 NAG D C3  1 
HETATM 13348 C C4  . NAG DA 10 .   ? -37.632 -0.744  20.935  1.00 95.01  ?  1403 NAG D C4  1 
HETATM 13349 C C5  . NAG DA 10 .   ? -37.580 -1.830  22.010  1.00 88.45  ?  1403 NAG D C5  1 
HETATM 13350 C C6  . NAG DA 10 .   ? -38.451 -1.525  23.207  1.00 87.38  ?  1403 NAG D C6  1 
HETATM 13351 C C7  . NAG DA 10 .   ? -35.952 -2.069  17.267  1.00 101.99 ?  1403 NAG D C7  1 
HETATM 13352 C C8  . NAG DA 10 .   ? -37.155 -2.273  16.390  1.00 92.97  ?  1403 NAG D C8  1 
HETATM 13353 N N2  . NAG DA 10 .   ? -36.145 -2.221  18.584  1.00 98.36  ?  1403 NAG D N2  1 
HETATM 13354 O O3  . NAG DA 10 .   ? -39.559 -1.580  19.741  1.00 101.63 ?  1403 NAG D O3  1 
HETATM 13355 O O4  . NAG DA 10 .   ? -36.330 -0.204  20.736  1.00 98.22  ?  1403 NAG D O4  1 
HETATM 13356 O O5  . NAG DA 10 .   ? -38.045 -3.073  21.470  1.00 82.36  ?  1403 NAG D O5  1 
HETATM 13357 O O6  . NAG DA 10 .   ? -39.107 -2.696  23.673  1.00 76.43  ?  1403 NAG D O6  1 
HETATM 13358 O O7  . NAG DA 10 .   ? -34.849 -1.780  16.801  1.00 100.07 ?  1403 NAG D O7  1 
HETATM 13359 C C1  . NAG EA 10 .   ? 19.429  2.477   30.344  1.00 87.27  ?  1404 NAG D C1  1 
HETATM 13360 C C2  . NAG EA 10 .   ? 20.629  3.376   30.654  1.00 92.52  ?  1404 NAG D C2  1 
HETATM 13361 C C3  . NAG EA 10 .   ? 20.870  3.454   32.160  1.00 93.89  ?  1404 NAG D C3  1 
HETATM 13362 C C4  . NAG EA 10 .   ? 19.598  3.883   32.878  1.00 98.23  ?  1404 NAG D C4  1 
HETATM 13363 C C5  . NAG EA 10 .   ? 18.455  2.942   32.511  1.00 96.42  ?  1404 NAG D C5  1 
HETATM 13364 C C6  . NAG EA 10 .   ? 17.128  3.359   33.104  1.00 98.72  ?  1404 NAG D C6  1 
HETATM 13365 C C7  . NAG EA 10 .   ? 22.419  3.592   28.995  1.00 96.55  ?  1404 NAG D C7  1 
HETATM 13366 C C8  . NAG EA 10 .   ? 23.634  2.956   28.388  1.00 85.77  ?  1404 NAG D C8  1 
HETATM 13367 N N2  . NAG EA 10 .   ? 21.821  2.902   29.970  1.00 96.85  ?  1404 NAG D N2  1 
HETATM 13368 O O3  . NAG EA 10 .   ? 21.911  4.389   32.420  1.00 89.42  ?  1404 NAG D O3  1 
HETATM 13369 O O4  . NAG EA 10 .   ? 19.803  3.867   34.287  1.00 103.56 ?  1404 NAG D O4  1 
HETATM 13370 O O5  . NAG EA 10 .   ? 18.281  2.926   31.086  1.00 89.30  ?  1404 NAG D O5  1 
HETATM 13371 O O6  . NAG EA 10 .   ? 17.299  4.062   34.327  1.00 97.74  ?  1404 NAG D O6  1 
HETATM 13372 O O7  . NAG EA 10 .   ? 21.999  4.684   28.621  1.00 96.99  ?  1404 NAG D O7  1 
HETATM 13373 C C1  . NAG FA 10 .   ? 20.215  17.872  -1.094  1.00 74.31  ?  1405 NAG D C1  1 
HETATM 13374 C C2  . NAG FA 10 .   ? 19.961  18.436  0.304   1.00 77.43  ?  1405 NAG D C2  1 
HETATM 13375 C C3  . NAG FA 10 .   ? 21.234  19.074  0.868   1.00 86.54  ?  1405 NAG D C3  1 
HETATM 13376 C C4  . NAG FA 10 .   ? 22.416  18.117  0.767   1.00 94.00  ?  1405 NAG D C4  1 
HETATM 13377 C C5  . NAG FA 10 .   ? 22.552  17.607  -0.662  1.00 94.04  ?  1405 NAG D C5  1 
HETATM 13378 C C6  . NAG FA 10 .   ? 23.648  16.578  -0.830  1.00 96.65  ?  1405 NAG D C6  1 
HETATM 13379 C C7  . NAG FA 10 .   ? 17.679  19.195  0.814   1.00 81.32  ?  1405 NAG D C7  1 
HETATM 13380 C C8  . NAG FA 10 .   ? 16.684  20.306  0.662   1.00 72.80  ?  1405 NAG D C8  1 
HETATM 13381 N N2  . NAG FA 10 .   ? 18.880  19.407  0.265   1.00 80.33  ?  1405 NAG D N2  1 
HETATM 13382 O O3  . NAG FA 10 .   ? 21.022  19.442  2.226   1.00 79.89  ?  1405 NAG D O3  1 
HETATM 13383 O O4  . NAG FA 10 .   ? 23.621  18.777  1.142   1.00 92.60  ?  1405 NAG D O4  1 
HETATM 13384 O O5  . NAG FA 10 .   ? 21.325  16.978  -1.057  1.00 91.01  ?  1405 NAG D O5  1 
HETATM 13385 O O6  . NAG FA 10 .   ? 23.802  16.197  -2.191  1.00 86.56  ?  1405 NAG D O6  1 
HETATM 13386 O O7  . NAG FA 10 .   ? 17.410  18.155  1.412   1.00 82.20  ?  1405 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  ? 0.9818 0.8382 0.9980 0.0473  -0.0031 -0.0522 47  THR A N   
2     C CA  . THR A 47  ? 0.9829 0.8302 0.9934 0.0485  -0.0047 -0.0300 47  THR A CA  
3     C C   . THR A 47  ? 1.0429 0.9181 1.0423 0.0431  -0.0060 -0.0177 47  THR A C   
4     O O   . THR A 47  ? 1.0385 0.9090 1.0319 0.0480  -0.0081 0.0006  47  THR A O   
5     C CB  . THR A 47  ? 0.9775 0.8126 0.9939 0.0445  -0.0076 -0.0334 47  THR A CB  
6     O OG1 . THR A 47  ? 1.0277 0.8921 1.0428 0.0351  -0.0083 -0.0393 47  THR A OG1 
7     C CG2 . THR A 47  ? 0.9437 0.7512 0.9684 0.0455  -0.0115 -0.0495 47  THR A CG2 
8     N N   . VAL A 48  ? 0.9153 0.8178 0.9122 0.0329  -0.0071 -0.0283 48  VAL A N   
9     C CA  . VAL A 48  ? 0.9819 0.9096 0.9668 0.0269  -0.0125 -0.0154 48  VAL A CA  
10    C C   . VAL A 48  ? 1.0157 0.9456 0.9832 0.0248  -0.0145 -0.0006 48  VAL A C   
11    O O   . VAL A 48  ? 1.0379 0.9677 0.9959 0.0266  -0.0237 0.0196  48  VAL A O   
12    C CB  . VAL A 48  ? 1.0140 0.9733 0.9971 0.0136  -0.0127 -0.0316 48  VAL A CB  
13    C CG1 . VAL A 48  ? 1.0635 1.0508 1.0274 0.0039  -0.0201 -0.0184 48  VAL A CG1 
14    C CG2 . VAL A 48  ? 0.9991 0.9557 0.9954 0.0137  -0.0138 -0.0387 48  VAL A CG2 
15    N N   . GLU A 49  ? 1.0677 0.9980 1.0315 0.0208  -0.0075 -0.0111 49  GLU A N   
16    C CA  . GLU A 49  ? 1.0999 1.0274 1.0453 0.0161  -0.0082 0.0036  49  GLU A CA  
17    C C   . GLU A 49  ? 1.0285 0.9217 0.9798 0.0313  -0.0095 0.0194  49  GLU A C   
18    O O   . GLU A 49  ? 1.0220 0.9043 0.9604 0.0319  -0.0166 0.0404  49  GLU A O   
19    C CB  . GLU A 49  ? 1.0967 1.0439 1.0384 0.0047  0.0013  -0.0171 49  GLU A CB  
20    C CG  . GLU A 49  ? 1.1067 1.0956 1.0402 -0.0141 0.0036  -0.0351 49  GLU A CG  
21    C CD  . GLU A 49  ? 1.0550 1.0529 1.0144 -0.0088 0.0081  -0.0663 49  GLU A CD  
22    O OE1 . GLU A 49  ? 1.0069 0.9885 0.9869 0.0036  0.0116  -0.0825 49  GLU A OE1 
23    O OE2 . GLU A 49  ? 1.0563 1.0753 1.0155 -0.0168 0.0061  -0.0744 49  GLU A OE2 
24    N N   . GLU A 50  ? 1.0581 0.9322 1.0280 0.0427  -0.0044 0.0096  50  GLU A N   
25    C CA  . GLU A 50  ? 0.9820 0.8276 0.9577 0.0551  -0.0046 0.0225  50  GLU A CA  
26    C C   . GLU A 50  ? 0.9660 0.8077 0.9452 0.0617  -0.0122 0.0377  50  GLU A C   
27    O O   . GLU A 50  ? 0.9378 0.7669 0.9141 0.0679  -0.0168 0.0527  50  GLU A O   
28    C CB  . GLU A 50  ? 0.9190 0.7455 0.9101 0.0627  -0.0004 0.0101  50  GLU A CB  
29    C CG  . GLU A 50  ? 0.9172 0.7467 0.9128 0.0616  0.0037  -0.0092 50  GLU A CG  
30    C CD  . GLU A 50  ? 0.8576 0.6613 0.8676 0.0704  0.0015  -0.0190 50  GLU A CD  
31    O OE1 . GLU A 50  ? 0.8466 0.6377 0.8604 0.0700  -0.0022 -0.0174 50  GLU A OE1 
32    O OE2 . GLU A 50  ? 0.8297 0.6252 0.8458 0.0760  0.0020  -0.0279 50  GLU A OE2 
33    N N   . ALA A 51  ? 0.9283 0.7824 0.9161 0.0604  -0.0143 0.0314  51  ALA A N   
34    C CA  . ALA A 51  ? 0.9207 0.7794 0.9179 0.0671  -0.0211 0.0398  51  ALA A CA  
35    C C   . ALA A 51  ? 0.9488 0.8158 0.9363 0.0686  -0.0340 0.0549  51  ALA A C   
36    O O   . ALA A 51  ? 0.9174 0.7771 0.9137 0.0800  -0.0422 0.0644  51  ALA A O   
37    C CB  . ALA A 51  ? 0.9534 0.8292 0.9601 0.0616  -0.0203 0.0277  51  ALA A CB  
38    N N   . ASN A 52  ? 0.9420 0.8243 0.9113 0.0563  -0.0376 0.0565  52  ASN A N   
39    C CA  . ASN A 52  ? 0.9627 0.8474 0.9158 0.0540  -0.0538 0.0747  52  ASN A CA  
40    C C   . ASN A 52  ? 0.9307 0.7879 0.8703 0.0554  -0.0573 0.0903  52  ASN A C   
41    O O   . ASN A 52  ? 0.9178 0.7612 0.8513 0.0609  -0.0744 0.1080  52  ASN A O   
42    C CB  . ASN A 52  ? 1.0326 0.9437 0.9646 0.0349  -0.0562 0.0723  52  ASN A CB  
43    C CG  . ASN A 52  ? 1.0605 0.9989 1.0037 0.0339  -0.0595 0.0622  52  ASN A CG  
44    O OD1 . ASN A 52  ? 1.0388 0.9800 0.9977 0.0460  -0.0699 0.0667  52  ASN A OD1 
45    N ND2 . ASN A 52  ? 1.1040 1.0661 1.0418 0.0191  -0.0506 0.0455  52  ASN A ND2 
46    N N   . ALA A 53  ? 0.9991 0.8470 0.9347 0.0509  -0.0432 0.0831  53  ALA A N   
47    C CA  . ALA A 53  ? 0.9710 0.7938 0.8945 0.0506  -0.0446 0.0959  53  ALA A CA  
48    C C   . ALA A 53  ? 0.8992 0.6983 0.8433 0.0704  -0.0479 0.1008  53  ALA A C   
49    O O   . ALA A 53  ? 0.8824 0.6588 0.8199 0.0747  -0.0593 0.1162  53  ALA A O   
50    C CB  . ALA A 53  ? 0.9843 0.8108 0.9021 0.0409  -0.0285 0.0828  53  ALA A CB  
51    N N   . LEU A 54  ? 0.9415 0.7451 0.9097 0.0807  -0.0386 0.0870  54  LEU A N   
52    C CA  . LEU A 54  ? 0.8881 0.6791 0.8771 0.0965  -0.0405 0.0875  54  LEU A CA  
53    C C   . LEU A 54  ? 0.9007 0.6971 0.9001 0.1068  -0.0586 0.0945  54  LEU A C   
54    O O   . LEU A 54  ? 0.8737 0.6534 0.8830 0.1192  -0.0682 0.1004  54  LEU A O   
55    C CB  . LEU A 54  ? 0.8624 0.6614 0.8692 0.0988  -0.0280 0.0720  54  LEU A CB  
56    C CG  . LEU A 54  ? 0.8159 0.5984 0.8230 0.0982  -0.0155 0.0666  54  LEU A CG  
57    C CD1 . LEU A 54  ? 0.7760 0.5403 0.7872 0.1068  -0.0163 0.0733  54  LEU A CD1 
58    C CD2 . LEU A 54  ? 0.8305 0.6114 0.8224 0.0887  -0.0102 0.0634  54  LEU A CD2 
59    N N   . LEU A 55  ? 0.8771 0.6973 0.8767 0.1029  -0.0650 0.0919  55  LEU A N   
60    C CA  . LEU A 55  ? 0.8894 0.7191 0.9019 0.1143  -0.0851 0.0963  55  LEU A CA  
61    C C   . LEU A 55  ? 0.8948 0.6985 0.8893 0.1162  -0.1066 0.1177  55  LEU A C   
62    O O   . LEU A 55  ? 0.8804 0.6751 0.8918 0.1331  -0.1262 0.1217  55  LEU A O   
63    C CB  . LEU A 55  ? 0.9388 0.8006 0.9506 0.1064  -0.0877 0.0899  55  LEU A CB  
64    C CG  . LEU A 55  ? 0.9387 0.8288 0.9793 0.1120  -0.0813 0.0709  55  LEU A CG  
65    C CD1 . LEU A 55  ? 0.9891 0.9064 1.0223 0.0978  -0.0772 0.0629  55  LEU A CD1 
66    C CD2 . LEU A 55  ? 0.9284 0.8296 0.9962 0.1310  -0.0994 0.0685  55  LEU A CD2 
67    N N   . LYS A 56  ? 0.9641 0.7554 0.9243 0.0977  -0.1046 0.1302  56  LYS A N   
68    C CA  . LYS A 56  ? 0.9744 0.7350 0.9095 0.0931  -0.1250 0.1533  56  LYS A CA  
69    C C   . LYS A 56  ? 0.9280 0.6544 0.8735 0.1057  -0.1262 0.1566  56  LYS A C   
70    O O   . LYS A 56  ? 0.9242 0.6211 0.8678 0.1146  -0.1502 0.1713  56  LYS A O   
71    C CB  . LYS A 56  ? 1.0199 0.7829 0.9138 0.0643  -0.1187 0.1623  56  LYS A CB  
72    C CG  . LYS A 56  ? 1.0241 0.7500 0.8864 0.0520  -0.1304 0.1842  56  LYS A CG  
73    C CD  . LYS A 56  ? 1.0807 0.8132 0.8977 0.0217  -0.1399 0.2002  56  LYS A CD  
74    C CE  . LYS A 56  ? 1.0892 0.7911 0.8689 -0.0005 -0.1423 0.2175  56  LYS A CE  
75    N NZ  . LYS A 56  ? 1.1252 0.8092 0.8590 -0.0242 -0.1694 0.2461  56  LYS A NZ  
76    N N   . TRP A 57  ? 1.0250 0.7532 0.9817 0.1067  -0.1027 0.1428  57  TRP A N   
77    C CA  . TRP A 57  ? 0.9816 0.6821 0.9497 0.1177  -0.1015 0.1429  57  TRP A CA  
78    C C   . TRP A 57  ? 0.9524 0.6551 0.9588 0.1427  -0.1125 0.1328  57  TRP A C   
79    O O   . TRP A 57  ? 0.9354 0.6102 0.9509 0.1549  -0.1264 0.1375  57  TRP A O   
80    C CB  . TRP A 57  ? 0.9525 0.6586 0.9231 0.1122  -0.0751 0.1298  57  TRP A CB  
81    C CG  . TRP A 57  ? 0.9095 0.5930 0.8930 0.1224  -0.0716 0.1273  57  TRP A CG  
82    C CD1 . TRP A 57  ? 0.9095 0.5590 0.8829 0.1233  -0.0843 0.1404  57  TRP A CD1 
83    C CD2 . TRP A 57  ? 0.8668 0.5592 0.8733 0.1305  -0.0551 0.1107  57  TRP A CD2 
84    N NE1 . TRP A 57  ? 0.8696 0.5090 0.8616 0.1332  -0.0753 0.1305  57  TRP A NE1 
85    C CE2 . TRP A 57  ? 0.8435 0.5108 0.8550 0.1370  -0.0572 0.1126  57  TRP A CE2 
86    C CE3 . TRP A 57  ? 0.8520 0.5690 0.8723 0.1304  -0.0401 0.0953  57  TRP A CE3 
87    C CZ2 . TRP A 57  ? 0.8080 0.4792 0.8382 0.1432  -0.0435 0.0985  57  TRP A CZ2 
88    C CZ3 . TRP A 57  ? 0.8153 0.5324 0.8506 0.1349  -0.0282 0.0842  57  TRP A CZ3 
89    C CH2 . TRP A 57  ? 0.7939 0.4910 0.8343 0.1412  -0.0293 0.0853  57  TRP A CH2 
90    N N   . LYS A 58  ? 0.9058 0.6435 0.9364 0.1495  -0.1064 0.1162  58  LYS A N   
91    C CA  . LYS A 58  ? 0.8886 0.6405 0.9587 0.1709  -0.1155 0.1009  58  LYS A CA  
92    C C   . LYS A 58  ? 0.9031 0.6391 0.9799 0.1858  -0.1488 0.1116  58  LYS A C   
93    O O   . LYS A 58  ? 0.8830 0.6170 0.9935 0.2073  -0.1616 0.0999  58  LYS A O   
94    C CB  . LYS A 58  ? 0.9018 0.6976 0.9903 0.1691  -0.1036 0.0823  58  LYS A CB  
95    C CG  . LYS A 58  ? 0.8932 0.7168 1.0247 0.1875  -0.1101 0.0609  58  LYS A CG  
96    C CD  . LYS A 58  ? 0.9210 0.7892 1.0647 0.1806  -0.1008 0.0450  58  LYS A CD  
97    C CE  . LYS A 58  ? 0.9246 0.8266 1.1087 0.1990  -0.1170 0.0263  58  LYS A CE  
98    N NZ  . LYS A 58  ? 0.9588 0.9047 1.1501 0.1894  -0.1108 0.0133  58  LYS A NZ  
99    N N   . SER A 59  ? 0.9396 0.6635 0.9846 0.1742  -0.1650 0.1329  59  SER A N   
100   C CA  . SER A 59  ? 0.9575 0.6602 1.0030 0.1864  -0.2021 0.1475  59  SER A CA  
101   C C   . SER A 59  ? 0.9406 0.5923 0.9842 0.1957  -0.2194 0.1588  59  SER A C   
102   O O   . SER A 59  ? 0.9412 0.5728 1.0040 0.2165  -0.2519 0.1616  59  SER A O   
103   C CB  . SER A 59  ? 1.0065 0.7065 1.0091 0.1649  -0.2141 0.1704  59  SER A CB  
104   O OG  . SER A 59  ? 1.0257 0.6799 1.0041 0.1642  -0.2478 0.1968  59  SER A OG  
105   N N   . THR A 60  ? 1.0190 0.6489 1.0418 0.1816  -0.1998 0.1638  60  THR A N   
106   C CA  . THR A 60  ? 1.0084 0.5881 1.0259 0.1865  -0.2140 0.1744  60  THR A CA  
107   C C   . THR A 60  ? 0.9704 0.5522 1.0398 0.2161  -0.2180 0.1500  60  THR A C   
108   O O   . THR A 60  ? 0.9680 0.5075 1.0448 0.2290  -0.2419 0.1556  60  THR A O   
109   C CB  . THR A 60  ? 1.0051 0.5717 0.9895 0.1619  -0.1882 0.1816  60  THR A CB  
110   O OG1 . THR A 60  ? 1.0474 0.6003 0.9813 0.1338  -0.1947 0.2065  60  THR A OG1 
111   C CG2 . THR A 60  ? 0.9853 0.5123 0.9760 0.1685  -0.1906 0.1813  60  THR A CG2 
112   N N   . PHE A 61  ? 0.9752 0.6064 1.0807 0.2261  -0.1978 0.1219  61  PHE A N   
113   C CA  . PHE A 61  ? 0.9418 0.5862 1.0945 0.2476  -0.1934 0.0936  61  PHE A CA  
114   C C   . PHE A 61  ? 0.9434 0.5755 1.1323 0.2768  -0.2306 0.0859  61  PHE A C   
115   O O   . PHE A 61  ? 0.9649 0.6048 1.1572 0.2844  -0.2547 0.0921  61  PHE A O   
116   C CB  . PHE A 61  ? 0.9295 0.6329 1.1069 0.2457  -0.1653 0.0668  61  PHE A CB  
117   C CG  . PHE A 61  ? 0.9254 0.6368 1.0726 0.2208  -0.1326 0.0716  61  PHE A CG  
118   C CD1 . PHE A 61  ? 0.9204 0.5957 1.0329 0.2060  -0.1252 0.0901  61  PHE A CD1 
119   C CD2 . PHE A 61  ? 0.9295 0.6841 1.0839 0.2118  -0.1111 0.0565  61  PHE A CD2 
120   C CE1 . PHE A 61  ? 0.9133 0.5980 1.0036 0.1866  -0.0984 0.0913  61  PHE A CE1 
121   C CE2 . PHE A 61  ? 0.9256 0.6820 1.0545 0.1916  -0.0862 0.0606  61  PHE A CE2 
122   C CZ  . PHE A 61  ? 0.9140 0.6366 1.0132 0.1809  -0.0806 0.0769  61  PHE A CZ  
123   N N   . THR A 62  ? 1.0386 0.6565 1.2531 0.2905  -0.2333 0.0705  62  THR A N   
124   C CA  . THR A 62  ? 1.0679 0.6836 1.3121 0.3102  -0.2588 0.0580  62  THR A CA  
125   C C   . THR A 62  ? 1.0383 0.7060 1.3440 0.3314  -0.2493 0.0134  62  THR A C   
126   O O   . THR A 62  ? 0.9980 0.6908 1.3170 0.3273  -0.2209 -0.0054 62  THR A O   
127   C CB  . THR A 62  ? 1.1148 0.6786 1.3359 0.3030  -0.2673 0.0729  62  THR A CB  
128   O OG1 . THR A 62  ? 1.0945 0.6691 1.3432 0.3091  -0.2481 0.0466  62  THR A OG1 
129   C CG2 . THR A 62  ? 1.1249 0.6486 1.2848 0.2737  -0.2595 0.1091  62  THR A CG2 
130   N N   . ASN A 63  ? 1.0891 0.7752 1.4318 0.3526  -0.2742 -0.0047 63  ASN A N   
131   C CA  . ASN A 63  ? 1.0715 0.8120 1.4758 0.3722  -0.2691 -0.0516 63  ASN A CA  
132   C C   . ASN A 63  ? 1.0097 0.8129 1.4385 0.3697  -0.2421 -0.0766 63  ASN A C   
133   O O   . ASN A 63  ? 0.9851 0.8340 1.4533 0.3743  -0.2233 -0.1145 63  ASN A O   
134   C CB  . ASN A 63  ? 1.0821 0.8081 1.4994 0.3739  -0.2600 -0.0682 63  ASN A CB  
135   C CG  . ASN A 63  ? 1.1500 0.8262 1.5622 0.3827  -0.2917 -0.0569 63  ASN A CG  
136   O OD1 . ASN A 63  ? 1.1917 0.8312 1.5757 0.3810  -0.3179 -0.0271 63  ASN A OD1 
137   N ND2 . ASN A 63  ? 1.1652 0.8398 1.6045 0.3911  -0.2905 -0.0815 63  ASN A ND2 
138   N N   . GLN A 64  ? 1.0028 0.8109 1.4089 0.3609  -0.2404 -0.0573 64  GLN A N   
139   C CA  . GLN A 64  ? 1.0072 0.8770 1.4140 0.3410  -0.2054 -0.0741 64  GLN A CA  
140   C C   . GLN A 64  ? 1.0059 0.9386 1.4599 0.3564  -0.2166 -0.1053 64  GLN A C   
141   O O   . GLN A 64  ? 1.0179 0.9428 1.4757 0.3706  -0.2478 -0.0943 64  GLN A O   
142   C CB  . GLN A 64  ? 1.0342 0.8861 1.3808 0.3111  -0.1888 -0.0386 64  GLN A CB  
143   C CG  . GLN A 64  ? 1.0399 0.9261 1.3707 0.2839  -0.1480 -0.0472 64  GLN A CG  
144   C CD  . GLN A 64  ? 1.0217 0.8866 1.3416 0.2748  -0.1272 -0.0480 64  GLN A CD  
145   O OE1 . GLN A 64  ? 1.0179 0.8326 1.3020 0.2672  -0.1276 -0.0210 64  GLN A OE1 
146   N NE2 . GLN A 64  ? 1.0127 0.9197 1.3625 0.2730  -0.1084 -0.0804 64  GLN A NE2 
147   N N   . THR A 65  ? 0.9415 0.9389 1.4303 0.3515  -0.1918 -0.1448 65  THR A N   
148   C CA  . THR A 65  ? 0.9343 1.0034 1.4709 0.3620  -0.1972 -0.1810 65  THR A CA  
149   C C   . THR A 65  ? 0.9658 1.0697 1.4723 0.3322  -0.1743 -0.1725 65  THR A C   
150   O O   . THR A 65  ? 0.9906 1.0720 1.4470 0.3031  -0.1489 -0.1475 65  THR A O   
151   C CB  . THR A 65  ? 0.9022 1.0317 1.4938 0.3684  -0.1819 -0.2333 65  THR A CB  
152   O OG1 . THR A 65  ? 0.9180 1.0907 1.4889 0.3319  -0.1398 -0.2429 65  THR A OG1 
153   C CG2 . THR A 65  ? 0.8795 0.9664 1.4833 0.3842  -0.1887 -0.2374 65  THR A CG2 
154   N N   . SER A 66  ? 0.8677 1.0273 1.4081 0.3409  -0.1855 -0.1956 66  SER A N   
155   C CA  . SER A 66  ? 0.8984 1.0939 1.4152 0.3136  -0.1667 -0.1914 66  SER A CA  
156   C C   . SER A 66  ? 0.9077 1.1470 1.4176 0.2806  -0.1255 -0.2119 66  SER A C   
157   O O   . SER A 66  ? 0.9418 1.1958 1.4209 0.2521  -0.1069 -0.2026 66  SER A O   
158   C CB  . SER A 66  ? 0.8879 1.1364 1.4466 0.3316  -0.1904 -0.2145 66  SER A CB  
159   O OG  . SER A 66  ? 0.8444 1.1526 1.4703 0.3523  -0.1956 -0.2649 66  SER A OG  
160   N N   . SER A 67  ? 0.8413 1.0999 1.3769 0.2821  -0.1123 -0.2392 67  SER A N   
161   C CA  . SER A 67  ? 0.8542 1.1504 1.3778 0.2474  -0.0750 -0.2564 67  SER A CA  
162   C C   . SER A 67  ? 0.8825 1.1189 1.3507 0.2258  -0.0561 -0.2221 67  SER A C   
163   O O   . SER A 67  ? 0.8980 1.1542 1.3514 0.1974  -0.0286 -0.2319 67  SER A O   
164   C CB  . SER A 67  ? 0.8109 1.1686 1.3912 0.2564  -0.0691 -0.3079 67  SER A CB  
165   O OG  . SER A 67  ? 0.7849 1.1021 1.3801 0.2810  -0.0812 -0.3076 67  SER A OG  
166   N N   . SER A 68  ? 0.8434 1.0095 1.2802 0.2372  -0.0713 -0.1832 68  SER A N   
167   C CA  . SER A 68  ? 0.8608 0.9739 1.2484 0.2186  -0.0550 -0.1529 68  SER A CA  
168   C C   . SER A 68  ? 0.9089 1.0264 1.2554 0.1839  -0.0331 -0.1392 68  SER A C   
169   O O   . SER A 68  ? 0.9315 1.0733 1.2766 0.1765  -0.0354 -0.1403 68  SER A O   
170   C CB  . SER A 68  ? 0.8487 0.8935 1.2119 0.2350  -0.0762 -0.1169 68  SER A CB  
171   O OG  . SER A 68  ? 0.8581 0.8586 1.1746 0.2159  -0.0602 -0.0897 68  SER A OG  
172   N N   . LYS A 69  ? 0.8008 0.8927 1.1143 0.1629  -0.0136 -0.1267 69  LYS A N   
173   C CA  . LYS A 69  ? 0.8527 0.9384 1.1262 0.1311  0.0034  -0.1127 69  LYS A CA  
174   C C   . LYS A 69  ? 0.8650 0.9143 1.1102 0.1326  -0.0068 -0.0840 69  LYS A C   
175   O O   . LYS A 69  ? 0.9100 0.9641 1.1335 0.1112  0.0013  -0.0788 69  LYS A O   
176   C CB  . LYS A 69  ? 0.8682 0.9262 1.1122 0.1125  0.0202  -0.1026 69  LYS A CB  
177   C CG  . LYS A 69  ? 0.8742 0.9761 1.1355 0.0978  0.0360  -0.1315 69  LYS A CG  
178   C CD  . LYS A 69  ? 0.9141 1.0660 1.1737 0.0681  0.0487  -0.1494 69  LYS A CD  
179   C CE  . LYS A 69  ? 0.9316 1.1088 1.1791 0.0364  0.0691  -0.1641 69  LYS A CE  
180   N NZ  . LYS A 69  ? 0.9033 1.0682 1.1612 0.0497  0.0710  -0.1688 69  LYS A NZ  
181   N N   . LEU A 70  ? 0.8713 0.8849 1.1152 0.1551  -0.0248 -0.0663 70  LEU A N   
182   C CA  . LEU A 70  ? 0.8774 0.8584 1.0915 0.1536  -0.0331 -0.0400 70  LEU A CA  
183   C C   . LEU A 70  ? 0.8983 0.9080 1.1246 0.1583  -0.0465 -0.0445 70  LEU A C   
184   O O   . LEU A 70  ? 0.9051 0.8934 1.1102 0.1590  -0.0568 -0.0249 70  LEU A O   
185   C CB  . LEU A 70  ? 0.8357 0.7696 1.0381 0.1695  -0.0465 -0.0189 70  LEU A CB  
186   C CG  . LEU A 70  ? 0.8127 0.7081 0.9881 0.1604  -0.0337 -0.0049 70  LEU A CG  
187   C CD1 . LEU A 70  ? 0.8161 0.7263 1.0002 0.1510  -0.0160 -0.0214 70  LEU A CD1 
188   C CD2 . LEU A 70  ? 0.7763 0.6326 0.9458 0.1754  -0.0479 0.0110  70  LEU A CD2 
189   N N   . SER A 71  ? 0.8332 0.8955 1.0937 0.1601  -0.0464 -0.0721 71  SER A N   
190   C CA  . SER A 71  ? 0.8522 0.9496 1.1246 0.1606  -0.0563 -0.0797 71  SER A CA  
191   C C   . SER A 71  ? 0.9020 0.9954 1.1406 0.1335  -0.0429 -0.0695 71  SER A C   
192   O O   . SER A 71  ? 0.9193 1.0289 1.1572 0.1326  -0.0521 -0.0680 71  SER A O   
193   C CB  . SER A 71  ? 0.8396 1.0019 1.1567 0.1637  -0.0545 -0.1168 71  SER A CB  
194   O OG  . SER A 71  ? 0.7958 0.9627 1.1469 0.1866  -0.0629 -0.1325 71  SER A OG  
195   N N   . SER A 72  ? 0.8287 0.9003 1.0405 0.1116  -0.0232 -0.0634 72  SER A N   
196   C CA  . SER A 72  ? 0.8810 0.9419 1.0624 0.0867  -0.0128 -0.0553 72  SER A CA  
197   C C   . SER A 72  ? 0.8779 0.8998 1.0331 0.0908  -0.0209 -0.0320 72  SER A C   
198   O O   . SER A 72  ? 0.9190 0.9354 1.0547 0.0740  -0.0160 -0.0288 72  SER A O   
199   C CB  . SER A 72  ? 0.9127 0.9562 1.0732 0.0634  0.0055  -0.0549 72  SER A CB  
200   O OG  . SER A 72  ? 0.8718 0.8845 1.0282 0.0742  0.0067  -0.0456 72  SER A OG  
201   N N   . TRP A 73  ? 0.9295 0.9257 1.0833 0.1104  -0.0332 -0.0175 73  TRP A N   
202   C CA  . TRP A 73  ? 0.9229 0.8874 1.0498 0.1103  -0.0391 0.0026  73  TRP A CA  
203   C C   . TRP A 73  ? 0.9475 0.9342 1.0781 0.1148  -0.0548 0.0041  73  TRP A C   
204   O O   . TRP A 73  ? 0.9279 0.9116 1.0651 0.1313  -0.0738 0.0125  73  TRP A O   
205   C CB  . TRP A 73  ? 0.8716 0.8009 0.9910 0.1236  -0.0452 0.0177  73  TRP A CB  
206   C CG  . TRP A 73  ? 0.8415 0.7472 0.9532 0.1184  -0.0305 0.0183  73  TRP A CG  
207   C CD1 . TRP A 73  ? 0.8571 0.7721 0.9724 0.1060  -0.0159 0.0063  73  TRP A CD1 
208   C CD2 . TRP A 73  ? 0.7967 0.6666 0.8933 0.1230  -0.0301 0.0320  73  TRP A CD2 
209   N NE1 . TRP A 73  ? 0.8202 0.7068 0.9239 0.1043  -0.0078 0.0125  73  TRP A NE1 
210   C CE2 . TRP A 73  ? 0.7788 0.6390 0.8730 0.1156  -0.0156 0.0269  73  TRP A CE2 
211   C CE3 . TRP A 73  ? 0.7781 0.6243 0.8606 0.1296  -0.0408 0.0482  73  TRP A CE3 
212   C CZ2 . TRP A 73  ? 0.7341 0.5642 0.8162 0.1175  -0.0116 0.0359  73  TRP A CZ2 
213   C CZ3 . TRP A 73  ? 0.7409 0.5576 0.8103 0.1294  -0.0352 0.0564  73  TRP A CZ3 
214   C CH2 . TRP A 73  ? 0.7151 0.5253 0.7864 0.1249  -0.0207 0.0494  73  TRP A CH2 
215   N N   . VAL A 74  ? 0.9101 0.9167 1.0347 0.0988  -0.0489 -0.0035 74  VAL A N   
216   C CA  . VAL A 74  ? 0.9319 0.9660 1.0607 0.1009  -0.0631 -0.0045 74  VAL A CA  
217   C C   . VAL A 74  ? 0.9692 0.9928 1.0699 0.0858  -0.0601 0.0033  74  VAL A C   
218   O O   . VAL A 74  ? 0.9714 0.9887 1.0576 0.0892  -0.0729 0.0167  74  VAL A O   
219   C CB  . VAL A 74  ? 0.9452 1.0278 1.1002 0.0960  -0.0608 -0.0271 74  VAL A CB  
220   C CG1 . VAL A 74  ? 0.9392 1.0541 1.1081 0.1068  -0.0816 -0.0291 74  VAL A CG1 
221   C CG2 . VAL A 74  ? 0.9166 1.0141 1.0985 0.1035  -0.0554 -0.0422 74  VAL A CG2 
222   N N   . ASN A 75  ? 0.9970 1.0177 1.0888 0.0674  -0.0442 -0.0058 75  ASN A N   
223   C CA  . ASN A 75  ? 1.0361 1.0541 1.1086 0.0536  -0.0417 -0.0061 75  ASN A CA  
224   C C   . ASN A 75  ? 1.0232 1.0030 1.0760 0.0512  -0.0347 0.0020  75  ASN A C   
225   O O   . ASN A 75  ? 0.9913 0.9467 1.0430 0.0484  -0.0248 0.0000  75  ASN A O   
226   C CB  . ASN A 75  ? 1.0611 1.0952 1.1369 0.0351  -0.0320 -0.0226 75  ASN A CB  
227   C CG  . ASN A 75  ? 1.0737 1.0991 1.1324 0.0209  -0.0283 -0.0271 75  ASN A CG  
228   O OD1 . ASN A 75  ? 1.0791 1.1067 1.1269 0.0233  -0.0343 -0.0216 75  ASN A OD1 
229   N ND2 . ASN A 75  ? 1.0624 1.0776 1.1180 0.0041  -0.0190 -0.0385 75  ASN A ND2 
230   N N   . PRO A 76  ? 1.0419 1.0183 1.0786 0.0506  -0.0401 0.0097  76  PRO A N   
231   C CA  . PRO A 76  ? 1.0201 0.9685 1.0418 0.0480  -0.0329 0.0124  76  PRO A CA  
232   C C   . PRO A 76  ? 1.0217 0.9625 1.0405 0.0358  -0.0232 -0.0034 76  PRO A C   
233   O O   . PRO A 76  ? 0.9916 0.9120 1.0038 0.0357  -0.0183 -0.0060 76  PRO A O   
234   C CB  . PRO A 76  ? 1.0501 1.0077 1.0547 0.0463  -0.0423 0.0230  76  PRO A CB  
235   C CG  . PRO A 76  ? 1.0797 1.0707 1.0865 0.0416  -0.0520 0.0203  76  PRO A CG  
236   C CD  . PRO A 76  ? 1.0592 1.0601 1.0897 0.0510  -0.0544 0.0162  76  PRO A CD  
237   N N   . ASN A 77  ? 1.0886 1.0447 1.1138 0.0259  -0.0217 -0.0155 77  ASN A N   
238   C CA  . ASN A 77  ? 1.0663 1.0088 1.0897 0.0145  -0.0159 -0.0311 77  ASN A CA  
239   C C   . ASN A 77  ? 1.0192 0.9239 1.0438 0.0146  -0.0115 -0.0306 77  ASN A C   
240   O O   . ASN A 77  ? 1.0120 0.9124 1.0404 0.0171  -0.0100 -0.0226 77  ASN A O   
241   C CB  . ASN A 77  ? 1.0856 1.0532 1.1133 0.0013  -0.0165 -0.0435 77  ASN A CB  
242   C CG  . ASN A 77  ? 1.1084 1.1112 1.1314 -0.0024 -0.0215 -0.0472 77  ASN A CG  
243   O OD1 . ASN A 77  ? 1.1166 1.1219 1.1298 0.0006  -0.0231 -0.0431 77  ASN A OD1 
244   N ND2 . ASN A 77  ? 1.1108 1.1437 1.1388 -0.0118 -0.0238 -0.0554 77  ASN A ND2 
245   N N   . THR A 78  ? 1.0786 0.9571 1.1004 0.0116  -0.0108 -0.0409 78  THR A N   
246   C CA  . THR A 78  ? 1.0365 0.8732 1.0561 0.0116  -0.0111 -0.0387 78  THR A CA  
247   C C   . THR A 78  ? 1.0499 0.8776 1.0662 -0.0033 -0.0104 -0.0371 78  THR A C   
248   O O   . THR A 78  ? 1.0290 0.8289 1.0392 -0.0062 -0.0105 -0.0290 78  THR A O   
249   C CB  . THR A 78  ? 1.0105 0.8219 1.0320 0.0125  -0.0154 -0.0538 78  THR A CB  
250   O OG1 . THR A 78  ? 1.0136 0.8483 1.0385 0.0202  -0.0137 -0.0617 78  THR A OG1 
251   C CG2 . THR A 78  ? 0.9660 0.7330 0.9847 0.0178  -0.0198 -0.0482 78  THR A CG2 
252   N N   . SER A 79  ? 0.9982 0.8515 1.0168 -0.0158 -0.0097 -0.0454 79  SER A N   
253   C CA  . SER A 79  ? 1.0144 0.8646 1.0281 -0.0354 -0.0077 -0.0465 79  SER A CA  
254   C C   . SER A 79  ? 1.0253 0.8951 1.0426 -0.0345 -0.0024 -0.0373 79  SER A C   
255   O O   . SER A 79  ? 1.0336 0.9001 1.0442 -0.0534 0.0010  -0.0379 79  SER A O   
256   C CB  . SER A 79  ? 1.0394 0.9204 1.0568 -0.0491 -0.0072 -0.0597 79  SER A CB  
257   O OG  . SER A 79  ? 1.0584 0.9865 1.0867 -0.0379 -0.0070 -0.0599 79  SER A OG  
258   N N   . SER A 80  ? 0.9857 0.8761 1.0132 -0.0151 -0.0022 -0.0303 80  SER A N   
259   C CA  . SER A 80  ? 0.9948 0.9025 1.0305 -0.0118 0.0017  -0.0258 80  SER A CA  
260   C C   . SER A 80  ? 0.9567 0.8430 0.9918 0.0058  0.0013  -0.0141 80  SER A C   
261   O O   . SER A 80  ? 0.9487 0.8326 0.9856 0.0052  0.0055  -0.0109 80  SER A O   
262   C CB  . SER A 80  ? 1.0334 0.9922 1.0879 -0.0049 -0.0006 -0.0319 80  SER A CB  
263   O OG  . SER A 80  ? 1.0425 1.0094 1.0985 0.0094  -0.0083 -0.0278 80  SER A OG  
264   N N   . PHE A 81  ? 1.0363 0.9104 1.0684 0.0190  -0.0029 -0.0095 81  PHE A N   
265   C CA  . PHE A 81  ? 0.9856 0.8402 1.0158 0.0334  -0.0029 0.0007  81  PHE A CA  
266   C C   . PHE A 81  ? 0.9488 0.7679 0.9697 0.0274  -0.0001 0.0037  81  PHE A C   
267   O O   . PHE A 81  ? 0.9231 0.7363 0.9453 0.0328  0.0028  0.0103  81  PHE A O   
268   C CB  . PHE A 81  ? 0.9720 0.8222 0.9970 0.0414  -0.0064 0.0016  81  PHE A CB  
269   C CG  . PHE A 81  ? 0.9199 0.7501 0.9411 0.0525  -0.0055 0.0100  81  PHE A CG  
270   C CD1 . PHE A 81  ? 0.9005 0.7355 0.9258 0.0629  -0.0063 0.0204  81  PHE A CD1 
271   C CD2 . PHE A 81  ? 0.8908 0.6984 0.9066 0.0531  -0.0051 0.0052  81  PHE A CD2 
272   C CE1 . PHE A 81  ? 0.8546 0.6712 0.8752 0.0708  -0.0051 0.0277  81  PHE A CE1 
273   C CE2 . PHE A 81  ? 0.8497 0.6438 0.8630 0.0621  -0.0038 0.0109  81  PHE A CE2 
274   C CZ  . PHE A 81  ? 0.8323 0.6304 0.8461 0.0695  -0.0030 0.0231  81  PHE A CZ  
275   N N   . CYS A 82  ? 0.9900 0.7833 1.0012 0.0160  -0.0028 -0.0012 82  CYS A N   
276   C CA  . CYS A 82  ? 0.9580 0.7108 0.9576 0.0108  -0.0055 0.0037  82  CYS A CA  
277   C C   . CYS A 82  ? 0.9869 0.7337 0.9753 -0.0109 -0.0033 0.0065  82  CYS A C   
278   O O   . CYS A 82  ? 0.9679 0.6781 0.9411 -0.0197 -0.0080 0.0132  82  CYS A O   
279   C CB  . CYS A 82  ? 0.9412 0.6626 0.9370 0.0111  -0.0145 -0.0038 82  CYS A CB  
280   S SG  . CYS A 82  ? 0.9031 0.6289 0.9093 0.0330  -0.0157 -0.0094 82  CYS A SG  
281   N N   . THR A 83  ? 0.9158 0.6992 0.9100 -0.0219 0.0028  0.0007  83  THR A N   
282   C CA  . THR A 83  ? 0.9426 0.7282 0.9247 -0.0479 0.0071  0.0005  83  THR A CA  
283   C C   . THR A 83  ? 0.9704 0.8041 0.9678 -0.0478 0.0171  -0.0053 83  THR A C   
284   O O   . THR A 83  ? 0.9756 0.8112 0.9635 -0.0645 0.0227  -0.0045 83  THR A O   
285   C CB  . THR A 83  ? 0.9686 0.7530 0.9414 -0.0712 0.0049  -0.0070 83  THR A CB  
286   O OG1 . THR A 83  ? 1.0019 0.8411 0.9925 -0.0724 0.0116  -0.0190 83  THR A OG1 
287   C CG2 . THR A 83  ? 0.9505 0.7026 0.9214 -0.0631 -0.0054 -0.0092 83  THR A CG2 
288   N N   . SER A 84  ? 0.8600 0.7333 0.8811 -0.0298 0.0179  -0.0125 84  SER A N   
289   C CA  . SER A 84  ? 0.8931 0.8159 0.9355 -0.0280 0.0238  -0.0238 84  SER A CA  
290   C C   . SER A 84  ? 0.8828 0.8155 0.9452 0.0006  0.0213  -0.0213 84  SER A C   
291   O O   . SER A 84  ? 0.9083 0.8783 0.9923 0.0052  0.0244  -0.0332 84  SER A O   
292   C CB  . SER A 84  ? 0.9231 0.8891 0.9804 -0.0327 0.0229  -0.0376 84  SER A CB  
293   O OG  . SER A 84  ? 0.9300 0.9013 0.9983 -0.0101 0.0139  -0.0343 84  SER A OG  
294   N N   . TRP A 85  ? 0.9416 0.8437 0.9986 0.0187  0.0151  -0.0086 85  TRP A N   
295   C CA  . TRP A 85  ? 0.9007 0.8047 0.9716 0.0420  0.0117  -0.0041 85  TRP A CA  
296   C C   . TRP A 85  ? 0.8801 0.7717 0.9480 0.0392  0.0187  -0.0030 85  TRP A C   
297   O O   . TRP A 85  ? 0.8546 0.7125 0.9017 0.0293  0.0212  0.0053  85  TRP A O   
298   C CB  . TRP A 85  ? 0.8476 0.7252 0.9089 0.0558  0.0046  0.0084  85  TRP A CB  
299   C CG  . TRP A 85  ? 0.8715 0.7683 0.9377 0.0618  -0.0039 0.0079  85  TRP A CG  
300   C CD1 . TRP A 85  ? 0.9293 0.8532 1.0006 0.0522  -0.0051 -0.0016 85  TRP A CD1 
301   C CD2 . TRP A 85  ? 0.8462 0.7375 0.9093 0.0755  -0.0131 0.0180  85  TRP A CD2 
302   N NE1 . TRP A 85  ? 0.9392 0.8757 1.0116 0.0605  -0.0150 0.0019  85  TRP A NE1 
303   C CE2 . TRP A 85  ? 0.8925 0.8086 0.9581 0.0735  -0.0203 0.0148  85  TRP A CE2 
304   C CE3 . TRP A 85  ? 0.7975 0.6661 0.8535 0.0861  -0.0159 0.0296  85  TRP A CE3 
305   C CZ2 . TRP A 85  ? 0.8955 0.8133 0.9538 0.0805  -0.0313 0.0244  85  TRP A CZ2 
306   C CZ3 . TRP A 85  ? 0.8047 0.6741 0.8528 0.0915  -0.0260 0.0389  85  TRP A CZ3 
307   C CH2 . TRP A 85  ? 0.8549 0.7483 0.9029 0.0881  -0.0341 0.0370  85  TRP A CH2 
308   N N   . TYR A 86  ? 0.8742 0.7938 0.9646 0.0486  0.0203  -0.0129 86  TYR A N   
309   C CA  . TYR A 86  ? 0.8666 0.7818 0.9563 0.0445  0.0282  -0.0154 86  TYR A CA  
310   C C   . TYR A 86  ? 0.7910 0.6648 0.8678 0.0567  0.0255  0.0004  86  TYR A C   
311   O O   . TYR A 86  ? 0.7418 0.6055 0.8250 0.0763  0.0175  0.0075  86  TYR A O   
312   C CB  . TYR A 86  ? 0.8711 0.8283 0.9942 0.0560  0.0290  -0.0344 86  TYR A CB  
313   C CG  . TYR A 86  ? 0.8666 0.8261 0.9925 0.0518  0.0380  -0.0412 86  TYR A CG  
314   C CD1 . TYR A 86  ? 0.9314 0.9150 1.0499 0.0242  0.0508  -0.0536 86  TYR A CD1 
315   C CD2 . TYR A 86  ? 0.8016 0.7406 0.9352 0.0723  0.0340  -0.0358 86  TYR A CD2 
316   C CE1 . TYR A 86  ? 0.9314 0.9217 1.0506 0.0176  0.0596  -0.0612 86  TYR A CE1 
317   C CE2 . TYR A 86  ? 0.8007 0.7442 0.9375 0.0679  0.0427  -0.0440 86  TYR A CE2 
318   C CZ  . TYR A 86  ? 0.8668 0.8376 0.9968 0.0408  0.0557  -0.0572 86  TYR A CZ  
319   O OH  . TYR A 86  ? 0.8691 0.8486 1.0005 0.0337  0.0649  -0.0665 86  TYR A OH  
320   N N   . GLY A 87  ? 0.8746 0.7244 0.9311 0.0428  0.0311  0.0063  87  GLY A N   
321   C CA  . GLY A 87  ? 0.8084 0.6262 0.8557 0.0526  0.0299  0.0174  87  GLY A CA  
322   C C   . GLY A 87  ? 0.7620 0.5453 0.7919 0.0555  0.0237  0.0294  87  GLY A C   
323   O O   . GLY A 87  ? 0.7129 0.4730 0.7358 0.0624  0.0228  0.0364  87  GLY A O   
324   N N   . VAL A 88  ? 0.8121 0.5947 0.8373 0.0503  0.0194  0.0290  88  VAL A N   
325   C CA  . VAL A 88  ? 0.7794 0.5353 0.7934 0.0537  0.0134  0.0343  88  VAL A CA  
326   C C   . VAL A 88  ? 0.8020 0.5349 0.7997 0.0361  0.0098  0.0344  88  VAL A C   
327   O O   . VAL A 88  ? 0.8516 0.5944 0.8447 0.0185  0.0119  0.0309  88  VAL A O   
328   C CB  . VAL A 88  ? 0.7865 0.5570 0.8077 0.0625  0.0093  0.0323  88  VAL A CB  
329   C CG1 . VAL A 88  ? 0.7791 0.5695 0.8138 0.0763  0.0083  0.0343  88  VAL A CG1 
330   C CG2 . VAL A 88  ? 0.8408 0.6259 0.8623 0.0504  0.0082  0.0254  88  VAL A CG2 
331   N N   . ALA A 89  ? 0.8389 0.5402 0.8280 0.0402  0.0030  0.0376  89  ALA A N   
332   C CA  . ALA A 89  ? 0.8506 0.5195 0.8251 0.0275  -0.0066 0.0382  89  ALA A CA  
333   C C   . ALA A 89  ? 0.8225 0.4753 0.8029 0.0409  -0.0153 0.0317  89  ALA A C   
334   O O   . ALA A 89  ? 0.7884 0.4457 0.7769 0.0563  -0.0138 0.0302  89  ALA A O   
335   C CB  . ALA A 89  ? 0.8449 0.4868 0.8022 0.0166  -0.0106 0.0473  89  ALA A CB  
336   N N   . CYS A 90  ? 0.8209 0.4572 0.7983 0.0338  -0.0240 0.0254  90  CYS A N   
337   C CA  . CYS A 90  ? 0.8073 0.4373 0.7959 0.0462  -0.0315 0.0124  90  CYS A CA  
338   C C   . CYS A 90  ? 0.7981 0.3816 0.7816 0.0456  -0.0495 0.0095  90  CYS A C   
339   O O   . CYS A 90  ? 0.8152 0.3672 0.7808 0.0294  -0.0581 0.0195  90  CYS A O   
340   C CB  . CYS A 90  ? 0.8419 0.4949 0.8372 0.0418  -0.0286 0.0018  90  CYS A CB  
341   S SG  . CYS A 90  ? 0.8631 0.5673 0.8653 0.0445  -0.0144 0.0048  90  CYS A SG  
342   N N   . SER A 91  ? 0.7705 0.3509 0.7701 0.0625  -0.0568 -0.0055 91  SER A N   
343   C CA  . SER A 91  ? 0.7887 0.3286 0.7931 0.0674  -0.0780 -0.0162 91  SER A CA  
344   C C   . SER A 91  ? 0.7845 0.3452 0.8107 0.0765  -0.0784 -0.0419 91  SER A C   
345   O O   . SER A 91  ? 0.7697 0.3713 0.8095 0.0861  -0.0664 -0.0531 91  SER A O   
346   C CB  . SER A 91  ? 0.7954 0.3145 0.8044 0.0819  -0.0895 -0.0159 91  SER A CB  
347   O OG  . SER A 91  ? 0.8339 0.3118 0.8517 0.0901  -0.1147 -0.0283 91  SER A OG  
348   N N   . LEU A 92  ? 0.8105 0.3437 0.8379 0.0704  -0.0921 -0.0514 92  LEU A N   
349   C CA  . LEU A 92  ? 0.8109 0.3644 0.8599 0.0768  -0.0929 -0.0794 92  LEU A CA  
350   C C   . LEU A 92  ? 0.7739 0.3860 0.8244 0.0716  -0.0703 -0.0819 92  LEU A C   
351   O O   . LEU A 92  ? 0.7603 0.4083 0.8278 0.0789  -0.0645 -0.1037 92  LEU A O   
352   C CB  . LEU A 92  ? 0.8162 0.3691 0.8927 0.0990  -0.1048 -0.1055 92  LEU A CB  
353   C CG  . LEU A 92  ? 0.8583 0.3506 0.9366 0.1081  -0.1330 -0.1043 92  LEU A CG  
354   C CD1 . LEU A 92  ? 0.8614 0.3636 0.9750 0.1330  -0.1451 -0.1370 92  LEU A CD1 
355   C CD2 . LEU A 92  ? 0.9060 0.3465 0.9730 0.0951  -0.1518 -0.1012 92  LEU A CD2 
356   N N   . GLY A 93  ? 0.7811 0.4044 0.8133 0.0578  -0.0589 -0.0603 93  GLY A N   
357   C CA  . GLY A 93  ? 0.8059 0.4787 0.8378 0.0535  -0.0425 -0.0591 93  GLY A CA  
358   C C   . GLY A 93  ? 0.7930 0.4980 0.8284 0.0636  -0.0321 -0.0567 93  GLY A C   
359   O O   . GLY A 93  ? 0.8185 0.5614 0.8576 0.0625  -0.0245 -0.0654 93  GLY A O   
360   N N   . SER A 94  ? 0.8385 0.5287 0.8704 0.0708  -0.0322 -0.0447 94  SER A N   
361   C CA  . SER A 94  ? 0.8301 0.5467 0.8617 0.0771  -0.0223 -0.0398 94  SER A CA  
362   C C   . SER A 94  ? 0.8014 0.5013 0.8233 0.0783  -0.0200 -0.0189 94  SER A C   
363   O O   . SER A 94  ? 0.7798 0.4466 0.7982 0.0785  -0.0283 -0.0144 94  SER A O   
364   C CB  . SER A 94  ? 0.8168 0.5426 0.8623 0.0873  -0.0244 -0.0600 94  SER A CB  
365   O OG  . SER A 94  ? 0.8102 0.5526 0.8511 0.0902  -0.0158 -0.0520 94  SER A OG  
366   N N   . ILE A 95  ? 0.8251 0.5464 0.8418 0.0782  -0.0107 -0.0068 95  ILE A N   
367   C CA  . ILE A 95  ? 0.7979 0.5080 0.8086 0.0790  -0.0076 0.0094  95  ILE A CA  
368   C C   . ILE A 95  ? 0.7615 0.4536 0.7734 0.0869  -0.0103 0.0082  95  ILE A C   
369   O O   . ILE A 95  ? 0.7586 0.4633 0.7754 0.0931  -0.0080 0.0004  95  ILE A O   
370   C CB  . ILE A 95  ? 0.8055 0.5391 0.8145 0.0802  -0.0006 0.0199  95  ILE A CB  
371   C CG1 . ILE A 95  ? 0.7746 0.4991 0.7821 0.0820  0.0027  0.0314  95  ILE A CG1 
372   C CG2 . ILE A 95  ? 0.8154 0.5655 0.8228 0.0835  0.0020  0.0174  95  ILE A CG2 
373   C CD1 . ILE A 95  ? 0.7796 0.5225 0.7904 0.0854  0.0054  0.0392  95  ILE A CD1 
374   N N   . ILE A 96  ? 0.8100 0.4747 0.8161 0.0843  -0.0157 0.0151  96  ILE A N   
375   C CA  . ILE A 96  ? 0.7803 0.4273 0.7862 0.0913  -0.0202 0.0160  96  ILE A CA  
376   C C   . ILE A 96  ? 0.7657 0.4103 0.7629 0.0876  -0.0137 0.0306  96  ILE A C   
377   O O   . ILE A 96  ? 0.7437 0.3796 0.7403 0.0929  -0.0151 0.0321  96  ILE A O   
378   C CB  . ILE A 96  ? 0.7789 0.3909 0.7842 0.0917  -0.0374 0.0108  96  ILE A CB  
379   C CG1 . ILE A 96  ? 0.7987 0.3864 0.7863 0.0753  -0.0420 0.0245  96  ILE A CG1 
380   C CG2 . ILE A 96  ? 0.7929 0.4081 0.8117 0.0967  -0.0445 -0.0084 96  ILE A CG2 
381   C CD1 . ILE A 96  ? 0.8008 0.3432 0.7793 0.0724  -0.0626 0.0270  96  ILE A CD1 
382   N N   . ARG A 97  ? 0.8224 0.4793 0.8157 0.0791  -0.0065 0.0380  97  ARG A N   
383   C CA  . ARG A 97  ? 0.8196 0.4774 0.8071 0.0730  -0.0007 0.0468  97  ARG A CA  
384   C C   . ARG A 97  ? 0.8275 0.5139 0.8237 0.0745  0.0086  0.0473  97  ARG A C   
385   O O   . ARG A 97  ? 0.8575 0.5579 0.8572 0.0702  0.0087  0.0444  97  ARG A O   
386   C CB  . ARG A 97  ? 0.8518 0.4907 0.8246 0.0558  -0.0063 0.0514  97  ARG A CB  
387   C CG  . ARG A 97  ? 0.8548 0.4840 0.8159 0.0477  -0.0054 0.0588  97  ARG A CG  
388   C CD  . ARG A 97  ? 0.8908 0.4939 0.8295 0.0262  -0.0152 0.0659  97  ARG A CD  
389   N NE  . ARG A 97  ? 0.8730 0.4386 0.8011 0.0293  -0.0317 0.0712  97  ARG A NE  
390   C CZ  . ARG A 97  ? 0.8972 0.4276 0.8017 0.0117  -0.0469 0.0809  97  ARG A CZ  
391   N NH1 . ARG A 97  ? 0.9404 0.4697 0.8260 -0.0145 -0.0451 0.0864  97  ARG A NH1 
392   N NH2 . ARG A 97  ? 0.8816 0.3768 0.7804 0.0192  -0.0661 0.0848  97  ARG A NH2 
393   N N   . LEU A 98  ? 0.7684 0.4624 0.7696 0.0813  0.0144  0.0499  98  LEU A N   
394   C CA  . LEU A 98  ? 0.7756 0.4915 0.7885 0.0863  0.0187  0.0494  98  LEU A CA  
395   C C   . LEU A 98  ? 0.7771 0.4978 0.7942 0.0845  0.0246  0.0481  98  LEU A C   
396   O O   . LEU A 98  ? 0.7481 0.4588 0.7636 0.0891  0.0267  0.0504  98  LEU A O   
397   C CB  . LEU A 98  ? 0.7559 0.4739 0.7716 0.0971  0.0168  0.0525  98  LEU A CB  
398   C CG  . LEU A 98  ? 0.7669 0.4996 0.7943 0.1043  0.0149  0.0540  98  LEU A CG  
399   C CD1 . LEU A 98  ? 0.8066 0.5587 0.8406 0.1018  0.0114  0.0502  98  LEU A CD1 
400   C CD2 . LEU A 98  ? 0.7575 0.4830 0.7799 0.1105  0.0106  0.0614  98  LEU A CD2 
401   N N   . ASN A 99  ? 0.7451 0.4858 0.7689 0.0762  0.0282  0.0418  99  ASN A N   
402   C CA  . ASN A 99  ? 0.7606 0.5141 0.7890 0.0698  0.0354  0.0352  99  ASN A CA  
403   C C   . ASN A 99  ? 0.7867 0.5718 0.8404 0.0781  0.0371  0.0232  99  ASN A C   
404   O O   . ASN A 99  ? 0.8368 0.6460 0.8978 0.0708  0.0379  0.0150  99  ASN A O   
405   C CB  . ASN A 99  ? 0.8111 0.5633 0.8219 0.0464  0.0377  0.0351  99  ASN A CB  
406   C CG  . ASN A 99  ? 0.8478 0.6136 0.8569 0.0347  0.0459  0.0288  99  ASN A CG  
407   O OD1 . ASN A 99  ? 0.8332 0.6099 0.8582 0.0464  0.0504  0.0220  99  ASN A OD1 
408   N ND2 . ASN A 99  ? 0.8976 0.6622 0.8854 0.0089  0.0472  0.0306  99  ASN A ND2 
409   N N   . LEU A 100 ? 0.7398 0.5245 0.8085 0.0936  0.0360  0.0207  100 LEU A N   
410   C CA  . LEU A 100 ? 0.7539 0.5634 0.8512 0.1065  0.0326  0.0077  100 LEU A CA  
411   C C   . LEU A 100 ? 0.7531 0.5715 0.8664 0.1106  0.0379  -0.0052 100 LEU A C   
412   O O   . LEU A 100 ? 0.7326 0.5520 0.8685 0.1285  0.0307  -0.0120 100 LEU A O   
413   C CB  . LEU A 100 ? 0.7209 0.5158 0.8227 0.1237  0.0195  0.0176  100 LEU A CB  
414   C CG  . LEU A 100 ? 0.7349 0.5319 0.8270 0.1203  0.0138  0.0250  100 LEU A CG  
415   C CD1 . LEU A 100 ? 0.7209 0.5061 0.8141 0.1339  -0.0002 0.0352  100 LEU A CD1 
416   C CD2 . LEU A 100 ? 0.7893 0.6215 0.8952 0.1130  0.0162  0.0107  100 LEU A CD2 
417   N N   . THR A 101 ? 0.7484 0.5716 0.8492 0.0934  0.0489  -0.0089 101 THR A N   
418   C CA  . THR A 101 ? 0.7614 0.6015 0.8772 0.0929  0.0564  -0.0254 101 THR A CA  
419   C C   . THR A 101 ? 0.7883 0.6726 0.9397 0.0986  0.0573  -0.0519 101 THR A C   
420   O O   . THR A 101 ? 0.8317 0.7451 0.9867 0.0877  0.0597  -0.0603 101 THR A O   
421   C CB  . THR A 101 ? 0.8099 0.6532 0.9013 0.0676  0.0672  -0.0244 101 THR A CB  
422   O OG1 . THR A 101 ? 0.7743 0.5785 0.8363 0.0644  0.0628  -0.0018 101 THR A OG1 
423   C CG2 . THR A 101 ? 0.8191 0.6782 0.9226 0.0662  0.0756  -0.0405 101 THR A CG2 
424   N N   . ASN A 102 ? 0.7394 0.6292 0.9193 0.1160  0.0544  -0.0672 102 ASN A N   
425   C CA  . ASN A 102 ? 0.7474 0.6850 0.9681 0.1224  0.0560  -0.1008 102 ASN A CA  
426   C C   . ASN A 102 ? 0.7494 0.7105 0.9914 0.1325  0.0458  -0.1084 102 ASN A C   
427   O O   . ASN A 102 ? 0.7721 0.7854 1.0355 0.1236  0.0526  -0.1344 102 ASN A O   
428   C CB  . ASN A 102 ? 0.7952 0.7749 1.0112 0.0943  0.0749  -0.1204 102 ASN A CB  
429   C CG  . ASN A 102 ? 0.7742 0.8047 1.0354 0.1015  0.0793  -0.1610 102 ASN A CG  
430   O OD1 . ASN A 102 ? 0.7266 0.7486 1.0217 0.1300  0.0674  -0.1728 102 ASN A OD1 
431   N ND2 . ASN A 102 ? 0.8049 0.8890 1.0672 0.0742  0.0954  -0.1841 102 ASN A ND2 
432   N N   . THR A 103 ? 0.7519 0.6781 0.9876 0.1492  0.0295  -0.0868 103 THR A N   
433   C CA  . THR A 103 ? 0.7566 0.7005 1.0083 0.1591  0.0173  -0.0898 103 THR A CA  
434   C C   . THR A 103 ? 0.7208 0.6664 1.0130 0.1901  -0.0038 -0.1034 103 THR A C   
435   O O   . THR A 103 ? 0.7237 0.6927 1.0376 0.2009  -0.0163 -0.1121 103 THR A O   
436   C CB  . THR A 103 ? 0.7577 0.6657 0.9742 0.1546  0.0114  -0.0580 103 THR A CB  
437   O OG1 . THR A 103 ? 0.7834 0.6808 0.9647 0.1297  0.0267  -0.0458 103 THR A OG1 
438   C CG2 . THR A 103 ? 0.7779 0.7109 1.0049 0.1571  0.0029  -0.0617 103 THR A CG2 
439   N N   . GLY A 104 ? 0.7736 0.6933 1.0769 0.2047  -0.0102 -0.1058 104 GLY A N   
440   C CA  . GLY A 104 ? 0.7461 0.6570 1.0869 0.2351  -0.0351 -0.1171 104 GLY A CA  
441   C C   . GLY A 104 ? 0.7395 0.6012 1.0607 0.2473  -0.0590 -0.0853 104 GLY A C   
442   O O   . GLY A 104 ? 0.7330 0.5939 1.0817 0.2699  -0.0843 -0.0913 104 GLY A O   
443   N N   . ILE A 105 ? 0.8343 0.6574 1.1089 0.2319  -0.0527 -0.0530 105 ILE A N   
444   C CA  . ILE A 105 ? 0.8334 0.6136 1.0826 0.2364  -0.0724 -0.0226 105 ILE A CA  
445   C C   . ILE A 105 ? 0.8180 0.5490 1.0665 0.2488  -0.0893 -0.0131 105 ILE A C   
446   O O   . ILE A 105 ? 0.8057 0.5231 1.0494 0.2433  -0.0768 -0.0165 105 ILE A O   
447   C CB  . ILE A 105 ? 0.8403 0.6079 1.0434 0.2130  -0.0573 0.0021  105 ILE A CB  
448   C CG1 . ILE A 105 ? 0.8647 0.6732 1.0680 0.2014  -0.0461 -0.0057 105 ILE A CG1 
449   C CG2 . ILE A 105 ? 0.8433 0.5699 1.0167 0.2126  -0.0746 0.0312  105 ILE A CG2 
450   C CD1 . ILE A 105 ? 0.8696 0.6712 1.0364 0.1788  -0.0280 0.0084  105 ILE A CD1 
451   N N   . GLU A 106 ? 0.9392 0.6414 1.1908 0.2642  -0.1195 -0.0006 106 GLU A N   
452   C CA  . GLU A 106 ? 0.9371 0.5830 1.1818 0.2732  -0.1409 0.0133  106 GLU A CA  
453   C C   . GLU A 106 ? 0.9594 0.5645 1.1572 0.2604  -0.1557 0.0511  106 GLU A C   
454   O O   . GLU A 106 ? 0.9777 0.5886 1.1737 0.2650  -0.1739 0.0600  106 GLU A O   
455   C CB  . GLU A 106 ? 0.9422 0.5944 1.2275 0.2969  -0.1640 -0.0073 106 GLU A CB  
456   C CG  . GLU A 106 ? 0.9801 0.5919 1.2554 0.2965  -0.1730 -0.0014 106 GLU A CG  
457   C CD  . GLU A 106 ? 1.0302 0.6309 1.3258 0.3142  -0.2053 -0.0053 106 GLU A CD  
458   O OE1 . GLU A 106 ? 1.0656 0.6350 1.3325 0.3100  -0.2272 0.0232  106 GLU A OE1 
459   O OE2 . GLU A 106 ? 1.0377 0.6615 1.3778 0.3315  -0.2100 -0.0378 106 GLU A OE2 
460   N N   . GLY A 107 ? 0.9425 0.5111 1.1023 0.2424  -0.1477 0.0715  107 GLY A N   
461   C CA  . GLY A 107 ? 0.9701 0.5072 1.0821 0.2240  -0.1579 0.1046  107 GLY A CA  
462   C C   . GLY A 107 ? 0.9708 0.4843 1.0461 0.2010  -0.1402 0.1180  107 GLY A C   
463   O O   . GLY A 107 ? 0.9533 0.4599 1.0388 0.2024  -0.1289 0.1064  107 GLY A O   
464   N N   . THR A 108 ? 0.9709 0.4805 1.0041 0.1780  -0.1360 0.1394  108 THR A N   
465   C CA  . THR A 108 ? 0.9798 0.4743 0.9771 0.1537  -0.1200 0.1507  108 THR A CA  
466   C C   . THR A 108 ? 0.9830 0.5146 0.9618 0.1363  -0.0972 0.1499  108 THR A C   
467   O O   . THR A 108 ? 0.9883 0.5474 0.9724 0.1391  -0.0979 0.1475  108 THR A O   
468   C CB  . THR A 108 ? 1.0214 0.4664 0.9798 0.1372  -0.1425 0.1781  108 THR A CB  
469   O OG1 . THR A 108 ? 1.0562 0.5100 0.9844 0.1214  -0.1504 0.1953  108 THR A OG1 
470   C CG2 . THR A 108 ? 1.0356 0.4558 1.0137 0.1539  -0.1665 0.1772  108 THR A CG2 
471   N N   . PHE A 109 ? 0.9644 0.4971 0.9237 0.1190  -0.0780 0.1498  109 PHE A N   
472   C CA  . PHE A 109 ? 0.9751 0.5382 0.9164 0.1022  -0.0598 0.1476  109 PHE A CA  
473   C C   . PHE A 109 ? 1.0294 0.5833 0.9297 0.0770  -0.0669 0.1659  109 PHE A C   
474   O O   . PHE A 109 ? 1.0496 0.6287 0.9343 0.0600  -0.0510 0.1607  109 PHE A O   
475   C CB  . PHE A 109 ? 0.9480 0.5236 0.8936 0.0979  -0.0368 0.1339  109 PHE A CB  
476   C CG  . PHE A 109 ? 0.8991 0.4871 0.8781 0.1160  -0.0281 0.1167  109 PHE A CG  
477   C CD1 . PHE A 109 ? 0.8832 0.4951 0.8834 0.1277  -0.0279 0.1074  109 PHE A CD1 
478   C CD2 . PHE A 109 ? 0.8767 0.4554 0.8633 0.1178  -0.0193 0.1089  109 PHE A CD2 
479   C CE1 . PHE A 109 ? 0.8503 0.4772 0.8764 0.1384  -0.0190 0.0912  109 PHE A CE1 
480   C CE2 . PHE A 109 ? 0.8410 0.4350 0.8544 0.1299  -0.0108 0.0926  109 PHE A CE2 
481   C CZ  . PHE A 109 ? 0.8302 0.4488 0.8622 0.1390  -0.0104 0.0840  109 PHE A CZ  
482   N N   . GLU A 110 ? 1.0988 0.6176 0.9811 0.0729  -0.0917 0.1859  110 GLU A N   
483   C CA  . GLU A 110 ? 1.1545 0.6634 0.9906 0.0424  -0.0991 0.2053  110 GLU A CA  
484   C C   . GLU A 110 ? 1.1825 0.7289 1.0084 0.0329  -0.0958 0.2042  110 GLU A C   
485   O O   . GLU A 110 ? 1.2237 0.7901 1.0198 0.0054  -0.0852 0.2052  110 GLU A O   
486   C CB  . GLU A 110 ? 1.1769 0.6321 0.9928 0.0394  -0.1315 0.2303  110 GLU A CB  
487   C CG  . GLU A 110 ? 1.2342 0.6738 0.9938 0.0005  -0.1398 0.2534  110 GLU A CG  
488   C CD  . GLU A 110 ? 1.2557 0.6295 0.9900 -0.0062 -0.1732 0.2804  110 GLU A CD  
489   O OE1 . GLU A 110 ? 1.2616 0.6111 0.9994 0.0080  -0.2041 0.2943  110 GLU A OE1 
490   O OE2 . GLU A 110 ? 1.2698 0.6146 0.9808 -0.0260 -0.1703 0.2873  110 GLU A OE2 
491   N N   . ASP A 111 ? 1.0596 0.6199 0.9113 0.0541  -0.1043 0.1992  111 ASP A N   
492   C CA  . ASP A 111 ? 1.0868 0.6841 0.9332 0.0470  -0.1007 0.1954  111 ASP A CA  
493   C C   . ASP A 111 ? 1.0573 0.6928 0.9351 0.0599  -0.0777 0.1700  111 ASP A C   
494   O O   . ASP A 111 ? 1.0661 0.7278 0.9545 0.0648  -0.0781 0.1633  111 ASP A O   
495   C CB  . ASP A 111 ? 1.0993 0.6866 0.9477 0.0574  -0.1288 0.2087  111 ASP A CB  
496   C CG  . ASP A 111 ? 1.1498 0.7105 0.9510 0.0321  -0.1517 0.2365  111 ASP A CG  
497   O OD1 . ASP A 111 ? 1.1835 0.7518 0.9483 0.0008  -0.1398 0.2411  111 ASP A OD1 
498   O OD2 . ASP A 111 ? 1.1568 0.6898 0.9568 0.0423  -0.1828 0.2531  111 ASP A OD2 
499   N N   . PHE A 112 ? 0.9690 0.6059 0.8601 0.0640  -0.0595 0.1568  112 PHE A N   
500   C CA  . PHE A 112 ? 0.9426 0.6096 0.8552 0.0709  -0.0401 0.1358  112 PHE A CA  
501   C C   . PHE A 112 ? 0.9937 0.6897 0.8890 0.0519  -0.0301 0.1283  112 PHE A C   
502   O O   . PHE A 112 ? 1.0372 0.7340 0.9067 0.0312  -0.0269 0.1323  112 PHE A O   
503   C CB  . PHE A 112 ? 0.8957 0.5548 0.8218 0.0774  -0.0266 0.1258  112 PHE A CB  
504   C CG  . PHE A 112 ? 0.8546 0.5343 0.8029 0.0869  -0.0128 0.1079  112 PHE A CG  
505   C CD1 . PHE A 112 ? 0.8183 0.5020 0.7906 0.1023  -0.0147 0.1022  112 PHE A CD1 
506   C CD2 . PHE A 112 ? 0.8596 0.5547 0.8046 0.0790  0.0003  0.0957  112 PHE A CD2 
507   C CE1 . PHE A 112 ? 0.7870 0.4845 0.7730 0.1059  -0.0040 0.0889  112 PHE A CE1 
508   C CE2 . PHE A 112 ? 0.8214 0.5269 0.7840 0.0872  0.0079  0.0820  112 PHE A CE2 
509   C CZ  . PHE A 112 ? 0.7850 0.4890 0.7648 0.0987  0.0057  0.0807  112 PHE A CZ  
510   N N   . PRO A 113 ? 0.9084 0.6303 0.8175 0.0565  -0.0247 0.1152  113 PRO A N   
511   C CA  . PRO A 113 ? 0.9709 0.7231 0.8678 0.0398  -0.0167 0.1038  113 PRO A CA  
512   C C   . PRO A 113 ? 0.9712 0.7367 0.8767 0.0378  -0.0004 0.0838  113 PRO A C   
513   O O   . PRO A 113 ? 0.9604 0.7405 0.8846 0.0454  0.0062  0.0660  113 PRO A O   
514   C CB  . PRO A 113 ? 0.9723 0.7412 0.8846 0.0484  -0.0200 0.0971  113 PRO A CB  
515   C CG  . PRO A 113 ? 0.8975 0.6521 0.8361 0.0692  -0.0196 0.0949  113 PRO A CG  
516   C CD  . PRO A 113 ? 0.8656 0.5920 0.8020 0.0752  -0.0264 0.1086  113 PRO A CD  
517   N N   . PHE A 114 ? 0.9662 0.7250 0.8578 0.0269  0.0041  0.0863  114 PHE A N   
518   C CA  . PHE A 114 ? 0.9740 0.7481 0.8761 0.0261  0.0175  0.0658  114 PHE A CA  
519   C C   . PHE A 114 ? 1.0489 0.8618 0.9548 0.0170  0.0242  0.0426  114 PHE A C   
520   O O   . PHE A 114 ? 1.0248 0.8484 0.9540 0.0284  0.0295  0.0213  114 PHE A O   
521   C CB  . PHE A 114 ? 0.9953 0.7620 0.8787 0.0111  0.0213  0.0714  114 PHE A CB  
522   C CG  . PHE A 114 ? 0.9291 0.6574 0.8132 0.0212  0.0153  0.0890  114 PHE A CG  
523   C CD1 . PHE A 114 ? 0.8648 0.5832 0.7711 0.0383  0.0209  0.0813  114 PHE A CD1 
524   C CD2 . PHE A 114 ? 0.9346 0.6358 0.7971 0.0133  0.0020  0.1124  114 PHE A CD2 
525   C CE1 . PHE A 114 ? 0.8150 0.5029 0.7241 0.0467  0.0165  0.0933  114 PHE A CE1 
526   C CE2 . PHE A 114 ? 0.8861 0.5518 0.7539 0.0246  -0.0050 0.1243  114 PHE A CE2 
527   C CZ  . PHE A 114 ? 0.8291 0.4910 0.7212 0.0410  0.0039  0.1131  114 PHE A CZ  
528   N N   . SER A 115 ? 0.9488 0.7823 0.8318 -0.0042 0.0224  0.0453  115 SER A N   
529   C CA  . SER A 115 ? 1.0221 0.8993 0.9088 -0.0162 0.0301  0.0189  115 SER A CA  
530   C C   . SER A 115 ? 1.0140 0.8983 0.9221 -0.0017 0.0271  0.0075  115 SER A C   
531   O O   . SER A 115 ? 1.0088 0.9279 0.9260 -0.0081 0.0326  -0.0185 115 SER A O   
532   C CB  . SER A 115 ? 1.0412 0.9411 0.8913 -0.0489 0.0297  0.0261  115 SER A CB  
533   O OG  . SER A 115 ? 1.0229 0.8915 0.8495 -0.0522 0.0147  0.0593  115 SER A OG  
534   N N   . SER A 116 ? 0.9514 0.8067 0.8689 0.0161  0.0188  0.0233  116 SER A N   
535   C CA  . SER A 116 ? 0.9356 0.7972 0.8679 0.0246  0.0154  0.0153  116 SER A CA  
536   C C   . SER A 116 ? 0.8364 0.6790 0.7956 0.0452  0.0157  0.0058  116 SER A C   
537   O O   . SER A 116 ? 0.8241 0.6709 0.7955 0.0497  0.0133  -0.0042 116 SER A O   
538   C CB  . SER A 116 ? 0.9371 0.7879 0.8574 0.0244  0.0043  0.0387  116 SER A CB  
539   O OG  . SER A 116 ? 0.9800 0.8339 0.8702 0.0059  -0.0012 0.0555  116 SER A OG  
540   N N   . LEU A 117 ? 0.9493 0.7704 0.9156 0.0552  0.0175  0.0093  117 LEU A N   
541   C CA  . LEU A 117 ? 0.8674 0.6661 0.8523 0.0709  0.0154  0.0056  117 LEU A CA  
542   C C   . LEU A 117 ? 0.8439 0.6426 0.8409 0.0765  0.0179  -0.0118 117 LEU A C   
543   O O   . LEU A 117 ? 0.7988 0.5792 0.7973 0.0830  0.0184  -0.0047 117 LEU A O   
544   C CB  . LEU A 117 ? 0.8118 0.5851 0.7948 0.0783  0.0131  0.0263  117 LEU A CB  
545   C CG  . LEU A 117 ? 0.8305 0.6050 0.8049 0.0758  0.0080  0.0428  117 LEU A CG  
546   C CD1 . LEU A 117 ? 0.7723 0.5265 0.7531 0.0857  0.0061  0.0550  117 LEU A CD1 
547   C CD2 . LEU A 117 ? 0.8607 0.6496 0.8396 0.0735  0.0048  0.0363  117 LEU A CD2 
548   N N   . PRO A 118 ? 0.8307 0.6517 0.8392 0.0750  0.0182  -0.0373 118 PRO A N   
549   C CA  . PRO A 118 ? 0.8065 0.6331 0.8310 0.0822  0.0181  -0.0580 118 PRO A CA  
550   C C   . PRO A 118 ? 0.7363 0.5287 0.7749 0.0988  0.0082  -0.0572 118 PRO A C   
551   O O   . PRO A 118 ? 0.7113 0.5020 0.7609 0.1067  0.0057  -0.0678 118 PRO A O   
552   C CB  . PRO A 118 ? 0.8298 0.6928 0.8679 0.0776  0.0192  -0.0897 118 PRO A CB  
553   C CG  . PRO A 118 ? 0.8445 0.7043 0.8790 0.0746  0.0158  -0.0851 118 PRO A CG  
554   C CD  . PRO A 118 ? 0.8722 0.7170 0.8832 0.0679  0.0176  -0.0519 118 PRO A CD  
555   N N   . ASN A 119 ? 0.8647 0.6308 0.9012 0.1020  0.0018  -0.0448 119 ASN A N   
556   C CA  . ASN A 119 ? 0.8186 0.5507 0.8633 0.1123  -0.0102 -0.0445 119 ASN A CA  
557   C C   . ASN A 119 ? 0.7887 0.4950 0.8205 0.1116  -0.0095 -0.0198 119 ASN A C   
558   O O   . ASN A 119 ? 0.7675 0.4444 0.7977 0.1135  -0.0191 -0.0139 119 ASN A O   
559   C CB  . ASN A 119 ? 0.8238 0.5438 0.8738 0.1118  -0.0191 -0.0516 119 ASN A CB  
560   C CG  . ASN A 119 ? 0.8411 0.5849 0.9098 0.1149  -0.0222 -0.0823 119 ASN A CG  
561   O OD1 . ASN A 119 ? 0.8337 0.5951 0.9176 0.1218  -0.0231 -0.1030 119 ASN A OD1 
562   N ND2 . ASN A 119 ? 0.8636 0.6122 0.9333 0.1091  -0.0235 -0.0887 119 ASN A ND2 
563   N N   . LEU A 120 ? 0.8012 0.5173 0.8228 0.1073  0.0007  -0.0062 120 LEU A N   
564   C CA  . LEU A 120 ? 0.7678 0.4651 0.7813 0.1070  0.0024  0.0118  120 LEU A CA  
565   C C   . LEU A 120 ? 0.7439 0.4243 0.7607 0.1131  -0.0034 0.0091  120 LEU A C   
566   O O   . LEU A 120 ? 0.7472 0.4391 0.7699 0.1172  -0.0019 -0.0010 120 LEU A O   
567   C CB  . LEU A 120 ? 0.7679 0.4764 0.7735 0.1034  0.0117  0.0234  120 LEU A CB  
568   C CG  . LEU A 120 ? 0.7922 0.5122 0.7928 0.0985  0.0133  0.0311  120 LEU A CG  
569   C CD1 . LEU A 120 ? 0.7922 0.5134 0.7853 0.0969  0.0169  0.0436  120 LEU A CD1 
570   C CD2 . LEU A 120 ? 0.7846 0.4972 0.7878 0.0978  0.0102  0.0357  120 LEU A CD2 
571   N N   . THR A 121 ? 0.7905 0.4455 0.8018 0.1115  -0.0109 0.0176  121 THR A N   
572   C CA  . THR A 121 ? 0.7756 0.4119 0.7850 0.1149  -0.0187 0.0194  121 THR A CA  
573   C C   . THR A 121 ? 0.7679 0.3955 0.7641 0.1067  -0.0135 0.0355  121 THR A C   
574   O O   . THR A 121 ? 0.7607 0.3802 0.7537 0.1079  -0.0164 0.0378  121 THR A O   
575   C CB  . THR A 121 ? 0.7794 0.3882 0.7912 0.1184  -0.0383 0.0136  121 THR A CB  
576   O OG1 . THR A 121 ? 0.7907 0.3749 0.7854 0.1058  -0.0434 0.0288  121 THR A OG1 
577   C CG2 . THR A 121 ? 0.7909 0.4088 0.8171 0.1237  -0.0429 -0.0041 121 THR A CG2 
578   N N   . PHE A 122 ? 0.8041 0.4377 0.7948 0.0981  -0.0059 0.0437  122 PHE A N   
579   C CA  . PHE A 122 ? 0.8058 0.4412 0.7888 0.0897  0.0014  0.0528  122 PHE A CA  
580   C C   . PHE A 122 ? 0.8001 0.4578 0.7909 0.0916  0.0129  0.0533  122 PHE A C   
581   O O   . PHE A 122 ? 0.8154 0.4824 0.8093 0.0897  0.0134  0.0525  122 PHE A O   
582   C CB  . PHE A 122 ? 0.8383 0.4598 0.8079 0.0747  -0.0042 0.0590  122 PHE A CB  
583   C CG  . PHE A 122 ? 0.8594 0.4929 0.8226 0.0625  0.0054  0.0633  122 PHE A CG  
584   C CD1 . PHE A 122 ? 0.8639 0.4915 0.8181 0.0575  0.0055  0.0668  122 PHE A CD1 
585   C CD2 . PHE A 122 ? 0.8856 0.5407 0.8537 0.0552  0.0139  0.0608  122 PHE A CD2 
586   C CE1 . PHE A 122 ? 0.8963 0.5410 0.8462 0.0443  0.0156  0.0665  122 PHE A CE1 
587   C CE2 . PHE A 122 ? 0.9186 0.5925 0.8860 0.0441  0.0233  0.0584  122 PHE A CE2 
588   C CZ  . PHE A 122 ? 0.9253 0.5946 0.8833 0.0378  0.0249  0.0607  122 PHE A CZ  
589   N N   . VAL A 123 ? 0.7762 0.4405 0.7704 0.0954  0.0200  0.0542  123 VAL A N   
590   C CA  . VAL A 123 ? 0.7732 0.4512 0.7756 0.0993  0.0262  0.0552  123 VAL A CA  
591   C C   . VAL A 123 ? 0.7756 0.4577 0.7818 0.0973  0.0324  0.0543  123 VAL A C   
592   O O   . VAL A 123 ? 0.7630 0.4391 0.7667 0.0982  0.0350  0.0540  123 VAL A O   
593   C CB  . VAL A 123 ? 0.7627 0.4421 0.7655 0.1052  0.0266  0.0557  123 VAL A CB  
594   C CG1 . VAL A 123 ? 0.7632 0.4458 0.7714 0.1089  0.0285  0.0596  123 VAL A CG1 
595   C CG2 . VAL A 123 ? 0.7795 0.4647 0.7806 0.1050  0.0223  0.0531  123 VAL A CG2 
596   N N   . ASP A 124 ? 0.7433 0.4399 0.7577 0.0943  0.0351  0.0507  124 ASP A N   
597   C CA  . ASP A 124 ? 0.7597 0.4685 0.7843 0.0934  0.0416  0.0437  124 ASP A CA  
598   C C   . ASP A 124 ? 0.7672 0.4904 0.8116 0.1036  0.0400  0.0381  124 ASP A C   
599   O O   . ASP A 124 ? 0.7960 0.5356 0.8475 0.1016  0.0384  0.0339  124 ASP A O   
600   C CB  . ASP A 124 ? 0.8082 0.5279 0.8255 0.0768  0.0459  0.0392  124 ASP A CB  
601   C CG  . ASP A 124 ? 0.8364 0.5731 0.8632 0.0733  0.0544  0.0282  124 ASP A CG  
602   O OD1 . ASP A 124 ? 0.8132 0.5524 0.8575 0.0869  0.0556  0.0224  124 ASP A OD1 
603   O OD2 . ASP A 124 ? 0.8873 0.6339 0.9029 0.0554  0.0590  0.0249  124 ASP A OD2 
604   N N   . LEU A 125 ? 0.7340 0.4495 0.7875 0.1144  0.0384  0.0378  125 LEU A N   
605   C CA  . LEU A 125 ? 0.7416 0.4633 0.8152 0.1269  0.0314  0.0330  125 LEU A CA  
606   C C   . LEU A 125 ? 0.7486 0.4764 0.8419 0.1329  0.0343  0.0193  125 LEU A C   
607   O O   . LEU A 125 ? 0.7442 0.4628 0.8530 0.1464  0.0249  0.0170  125 LEU A O   
608   C CB  . LEU A 125 ? 0.7244 0.4245 0.7891 0.1338  0.0213  0.0467  125 LEU A CB  
609   C CG  . LEU A 125 ? 0.7238 0.4223 0.7710 0.1274  0.0193  0.0563  125 LEU A CG  
610   C CD1 . LEU A 125 ? 0.7260 0.4073 0.7604 0.1286  0.0113  0.0683  125 LEU A CD1 
611   C CD2 . LEU A 125 ? 0.7495 0.4683 0.8055 0.1274  0.0161  0.0519  125 LEU A CD2 
612   N N   . SER A 126 ? 0.7450 0.4864 0.8366 0.1219  0.0454  0.0098  126 SER A N   
613   C CA  . SER A 126 ? 0.7555 0.5063 0.8648 0.1249  0.0505  -0.0064 126 SER A CA  
614   C C   . SER A 126 ? 0.7827 0.5652 0.9254 0.1330  0.0487  -0.0286 126 SER A C   
615   O O   . SER A 126 ? 0.8044 0.6075 0.9534 0.1316  0.0466  -0.0322 126 SER A O   
616   C CB  . SER A 126 ? 0.7803 0.5406 0.8745 0.1071  0.0627  -0.0098 126 SER A CB  
617   O OG  . SER A 126 ? 0.8321 0.6179 0.9202 0.0909  0.0681  -0.0149 126 SER A OG  
618   N N   . MET A 127 ? 0.7025 0.4905 0.8693 0.1421  0.0490  -0.0467 127 MET A N   
619   C CA  . MET A 127 ? 0.7179 0.5426 0.9242 0.1516  0.0476  -0.0763 127 MET A CA  
620   C C   . MET A 127 ? 0.7051 0.5271 0.9318 0.1711  0.0296  -0.0755 127 MET A C   
621   O O   . MET A 127 ? 0.7224 0.5833 0.9721 0.1729  0.0291  -0.0937 127 MET A O   
622   C CB  . MET A 127 ? 0.7654 0.6388 0.9717 0.1298  0.0638  -0.0940 127 MET A CB  
623   C CG  . MET A 127 ? 0.7914 0.6658 0.9722 0.1077  0.0784  -0.0915 127 MET A CG  
624   S SD  . MET A 127 ? 0.8579 0.7934 1.0397 0.0779  0.0962  -0.1174 127 MET A SD  
625   C CE  . MET A 127 ? 0.8216 0.8042 1.0638 0.0969  0.0957  -0.1625 127 MET A CE  
626   N N   . ASN A 128 ? 0.7628 0.5401 0.9798 0.1839  0.0139  -0.0547 128 ASN A N   
627   C CA  . ASN A 128 ? 0.7566 0.5222 0.9870 0.2019  -0.0077 -0.0488 128 ASN A CA  
628   C C   . ASN A 128 ? 0.7403 0.4660 0.9831 0.2200  -0.0265 -0.0468 128 ASN A C   
629   O O   . ASN A 128 ? 0.7342 0.4512 0.9839 0.2200  -0.0205 -0.0575 128 ASN A O   
630   C CB  . ASN A 128 ? 0.7579 0.5062 0.9540 0.1929  -0.0106 -0.0203 128 ASN A CB  
631   C CG  . ASN A 128 ? 0.7809 0.5659 0.9718 0.1789  0.0016  -0.0251 128 ASN A CG  
632   O OD1 . ASN A 128 ? 0.7978 0.6133 1.0114 0.1850  -0.0039 -0.0387 128 ASN A OD1 
633   N ND2 . ASN A 128 ? 0.7834 0.5650 0.9450 0.1596  0.0165  -0.0148 128 ASN A ND2 
634   N N   . ARG A 129 ? 0.8675 0.5676 1.1129 0.2344  -0.0510 -0.0338 129 ARG A N   
635   C CA  . ARG A 129 ? 0.8635 0.5159 1.1156 0.2496  -0.0743 -0.0277 129 ARG A CA  
636   C C   . ARG A 129 ? 0.8730 0.4769 1.0802 0.2393  -0.0860 0.0101  129 ARG A C   
637   O O   . ARG A 129 ? 0.8912 0.4664 1.0910 0.2459  -0.1098 0.0241  129 ARG A O   
638   C CB  . ARG A 129 ? 0.8631 0.5260 1.1594 0.2757  -0.0990 -0.0481 129 ARG A CB  
639   C CG  . ARG A 129 ? 0.8528 0.5687 1.2002 0.2863  -0.0881 -0.0925 129 ARG A CG  
640   C CD  . ARG A 129 ? 0.8647 0.5938 1.2493 0.3076  -0.1113 -0.1132 129 ARG A CD  
641   N NE  . ARG A 129 ? 0.9146 0.5877 1.2744 0.3110  -0.1364 -0.0859 129 ARG A NE  
642   C CZ  . ARG A 129 ? 0.9480 0.5928 1.3095 0.3137  -0.1437 -0.0896 129 ARG A CZ  
643   N NH1 . ARG A 129 ? 0.9359 0.6041 1.3230 0.3145  -0.1281 -0.1199 129 ARG A NH1 
644   N NH2 . ARG A 129 ? 0.9976 0.5900 1.3343 0.3140  -0.1675 -0.0631 129 ARG A NH2 
645   N N   . PHE A 130 ? 0.8230 0.4273 0.9930 0.2170  -0.0657 0.0260  130 PHE A N   
646   C CA  . PHE A 130 ? 0.8419 0.4097 0.9693 0.2024  -0.0717 0.0565  130 PHE A CA  
647   C C   . PHE A 130 ? 0.8751 0.3969 0.9911 0.1996  -0.0797 0.0644  130 PHE A C   
648   O O   . PHE A 130 ? 0.8655 0.3897 0.9921 0.1988  -0.0665 0.0498  130 PHE A O   
649   C CB  . PHE A 130 ? 0.8169 0.4045 0.9159 0.1819  -0.0481 0.0640  130 PHE A CB  
650   C CG  . PHE A 130 ? 0.8189 0.4396 0.9187 0.1801  -0.0438 0.0630  130 PHE A CG  
651   C CD1 . PHE A 130 ? 0.8382 0.4526 0.9262 0.1803  -0.0597 0.0778  130 PHE A CD1 
652   C CD2 . PHE A 130 ? 0.8074 0.4640 0.9170 0.1755  -0.0250 0.0479  130 PHE A CD2 
653   C CE1 . PHE A 130 ? 0.8448 0.4902 0.9344 0.1779  -0.0555 0.0751  130 PHE A CE1 
654   C CE2 . PHE A 130 ? 0.8159 0.4989 0.9247 0.1717  -0.0220 0.0470  130 PHE A CE2 
655   C CZ  . PHE A 130 ? 0.8338 0.5123 0.9343 0.1738  -0.0365 0.0594  130 PHE A CZ  
656   N N   . SER A 131 ? 0.9226 0.4110 1.0108 0.1924  -0.0975 0.0874  131 SER A N   
657   C CA  . SER A 131 ? 0.9593 0.4098 1.0269 0.1816  -0.1024 0.0979  131 SER A CA  
658   C C   . SER A 131 ? 0.9793 0.4043 0.9987 0.1561  -0.1049 0.1268  131 SER A C   
659   O O   . SER A 131 ? 0.9754 0.4092 0.9780 0.1498  -0.1079 0.1391  131 SER A O   
660   C CB  . SER A 131 ? 1.0052 0.4367 1.0897 0.1959  -0.1266 0.0949  131 SER A CB  
661   O OG  . SER A 131 ? 1.0294 0.4559 1.1055 0.1987  -0.1484 0.1106  131 SER A OG  
662   N N   . GLY A 132 ? 0.9936 0.3878 0.9898 0.1396  -0.1040 0.1361  132 GLY A N   
663   C CA  . GLY A 132 ? 1.0152 0.3885 0.9634 0.1105  -0.1043 0.1600  132 GLY A CA  
664   C C   . GLY A 132 ? 1.0029 0.3830 0.9374 0.0949  -0.0804 0.1538  132 GLY A C   
665   O O   . GLY A 132 ? 0.9840 0.3660 0.9408 0.1036  -0.0701 0.1366  132 GLY A O   
666   N N   . THR A 133 ? 0.9626 0.3633 0.8651 0.0707  -0.0674 0.1625  133 THR A N   
667   C CA  . THR A 133 ? 0.9393 0.3639 0.8323 0.0545  -0.0423 0.1525  133 THR A CA  
668   C C   . THR A 133 ? 0.9170 0.3939 0.8175 0.0562  -0.0233 0.1408  133 THR A C   
669   O O   . THR A 133 ? 0.9091 0.4021 0.8160 0.0648  -0.0284 0.1427  133 THR A O   
670   C CB  . THR A 133 ? 0.9918 0.3948 0.8403 0.0206  -0.0440 0.1685  133 THR A CB  
671   O OG1 . THR A 133 ? 1.0242 0.4297 0.8432 0.0043  -0.0540 0.1855  133 THR A OG1 
672   C CG2 . THR A 133 ? 1.0353 0.3797 0.8750 0.0171  -0.0629 0.1794  133 THR A CG2 
673   N N   . ILE A 134 ? 0.9081 0.4101 0.8091 0.0484  -0.0032 0.1277  134 ILE A N   
674   C CA  . ILE A 134 ? 0.8923 0.4382 0.7996 0.0492  0.0118  0.1157  134 ILE A CA  
675   C C   . ILE A 134 ? 0.9498 0.5109 0.8271 0.0236  0.0156  0.1203  134 ILE A C   
676   O O   . ILE A 134 ? 0.9864 0.5457 0.8449 0.0032  0.0219  0.1197  134 ILE A O   
677   C CB  . ILE A 134 ? 0.8579 0.4234 0.7833 0.0558  0.0275  0.0981  134 ILE A CB  
678   C CG1 . ILE A 134 ? 0.8084 0.3683 0.7621 0.0771  0.0256  0.0908  134 ILE A CG1 
679   C CG2 . ILE A 134 ? 0.8524 0.4558 0.7818 0.0555  0.0379  0.0866  134 ILE A CG2 
680   C CD1 . ILE A 134 ? 0.7865 0.3573 0.7518 0.0791  0.0381  0.0768  134 ILE A CD1 
681   N N   . SER A 135 ? 0.8609 0.4411 0.7340 0.0226  0.0127  0.1224  135 SER A N   
682   C CA  . SER A 135 ? 0.9252 0.5251 0.7699 -0.0037 0.0160  0.1243  135 SER A CA  
683   C C   . SER A 135 ? 0.9451 0.5874 0.7980 -0.0095 0.0344  0.1012  135 SER A C   
684   O O   . SER A 135 ? 0.9043 0.5625 0.7850 0.0105  0.0408  0.0864  135 SER A O   
685   C CB  . SER A 135 ? 0.9397 0.5509 0.7799 -0.0025 0.0074  0.1306  135 SER A CB  
686   O OG  . SER A 135 ? 1.0056 0.6371 0.8149 -0.0319 0.0098  0.1326  135 SER A OG  
687   N N   . PRO A 136 ? 0.8765 0.5388 0.7053 -0.0380 0.0416  0.0968  136 PRO A N   
688   C CA  . PRO A 136 ? 0.9123 0.6232 0.7543 -0.0416 0.0568  0.0695  136 PRO A CA  
689   C C   . PRO A 136 ? 0.9236 0.6653 0.7842 -0.0286 0.0575  0.0556  136 PRO A C   
690   O O   . PRO A 136 ? 0.9427 0.7169 0.8262 -0.0195 0.0652  0.0312  136 PRO A O   
691   C CB  . PRO A 136 ? 0.9716 0.7009 0.7804 -0.0801 0.0633  0.0678  136 PRO A CB  
692   C CG  . PRO A 136 ? 0.9586 0.6364 0.7363 -0.0951 0.0513  0.0967  136 PRO A CG  
693   C CD  . PRO A 136 ? 0.9172 0.5596 0.7050 -0.0702 0.0349  0.1149  136 PRO A CD  
694   N N   . GLU A 137 ? 0.9262 0.6572 0.7782 -0.0272 0.0477  0.0697  137 GLU A N   
695   C CA  . GLU A 137 ? 0.9392 0.6966 0.8078 -0.0161 0.0478  0.0568  137 GLU A CA  
696   C C   . GLU A 137 ? 0.8687 0.6211 0.7711 0.0141  0.0474  0.0474  137 GLU A C   
697   O O   . GLU A 137 ? 0.8740 0.6492 0.7939 0.0232  0.0486  0.0306  137 GLU A O   
698   C CB  . GLU A 137 ? 0.9406 0.6846 0.7924 -0.0206 0.0359  0.0760  137 GLU A CB  
699   C CG  . GLU A 137 ? 0.9839 0.7229 0.7948 -0.0532 0.0312  0.0922  137 GLU A CG  
700   C CD  . GLU A 137 ? 1.0415 0.8251 0.8378 -0.0761 0.0369  0.0791  137 GLU A CD  
701   O OE1 . GLU A 137 ? 1.0687 0.8957 0.8787 -0.0812 0.0512  0.0500  137 GLU A OE1 
702   O OE2 . GLU A 137 ? 1.0537 0.8312 0.8262 -0.0887 0.0260  0.0959  137 GLU A OE2 
703   N N   . TRP A 138 ? 0.9824 0.7049 0.8931 0.0278  0.0449  0.0573  138 TRP A N   
704   C CA  . TRP A 138 ? 0.9066 0.6252 0.8432 0.0505  0.0446  0.0498  138 TRP A CA  
705   C C   . TRP A 138 ? 0.9156 0.6598 0.8676 0.0544  0.0501  0.0268  138 TRP A C   
706   O O   . TRP A 138 ? 0.8638 0.6074 0.8339 0.0700  0.0463  0.0194  138 TRP A O   
707   C CB  . TRP A 138 ? 0.8476 0.5375 0.7884 0.0592  0.0433  0.0603  138 TRP A CB  
708   C CG  . TRP A 138 ? 0.8180 0.4842 0.7584 0.0663  0.0342  0.0763  138 TRP A CG  
709   C CD1 . TRP A 138 ? 0.8308 0.4717 0.7591 0.0611  0.0273  0.0909  138 TRP A CD1 
710   C CD2 . TRP A 138 ? 0.7786 0.4450 0.7335 0.0801  0.0293  0.0773  138 TRP A CD2 
711   N NE1 . TRP A 138 ? 0.8040 0.4319 0.7425 0.0740  0.0171  0.0987  138 TRP A NE1 
712   C CE2 . TRP A 138 ? 0.7740 0.4206 0.7285 0.0845  0.0199  0.0899  138 TRP A CE2 
713   C CE3 . TRP A 138 ? 0.7539 0.4341 0.7217 0.0881  0.0305  0.0680  138 TRP A CE3 
714   C CZ2 . TRP A 138 ? 0.7510 0.3993 0.7203 0.0967  0.0138  0.0907  138 TRP A CZ2 
715   C CZ3 . TRP A 138 ? 0.7307 0.4086 0.7082 0.0967  0.0254  0.0716  138 TRP A CZ3 
716   C CH2 . TRP A 138 ? 0.7316 0.3976 0.7110 0.1009  0.0182  0.0815  138 TRP A CH2 
717   N N   . GLY A 139 ? 0.8296 0.5967 0.7751 0.0395  0.0573  0.0145  139 GLY A N   
718   C CA  . GLY A 139 ? 0.8368 0.6344 0.8016 0.0445  0.0603  -0.0120 139 GLY A CA  
719   C C   . GLY A 139 ? 0.8598 0.6891 0.8362 0.0450  0.0590  -0.0327 139 GLY A C   
720   O O   . GLY A 139 ? 0.8496 0.7081 0.8464 0.0504  0.0594  -0.0596 139 GLY A O   
721   N N   . ARG A 140 ? 0.8134 0.6398 0.7797 0.0404  0.0564  -0.0234 140 ARG A N   
722   C CA  . ARG A 140 ? 0.8323 0.6901 0.8095 0.0395  0.0558  -0.0446 140 ARG A CA  
723   C C   . ARG A 140 ? 0.7606 0.6040 0.7610 0.0627  0.0457  -0.0504 140 ARG A C   
724   O O   . ARG A 140 ? 0.7601 0.6276 0.7776 0.0668  0.0431  -0.0745 140 ARG A O   
725   C CB  . ARG A 140 ? 0.9081 0.7727 0.8600 0.0196  0.0573  -0.0322 140 ARG A CB  
726   C CG  . ARG A 140 ? 0.9855 0.8803 0.9133 -0.0114 0.0667  -0.0376 140 ARG A CG  
727   C CD  . ARG A 140 ? 1.0456 0.9405 0.9426 -0.0328 0.0643  -0.0199 140 ARG A CD  
728   N NE  . ARG A 140 ? 1.0316 0.9603 0.9392 -0.0337 0.0648  -0.0401 140 ARG A NE  
729   C CZ  . ARG A 140 ? 1.0616 0.9938 0.9483 -0.0475 0.0608  -0.0281 140 ARG A CZ  
730   N NH1 . ARG A 140 ? 1.0813 0.9822 0.9357 -0.0598 0.0530  0.0055  140 ARG A NH1 
731   N NH2 . ARG A 140 ? 1.0437 1.0107 0.9433 -0.0483 0.0627  -0.0514 140 ARG A NH2 
732   N N   . PHE A 141 ? 0.8639 0.6696 0.8647 0.0760  0.0396  -0.0306 141 PHE A N   
733   C CA  . PHE A 141 ? 0.8094 0.5967 0.8245 0.0919  0.0295  -0.0314 141 PHE A CA  
734   C C   . PHE A 141 ? 0.7797 0.5681 0.8168 0.1061  0.0214  -0.0513 141 PHE A C   
735   O O   . PHE A 141 ? 0.7416 0.5088 0.7803 0.1139  0.0170  -0.0434 141 PHE A O   
736   C CB  . PHE A 141 ? 0.7595 0.5132 0.7654 0.0961  0.0271  -0.0059 141 PHE A CB  
737   C CG  . PHE A 141 ? 0.7819 0.5338 0.7721 0.0869  0.0298  0.0110  141 PHE A CG  
738   C CD1 . PHE A 141 ? 0.8108 0.5732 0.7999 0.0837  0.0272  0.0087  141 PHE A CD1 
739   C CD2 . PHE A 141 ? 0.7772 0.5159 0.7546 0.0820  0.0327  0.0281  141 PHE A CD2 
740   C CE1 . PHE A 141 ? 0.8369 0.5978 0.8118 0.0761  0.0264  0.0246  141 PHE A CE1 
741   C CE2 . PHE A 141 ? 0.7967 0.5298 0.7615 0.0760  0.0301  0.0435  141 PHE A CE2 
742   C CZ  . PHE A 141 ? 0.8276 0.5726 0.7907 0.0732  0.0264  0.0424  141 PHE A CZ  
743   N N   . SER A 142 ? 0.7761 0.5904 0.8317 0.1096  0.0177  -0.0791 142 SER A N   
744   C CA  . SER A 142 ? 0.7429 0.5658 0.8242 0.1241  0.0076  -0.1041 142 SER A CA  
745   C C   . SER A 142 ? 0.6926 0.4728 0.7810 0.1410  -0.0106 -0.0952 142 SER A C   
746   O O   . SER A 142 ? 0.6766 0.4509 0.7790 0.1532  -0.0220 -0.1049 142 SER A O   
747   C CB  . SER A 142 ? 0.7507 0.6138 0.8547 0.1253  0.0065  -0.1404 142 SER A CB  
748   O OG  . SER A 142 ? 0.7500 0.6028 0.8547 0.1265  0.0016  -0.1399 142 SER A OG  
749   N N   . LYS A 143 ? 0.8076 0.5585 0.8850 0.1401  -0.0150 -0.0771 143 LYS A N   
750   C CA  . LYS A 143 ? 0.7750 0.4842 0.8531 0.1498  -0.0330 -0.0677 143 LYS A CA  
751   C C   . LYS A 143 ? 0.7608 0.4431 0.8165 0.1430  -0.0294 -0.0378 143 LYS A C   
752   O O   . LYS A 143 ? 0.7463 0.3946 0.7952 0.1446  -0.0428 -0.0263 143 LYS A O   
753   C CB  . LYS A 143 ? 0.7773 0.4730 0.8589 0.1505  -0.0414 -0.0715 143 LYS A CB  
754   C CG  . LYS A 143 ? 0.7835 0.5037 0.8927 0.1599  -0.0486 -0.1066 143 LYS A CG  
755   C CD  . LYS A 143 ? 0.7783 0.4698 0.8959 0.1660  -0.0661 -0.1132 143 LYS A CD  
756   C CE  . LYS A 143 ? 0.8009 0.4957 0.9027 0.1518  -0.0548 -0.1012 143 LYS A CE  
757   N NZ  . LYS A 143 ? 0.8311 0.5764 0.9363 0.1430  -0.0372 -0.1164 143 LYS A NZ  
758   N N   . LEU A 144 ? 0.8036 0.5003 0.8474 0.1340  -0.0129 -0.0266 144 LEU A N   
759   C CA  . LEU A 144 ? 0.7857 0.4635 0.8128 0.1276  -0.0078 -0.0034 144 LEU A CA  
760   C C   . LEU A 144 ? 0.7719 0.4314 0.7974 0.1318  -0.0172 0.0003  144 LEU A C   
761   O O   . LEU A 144 ? 0.7764 0.4477 0.8117 0.1379  -0.0198 -0.0120 144 LEU A O   
762   C CB  . LEU A 144 ? 0.7921 0.4868 0.8109 0.1196  0.0084  0.0037  144 LEU A CB  
763   C CG  . LEU A 144 ? 0.7684 0.4497 0.7755 0.1143  0.0148  0.0227  144 LEU A CG  
764   C CD1 . LEU A 144 ? 0.7668 0.4439 0.7706 0.1112  0.0145  0.0308  144 LEU A CD1 
765   C CD2 . LEU A 144 ? 0.7745 0.4654 0.7763 0.1091  0.0257  0.0267  144 LEU A CD2 
766   N N   . GLU A 145 ? 0.7967 0.4310 0.8087 0.1261  -0.0224 0.0165  145 GLU A N   
767   C CA  . GLU A 145 ? 0.7968 0.4126 0.8006 0.1252  -0.0321 0.0237  145 GLU A CA  
768   C C   . GLU A 145 ? 0.7968 0.4139 0.7861 0.1137  -0.0195 0.0379  145 GLU A C   
769   O O   . GLU A 145 ? 0.8040 0.4170 0.7876 0.1119  -0.0225 0.0409  145 GLU A O   
770   C CB  . GLU A 145 ? 0.8051 0.3870 0.8009 0.1239  -0.0535 0.0294  145 GLU A CB  
771   C CG  . GLU A 145 ? 0.8032 0.3785 0.8176 0.1382  -0.0711 0.0118  145 GLU A CG  
772   C CD  . GLU A 145 ? 0.8146 0.3488 0.8190 0.1348  -0.0936 0.0194  145 GLU A CD  
773   O OE1 . GLU A 145 ? 0.8303 0.3358 0.8127 0.1241  -0.1048 0.0370  145 GLU A OE1 
774   O OE2 . GLU A 145 ? 0.8156 0.3452 0.8320 0.1405  -0.1007 0.0077  145 GLU A OE2 
775   N N   . TYR A 146 ? 0.7571 0.3819 0.7426 0.1066  -0.0068 0.0444  146 TYR A N   
776   C CA  . TYR A 146 ? 0.7587 0.3888 0.7366 0.0971  0.0045  0.0524  146 TYR A CA  
777   C C   . TYR A 146 ? 0.7416 0.3891 0.7281 0.1000  0.0181  0.0505  146 TYR A C   
778   O O   . TYR A 146 ? 0.7403 0.3926 0.7306 0.1012  0.0190  0.0506  146 TYR A O   
779   C CB  . TYR A 146 ? 0.7840 0.4044 0.7492 0.0838  0.0014  0.0607  146 TYR A CB  
780   C CG  . TYR A 146 ? 0.8060 0.4368 0.7640 0.0713  0.0115  0.0639  146 TYR A CG  
781   C CD1 . TYR A 146 ? 0.8062 0.4575 0.7746 0.0708  0.0248  0.0600  146 TYR A CD1 
782   C CD2 . TYR A 146 ? 0.8352 0.4576 0.7775 0.0600  0.0064  0.0689  146 TYR A CD2 
783   C CE1 . TYR A 146 ? 0.8377 0.5045 0.8053 0.0605  0.0342  0.0567  146 TYR A CE1 
784   C CE2 . TYR A 146 ? 0.8688 0.5075 0.8053 0.0461  0.0173  0.0679  146 TYR A CE2 
785   C CZ  . TYR A 146 ? 0.8713 0.5340 0.8228 0.0470  0.0321  0.0597  146 TYR A CZ  
786   O OH  . TYR A 146 ? 0.9152 0.5998 0.8668 0.0346  0.0432  0.0526  146 TYR A OH  
787   N N   . PHE A 147 ? 0.7517 0.4061 0.7404 0.1004  0.0267  0.0494  147 PHE A N   
788   C CA  . PHE A 147 ? 0.7418 0.4043 0.7363 0.1028  0.0352  0.0494  147 PHE A CA  
789   C C   . PHE A 147 ? 0.7444 0.4090 0.7417 0.0999  0.0425  0.0498  147 PHE A C   
790   O O   . PHE A 147 ? 0.7490 0.4134 0.7443 0.0975  0.0457  0.0471  147 PHE A O   
791   C CB  . PHE A 147 ? 0.7452 0.4123 0.7400 0.1049  0.0371  0.0447  147 PHE A CB  
792   C CG  . PHE A 147 ? 0.7520 0.4209 0.7457 0.1034  0.0414  0.0482  147 PHE A CG  
793   C CD1 . PHE A 147 ? 0.7520 0.4201 0.7470 0.1048  0.0390  0.0539  147 PHE A CD1 
794   C CD2 . PHE A 147 ? 0.7697 0.4397 0.7588 0.0987  0.0460  0.0467  147 PHE A CD2 
795   C CE1 . PHE A 147 ? 0.7683 0.4332 0.7591 0.1028  0.0384  0.0600  147 PHE A CE1 
796   C CE2 . PHE A 147 ? 0.7903 0.4550 0.7723 0.0937  0.0465  0.0534  147 PHE A CE2 
797   C CZ  . PHE A 147 ? 0.7889 0.4492 0.7713 0.0964  0.0413  0.0611  147 PHE A CZ  
798   N N   . ASP A 148 ? 0.7377 0.4076 0.7422 0.1007  0.0445  0.0501  148 ASP A N   
799   C CA  . ASP A 148 ? 0.7511 0.4285 0.7650 0.0996  0.0507  0.0444  148 ASP A CA  
800   C C   . ASP A 148 ? 0.7470 0.4245 0.7743 0.1084  0.0491  0.0435  148 ASP A C   
801   O O   . ASP A 148 ? 0.7530 0.4364 0.7853 0.1113  0.0448  0.0449  148 ASP A O   
802   C CB  . ASP A 148 ? 0.7866 0.4768 0.7989 0.0896  0.0527  0.0406  148 ASP A CB  
803   C CG  . ASP A 148 ? 0.8176 0.5230 0.8389 0.0849  0.0611  0.0293  148 ASP A CG  
804   O OD1 . ASP A 148 ? 0.8031 0.5068 0.8378 0.0937  0.0636  0.0235  148 ASP A OD1 
805   O OD2 . ASP A 148 ? 0.8652 0.5841 0.8793 0.0705  0.0645  0.0254  148 ASP A OD2 
806   N N   . LEU A 149 ? 0.7478 0.4166 0.7807 0.1124  0.0504  0.0413  149 LEU A N   
807   C CA  . LEU A 149 ? 0.7520 0.4131 0.7982 0.1218  0.0443  0.0407  149 LEU A CA  
808   C C   . LEU A 149 ? 0.7636 0.4269 0.8271 0.1255  0.0476  0.0272  149 LEU A C   
809   O O   . LEU A 149 ? 0.7662 0.4113 0.8377 0.1327  0.0410  0.0270  149 LEU A O   
810   C CB  . LEU A 149 ? 0.7499 0.3893 0.7825 0.1213  0.0379  0.0528  149 LEU A CB  
811   C CG  . LEU A 149 ? 0.7512 0.3927 0.7691 0.1172  0.0343  0.0624  149 LEU A CG  
812   C CD1 . LEU A 149 ? 0.7720 0.3972 0.7730 0.1105  0.0301  0.0723  149 LEU A CD1 
813   C CD2 . LEU A 149 ? 0.7575 0.4087 0.7842 0.1231  0.0275  0.0634  149 LEU A CD2 
814   N N   . SER A 150 ? 0.7682 0.4531 0.8369 0.1190  0.0567  0.0153  150 SER A N   
815   C CA  . SER A 150 ? 0.7864 0.4807 0.8720 0.1198  0.0625  -0.0018 150 SER A CA  
816   C C   . SER A 150 ? 0.7996 0.5068 0.9160 0.1322  0.0572  -0.0179 150 SER A C   
817   O O   . SER A 150 ? 0.8014 0.5161 0.9247 0.1380  0.0504  -0.0158 150 SER A O   
818   C CB  . SER A 150 ? 0.8169 0.5345 0.8939 0.1044  0.0736  -0.0094 150 SER A CB  
819   O OG  . SER A 150 ? 0.8054 0.5104 0.8572 0.0961  0.0740  0.0047  150 SER A OG  
820   N N   . ILE A 151 ? 0.7361 0.4482 0.8739 0.1371  0.0595  -0.0369 151 ILE A N   
821   C CA  . ILE A 151 ? 0.7451 0.4737 0.9205 0.1517  0.0534  -0.0602 151 ILE A CA  
822   C C   . ILE A 151 ? 0.7310 0.4369 0.9144 0.1686  0.0342  -0.0490 151 ILE A C   
823   O O   . ILE A 151 ? 0.7378 0.4645 0.9309 0.1725  0.0301  -0.0516 151 ILE A O   
824   C CB  . ILE A 151 ? 0.7767 0.5567 0.9657 0.1419  0.0649  -0.0815 151 ILE A CB  
825   C CG1 . ILE A 151 ? 0.8040 0.6041 0.9797 0.1218  0.0816  -0.0903 151 ILE A CG1 
826   C CG2 . ILE A 151 ? 0.7758 0.5820 1.0103 0.1581  0.0591  -0.1124 151 ILE A CG2 
827   C CD1 . ILE A 151 ? 0.8442 0.6653 0.9928 0.0992  0.0906  -0.0813 151 ILE A CD1 
828   N N   . ASN A 152 ? 0.7928 0.4552 0.9685 0.1757  0.0216  -0.0353 152 ASN A N   
829   C CA  . ASN A 152 ? 0.7911 0.4240 0.9661 0.1878  0.0003  -0.0197 152 ASN A CA  
830   C C   . ASN A 152 ? 0.7961 0.3850 0.9766 0.1966  -0.0149 -0.0183 152 ASN A C   
831   O O   . ASN A 152 ? 0.7985 0.3874 0.9936 0.1973  -0.0086 -0.0359 152 ASN A O   
832   C CB  . ASN A 152 ? 0.7862 0.4074 0.9237 0.1753  0.0013  0.0082  152 ASN A CB  
833   C CG  . ASN A 152 ? 0.7871 0.4391 0.9267 0.1747  0.0035  0.0081  152 ASN A CG  
834   O OD1 . ASN A 152 ? 0.7961 0.4621 0.9606 0.1877  -0.0071 -0.0021 152 ASN A OD1 
835   N ND2 . ASN A 152 ? 0.7782 0.4411 0.8937 0.1598  0.0161  0.0176  152 ASN A ND2 
836   N N   . GLN A 153 ? 0.8833 0.4330 1.0499 0.2010  -0.0361 0.0031  153 GLN A N   
837   C CA  . GLN A 153 ? 0.9113 0.4190 1.0680 0.2026  -0.0518 0.0103  153 GLN A CA  
838   C C   . GLN A 153 ? 0.9308 0.4011 1.0410 0.1831  -0.0547 0.0419  153 GLN A C   
839   O O   . GLN A 153 ? 0.9730 0.4110 1.0658 0.1800  -0.0725 0.0591  153 GLN A O   
840   C CB  . GLN A 153 ? 0.9428 0.4479 1.1207 0.2208  -0.0749 0.0050  153 GLN A CB  
841   C CG  . GLN A 153 ? 0.9156 0.4684 1.1344 0.2371  -0.0736 -0.0198 153 GLN A CG  
842   C CD  . GLN A 153 ? 0.9476 0.5004 1.1890 0.2554  -0.0988 -0.0249 153 GLN A CD  
843   O OE1 . GLN A 153 ? 0.9847 0.5022 1.2026 0.2534  -0.1185 0.0000  153 GLN A OE1 
844   N NE2 . GLN A 153 ? 0.9364 0.5315 1.2252 0.2721  -0.0990 -0.0591 153 GLN A NE2 
845   N N   . LEU A 154 ? 0.9092 0.3888 1.0008 0.1672  -0.0366 0.0485  154 LEU A N   
846   C CA  . LEU A 154 ? 0.9312 0.3889 0.9802 0.1456  -0.0355 0.0728  154 LEU A CA  
847   C C   . LEU A 154 ? 0.9547 0.3763 0.9908 0.1345  -0.0367 0.0752  154 LEU A C   
848   O O   . LEU A 154 ? 0.9474 0.3716 1.0056 0.1411  -0.0301 0.0559  154 LEU A O   
849   C CB  . LEU A 154 ? 0.9110 0.4072 0.9446 0.1325  -0.0128 0.0730  154 LEU A CB  
850   C CG  . LEU A 154 ? 0.8998 0.4211 0.9272 0.1324  -0.0120 0.0800  154 LEU A CG  
851   C CD1 . LEU A 154 ? 0.8934 0.4277 0.9500 0.1516  -0.0225 0.0710  154 LEU A CD1 
852   C CD2 . LEU A 154 ? 0.8706 0.4265 0.8932 0.1246  0.0085  0.0729  154 LEU A CD2 
853   N N   . VAL A 155 ? 0.9496 0.3396 0.9478 0.1146  -0.0447 0.0981  155 VAL A N   
854   C CA  . VAL A 155 ? 0.9814 0.3343 0.9592 0.0975  -0.0465 0.1039  155 VAL A CA  
855   C C   . VAL A 155 ? 1.0072 0.3668 0.9419 0.0671  -0.0357 0.1200  155 VAL A C   
856   O O   . VAL A 155 ? 1.0043 0.3905 0.9260 0.0614  -0.0311 0.1274  155 VAL A O   
857   C CB  . VAL A 155 ? 1.0298 0.3490 1.0090 0.0998  -0.0681 0.1123  155 VAL A CB  
858   C CG1 . VAL A 155 ? 1.0283 0.3554 1.0498 0.1261  -0.0709 0.0871  155 VAL A CG1 
859   C CG2 . VAL A 155 ? 1.0527 0.3660 1.0158 0.0986  -0.0865 0.1329  155 VAL A CG2 
860   N N   . GLY A 156 ? 1.0079 0.3453 0.9217 0.0465  -0.0316 0.1228  156 GLY A N   
861   C CA  . GLY A 156 ? 1.0395 0.3891 0.9146 0.0148  -0.0201 0.1330  156 GLY A CA  
862   C C   . GLY A 156 ? 1.0220 0.4226 0.9058 0.0111  0.0071  0.1140  156 GLY A C   
863   O O   . GLY A 156 ? 0.9842 0.4061 0.8986 0.0297  0.0171  0.0958  156 GLY A O   
864   N N   . GLU A 157 ? 0.9635 0.3858 0.8192 -0.0149 0.0179  0.1173  157 GLU A N   
865   C CA  . GLU A 157 ? 0.9578 0.4283 0.8209 -0.0194 0.0400  0.0988  157 GLU A CA  
866   C C   . GLU A 157 ? 0.9286 0.4429 0.8073 -0.0046 0.0468  0.0911  157 GLU A C   
867   O O   . GLU A 157 ? 0.9237 0.4365 0.7996 0.0010  0.0376  0.1010  157 GLU A O   
868   C CB  . GLU A 157 ? 1.0132 0.4929 0.8436 -0.0544 0.0484  0.1000  157 GLU A CB  
869   C CG  . GLU A 157 ? 1.0476 0.4756 0.8512 -0.0771 0.0381  0.1136  157 GLU A CG  
870   C CD  . GLU A 157 ? 1.0820 0.5277 0.8686 -0.1060 0.0537  0.1029  157 GLU A CD  
871   O OE1 . GLU A 157 ? 1.0783 0.5783 0.8807 -0.1028 0.0714  0.0825  157 GLU A OE1 
872   O OE2 . GLU A 157 ? 1.1140 0.5188 0.8714 -0.1323 0.0465  0.1146  157 GLU A OE2 
873   N N   . ILE A 158 ? 0.8662 0.4176 0.7612 0.0014  0.0610  0.0733  158 ILE A N   
874   C CA  . ILE A 158 ? 0.8284 0.4182 0.7364 0.0128  0.0660  0.0645  158 ILE A CA  
875   C C   . ILE A 158 ? 0.8337 0.4523 0.7236 -0.0082 0.0721  0.0599  158 ILE A C   
876   O O   . ILE A 158 ? 0.8412 0.4741 0.7227 -0.0254 0.0810  0.0504  158 ILE A O   
877   C CB  . ILE A 158 ? 0.7943 0.4062 0.7255 0.0277  0.0738  0.0489  158 ILE A CB  
878   C CG1 . ILE A 158 ? 0.7899 0.3822 0.7388 0.0449  0.0696  0.0499  158 ILE A CG1 
879   C CG2 . ILE A 158 ? 0.7648 0.4102 0.7062 0.0369  0.0754  0.0402  158 ILE A CG2 
880   C CD1 . ILE A 158 ? 0.7695 0.3781 0.7329 0.0510  0.0774  0.0363  158 ILE A CD1 
881   N N   . PRO A 159 ? 0.8286 0.4612 0.7134 -0.0090 0.0686  0.0632  159 PRO A N   
882   C CA  . PRO A 159 ? 0.8972 0.5630 0.7654 -0.0320 0.0754  0.0547  159 PRO A CA  
883   C C   . PRO A 159 ? 0.9189 0.6298 0.8077 -0.0266 0.0859  0.0288  159 PRO A C   
884   O O   . PRO A 159 ? 0.8720 0.5885 0.7861 -0.0022 0.0843  0.0211  159 PRO A O   
885   C CB  . PRO A 159 ? 0.9015 0.5730 0.7658 -0.0288 0.0684  0.0617  159 PRO A CB  
886   C CG  . PRO A 159 ? 0.8284 0.4839 0.7167 0.0011  0.0612  0.0662  159 PRO A CG  
887   C CD  . PRO A 159 ? 0.7858 0.4101 0.6814 0.0098  0.0593  0.0715  159 PRO A CD  
888   N N   . PRO A 160 ? 0.8677 0.6124 0.7460 -0.0500 0.0953  0.0138  160 PRO A N   
889   C CA  . PRO A 160 ? 0.9003 0.6934 0.8037 -0.0418 0.1019  -0.0152 160 PRO A CA  
890   C C   . PRO A 160 ? 0.9018 0.7206 0.8250 -0.0247 0.0974  -0.0275 160 PRO A C   
891   O O   . PRO A 160 ? 0.8556 0.6999 0.8064 -0.0067 0.0957  -0.0481 160 PRO A O   
892   C CB  . PRO A 160 ? 0.9476 0.7753 0.8336 -0.0755 0.1134  -0.0300 160 PRO A CB  
893   C CG  . PRO A 160 ? 0.9360 0.7222 0.7833 -0.1026 0.1119  -0.0040 160 PRO A CG  
894   C CD  . PRO A 160 ? 0.9046 0.6480 0.7475 -0.0867 0.0988  0.0211  160 PRO A CD  
895   N N   . GLU A 161 ? 0.9245 0.7355 0.8343 -0.0302 0.0935  -0.0158 161 GLU A N   
896   C CA  . GLU A 161 ? 0.9153 0.7490 0.8429 -0.0159 0.0894  -0.0283 161 GLU A CA  
897   C C   . GLU A 161 ? 0.8176 0.6328 0.7710 0.0166  0.0801  -0.0267 161 GLU A C   
898   O O   . GLU A 161 ? 0.7853 0.6207 0.7597 0.0310  0.0753  -0.0433 161 GLU A O   
899   C CB  . GLU A 161 ? 0.9479 0.7710 0.8528 -0.0289 0.0860  -0.0117 161 GLU A CB  
900   C CG  . GLU A 161 ? 0.9908 0.8484 0.8714 -0.0637 0.0944  -0.0209 161 GLU A CG  
901   C CD  . GLU A 161 ? 0.9825 0.8144 0.8260 -0.0936 0.0964  -0.0006 161 GLU A CD  
902   O OE1 . GLU A 161 ? 0.9553 0.7474 0.7984 -0.0847 0.0928  0.0145  161 GLU A OE1 
903   O OE2 . GLU A 161 ? 0.9952 0.8461 0.8083 -0.1282 0.1010  -0.0001 161 GLU A OE2 
904   N N   . LEU A 162 ? 0.9118 0.6897 0.8635 0.0265  0.0768  -0.0086 162 LEU A N   
905   C CA  . LEU A 162 ? 0.8256 0.5892 0.7966 0.0509  0.0690  -0.0072 162 LEU A CA  
906   C C   . LEU A 162 ? 0.8134 0.6018 0.8057 0.0619  0.0661  -0.0293 162 LEU A C   
907   O O   . LEU A 162 ? 0.7630 0.5442 0.7698 0.0797  0.0560  -0.0314 162 LEU A O   
908   C CB  . LEU A 162 ? 0.7756 0.5054 0.7417 0.0550  0.0687  0.0099  162 LEU A CB  
909   C CG  . LEU A 162 ? 0.7534 0.4537 0.7081 0.0538  0.0655  0.0303  162 LEU A CG  
910   C CD1 . LEU A 162 ? 0.6914 0.3685 0.6542 0.0656  0.0635  0.0379  162 LEU A CD1 
911   C CD2 . LEU A 162 ? 0.7496 0.4548 0.7055 0.0585  0.0598  0.0331  162 LEU A CD2 
912   N N   . GLY A 163 ? 0.8081 0.6249 0.8022 0.0508  0.0730  -0.0462 163 GLY A N   
913   C CA  . GLY A 163 ? 0.7904 0.6346 0.8083 0.0627  0.0676  -0.0701 163 GLY A CA  
914   C C   . GLY A 163 ? 0.7758 0.6461 0.8157 0.0748  0.0590  -0.0923 163 GLY A C   
915   O O   . GLY A 163 ? 0.7429 0.6265 0.8069 0.0917  0.0476  -0.1107 163 GLY A O   
916   N N   . LYS A 164 ? 0.7486 0.6256 0.7819 0.0673  0.0621  -0.0920 164 LYS A N   
917   C CA  . LYS A 164 ? 0.7280 0.6321 0.7843 0.0778  0.0547  -0.1169 164 LYS A CA  
918   C C   . LYS A 164 ? 0.6884 0.5587 0.7495 0.0958  0.0414  -0.1040 164 LYS A C   
919   O O   . LYS A 164 ? 0.6748 0.5607 0.7515 0.1026  0.0354  -0.1214 164 LYS A O   
920   C CB  . LYS A 164 ? 0.7735 0.7169 0.8205 0.0545  0.0673  -0.1310 164 LYS A CB  
921   C CG  . LYS A 164 ? 0.8180 0.7389 0.8367 0.0404  0.0716  -0.1053 164 LYS A CG  
922   C CD  . LYS A 164 ? 0.8782 0.8320 0.8734 0.0069  0.0856  -0.1109 164 LYS A CD  
923   C CE  . LYS A 164 ? 0.9182 0.8657 0.8928 -0.0054 0.0858  -0.0967 164 LYS A CE  
924   N NZ  . LYS A 164 ? 0.9530 0.9410 0.9043 -0.0413 0.0977  -0.1072 164 LYS A NZ  
925   N N   . LEU A 165 ? 0.8337 0.6611 0.8823 0.1017  0.0373  -0.0764 165 LEU A N   
926   C CA  . LEU A 165 ? 0.7884 0.5841 0.8402 0.1160  0.0242  -0.0647 165 LEU A CA  
927   C C   . LEU A 165 ? 0.7520 0.5397 0.8228 0.1342  0.0064  -0.0758 165 LEU A C   
928   O O   . LEU A 165 ? 0.7300 0.4901 0.7936 0.1386  -0.0005 -0.0600 165 LEU A O   
929   C CB  . LEU A 165 ? 0.7617 0.5230 0.7930 0.1115  0.0282  -0.0348 165 LEU A CB  
930   C CG  . LEU A 165 ? 0.7794 0.5379 0.7932 0.0981  0.0385  -0.0204 165 LEU A CG  
931   C CD1 . LEU A 165 ? 0.7423 0.4724 0.7440 0.0968  0.0412  0.0021  165 LEU A CD1 
932   C CD2 . LEU A 165 ? 0.7813 0.5415 0.7978 0.1006  0.0339  -0.0220 165 LEU A CD2 
933   N N   . SER A 166 ? 0.8301 0.6440 0.9263 0.1444  -0.0027 -0.1051 166 SER A N   
934   C CA  . SER A 166 ? 0.8034 0.6140 0.9218 0.1633  -0.0234 -0.1204 166 SER A CA  
935   C C   . SER A 166 ? 0.7754 0.5366 0.8887 0.1749  -0.0446 -0.1021 166 SER A C   
936   O O   . SER A 166 ? 0.7642 0.5104 0.8875 0.1883  -0.0654 -0.1059 166 SER A O   
937   C CB  . SER A 166 ? 0.7972 0.6490 0.9497 0.1738  -0.0304 -0.1608 166 SER A CB  
938   O OG  . SER A 166 ? 0.7908 0.6384 0.9486 0.1762  -0.0336 -0.1665 166 SER A OG  
939   N N   . ASN A 167 ? 0.8160 0.5518 0.9124 0.1683  -0.0413 -0.0825 167 ASN A N   
940   C CA  . ASN A 167 ? 0.7980 0.4880 0.8846 0.1731  -0.0597 -0.0646 167 ASN A CA  
941   C C   . ASN A 167 ? 0.7966 0.4621 0.8546 0.1601  -0.0519 -0.0341 167 ASN A C   
942   O O   . ASN A 167 ? 0.7914 0.4219 0.8356 0.1577  -0.0648 -0.0175 167 ASN A O   
943   C CB  . ASN A 167 ? 0.7941 0.4748 0.8831 0.1734  -0.0627 -0.0669 167 ASN A CB  
944   C CG  . ASN A 167 ? 0.7872 0.4701 0.9055 0.1910  -0.0839 -0.0951 167 ASN A CG  
945   O OD1 . ASN A 167 ? 0.7792 0.4363 0.9064 0.2044  -0.1093 -0.0981 167 ASN A OD1 
946   N ND2 . ASN A 167 ? 0.7938 0.5076 0.9279 0.1911  -0.0756 -0.1172 167 ASN A ND2 
947   N N   . LEU A 168 ? 0.7918 0.4754 0.8408 0.1499  -0.0319 -0.0280 168 LEU A N   
948   C CA  . LEU A 168 ? 0.7872 0.4539 0.8144 0.1382  -0.0228 -0.0048 168 LEU A CA  
949   C C   . LEU A 168 ? 0.7911 0.4365 0.8091 0.1383  -0.0370 0.0044  168 LEU A C   
950   O O   . LEU A 168 ? 0.8008 0.4536 0.8281 0.1459  -0.0468 -0.0060 168 LEU A O   
951   C CB  . LEU A 168 ? 0.7952 0.4824 0.8180 0.1292  -0.0018 -0.0036 168 LEU A CB  
952   C CG  . LEU A 168 ? 0.7779 0.4535 0.7855 0.1190  0.0101  0.0147  168 LEU A CG  
953   C CD1 . LEU A 168 ? 0.7677 0.4415 0.7735 0.1170  0.0141  0.0198  168 LEU A CD1 
954   C CD2 . LEU A 168 ? 0.7830 0.4696 0.7873 0.1122  0.0245  0.0150  168 LEU A CD2 
955   N N   . ASP A 169 ? 0.8269 0.4491 0.8255 0.1278  -0.0385 0.0232  169 ASP A N   
956   C CA  . ASP A 169 ? 0.8458 0.4485 0.8274 0.1205  -0.0502 0.0355  169 ASP A CA  
957   C C   . ASP A 169 ? 0.8566 0.4694 0.8246 0.1060  -0.0318 0.0448  169 ASP A C   
958   O O   . ASP A 169 ? 0.8799 0.4926 0.8390 0.1008  -0.0354 0.0479  169 ASP A O   
959   C CB  . ASP A 169 ? 0.8546 0.4231 0.8210 0.1145  -0.0687 0.0481  169 ASP A CB  
960   C CG  . ASP A 169 ? 0.8857 0.4376 0.8236 0.0949  -0.0725 0.0664  169 ASP A CG  
961   O OD1 . ASP A 169 ? 0.9054 0.4596 0.8370 0.0931  -0.0776 0.0682  169 ASP A OD1 
962   O OD2 . ASP A 169 ? 0.8976 0.4372 0.8185 0.0794  -0.0705 0.0779  169 ASP A OD2 
963   N N   . THR A 170 ? 0.7970 0.4204 0.7657 0.1005  -0.0133 0.0470  170 THR A N   
964   C CA  . THR A 170 ? 0.8040 0.4382 0.7660 0.0893  0.0028  0.0509  170 THR A CA  
965   C C   . THR A 170 ? 0.7759 0.4256 0.7507 0.0938  0.0195  0.0451  170 THR A C   
966   O O   . THR A 170 ? 0.7582 0.4081 0.7386 0.0978  0.0208  0.0451  170 THR A O   
967   C CB  . THR A 170 ? 0.8273 0.4537 0.7738 0.0742  0.0028  0.0609  170 THR A CB  
968   O OG1 . THR A 170 ? 0.8628 0.4709 0.7898 0.0644  -0.0141 0.0698  170 THR A OG1 
969   C CG2 . THR A 170 ? 0.8390 0.4844 0.7869 0.0651  0.0209  0.0579  170 THR A CG2 
970   N N   . LEU A 171 ? 0.7475 0.4077 0.7252 0.0918  0.0305  0.0409  171 LEU A N   
971   C CA  . LEU A 171 ? 0.7290 0.3957 0.7149 0.0939  0.0427  0.0378  171 LEU A CA  
972   C C   . LEU A 171 ? 0.7365 0.4064 0.7237 0.0879  0.0527  0.0370  171 LEU A C   
973   O O   . LEU A 171 ? 0.7576 0.4324 0.7420 0.0825  0.0561  0.0330  171 LEU A O   
974   C CB  . LEU A 171 ? 0.7350 0.4097 0.7247 0.0962  0.0453  0.0302  171 LEU A CB  
975   C CG  . LEU A 171 ? 0.7329 0.4076 0.7241 0.0933  0.0553  0.0300  171 LEU A CG  
976   C CD1 . LEU A 171 ? 0.7219 0.3927 0.7135 0.0958  0.0536  0.0354  171 LEU A CD1 
977   C CD2 . LEU A 171 ? 0.7599 0.4454 0.7505 0.0893  0.0589  0.0216  171 LEU A CD2 
978   N N   . HIS A 172 ? 0.7528 0.4226 0.7468 0.0896  0.0566  0.0382  172 HIS A N   
979   C CA  . HIS A 172 ? 0.7666 0.4431 0.7693 0.0871  0.0645  0.0320  172 HIS A CA  
980   C C   . HIS A 172 ? 0.7489 0.4175 0.7628 0.0950  0.0659  0.0312  172 HIS A C   
981   O O   . HIS A 172 ? 0.7367 0.4015 0.7534 0.1004  0.0611  0.0363  172 HIS A O   
982   C CB  . HIS A 172 ? 0.7923 0.4796 0.7955 0.0810  0.0646  0.0307  172 HIS A CB  
983   C CG  . HIS A 172 ? 0.8316 0.5229 0.8183 0.0674  0.0621  0.0331  172 HIS A CG  
984   N ND1 . HIS A 172 ? 0.8723 0.5720 0.8511 0.0550  0.0612  0.0344  172 HIS A ND1 
985   C CD2 . HIS A 172 ? 0.8462 0.5335 0.8205 0.0622  0.0584  0.0355  172 HIS A CD2 
986   C CE1 . HIS A 172 ? 0.9097 0.6061 0.8681 0.0409  0.0560  0.0398  172 HIS A CE1 
987   N NE2 . HIS A 172 ? 0.8932 0.5820 0.8498 0.0467  0.0532  0.0406  172 HIS A NE2 
988   N N   . LEU A 173 ? 0.7629 0.4265 0.7817 0.0948  0.0705  0.0254  173 LEU A N   
989   C CA  . LEU A 173 ? 0.7585 0.4057 0.7850 0.1006  0.0679  0.0262  173 LEU A CA  
990   C C   . LEU A 173 ? 0.7739 0.4219 0.8168 0.1026  0.0719  0.0126  173 LEU A C   
991   O O   . LEU A 173 ? 0.7804 0.4107 0.8255 0.1030  0.0712  0.0105  173 LEU A O   
992   C CB  . LEU A 173 ? 0.7621 0.3953 0.7749 0.0957  0.0669  0.0331  173 LEU A CB  
993   C CG  . LEU A 173 ? 0.7586 0.3953 0.7593 0.0938  0.0631  0.0415  173 LEU A CG  
994   C CD1 . LEU A 173 ? 0.7827 0.4201 0.7712 0.0843  0.0663  0.0407  173 LEU A CD1 
995   C CD2 . LEU A 173 ? 0.7575 0.3842 0.7581 0.0980  0.0554  0.0503  173 LEU A CD2 
996   N N   . VAL A 174 ? 0.7725 0.4423 0.8270 0.1021  0.0760  0.0014  174 VAL A N   
997   C CA  . VAL A 174 ? 0.7971 0.4806 0.8679 0.1004  0.0831  -0.0177 174 VAL A CA  
998   C C   . VAL A 174 ? 0.7958 0.4739 0.8942 0.1143  0.0770  -0.0299 174 VAL A C   
999   O O   . VAL A 174 ? 0.7870 0.4628 0.8935 0.1236  0.0685  -0.0255 174 VAL A O   
1000  C CB  . VAL A 174 ? 0.8331 0.5487 0.9004 0.0883  0.0907  -0.0259 174 VAL A CB  
1001  C CG1 . VAL A 174 ? 0.8644 0.5981 0.9411 0.0809  0.1002  -0.0454 174 VAL A CG1 
1002  C CG2 . VAL A 174 ? 0.8356 0.5483 0.8757 0.0784  0.0888  -0.0097 174 VAL A CG2 
1003  N N   . GLU A 175 ? 0.7828 0.4591 0.8978 0.1164  0.0799  -0.0472 175 GLU A N   
1004  C CA  . GLU A 175 ? 0.7854 0.4604 0.9344 0.1316  0.0726  -0.0666 175 GLU A CA  
1005  C C   . GLU A 175 ? 0.7712 0.4089 0.9221 0.1458  0.0540  -0.0513 175 GLU A C   
1006  O O   . GLU A 175 ? 0.7695 0.4129 0.9417 0.1595  0.0436  -0.0575 175 GLU A O   
1007  C CB  . GLU A 175 ? 0.8012 0.5213 0.9723 0.1318  0.0786  -0.0879 175 GLU A CB  
1008  C CG  . GLU A 175 ? 0.8287 0.5855 1.0027 0.1165  0.0949  -0.1094 175 GLU A CG  
1009  C CD  . GLU A 175 ? 0.8480 0.6537 1.0475 0.1141  0.1013  -0.1366 175 GLU A CD  
1010  O OE1 . GLU A 175 ? 0.8325 0.6417 1.0602 0.1313  0.0912  -0.1467 175 GLU A OE1 
1011  O OE2 . GLU A 175 ? 0.8811 0.7240 1.0717 0.0935  0.1156  -0.1485 175 GLU A OE2 
1012  N N   . ASN A 176 ? 0.8456 0.4476 0.9718 0.1401  0.0494  -0.0312 176 ASN A N   
1013  C CA  . ASN A 176 ? 0.8495 0.4100 0.9676 0.1464  0.0311  -0.0133 176 ASN A CA  
1014  C C   . ASN A 176 ? 0.8699 0.3921 0.9851 0.1434  0.0253  -0.0141 176 ASN A C   
1015  O O   . ASN A 176 ? 0.8751 0.4065 1.0011 0.1401  0.0355  -0.0322 176 ASN A O   
1016  C CB  . ASN A 176 ? 0.8412 0.3979 0.9266 0.1357  0.0316  0.0117  176 ASN A CB  
1017  C CG  . ASN A 176 ? 0.8287 0.4056 0.9194 0.1428  0.0277  0.0155  176 ASN A CG  
1018  O OD1 . ASN A 176 ? 0.8364 0.3983 0.9351 0.1535  0.0115  0.0210  176 ASN A OD1 
1019  N ND2 . ASN A 176 ? 0.8152 0.4242 0.9003 0.1360  0.0405  0.0131  176 ASN A ND2 
1020  N N   . LYS A 177 ? 0.8971 0.3750 0.9951 0.1420  0.0082  0.0058  177 LYS A N   
1021  C CA  . LYS A 177 ? 0.9275 0.3612 1.0156 0.1344  0.0003  0.0094  177 LYS A CA  
1022  C C   . LYS A 177 ? 0.9512 0.3659 0.9952 0.1109  0.0024  0.0347  177 LYS A C   
1023  O O   . LYS A 177 ? 0.9893 0.3569 1.0132 0.1013  -0.0129 0.0502  177 LYS A O   
1024  C CB  . LYS A 177 ? 0.9545 0.3543 1.0538 0.1493  -0.0243 0.0079  177 LYS A CB  
1025  C CG  . LYS A 177 ? 0.9469 0.3758 1.0899 0.1704  -0.0248 -0.0240 177 LYS A CG  
1026  C CD  . LYS A 177 ? 0.9430 0.3795 1.1032 0.1668  -0.0115 -0.0489 177 LYS A CD  
1027  C CE  . LYS A 177 ? 0.9134 0.4031 1.1183 0.1799  0.0004  -0.0845 177 LYS A CE  
1028  N NZ  . LYS A 177 ? 0.8846 0.4196 1.0909 0.1760  0.0172  -0.0835 177 LYS A NZ  
1029  N N   . LEU A 178 ? 0.9026 0.3547 0.9314 0.0998  0.0206  0.0374  178 LEU A N   
1030  C CA  . LEU A 178 ? 0.9230 0.3713 0.9160 0.0772  0.0259  0.0535  178 LEU A CA  
1031  C C   . LEU A 178 ? 0.9513 0.3852 0.9335 0.0610  0.0332  0.0481  178 LEU A C   
1032  O O   . LEU A 178 ? 0.9395 0.3905 0.9396 0.0650  0.0443  0.0295  178 LEU A O   
1033  C CB  . LEU A 178 ? 0.8956 0.3896 0.8834 0.0743  0.0408  0.0521  178 LEU A CB  
1034  C CG  . LEU A 178 ? 0.8642 0.3792 0.8638 0.0885  0.0375  0.0538  178 LEU A CG  
1035  C CD1 . LEU A 178 ? 0.8415 0.3950 0.8376 0.0854  0.0508  0.0495  178 LEU A CD1 
1036  C CD2 . LEU A 178 ? 0.8834 0.3774 0.8677 0.0866  0.0222  0.0723  178 LEU A CD2 
1037  N N   . ASN A 179 ? 1.0287 0.4334 0.9792 0.0394  0.0273  0.0641  179 ASN A N   
1038  C CA  . ASN A 179 ? 1.0633 0.4510 0.9991 0.0193  0.0331  0.0605  179 ASN A CA  
1039  C C   . ASN A 179 ? 1.0916 0.4995 0.9944 -0.0083 0.0441  0.0686  179 ASN A C   
1040  O O   . ASN A 179 ? 1.0928 0.5183 0.9821 -0.0127 0.0436  0.0787  179 ASN A O   
1041  C CB  . ASN A 179 ? 1.1003 0.4231 1.0288 0.0153  0.0119  0.0698  179 ASN A CB  
1042  C CG  . ASN A 179 ? 1.1254 0.4114 1.0242 0.0048  -0.0087 0.0970  179 ASN A CG  
1043  O OD1 . ASN A 179 ? 1.1118 0.4235 1.0035 0.0065  -0.0075 0.1060  179 ASN A OD1 
1044  N ND2 . ASN A 179 ? 1.1630 0.3860 1.0429 -0.0074 -0.0294 0.1106  179 ASN A ND2 
1045  N N   . GLY A 180 ? 1.0016 0.4106 0.8934 -0.0277 0.0543  0.0609  180 GLY A N   
1046  C CA  . GLY A 180 ? 1.0331 0.4724 0.9001 -0.0542 0.0675  0.0604  180 GLY A CA  
1047  C C   . GLY A 180 ? 1.0171 0.5100 0.9033 -0.0476 0.0857  0.0389  180 GLY A C   
1048  O O   . GLY A 180 ? 0.9823 0.4852 0.8952 -0.0271 0.0887  0.0268  180 GLY A O   
1049  N N   . SER A 181 ? 1.0111 0.5409 0.8830 -0.0668 0.0967  0.0330  181 SER A N   
1050  C CA  . SER A 181 ? 1.0083 0.5900 0.8976 -0.0605 0.1097  0.0130  181 SER A CA  
1051  C C   . SER A 181 ? 0.9898 0.6063 0.8918 -0.0430 0.1089  0.0110  181 SER A C   
1052  O O   . SER A 181 ? 0.9984 0.6135 0.8891 -0.0466 0.1039  0.0211  181 SER A O   
1053  C CB  . SER A 181 ? 1.0580 0.6660 0.9310 -0.0893 0.1210  0.0018  181 SER A CB  
1054  O OG  . SER A 181 ? 1.0706 0.6493 0.9343 -0.1053 0.1231  0.0004  181 SER A OG  
1055  N N   . ILE A 182 ? 0.9012 0.5471 0.8251 -0.0254 0.1124  -0.0018 182 ILE A N   
1056  C CA  . ILE A 182 ? 0.8846 0.5598 0.8207 -0.0092 0.1093  -0.0050 182 ILE A CA  
1057  C C   . ILE A 182 ? 0.9428 0.6542 0.8722 -0.0236 0.1138  -0.0157 182 ILE A C   
1058  O O   . ILE A 182 ? 0.9823 0.7197 0.9119 -0.0360 0.1212  -0.0308 182 ILE A O   
1059  C CB  . ILE A 182 ? 0.8517 0.5454 0.8073 0.0084  0.1087  -0.0145 182 ILE A CB  
1060  C CG1 . ILE A 182 ? 0.8044 0.4714 0.7677 0.0195  0.1063  -0.0081 182 ILE A CG1 
1061  C CG2 . ILE A 182 ? 0.8359 0.5538 0.8018 0.0229  0.1022  -0.0176 182 ILE A CG2 
1062  C CD1 . ILE A 182 ? 0.7855 0.4708 0.7609 0.0298  0.1063  -0.0160 182 ILE A CD1 
1063  N N   . PRO A 183 ? 0.8658 0.5849 0.7907 -0.0235 0.1101  -0.0114 183 PRO A N   
1064  C CA  . PRO A 183 ? 0.9300 0.6919 0.8519 -0.0383 0.1156  -0.0274 183 PRO A CA  
1065  C C   . PRO A 183 ? 0.9286 0.7335 0.8762 -0.0238 0.1156  -0.0507 183 PRO A C   
1066  O O   . PRO A 183 ? 0.8710 0.6717 0.8361 0.0005  0.1073  -0.0499 183 PRO A O   
1067  C CB  . PRO A 183 ? 0.9313 0.6920 0.8484 -0.0350 0.1100  -0.0191 183 PRO A CB  
1068  C CG  . PRO A 183 ? 0.8738 0.5848 0.7834 -0.0262 0.1020  0.0050  183 PRO A CG  
1069  C CD  . PRO A 183 ? 0.8231 0.5177 0.7475 -0.0105 0.1013  0.0048  183 PRO A CD  
1070  N N   . SER A 184 ? 0.9837 0.8305 0.9326 -0.0406 0.1234  -0.0721 184 SER A N   
1071  C CA  . SER A 184 ? 0.9397 0.8308 0.9166 -0.0254 0.1199  -0.0976 184 SER A CA  
1072  C C   . SER A 184 ? 0.9014 0.8082 0.8986 -0.0030 0.1087  -0.1054 184 SER A C   
1073  O O   . SER A 184 ? 0.8611 0.7821 0.8825 0.0197  0.0973  -0.1174 184 SER A O   
1074  C CB  . SER A 184 ? 0.9509 0.8914 0.9280 -0.0492 0.1309  -0.1234 184 SER A CB  
1075  O OG  . SER A 184 ? 0.9951 0.9141 0.9446 -0.0782 0.1420  -0.1126 184 SER A OG  
1076  N N   . GLU A 185 ? 0.9235 0.8251 0.9100 -0.0096 0.1098  -0.0982 185 GLU A N   
1077  C CA  . GLU A 185 ? 0.8902 0.8073 0.8956 0.0090  0.1002  -0.1080 185 GLU A CA  
1078  C C   . GLU A 185 ? 0.8430 0.7245 0.8585 0.0369  0.0859  -0.0923 185 GLU A C   
1079  O O   . GLU A 185 ? 0.8106 0.7013 0.8449 0.0553  0.0745  -0.1021 185 GLU A O   
1080  C CB  . GLU A 185 ? 0.9262 0.8442 0.9132 -0.0083 0.1057  -0.1015 185 GLU A CB  
1081  C CG  . GLU A 185 ? 0.9518 0.9153 0.9277 -0.0402 0.1191  -0.1214 185 GLU A CG  
1082  C CD  . GLU A 185 ? 0.9999 0.9429 0.9436 -0.0704 0.1295  -0.1060 185 GLU A CD  
1083  O OE1 . GLU A 185 ? 1.0241 0.9154 0.9565 -0.0640 0.1256  -0.0804 185 GLU A OE1 
1084  O OE2 . GLU A 185 ? 1.0043 0.9837 0.9344 -0.1019 0.1412  -0.1215 185 GLU A OE2 
1085  N N   . ILE A 186 ? 0.9305 0.7728 0.9338 0.0389  0.0861  -0.0702 186 ILE A N   
1086  C CA  . ILE A 186 ? 0.8731 0.6880 0.8833 0.0599  0.0741  -0.0574 186 ILE A CA  
1087  C C   . ILE A 186 ? 0.8572 0.6905 0.8882 0.0765  0.0610  -0.0731 186 ILE A C   
1088  O O   . ILE A 186 ? 0.8244 0.6421 0.8626 0.0933  0.0464  -0.0677 186 ILE A O   
1089  C CB  . ILE A 186 ? 0.8528 0.6327 0.8490 0.0560  0.0787  -0.0374 186 ILE A CB  
1090  C CG1 . ILE A 186 ? 0.8686 0.6267 0.8468 0.0419  0.0864  -0.0229 186 ILE A CG1 
1091  C CG2 . ILE A 186 ? 0.7967 0.5544 0.7968 0.0718  0.0686  -0.0256 186 ILE A CG2 
1092  C CD1 . ILE A 186 ? 0.8553 0.6071 0.8314 0.0465  0.0815  -0.0152 186 ILE A CD1 
1093  N N   . GLY A 187 ? 0.8456 0.7115 0.8858 0.0713  0.0639  -0.0929 187 GLY A N   
1094  C CA  . GLY A 187 ? 0.8301 0.7165 0.8926 0.0883  0.0480  -0.1104 187 GLY A CA  
1095  C C   . GLY A 187 ? 0.8018 0.7074 0.8885 0.1055  0.0331  -0.1295 187 GLY A C   
1096  O O   . GLY A 187 ? 0.7832 0.7028 0.8919 0.1229  0.0147  -0.1456 187 GLY A O   
1097  N N   . ARG A 188 ? 0.8200 0.7267 0.9042 0.1013  0.0388  -0.1296 188 ARG A N   
1098  C CA  . ARG A 188 ? 0.7902 0.7136 0.8986 0.1174  0.0253  -0.1495 188 ARG A CA  
1099  C C   . ARG A 188 ? 0.7580 0.6376 0.8654 0.1355  0.0068  -0.1312 188 ARG A C   
1100  O O   . ARG A 188 ? 0.7319 0.6171 0.8607 0.1516  -0.0088 -0.1472 188 ARG A O   
1101  C CB  . ARG A 188 ? 0.8091 0.7583 0.9131 0.1010  0.0407  -0.1598 188 ARG A CB  
1102  C CG  . ARG A 188 ? 0.8309 0.8335 0.9384 0.0803  0.0567  -0.1856 188 ARG A CG  
1103  C CD  . ARG A 188 ? 0.8469 0.8778 0.9479 0.0616  0.0693  -0.1968 188 ARG A CD  
1104  N NE  . ARG A 188 ? 0.8567 0.9440 0.9582 0.0363  0.0853  -0.2237 188 ARG A NE  
1105  C CZ  . ARG A 188 ? 0.8421 0.9833 0.9552 0.0239  0.0926  -0.2548 188 ARG A CZ  
1106  N NH1 . ARG A 188 ? 0.8232 0.9686 0.9502 0.0362  0.0852  -0.2639 188 ARG A NH1 
1107  N NH2 . ARG A 188 ? 0.8416 1.0372 0.9523 -0.0037 0.1085  -0.2796 188 ARG A NH2 
1108  N N   . LEU A 189 ? 0.8349 0.6730 0.9188 0.1317  0.0081  -0.1005 189 LEU A N   
1109  C CA  . LEU A 189 ? 0.8044 0.6021 0.8811 0.1415  -0.0060 -0.0811 189 LEU A CA  
1110  C C   . LEU A 189 ? 0.7921 0.5749 0.8774 0.1570  -0.0314 -0.0820 189 LEU A C   
1111  O O   . LEU A 189 ? 0.7970 0.5547 0.8648 0.1532  -0.0360 -0.0625 189 LEU A O   
1112  C CB  . LEU A 189 ? 0.8037 0.5723 0.8541 0.1286  0.0070  -0.0529 189 LEU A CB  
1113  C CG  . LEU A 189 ? 0.8174 0.5919 0.8568 0.1141  0.0268  -0.0478 189 LEU A CG  
1114  C CD1 . LEU A 189 ? 0.7878 0.5322 0.8089 0.1077  0.0335  -0.0236 189 LEU A CD1 
1115  C CD2 . LEU A 189 ? 0.8185 0.6041 0.8660 0.1170  0.0250  -0.0573 189 LEU A CD2 
1116  N N   . THR A 190 ? 0.8243 0.6232 0.9372 0.1744  -0.0502 -0.1065 190 THR A N   
1117  C CA  . THR A 190 ? 0.8214 0.6056 0.9448 0.1911  -0.0799 -0.1097 190 THR A CA  
1118  C C   . THR A 190 ? 0.8125 0.5421 0.9165 0.1939  -0.1001 -0.0828 190 THR A C   
1119  O O   . THR A 190 ? 0.8243 0.5310 0.9237 0.2008  -0.1250 -0.0749 190 THR A O   
1120  C CB  . THR A 190 ? 0.8060 0.6214 0.9698 0.2120  -0.0979 -0.1469 190 THR A CB  
1121  O OG1 . THR A 190 ? 0.7843 0.5959 0.9588 0.2176  -0.0993 -0.1557 190 THR A OG1 
1122  C CG2 . THR A 190 ? 0.8174 0.6934 0.9991 0.2053  -0.0788 -0.1759 190 THR A CG2 
1123  N N   . LYS A 191 ? 0.8512 0.5599 0.9415 0.1866  -0.0912 -0.0684 191 LYS A N   
1124  C CA  . LYS A 191 ? 0.8459 0.5058 0.9160 0.1847  -0.1086 -0.0445 191 LYS A CA  
1125  C C   . LYS A 191 ? 0.8553 0.4980 0.8917 0.1634  -0.0919 -0.0159 191 LYS A C   
1126  O O   . LYS A 191 ? 0.8587 0.4657 0.8740 0.1560  -0.1035 0.0043  191 LYS A O   
1127  C CB  . LYS A 191 ? 0.8248 0.4745 0.9045 0.1907  -0.1124 -0.0507 191 LYS A CB  
1128  C CG  . LYS A 191 ? 0.8153 0.4665 0.9276 0.2138  -0.1397 -0.0773 191 LYS A CG  
1129  C CD  . LYS A 191 ? 0.8015 0.4358 0.9199 0.2176  -0.1450 -0.0813 191 LYS A CD  
1130  C CE  . LYS A 191 ? 0.7964 0.4477 0.9561 0.2410  -0.1657 -0.1179 191 LYS A CE  
1131  N NZ  . LYS A 191 ? 0.8000 0.4485 0.9656 0.2393  -0.1642 -0.1244 191 LYS A NZ  
1132  N N   . VAL A 192 ? 0.8044 0.4722 0.8360 0.1524  -0.0658 -0.0157 192 VAL A N   
1133  C CA  . VAL A 192 ? 0.8103 0.4672 0.8171 0.1346  -0.0497 0.0051  192 VAL A CA  
1134  C C   . VAL A 192 ? 0.8399 0.4803 0.8280 0.1272  -0.0634 0.0181  192 VAL A C   
1135  O O   . VAL A 192 ? 0.8596 0.5057 0.8546 0.1349  -0.0789 0.0104  192 VAL A O   
1136  C CB  . VAL A 192 ? 0.8126 0.4960 0.8218 0.1266  -0.0223 -0.0003 192 VAL A CB  
1137  C CG1 . VAL A 192 ? 0.8416 0.5423 0.8518 0.1237  -0.0195 -0.0071 192 VAL A CG1 
1138  C CG2 . VAL A 192 ? 0.7995 0.4725 0.7935 0.1140  -0.0064 0.0151  192 VAL A CG2 
1139  N N   . THR A 193 ? 0.7951 0.4179 0.7591 0.1108  -0.0587 0.0368  193 THR A N   
1140  C CA  . THR A 193 ? 0.8360 0.4477 0.7760 0.0964  -0.0677 0.0502  193 THR A CA  
1141  C C   . THR A 193 ? 0.8548 0.4838 0.7832 0.0786  -0.0426 0.0537  193 THR A C   
1142  O O   . THR A 193 ? 0.8973 0.5306 0.8106 0.0666  -0.0449 0.0580  193 THR A O   
1143  C CB  . THR A 193 ? 0.8490 0.4235 0.7655 0.0871  -0.0901 0.0683  193 THR A CB  
1144  O OG1 . THR A 193 ? 0.8292 0.3989 0.7432 0.0807  -0.0773 0.0727  193 THR A OG1 
1145  C CG2 . THR A 193 ? 0.8655 0.4158 0.7924 0.1054  -0.1229 0.0647  193 THR A CG2 
1146  N N   . GLU A 194 ? 0.7977 0.4372 0.7341 0.0769  -0.0207 0.0506  194 GLU A N   
1147  C CA  . GLU A 194 ? 0.8094 0.4659 0.7426 0.0643  0.0014  0.0487  194 GLU A CA  
1148  C C   . GLU A 194 ? 0.7680 0.4377 0.7212 0.0734  0.0195  0.0383  194 GLU A C   
1149  O O   . GLU A 194 ? 0.7329 0.3977 0.6948 0.0815  0.0201  0.0383  194 GLU A O   
1150  C CB  . GLU A 194 ? 0.8273 0.4789 0.7451 0.0480  0.0055  0.0578  194 GLU A CB  
1151  C CG  . GLU A 194 ? 0.8423 0.5164 0.7648 0.0380  0.0278  0.0495  194 GLU A CG  
1152  C CD  . GLU A 194 ? 0.8839 0.5640 0.7915 0.0180  0.0318  0.0534  194 GLU A CD  
1153  O OE1 . GLU A 194 ? 0.9366 0.6165 0.8199 -0.0015 0.0245  0.0602  194 GLU A OE1 
1154  O OE2 . GLU A 194 ? 0.8683 0.5555 0.7875 0.0199  0.0416  0.0490  194 GLU A OE2 
1155  N N   . ILE A 195 ? 0.7796 0.4640 0.7377 0.0699  0.0329  0.0302  195 ILE A N   
1156  C CA  . ILE A 195 ? 0.7480 0.4380 0.7193 0.0738  0.0484  0.0232  195 ILE A CA  
1157  C C   . ILE A 195 ? 0.7620 0.4584 0.7341 0.0646  0.0619  0.0193  195 ILE A C   
1158  O O   . ILE A 195 ? 0.8025 0.5087 0.7684 0.0553  0.0644  0.0150  195 ILE A O   
1159  C CB  . ILE A 195 ? 0.7521 0.4520 0.7309 0.0778  0.0506  0.0137  195 ILE A CB  
1160  C CG1 . ILE A 195 ? 0.7456 0.4471 0.7305 0.0882  0.0385  0.0108  195 ILE A CG1 
1161  C CG2 . ILE A 195 ? 0.7355 0.4348 0.7205 0.0756  0.0650  0.0097  195 ILE A CG2 
1162  C CD1 . ILE A 195 ? 0.7682 0.4890 0.7620 0.0899  0.0402  -0.0031 195 ILE A CD1 
1163  N N   . ALA A 196 ? 0.7825 0.4752 0.7637 0.0676  0.0693  0.0186  196 ALA A N   
1164  C CA  . ALA A 196 ? 0.7972 0.4975 0.7870 0.0628  0.0804  0.0096  196 ALA A CA  
1165  C C   . ALA A 196 ? 0.7627 0.4515 0.7665 0.0718  0.0844  0.0070  196 ALA A C   
1166  O O   . ALA A 196 ? 0.7384 0.4195 0.7464 0.0788  0.0805  0.0129  196 ALA A O   
1167  C CB  . ALA A 196 ? 0.8246 0.5348 0.8122 0.0556  0.0809  0.0095  196 ALA A CB  
1168  N N   . ILE A 197 ? 0.7983 0.4833 0.8067 0.0703  0.0903  -0.0005 197 ILE A N   
1169  C CA  . ILE A 197 ? 0.7815 0.4478 0.7991 0.0759  0.0909  -0.0012 197 ILE A CA  
1170  C C   . ILE A 197 ? 0.7979 0.4634 0.8299 0.0748  0.0970  -0.0162 197 ILE A C   
1171  O O   . ILE A 197 ? 0.7981 0.4426 0.8342 0.0760  0.0961  -0.0179 197 ILE A O   
1172  C CB  . ILE A 197 ? 0.7822 0.4372 0.7890 0.0725  0.0896  0.0049  197 ILE A CB  
1173  C CG1 . ILE A 197 ? 0.7811 0.4490 0.7781 0.0721  0.0853  0.0100  197 ILE A CG1 
1174  C CG2 . ILE A 197 ? 0.7728 0.4048 0.7792 0.0760  0.0842  0.0135  197 ILE A CG2 
1175  C CD1 . ILE A 197 ? 0.8006 0.4699 0.7902 0.0663  0.0864  0.0091  197 ILE A CD1 
1176  N N   . TYR A 198 ? 0.7517 0.4396 0.7907 0.0706  0.1026  -0.0282 198 TYR A N   
1177  C CA  . TYR A 198 ? 0.7700 0.4638 0.8255 0.0688  0.1096  -0.0480 198 TYR A CA  
1178  C C   . TYR A 198 ? 0.7557 0.4381 0.8365 0.0821  0.1051  -0.0576 198 TYR A C   
1179  O O   . TYR A 198 ? 0.7385 0.4153 0.8233 0.0911  0.0976  -0.0493 198 TYR A O   
1180  C CB  . TYR A 198 ? 0.8108 0.5389 0.8642 0.0561  0.1180  -0.0608 198 TYR A CB  
1181  C CG  . TYR A 198 ? 0.8305 0.5805 0.8846 0.0527  0.1180  -0.0617 198 TYR A CG  
1182  C CD1 . TYR A 198 ? 0.8453 0.5976 0.8764 0.0457  0.1124  -0.0441 198 TYR A CD1 
1183  C CD2 . TYR A 198 ? 0.8396 0.6093 0.9183 0.0554  0.1227  -0.0825 198 TYR A CD2 
1184  C CE1 . TYR A 198 ? 0.8777 0.6478 0.9053 0.0380  0.1124  -0.0441 198 TYR A CE1 
1185  C CE2 . TYR A 198 ? 0.8686 0.6643 0.9468 0.0479  0.1245  -0.0857 198 TYR A CE2 
1186  C CZ  . TYR A 198 ? 0.8934 0.6874 0.9434 0.0376  0.1197  -0.0649 198 TYR A CZ  
1187  O OH  . TYR A 198 ? 0.9347 0.7514 0.9804 0.0264  0.1211  -0.0668 198 TYR A OH  
1188  N N   . ASP A 199 ? 0.8383 0.5178 0.9383 0.0840  0.1081  -0.0774 199 ASP A N   
1189  C CA  . ASP A 199 ? 0.8292 0.4934 0.9588 0.0996  0.0998  -0.0909 199 ASP A CA  
1190  C C   . ASP A 199 ? 0.8136 0.4336 0.9356 0.1092  0.0844  -0.0698 199 ASP A C   
1191  O O   . ASP A 199 ? 0.8021 0.4161 0.9338 0.1213  0.0738  -0.0646 199 ASP A O   
1192  C CB  . ASP A 199 ? 0.8317 0.5306 0.9835 0.1055  0.1015  -0.1072 199 ASP A CB  
1193  C CG  . ASP A 199 ? 0.8263 0.5239 1.0185 0.1215  0.0950  -0.1344 199 ASP A CG  
1194  O OD1 . ASP A 199 ? 0.8203 0.4755 1.0195 0.1316  0.0832  -0.1320 199 ASP A OD1 
1195  O OD2 . ASP A 199 ? 0.8311 0.5696 1.0479 0.1232  0.1005  -0.1590 199 ASP A OD2 
1196  N N   . ASN A 200 ? 0.8692 0.4604 0.9720 0.1008  0.0832  -0.0583 200 ASN A N   
1197  C CA  . ASN A 200 ? 0.8708 0.4206 0.9575 0.1015  0.0697  -0.0367 200 ASN A CA  
1198  C C   . ASN A 200 ? 0.8981 0.4124 0.9798 0.0937  0.0666  -0.0391 200 ASN A C   
1199  O O   . ASN A 200 ? 0.9080 0.4283 1.0062 0.0930  0.0730  -0.0603 200 ASN A O   
1200  C CB  . ASN A 200 ? 0.8608 0.4200 0.9186 0.0916  0.0732  -0.0158 200 ASN A CB  
1201  C CG  . ASN A 200 ? 0.8388 0.4080 0.8987 0.1010  0.0669  -0.0063 200 ASN A CG  
1202  O OD1 . ASN A 200 ? 0.8403 0.3848 0.8984 0.1071  0.0536  0.0054  200 ASN A OD1 
1203  N ND2 . ASN A 200 ? 0.8259 0.4296 0.8875 0.1006  0.0751  -0.0105 200 ASN A ND2 
1204  N N   . LEU A 201 ? 0.8601 0.3378 0.9173 0.0849  0.0569  -0.0180 201 LEU A N   
1205  C CA  . LEU A 201 ? 0.9001 0.3377 0.9447 0.0720  0.0520  -0.0158 201 LEU A CA  
1206  C C   . LEU A 201 ? 0.8963 0.3412 0.9067 0.0481  0.0624  -0.0029 201 LEU A C   
1207  O O   . LEU A 201 ? 0.9336 0.3431 0.9197 0.0313  0.0555  0.0104  201 LEU A O   
1208  C CB  . LEU A 201 ? 0.9493 0.3308 0.9924 0.0784  0.0274  -0.0028 201 LEU A CB  
1209  C CG  . LEU A 201 ? 0.9568 0.3325 1.0396 0.1056  0.0131  -0.0187 201 LEU A CG  
1210  C CD1 . LEU A 201 ? 1.0079 0.3332 1.0799 0.1119  -0.0149 -0.0007 201 LEU A CD1 
1211  C CD2 . LEU A 201 ? 0.9626 0.3432 1.0765 0.1123  0.0185  -0.0496 201 LEU A CD2 
1212  N N   . LEU A 202 ? 0.8790 0.3708 0.8871 0.0452  0.0777  -0.0076 202 LEU A N   
1213  C CA  . LEU A 202 ? 0.8986 0.4074 0.8817 0.0262  0.0868  -0.0011 202 LEU A CA  
1214  C C   . LEU A 202 ? 0.9327 0.4337 0.9090 0.0090  0.0941  -0.0112 202 LEU A C   
1215  O O   . LEU A 202 ? 0.9306 0.4321 0.9248 0.0136  0.0981  -0.0280 202 LEU A O   
1216  C CB  . LEU A 202 ? 0.8748 0.4319 0.8621 0.0314  0.0963  -0.0058 202 LEU A CB  
1217  C CG  . LEU A 202 ? 0.8411 0.4079 0.8336 0.0457  0.0902  0.0031  202 LEU A CG  
1218  C CD1 . LEU A 202 ? 0.8271 0.4327 0.8191 0.0479  0.0962  0.0002  202 LEU A CD1 
1219  C CD2 . LEU A 202 ? 0.8528 0.3971 0.8284 0.0409  0.0806  0.0206  202 LEU A CD2 
1220  N N   . THR A 203 ? 0.9257 0.4226 0.8757 -0.0130 0.0967  -0.0028 203 THR A N   
1221  C CA  . THR A 203 ? 0.9628 0.4523 0.9012 -0.0345 0.1038  -0.0108 203 THR A CA  
1222  C C   . THR A 203 ? 0.9833 0.5190 0.9091 -0.0499 0.1166  -0.0159 203 THR A C   
1223  O O   . THR A 203 ? 0.9735 0.5407 0.8997 -0.0431 0.1176  -0.0127 203 THR A O   
1224  C CB  . THR A 203 ? 0.9993 0.4314 0.9149 -0.0526 0.0916  0.0035  203 THR A CB  
1225  O OG1 . THR A 203 ? 1.0183 0.4506 0.9060 -0.0681 0.0881  0.0216  203 THR A OG1 
1226  C CG2 . THR A 203 ? 0.9877 0.3720 0.9203 -0.0331 0.0737  0.0070  203 THR A CG2 
1227  N N   . GLY A 204 ? 0.9809 0.5215 0.8979 -0.0704 0.1252  -0.0263 204 GLY A N   
1228  C CA  . GLY A 204 ? 1.0086 0.5948 0.9162 -0.0866 0.1362  -0.0352 204 GLY A CA  
1229  C C   . GLY A 204 ? 0.9945 0.6314 0.9230 -0.0702 0.1422  -0.0501 204 GLY A C   
1230  O O   . GLY A 204 ? 0.9619 0.5995 0.9084 -0.0505 0.1400  -0.0531 204 GLY A O   
1231  N N   . PRO A 205 ? 0.9371 0.6187 0.8632 -0.0796 0.1485  -0.0607 205 PRO A N   
1232  C CA  . PRO A 205 ? 0.9327 0.6591 0.8769 -0.0652 0.1497  -0.0743 205 PRO A CA  
1233  C C   . PRO A 205 ? 0.9070 0.6459 0.8620 -0.0417 0.1405  -0.0673 205 PRO A C   
1234  O O   . PRO A 205 ? 0.8990 0.6239 0.8487 -0.0379 0.1357  -0.0554 205 PRO A O   
1235  C CB  . PRO A 205 ? 0.9739 0.7425 0.9139 -0.0836 0.1568  -0.0904 205 PRO A CB  
1236  C CG  . PRO A 205 ? 0.9953 0.7526 0.9159 -0.1029 0.1586  -0.0827 205 PRO A CG  
1237  C CD  . PRO A 205 ? 0.9765 0.6716 0.8829 -0.1066 0.1539  -0.0630 205 PRO A CD  
1238  N N   . ILE A 206 ? 0.9121 0.6757 0.8802 -0.0278 0.1369  -0.0743 206 ILE A N   
1239  C CA  . ILE A 206 ? 0.8915 0.6702 0.8682 -0.0086 0.1261  -0.0699 206 ILE A CA  
1240  C C   . ILE A 206 ? 0.9176 0.7324 0.8985 -0.0109 0.1239  -0.0817 206 ILE A C   
1241  O O   . ILE A 206 ? 0.9385 0.7845 0.9236 -0.0196 0.1274  -0.0982 206 ILE A O   
1242  C CB  . ILE A 206 ? 0.8779 0.6674 0.8618 0.0028  0.1198  -0.0716 206 ILE A CB  
1243  C CG1 . ILE A 206 ? 0.8535 0.6162 0.8364 0.0038  0.1237  -0.0651 206 ILE A CG1 
1244  C CG2 . ILE A 206 ? 0.8650 0.6649 0.8547 0.0199  0.1053  -0.0663 206 ILE A CG2 
1245  C CD1 . ILE A 206 ? 0.8635 0.6419 0.8481 0.0049  0.1218  -0.0701 206 ILE A CD1 
1246  N N   . PRO A 207 ? 0.9135 0.7303 0.8959 -0.0040 0.1187  -0.0773 207 PRO A N   
1247  C CA  . PRO A 207 ? 0.9319 0.7897 0.9226 -0.0071 0.1178  -0.0948 207 PRO A CA  
1248  C C   . PRO A 207 ? 0.9160 0.8079 0.9266 0.0086  0.1062  -0.1104 207 PRO A C   
1249  O O   . PRO A 207 ? 0.8966 0.7769 0.9132 0.0277  0.0925  -0.1020 207 PRO A O   
1250  C CB  . PRO A 207 ? 0.9219 0.7710 0.9120 0.0005  0.1128  -0.0863 207 PRO A CB  
1251  C CG  . PRO A 207 ? 0.9092 0.7100 0.8845 -0.0008 0.1147  -0.0631 207 PRO A CG  
1252  C CD  . PRO A 207 ? 0.8832 0.6687 0.8613 0.0054  0.1141  -0.0594 207 PRO A CD  
1253  N N   . SER A 208 ? 0.8980 0.8321 0.9174 -0.0010 0.1101  -0.1333 208 SER A N   
1254  C CA  . SER A 208 ? 0.8853 0.8544 0.9266 0.0155  0.0954  -0.1506 208 SER A CA  
1255  C C   . SER A 208 ? 0.8627 0.8446 0.9236 0.0380  0.0780  -0.1577 208 SER A C   
1256  O O   . SER A 208 ? 0.8550 0.8502 0.9334 0.0577  0.0581  -0.1658 208 SER A O   
1257  C CB  . SER A 208 ? 0.8878 0.9052 0.9376 -0.0004 0.1039  -0.1774 208 SER A CB  
1258  O OG  . SER A 208 ? 0.8825 0.9273 0.9333 -0.0159 0.1147  -0.1924 208 SER A OG  
1259  N N   . SER A 209 ? 0.8517 0.8276 0.9095 0.0352  0.0831  -0.1547 209 SER A N   
1260  C CA  . SER A 209 ? 0.8254 0.8092 0.9020 0.0563  0.0672  -0.1619 209 SER A CA  
1261  C C   . SER A 209 ? 0.8137 0.7558 0.8876 0.0771  0.0492  -0.1397 209 SER A C   
1262  O O   . SER A 209 ? 0.7886 0.7316 0.8789 0.0967  0.0313  -0.1453 209 SER A O   
1263  C CB  . SER A 209 ? 0.8267 0.8127 0.8960 0.0444  0.0788  -0.1620 209 SER A CB  
1264  O OG  . SER A 209 ? 0.8450 0.7831 0.8877 0.0351  0.0873  -0.1323 209 SER A OG  
1265  N N   . PHE A 210 ? 0.8943 0.8014 0.9480 0.0714  0.0535  -0.1168 210 PHE A N   
1266  C CA  . PHE A 210 ? 0.8830 0.7553 0.9299 0.0847  0.0383  -0.0966 210 PHE A CA  
1267  C C   . PHE A 210 ? 0.8871 0.7690 0.9467 0.1012  0.0132  -0.1036 210 PHE A C   
1268  O O   . PHE A 210 ? 0.8784 0.7316 0.9314 0.1115  -0.0045 -0.0879 210 PHE A O   
1269  C CB  . PHE A 210 ? 0.8916 0.7363 0.9175 0.0722  0.0502  -0.0776 210 PHE A CB  
1270  C CG  . PHE A 210 ? 0.8615 0.6778 0.8757 0.0663  0.0622  -0.0621 210 PHE A CG  
1271  C CD1 . PHE A 210 ? 0.8564 0.6775 0.8723 0.0623  0.0695  -0.0659 210 PHE A CD1 
1272  C CD2 . PHE A 210 ? 0.8416 0.6303 0.8436 0.0637  0.0652  -0.0456 210 PHE A CD2 
1273  C CE1 . PHE A 210 ? 0.8342 0.6283 0.8390 0.0578  0.0769  -0.0506 210 PHE A CE1 
1274  C CE2 . PHE A 210 ? 0.8080 0.5735 0.8038 0.0611  0.0735  -0.0341 210 PHE A CE2 
1275  C CZ  . PHE A 210 ? 0.8041 0.5699 0.8008 0.0590  0.0780  -0.0351 210 PHE A CZ  
1276  N N   . GLY A 211 ? 0.8350 0.7556 0.9111 0.1024  0.0097  -0.1266 211 GLY A N   
1277  C CA  . GLY A 211 ? 0.8397 0.7706 0.9323 0.1215  -0.0194 -0.1361 211 GLY A CA  
1278  C C   . GLY A 211 ? 0.8037 0.7311 0.9174 0.1438  -0.0415 -0.1447 211 GLY A C   
1279  O O   . GLY A 211 ? 0.8048 0.7212 0.9279 0.1624  -0.0725 -0.1447 211 GLY A O   
1280  N N   . ASN A 212 ? 0.8591 0.7936 0.9795 0.1417  -0.0280 -0.1522 212 ASN A N   
1281  C CA  . ASN A 212 ? 0.8235 0.7557 0.9651 0.1615  -0.0464 -0.1631 212 ASN A CA  
1282  C C   . ASN A 212 ? 0.8103 0.6876 0.9327 0.1667  -0.0577 -0.1336 212 ASN A C   
1283  O O   . ASN A 212 ? 0.7829 0.6488 0.9211 0.1844  -0.0782 -0.1398 212 ASN A O   
1284  C CB  . ASN A 212 ? 0.8063 0.7747 0.9609 0.1531  -0.0259 -0.1853 212 ASN A CB  
1285  C CG  . ASN A 212 ? 0.8054 0.8377 0.9855 0.1489  -0.0191 -0.2229 212 ASN A CG  
1286  O OD1 . ASN A 212 ? 0.8162 0.8662 1.0063 0.1542  -0.0295 -0.2327 212 ASN A OD1 
1287  N ND2 . ASN A 212 ? 0.7925 0.8631 0.9819 0.1370  -0.0015 -0.2449 212 ASN A ND2 
1288  N N   . LEU A 213 ? 0.7915 0.7427 0.9422 0.1940  0.0950  -0.0964 213 LEU A N   
1289  C CA  . LEU A 213 ? 0.7934 0.6911 0.9159 0.1882  0.0980  -0.0912 213 LEU A CA  
1290  C C   . LEU A 213 ? 0.7966 0.6640 0.8999 0.2109  0.0954  -0.0846 213 LEU A C   
1291  O O   . LEU A 213 ? 0.7909 0.6399 0.8846 0.2052  0.0899  -0.0773 213 LEU A O   
1292  C CB  . LEU A 213 ? 0.7829 0.6786 0.9060 0.1620  0.0932  -0.0870 213 LEU A CB  
1293  C CG  . LEU A 213 ? 0.7805 0.7012 0.9153 0.1425  0.0960  -0.0898 213 LEU A CG  
1294  C CD1 . LEU A 213 ? 0.7708 0.6863 0.9015 0.1248  0.0898  -0.0835 213 LEU A CD1 
1295  C CD2 . LEU A 213 ? 0.7888 0.6976 0.9119 0.1389  0.1068  -0.0970 213 LEU A CD2 
1296  N N   . THR A 214 ? 0.8470 0.7067 0.9410 0.2392  0.1009  -0.0867 214 THR A N   
1297  C CA  . THR A 214 ? 0.8514 0.6858 0.9232 0.2695  0.0990  -0.0789 214 THR A CA  
1298  C C   . THR A 214 ? 0.8614 0.6290 0.8991 0.2622  0.1073  -0.0712 214 THR A C   
1299  O O   . THR A 214 ? 0.8634 0.6105 0.8826 0.2789  0.1038  -0.0616 214 THR A O   
1300  C CB  . THR A 214 ? 0.8627 0.6934 0.9237 0.3046  0.1064  -0.0825 214 THR A CB  
1301  O OG1 . THR A 214 ? 0.8795 0.6688 0.9237 0.2964  0.1231  -0.0881 214 THR A OG1 
1302  C CG2 . THR A 214 ? 0.8479 0.7541 0.9457 0.3136  0.0977  -0.0920 214 THR A CG2 
1303  N N   . LYS A 215 ? 0.9097 0.6453 0.9379 0.2373  0.1190  -0.0770 215 LYS A N   
1304  C CA  . LYS A 215 ? 0.9209 0.5953 0.9185 0.2264  0.1308  -0.0745 215 LYS A CA  
1305  C C   . LYS A 215 ? 0.9042 0.5871 0.9095 0.2010  0.1218  -0.0709 215 LYS A C   
1306  O O   . LYS A 215 ? 0.9114 0.5504 0.8951 0.1878  0.1320  -0.0710 215 LYS A O   
1307  C CB  . LYS A 215 ? 0.9358 0.5778 0.9213 0.2101  0.1486  -0.0875 215 LYS A CB  
1308  C CG  . LYS A 215 ? 0.9572 0.5747 0.9263 0.2361  0.1617  -0.0912 215 LYS A CG  
1309  C CD  . LYS A 215 ? 0.9804 0.5372 0.9102 0.2656  0.1732  -0.0807 215 LYS A CD  
1310  C CE  . LYS A 215 ? 0.9927 0.5559 0.9154 0.3080  0.1739  -0.0777 215 LYS A CE  
1311  N NZ  . LYS A 215 ? 1.0539 0.5364 0.9292 0.3286  0.1991  -0.0772 215 LYS A NZ  
1312  N N   . LEU A 216 ? 0.8458 0.5822 0.8803 0.1929  0.1053  -0.0690 216 LEU A N   
1313  C CA  . LEU A 216 ? 0.8304 0.5753 0.8712 0.1702  0.0971  -0.0662 216 LEU A CA  
1314  C C   . LEU A 216 ? 0.8315 0.5496 0.8540 0.1804  0.0947  -0.0557 216 LEU A C   
1315  O O   . LEU A 216 ? 0.8354 0.5595 0.8541 0.2071  0.0890  -0.0487 216 LEU A O   
1316  C CB  . LEU A 216 ? 0.8152 0.6157 0.8867 0.1620  0.0833  -0.0662 216 LEU A CB  
1317  C CG  . LEU A 216 ? 0.7998 0.6125 0.8784 0.1379  0.0766  -0.0652 216 LEU A CG  
1318  C CD1 . LEU A 216 ? 0.8000 0.6061 0.8733 0.1194  0.0843  -0.0738 216 LEU A CD1 
1319  C CD2 . LEU A 216 ? 0.7916 0.6484 0.8947 0.1344  0.0667  -0.0637 216 LEU A CD2 
1320  N N   . VAL A 217 ? 0.8777 0.5692 0.8877 0.1605  0.0993  -0.0558 217 VAL A N   
1321  C CA  . VAL A 217 ? 0.8788 0.5465 0.8712 0.1671  0.0976  -0.0456 217 VAL A CA  
1322  C C   . VAL A 217 ? 0.8579 0.5551 0.8669 0.1477  0.0844  -0.0442 217 VAL A C   
1323  O O   . VAL A 217 ? 0.8538 0.5535 0.8589 0.1562  0.0759  -0.0353 217 VAL A O   
1324  C CB  . VAL A 217 ? 0.9006 0.5021 0.8575 0.1629  0.1192  -0.0464 217 VAL A CB  
1325  C CG1 . VAL A 217 ? 0.9245 0.4899 0.8618 0.1805  0.1354  -0.0492 217 VAL A CG1 
1326  C CG2 . VAL A 217 ? 0.8949 0.4934 0.8561 0.1276  0.1264  -0.0589 217 VAL A CG2 
1327  N N   . ASN A 218 ? 0.8038 0.5236 0.8285 0.1244  0.0826  -0.0529 218 ASN A N   
1328  C CA  . ASN A 218 ? 0.7863 0.5285 0.8214 0.1078  0.0724  -0.0521 218 ASN A CA  
1329  C C   . ASN A 218 ? 0.7744 0.5580 0.8316 0.1004  0.0641  -0.0554 218 ASN A C   
1330  O O   . ASN A 218 ? 0.7792 0.5687 0.8387 0.0937  0.0701  -0.0638 218 ASN A O   
1331  C CB  . ASN A 218 ? 0.7887 0.5106 0.8115 0.0871  0.0819  -0.0603 218 ASN A CB  
1332  C CG  . ASN A 218 ? 0.8011 0.4789 0.7997 0.0897  0.0923  -0.0557 218 ASN A CG  
1333  O OD1 . ASN A 218 ? 0.8044 0.4707 0.7940 0.1089  0.0882  -0.0434 218 ASN A OD1 
1334  N ND2 . ASN A 218 ? 0.8107 0.4654 0.7975 0.0701  0.1070  -0.0668 218 ASN A ND2 
1335  N N   . LEU A 219 ? 0.6901 0.4991 0.7604 0.1010  0.0521  -0.0496 219 LEU A N   
1336  C CA  . LEU A 219 ? 0.6710 0.5103 0.7570 0.0936  0.0481  -0.0511 219 LEU A CA  
1337  C C   . LEU A 219 ? 0.6568 0.5030 0.7423 0.0835  0.0407  -0.0475 219 LEU A C   
1338  O O   . LEU A 219 ? 0.6494 0.5001 0.7391 0.0866  0.0331  -0.0425 219 LEU A O   
1339  C CB  . LEU A 219 ? 0.6684 0.5321 0.7720 0.1037  0.0450  -0.0505 219 LEU A CB  
1340  C CG  . LEU A 219 ? 0.6643 0.5523 0.7813 0.0945  0.0475  -0.0533 219 LEU A CG  
1341  C CD1 . LEU A 219 ? 0.6714 0.5528 0.7794 0.0891  0.0562  -0.0575 219 LEU A CD1 
1342  C CD2 . LEU A 219 ? 0.6721 0.5879 0.8092 0.1022  0.0478  -0.0574 219 LEU A CD2 
1343  N N   . TYR A 220 ? 0.7245 0.5739 0.8035 0.0736  0.0426  -0.0509 220 TYR A N   
1344  C CA  . TYR A 220 ? 0.7170 0.5715 0.7913 0.0676  0.0365  -0.0479 220 TYR A CA  
1345  C C   . TYR A 220 ? 0.7281 0.5954 0.8015 0.0662  0.0382  -0.0463 220 TYR A C   
1346  O O   . TYR A 220 ? 0.7436 0.6163 0.8093 0.0660  0.0430  -0.0511 220 TYR A O   
1347  C CB  . TYR A 220 ? 0.7201 0.5690 0.7826 0.0610  0.0378  -0.0543 220 TYR A CB  
1348  C CG  . TYR A 220 ? 0.7201 0.5466 0.7775 0.0602  0.0421  -0.0560 220 TYR A CG  
1349  C CD1 . TYR A 220 ? 0.7126 0.5277 0.7704 0.0677  0.0379  -0.0473 220 TYR A CD1 
1350  C CD2 . TYR A 220 ? 0.7336 0.5488 0.7831 0.0522  0.0522  -0.0673 220 TYR A CD2 
1351  C CE1 . TYR A 220 ? 0.7220 0.5095 0.7676 0.0705  0.0444  -0.0463 220 TYR A CE1 
1352  C CE2 . TYR A 220 ? 0.7402 0.5247 0.7793 0.0506  0.0611  -0.0680 220 TYR A CE2 
1353  C CZ  . TYR A 220 ? 0.7360 0.5039 0.7708 0.0614  0.0575  -0.0558 220 TYR A CZ  
1354  O OH  . TYR A 220 ? 0.7493 0.4800 0.7664 0.0631  0.0688  -0.0542 220 TYR A OH  
1355  N N   . LEU A 221 ? 0.7014 0.5718 0.7803 0.0652  0.0359  -0.0405 221 LEU A N   
1356  C CA  . LEU A 221 ? 0.7216 0.5934 0.7936 0.0633  0.0420  -0.0375 221 LEU A CA  
1357  C C   . LEU A 221 ? 0.7215 0.5855 0.7866 0.0607  0.0395  -0.0319 221 LEU A C   
1358  O O   . LEU A 221 ? 0.7409 0.5990 0.8035 0.0568  0.0476  -0.0291 221 LEU A O   
1359  C CB  . LEU A 221 ? 0.7374 0.6172 0.8234 0.0612  0.0502  -0.0392 221 LEU A CB  
1360  C CG  . LEU A 221 ? 0.7400 0.6275 0.8336 0.0656  0.0541  -0.0449 221 LEU A CG  
1361  C CD1 . LEU A 221 ? 0.7528 0.6561 0.8669 0.0645  0.0589  -0.0484 221 LEU A CD1 
1362  C CD2 . LEU A 221 ? 0.7571 0.6433 0.8349 0.0675  0.0612  -0.0466 221 LEU A CD2 
1363  N N   . PHE A 222 ? 0.7868 0.6477 0.8471 0.0618  0.0307  -0.0309 222 PHE A N   
1364  C CA  . PHE A 222 ? 0.7829 0.6370 0.8428 0.0587  0.0278  -0.0272 222 PHE A CA  
1365  C C   . PHE A 222 ? 0.8047 0.6444 0.8432 0.0609  0.0345  -0.0219 222 PHE A C   
1366  O O   . PHE A 222 ? 0.8207 0.6492 0.8589 0.0547  0.0433  -0.0202 222 PHE A O   
1367  C CB  . PHE A 222 ? 0.7594 0.6138 0.8199 0.0599  0.0173  -0.0273 222 PHE A CB  
1368  C CG  . PHE A 222 ? 0.7541 0.6112 0.8058 0.0625  0.0146  -0.0303 222 PHE A CG  
1369  C CD1 . PHE A 222 ? 0.7515 0.6100 0.8088 0.0617  0.0166  -0.0352 222 PHE A CD1 
1370  C CD2 . PHE A 222 ? 0.7571 0.6159 0.7950 0.0652  0.0111  -0.0302 222 PHE A CD2 
1371  C CE1 . PHE A 222 ? 0.7564 0.6171 0.8067 0.0592  0.0174  -0.0418 222 PHE A CE1 
1372  C CE2 . PHE A 222 ? 0.7610 0.6301 0.7946 0.0646  0.0097  -0.0374 222 PHE A CE2 
1373  C CZ  . PHE A 222 ? 0.7622 0.6319 0.8029 0.0593  0.0138  -0.0441 222 PHE A CZ  
1374  N N   . ILE A 223 ? 0.7628 0.6021 0.7811 0.0703  0.0322  -0.0203 223 ILE A N   
1375  C CA  . ILE A 223 ? 0.7804 0.6018 0.7719 0.0785  0.0381  -0.0134 223 ILE A CA  
1376  C C   . ILE A 223 ? 0.8089 0.6193 0.7857 0.0820  0.0521  -0.0095 223 ILE A C   
1377  O O   . ILE A 223 ? 0.8213 0.6424 0.7849 0.0928  0.0524  -0.0105 223 ILE A O   
1378  C CB  . ILE A 223 ? 0.7778 0.6093 0.7515 0.0918  0.0300  -0.0142 223 ILE A CB  
1379  C CG1 . ILE A 223 ? 0.7526 0.5915 0.7389 0.0867  0.0191  -0.0176 223 ILE A CG1 
1380  C CG2 . ILE A 223 ? 0.8006 0.6116 0.7395 0.1075  0.0374  -0.0058 223 ILE A CG2 
1381  C CD1 . ILE A 223 ? 0.7491 0.6134 0.7353 0.0909  0.0112  -0.0259 223 ILE A CD1 
1382  N N   . ASN A 224 ? 0.7770 0.5676 0.7555 0.0721  0.0651  -0.0067 224 ASN A N   
1383  C CA  . ASN A 224 ? 0.8084 0.5861 0.7750 0.0714  0.0821  -0.0035 224 ASN A CA  
1384  C C   . ASN A 224 ? 0.8289 0.5769 0.7908 0.0580  0.0995  -0.0015 224 ASN A C   
1385  O O   . ASN A 224 ? 0.8192 0.5557 0.7824 0.0524  0.0973  -0.0023 224 ASN A O   
1386  C CB  . ASN A 224 ? 0.8044 0.6078 0.7972 0.0650  0.0805  -0.0109 224 ASN A CB  
1387  C CG  . ASN A 224 ? 0.8072 0.6260 0.7887 0.0785  0.0755  -0.0123 224 ASN A CG  
1388  O OD1 . ASN A 224 ? 0.8314 0.6405 0.7817 0.0924  0.0817  -0.0066 224 ASN A OD1 
1389  N ND2 . ASN A 224 ? 0.7856 0.6279 0.7898 0.0757  0.0652  -0.0208 224 ASN A ND2 
1390  N N   . SER A 225 ? 0.8290 0.5640 0.7848 0.0513  0.1187  -0.0005 225 SER A N   
1391  C CA  . SER A 225 ? 0.8539 0.5614 0.8078 0.0326  0.1406  -0.0025 225 SER A CA  
1392  C C   . SER A 225 ? 0.8673 0.5985 0.8531 0.0145  0.1498  -0.0134 225 SER A C   
1393  O O   . SER A 225 ? 0.9017 0.6107 0.8770 0.0023  0.1749  -0.0138 225 SER A O   
1394  C CB  . SER A 225 ? 0.8915 0.5462 0.7936 0.0429  0.1635  0.0109  225 SER A CB  
1395  O OG  . SER A 225 ? 0.8845 0.5120 0.7600 0.0547  0.1601  0.0179  225 SER A OG  
1396  N N   . LEU A 226 ? 0.8072 0.5826 0.8300 0.0136  0.1314  -0.0226 226 LEU A N   
1397  C CA  . LEU A 226 ? 0.8213 0.6270 0.8769 0.0003  0.1373  -0.0346 226 LEU A CA  
1398  C C   . LEU A 226 ? 0.8327 0.6435 0.9099 -0.0236 0.1492  -0.0479 226 LEU A C   
1399  O O   . LEU A 226 ? 0.8169 0.6202 0.8951 -0.0289 0.1439  -0.0505 226 LEU A O   
1400  C CB  . LEU A 226 ? 0.7932 0.6394 0.8776 0.0094  0.1151  -0.0405 226 LEU A CB  
1401  C CG  . LEU A 226 ? 0.7763 0.6218 0.8444 0.0280  0.1056  -0.0329 226 LEU A CG  
1402  C CD1 . LEU A 226 ? 0.7496 0.6254 0.8431 0.0344  0.0901  -0.0397 226 LEU A CD1 
1403  C CD2 . LEU A 226 ? 0.8091 0.6420 0.8566 0.0309  0.1225  -0.0284 226 LEU A CD2 
1404  N N   . SER A 227 ? 0.8573 0.6847 0.9532 -0.0392 0.1660  -0.0589 227 SER A N   
1405  C CA  . SER A 227 ? 0.8656 0.6972 0.9796 -0.0669 0.1846  -0.0752 227 SER A CA  
1406  C C   . SER A 227 ? 0.8662 0.7600 1.0282 -0.0768 0.1808  -0.0961 227 SER A C   
1407  O O   . SER A 227 ? 0.8725 0.7959 1.0475 -0.0612 0.1679  -0.0950 227 SER A O   
1408  C CB  . SER A 227 ? 0.8944 0.6746 0.9747 -0.0807 0.2197  -0.0696 227 SER A CB  
1409  O OG  . SER A 227 ? 0.8910 0.6647 0.9834 -0.1105 0.2398  -0.0863 227 SER A OG  
1410  N N   . GLY A 228 ? 0.8553 0.7708 1.0434 -0.1025 0.1927  -0.1173 228 GLY A N   
1411  C CA  . GLY A 228 ? 0.8401 0.8232 1.0754 -0.1120 0.1906  -0.1413 228 GLY A CA  
1412  C C   . GLY A 228 ? 0.8180 0.8537 1.0823 -0.0948 0.1584  -0.1496 228 GLY A C   
1413  O O   . GLY A 228 ? 0.8177 0.8368 1.0676 -0.0794 0.1390  -0.1380 228 GLY A O   
1414  N N   . SER A 229 ? 0.8281 0.9298 1.1321 -0.0956 0.1540  -0.1706 229 SER A N   
1415  C CA  . SER A 229 ? 0.7998 0.9550 1.1285 -0.0746 0.1254  -0.1793 229 SER A CA  
1416  C C   . SER A 229 ? 0.8027 0.9519 1.1180 -0.0406 0.1067  -0.1604 229 SER A C   
1417  O O   . SER A 229 ? 0.8163 0.9437 1.1176 -0.0355 0.1157  -0.1492 229 SER A O   
1418  C CB  . SER A 229 ? 0.7579 0.9925 1.1333 -0.0852 0.1279  -0.2118 229 SER A CB  
1419  O OG  . SER A 229 ? 0.7483 0.9896 1.1381 -0.1220 0.1487  -0.2337 229 SER A OG  
1420  N N   . ILE A 230 ? 0.8252 0.9911 1.1424 -0.0175 0.0821  -0.1577 230 ILE A N   
1421  C CA  . ILE A 230 ? 0.8139 0.9718 1.1177 0.0137  0.0670  -0.1425 230 ILE A CA  
1422  C C   . ILE A 230 ? 0.7889 0.9949 1.1166 0.0247  0.0689  -0.1552 230 ILE A C   
1423  O O   . ILE A 230 ? 0.7623 1.0300 1.1222 0.0233  0.0662  -0.1780 230 ILE A O   
1424  C CB  . ILE A 230 ? 0.7964 0.9577 1.0933 0.0352  0.0444  -0.1373 230 ILE A CB  
1425  C CG1 . ILE A 230 ? 0.8185 0.9446 1.0987 0.0212  0.0435  -0.1304 230 ILE A CG1 
1426  C CG2 . ILE A 230 ? 0.7831 0.9176 1.0575 0.0630  0.0348  -0.1196 230 ILE A CG2 
1427  C CD1 . ILE A 230 ? 0.8029 0.9192 1.0683 0.0416  0.0239  -0.1206 230 ILE A CD1 
1428  N N   . PRO A 231 ? 0.8010 0.9859 1.1150 0.0365  0.0734  -0.1439 231 PRO A N   
1429  C CA  . PRO A 231 ? 0.7789 1.0090 1.1141 0.0502  0.0750  -0.1559 231 PRO A CA  
1430  C C   . PRO A 231 ? 0.7497 1.0139 1.0916 0.0833  0.0541  -0.1598 231 PRO A C   
1431  O O   . PRO A 231 ? 0.7505 0.9788 1.0665 0.1036  0.0419  -0.1434 231 PRO A O   
1432  C CB  . PRO A 231 ? 0.7934 0.9809 1.1044 0.0566  0.0833  -0.1400 231 PRO A CB  
1433  C CG  . PRO A 231 ? 0.8219 0.9527 1.1047 0.0395  0.0906  -0.1244 231 PRO A CG  
1434  C CD  . PRO A 231 ? 0.8220 0.9458 1.1017 0.0371  0.0783  -0.1224 231 PRO A CD  
1435  N N   . SER A 232 ? 0.7724 1.1071 1.1473 0.0899  0.0518  -0.1827 232 SER A N   
1436  C CA  . SER A 232 ? 0.7446 1.1179 1.1231 0.1268  0.0320  -0.1876 232 SER A CA  
1437  C C   . SER A 232 ? 0.7468 1.0909 1.1004 0.1616  0.0281  -0.1720 232 SER A C   
1438  O O   . SER A 232 ? 0.7354 1.0815 1.0740 0.1964  0.0134  -0.1665 232 SER A O   
1439  C CB  . SER A 232 ? 0.7082 1.1741 1.1298 0.1274  0.0306  -0.2194 232 SER A CB  
1440  O OG  . SER A 232 ? 0.7080 1.1949 1.1524 0.1019  0.0512  -0.2328 232 SER A OG  
1441  N N   . GLU A 233 ? 0.7860 1.1010 1.1320 0.1538  0.0424  -0.1651 233 GLU A N   
1442  C CA  . GLU A 233 ? 0.7911 1.0706 1.1110 0.1830  0.0414  -0.1515 233 GLU A CA  
1443  C C   . GLU A 233 ? 0.8043 1.0157 1.0858 0.1919  0.0349  -0.1296 233 GLU A C   
1444  O O   . GLU A 233 ? 0.8060 0.9878 1.0628 0.2204  0.0326  -0.1201 233 GLU A O   
1445  C CB  . GLU A 233 ? 0.8056 1.0670 1.1244 0.1687  0.0587  -0.1501 233 GLU A CB  
1446  C CG  . GLU A 233 ? 0.7902 1.1163 1.1439 0.1641  0.0681  -0.1715 233 GLU A CG  
1447  C CD  . GLU A 233 ? 0.7874 1.1480 1.1698 0.1267  0.0779  -0.1868 233 GLU A CD  
1448  O OE1 . GLU A 233 ? 0.8114 1.1272 1.1793 0.0995  0.0857  -0.1763 233 GLU A OE1 
1449  O OE2 . GLU A 233 ? 0.7600 1.1929 1.1782 0.1250  0.0791  -0.2109 233 GLU A OE2 
1450  N N   . ILE A 234 ? 0.8218 1.0068 1.0967 0.1679  0.0338  -0.1226 234 ILE A N   
1451  C CA  . ILE A 234 ? 0.8282 0.9538 1.0694 0.1732  0.0290  -0.1043 234 ILE A CA  
1452  C C   . ILE A 234 ? 0.8172 0.9465 1.0452 0.2053  0.0156  -0.1009 234 ILE A C   
1453  O O   . ILE A 234 ? 0.8222 0.9005 1.0179 0.2198  0.0155  -0.0864 234 ILE A O   
1454  C CB  . ILE A 234 ? 0.8367 0.9409 1.0753 0.1428  0.0305  -0.0993 234 ILE A CB  
1455  C CG1 . ILE A 234 ? 0.8493 0.9223 1.0789 0.1223  0.0443  -0.0938 234 ILE A CG1 
1456  C CG2 . ILE A 234 ? 0.8320 0.8998 1.0462 0.1497  0.0208  -0.0866 234 ILE A CG2 
1457  C CD1 . ILE A 234 ? 0.8554 0.8963 1.0711 0.1015  0.0456  -0.0850 234 ILE A CD1 
1458  N N   . GLY A 235 ? 0.8673 1.0579 1.1182 0.2182  0.0059  -0.1154 235 GLY A N   
1459  C CA  . GLY A 235 ? 0.8556 1.0556 1.0907 0.2552  -0.0074 -0.1126 235 GLY A CA  
1460  C C   . GLY A 235 ? 0.8571 1.0401 1.0689 0.2946  -0.0050 -0.1063 235 GLY A C   
1461  O O   . GLY A 235 ? 0.8546 1.0272 1.0403 0.3300  -0.0128 -0.0987 235 GLY A O   
1462  N N   . ASN A 236 ? 0.8543 1.0313 1.0715 0.2910  0.0069  -0.1088 236 ASN A N   
1463  C CA  . ASN A 236 ? 0.8580 1.0208 1.0547 0.3285  0.0112  -0.1054 236 ASN A CA  
1464  C C   . ASN A 236 ? 0.8823 0.9606 1.0419 0.3256  0.0252  -0.0889 236 ASN A C   
1465  O O   . ASN A 236 ? 0.8915 0.9479 1.0322 0.3516  0.0332  -0.0867 236 ASN A O   
1466  C CB  . ASN A 236 ? 0.8451 1.0699 1.0756 0.3307  0.0149  -0.1240 236 ASN A CB  
1467  C CG  . ASN A 236 ? 0.8143 1.1309 1.0796 0.3430  0.0017  -0.1451 236 ASN A CG  
1468  O OD1 . ASN A 236 ? 0.8012 1.1700 1.1061 0.3108  0.0033  -0.1625 236 ASN A OD1 
1469  N ND2 . ASN A 236 ? 0.8024 1.1392 1.0510 0.3901  -0.0100 -0.1450 236 ASN A ND2 
1470  N N   . LEU A 237 ? 0.8815 0.9144 1.0303 0.2951  0.0291  -0.0794 237 LEU A N   
1471  C CA  . LEU A 237 ? 0.8992 0.8577 1.0139 0.2909  0.0425  -0.0678 237 LEU A CA  
1472  C C   . LEU A 237 ? 0.9083 0.8195 0.9819 0.3230  0.0436  -0.0552 237 LEU A C   
1473  O O   . LEU A 237 ? 0.9038 0.8108 0.9687 0.3240  0.0353  -0.0486 237 LEU A O   
1474  C CB  . LEU A 237 ? 0.9007 0.8340 1.0170 0.2513  0.0454  -0.0640 237 LEU A CB  
1475  C CG  . LEU A 237 ? 0.9018 0.8557 1.0422 0.2212  0.0508  -0.0719 237 LEU A CG  
1476  C CD1 . LEU A 237 ? 0.9113 0.8563 1.0475 0.2298  0.0626  -0.0768 237 LEU A CD1 
1477  C CD2 . LEU A 237 ? 0.8920 0.9077 1.0680 0.2097  0.0437  -0.0819 237 LEU A CD2 
1478  N N   . PRO A 238 ? 0.9476 0.8169 0.9912 0.3495  0.0557  -0.0510 238 PRO A N   
1479  C CA  . PRO A 238 ? 0.9649 0.7875 0.9635 0.3872  0.0594  -0.0381 238 PRO A CA  
1480  C C   . PRO A 238 ? 0.9882 0.7353 0.9517 0.3703  0.0712  -0.0257 238 PRO A C   
1481  O O   . PRO A 238 ? 1.0220 0.7409 0.9542 0.3918  0.0705  -0.0141 238 PRO A O   
1482  C CB  . PRO A 238 ? 1.0119 0.8098 0.9892 0.4186  0.0724  -0.0392 238 PRO A CB  
1483  C CG  . PRO A 238 ? 0.9787 0.7931 0.9856 0.3874  0.0789  -0.0514 238 PRO A CG  
1484  C CD  . PRO A 238 ? 0.9595 0.8067 1.0014 0.3421  0.0705  -0.0563 238 PRO A CD  
1485  N N   . ASN A 239 ? 1.0436 0.7611 1.0116 0.3324  0.0827  -0.0295 239 ASN A N   
1486  C CA  . ASN A 239 ? 1.0570 0.7072 0.9951 0.3123  0.0973  -0.0228 239 ASN A CA  
1487  C C   . ASN A 239 ? 1.0374 0.7088 0.9962 0.2777  0.0870  -0.0234 239 ASN A C   
1488  O O   . ASN A 239 ? 1.0438 0.6701 0.9836 0.2574  0.0981  -0.0207 239 ASN A O   
1489  C CB  . ASN A 239 ? 1.0732 0.6788 1.0001 0.2942  0.1179  -0.0304 239 ASN A CB  
1490  C CG  . ASN A 239 ? 1.1000 0.6648 0.9953 0.3293  0.1331  -0.0284 239 ASN A CG  
1491  O OD1 . ASN A 239 ? 1.1231 0.6346 0.9753 0.3581  0.1437  -0.0167 239 ASN A OD1 
1492  N ND2 . ASN A 239 ? 1.0997 0.6863 1.0125 0.3291  0.1356  -0.0392 239 ASN A ND2 
1493  N N   . LEU A 240 ? 0.9490 0.6869 0.9452 0.2704  0.0681  -0.0281 240 LEU A N   
1494  C CA  . LEU A 240 ? 0.9331 0.6882 0.9470 0.2391  0.0597  -0.0289 240 LEU A CA  
1495  C C   . LEU A 240 ? 0.9356 0.6610 0.9242 0.2448  0.0585  -0.0182 240 LEU A C   
1496  O O   . LEU A 240 ? 0.9416 0.6678 0.9140 0.2761  0.0532  -0.0112 240 LEU A O   
1497  C CB  . LEU A 240 ? 0.9173 0.7420 0.9711 0.2325  0.0434  -0.0363 240 LEU A CB  
1498  C CG  . LEU A 240 ? 0.9057 0.7440 0.9770 0.1986  0.0384  -0.0383 240 LEU A CG  
1499  C CD1 . LEU A 240 ? 0.9062 0.7285 0.9790 0.1753  0.0491  -0.0431 240 LEU A CD1 
1500  C CD2 . LEU A 240 ? 0.8976 0.7942 1.0017 0.1923  0.0258  -0.0453 240 LEU A CD2 
1501  N N   . ARG A 241 ? 1.0208 0.7221 1.0045 0.2163  0.0638  -0.0178 241 ARG A N   
1502  C CA  . ARG A 241 ? 1.0239 0.6965 0.9849 0.2158  0.0650  -0.0089 241 ARG A CA  
1503  C C   . ARG A 241 ? 1.0029 0.7110 0.9873 0.1931  0.0510  -0.0111 241 ARG A C   
1504  O O   . ARG A 241 ? 1.0003 0.7173 0.9796 0.2027  0.0414  -0.0049 241 ARG A O   
1505  C CB  . ARG A 241 ? 1.0421 0.6492 0.9717 0.2022  0.0881  -0.0084 241 ARG A CB  
1506  C CG  . ARG A 241 ? 1.0711 0.6184 0.9540 0.2293  0.1028  0.0039  241 ARG A CG  
1507  C CD  . ARG A 241 ? 1.0968 0.5753 0.9496 0.2150  0.1318  0.0001  241 ARG A CD  
1508  N NE  . ARG A 241 ? 1.1184 0.5649 0.9503 0.2404  0.1445  0.0013  241 ARG A NE  
1509  C CZ  . ARG A 241 ? 1.1363 0.5414 0.9562 0.2260  0.1665  -0.0084 241 ARG A CZ  
1510  N NH1 . ARG A 241 ? 1.1342 0.5291 0.9623 0.1856  0.1782  -0.0220 241 ARG A NH1 
1511  N NH2 . ARG A 241 ? 1.1565 0.5334 0.9563 0.2534  0.1770  -0.0066 241 ARG A NH2 
1512  N N   . GLU A 242 ? 0.8682 0.5954 0.8748 0.1655  0.0502  -0.0195 242 GLU A N   
1513  C CA  . GLU A 242 ? 0.8510 0.6046 0.8745 0.1456  0.0396  -0.0212 242 GLU A CA  
1514  C C   . GLU A 242 ? 0.8419 0.6396 0.8957 0.1369  0.0313  -0.0279 242 GLU A C   
1515  O O   . GLU A 242 ? 0.8424 0.6420 0.9025 0.1296  0.0381  -0.0338 242 GLU A O   
1516  C CB  . GLU A 242 ? 0.8470 0.5773 0.8610 0.1220  0.0490  -0.0249 242 GLU A CB  
1517  C CG  . GLU A 242 ? 0.8640 0.5446 0.8468 0.1246  0.0637  -0.0207 242 GLU A CG  
1518  C CD  . GLU A 242 ? 0.8594 0.5332 0.8383 0.1013  0.0679  -0.0250 242 GLU A CD  
1519  O OE1 . GLU A 242 ? 0.8424 0.5500 0.8414 0.0859  0.0591  -0.0315 242 GLU A OE1 
1520  O OE2 . GLU A 242 ? 0.8758 0.5100 0.8296 0.0998  0.0815  -0.0221 242 GLU A OE2 
1521  N N   . LEU A 243 ? 0.7164 0.5467 0.7865 0.1366  0.0189  -0.0280 243 LEU A N   
1522  C CA  . LEU A 243 ? 0.7071 0.5735 0.8029 0.1257  0.0149  -0.0346 243 LEU A CA  
1523  C C   . LEU A 243 ? 0.6926 0.5663 0.7927 0.1097  0.0090  -0.0340 243 LEU A C   
1524  O O   . LEU A 243 ? 0.6938 0.5802 0.7973 0.1137  0.0002  -0.0334 243 LEU A O   
1525  C CB  . LEU A 243 ? 0.7180 0.6208 0.8318 0.1409  0.0091  -0.0401 243 LEU A CB  
1526  C CG  . LEU A 243 ? 0.7217 0.6613 0.8628 0.1275  0.0098  -0.0495 243 LEU A CG  
1527  C CD1 . LEU A 243 ? 0.7224 0.6511 0.8631 0.1173  0.0210  -0.0506 243 LEU A CD1 
1528  C CD2 . LEU A 243 ? 0.7311 0.7147 0.8926 0.1424  0.0046  -0.0592 243 LEU A CD2 
1529  N N   . CYS A 244 ? 0.7281 0.5945 0.8259 0.0940  0.0137  -0.0346 244 CYS A N   
1530  C CA  . CYS A 244 ? 0.7172 0.5859 0.8141 0.0821  0.0099  -0.0333 244 CYS A CA  
1531  C C   . CYS A 244 ? 0.7262 0.6086 0.8334 0.0728  0.0142  -0.0364 244 CYS A C   
1532  O O   . CYS A 244 ? 0.7278 0.6045 0.8285 0.0684  0.0210  -0.0366 244 CYS A O   
1533  C CB  . CYS A 244 ? 0.7062 0.5562 0.7865 0.0757  0.0124  -0.0318 244 CYS A CB  
1534  S SG  . CYS A 244 ? 0.7090 0.5349 0.7728 0.0811  0.0134  -0.0288 244 CYS A SG  
1535  N N   . LEU A 245 ? 0.6748 0.5746 0.7959 0.0692  0.0117  -0.0399 245 LEU A N   
1536  C CA  . LEU A 245 ? 0.6956 0.6016 0.8236 0.0573  0.0203  -0.0433 245 LEU A CA  
1537  C C   . LEU A 245 ? 0.6983 0.5950 0.8198 0.0479  0.0201  -0.0422 245 LEU A C   
1538  O O   . LEU A 245 ? 0.7226 0.6201 0.8488 0.0365  0.0295  -0.0465 245 LEU A O   
1539  C CB  . LEU A 245 ? 0.7235 0.6592 0.8754 0.0564  0.0231  -0.0532 245 LEU A CB  
1540  C CG  . LEU A 245 ? 0.7218 0.6683 0.8802 0.0683  0.0245  -0.0553 245 LEU A CG  
1541  C CD1 . LEU A 245 ? 0.7434 0.7296 0.9278 0.0707  0.0242  -0.0675 245 LEU A CD1 
1542  C CD2 . LEU A 245 ? 0.7229 0.6549 0.8717 0.0638  0.0357  -0.0524 245 LEU A CD2 
1543  N N   . ASP A 246 ? 0.7844 0.6695 0.8936 0.0518  0.0118  -0.0374 246 ASP A N   
1544  C CA  . ASP A 246 ? 0.7858 0.6619 0.8880 0.0457  0.0105  -0.0369 246 ASP A CA  
1545  C C   . ASP A 246 ? 0.7939 0.6479 0.8776 0.0411  0.0213  -0.0323 246 ASP A C   
1546  O O   . ASP A 246 ? 0.7965 0.6445 0.8704 0.0449  0.0272  -0.0286 246 ASP A O   
1547  C CB  . ASP A 246 ? 0.7617 0.6318 0.8535 0.0526  -0.0001 -0.0326 246 ASP A CB  
1548  C CG  . ASP A 246 ? 0.7425 0.6023 0.8205 0.0582  0.0001  -0.0277 246 ASP A CG  
1549  O OD1 . ASP A 246 ? 0.7407 0.6034 0.8228 0.0624  0.0014  -0.0285 246 ASP A OD1 
1550  O OD2 . ASP A 246 ? 0.7358 0.5865 0.7990 0.0585  -0.0004 -0.0249 246 ASP A OD2 
1551  N N   . ARG A 247 ? 0.8052 0.6456 0.8812 0.0348  0.0249  -0.0328 247 ARG A N   
1552  C CA  . ARG A 247 ? 0.8185 0.6296 0.8678 0.0359  0.0359  -0.0262 247 ARG A CA  
1553  C C   . ARG A 247 ? 0.8426 0.6439 0.8861 0.0322  0.0521  -0.0248 247 ARG A C   
1554  O O   . ARG A 247 ? 0.8487 0.6378 0.8702 0.0426  0.0567  -0.0173 247 ARG A O   
1555  C CB  . ARG A 247 ? 0.8030 0.6093 0.8321 0.0503  0.0281  -0.0189 247 ARG A CB  
1556  C CG  . ARG A 247 ? 0.7893 0.5930 0.8130 0.0532  0.0187  -0.0186 247 ARG A CG  
1557  C CD  . ARG A 247 ? 0.7758 0.5844 0.7843 0.0658  0.0117  -0.0151 247 ARG A CD  
1558  N NE  . ARG A 247 ? 0.7529 0.5817 0.7762 0.0649  0.0027  -0.0187 247 ARG A NE  
1559  C CZ  . ARG A 247 ? 0.7477 0.5876 0.7649 0.0702  -0.0006 -0.0205 247 ARG A CZ  
1560  N NH1 . ARG A 247 ? 0.7616 0.6038 0.7602 0.0800  0.0007  -0.0200 247 ARG A NH1 
1561  N NH2 . ARG A 247 ? 0.7350 0.5845 0.7634 0.0663  -0.0041 -0.0243 247 ARG A NH2 
1562  N N   . ASN A 248 ? 0.7847 0.5954 0.8483 0.0175  0.0612  -0.0339 248 ASN A N   
1563  C CA  . ASN A 248 ? 0.8117 0.6134 0.8719 0.0102  0.0799  -0.0344 248 ASN A CA  
1564  C C   . ASN A 248 ? 0.8352 0.6237 0.8998 -0.0107 0.0980  -0.0437 248 ASN A C   
1565  O O   . ASN A 248 ? 0.8300 0.6125 0.8959 -0.0175 0.0957  -0.0489 248 ASN A O   
1566  C CB  . ASN A 248 ? 0.8125 0.6475 0.8978 0.0111  0.0758  -0.0401 248 ASN A CB  
1567  C CG  . ASN A 248 ? 0.8035 0.6354 0.8735 0.0262  0.0726  -0.0314 248 ASN A CG  
1568  O OD1 . ASN A 248 ? 0.8234 0.6357 0.8709 0.0293  0.0854  -0.0251 248 ASN A OD1 
1569  N ND2 . ASN A 248 ? 0.7768 0.6269 0.8567 0.0356  0.0570  -0.0321 248 ASN A ND2 
1570  N N   . ASN A 249 ? 0.8520 0.6351 0.9182 -0.0225 0.1182  -0.0475 249 ASN A N   
1571  C CA  . ASN A 249 ? 0.8727 0.6437 0.9449 -0.0478 0.1407  -0.0601 249 ASN A CA  
1572  C C   . ASN A 249 ? 0.8791 0.7013 0.9951 -0.0634 0.1417  -0.0796 249 ASN A C   
1573  O O   . ASN A 249 ? 0.8983 0.7177 1.0208 -0.0840 0.1655  -0.0900 249 ASN A O   
1574  C CB  . ASN A 249 ? 0.9021 0.6183 0.9346 -0.0508 0.1699  -0.0496 249 ASN A CB  
1575  C CG  . ASN A 249 ? 0.9043 0.5677 0.8916 -0.0371 0.1738  -0.0347 249 ASN A CG  
1576  O OD1 . ASN A 249 ? 0.9093 0.5444 0.8876 -0.0503 0.1857  -0.0402 249 ASN A OD1 
1577  N ND2 . ASN A 249 ? 0.9023 0.5544 0.8607 -0.0098 0.1644  -0.0176 249 ASN A ND2 
1578  N N   . LEU A 250 ? 0.8205 0.6899 0.9647 -0.0522 0.1170  -0.0851 250 LEU A N   
1579  C CA  . LEU A 250 ? 0.8302 0.7550 1.0144 -0.0592 0.1142  -0.1035 250 LEU A CA  
1580  C C   . LEU A 250 ? 0.8244 0.7752 1.0343 -0.0831 0.1214  -0.1274 250 LEU A C   
1581  O O   . LEU A 250 ? 0.8109 0.7545 1.0170 -0.0857 0.1140  -0.1304 250 LEU A O   
1582  C CB  . LEU A 250 ? 0.8235 0.7831 1.0217 -0.0354 0.0871  -0.1006 250 LEU A CB  
1583  C CG  . LEU A 250 ? 0.8332 0.8019 1.0322 -0.0206 0.0850  -0.0936 250 LEU A CG  
1584  C CD1 . LEU A 250 ? 0.8269 0.7495 0.9916 -0.0166 0.0960  -0.0762 250 LEU A CD1 
1585  C CD2 . LEU A 250 ? 0.8151 0.8030 1.0191 0.0028  0.0617  -0.0893 250 LEU A CD2 
1586  N N   . THR A 251 ? 0.8266 0.8121 1.0644 -0.1016 0.1363  -0.1470 251 THR A N   
1587  C CA  . THR A 251 ? 0.8075 0.8311 1.0767 -0.1280 0.1450  -0.1767 251 THR A CA  
1588  C C   . THR A 251 ? 0.7878 0.8945 1.1014 -0.1202 0.1287  -0.1973 251 THR A C   
1589  O O   . THR A 251 ? 0.7943 0.9189 1.1101 -0.0947 0.1137  -0.1866 251 THR A O   
1590  C CB  . THR A 251 ? 0.8147 0.8074 1.0775 -0.1619 0.1831  -0.1869 251 THR A CB  
1591  O OG1 . THR A 251 ? 0.8202 0.8394 1.0992 -0.1654 0.1947  -0.1922 251 THR A OG1 
1592  C CG2 . THR A 251 ? 0.8379 0.7427 1.0471 -0.1596 0.2000  -0.1612 251 THR A CG2 
1593  N N   . GLY A 252 ? 0.7654 0.9243 1.1132 -0.1412 0.1322  -0.2289 252 GLY A N   
1594  C CA  . GLY A 252 ? 0.7326 0.9788 1.1230 -0.1325 0.1184  -0.2525 252 GLY A CA  
1595  C C   . GLY A 252 ? 0.7169 1.0015 1.1130 -0.0999 0.0839  -0.2508 252 GLY A C   
1596  O O   . GLY A 252 ? 0.7318 0.9793 1.1028 -0.0885 0.0711  -0.2344 252 GLY A O   
1597  N N   . LYS A 253 ? 0.7272 1.0881 1.1547 -0.0827 0.0700  -0.2684 253 LYS A N   
1598  C CA  . LYS A 253 ? 0.7044 1.1091 1.1363 -0.0481 0.0394  -0.2697 253 LYS A CA  
1599  C C   . LYS A 253 ? 0.7226 1.0918 1.1249 -0.0094 0.0240  -0.2373 253 LYS A C   
1600  O O   . LYS A 253 ? 0.7414 1.0779 1.1320 -0.0071 0.0343  -0.2216 253 LYS A O   
1601  C CB  . LYS A 253 ? 0.6520 1.1593 1.1282 -0.0426 0.0317  -0.3052 253 LYS A CB  
1602  C CG  . LYS A 253 ? 0.6223 1.1794 1.1328 -0.0813 0.0447  -0.3447 253 LYS A CG  
1603  C CD  . LYS A 253 ? 0.5662 1.2333 1.1142 -0.0632 0.0242  -0.3790 253 LYS A CD  
1604  C CE  . LYS A 253 ? 0.5404 1.2660 1.1087 -0.0378 0.0192  -0.3854 253 LYS A CE  
1605  N NZ  . LYS A 253 ? 0.4971 1.3364 1.0991 -0.0120 -0.0027 -0.4186 253 LYS A NZ  
1606  N N   . ILE A 254 ? 0.7474 1.1211 1.1356 0.0201  0.0010  -0.2283 254 ILE A N   
1607  C CA  . ILE A 254 ? 0.7506 1.0991 1.1130 0.0581  -0.0121 -0.2030 254 ILE A CA  
1608  C C   . ILE A 254 ? 0.7181 1.1279 1.1017 0.0819  -0.0175 -0.2162 254 ILE A C   
1609  O O   . ILE A 254 ? 0.6822 1.1679 1.0930 0.0904  -0.0275 -0.2422 254 ILE A O   
1610  C CB  . ILE A 254 ? 0.7478 1.0813 1.0858 0.0824  -0.0316 -0.1905 254 ILE A CB  
1611  C CG1 . ILE A 254 ? 0.7799 1.0528 1.0961 0.0610  -0.0260 -0.1768 254 ILE A CG1 
1612  C CG2 . ILE A 254 ? 0.7443 1.0495 1.0538 0.1202  -0.0408 -0.1671 254 ILE A CG2 
1613  C CD1 . ILE A 254 ? 0.7752 1.0364 1.0694 0.0808  -0.0431 -0.1670 254 ILE A CD1 
1614  N N   . PRO A 255 ? 0.7636 1.1483 1.1366 0.0940  -0.0111 -0.2017 255 PRO A N   
1615  C CA  . PRO A 255 ? 0.7344 1.1770 1.1269 0.1181  -0.0148 -0.2149 255 PRO A CA  
1616  C C   . PRO A 255 ? 0.7093 1.1843 1.0912 0.1638  -0.0371 -0.2143 255 PRO A C   
1617  O O   . PRO A 255 ? 0.7230 1.1453 1.0676 0.1866  -0.0454 -0.1900 255 PRO A O   
1618  C CB  . PRO A 255 ? 0.7561 1.1458 1.1289 0.1226  -0.0033 -0.1941 255 PRO A CB  
1619  C CG  . PRO A 255 ? 0.7921 1.1168 1.1487 0.0894  0.0111  -0.1799 255 PRO A CG  
1620  C CD  . PRO A 255 ? 0.7981 1.1060 1.1430 0.0845  0.0011  -0.1761 255 PRO A CD  
1621  N N   . SER A 256 ? 0.7404 1.3046 1.1540 0.1779  -0.0454 -0.2426 256 SER A N   
1622  C CA  . SER A 256 ? 0.7153 1.3190 1.1166 0.2281  -0.0666 -0.2438 256 SER A CA  
1623  C C   . SER A 256 ? 0.7266 1.2885 1.0938 0.2695  -0.0676 -0.2195 256 SER A C   
1624  O O   . SER A 256 ? 0.7215 1.2789 1.0586 0.3143  -0.0815 -0.2084 256 SER A O   
1625  C CB  . SER A 256 ? 0.6663 1.3859 1.1122 0.2350  -0.0748 -0.2836 256 SER A CB  
1626  O OG  . SER A 256 ? 0.6540 1.4099 1.1311 0.2209  -0.0606 -0.2997 256 SER A OG  
1627  N N   . SER A 257 ? 0.7486 1.2768 1.1166 0.2562  -0.0516 -0.2114 257 SER A N   
1628  C CA  . SER A 257 ? 0.7622 1.2430 1.0972 0.2902  -0.0490 -0.1898 257 SER A CA  
1629  C C   . SER A 257 ? 0.7908 1.1795 1.0765 0.2996  -0.0491 -0.1583 257 SER A C   
1630  O O   . SER A 257 ? 0.8017 1.1459 1.0536 0.3311  -0.0466 -0.1409 257 SER A O   
1631  C CB  . SER A 257 ? 0.7743 1.2396 1.1225 0.2679  -0.0307 -0.1902 257 SER A CB  
1632  O OG  . SER A 257 ? 0.8026 1.2088 1.1451 0.2257  -0.0177 -0.1784 257 SER A OG  
1633  N N   . PHE A 258 ? 0.7592 1.1176 1.0396 0.2721  -0.0500 -0.1520 258 PHE A N   
1634  C CA  . PHE A 258 ? 0.7805 1.0580 1.0177 0.2772  -0.0490 -0.1251 258 PHE A CA  
1635  C C   . PHE A 258 ? 0.7754 1.0443 0.9774 0.3253  -0.0600 -0.1145 258 PHE A C   
1636  O O   . PHE A 258 ? 0.7934 0.9898 0.9543 0.3350  -0.0549 -0.0917 258 PHE A O   
1637  C CB  . PHE A 258 ? 0.7899 1.0493 1.0314 0.2415  -0.0494 -0.1239 258 PHE A CB  
1638  C CG  . PHE A 258 ? 0.8101 1.0277 1.0560 0.2026  -0.0341 -0.1178 258 PHE A CG  
1639  C CD1 . PHE A 258 ? 0.8141 1.0398 1.0763 0.1915  -0.0220 -0.1236 258 PHE A CD1 
1640  C CD2 . PHE A 258 ? 0.8240 0.9960 1.0553 0.1801  -0.0319 -0.1065 258 PHE A CD2 
1641  C CE1 . PHE A 258 ? 0.8333 1.0211 1.0943 0.1603  -0.0082 -0.1172 258 PHE A CE1 
1642  C CE2 . PHE A 258 ? 0.8403 0.9769 1.0713 0.1504  -0.0188 -0.1008 258 PHE A CE2 
1643  C CZ  . PHE A 258 ? 0.8459 0.9897 1.0903 0.1413  -0.0070 -0.1057 258 PHE A CZ  
1644  N N   . GLY A 259 ? 0.8202 1.1620 1.0354 0.3564  -0.0737 -0.1314 259 GLY A N   
1645  C CA  . GLY A 259 ? 0.8181 1.1532 0.9941 0.4100  -0.0833 -0.1206 259 GLY A CA  
1646  C C   . GLY A 259 ? 0.8357 1.1165 0.9741 0.4443  -0.0726 -0.1025 259 GLY A C   
1647  O O   . GLY A 259 ? 0.8815 1.1325 0.9745 0.4895  -0.0753 -0.0877 259 GLY A O   
1648  N N   . ASN A 260 ? 0.9014 1.1662 1.0542 0.4253  -0.0591 -0.1037 260 ASN A N   
1649  C CA  . ASN A 260 ? 0.9211 1.1286 1.0378 0.4539  -0.0465 -0.0882 260 ASN A CA  
1650  C C   . ASN A 260 ? 0.9519 1.0554 1.0279 0.4381  -0.0309 -0.0639 260 ASN A C   
1651  O O   . ASN A 260 ? 0.9732 1.0155 1.0071 0.4658  -0.0189 -0.0490 260 ASN A O   
1652  C CB  . ASN A 260 ? 0.9150 1.1531 1.0640 0.4417  -0.0384 -0.1019 260 ASN A CB  
1653  C CG  . ASN A 260 ? 0.8810 1.2249 1.0695 0.4603  -0.0510 -0.1285 260 ASN A CG  
1654  O OD1 . ASN A 260 ? 0.8668 1.2484 1.0409 0.5084  -0.0634 -0.1321 260 ASN A OD1 
1655  N ND2 . ASN A 260 ? 0.8669 1.2615 1.1042 0.4231  -0.0468 -0.1484 260 ASN A ND2 
1656  N N   . LEU A 261 ? 0.9348 1.0172 1.0212 0.3951  -0.0295 -0.0609 261 LEU A N   
1657  C CA  . LEU A 261 ? 0.9564 0.9525 1.0125 0.3741  -0.0142 -0.0432 261 LEU A CA  
1658  C C   . LEU A 261 ? 0.9705 0.9146 0.9766 0.4028  -0.0127 -0.0257 261 LEU A C   
1659  O O   . LEU A 261 ? 0.9694 0.9022 0.9686 0.3895  -0.0173 -0.0203 261 LEU A O   
1660  C CB  . LEU A 261 ? 0.9517 0.9495 1.0342 0.3240  -0.0142 -0.0470 261 LEU A CB  
1661  C CG  . LEU A 261 ? 0.9460 0.9817 1.0694 0.2944  -0.0111 -0.0614 261 LEU A CG  
1662  C CD1 . LEU A 261 ? 0.9362 1.0187 1.0934 0.2656  -0.0200 -0.0733 261 LEU A CD1 
1663  C CD2 . LEU A 261 ? 0.9580 0.9400 1.0715 0.2697  0.0043  -0.0543 261 LEU A CD2 
1664  N N   . LYS A 262 ? 1.0907 0.9994 1.0581 0.4446  -0.0041 -0.0163 262 LYS A N   
1665  C CA  . LYS A 262 ? 1.1119 0.9638 1.0226 0.4792  0.0016  0.0021  262 LYS A CA  
1666  C C   . LYS A 262 ? 1.1376 0.8948 1.0132 0.4544  0.0237  0.0173  262 LYS A C   
1667  O O   . LYS A 262 ? 1.1590 0.8613 0.9863 0.4738  0.0324  0.0330  262 LYS A O   
1668  C CB  . LYS A 262 ? 1.1237 0.9706 1.0016 0.5258  0.0053  0.0069  262 LYS A CB  
1669  C CG  . LYS A 262 ? 1.1264 1.0257 0.9907 0.5592  -0.0124 0.0061  262 LYS A CG  
1670  C CD  . LYS A 262 ? 1.0803 1.0928 1.0040 0.5615  -0.0361 -0.0192 262 LYS A CD  
1671  C CE  . LYS A 262 ? 1.0863 1.1557 0.9947 0.5941  -0.0536 -0.0238 262 LYS A CE  
1672  N NZ  . LYS A 262 ? 1.0443 1.2293 1.0105 0.5943  -0.0739 -0.0533 262 LYS A NZ  
1673  N N   . ASN A 263 ? 1.1633 0.9032 1.0609 0.4116  0.0340  0.0116  263 ASN A N   
1674  C CA  . ASN A 263 ? 1.1815 0.8446 1.0533 0.3835  0.0548  0.0198  263 ASN A CA  
1675  C C   . ASN A 263 ? 1.1632 0.8430 1.0629 0.3383  0.0484  0.0153  263 ASN A C   
1676  O O   . ASN A 263 ? 1.1738 0.8001 1.0538 0.3151  0.0635  0.0201  263 ASN A O   
1677  C CB  . ASN A 263 ? 1.1933 0.8223 1.0643 0.3707  0.0729  0.0147  263 ASN A CB  
1678  C CG  . ASN A 263 ? 1.2297 0.7806 1.0447 0.4027  0.0959  0.0258  263 ASN A CG  
1679  O OD1 . ASN A 263 ? 1.2486 0.7508 1.0216 0.4095  0.1059  0.0390  263 ASN A OD1 
1680  N ND2 . ASN A 263 ? 1.2384 0.7834 1.0538 0.4141  0.1043  0.0201  263 ASN A ND2 
1681  N N   . VAL A 264 ? 1.0190 0.7707 0.9627 0.3251  0.0282  0.0046  264 VAL A N   
1682  C CA  . VAL A 264 ? 1.0040 0.7698 0.9718 0.2854  0.0228  0.0004  264 VAL A CA  
1683  C C   . VAL A 264 ? 1.0076 0.7521 0.9513 0.2890  0.0204  0.0101  264 VAL A C   
1684  O O   . VAL A 264 ? 1.0080 0.7749 0.9420 0.3178  0.0089  0.0133  264 VAL A O   
1685  C CB  . VAL A 264 ? 0.9841 0.8238 0.9998 0.2715  0.0062  -0.0136 264 VAL A CB  
1686  C CG1 . VAL A 264 ? 0.9727 0.8253 1.0037 0.2421  -0.0014 -0.0153 264 VAL A CG1 
1687  C CG2 . VAL A 264 ? 0.9826 0.8339 1.0213 0.2556  0.0129  -0.0224 264 VAL A CG2 
1688  N N   . THR A 265 ? 0.9514 0.6565 0.8850 0.2608  0.0312  0.0135  265 THR A N   
1689  C CA  . THR A 265 ? 0.9550 0.6415 0.8687 0.2586  0.0303  0.0214  265 THR A CA  
1690  C C   . THR A 265 ? 0.9330 0.6579 0.8783 0.2289  0.0174  0.0141  265 THR A C   
1691  O O   . THR A 265 ? 0.9321 0.6633 0.8698 0.2325  0.0097  0.0181  265 THR A O   
1692  C CB  . THR A 265 ? 0.9839 0.5968 0.8596 0.2490  0.0549  0.0291  265 THR A CB  
1693  O OG1 . THR A 265 ? 0.9683 0.5758 0.8630 0.2136  0.0640  0.0189  265 THR A OG1 
1694  C CG2 . THR A 265 ? 1.0480 0.6099 0.8824 0.2818  0.0712  0.0384  265 THR A CG2 
1695  N N   . LEU A 266 ? 0.8486 0.5965 0.8252 0.2024  0.0159  0.0043  266 LEU A N   
1696  C CA  . LEU A 266 ? 0.8311 0.6071 0.8319 0.1765  0.0066  -0.0016 266 LEU A CA  
1697  C C   . LEU A 266 ? 0.8214 0.6463 0.8574 0.1702  -0.0032 -0.0118 266 LEU A C   
1698  O O   . LEU A 266 ? 0.8237 0.6517 0.8694 0.1683  0.0026  -0.0160 266 LEU A O   
1699  C CB  . LEU A 266 ? 0.8264 0.5761 0.8235 0.1495  0.0183  -0.0035 266 LEU A CB  
1700  C CG  . LEU A 266 ? 0.8077 0.5847 0.8270 0.1262  0.0107  -0.0097 266 LEU A CG  
1701  C CD1 . LEU A 266 ? 0.8013 0.5905 0.8197 0.1267  0.0001  -0.0069 266 LEU A CD1 
1702  C CD2 . LEU A 266 ? 0.8050 0.5639 0.8196 0.1056  0.0220  -0.0142 266 LEU A CD2 
1703  N N   . LEU A 267 ? 0.7352 0.5960 0.7890 0.1656  -0.0159 -0.0168 267 LEU A N   
1704  C CA  . LEU A 267 ? 0.7078 0.6115 0.7938 0.1547  -0.0214 -0.0282 267 LEU A CA  
1705  C C   . LEU A 267 ? 0.6956 0.6067 0.7916 0.1323  -0.0251 -0.0314 267 LEU A C   
1706  O O   . LEU A 267 ? 0.6991 0.6283 0.7983 0.1343  -0.0344 -0.0346 267 LEU A O   
1707  C CB  . LEU A 267 ? 0.7128 0.6605 0.8126 0.1752  -0.0312 -0.0365 267 LEU A CB  
1708  C CG  . LEU A 267 ? 0.7148 0.7098 0.8501 0.1602  -0.0334 -0.0521 267 LEU A CG  
1709  C CD1 . LEU A 267 ? 0.7170 0.7029 0.8607 0.1486  -0.0217 -0.0530 267 LEU A CD1 
1710  C CD2 . LEU A 267 ? 0.7142 0.7633 0.8659 0.1806  -0.0436 -0.0649 267 LEU A CD2 
1711  N N   . ASN A 268 ? 0.7589 0.6558 0.8570 0.1132  -0.0177 -0.0309 268 ASN A N   
1712  C CA  . ASN A 268 ? 0.7514 0.6497 0.8538 0.0954  -0.0188 -0.0327 268 ASN A CA  
1713  C C   . ASN A 268 ? 0.7667 0.6861 0.8894 0.0835  -0.0148 -0.0412 268 ASN A C   
1714  O O   . ASN A 268 ? 0.7664 0.6815 0.8916 0.0793  -0.0064 -0.0412 268 ASN A O   
1715  C CB  . ASN A 268 ? 0.7314 0.6021 0.8178 0.0864  -0.0128 -0.0270 268 ASN A CB  
1716  C CG  . ASN A 268 ? 0.7252 0.5779 0.7935 0.0902  -0.0152 -0.0215 268 ASN A CG  
1717  O OD1 . ASN A 268 ? 0.7329 0.5913 0.7983 0.0989  -0.0223 -0.0202 268 ASN A OD1 
1718  N ND2 . ASN A 268 ? 0.7176 0.5520 0.7739 0.0831  -0.0085 -0.0200 268 ASN A ND2 
1719  N N   . MET A 269 ? 0.7180 0.6590 0.8539 0.0768  -0.0188 -0.0496 269 MET A N   
1720  C CA  . MET A 269 ? 0.7442 0.6989 0.8968 0.0605  -0.0103 -0.0591 269 MET A CA  
1721  C C   . MET A 269 ? 0.7554 0.7037 0.9061 0.0460  -0.0090 -0.0633 269 MET A C   
1722  O O   . MET A 269 ? 0.7827 0.7446 0.9483 0.0309  -0.0012 -0.0752 269 MET A O   
1723  C CB  . MET A 269 ? 0.7691 0.7661 0.9468 0.0645  -0.0118 -0.0728 269 MET A CB  
1724  C CG  . MET A 269 ? 0.7595 0.7595 0.9402 0.0742  -0.0070 -0.0705 269 MET A CG  
1725  S SD  . MET A 269 ? 0.7703 0.8279 0.9823 0.0811  -0.0082 -0.0886 269 MET A SD  
1726  C CE  . MET A 269 ? 0.7644 0.8596 0.9854 0.0903  -0.0239 -0.0999 269 MET A CE  
1727  N N   . PHE A 270 ? 0.7976 0.7243 0.9299 0.0492  -0.0145 -0.0551 270 PHE A N   
1728  C CA  . PHE A 270 ? 0.8026 0.7202 0.9299 0.0387  -0.0137 -0.0587 270 PHE A CA  
1729  C C   . PHE A 270 ? 0.7996 0.6895 0.9158 0.0262  0.0012  -0.0560 270 PHE A C   
1730  O O   . PHE A 270 ? 0.7931 0.6713 0.9027 0.0277  0.0088  -0.0495 270 PHE A O   
1731  C CB  . PHE A 270 ? 0.7786 0.6821 0.8880 0.0479  -0.0231 -0.0504 270 PHE A CB  
1732  C CG  . PHE A 270 ? 0.7449 0.6253 0.8362 0.0540  -0.0210 -0.0381 270 PHE A CG  
1733  C CD1 . PHE A 270 ? 0.7341 0.5932 0.8102 0.0496  -0.0144 -0.0335 270 PHE A CD1 
1734  C CD2 . PHE A 270 ? 0.7311 0.6116 0.8186 0.0648  -0.0245 -0.0329 270 PHE A CD2 
1735  C CE1 . PHE A 270 ? 0.7139 0.5630 0.7765 0.0552  -0.0135 -0.0268 270 PHE A CE1 
1736  C CE2 . PHE A 270 ? 0.7099 0.5735 0.7835 0.0661  -0.0208 -0.0265 270 PHE A CE2 
1737  C CZ  . PHE A 270 ? 0.7024 0.5557 0.7661 0.0609  -0.0164 -0.0249 270 PHE A CZ  
1738  N N   . GLU A 271 ? 0.8375 0.7143 0.9482 0.0154  0.0065  -0.0611 271 GLU A N   
1739  C CA  . GLU A 271 ? 0.8435 0.6846 0.9352 0.0066  0.0234  -0.0574 271 GLU A CA  
1740  C C   . GLU A 271 ? 0.8613 0.7029 0.9611 -0.0035 0.0391  -0.0610 271 GLU A C   
1741  O O   . GLU A 271 ? 0.8605 0.6819 0.9435 0.0021  0.0473  -0.0505 271 GLU A O   
1742  C CB  . GLU A 271 ? 0.8247 0.6391 0.8878 0.0208  0.0216  -0.0419 271 GLU A CB  
1743  C CG  . GLU A 271 ? 0.8180 0.6187 0.8654 0.0257  0.0153  -0.0396 271 GLU A CG  
1744  C CD  . GLU A 271 ? 0.8060 0.5901 0.8277 0.0409  0.0136  -0.0277 271 GLU A CD  
1745  O OE1 . GLU A 271 ? 0.8221 0.5798 0.8210 0.0451  0.0258  -0.0218 271 GLU A OE1 
1746  O OE2 . GLU A 271 ? 0.7807 0.5795 0.8034 0.0495  0.0012  -0.0251 271 GLU A OE2 
1747  N N   . ASN A 272 ? 0.8198 0.6899 0.9464 -0.0181 0.0431  -0.0780 272 ASN A N   
1748  C CA  . ASN A 272 ? 0.8379 0.7152 0.9772 -0.0314 0.0598  -0.0857 272 ASN A CA  
1749  C C   . ASN A 272 ? 0.8489 0.7330 1.0032 -0.0569 0.0743  -0.1063 272 ASN A C   
1750  O O   . ASN A 272 ? 0.8438 0.7196 0.9937 -0.0629 0.0722  -0.1126 272 ASN A O   
1751  C CB  . ASN A 272 ? 0.8440 0.7648 1.0082 -0.0216 0.0490  -0.0895 272 ASN A CB  
1752  C CG  . ASN A 272 ? 0.8361 0.7404 0.9850 -0.0077 0.0497  -0.0736 272 ASN A CG  
1753  O OD1 . ASN A 272 ? 0.8465 0.7312 0.9851 -0.0140 0.0662  -0.0700 272 ASN A OD1 
1754  N ND2 . ASN A 272 ? 0.8164 0.7274 0.9619 0.0108  0.0333  -0.0652 272 ASN A ND2 
1755  N N   . GLN A 273 ? 0.8709 0.7717 1.0438 -0.0738 0.0906  -0.1193 273 GLN A N   
1756  C CA  . GLN A 273 ? 0.8719 0.7889 1.0657 -0.1030 0.1070  -0.1450 273 GLN A CA  
1757  C C   . GLN A 273 ? 0.8657 0.8582 1.1047 -0.1068 0.0975  -0.1682 273 GLN A C   
1758  O O   . GLN A 273 ? 0.8608 0.8777 1.1233 -0.1326 0.1158  -0.1914 273 GLN A O   
1759  C CB  . GLN A 273 ? 0.8874 0.7553 1.0612 -0.1245 0.1414  -0.1442 273 GLN A CB  
1760  C CG  . GLN A 273 ? 0.8973 0.6914 1.0203 -0.1123 0.1508  -0.1188 273 GLN A CG  
1761  C CD  . GLN A 273 ? 0.9202 0.6561 1.0160 -0.1342 0.1884  -0.1202 273 GLN A CD  
1762  O OE1 . GLN A 273 ? 0.9219 0.6502 1.0256 -0.1619 0.2066  -0.1406 273 GLN A OE1 
1763  N NE2 . GLN A 273 ? 0.9397 0.6327 1.0008 -0.1219 0.2022  -0.0995 273 GLN A NE2 
1764  N N   . LEU A 274 ? 0.7953 0.8247 1.0445 -0.0803 0.0705  -0.1627 274 LEU A N   
1765  C CA  . LEU A 274 ? 0.7863 0.8893 1.0729 -0.0747 0.0582  -0.1831 274 LEU A CA  
1766  C C   . LEU A 274 ? 0.7605 0.9070 1.0737 -0.0955 0.0596  -0.2144 274 LEU A C   
1767  O O   . LEU A 274 ? 0.7566 0.8829 1.0576 -0.1010 0.0567  -0.2158 274 LEU A O   
1768  C CB  . LEU A 274 ? 0.7929 0.9131 1.0742 -0.0392 0.0307  -0.1690 274 LEU A CB  
1769  C CG  . LEU A 274 ? 0.8094 0.9251 1.0842 -0.0175 0.0265  -0.1524 274 LEU A CG  
1770  C CD1 . LEU A 274 ? 0.8264 0.8876 1.0784 -0.0267 0.0446  -0.1356 274 LEU A CD1 
1771  C CD2 . LEU A 274 ? 0.8074 0.9153 1.0643 0.0130  0.0053  -0.1354 274 LEU A CD2 
1772  N N   . SER A 275 ? 0.7523 0.9628 1.1031 -0.1073 0.0643  -0.2421 275 SER A N   
1773  C CA  . SER A 275 ? 0.7197 0.9831 1.1017 -0.1317 0.0684  -0.2790 275 SER A CA  
1774  C C   . SER A 275 ? 0.6840 1.0429 1.1025 -0.1118 0.0466  -0.3010 275 SER A C   
1775  O O   . SER A 275 ? 0.6866 1.0605 1.1014 -0.0782 0.0300  -0.2849 275 SER A O   
1776  C CB  . SER A 275 ? 0.7162 0.9646 1.1091 -0.1756 0.1046  -0.2992 275 SER A CB  
1777  O OG  . SER A 275 ? 0.7163 0.9841 1.1239 -0.1777 0.1162  -0.3005 275 SER A OG  
1778  N N   . GLY A 276 ? 0.7602 1.1846 1.2123 -0.1316 0.0475  -0.3395 276 GLY A N   
1779  C CA  . GLY A 276 ? 0.7167 1.2412 1.2027 -0.1093 0.0253  -0.3642 276 GLY A CA  
1780  C C   . GLY A 276 ? 0.7122 1.2516 1.1816 -0.0710 -0.0064 -0.3535 276 GLY A C   
1781  O O   . GLY A 276 ? 0.7298 1.2256 1.1761 -0.0750 -0.0095 -0.3438 276 GLY A O   
1782  N N   . GLU A 277 ? 0.7754 1.3756 1.2538 -0.0316 -0.0288 -0.3551 277 GLU A N   
1783  C CA  . GLU A 277 ? 0.7657 1.3860 1.2260 0.0095  -0.0575 -0.3463 277 GLU A CA  
1784  C C   . GLU A 277 ? 0.7857 1.3670 1.2134 0.0528  -0.0691 -0.3086 277 GLU A C   
1785  O O   . GLU A 277 ? 0.7909 1.3639 1.2224 0.0565  -0.0603 -0.2999 277 GLU A O   
1786  C CB  . GLU A 277 ? 0.7086 1.4436 1.2041 0.0233  -0.0744 -0.3865 277 GLU A CB  
1787  C CG  . GLU A 277 ? 0.6753 1.4709 1.2184 -0.0246 -0.0560 -0.4336 277 GLU A CG  
1788  C CD  . GLU A 277 ? 0.6196 1.5247 1.1939 -0.0171 -0.0741 -0.4772 277 GLU A CD  
1789  O OE1 . GLU A 277 ? 0.6014 1.5439 1.1604 0.0329  -0.1025 -0.4698 277 GLU A OE1 
1790  O OE2 . GLU A 277 ? 0.5939 1.5476 1.2061 -0.0610 -0.0586 -0.5202 277 GLU A OE2 
1791  N N   . ILE A 278 ? 0.7606 1.3150 1.1547 0.0838  -0.0867 -0.2871 278 ILE A N   
1792  C CA  . ILE A 278 ? 0.7745 1.2875 1.1338 0.1240  -0.0952 -0.2532 278 ILE A CA  
1793  C C   . ILE A 278 ? 0.7372 1.3230 1.1098 0.1616  -0.1081 -0.2662 278 ILE A C   
1794  O O   . ILE A 278 ? 0.7042 1.3593 1.0851 0.1845  -0.1255 -0.2863 278 ILE A O   
1795  C CB  . ILE A 278 ? 0.7900 1.2568 1.1090 0.1456  -0.1074 -0.2295 278 ILE A CB  
1796  C CG1 . ILE A 278 ? 0.8242 1.2270 1.1319 0.1104  -0.0955 -0.2197 278 ILE A CG1 
1797  C CG2 . ILE A 278 ? 0.8005 1.2180 1.0822 0.1821  -0.1107 -0.1965 278 ILE A CG2 
1798  C CD1 . ILE A 278 ? 0.8326 1.2070 1.1093 0.1252  -0.1071 -0.2057 278 ILE A CD1 
1799  N N   . PRO A 279 ? 0.7748 1.3503 1.1482 0.1715  -0.1004 -0.2563 279 PRO A N   
1800  C CA  . PRO A 279 ? 0.7402 1.3850 1.1249 0.2105  -0.1116 -0.2688 279 PRO A CA  
1801  C C   . PRO A 279 ? 0.7346 1.3758 1.0801 0.2652  -0.1312 -0.2517 279 PRO A C   
1802  O O   . PRO A 279 ? 0.7647 1.3232 1.0662 0.2802  -0.1289 -0.2172 279 PRO A O   
1803  C CB  . PRO A 279 ? 0.7575 1.3627 1.1390 0.2088  -0.0967 -0.2526 279 PRO A CB  
1804  C CG  . PRO A 279 ? 0.8017 1.3085 1.1568 0.1825  -0.0828 -0.2240 279 PRO A CG  
1805  C CD  . PRO A 279 ? 0.8103 1.3114 1.1728 0.1492  -0.0812 -0.2339 279 PRO A CD  
1806  N N   . PRO A 280 ? 0.7948 1.5255 1.1531 0.2973  -0.1491 -0.2761 280 PRO A N   
1807  C CA  . PRO A 280 ? 0.7921 1.5184 1.1060 0.3558  -0.1666 -0.2588 280 PRO A CA  
1808  C C   . PRO A 280 ? 0.8125 1.4798 1.0858 0.3956  -0.1619 -0.2270 280 PRO A C   
1809  O O   . PRO A 280 ? 0.8263 1.4521 1.0494 0.4379  -0.1684 -0.2027 280 PRO A O   
1810  C CB  . PRO A 280 ? 0.7401 1.5910 1.0835 0.3822  -0.1857 -0.2977 280 PRO A CB  
1811  C CG  . PRO A 280 ? 0.7175 1.6271 1.1193 0.3251  -0.1779 -0.3364 280 PRO A CG  
1812  C CD  . PRO A 280 ? 0.7491 1.5908 1.1616 0.2803  -0.1533 -0.3229 280 PRO A CD  
1813  N N   . GLU A 281 ? 0.8323 1.4922 1.1235 0.3835  -0.1487 -0.2271 281 GLU A N   
1814  C CA  . GLU A 281 ? 0.8522 1.4542 1.1066 0.4178  -0.1416 -0.1998 281 GLU A CA  
1815  C C   . GLU A 281 ? 0.8946 1.3793 1.1039 0.4076  -0.1290 -0.1626 281 GLU A C   
1816  O O   . GLU A 281 ? 0.9132 1.3395 1.0814 0.4394  -0.1225 -0.1385 281 GLU A O   
1817  C CB  . GLU A 281 ? 0.8451 1.4711 1.1336 0.4014  -0.1295 -0.2120 281 GLU A CB  
1818  C CG  . GLU A 281 ? 0.7978 1.5459 1.1419 0.3982  -0.1369 -0.2546 281 GLU A CG  
1819  C CD  . GLU A 281 ? 0.7824 1.5758 1.1729 0.3427  -0.1340 -0.2838 281 GLU A CD  
1820  O OE1 . GLU A 281 ? 0.8029 1.5443 1.1790 0.3176  -0.1322 -0.2720 281 GLU A OE1 
1821  O OE2 . GLU A 281 ? 0.7497 1.6294 1.1902 0.3235  -0.1315 -0.3197 281 GLU A OE2 
1822  N N   . ILE A 282 ? 0.8647 1.3147 1.0798 0.3647  -0.1242 -0.1591 282 ILE A N   
1823  C CA  . ILE A 282 ? 0.8975 1.2473 1.0730 0.3544  -0.1133 -0.1279 282 ILE A CA  
1824  C C   . ILE A 282 ? 0.9057 1.2193 1.0279 0.4004  -0.1194 -0.1070 282 ILE A C   
1825  O O   . ILE A 282 ? 0.9304 1.1603 1.0120 0.4064  -0.1069 -0.0804 282 ILE A O   
1826  C CB  . ILE A 282 ? 0.9075 1.2412 1.1002 0.3056  -0.1098 -0.1318 282 ILE A CB  
1827  C CG1 . ILE A 282 ? 0.9191 1.2353 1.1388 0.2630  -0.0940 -0.1353 282 ILE A CG1 
1828  C CG2 . ILE A 282 ? 0.9286 1.1875 1.0794 0.3064  -0.1071 -0.1063 282 ILE A CG2 
1829  C CD1 . ILE A 282 ? 0.9374 1.2196 1.1622 0.2209  -0.0872 -0.1331 282 ILE A CD1 
1830  N N   . GLY A 283 ? 0.9627 1.3391 1.0822 0.4345  -0.1369 -0.1200 283 GLY A N   
1831  C CA  . GLY A 283 ? 0.9737 1.3177 1.0368 0.4851  -0.1417 -0.0999 283 GLY A CA  
1832  C C   . GLY A 283 ? 0.9911 1.2852 1.0128 0.5267  -0.1311 -0.0792 283 GLY A C   
1833  O O   . GLY A 283 ? 1.0184 1.2473 0.9798 0.5521  -0.1238 -0.0547 283 GLY A O   
1834  N N   . ASN A 284 ? 1.0307 1.3462 1.0781 0.5239  -0.1257 -0.0885 284 ASN A N   
1835  C CA  . ASN A 284 ? 1.0531 1.3098 1.0590 0.5510  -0.1112 -0.0689 284 ASN A CA  
1836  C C   . ASN A 284 ? 1.0850 1.2377 1.0669 0.5307  -0.0896 -0.0450 284 ASN A C   
1837  O O   . ASN A 284 ? 1.1091 1.1979 1.0495 0.5490  -0.0739 -0.0274 284 ASN A O   
1838  C CB  . ASN A 284 ? 1.0369 1.3550 1.0783 0.5549  -0.1126 -0.0885 284 ASN A CB  
1839  C CG  . ASN A 284 ? 1.0381 1.4362 1.0762 0.5846  -0.1278 -0.1060 284 ASN A CG  
1840  O OD1 . ASN A 284 ? 1.0925 1.4611 1.0735 0.6219  -0.1266 -0.0910 284 ASN A OD1 
1841  N ND2 . ASN A 284 ? 0.9973 1.4974 1.0957 0.5666  -0.1404 -0.1400 284 ASN A ND2 
1842  N N   . MET A 285 ? 0.9557 1.0859 0.9584 0.4780  -0.0852 -0.0450 285 MET A N   
1843  C CA  . MET A 285 ? 0.9803 1.0200 0.9622 0.4484  -0.0648 -0.0261 285 MET A CA  
1844  C C   . MET A 285 ? 1.0047 0.9716 0.9277 0.4694  -0.0565 -0.0028 285 MET A C   
1845  O O   . MET A 285 ? 1.0093 0.9490 0.9266 0.4437  -0.0546 0.0033  285 MET A O   
1846  C CB  . MET A 285 ? 0.9728 1.0209 0.9947 0.3913  -0.0643 -0.0350 285 MET A CB  
1847  C CG  . MET A 285 ? 0.9589 1.0590 1.0312 0.3659  -0.0651 -0.0545 285 MET A CG  
1848  S SD  . MET A 285 ? 0.9609 1.0512 1.0655 0.3044  -0.0595 -0.0597 285 MET A SD  
1849  C CE  . MET A 285 ? 0.9756 0.9967 1.0646 0.2898  -0.0391 -0.0460 285 MET A CE  
1850  N N   . THR A 286 ? 1.0574 0.9897 0.9328 0.5185  -0.0492 0.0106  286 THR A N   
1851  C CA  . THR A 286 ? 1.0885 0.9580 0.9023 0.5338  -0.0385 0.0316  286 THR A CA  
1852  C C   . THR A 286 ? 1.1130 0.8831 0.8963 0.5079  -0.0126 0.0490  286 THR A C   
1853  O O   . THR A 286 ? 1.1495 0.8633 0.8825 0.5143  0.0006  0.0654  286 THR A O   
1854  C CB  . THR A 286 ? 1.1277 0.9943 0.8987 0.5736  -0.0347 0.0380  286 THR A CB  
1855  O OG1 . THR A 286 ? 1.1355 0.9847 0.9120 0.5740  -0.0231 0.0367  286 THR A OG1 
1856  C CG2 . THR A 286 ? 1.1140 1.0794 0.9041 0.6005  -0.0604 0.0202  286 THR A CG2 
1857  N N   . ALA A 287 ? 1.0823 0.8337 0.8944 0.4744  -0.0033 0.0436  287 ALA A N   
1858  C CA  . ALA A 287 ? 1.1014 0.7743 0.8942 0.4395  0.0199  0.0534  287 ALA A CA  
1859  C C   . ALA A 287 ? 1.0811 0.7775 0.9117 0.3900  0.0127  0.0450  287 ALA A C   
1860  O O   . ALA A 287 ? 1.0897 0.7360 0.9123 0.3579  0.0294  0.0488  287 ALA A O   
1861  C CB  . ALA A 287 ? 1.1111 0.7477 0.9057 0.4279  0.0379  0.0512  287 ALA A CB  
1862  N N   . LEU A 288 ? 1.0146 0.7864 0.8847 0.3839  -0.0106 0.0322  288 LEU A N   
1863  C CA  . LEU A 288 ? 0.9970 0.7918 0.9031 0.3394  -0.0171 0.0233  288 LEU A CA  
1864  C C   . LEU A 288 ? 1.0075 0.7633 0.8857 0.3309  -0.0117 0.0341  288 LEU A C   
1865  O O   . LEU A 288 ? 1.0176 0.7719 0.8668 0.3600  -0.0169 0.0416  288 LEU A O   
1866  C CB  . LEU A 288 ? 0.9737 0.8533 0.9248 0.3360  -0.0396 0.0054  288 LEU A CB  
1867  C CG  . LEU A 288 ? 0.9588 0.8660 0.9516 0.2914  -0.0446 -0.0066 288 LEU A CG  
1868  C CD1 . LEU A 288 ? 0.9576 0.8487 0.9682 0.2657  -0.0328 -0.0093 288 LEU A CD1 
1869  C CD2 . LEU A 288 ? 0.9440 0.9287 0.9741 0.2907  -0.0628 -0.0256 288 LEU A CD2 
1870  N N   . ASP A 289 ? 1.0294 0.7563 0.9152 0.2927  -0.0009 0.0339  289 ASP A N   
1871  C CA  . ASP A 289 ? 1.0374 0.7315 0.9028 0.2780  0.0060  0.0411  289 ASP A CA  
1872  C C   . ASP A 289 ? 1.0155 0.7546 0.9155 0.2515  -0.0094 0.0311  289 ASP A C   
1873  O O   . ASP A 289 ? 1.0194 0.7598 0.9066 0.2549  -0.0146 0.0347  289 ASP A O   
1874  C CB  . ASP A 289 ? 1.0510 0.6840 0.8990 0.2542  0.0309  0.0449  289 ASP A CB  
1875  C CG  . ASP A 289 ? 1.0602 0.6642 0.8906 0.2357  0.0402  0.0493  289 ASP A CG  
1876  O OD1 . ASP A 289 ? 1.0706 0.6744 0.8797 0.2539  0.0346  0.0571  289 ASP A OD1 
1877  O OD2 . ASP A 289 ? 1.0574 0.6437 0.8961 0.2034  0.0529  0.0433  289 ASP A OD2 
1878  N N   . THR A 290 ? 0.9052 0.6767 0.8449 0.2265  -0.0151 0.0191  290 THR A N   
1879  C CA  . THR A 290 ? 0.8882 0.6938 0.8567 0.2019  -0.0262 0.0100  290 THR A CA  
1880  C C   . THR A 290 ? 0.8774 0.7353 0.8834 0.1977  -0.0379 -0.0034 290 THR A C   
1881  O O   . THR A 290 ? 0.8755 0.7359 0.8945 0.1939  -0.0325 -0.0068 290 THR A O   
1882  C CB  . THR A 290 ? 0.8800 0.6616 0.8526 0.1711  -0.0155 0.0094  290 THR A CB  
1883  O OG1 . THR A 290 ? 0.8955 0.6308 0.8354 0.1711  -0.0013 0.0185  290 THR A OG1 
1884  C CG2 . THR A 290 ? 0.8633 0.6741 0.8586 0.1513  -0.0257 0.0019  290 THR A CG2 
1885  N N   . LEU A 291 ? 0.7934 0.6924 0.8163 0.1967  -0.0519 -0.0126 291 LEU A N   
1886  C CA  . LEU A 291 ? 0.7903 0.7399 0.8494 0.1880  -0.0599 -0.0287 291 LEU A CA  
1887  C C   . LEU A 291 ? 0.7893 0.7494 0.8648 0.1612  -0.0630 -0.0364 291 LEU A C   
1888  O O   . LEU A 291 ? 0.7925 0.7629 0.8625 0.1640  -0.0712 -0.0388 291 LEU A O   
1889  C CB  . LEU A 291 ? 0.7917 0.7887 0.8562 0.2154  -0.0724 -0.0379 291 LEU A CB  
1890  C CG  . LEU A 291 ? 0.7896 0.8492 0.8939 0.2033  -0.0809 -0.0604 291 LEU A CG  
1891  C CD1 . LEU A 291 ? 0.7921 0.8544 0.9207 0.1829  -0.0709 -0.0660 291 LEU A CD1 
1892  C CD2 . LEU A 291 ? 0.7798 0.8937 0.8882 0.2352  -0.0938 -0.0717 291 LEU A CD2 
1893  N N   . SER A 292 ? 0.7515 0.7067 0.8435 0.1376  -0.0556 -0.0399 292 SER A N   
1894  C CA  . SER A 292 ? 0.7544 0.7078 0.8545 0.1147  -0.0549 -0.0447 292 SER A CA  
1895  C C   . SER A 292 ? 0.7739 0.7527 0.9011 0.0982  -0.0510 -0.0584 292 SER A C   
1896  O O   . SER A 292 ? 0.7711 0.7403 0.9036 0.0908  -0.0418 -0.0565 292 SER A O   
1897  C CB  . SER A 292 ? 0.7331 0.6469 0.8170 0.1038  -0.0465 -0.0337 292 SER A CB  
1898  O OG  . SER A 292 ? 0.7320 0.6420 0.8187 0.0874  -0.0457 -0.0372 292 SER A OG  
1899  N N   . LEU A 293 ? 0.7443 0.7552 0.8877 0.0913  -0.0564 -0.0736 293 LEU A N   
1900  C CA  . LEU A 293 ? 0.7747 0.8063 0.9428 0.0702  -0.0485 -0.0895 293 LEU A CA  
1901  C C   . LEU A 293 ? 0.7990 0.8186 0.9657 0.0503  -0.0447 -0.0963 293 LEU A C   
1902  O O   . LEU A 293 ? 0.8073 0.8507 0.9937 0.0331  -0.0396 -0.1152 293 LEU A O   
1903  C CB  . LEU A 293 ? 0.7701 0.8596 0.9642 0.0771  -0.0547 -0.1088 293 LEU A CB  
1904  C CG  . LEU A 293 ? 0.7430 0.8498 0.9350 0.1051  -0.0611 -0.1036 293 LEU A CG  
1905  C CD1 . LEU A 293 ? 0.7281 0.9028 0.9470 0.1142  -0.0690 -0.1262 293 LEU A CD1 
1906  C CD2 . LEU A 293 ? 0.7439 0.8237 0.9334 0.1014  -0.0492 -0.0932 293 LEU A CD2 
1907  N N   . HIS A 294 ? 0.8296 0.8126 0.9728 0.0518  -0.0454 -0.0828 294 HIS A N   
1908  C CA  . HIS A 294 ? 0.8259 0.7949 0.9634 0.0377  -0.0423 -0.0884 294 HIS A CA  
1909  C C   . HIS A 294 ? 0.8139 0.7555 0.9500 0.0180  -0.0247 -0.0897 294 HIS A C   
1910  O O   . HIS A 294 ? 0.8068 0.7353 0.9411 0.0174  -0.0162 -0.0820 294 HIS A O   
1911  C CB  . HIS A 294 ? 0.8042 0.7469 0.9168 0.0479  -0.0486 -0.0746 294 HIS A CB  
1912  C CG  . HIS A 294 ? 0.7673 0.6737 0.8618 0.0485  -0.0412 -0.0589 294 HIS A CG  
1913  N ND1 . HIS A 294 ? 0.7570 0.6367 0.8418 0.0379  -0.0303 -0.0571 294 HIS A ND1 
1914  C CD2 . HIS A 294 ? 0.7394 0.6336 0.8219 0.0593  -0.0425 -0.0461 294 HIS A CD2 
1915  C CE1 . HIS A 294 ? 0.7297 0.5901 0.7992 0.0445  -0.0278 -0.0447 294 HIS A CE1 
1916  N NE2 . HIS A 294 ? 0.7167 0.5866 0.7868 0.0548  -0.0347 -0.0393 294 HIS A NE2 
1917  N N   . THR A 295 ? 0.8461 0.7760 0.9795 0.0029  -0.0178 -0.0997 295 THR A N   
1918  C CA  . THR A 295 ? 0.8448 0.7388 0.9688 -0.0147 0.0027  -0.1008 295 THR A CA  
1919  C C   . THR A 295 ? 0.8546 0.7638 0.9984 -0.0282 0.0157  -0.1104 295 THR A C   
1920  O O   . THR A 295 ? 0.8539 0.7384 0.9870 -0.0282 0.0274  -0.0993 295 THR A O   
1921  C CB  . THR A 295 ? 0.8297 0.6791 0.9228 -0.0039 0.0071  -0.0796 295 THR A CB  
1922  O OG1 . THR A 295 ? 0.8150 0.6621 0.8950 0.0104  -0.0069 -0.0716 295 THR A OG1 
1923  C CG2 . THR A 295 ? 0.8410 0.6455 0.9130 -0.0156 0.0276  -0.0794 295 THR A CG2 
1924  N N   . ASN A 296 ? 0.8084 0.7635 0.9817 -0.0393 0.0137  -0.1331 296 ASN A N   
1925  C CA  . ASN A 296 ? 0.8133 0.7940 1.0110 -0.0544 0.0263  -0.1477 296 ASN A CA  
1926  C C   . ASN A 296 ? 0.8063 0.8118 1.0257 -0.0815 0.0370  -0.1778 296 ASN A C   
1927  O O   . ASN A 296 ? 0.8014 0.7976 1.0137 -0.0880 0.0353  -0.1856 296 ASN A O   
1928  C CB  . ASN A 296 ? 0.8205 0.8505 1.0386 -0.0355 0.0106  -0.1482 296 ASN A CB  
1929  C CG  . ASN A 296 ? 0.8276 0.8325 1.0320 -0.0224 0.0132  -0.1268 296 ASN A CG  
1930  O OD1 . ASN A 296 ? 0.8318 0.8299 1.0409 -0.0337 0.0292  -0.1283 296 ASN A OD1 
1931  N ND2 . ASN A 296 ? 0.8249 0.8161 1.0115 0.0002  -0.0008 -0.1084 296 ASN A ND2 
1932  N N   . LYS A 297 ? 0.8186 0.8585 1.0659 -0.0989 0.0490  -0.1973 297 LYS A N   
1933  C CA  . LYS A 297 ? 0.8024 0.8760 1.0765 -0.1293 0.0616  -0.2321 297 LYS A CA  
1934  C C   . LYS A 297 ? 0.7801 0.9448 1.0959 -0.1235 0.0451  -0.2576 297 LYS A C   
1935  O O   . LYS A 297 ? 0.7597 0.9677 1.1071 -0.1495 0.0589  -0.2887 297 LYS A O   
1936  C CB  . LYS A 297 ? 0.8092 0.8435 1.0790 -0.1614 0.0970  -0.2391 297 LYS A CB  
1937  C CG  . LYS A 297 ? 0.8276 0.7729 1.0521 -0.1664 0.1154  -0.2193 297 LYS A CG  
1938  C CD  . LYS A 297 ? 0.8420 0.7386 1.0533 -0.1945 0.1537  -0.2230 297 LYS A CD  
1939  C CE  . LYS A 297 ? 0.8643 0.6685 1.0219 -0.1891 0.1709  -0.1983 297 LYS A CE  
1940  N NZ  . LYS A 297 ? 0.8868 0.6353 1.0208 -0.2067 0.2081  -0.1932 297 LYS A NZ  
1941  N N   . LEU A 298 ? 0.8027 0.9970 1.1168 -0.0885 0.0171  -0.2455 298 LEU A N   
1942  C CA  . LEU A 298 ? 0.7756 1.0557 1.1215 -0.0734 -0.0014 -0.2672 298 LEU A CA  
1943  C C   . LEU A 298 ? 0.7455 1.0757 1.1128 -0.0894 -0.0054 -0.3018 298 LEU A C   
1944  O O   . LEU A 298 ? 0.7525 1.0460 1.1032 -0.1021 -0.0012 -0.3019 298 LEU A O   
1945  C CB  . LEU A 298 ? 0.7848 1.0687 1.1122 -0.0297 -0.0272 -0.2429 298 LEU A CB  
1946  C CG  . LEU A 298 ? 0.8129 1.0505 1.1191 -0.0130 -0.0245 -0.2113 298 LEU A CG  
1947  C CD1 . LEU A 298 ? 0.8069 1.0636 1.1027 0.0275  -0.0457 -0.1971 298 LEU A CD1 
1948  C CD2 . LEU A 298 ? 0.8102 1.0578 1.1363 -0.0306 -0.0060 -0.2201 298 LEU A CD2 
1949  N N   . THR A 299 ? 0.7819 1.2007 1.1867 -0.0879 -0.0137 -0.3334 299 THR A N   
1950  C CA  . THR A 299 ? 0.7456 1.2291 1.1763 -0.1025 -0.0191 -0.3727 299 THR A CA  
1951  C C   . THR A 299 ? 0.7097 1.2852 1.1585 -0.0646 -0.0484 -0.3861 299 THR A C   
1952  O O   . THR A 299 ? 0.7125 1.2966 1.1543 -0.0306 -0.0602 -0.3662 299 THR A O   
1953  C CB  . THR A 299 ? 0.7235 1.2312 1.1882 -0.1524 0.0098  -0.4114 299 THR A CB  
1954  O OG1 . THR A 299 ? 0.7122 1.2532 1.2006 -0.1545 0.0186  -0.4170 299 THR A OG1 
1955  C CG2 . THR A 299 ? 0.7562 1.1665 1.1940 -0.1871 0.0400  -0.3997 299 THR A CG2 
1956  N N   . GLY A 300 ? 0.7232 1.3669 1.1923 -0.0688 -0.0595 -0.4209 300 GLY A N   
1957  C CA  . GLY A 300 ? 0.6823 1.4215 1.1668 -0.0304 -0.0873 -0.4381 300 GLY A CA  
1958  C C   . GLY A 300 ? 0.6987 1.4139 1.1422 0.0165  -0.1126 -0.4072 300 GLY A C   
1959  O O   . GLY A 300 ? 0.7406 1.3689 1.1476 0.0167  -0.1087 -0.3740 300 GLY A O   
1960  N N   . PRO A 301 ? 0.7071 1.4999 1.1540 0.0588  -0.1378 -0.4178 301 PRO A N   
1961  C CA  . PRO A 301 ? 0.7193 1.4914 1.1236 0.1046  -0.1597 -0.3907 301 PRO A CA  
1962  C C   . PRO A 301 ? 0.7513 1.4561 1.1173 0.1396  -0.1613 -0.3436 301 PRO A C   
1963  O O   . PRO A 301 ? 0.7579 1.4477 1.1325 0.1363  -0.1504 -0.3343 301 PRO A O   
1964  C CB  . PRO A 301 ? 0.6655 1.5528 1.0877 0.1377  -0.1835 -0.4241 301 PRO A CB  
1965  C CG  . PRO A 301 ? 0.6314 1.5884 1.0969 0.1288  -0.1773 -0.4515 301 PRO A CG  
1966  C CD  . PRO A 301 ? 0.6511 1.5600 1.1404 0.0674  -0.1465 -0.4586 301 PRO A CD  
1967  N N   . ILE A 302 ? 0.7835 1.4468 1.1058 0.1720  -0.1734 -0.3153 302 ILE A N   
1968  C CA  . ILE A 302 ? 0.8072 1.4093 1.0896 0.2075  -0.1743 -0.2737 302 ILE A CA  
1969  C C   . ILE A 302 ? 0.7753 1.4419 1.0583 0.2542  -0.1884 -0.2799 302 ILE A C   
1970  O O   . ILE A 302 ? 0.7421 1.4857 1.0291 0.2816  -0.2069 -0.3024 302 ILE A O   
1971  C CB  . ILE A 302 ? 0.8320 1.3732 1.0665 0.2270  -0.1800 -0.2446 302 ILE A CB  
1972  C CG1 . ILE A 302 ? 0.8721 1.3237 1.0935 0.1925  -0.1629 -0.2222 302 ILE A CG1 
1973  C CG2 . ILE A 302 ? 0.8365 1.3518 1.0285 0.2788  -0.1870 -0.2145 302 ILE A CG2 
1974  C CD1 . ILE A 302 ? 0.8764 1.3336 1.1207 0.1497  -0.1559 -0.2453 302 ILE A CD1 
1975  N N   . PRO A 303 ? 0.8166 1.4579 1.0944 0.2675  -0.1809 -0.2622 303 PRO A N   
1976  C CA  . PRO A 303 ? 0.7889 1.4866 1.0617 0.3176  -0.1938 -0.2662 303 PRO A CA  
1977  C C   . PRO A 303 ? 0.7965 1.4700 1.0142 0.3718  -0.2072 -0.2415 303 PRO A C   
1978  O O   . PRO A 303 ? 0.8317 1.4129 1.0066 0.3771  -0.1986 -0.2054 303 PRO A O   
1979  C CB  . PRO A 303 ? 0.8056 1.4578 1.0785 0.3140  -0.1784 -0.2475 303 PRO A CB  
1980  C CG  . PRO A 303 ? 0.8478 1.4003 1.1038 0.2785  -0.1612 -0.2206 303 PRO A CG  
1981  C CD  . PRO A 303 ? 0.8507 1.4116 1.1242 0.2401  -0.1605 -0.2382 303 PRO A CD  
1982  N N   . SER A 304 ? 0.8333 1.5928 1.0510 0.4127  -0.2272 -0.2627 304 SER A N   
1983  C CA  . SER A 304 ? 0.8563 1.5821 1.0085 0.4626  -0.2341 -0.2376 304 SER A CA  
1984  C C   . SER A 304 ? 0.8883 1.5374 0.9930 0.4962  -0.2229 -0.1998 304 SER A C   
1985  O O   . SER A 304 ? 0.9247 1.5112 0.9673 0.5278  -0.2196 -0.1704 304 SER A O   
1986  C CB  . SER A 304 ? 0.8704 1.6760 1.0137 0.4857  -0.2453 -0.2651 304 SER A CB  
1987  O OG  . SER A 304 ? 0.8849 1.7361 1.0402 0.4993  -0.2437 -0.2789 304 SER A OG  
1988  N N   . THR A 305 ? 0.8817 1.5323 1.0130 0.4878  -0.2145 -0.2012 305 THR A N   
1989  C CA  . THR A 305 ? 0.9108 1.4861 1.0017 0.5133  -0.2012 -0.1684 305 THR A CA  
1990  C C   . THR A 305 ? 0.9395 1.4079 1.0050 0.4975  -0.1861 -0.1348 305 THR A C   
1991  O O   . THR A 305 ? 0.9608 1.3625 0.9965 0.5121  -0.1721 -0.1101 305 THR A O   
1992  C CB  . THR A 305 ? 0.8941 1.5060 1.0238 0.5048  -0.1958 -0.1830 305 THR A CB  
1993  O OG1 . THR A 305 ? 0.8881 1.4946 1.0678 0.4499  -0.1861 -0.1933 305 THR A OG1 
1994  C CG2 . THR A 305 ? 0.8834 1.5971 1.0344 0.5140  -0.2072 -0.2179 305 THR A CG2 
1995  N N   . LEU A 306 ? 0.9092 1.3501 0.9814 0.4575  -0.1832 -0.1339 306 LEU A N   
1996  C CA  . LEU A 306 ? 0.9439 1.2792 0.9819 0.4397  -0.1658 -0.1017 306 LEU A CA  
1997  C C   . LEU A 306 ? 0.9662 1.2456 0.9376 0.4859  -0.1637 -0.0736 306 LEU A C   
1998  O O   . LEU A 306 ? 0.9939 1.1844 0.9307 0.4818  -0.1453 -0.0463 306 LEU A O   
1999  C CB  . LEU A 306 ? 0.9500 1.2725 1.0101 0.3894  -0.1633 -0.1083 306 LEU A CB  
2000  C CG  . LEU A 306 ? 0.9425 1.2937 1.0575 0.3420  -0.1574 -0.1296 306 LEU A CG  
2001  C CD1 . LEU A 306 ? 0.9576 1.2777 1.0851 0.2954  -0.1506 -0.1308 306 LEU A CD1 
2002  C CD2 . LEU A 306 ? 0.9519 1.2655 1.0680 0.3388  -0.1431 -0.1168 306 LEU A CD2 
2003  N N   . GLY A 307 ? 1.0224 1.3526 0.9737 0.5293  -0.1803 -0.0809 307 GLY A N   
2004  C CA  . GLY A 307 ? 1.0648 1.3320 0.9433 0.5610  -0.1706 -0.0541 307 GLY A CA  
2005  C C   . GLY A 307 ? 1.1028 1.3117 0.9363 0.5870  -0.1529 -0.0324 307 GLY A C   
2006  O O   . GLY A 307 ? 1.1541 1.2898 0.9253 0.6059  -0.1376 -0.0068 307 GLY A O   
2007  N N   . ASN A 308 ? 1.1117 1.3501 0.9743 0.5871  -0.1527 -0.0430 308 ASN A N   
2008  C CA  . ASN A 308 ? 1.1577 1.3370 0.9771 0.6106  -0.1350 -0.0230 308 ASN A CA  
2009  C C   . ASN A 308 ? 1.1694 1.2448 0.9683 0.5902  -0.1112 0.0030  308 ASN A C   
2010  O O   . ASN A 308 ? 1.2217 1.2266 0.9681 0.6080  -0.0916 0.0241  308 ASN A O   
2011  C CB  . ASN A 308 ? 1.1430 1.3822 0.9977 0.6169  -0.1407 -0.0418 308 ASN A CB  
2012  C CG  . ASN A 308 ? 1.1194 1.4752 1.0152 0.6214  -0.1638 -0.0767 308 ASN A CG  
2013  O OD1 . ASN A 308 ? 1.0629 1.4742 1.0135 0.5902  -0.1753 -0.0990 308 ASN A OD1 
2014  N ND2 . ASN A 308 ? 1.1716 1.5653 1.0392 0.6597  -0.1690 -0.0836 308 ASN A ND2 
2015  N N   . ILE A 309 ? 1.0762 1.1402 0.9131 0.5532  -0.1110 0.0001  309 ILE A N   
2016  C CA  . ILE A 309 ? 1.0957 1.0671 0.9157 0.5314  -0.0879 0.0202  309 ILE A CA  
2017  C C   . ILE A 309 ? 1.1271 1.0284 0.8936 0.5324  -0.0747 0.0416  309 ILE A C   
2018  O O   . ILE A 309 ? 1.1215 1.0251 0.8991 0.5122  -0.0804 0.0399  309 ILE A O   
2019  C CB  . ILE A 309 ? 1.0808 1.0649 0.9567 0.4733  -0.0870 0.0070  309 ILE A CB  
2020  C CG1 . ILE A 309 ? 1.0582 1.1050 0.9827 0.4668  -0.0944 -0.0134 309 ILE A CG1 
2021  C CG2 . ILE A 309 ? 1.1031 0.9982 0.9597 0.4443  -0.0624 0.0244  309 ILE A CG2 
2022  C CD1 . ILE A 309 ? 1.0326 1.1589 1.0149 0.4342  -0.1102 -0.0402 309 ILE A CD1 
2023  N N   . LYS A 310 ? 1.1433 0.9826 0.8505 0.5537  -0.0552 0.0605  310 LYS A N   
2024  C CA  . LYS A 310 ? 1.1852 0.9554 0.8369 0.5559  -0.0378 0.0804  310 LYS A CA  
2025  C C   . LYS A 310 ? 1.1900 0.8817 0.8375 0.5182  -0.0149 0.0918  310 LYS A C   
2026  O O   . LYS A 310 ? 1.2160 0.8574 0.8281 0.5109  -0.0009 0.1045  310 LYS A O   
2027  C CB  . LYS A 310 ? 1.2667 0.9979 0.8539 0.5930  -0.0222 0.0946  310 LYS A CB  
2028  C CG  . LYS A 310 ? 1.2842 1.0936 0.8699 0.6340  -0.0433 0.0818  310 LYS A CG  
2029  C CD  . LYS A 310 ? 1.2379 1.1325 0.8582 0.6341  -0.0716 0.0630  310 LYS A CD  
2030  C CE  . LYS A 310 ? 1.2819 1.2372 0.8776 0.6783  -0.0860 0.0531  310 LYS A CE  
2031  N NZ  . LYS A 310 ? 1.2539 1.2757 0.8685 0.6780  -0.1078 0.0370  310 LYS A NZ  
2032  N N   . THR A 311 ? 1.1540 0.8364 0.8356 0.4939  -0.0095 0.0858  311 THR A N   
2033  C CA  . THR A 311 ? 1.1623 0.7798 0.8447 0.4558  0.0114  0.0914  311 THR A CA  
2034  C C   . THR A 311 ? 1.1333 0.7963 0.8697 0.4092  -0.0022 0.0763  311 THR A C   
2035  O O   . THR A 311 ? 1.1373 0.7628 0.8788 0.3703  0.0129  0.0772  311 THR A O   
2036  C CB  . THR A 311 ? 1.1666 0.7528 0.8557 0.4448  0.0276  0.0898  311 THR A CB  
2037  O OG1 . THR A 311 ? 1.1419 0.7959 0.8690 0.4612  0.0078  0.0761  311 THR A OG1 
2038  C CG2 . THR A 311 ? 1.2162 0.7342 0.8471 0.4588  0.0543  0.1046  311 THR A CG2 
2039  N N   . LEU A 312 ? 1.0792 0.8235 0.8550 0.4108  -0.0288 0.0608  312 LEU A N   
2040  C CA  . LEU A 312 ? 1.0550 0.8395 0.8802 0.3666  -0.0397 0.0459  312 LEU A CA  
2041  C C   . LEU A 312 ? 1.0656 0.8219 0.8719 0.3511  -0.0347 0.0531  312 LEU A C   
2042  O O   . LEU A 312 ? 1.0749 0.8393 0.8552 0.3765  -0.0422 0.0579  312 LEU A O   
2043  C CB  . LEU A 312 ? 1.0290 0.9018 0.8962 0.3721  -0.0653 0.0257  312 LEU A CB  
2044  C CG  . LEU A 312 ? 1.0086 0.9212 0.9282 0.3277  -0.0736 0.0084  312 LEU A CG  
2045  C CD1 . LEU A 312 ? 1.0042 0.8975 0.9464 0.2992  -0.0617 0.0067  312 LEU A CD1 
2046  C CD2 . LEU A 312 ? 0.9902 0.9858 0.9457 0.3341  -0.0946 -0.0136 312 LEU A CD2 
2047  N N   . ALA A 313 ? 1.0025 0.7295 0.8210 0.3112  -0.0223 0.0528  313 ALA A N   
2048  C CA  . ALA A 313 ? 1.0107 0.7156 0.8166 0.2925  -0.0166 0.0570  313 ALA A CA  
2049  C C   . ALA A 313 ? 0.9855 0.7376 0.8347 0.2619  -0.0317 0.0424  313 ALA A C   
2050  O O   . ALA A 313 ? 0.9897 0.7463 0.8313 0.2580  -0.0360 0.0429  313 ALA A O   
2051  C CB  . ALA A 313 ? 1.0299 0.6680 0.8136 0.2709  0.0109  0.0653  313 ALA A CB  
2052  N N   . VAL A 314 ? 0.9075 0.6894 0.7975 0.2410  -0.0375 0.0303  314 VAL A N   
2053  C CA  . VAL A 314 ? 0.8861 0.7027 0.8120 0.2129  -0.0478 0.0176  314 VAL A CA  
2054  C C   . VAL A 314 ? 0.8741 0.7461 0.8346 0.2156  -0.0632 0.0028  314 VAL A C   
2055  O O   . VAL A 314 ? 0.8718 0.7518 0.8426 0.2224  -0.0614 0.0005  314 VAL A O   
2056  C CB  . VAL A 314 ? 0.8757 0.6700 0.8139 0.1820  -0.0356 0.0165  314 VAL A CB  
2057  C CG1 . VAL A 314 ? 0.8573 0.6813 0.8248 0.1590  -0.0448 0.0056  314 VAL A CG1 
2058  C CG2 . VAL A 314 ? 0.8923 0.6380 0.7995 0.1761  -0.0182 0.0264  314 VAL A CG2 
2059  N N   . LEU A 315 ? 0.8250 0.7351 0.8035 0.2085  -0.0763 -0.0090 315 LEU A N   
2060  C CA  . LEU A 315 ? 0.8202 0.7854 0.8335 0.2052  -0.0881 -0.0274 315 LEU A CA  
2061  C C   . LEU A 315 ? 0.8213 0.7995 0.8569 0.1760  -0.0907 -0.0390 315 LEU A C   
2062  O O   . LEU A 315 ? 0.8266 0.8130 0.8554 0.1764  -0.0976 -0.0426 315 LEU A O   
2063  C CB  . LEU A 315 ? 0.8210 0.8291 0.8288 0.2360  -0.1021 -0.0349 315 LEU A CB  
2064  C CG  . LEU A 315 ? 0.8126 0.8862 0.8582 0.2344  -0.1126 -0.0581 315 LEU A CG  
2065  C CD1 . LEU A 315 ? 0.8086 0.8815 0.8654 0.2378  -0.1056 -0.0567 315 LEU A CD1 
2066  C CD2 . LEU A 315 ? 0.8041 0.9291 0.8434 0.2660  -0.1287 -0.0688 315 LEU A CD2 
2067  N N   . HIS A 316 ? 0.7996 0.7762 0.8580 0.1526  -0.0841 -0.0444 316 HIS A N   
2068  C CA  . HIS A 316 ? 0.8091 0.7893 0.8835 0.1270  -0.0828 -0.0541 316 HIS A CA  
2069  C C   . HIS A 316 ? 0.8271 0.8474 0.9330 0.1157  -0.0842 -0.0736 316 HIS A C   
2070  O O   . HIS A 316 ? 0.8280 0.8492 0.9476 0.1088  -0.0769 -0.0747 316 HIS A O   
2071  C CB  . HIS A 316 ? 0.7949 0.7361 0.8634 0.1104  -0.0712 -0.0440 316 HIS A CB  
2072  C CG  . HIS A 316 ? 0.7775 0.6856 0.8196 0.1156  -0.0676 -0.0300 316 HIS A CG  
2073  N ND1 . HIS A 316 ? 0.7570 0.6383 0.7929 0.1041  -0.0581 -0.0232 316 HIS A ND1 
2074  C CD2 . HIS A 316 ? 0.7818 0.6817 0.8018 0.1306  -0.0708 -0.0231 316 HIS A CD2 
2075  C CE1 . HIS A 316 ? 0.7540 0.6147 0.7687 0.1087  -0.0549 -0.0149 316 HIS A CE1 
2076  N NE2 . HIS A 316 ? 0.7709 0.6382 0.7739 0.1244  -0.0613 -0.0132 316 HIS A NE2 
2077  N N   . LEU A 317 ? 0.7757 0.8306 0.8934 0.1121  -0.0922 -0.0909 317 LEU A N   
2078  C CA  . LEU A 317 ? 0.7882 0.8837 0.9377 0.0951  -0.0907 -0.1147 317 LEU A CA  
2079  C C   . LEU A 317 ? 0.8116 0.8963 0.9668 0.0683  -0.0841 -0.1265 317 LEU A C   
2080  O O   . LEU A 317 ? 0.8043 0.9222 0.9841 0.0507  -0.0809 -0.1504 317 LEU A O   
2081  C CB  . LEU A 317 ? 0.7642 0.9225 0.9268 0.1143  -0.1048 -0.1324 317 LEU A CB  
2082  C CG  . LEU A 317 ? 0.7422 0.9220 0.9028 0.1436  -0.1103 -0.1267 317 LEU A CG  
2083  C CD1 . LEU A 317 ? 0.7208 0.9786 0.9072 0.1544  -0.1218 -0.1540 317 LEU A CD1 
2084  C CD2 . LEU A 317 ? 0.7468 0.9001 0.9135 0.1343  -0.0973 -0.1170 317 LEU A CD2 
2085  N N   . TYR A 318 ? 0.8596 0.8991 0.9922 0.0645  -0.0804 -0.1120 318 TYR A N   
2086  C CA  . TYR A 318 ? 0.8555 0.8814 0.9867 0.0455  -0.0751 -0.1222 318 TYR A CA  
2087  C C   . TYR A 318 ? 0.8413 0.8443 0.9813 0.0205  -0.0568 -0.1278 318 TYR A C   
2088  O O   . TYR A 318 ? 0.8399 0.8324 0.9836 0.0188  -0.0487 -0.1199 318 TYR A O   
2089  C CB  . TYR A 318 ? 0.8504 0.8389 0.9533 0.0532  -0.0771 -0.1053 318 TYR A CB  
2090  C CG  . TYR A 318 ? 0.8263 0.7736 0.9133 0.0550  -0.0688 -0.0844 318 TYR A CG  
2091  C CD1 . TYR A 318 ? 0.8095 0.7508 0.8859 0.0713  -0.0722 -0.0688 318 TYR A CD1 
2092  C CD2 . TYR A 318 ? 0.8083 0.7223 0.8879 0.0415  -0.0564 -0.0816 318 TYR A CD2 
2093  C CE1 . TYR A 318 ? 0.7735 0.6846 0.8382 0.0705  -0.0645 -0.0546 318 TYR A CE1 
2094  C CE2 . TYR A 318 ? 0.7786 0.6647 0.8440 0.0458  -0.0507 -0.0655 318 TYR A CE2 
2095  C CZ  . TYR A 318 ? 0.7602 0.6486 0.8207 0.0586  -0.0553 -0.0538 318 TYR A CZ  
2096  O OH  . TYR A 318 ? 0.7291 0.5965 0.7783 0.0603  -0.0493 -0.0424 318 TYR A OH  
2097  N N   . LEU A 319 ? 0.8495 0.8412 0.9895 0.0016  -0.0485 -0.1419 319 LEU A N   
2098  C CA  . LEU A 319 ? 0.8447 0.8042 0.9850 -0.0224 -0.0267 -0.1476 319 LEU A CA  
2099  C C   . LEU A 319 ? 0.8440 0.8343 1.0124 -0.0367 -0.0179 -0.1631 319 LEU A C   
2100  O O   . LEU A 319 ? 0.8455 0.8147 1.0118 -0.0402 -0.0060 -0.1530 319 LEU A O   
2101  C CB  . LEU A 319 ? 0.8394 0.7439 0.9519 -0.0158 -0.0178 -0.1227 319 LEU A CB  
2102  C CG  . LEU A 319 ? 0.8401 0.7017 0.9260 -0.0176 -0.0112 -0.1184 319 LEU A CG  
2103  C CD1 . LEU A 319 ? 0.8338 0.6497 0.8931 -0.0088 -0.0017 -0.0971 319 LEU A CD1 
2104  C CD2 . LEU A 319 ? 0.8510 0.7022 0.9419 -0.0425 0.0048  -0.1407 319 LEU A CD2 
2105  N N   . ASN A 320 ? 0.8353 0.8817 1.0308 -0.0438 -0.0245 -0.1898 320 ASN A N   
2106  C CA  . ASN A 320 ? 0.8251 0.9162 1.0532 -0.0587 -0.0173 -0.2116 320 ASN A CA  
2107  C C   . ASN A 320 ? 0.8055 0.9372 1.0569 -0.0822 -0.0136 -0.2483 320 ASN A C   
2108  O O   . ASN A 320 ? 0.8061 0.9172 1.0444 -0.0897 -0.0124 -0.2541 320 ASN A O   
2109  C CB  . ASN A 320 ? 0.8256 0.9645 1.0666 -0.0318 -0.0354 -0.2063 320 ASN A CB  
2110  C CG  . ASN A 320 ? 0.8411 0.9510 1.0742 -0.0242 -0.0283 -0.1840 320 ASN A CG  
2111  O OD1 . ASN A 320 ? 0.8379 0.9547 1.0875 -0.0404 -0.0135 -0.1928 320 ASN A OD1 
2112  N ND2 . ASN A 320 ? 0.8570 0.9360 1.0648 -0.0007 -0.0377 -0.1567 320 ASN A ND2 
2113  N N   . GLN A 321 ? 0.8747 1.0682 1.1620 -0.0946 -0.0112 -0.2759 321 GLN A N   
2114  C CA  . GLN A 321 ? 0.8471 1.0930 1.1626 -0.1194 -0.0075 -0.3173 321 GLN A CA  
2115  C C   . GLN A 321 ? 0.8157 1.1593 1.1612 -0.0990 -0.0320 -0.3394 321 GLN A C   
2116  O O   . GLN A 321 ? 0.7823 1.1921 1.1644 -0.1202 -0.0271 -0.3786 321 GLN A O   
2117  C CB  . GLN A 321 ? 0.8408 1.0748 1.1741 -0.1618 0.0249  -0.3399 321 GLN A CB  
2118  C CG  . GLN A 321 ? 0.8713 1.0066 1.1694 -0.1753 0.0513  -0.3145 321 GLN A CG  
2119  C CD  . GLN A 321 ? 0.8686 0.9867 1.1791 -0.2174 0.0873  -0.3370 321 GLN A CD  
2120  O OE1 . GLN A 321 ? 0.8528 0.9909 1.1815 -0.2500 0.1020  -0.3730 321 GLN A OE1 
2121  N NE2 . GLN A 321 ? 0.8847 0.9650 1.1841 -0.2183 0.1036  -0.3173 321 GLN A NE2 
2122  N N   . LEU A 322 ? 0.8057 1.1602 1.1346 -0.0572 -0.0569 -0.3160 322 LEU A N   
2123  C CA  . LEU A 322 ? 0.7733 1.2155 1.1215 -0.0297 -0.0805 -0.3337 322 LEU A CA  
2124  C C   . LEU A 322 ? 0.7461 1.2395 1.1051 -0.0355 -0.0909 -0.3657 322 LEU A C   
2125  O O   . LEU A 322 ? 0.7620 1.2119 1.1004 -0.0450 -0.0881 -0.3609 322 LEU A O   
2126  C CB  . LEU A 322 ? 0.7881 1.2165 1.1071 0.0178  -0.1003 -0.2987 322 LEU A CB  
2127  C CG  . LEU A 322 ? 0.8147 1.1925 1.1202 0.0264  -0.0916 -0.2671 322 LEU A CG  
2128  C CD1 . LEU A 322 ? 0.8526 1.1432 1.1251 0.0197  -0.0820 -0.2367 322 LEU A CD1 
2129  C CD2 . LEU A 322 ? 0.8057 1.2039 1.0993 0.0698  -0.1082 -0.2500 322 LEU A CD2 
2130  N N   . ASN A 323 ? 0.7702 1.3615 1.1626 -0.0291 -0.1031 -0.4009 323 ASN A N   
2131  C CA  . ASN A 323 ? 0.7366 1.3938 1.1448 -0.0349 -0.1141 -0.4387 323 ASN A CA  
2132  C C   . ASN A 323 ? 0.7042 1.4454 1.1129 0.0144  -0.1452 -0.4452 323 ASN A C   
2133  O O   . ASN A 323 ? 0.7142 1.4450 1.1025 0.0545  -0.1568 -0.4145 323 ASN A O   
2134  C CB  . ASN A 323 ? 0.7043 1.4090 1.1576 -0.0855 -0.0933 -0.4888 323 ASN A CB  
2135  C CG  . ASN A 323 ? 0.6639 1.4573 1.1594 -0.0844 -0.0946 -0.5159 323 ASN A CG  
2136  O OD1 . ASN A 323 ? 0.6372 1.5051 1.1390 -0.0425 -0.1201 -0.5198 323 ASN A OD1 
2137  N ND2 . ASN A 323 ? 0.6586 1.4429 1.1809 -0.1301 -0.0651 -0.5354 323 ASN A ND2 
2138  N N   . GLY A 324 ? 0.6959 1.5171 1.1235 0.0134  -0.1580 -0.4848 324 GLY A N   
2139  C CA  . GLY A 324 ? 0.6609 1.5688 1.0862 0.0634  -0.1878 -0.4944 324 GLY A CA  
2140  C C   . GLY A 324 ? 0.6873 1.5509 1.0609 0.1050  -0.2052 -0.4589 324 GLY A C   
2141  O O   . GLY A 324 ? 0.7264 1.5061 1.0724 0.0907  -0.1959 -0.4351 324 GLY A O   
2142  N N   . SER A 325 ? 0.7120 1.6336 1.0700 0.1594  -0.2297 -0.4555 325 SER A N   
2143  C CA  . SER A 325 ? 0.7322 1.6202 1.0384 0.2027  -0.2455 -0.4248 325 SER A CA  
2144  C C   . SER A 325 ? 0.7648 1.5820 1.0297 0.2401  -0.2444 -0.3735 325 SER A C   
2145  O O   . SER A 325 ? 0.7611 1.5807 1.0383 0.2455  -0.2389 -0.3666 325 SER A O   
2146  C CB  . SER A 325 ? 0.7059 1.6813 1.0040 0.2402  -0.2648 -0.4491 325 SER A CB  
2147  O OG  . SER A 325 ? 0.7140 1.7520 1.0508 0.2026  -0.2559 -0.4978 325 SER A OG  
2148  N N   . ILE A 326 ? 0.7833 1.5349 0.9986 0.2634  -0.2476 -0.3387 326 ILE A N   
2149  C CA  . ILE A 326 ? 0.8134 1.4920 0.9846 0.2968  -0.2438 -0.2916 326 ILE A CA  
2150  C C   . ILE A 326 ? 0.7871 1.5242 0.9421 0.3549  -0.2607 -0.2916 326 ILE A C   
2151  O O   . ILE A 326 ? 0.7668 1.5607 0.9059 0.3875  -0.2776 -0.3057 326 ILE A O   
2152  C CB  . ILE A 326 ? 0.8490 1.4489 0.9723 0.3046  -0.2408 -0.2591 326 ILE A CB  
2153  C CG1 . ILE A 326 ? 0.8727 1.4228 1.0116 0.2517  -0.2256 -0.2621 326 ILE A CG1 
2154  C CG2 . ILE A 326 ? 0.8765 1.3991 0.9561 0.3329  -0.2324 -0.2140 326 ILE A CG2 
2155  C CD1 . ILE A 326 ? 0.8980 1.3962 0.9982 0.2571  -0.2258 -0.2424 326 ILE A CD1 
2156  N N   . PRO A 327 ? 0.8281 1.5517 0.9828 0.3702  -0.2549 -0.2765 327 PRO A N   
2157  C CA  . PRO A 327 ? 0.8160 1.5778 0.9443 0.4264  -0.2652 -0.2723 327 PRO A CA  
2158  C C   . PRO A 327 ? 0.8558 1.5522 0.9114 0.4694  -0.2644 -0.2352 327 PRO A C   
2159  O O   . PRO A 327 ? 0.8748 1.4864 0.9027 0.4710  -0.2562 -0.2000 327 PRO A O   
2160  C CB  . PRO A 327 ? 0.8153 1.5568 0.9583 0.4273  -0.2556 -0.2597 327 PRO A CB  
2161  C CG  . PRO A 327 ? 0.8234 1.5429 1.0121 0.3621  -0.2392 -0.2715 327 PRO A CG  
2162  C CD  . PRO A 327 ? 0.8480 1.5168 1.0235 0.3334  -0.2346 -0.2644 327 PRO A CD  
2163  N N   . PRO A 328 ? 0.8416 1.5740 0.8636 0.5040  -0.2705 -0.2432 328 PRO A N   
2164  C CA  . PRO A 328 ? 0.8969 1.5641 0.8453 0.5458  -0.2656 -0.2080 328 PRO A CA  
2165  C C   . PRO A 328 ? 0.9251 1.5119 0.8321 0.5702  -0.2508 -0.1689 328 PRO A C   
2166  O O   . PRO A 328 ? 0.9643 1.4727 0.8133 0.5911  -0.2400 -0.1351 328 PRO A O   
2167  C CB  . PRO A 328 ? 0.9458 1.6835 0.8743 0.5801  -0.2743 -0.2312 328 PRO A CB  
2168  C CG  . PRO A 328 ? 0.9075 1.7427 0.9022 0.5452  -0.2847 -0.2807 328 PRO A CG  
2169  C CD  . PRO A 328 ? 0.8527 1.6873 0.9020 0.5052  -0.2798 -0.2871 328 PRO A CD  
2170  N N   . GLU A 329 ? 0.9554 1.5574 0.8896 0.5659  -0.2476 -0.1740 329 GLU A N   
2171  C CA  . GLU A 329 ? 0.9840 1.5096 0.8808 0.5865  -0.2319 -0.1398 329 GLU A CA  
2172  C C   . GLU A 329 ? 0.9639 1.3982 0.8561 0.5625  -0.2185 -0.1102 329 GLU A C   
2173  O O   . GLU A 329 ? 0.9969 1.3511 0.8471 0.5777  -0.2013 -0.0790 329 GLU A O   
2174  C CB  . GLU A 329 ? 0.9711 1.5437 0.9031 0.5859  -0.2327 -0.1566 329 GLU A CB  
2175  C CG  . GLU A 329 ? 1.0051 1.6673 0.9370 0.6134  -0.2440 -0.1863 329 GLU A CG  
2176  C CD  . GLU A 329 ? 0.9626 1.7270 0.9580 0.5814  -0.2581 -0.2331 329 GLU A CD  
2177  O OE1 . GLU A 329 ? 0.9238 1.6863 0.9449 0.5477  -0.2612 -0.2404 329 GLU A OE1 
2178  O OE2 . GLU A 329 ? 0.9724 1.8179 0.9904 0.5889  -0.2643 -0.2641 329 GLU A OE2 
2179  N N   . LEU A 330 ? 0.9501 1.3937 0.8826 0.5250  -0.2246 -0.1211 330 LEU A N   
2180  C CA  . LEU A 330 ? 0.9669 1.3186 0.8893 0.4953  -0.2074 -0.0949 330 LEU A CA  
2181  C C   . LEU A 330 ? 1.0003 1.2764 0.8558 0.5222  -0.1982 -0.0623 330 LEU A C   
2182  O O   . LEU A 330 ? 1.0272 1.2167 0.8618 0.5029  -0.1776 -0.0370 330 LEU A O   
2183  C CB  . LEU A 330 ? 0.9619 1.3256 0.9302 0.4367  -0.2067 -0.1141 330 LEU A CB  
2184  C CG  . LEU A 330 ? 0.9377 1.3622 0.9700 0.4011  -0.2092 -0.1457 330 LEU A CG  
2185  C CD1 . LEU A 330 ? 0.9497 1.3486 1.0118 0.3437  -0.1995 -0.1534 330 LEU A CD1 
2186  C CD2 . LEU A 330 ? 0.9374 1.3476 0.9778 0.4069  -0.1998 -0.1372 330 LEU A CD2 
2187  N N   . GLY A 331 ? 1.0614 1.3618 0.8813 0.5522  -0.2050 -0.0648 331 GLY A N   
2188  C CA  . GLY A 331 ? 1.1084 1.3335 0.8595 0.5740  -0.1898 -0.0349 331 GLY A CA  
2189  C C   . GLY A 331 ? 1.1564 1.3116 0.8564 0.5994  -0.1679 -0.0077 331 GLY A C   
2190  O O   . GLY A 331 ? 1.2070 1.2887 0.8489 0.6126  -0.1495 0.0180  331 GLY A O   
2191  N N   . GLU A 332 ? 1.1340 1.3094 0.8533 0.6052  -0.1678 -0.0141 332 GLU A N   
2192  C CA  . GLU A 332 ? 1.1909 1.3017 0.8633 0.6284  -0.1469 0.0090  332 GLU A CA  
2193  C C   . GLU A 332 ? 1.1700 1.2111 0.8542 0.6004  -0.1291 0.0253  332 GLU A C   
2194  O O   . GLU A 332 ? 1.2088 1.1995 0.8630 0.6134  -0.1113 0.0405  332 GLU A O   
2195  C CB  . GLU A 332 ? 1.2105 1.3866 0.8896 0.6573  -0.1569 -0.0084 332 GLU A CB  
2196  C CG  . GLU A 332 ? 1.2115 1.4842 0.9037 0.6746  -0.1795 -0.0373 332 GLU A CG  
2197  C CD  . GLU A 332 ? 1.2898 1.5398 0.9119 0.7154  -0.1732 -0.0249 332 GLU A CD  
2198  O OE1 . GLU A 332 ? 1.3526 1.5191 0.9145 0.7365  -0.1508 0.0041  332 GLU A OE1 
2199  O OE2 . GLU A 332 ? 1.2923 1.6065 0.9185 0.7259  -0.1889 -0.0453 332 GLU A OE2 
2200  N N   . MET A 333 ? 1.1430 1.1810 0.8689 0.5630  -0.1329 0.0208  333 MET A N   
2201  C CA  . MET A 333 ? 1.1416 1.1139 0.8777 0.5355  -0.1153 0.0341  333 MET A CA  
2202  C C   . MET A 333 ? 1.1819 1.0591 0.8636 0.5302  -0.0906 0.0609  333 MET A C   
2203  O O   . MET A 333 ? 1.1851 1.0411 0.8745 0.4999  -0.0872 0.0628  333 MET A O   
2204  C CB  . MET A 333 ? 1.1165 1.1297 0.9199 0.4826  -0.1239 0.0127  333 MET A CB  
2205  C CG  . MET A 333 ? 1.0815 1.1988 0.9339 0.4874  -0.1480 -0.0185 333 MET A CG  
2206  S SD  . MET A 333 ? 1.0565 1.2307 0.9860 0.4263  -0.1557 -0.0492 333 MET A SD  
2207  C CE  . MET A 333 ? 1.0759 1.1630 1.0050 0.3808  -0.1325 -0.0302 333 MET A CE  
2208  N N   . GLU A 334 ? 1.2085 1.0307 0.8351 0.5531  -0.0699 0.0787  334 GLU A N   
2209  C CA  . GLU A 334 ? 1.2580 0.9988 0.8246 0.5549  -0.0447 0.1011  334 GLU A CA  
2210  C C   . GLU A 334 ? 1.2565 0.9296 0.8289 0.5145  -0.0245 0.1108  334 GLU A C   
2211  O O   . GLU A 334 ? 1.2808 0.9075 0.8225 0.5049  -0.0101 0.1223  334 GLU A O   
2212  C CB  . GLU A 334 ? 1.3354 1.0282 0.8439 0.5856  -0.0236 0.1158  334 GLU A CB  
2213  C CG  . GLU A 334 ? 1.3743 1.1238 0.8600 0.6314  -0.0391 0.1085  334 GLU A CG  
2214  C CD  . GLU A 334 ? 1.4316 1.1613 0.8856 0.6605  -0.0271 0.1143  334 GLU A CD  
2215  O OE1 . GLU A 334 ? 1.4011 1.1337 0.8881 0.6465  -0.0268 0.1093  334 GLU A OE1 
2216  O OE2 . GLU A 334 ? 1.5104 1.2214 0.9045 0.6992  -0.0177 0.1234  334 GLU A OE2 
2217  N N   . SER A 335 ? 1.1903 0.8575 0.8000 0.4909  -0.0218 0.1051  335 SER A N   
2218  C CA  . SER A 335 ? 1.2007 0.8104 0.8177 0.4480  -0.0007 0.1096  335 SER A CA  
2219  C C   . SER A 335 ? 1.1720 0.8297 0.8429 0.4027  -0.0151 0.0927  335 SER A C   
2220  O O   . SER A 335 ? 1.1738 0.8006 0.8576 0.3624  -0.0002 0.0919  335 SER A O   
2221  C CB  . SER A 335 ? 1.1977 0.7824 0.8297 0.4348  0.0124  0.1078  335 SER A CB  
2222  O OG  . SER A 335 ? 1.2327 0.7669 0.8149 0.4593  0.0331  0.1211  335 SER A OG  
2223  N N   . MET A 336 ? 1.0732 0.8054 0.7737 0.4094  -0.0423 0.0781  336 MET A N   
2224  C CA  . MET A 336 ? 1.0470 0.8240 0.7997 0.3682  -0.0553 0.0605  336 MET A CA  
2225  C C   . MET A 336 ? 1.0625 0.8014 0.8008 0.3426  -0.0427 0.0672  336 MET A C   
2226  O O   . MET A 336 ? 1.0868 0.8023 0.7835 0.3621  -0.0378 0.0784  336 MET A O   
2227  C CB  . MET A 336 ? 1.0249 0.8825 0.8040 0.3820  -0.0831 0.0422  336 MET A CB  
2228  C CG  . MET A 336 ? 1.0029 0.9028 0.8333 0.3413  -0.0944 0.0228  336 MET A CG  
2229  S SD  . MET A 336 ? 0.9903 0.8718 0.8590 0.2994  -0.0828 0.0190  336 MET A SD  
2230  C CE  . MET A 336 ? 0.9736 0.9048 0.8697 0.3165  -0.0933 0.0063  336 MET A CE  
2231  N N   . ILE A 337 ? 1.0291 0.7639 0.8007 0.3005  -0.0370 0.0599  337 ILE A N   
2232  C CA  . ILE A 337 ? 1.0388 0.7486 0.8056 0.2730  -0.0262 0.0620  337 ILE A CA  
2233  C C   . ILE A 337 ? 1.0121 0.7708 0.8234 0.2464  -0.0429 0.0453  337 ILE A C   
2234  O O   . ILE A 337 ? 1.0181 0.7842 0.8242 0.2412  -0.0468 0.0436  337 ILE A O   
2235  C CB  . ILE A 337 ? 1.0511 0.7066 0.8095 0.2490  -0.0002 0.0678  337 ILE A CB  
2236  C CG1 . ILE A 337 ? 1.0904 0.6805 0.7926 0.2723  0.0235  0.0857  337 ILE A CG1 
2237  C CG2 . ILE A 337 ? 1.0519 0.7035 0.8214 0.2155  0.0069  0.0625  337 ILE A CG2 
2238  C CD1 . ILE A 337 ? 1.1039 0.6417 0.7990 0.2484  0.0509  0.0874  337 ILE A CD1 
2239  N N   . ASP A 338 ? 0.9469 0.7354 0.7988 0.2305  -0.0509 0.0333  338 ASP A N   
2240  C CA  . ASP A 338 ? 0.9258 0.7510 0.8157 0.2057  -0.0626 0.0184  338 ASP A CA  
2241  C C   . ASP A 338 ? 0.9139 0.7908 0.8322 0.2135  -0.0799 0.0042  338 ASP A C   
2242  O O   . ASP A 338 ? 0.9052 0.7912 0.8415 0.2125  -0.0792 0.0006  338 ASP A O   
2243  C CB  . ASP A 338 ? 0.9115 0.7205 0.8205 0.1766  -0.0519 0.0165  338 ASP A CB  
2244  C CG  . ASP A 338 ? 0.8929 0.7292 0.8318 0.1552  -0.0607 0.0041  338 ASP A CG  
2245  O OD1 . ASP A 338 ? 0.8972 0.7558 0.8386 0.1579  -0.0717 -0.0025 338 ASP A OD1 
2246  O OD2 . ASP A 338 ? 0.8760 0.7092 0.8326 0.1371  -0.0556 0.0008  338 ASP A OD2 
2247  N N   . LEU A 339 ? 0.8746 0.7876 0.7983 0.2193  -0.0942 -0.0065 339 LEU A N   
2248  C CA  . LEU A 339 ? 0.8676 0.8374 0.8190 0.2248  -0.1097 -0.0252 339 LEU A CA  
2249  C C   . LEU A 339 ? 0.8677 0.8592 0.8480 0.1963  -0.1147 -0.0420 339 LEU A C   
2250  O O   . LEU A 339 ? 0.8750 0.8677 0.8457 0.1941  -0.1187 -0.0446 339 LEU A O   
2251  C CB  . LEU A 339 ? 0.8715 0.8702 0.8012 0.2600  -0.1219 -0.0270 339 LEU A CB  
2252  C CG  . LEU A 339 ? 0.8585 0.9284 0.8165 0.2694  -0.1391 -0.0508 339 LEU A CG  
2253  C CD1 . LEU A 339 ? 0.8484 0.9343 0.8334 0.2649  -0.1366 -0.0569 339 LEU A CD1 
2254  C CD2 . LEU A 339 ? 0.8572 0.9540 0.7853 0.3122  -0.1507 -0.0497 339 LEU A CD2 
2255  N N   . GLU A 340 ? 0.8300 0.8346 0.8424 0.1752  -0.1124 -0.0530 340 GLU A N   
2256  C CA  . GLU A 340 ? 0.8415 0.8522 0.8752 0.1475  -0.1114 -0.0666 340 GLU A CA  
2257  C C   . GLU A 340 ? 0.8492 0.9058 0.9162 0.1375  -0.1159 -0.0895 340 GLU A C   
2258  O O   . GLU A 340 ? 0.8460 0.9082 0.9292 0.1332  -0.1109 -0.0909 340 GLU A O   
2259  C CB  . GLU A 340 ? 0.8364 0.8059 0.8701 0.1278  -0.0982 -0.0561 340 GLU A CB  
2260  C CG  . GLU A 340 ? 0.8190 0.7497 0.8256 0.1355  -0.0907 -0.0365 340 GLU A CG  
2261  C CD  . GLU A 340 ? 0.8042 0.7073 0.8102 0.1170  -0.0812 -0.0317 340 GLU A CD  
2262  O OE1 . GLU A 340 ? 0.7934 0.6919 0.8138 0.1050  -0.0753 -0.0333 340 GLU A OE1 
2263  O OE2 . GLU A 340 ? 0.8019 0.6902 0.7916 0.1162  -0.0795 -0.0269 340 GLU A OE2 
2264  N N   . ILE A 341 ? 0.8626 0.9537 0.9400 0.1324  -0.1241 -0.1096 341 ILE A N   
2265  C CA  . ILE A 341 ? 0.8612 0.9985 0.9725 0.1159  -0.1253 -0.1373 341 ILE A CA  
2266  C C   . ILE A 341 ? 0.8751 1.0025 0.9945 0.0877  -0.1189 -0.1525 341 ILE A C   
2267  O O   . ILE A 341 ? 0.8593 1.0280 1.0007 0.0743  -0.1212 -0.1805 341 ILE A O   
2268  C CB  . ILE A 341 ? 0.8337 1.0363 0.9526 0.1397  -0.1413 -0.1543 341 ILE A CB  
2269  C CG1 . ILE A 341 ? 0.8209 1.0193 0.9209 0.1733  -0.1452 -0.1346 341 ILE A CG1 
2270  C CG2 . ILE A 341 ? 0.8177 1.0760 0.9768 0.1219  -0.1405 -0.1850 341 ILE A CG2 
2271  C CD1 . ILE A 341 ? 0.8082 1.0301 0.8816 0.2106  -0.1594 -0.1313 341 ILE A CD1 
2272  N N   . SER A 342 ? 0.8801 0.9538 0.9807 0.0789  -0.1100 -0.1362 342 SER A N   
2273  C CA  . SER A 342 ? 0.8780 0.9338 0.9782 0.0577  -0.1030 -0.1477 342 SER A CA  
2274  C C   . SER A 342 ? 0.8658 0.9191 0.9883 0.0292  -0.0881 -0.1648 342 SER A C   
2275  O O   . SER A 342 ? 0.8645 0.9231 1.0014 0.0248  -0.0819 -0.1635 342 SER A O   
2276  C CB  . SER A 342 ? 0.8846 0.8863 0.9586 0.0589  -0.0964 -0.1259 342 SER A CB  
2277  O OG  . SER A 342 ? 0.8957 0.8901 0.9499 0.0812  -0.1034 -0.1058 342 SER A OG  
2278  N N   . GLU A 343 ? 0.9202 0.9613 1.0427 0.0095  -0.0800 -0.1812 343 GLU A N   
2279  C CA  . GLU A 343 ? 0.9150 0.9334 1.0480 -0.0200 -0.0591 -0.1950 343 GLU A CA  
2280  C C   . GLU A 343 ? 0.9030 0.9681 1.0694 -0.0331 -0.0558 -0.2161 343 GLU A C   
2281  O O   . GLU A 343 ? 0.9045 0.9539 1.0773 -0.0413 -0.0433 -0.2095 343 GLU A O   
2282  C CB  . GLU A 343 ? 0.9208 0.8762 1.0319 -0.0207 -0.0445 -0.1702 343 GLU A CB  
2283  C CG  . GLU A 343 ? 0.9217 0.8475 1.0043 0.0001  -0.0523 -0.1459 343 GLU A CG  
2284  C CD  . GLU A 343 ? 0.9203 0.7889 0.9797 -0.0024 -0.0368 -0.1304 343 GLU A CD  
2285  O OE1 . GLU A 343 ? 0.9300 0.7690 0.9844 -0.0202 -0.0193 -0.1407 343 GLU A OE1 
2286  O OE2 . GLU A 343 ? 0.9090 0.7621 0.9531 0.0140  -0.0409 -0.1090 343 GLU A OE2 
2287  N N   . ASN A 344 ? 0.8659 0.9943 1.0538 -0.0332 -0.0677 -0.2430 344 ASN A N   
2288  C CA  . ASN A 344 ? 0.8448 1.0339 1.0682 -0.0432 -0.0674 -0.2684 344 ASN A CA  
2289  C C   . ASN A 344 ? 0.8201 1.0583 1.0660 -0.0645 -0.0669 -0.3096 344 ASN A C   
2290  O O   . ASN A 344 ? 0.8255 1.0366 1.0577 -0.0764 -0.0618 -0.3170 344 ASN A O   
2291  C CB  . ASN A 344 ? 0.8402 1.0748 1.0676 -0.0088 -0.0880 -0.2573 344 ASN A CB  
2292  C CG  . ASN A 344 ? 0.8540 1.0630 1.0805 -0.0039 -0.0802 -0.2354 344 ASN A CG  
2293  O OD1 . ASN A 344 ? 0.8441 1.0700 1.0948 -0.0228 -0.0678 -0.2498 344 ASN A OD1 
2294  N ND2 . ASN A 344 ? 0.8763 1.0451 1.0752 0.0195  -0.0857 -0.2024 344 ASN A ND2 
2295  N N   . LYS A 345 ? 0.7902 1.1037 1.0716 -0.0699 -0.0714 -0.3391 345 LYS A N   
2296  C CA  . LYS A 345 ? 0.7578 1.1350 1.0668 -0.0909 -0.0723 -0.3848 345 LYS A CA  
2297  C C   . LYS A 345 ? 0.7258 1.1973 1.0505 -0.0587 -0.1012 -0.4003 345 LYS A C   
2298  O O   . LYS A 345 ? 0.6988 1.2525 1.0604 -0.0708 -0.1038 -0.4409 345 LYS A O   
2299  C CB  . LYS A 345 ? 0.7456 1.1335 1.0866 -0.1350 -0.0455 -0.4163 345 LYS A CB  
2300  C CG  . LYS A 345 ? 0.7744 1.0650 1.0930 -0.1655 -0.0137 -0.4035 345 LYS A CG  
2301  C CD  . LYS A 345 ? 0.7723 1.0694 1.1187 -0.2116 0.0171  -0.4367 345 LYS A CD  
2302  C CE  . LYS A 345 ? 0.8071 0.9977 1.1217 -0.2365 0.0512  -0.4201 345 LYS A CE  
2303  N NZ  . LYS A 345 ? 0.8211 0.9496 1.1047 -0.2101 0.0500  -0.3716 345 LYS A NZ  
2304  N N   . LEU A 346 ? 0.7956 1.2570 1.0904 -0.0162 -0.1220 -0.3690 346 LEU A N   
2305  C CA  . LEU A 346 ? 0.7669 1.3074 1.0650 0.0221  -0.1486 -0.3784 346 LEU A CA  
2306  C C   . LEU A 346 ? 0.7437 1.3334 1.0458 0.0194  -0.1599 -0.4104 346 LEU A C   
2307  O O   . LEU A 346 ? 0.7595 1.3056 1.0510 -0.0046 -0.1495 -0.4146 346 LEU A O   
2308  C CB  . LEU A 346 ? 0.7914 1.2937 1.0495 0.0671  -0.1621 -0.3338 346 LEU A CB  
2309  C CG  . LEU A 346 ? 0.8128 1.2679 1.0611 0.0773  -0.1542 -0.3003 346 LEU A CG  
2310  C CD1 . LEU A 346 ? 0.8148 1.2738 1.0332 0.1271  -0.1712 -0.2739 346 LEU A CD1 
2311  C CD2 . LEU A 346 ? 0.7947 1.2881 1.0812 0.0581  -0.1442 -0.3209 346 LEU A CD2 
2312  N N   . THR A 347 ? 0.7883 1.4721 1.1042 0.0467  -0.1817 -0.4341 347 THR A N   
2313  C CA  . THR A 347 ? 0.7589 1.5072 1.0819 0.0471  -0.1951 -0.4701 347 THR A CA  
2314  C C   . THR A 347 ? 0.7417 1.5453 1.0411 0.1057  -0.2246 -0.4611 347 THR A C   
2315  O O   . THR A 347 ? 0.7474 1.5448 1.0296 0.1431  -0.2325 -0.4321 347 THR A O   
2316  C CB  . THR A 347 ? 0.7126 1.5450 1.0886 0.0088  -0.1876 -0.5289 347 THR A CB  
2317  O OG1 . THR A 347 ? 0.6822 1.5814 1.0865 0.0221  -0.1931 -0.5398 347 THR A OG1 
2318  C CG2 . THR A 347 ? 0.7322 1.4989 1.1219 -0.0508 -0.1543 -0.5399 347 THR A CG2 
2319  N N   . GLY A 348 ? 0.7613 1.6152 1.0561 0.1149  -0.2394 -0.4861 348 GLY A N   
2320  C CA  . GLY A 348 ? 0.7421 1.6566 1.0127 0.1714  -0.2655 -0.4832 348 GLY A CA  
2321  C C   . GLY A 348 ? 0.7797 1.6232 0.9918 0.2090  -0.2730 -0.4356 348 GLY A C   
2322  O O   . GLY A 348 ? 0.8220 1.5706 1.0138 0.1892  -0.2573 -0.4060 348 GLY A O   
2323  N N   . PRO A 349 ? 0.7537 1.6319 0.9327 0.2635  -0.2901 -0.4246 349 PRO A N   
2324  C CA  . PRO A 349 ? 0.7687 1.5865 0.8897 0.3013  -0.2975 -0.3826 349 PRO A CA  
2325  C C   . PRO A 349 ? 0.7685 1.5137 0.8605 0.3241  -0.2886 -0.3347 349 PRO A C   
2326  O O   . PRO A 349 ? 0.7589 1.5218 0.8716 0.3270  -0.2861 -0.3354 349 PRO A O   
2327  C CB  . PRO A 349 ? 0.8140 1.6806 0.9065 0.3442  -0.3045 -0.3891 349 PRO A CB  
2328  C CG  . PRO A 349 ? 0.8216 1.7625 0.9462 0.3491  -0.3034 -0.4165 349 PRO A CG  
2329  C CD  . PRO A 349 ? 0.7839 1.7432 0.9697 0.2902  -0.2934 -0.4479 349 PRO A CD  
2330  N N   . VAL A 350 ? 0.8323 1.4949 0.8763 0.3381  -0.2820 -0.2947 350 VAL A N   
2331  C CA  . VAL A 350 ? 0.8429 1.4347 0.8506 0.3637  -0.2725 -0.2497 350 VAL A CA  
2332  C C   . VAL A 350 ? 0.8847 1.5132 0.8524 0.4279  -0.2879 -0.2401 350 VAL A C   
2333  O O   . VAL A 350 ? 0.9173 1.5648 0.8561 0.4495  -0.2933 -0.2448 350 VAL A O   
2334  C CB  . VAL A 350 ? 0.8442 1.3380 0.8176 0.3510  -0.2569 -0.2148 350 VAL A CB  
2335  C CG1 . VAL A 350 ? 0.8611 1.2841 0.7963 0.3753  -0.2450 -0.1724 350 VAL A CG1 
2336  C CG2 . VAL A 350 ? 0.8216 1.2798 0.8301 0.2942  -0.2420 -0.2234 350 VAL A CG2 
2337  N N   . PRO A 351 ? 0.8803 1.5023 0.8407 0.4521  -0.2838 -0.2252 351 PRO A N   
2338  C CA  . PRO A 351 ? 0.9393 1.5655 0.8515 0.5019  -0.2813 -0.2128 351 PRO A CA  
2339  C C   . PRO A 351 ? 0.9828 1.5282 0.8263 0.5305  -0.2715 -0.1730 351 PRO A C   
2340  O O   . PRO A 351 ? 0.9706 1.4393 0.7985 0.5185  -0.2617 -0.1439 351 PRO A O   
2341  C CB  . PRO A 351 ? 0.9392 1.5586 0.8593 0.5124  -0.2748 -0.2033 351 PRO A CB  
2342  C CG  . PRO A 351 ? 0.8766 1.5224 0.8638 0.4655  -0.2773 -0.2250 351 PRO A CG  
2343  C CD  . PRO A 351 ? 0.8495 1.4500 0.8430 0.4270  -0.2726 -0.2209 351 PRO A CD  
2344  N N   . ASP A 352 ? 1.0581 1.6222 0.8595 0.5691  -0.2722 -0.1734 352 ASP A N   
2345  C CA  . ASP A 352 ? 1.1121 1.5996 0.8430 0.5997  -0.2587 -0.1364 352 ASP A CA  
2346  C C   . ASP A 352 ? 1.1402 1.5481 0.8340 0.6167  -0.2400 -0.0996 352 ASP A C   
2347  O O   . ASP A 352 ? 1.1777 1.5036 0.8185 0.6286  -0.2228 -0.0663 352 ASP A O   
2348  C CB  . ASP A 352 ? 1.1719 1.7007 0.8653 0.6415  -0.2623 -0.1468 352 ASP A CB  
2349  C CG  . ASP A 352 ? 1.1489 1.7701 0.8843 0.6263  -0.2799 -0.1902 352 ASP A CG  
2350  O OD1 . ASP A 352 ? 1.1330 1.8349 0.9123 0.6206  -0.2900 -0.2248 352 ASP A OD1 
2351  O OD2 . ASP A 352 ? 1.1493 1.7621 0.8741 0.6186  -0.2820 -0.1911 352 ASP A OD2 
2352  N N   . SER A 353 ? 1.0944 1.5241 0.8150 0.6161  -0.2409 -0.1066 353 SER A N   
2353  C CA  . SER A 353 ? 1.1212 1.4776 0.8103 0.6298  -0.2225 -0.0751 353 SER A CA  
2354  C C   . SER A 353 ? 1.0948 1.3651 0.7821 0.6004  -0.2080 -0.0477 353 SER A C   
2355  O O   . SER A 353 ? 1.1276 1.3214 0.7784 0.6100  -0.1875 -0.0188 353 SER A O   
2356  C CB  . SER A 353 ? 1.1020 1.5084 0.8296 0.6298  -0.2284 -0.0927 353 SER A CB  
2357  O OG  . SER A 353 ? 1.0278 1.4739 0.8255 0.5863  -0.2389 -0.1147 353 SER A OG  
2358  N N   . PHE A 354 ? 1.0607 1.3412 0.7847 0.5648  -0.2169 -0.0579 354 PHE A N   
2359  C CA  . PHE A 354 ? 1.0553 1.2571 0.7748 0.5394  -0.2032 -0.0338 354 PHE A CA  
2360  C C   . PHE A 354 ? 1.1038 1.2222 0.7550 0.5560  -0.1819 -0.0013 354 PHE A C   
2361  O O   . PHE A 354 ? 1.1237 1.1658 0.7609 0.5381  -0.1631 0.0216  354 PHE A O   
2362  C CB  . PHE A 354 ? 1.0434 1.2681 0.8122 0.4874  -0.2086 -0.0555 354 PHE A CB  
2363  C CG  . PHE A 354 ? 1.0199 1.2779 0.8532 0.4470  -0.2107 -0.0779 354 PHE A CG  
2364  C CD1 . PHE A 354 ? 0.9893 1.3209 0.8532 0.4612  -0.2248 -0.1011 354 PHE A CD1 
2365  C CD2 . PHE A 354 ? 1.0292 1.2466 0.8905 0.3966  -0.1976 -0.0764 354 PHE A CD2 
2366  C CE1 . PHE A 354 ? 0.9722 1.3312 0.8930 0.4224  -0.2234 -0.1217 354 PHE A CE1 
2367  C CE2 . PHE A 354 ? 1.0138 1.2556 0.9278 0.3617  -0.1970 -0.0951 354 PHE A CE2 
2368  C CZ  . PHE A 354 ? 0.9872 1.2974 0.9308 0.3729  -0.2088 -0.1174 354 PHE A CZ  
2369  N N   . GLY A 355 ? 1.1652 1.2971 0.7743 0.5877  -0.1820 -0.0010 355 GLY A N   
2370  C CA  . GLY A 355 ? 1.2244 1.2764 0.7651 0.6061  -0.1581 0.0291  355 GLY A CA  
2371  C C   . GLY A 355 ? 1.2735 1.2536 0.7742 0.6215  -0.1326 0.0543  355 GLY A C   
2372  O O   . GLY A 355 ? 1.3245 1.2233 0.7727 0.6258  -0.1065 0.0802  355 GLY A O   
2373  N N   . LYS A 356 ? 1.2391 1.2475 0.7630 0.6285  -0.1378 0.0457  356 LYS A N   
2374  C CA  . LYS A 356 ? 1.2851 1.2270 0.7747 0.6408  -0.1140 0.0670  356 LYS A CA  
2375  C C   . LYS A 356 ? 1.2521 1.1308 0.7612 0.6034  -0.0982 0.0807  356 LYS A C   
2376  O O   . LYS A 356 ? 1.2944 1.1033 0.7704 0.6070  -0.0730 0.0998  356 LYS A O   
2377  C CB  . LYS A 356 ? 1.2910 1.2908 0.7961 0.6650  -0.1260 0.0513  356 LYS A CB  
2378  C CG  . LYS A 356 ? 1.3617 1.3895 0.8193 0.7139  -0.1278 0.0477  356 LYS A CG  
2379  C CD  . LYS A 356 ? 1.3545 1.4611 0.8400 0.7335  -0.1451 0.0244  356 LYS A CD  
2380  C CE  . LYS A 356 ? 1.3107 1.5278 0.8446 0.7302  -0.1747 -0.0121 356 LYS A CE  
2381  N NZ  . LYS A 356 ? 1.2818 1.5798 0.8629 0.7319  -0.1910 -0.0395 356 LYS A NZ  
2382  N N   . LEU A 357 ? 1.2097 1.1123 0.7709 0.5684  -0.1115 0.0693  357 LEU A N   
2383  C CA  . LEU A 357 ? 1.2001 1.0469 0.7806 0.5335  -0.0970 0.0796  357 LEU A CA  
2384  C C   . LEU A 357 ? 1.2417 1.0070 0.7766 0.5224  -0.0716 0.1017  357 LEU A C   
2385  O O   . LEU A 357 ? 1.2409 1.0134 0.7925 0.4933  -0.0740 0.0956  357 LEU A O   
2386  C CB  . LEU A 357 ? 1.1642 1.0686 0.8178 0.4884  -0.1141 0.0539  357 LEU A CB  
2387  C CG  . LEU A 357 ? 1.1249 1.1225 0.8263 0.4962  -0.1406 0.0261  357 LEU A CG  
2388  C CD1 . LEU A 357 ? 1.1000 1.1361 0.8677 0.4431  -0.1484 0.0023  357 LEU A CD1 
2389  C CD2 . LEU A 357 ? 1.1208 1.1165 0.8186 0.5215  -0.1375 0.0306  357 LEU A CD2 
2390  N N   . THR A 358 ? 1.2426 0.9353 0.7251 0.5336  -0.0419 0.1221  358 THR A N   
2391  C CA  . THR A 358 ? 1.2888 0.9048 0.7225 0.5246  -0.0133 0.1413  358 THR A CA  
2392  C C   . THR A 358 ? 1.2888 0.8496 0.7391 0.4819  0.0057  0.1470  358 THR A C   
2393  O O   . THR A 358 ? 1.3222 0.8322 0.7443 0.4643  0.0282  0.1570  358 THR A O   
2394  C CB  . THR A 358 ? 1.3616 0.9181 0.7297 0.5519  0.0150  0.1584  358 THR A CB  
2395  O OG1 . THR A 358 ? 1.3771 0.8727 0.7414 0.5335  0.0403  0.1666  358 THR A OG1 
2396  C CG2 . THR A 358 ? 1.3864 0.9989 0.7434 0.5960  -0.0030 0.1503  358 THR A CG2 
2397  N N   . ALA A 359 ? 1.2246 0.8068 0.7283 0.4525  0.0007  0.1338  359 ALA A N   
2398  C CA  . ALA A 359 ? 1.2171 0.7652 0.7466 0.4012  0.0203  0.1305  359 ALA A CA  
2399  C C   . ALA A 359 ? 1.1695 0.7820 0.7683 0.3613  -0.0007 0.1080  359 ALA A C   
2400  O O   . ALA A 359 ? 1.1595 0.7608 0.7887 0.3226  0.0093  0.1014  359 ALA A O   
2401  C CB  . ALA A 359 ? 1.2269 0.7312 0.7517 0.3990  0.0385  0.1359  359 ALA A CB  
2402  N N   . LEU A 360 ? 1.1145 0.7931 0.7359 0.3710  -0.0284 0.0951  360 LEU A N   
2403  C CA  . LEU A 360 ? 1.0784 0.8129 0.7608 0.3369  -0.0468 0.0738  360 LEU A CA  
2404  C C   . LEU A 360 ? 1.0879 0.8051 0.7763 0.3028  -0.0366 0.0724  360 LEU A C   
2405  O O   . LEU A 360 ? 1.1157 0.8125 0.7693 0.3114  -0.0292 0.0808  360 LEU A O   
2406  C CB  . LEU A 360 ? 1.0564 0.8628 0.7578 0.3558  -0.0757 0.0578  360 LEU A CB  
2407  C CG  . LEU A 360 ? 1.0249 0.8855 0.7851 0.3229  -0.0926 0.0344  360 LEU A CG  
2408  C CD1 . LEU A 360 ? 1.0019 0.8804 0.8006 0.3103  -0.0954 0.0255  360 LEU A CD1 
2409  C CD2 . LEU A 360 ? 1.0140 0.9365 0.7835 0.3378  -0.1156 0.0174  360 LEU A CD2 
2410  N N   . GLU A 361 ? 1.0551 0.7825 0.7858 0.2663  -0.0360 0.0615  361 GLU A N   
2411  C CA  . GLU A 361 ? 1.0593 0.7803 0.8010 0.2355  -0.0285 0.0572  361 GLU A CA  
2412  C C   . GLU A 361 ? 1.0286 0.8000 0.8143 0.2172  -0.0482 0.0393  361 GLU A C   
2413  O O   . GLU A 361 ? 1.0353 0.8162 0.8204 0.2092  -0.0511 0.0349  361 GLU A O   
2414  C CB  . GLU A 361 ? 1.0657 0.7482 0.8106 0.2095  -0.0057 0.0601  361 GLU A CB  
2415  C CG  . GLU A 361 ? 1.1035 0.7241 0.8015 0.2215  0.0206  0.0764  361 GLU A CG  
2416  C CD  . GLU A 361 ? 1.1175 0.7030 0.8178 0.1889  0.0464  0.0742  361 GLU A CD  
2417  O OE1 . GLU A 361 ? 1.0982 0.7131 0.8350 0.1606  0.0417  0.0606  361 GLU A OE1 
2418  O OE2 . GLU A 361 ? 1.1488 0.6778 0.8129 0.1923  0.0724  0.0848  361 GLU A OE2 
2419  N N   . TRP A 362 ? 0.9758 0.7761 0.7972 0.2105  -0.0596 0.0288  362 TRP A N   
2420  C CA  . TRP A 362 ? 0.9534 0.7936 0.8118 0.1940  -0.0748 0.0120  362 TRP A CA  
2421  C C   . TRP A 362 ? 0.9455 0.8291 0.8185 0.2102  -0.0928 0.0006  362 TRP A C   
2422  O O   . TRP A 362 ? 0.9402 0.8297 0.8162 0.2232  -0.0940 0.0021  362 TRP A O   
2423  C CB  . TRP A 362 ? 0.9310 0.7681 0.8193 0.1685  -0.0695 0.0070  362 TRP A CB  
2424  C CG  . TRP A 362 ? 0.9339 0.7431 0.8160 0.1504  -0.0539 0.0119  362 TRP A CG  
2425  C CD1 . TRP A 362 ? 0.9269 0.7432 0.8192 0.1341  -0.0540 0.0054  362 TRP A CD1 
2426  C CD2 . TRP A 362 ? 0.9480 0.7218 0.8137 0.1464  -0.0351 0.0213  362 TRP A CD2 
2427  N NE1 . TRP A 362 ? 0.9359 0.7318 0.8217 0.1209  -0.0381 0.0087  362 TRP A NE1 
2428  C CE2 . TRP A 362 ? 0.9510 0.7197 0.8213 0.1255  -0.0253 0.0174  362 TRP A CE2 
2429  C CE3 . TRP A 362 ? 0.9619 0.7074 0.8080 0.1588  -0.0242 0.0312  362 TRP A CE3 
2430  C CZ2 . TRP A 362 ? 0.9703 0.7114 0.8300 0.1127  -0.0049 0.0201  362 TRP A CZ2 
2431  C CZ3 . TRP A 362 ? 0.9800 0.6882 0.8117 0.1460  -0.0021 0.0359  362 TRP A CZ3 
2432  C CH2 . TRP A 362 ? 0.9846 0.6934 0.8252 0.1212  0.0075  0.0289  362 TRP A CH2 
2433  N N   . LEU A 363 ? 0.8787 0.7957 0.7619 0.2087  -0.1061 -0.0134 363 LEU A N   
2434  C CA  . LEU A 363 ? 0.8721 0.8403 0.7765 0.2171  -0.1226 -0.0315 363 LEU A CA  
2435  C C   . LEU A 363 ? 0.8718 0.8606 0.8080 0.1899  -0.1274 -0.0506 363 LEU A C   
2436  O O   . LEU A 363 ? 0.8818 0.8738 0.8118 0.1852  -0.1306 -0.0566 363 LEU A O   
2437  C CB  . LEU A 363 ? 0.8796 0.8718 0.7576 0.2480  -0.1336 -0.0328 363 LEU A CB  
2438  C CG  . LEU A 363 ? 0.8658 0.9224 0.7668 0.2593  -0.1516 -0.0556 363 LEU A CG  
2439  C CD1 . LEU A 363 ? 0.8547 0.9224 0.7635 0.2738  -0.1517 -0.0532 363 LEU A CD1 
2440  C CD2 . LEU A 363 ? 0.8679 0.9547 0.7427 0.2888  -0.1642 -0.0603 363 LEU A CD2 
2441  N N   . PHE A 364 ? 0.8445 0.8436 0.8114 0.1728  -0.1258 -0.0601 364 PHE A N   
2442  C CA  . PHE A 364 ? 0.8563 0.8638 0.8489 0.1465  -0.1251 -0.0768 364 PHE A CA  
2443  C C   . PHE A 364 ? 0.8571 0.9165 0.8752 0.1445  -0.1351 -0.1018 364 PHE A C   
2444  O O   . PHE A 364 ? 0.8491 0.9277 0.8865 0.1439  -0.1348 -0.1071 364 PHE A O   
2445  C CB  . PHE A 364 ? 0.8535 0.8319 0.8584 0.1276  -0.1128 -0.0699 364 PHE A CB  
2446  C CG  . PHE A 364 ? 0.8456 0.7860 0.8356 0.1194  -0.1037 -0.0575 364 PHE A CG  
2447  C CD1 . PHE A 364 ? 0.8288 0.7458 0.7958 0.1296  -0.0983 -0.0405 364 PHE A CD1 
2448  C CD2 . PHE A 364 ? 0.8540 0.7821 0.8517 0.1018  -0.0986 -0.0641 364 PHE A CD2 
2449  C CE1 . PHE A 364 ? 0.8170 0.7092 0.7745 0.1208  -0.0898 -0.0334 364 PHE A CE1 
2450  C CE2 . PHE A 364 ? 0.8304 0.7316 0.8147 0.0982  -0.0915 -0.0545 364 PHE A CE2 
2451  C CZ  . PHE A 364 ? 0.8129 0.7013 0.7799 0.1069  -0.0880 -0.0406 364 PHE A CZ  
2452  N N   . LEU A 365 ? 0.8433 0.9289 0.8627 0.1428  -0.1432 -0.1194 365 LEU A N   
2453  C CA  . LEU A 365 ? 0.8306 0.9711 0.8779 0.1350  -0.1510 -0.1497 365 LEU A CA  
2454  C C   . LEU A 365 ? 0.8368 0.9720 0.8982 0.1052  -0.1445 -0.1700 365 LEU A C   
2455  O O   . LEU A 365 ? 0.8183 0.9990 0.9009 0.0948  -0.1493 -0.1998 365 LEU A O   
2456  C CB  . LEU A 365 ? 0.8110 1.0018 0.8473 0.1640  -0.1680 -0.1592 365 LEU A CB  
2457  C CG  . LEU A 365 ? 0.7986 0.9989 0.8152 0.2003  -0.1745 -0.1423 365 LEU A CG  
2458  C CD1 . LEU A 365 ? 0.7855 1.0290 0.7817 0.2322  -0.1906 -0.1503 365 LEU A CD1 
2459  C CD2 . LEU A 365 ? 0.7835 1.0143 0.8279 0.1994  -0.1746 -0.1516 365 LEU A CD2 
2460  N N   . ARG A 366 ? 0.8923 0.9741 0.9414 0.0919  -0.1328 -0.1564 366 ARG A N   
2461  C CA  . ARG A 366 ? 0.8902 0.9556 0.9429 0.0689  -0.1247 -0.1723 366 ARG A CA  
2462  C C   . ARG A 366 ? 0.8786 0.9478 0.9585 0.0413  -0.1124 -0.1921 366 ARG A C   
2463  O O   . ARG A 366 ? 0.8758 0.9512 0.9707 0.0388  -0.1085 -0.1884 366 ARG A O   
2464  C CB  . ARG A 366 ? 0.9019 0.9109 0.9314 0.0678  -0.1152 -0.1512 366 ARG A CB  
2465  C CG  . ARG A 366 ? 0.9026 0.8792 0.9302 0.0675  -0.1058 -0.1295 366 ARG A CG  
2466  C CD  . ARG A 366 ? 0.8960 0.8284 0.9027 0.0674  -0.0975 -0.1141 366 ARG A CD  
2467  N NE  . ARG A 366 ? 0.8921 0.8039 0.8952 0.0532  -0.0892 -0.1273 366 ARG A NE  
2468  C CZ  . ARG A 366 ? 0.8883 0.7795 0.8993 0.0355  -0.0757 -0.1360 366 ARG A CZ  
2469  N NH1 . ARG A 366 ? 0.8826 0.7755 0.9083 0.0288  -0.0701 -0.1333 366 ARG A NH1 
2470  N NH2 . ARG A 366 ? 0.8957 0.7599 0.8966 0.0247  -0.0656 -0.1473 366 ARG A NH2 
2471  N N   . ASP A 367 ? 0.9575 1.0199 1.0417 0.0197  -0.1042 -0.2142 367 ASP A N   
2472  C CA  . ASP A 367 ? 0.9504 1.0052 1.0549 -0.0112 -0.0865 -0.2352 367 ASP A CA  
2473  C C   . ASP A 367 ? 0.9301 1.0485 1.0685 -0.0172 -0.0916 -0.2579 367 ASP A C   
2474  O O   . ASP A 367 ? 0.9278 1.0439 1.0806 -0.0252 -0.0828 -0.2543 367 ASP A O   
2475  C CB  . ASP A 367 ? 0.9607 0.9536 1.0532 -0.0186 -0.0684 -0.2132 367 ASP A CB  
2476  C CG  . ASP A 367 ? 0.9611 0.9274 1.0621 -0.0504 -0.0446 -0.2322 367 ASP A CG  
2477  O OD1 . ASP A 367 ? 0.9490 0.9576 1.0786 -0.0696 -0.0414 -0.2608 367 ASP A OD1 
2478  O OD2 . ASP A 367 ? 0.9728 0.8763 1.0500 -0.0557 -0.0277 -0.2197 367 ASP A OD2 
2479  N N   . ASN A 368 ? 0.9187 1.0990 1.0692 -0.0110 -0.1069 -0.2824 368 ASN A N   
2480  C CA  . ASN A 368 ? 0.8898 1.1446 1.0744 -0.0150 -0.1137 -0.3109 368 ASN A CA  
2481  C C   . ASN A 368 ? 0.8664 1.1720 1.0662 -0.0295 -0.1182 -0.3518 368 ASN A C   
2482  O O   . ASN A 368 ? 0.8774 1.1492 1.0621 -0.0421 -0.1113 -0.3578 368 ASN A O   
2483  C CB  . ASN A 368 ? 0.8842 1.1782 1.0647 0.0237  -0.1343 -0.2936 368 ASN A CB  
2484  C CG  . ASN A 368 ? 0.8889 1.1732 1.0804 0.0247  -0.1271 -0.2784 368 ASN A CG  
2485  O OD1 . ASN A 368 ? 0.8682 1.1941 1.0916 0.0088  -0.1219 -0.3018 368 ASN A OD1 
2486  N ND2 . ASN A 368 ? 0.9147 1.1462 1.0808 0.0418  -0.1257 -0.2412 368 ASN A ND2 
2487  N N   . GLN A 369 ? 0.9061 1.2967 1.1363 -0.0272 -0.1297 -0.3824 369 GLN A N   
2488  C CA  . GLN A 369 ? 0.8757 1.3313 1.1248 -0.0399 -0.1363 -0.4270 369 GLN A CA  
2489  C C   . GLN A 369 ? 0.8495 1.3864 1.0969 0.0016  -0.1665 -0.4331 369 GLN A C   
2490  O O   . GLN A 369 ? 0.8088 1.4336 1.0847 -0.0023 -0.1764 -0.4751 369 GLN A O   
2491  C CB  . GLN A 369 ? 0.8481 1.3417 1.1398 -0.0826 -0.1183 -0.4702 369 GLN A CB  
2492  C CG  . GLN A 369 ? 0.8725 1.2865 1.1632 -0.1161 -0.0867 -0.4576 369 GLN A CG  
2493  C CD  . GLN A 369 ? 0.8602 1.2716 1.1732 -0.1678 -0.0594 -0.5008 369 GLN A CD  
2494  O OE1 . GLN A 369 ? 0.8838 1.2225 1.1741 -0.1883 -0.0399 -0.4983 369 GLN A OE1 
2495  N NE2 . GLN A 369 ? 0.8226 1.3128 1.1792 -0.1893 -0.0560 -0.5421 369 GLN A NE2 
2496  N N   . LEU A 370 ? 0.8127 1.3213 1.0248 0.0423  -0.1800 -0.3925 370 LEU A N   
2497  C CA  . LEU A 370 ? 0.8166 1.3872 1.0148 0.0874  -0.2059 -0.3920 370 LEU A CA  
2498  C C   . LEU A 370 ? 0.8347 1.4328 1.0215 0.0903  -0.2164 -0.4137 370 LEU A C   
2499  O O   . LEU A 370 ? 0.8423 1.3900 1.0203 0.0649  -0.2040 -0.4154 370 LEU A O   
2500  C CB  . LEU A 370 ? 0.8120 1.3301 0.9701 0.1258  -0.2110 -0.3417 370 LEU A CB  
2501  C CG  . LEU A 370 ? 0.8339 1.2934 0.9934 0.1174  -0.1957 -0.3125 370 LEU A CG  
2502  C CD1 . LEU A 370 ? 0.8566 1.2722 0.9763 0.1551  -0.2004 -0.2689 370 LEU A CD1 
2503  C CD2 . LEU A 370 ? 0.8048 1.3208 1.0025 0.1095  -0.1949 -0.3348 370 LEU A CD2 
2504  N N   . SER A 371 ? 0.8259 1.5057 1.0103 0.1245  -0.2395 -0.4307 371 SER A N   
2505  C CA  . SER A 371 ? 0.8082 1.5345 0.9879 0.1270  -0.2514 -0.4605 371 SER A CA  
2506  C C   . SER A 371 ? 0.7982 1.5691 0.9434 0.1856  -0.2767 -0.4473 371 SER A C   
2507  O O   . SER A 371 ? 0.8016 1.5690 0.9285 0.2226  -0.2835 -0.4185 371 SER A O   
2508  C CB  . SER A 371 ? 0.7661 1.5762 0.9955 0.0921  -0.2500 -0.5212 371 SER A CB  
2509  O OG  . SER A 371 ? 0.7476 1.6315 1.0009 0.1110  -0.2558 -0.5326 371 SER A OG  
2510  N N   . GLY A 372 ? 0.8212 1.6276 0.9534 0.1948  -0.2878 -0.4674 372 GLY A N   
2511  C CA  . GLY A 372 ? 0.8374 1.6708 0.9318 0.2486  -0.3006 -0.4506 372 GLY A CA  
2512  C C   . GLY A 372 ? 0.8565 1.6189 0.8945 0.2761  -0.3057 -0.4079 372 GLY A C   
2513  O O   . GLY A 372 ? 0.8890 1.5697 0.9197 0.2493  -0.2901 -0.3869 372 GLY A O   
2514  N N   . PRO A 373 ? 0.8855 1.6560 0.8815 0.3267  -0.3124 -0.3857 373 PRO A N   
2515  C CA  . PRO A 373 ? 0.9087 1.6089 0.8473 0.3542  -0.3125 -0.3429 373 PRO A CA  
2516  C C   . PRO A 373 ? 0.9304 1.5698 0.8453 0.3730  -0.3066 -0.2998 373 PRO A C   
2517  O O   . PRO A 373 ? 0.9151 1.5779 0.8468 0.3828  -0.3079 -0.2997 373 PRO A O   
2518  C CB  . PRO A 373 ? 0.9473 1.6829 0.8521 0.3985  -0.3167 -0.3414 373 PRO A CB  
2519  C CG  . PRO A 373 ? 0.9578 1.7684 0.8906 0.4122  -0.3200 -0.3656 373 PRO A CG  
2520  C CD  . PRO A 373 ? 0.9179 1.7613 0.9146 0.3612  -0.3174 -0.4009 373 PRO A CD  
2521  N N   . ILE A 374 ? 0.9803 1.5326 0.8577 0.3735  -0.2923 -0.2615 374 ILE A N   
2522  C CA  . ILE A 374 ? 1.0081 1.4872 0.8596 0.3861  -0.2777 -0.2179 374 ILE A CA  
2523  C C   . ILE A 374 ? 1.0116 1.4993 0.8103 0.4463  -0.2858 -0.1964 374 ILE A C   
2524  O O   . ILE A 374 ? 1.0233 1.5083 0.7815 0.4713  -0.2875 -0.1895 374 ILE A O   
2525  C CB  . ILE A 374 ? 1.0470 1.4366 0.8801 0.3622  -0.2580 -0.1896 374 ILE A CB  
2526  C CG1 . ILE A 374 ? 1.0494 1.4137 0.9284 0.3099  -0.2458 -0.2003 374 ILE A CG1 
2527  C CG2 . ILE A 374 ? 1.0748 1.3954 0.8677 0.3842  -0.2436 -0.1461 374 ILE A CG2 
2528  C CD1 . ILE A 374 ? 1.0366 1.4101 0.9482 0.2995  -0.2426 -0.2028 374 ILE A CD1 
2529  N N   . PRO A 375 ? 1.0271 1.5171 0.8230 0.4691  -0.2850 -0.1843 375 PRO A N   
2530  C CA  . PRO A 375 ? 1.0588 1.5241 0.8001 0.5166  -0.2753 -0.1580 375 PRO A CA  
2531  C C   . PRO A 375 ? 1.0954 1.4644 0.7821 0.5265  -0.2579 -0.1145 375 PRO A C   
2532  O O   . PRO A 375 ? 1.1055 1.4176 0.8023 0.4985  -0.2470 -0.0977 375 PRO A O   
2533  C CB  . PRO A 375 ? 1.0512 1.5313 0.8097 0.5269  -0.2736 -0.1574 375 PRO A CB  
2534  C CG  . PRO A 375 ? 1.0038 1.5399 0.8319 0.4862  -0.2849 -0.1920 375 PRO A CG  
2535  C CD  . PRO A 375 ? 1.0096 1.5132 0.8539 0.4441  -0.2821 -0.1950 375 PRO A CD  
2536  N N   . PRO A 376 ? 1.1275 1.4717 0.7582 0.5603  -0.2485 -0.0972 376 PRO A N   
2537  C CA  . PRO A 376 ? 1.1666 1.4167 0.7436 0.5666  -0.2269 -0.0574 376 PRO A CA  
2538  C C   . PRO A 376 ? 1.1811 1.3648 0.7436 0.5686  -0.2088 -0.0284 376 PRO A C   
2539  O O   . PRO A 376 ? 1.2056 1.3107 0.7387 0.5594  -0.1896 0.0001  376 PRO A O   
2540  C CB  . PRO A 376 ? 1.2244 1.4719 0.7461 0.6073  -0.2195 -0.0494 376 PRO A CB  
2541  C CG  . PRO A 376 ? 1.2149 1.5599 0.7685 0.6132  -0.2415 -0.0892 376 PRO A CG  
2542  C CD  . PRO A 376 ? 1.1661 1.5678 0.7801 0.5933  -0.2554 -0.1152 376 PRO A CD  
2543  N N   . GLY A 377 ? 1.1845 1.3979 0.7673 0.5789  -0.2130 -0.0366 377 GLY A N   
2544  C CA  . GLY A 377 ? 1.1975 1.3493 0.7687 0.5796  -0.1955 -0.0117 377 GLY A CA  
2545  C C   . GLY A 377 ? 1.1775 1.2975 0.7859 0.5396  -0.1933 -0.0068 377 GLY A C   
2546  O O   . GLY A 377 ? 1.1974 1.2507 0.7923 0.5330  -0.1723 0.0162  377 GLY A O   
2547  N N   . ILE A 378 ? 1.1229 1.2819 0.7846 0.4970  -0.2030 -0.0330 378 ILE A N   
2548  C CA  . ILE A 378 ? 1.1227 1.2483 0.8271 0.4447  -0.1902 -0.0338 378 ILE A CA  
2549  C C   . ILE A 378 ? 1.1588 1.1982 0.8304 0.4307  -0.1648 -0.0047 378 ILE A C   
2550  O O   . ILE A 378 ? 1.1663 1.1574 0.8445 0.4116  -0.1477 0.0091  378 ILE A O   
2551  C CB  . ILE A 378 ? 1.1019 1.2761 0.8585 0.4061  -0.2023 -0.0655 378 ILE A CB  
2552  C CG1 . ILE A 378 ? 1.0654 1.3240 0.8632 0.4098  -0.2224 -0.0982 378 ILE A CG1 
2553  C CG2 . ILE A 378 ? 1.1085 1.2388 0.8969 0.3583  -0.1871 -0.0617 378 ILE A CG2 
2554  C CD1 . ILE A 378 ? 1.0508 1.3377 0.9048 0.3618  -0.2251 -0.1274 378 ILE A CD1 
2555  N N   . ALA A 379 ? 1.1801 1.2027 0.8166 0.4389  -0.1612 0.0026  379 ALA A N   
2556  C CA  . ALA A 379 ? 1.2156 1.1652 0.8236 0.4224  -0.1362 0.0254  379 ALA A CA  
2557  C C   . ALA A 379 ? 1.2538 1.1425 0.7942 0.4582  -0.1164 0.0557  379 ALA A C   
2558  O O   . ALA A 379 ? 1.2906 1.1273 0.7943 0.4535  -0.0962 0.0723  379 ALA A O   
2559  C CB  . ALA A 379 ? 1.2231 1.1848 0.8317 0.4074  -0.1400 0.0158  379 ALA A CB  
2560  N N   . ASN A 380 ? 1.2883 1.1797 0.8090 0.4941  -0.1193 0.0630  380 ASN A N   
2561  C CA  . ASN A 380 ? 1.3296 1.1553 0.7779 0.5331  -0.0980 0.0930  380 ASN A CA  
2562  C C   . ASN A 380 ? 1.3608 1.1008 0.7964 0.5052  -0.0642 0.1132  380 ASN A C   
2563  O O   . ASN A 380 ? 1.4079 1.0772 0.7831 0.5187  -0.0373 0.1369  380 ASN A O   
2564  C CB  . ASN A 380 ? 1.3214 1.1777 0.7630 0.5683  -0.1051 0.0885  380 ASN A CB  
2565  C CG  . ASN A 380 ? 1.3687 1.2308 0.7580 0.6086  -0.1004 0.0920  380 ASN A CG  
2566  O OD1 . ASN A 380 ? 1.3889 1.2458 0.7524 0.6131  -0.0982 0.0946  380 ASN A OD1 
2567  N ND2 . ASN A 380 ? 1.4070 1.2802 0.7788 0.6404  -0.0985 0.0915  380 ASN A ND2 
2568  N N   . SER A 381 ? 1.3026 1.0475 0.7923 0.4660  -0.0634 0.1029  381 SER A N   
2569  C CA  . SER A 381 ? 1.3254 0.9987 0.8064 0.4421  -0.0333 0.1178  381 SER A CA  
2570  C C   . SER A 381 ? 1.3592 0.9866 0.8248 0.4116  -0.0096 0.1250  381 SER A C   
2571  O O   . SER A 381 ? 1.3462 1.0084 0.8459 0.3844  -0.0199 0.1103  381 SER A O   
2572  C CB  . SER A 381 ? 1.2874 0.9868 0.8319 0.4080  -0.0409 0.1022  381 SER A CB  
2573  O OG  . SER A 381 ? 1.2511 1.0164 0.8256 0.4271  -0.0682 0.0868  381 SER A OG  
2574  N N   . THR A 382 ? 1.3714 0.9190 0.7846 0.4159  0.0244  0.1464  382 THR A N   
2575  C CA  . THR A 382 ? 1.4078 0.9115 0.8073 0.3837  0.0516  0.1510  382 THR A CA  
2576  C C   . THR A 382 ? 1.3898 0.8988 0.8446 0.3315  0.0585  0.1367  382 THR A C   
2577  O O   . THR A 382 ? 1.4079 0.9101 0.8712 0.3001  0.0718  0.1316  382 THR A O   
2578  C CB  . THR A 382 ? 1.4665 0.8788 0.7896 0.4022  0.0905  0.1765  382 THR A CB  
2579  O OG1 . THR A 382 ? 1.4684 0.8349 0.7879 0.3969  0.1090  0.1826  382 THR A OG1 
2580  C CG2 . THR A 382 ? 1.4872 0.8933 0.7484 0.4615  0.0833  0.1927  382 THR A CG2 
2581  N N   . GLU A 383 ? 1.3108 0.8353 0.8022 0.3237  0.0496  0.1294  383 GLU A N   
2582  C CA  . GLU A 383 ? 1.2876 0.8252 0.8315 0.2792  0.0524  0.1147  383 GLU A CA  
2583  C C   . GLU A 383 ? 1.2396 0.8507 0.8432 0.2649  0.0206  0.0944  383 GLU A C   
2584  O O   . GLU A 383 ? 1.2164 0.8428 0.8623 0.2331  0.0200  0.0824  383 GLU A O   
2585  C CB  . GLU A 383 ? 1.2796 0.7871 0.8269 0.2768  0.0642  0.1181  383 GLU A CB  
2586  C CG  . GLU A 383 ? 1.3171 0.7560 0.8384 0.2528  0.1034  0.1246  383 GLU A CG  
2587  C CD  . GLU A 383 ? 1.3691 0.7337 0.8155 0.2828  0.1311  0.1473  383 GLU A CD  
2588  O OE1 . GLU A 383 ? 1.3691 0.7305 0.7863 0.3272  0.1199  0.1592  383 GLU A OE1 
2589  O OE2 . GLU A 383 ? 1.4113 0.7208 0.8260 0.2631  0.1654  0.1525  383 GLU A OE2 
2590  N N   . LEU A 384 ? 1.1408 0.7962 0.7462 0.2880  -0.0043 0.0894  384 LEU A N   
2591  C CA  . LEU A 384 ? 1.1001 0.8180 0.7577 0.2731  -0.0306 0.0689  384 LEU A CA  
2592  C C   . LEU A 384 ? 1.1033 0.8250 0.7824 0.2392  -0.0248 0.0604  384 LEU A C   
2593  O O   . LEU A 384 ? 1.1358 0.8414 0.7890 0.2384  -0.0142 0.0652  384 LEU A O   
2594  C CB  . LEU A 384 ? 1.0919 0.8541 0.7421 0.3019  -0.0541 0.0624  384 LEU A CB  
2595  C CG  . LEU A 384 ? 1.0532 0.8780 0.7540 0.2885  -0.0796 0.0388  384 LEU A CG  
2596  C CD1 . LEU A 384 ? 1.0217 0.8596 0.7622 0.2740  -0.0838 0.0312  384 LEU A CD1 
2597  C CD2 . LEU A 384 ? 1.0491 0.9212 0.7413 0.3184  -0.1013 0.0290  384 LEU A CD2 
2598  N N   . THR A 385 ? 1.0225 0.7663 0.7468 0.2136  -0.0313 0.0477  385 THR A N   
2599  C CA  . THR A 385 ? 1.0216 0.7727 0.7671 0.1853  -0.0267 0.0387  385 THR A CA  
2600  C C   . THR A 385 ? 0.9875 0.7825 0.7700 0.1768  -0.0479 0.0223  385 THR A C   
2601  O O   . THR A 385 ? 0.9925 0.7977 0.7810 0.1653  -0.0484 0.0154  385 THR A O   
2602  C CB  . THR A 385 ? 1.0195 0.7497 0.7790 0.1615  -0.0094 0.0386  385 THR A CB  
2603  O OG1 . THR A 385 ? 0.9920 0.7224 0.7658 0.1662  -0.0143 0.0394  385 THR A OG1 
2604  C CG2 . THR A 385 ? 1.0686 0.7518 0.7916 0.1576  0.0190  0.0497  385 THR A CG2 
2605  N N   . VAL A 386 ? 0.9565 0.7754 0.7624 0.1814  -0.0632 0.0150  386 VAL A N   
2606  C CA  . VAL A 386 ? 0.9320 0.7837 0.7705 0.1703  -0.0783 -0.0012 386 VAL A CA  
2607  C C   . VAL A 386 ? 0.9278 0.8118 0.7720 0.1867  -0.0957 -0.0105 386 VAL A C   
2608  O O   . VAL A 386 ? 0.9223 0.8109 0.7659 0.2001  -0.0983 -0.0072 386 VAL A O   
2609  C CB  . VAL A 386 ? 0.9048 0.7552 0.7730 0.1510  -0.0751 -0.0054 386 VAL A CB  
2610  C CG1 . VAL A 386 ? 0.8899 0.7649 0.7848 0.1415  -0.0871 -0.0208 386 VAL A CG1 
2611  C CG2 . VAL A 386 ? 0.9080 0.7385 0.7730 0.1356  -0.0598 -0.0011 386 VAL A CG2 
2612  N N   . LEU A 387 ? 0.9100 0.8195 0.7603 0.1857  -0.1071 -0.0242 387 LEU A N   
2613  C CA  . LEU A 387 ? 0.9078 0.8576 0.7667 0.1981  -0.1238 -0.0393 387 LEU A CA  
2614  C C   . LEU A 387 ? 0.9079 0.8775 0.7962 0.1769  -0.1301 -0.0602 387 LEU A C   
2615  O O   . LEU A 387 ? 0.9199 0.8938 0.8014 0.1742  -0.1329 -0.0681 387 LEU A O   
2616  C CB  . LEU A 387 ? 0.9227 0.8813 0.7474 0.2238  -0.1292 -0.0356 387 LEU A CB  
2617  C CG  . LEU A 387 ? 0.9163 0.9124 0.7335 0.2519  -0.1434 -0.0421 387 LEU A CG  
2618  C CD1 . LEU A 387 ? 0.9326 0.9369 0.7114 0.2790  -0.1485 -0.0385 387 LEU A CD1 
2619  C CD2 . LEU A 387 ? 0.8959 0.9397 0.7524 0.2387  -0.1572 -0.0691 387 LEU A CD2 
2620  N N   . GLN A 388 ? 0.9265 0.9039 0.8443 0.1622  -0.1301 -0.0691 388 GLN A N   
2621  C CA  . GLN A 388 ? 0.9379 0.9221 0.8794 0.1403  -0.1304 -0.0875 388 GLN A CA  
2622  C C   . GLN A 388 ? 0.9333 0.9626 0.8946 0.1395  -0.1414 -0.1117 388 GLN A C   
2623  O O   . GLN A 388 ? 0.9221 0.9719 0.9003 0.1411  -0.1438 -0.1158 388 GLN A O   
2624  C CB  . GLN A 388 ? 0.9356 0.8951 0.8932 0.1232  -0.1195 -0.0820 388 GLN A CB  
2625  C CG  . GLN A 388 ? 0.9180 0.8437 0.8608 0.1230  -0.1091 -0.0628 388 GLN A CG  
2626  C CD  . GLN A 388 ? 0.9170 0.8245 0.8574 0.1121  -0.1034 -0.0655 388 GLN A CD  
2627  O OE1 . GLN A 388 ? 0.9250 0.8353 0.8727 0.1034  -0.1047 -0.0800 388 GLN A OE1 
2628  N NE2 . GLN A 388 ? 0.8938 0.7829 0.8225 0.1128  -0.0955 -0.0531 388 GLN A NE2 
2629  N N   . LEU A 389 ? 0.8942 0.9417 0.8556 0.1350  -0.1471 -0.1305 389 LEU A N   
2630  C CA  . LEU A 389 ? 0.8765 0.9756 0.8573 0.1326  -0.1576 -0.1592 389 LEU A CA  
2631  C C   . LEU A 389 ? 0.8728 0.9713 0.8699 0.1056  -0.1522 -0.1846 389 LEU A C   
2632  O O   . LEU A 389 ? 0.8554 0.9993 0.8685 0.0998  -0.1595 -0.2135 389 LEU A O   
2633  C CB  . LEU A 389 ? 0.8673 1.0033 0.8278 0.1602  -0.1725 -0.1629 389 LEU A CB  
2634  C CG  . LEU A 389 ? 0.8648 1.0003 0.7994 0.1928  -0.1768 -0.1397 389 LEU A CG  
2635  C CD1 . LEU A 389 ? 0.8538 1.0341 0.7686 0.2221  -0.1922 -0.1489 389 LEU A CD1 
2636  C CD2 . LEU A 389 ? 0.8518 0.9993 0.8060 0.1942  -0.1761 -0.1380 389 LEU A CD2 
2637  N N   . ASP A 390 ? 0.9231 0.9724 0.9149 0.0899  -0.1385 -0.1765 390 ASP A N   
2638  C CA  . ASP A 390 ? 0.9197 0.9570 0.9176 0.0675  -0.1303 -0.1987 390 ASP A CA  
2639  C C   . ASP A 390 ? 0.9068 0.9610 0.9347 0.0433  -0.1230 -0.2229 390 ASP A C   
2640  O O   . ASP A 390 ? 0.8997 0.9718 0.9447 0.0436  -0.1238 -0.2198 390 ASP A O   
2641  C CB  . ASP A 390 ? 0.9299 0.9083 0.9108 0.0618  -0.1163 -0.1825 390 ASP A CB  
2642  C CG  . ASP A 390 ? 0.9269 0.8763 0.9136 0.0567  -0.1057 -0.1651 390 ASP A CG  
2643  O OD1 . ASP A 390 ? 0.9283 0.8801 0.9112 0.0709  -0.1100 -0.1444 390 ASP A OD1 
2644  O OD2 . ASP A 390 ? 0.9251 0.8470 0.9177 0.0384  -0.0915 -0.1727 390 ASP A OD2 
2645  N N   . THR A 391 ? 0.9157 0.9626 0.9489 0.0210  -0.1138 -0.2486 391 THR A N   
2646  C CA  . THR A 391 ? 0.9064 0.9581 0.9651 -0.0091 -0.0997 -0.2747 391 THR A CA  
2647  C C   . THR A 391 ? 0.8811 1.0072 0.9704 -0.0087 -0.1122 -0.2962 391 THR A C   
2648  O O   . THR A 391 ? 0.8736 1.0105 0.9821 -0.0148 -0.1079 -0.2946 391 THR A O   
2649  C CB  . THR A 391 ? 0.9169 0.9122 0.9721 -0.0199 -0.0806 -0.2556 391 THR A CB  
2650  O OG1 . THR A 391 ? 0.9337 0.8730 0.9579 -0.0078 -0.0752 -0.2302 391 THR A OG1 
2651  C CG2 . THR A 391 ? 0.9172 0.8921 0.9851 -0.0542 -0.0579 -0.2815 391 THR A CG2 
2652  N N   . ASN A 392 ? 0.9220 1.1031 1.0140 0.0014  -0.1287 -0.3171 392 ASN A N   
2653  C CA  . ASN A 392 ? 0.8918 1.1551 1.0089 0.0097  -0.1445 -0.3401 392 ASN A CA  
2654  C C   . ASN A 392 ? 0.8716 1.1859 0.9969 0.0015  -0.1522 -0.3795 392 ASN A C   
2655  O O   . ASN A 392 ? 0.8839 1.1627 0.9991 -0.0173 -0.1410 -0.3909 392 ASN A O   
2656  C CB  . ASN A 392 ? 0.8934 1.1755 0.9937 0.0509  -0.1630 -0.3106 392 ASN A CB  
2657  C CG  . ASN A 392 ? 0.8955 1.1693 1.0070 0.0545  -0.1586 -0.2920 392 ASN A CG  
2658  O OD1 . ASN A 392 ? 0.8724 1.1952 1.0139 0.0467  -0.1598 -0.3132 392 ASN A OD1 
2659  N ND2 . ASN A 392 ? 0.9211 1.1365 1.0098 0.0656  -0.1529 -0.2545 392 ASN A ND2 
2660  N N   . ASN A 393 ? 0.9331 1.3330 1.0756 0.0172  -0.1714 -0.4023 393 ASN A N   
2661  C CA  . ASN A 393 ? 0.9058 1.3707 1.0605 0.0102  -0.1809 -0.4458 393 ASN A CA  
2662  C C   . ASN A 393 ? 0.8904 1.4153 1.0264 0.0564  -0.2090 -0.4407 393 ASN A C   
2663  O O   . ASN A 393 ? 0.8519 1.4662 1.0071 0.0646  -0.2247 -0.4759 393 ASN A O   
2664  C CB  . ASN A 393 ? 0.8687 1.3974 1.0700 -0.0226 -0.1741 -0.4940 393 ASN A CB  
2665  C CG  . ASN A 393 ? 0.8846 1.3501 1.0998 -0.0709 -0.1417 -0.5030 393 ASN A CG  
2666  O OD1 . ASN A 393 ? 0.9123 1.3006 1.1114 -0.0727 -0.1274 -0.4670 393 ASN A OD1 
2667  N ND2 . ASN A 393 ? 0.8662 1.3643 1.1094 -0.1102 -0.1286 -0.5529 393 ASN A ND2 
2668  N N   . PHE A 394 ? 0.9032 1.3805 0.9992 0.0879  -0.2145 -0.3980 394 PHE A N   
2669  C CA  . PHE A 394 ? 0.8943 1.4137 0.9630 0.1347  -0.2369 -0.3868 394 PHE A CA  
2670  C C   . PHE A 394 ? 0.8877 1.4348 0.9412 0.1399  -0.2466 -0.4089 394 PHE A C   
2671  O O   . PHE A 394 ? 0.8980 1.4154 0.9558 0.1091  -0.2346 -0.4252 394 PHE A O   
2672  C CB  . PHE A 394 ? 0.9272 1.3816 0.9573 0.1632  -0.2346 -0.3341 394 PHE A CB  
2673  C CG  . PHE A 394 ? 0.9282 1.3726 0.9677 0.1706  -0.2309 -0.3135 394 PHE A CG  
2674  C CD1 . PHE A 394 ? 0.9382 1.3415 1.0015 0.1375  -0.2130 -0.3099 394 PHE A CD1 
2675  C CD2 . PHE A 394 ? 0.9203 1.3923 0.9405 0.2129  -0.2440 -0.2968 394 PHE A CD2 
2676  C CE1 . PHE A 394 ? 0.9393 1.3344 1.0110 0.1442  -0.2096 -0.2921 394 PHE A CE1 
2677  C CE2 . PHE A 394 ? 0.9211 1.3820 0.9491 0.2199  -0.2397 -0.2792 394 PHE A CE2 
2678  C CZ  . PHE A 394 ? 0.9304 1.3544 0.9856 0.1846  -0.2230 -0.2773 394 PHE A CZ  
2679  N N   . THR A 395 ? 0.9009 1.5041 0.9327 0.1822  -0.2680 -0.4091 395 THR A N   
2680  C CA  . THR A 395 ? 0.8912 1.5332 0.9054 0.1949  -0.2807 -0.4306 395 THR A CA  
2681  C C   . THR A 395 ? 0.9059 1.5393 0.8676 0.2477  -0.2932 -0.3949 395 THR A C   
2682  O O   . THR A 395 ? 0.9154 1.5288 0.8584 0.2760  -0.2940 -0.3612 395 THR A O   
2683  C CB  . THR A 395 ? 0.8502 1.5930 0.8995 0.1899  -0.2905 -0.4807 395 THR A CB  
2684  O OG1 . THR A 395 ? 0.8507 1.6445 0.9039 0.2249  -0.2992 -0.4721 395 THR A OG1 
2685  C CG2 . THR A 395 ? 0.8393 1.5864 0.9380 0.1332  -0.2731 -0.5187 395 THR A CG2 
2686  N N   . GLY A 396 ? 0.8922 1.5360 0.8275 0.2601  -0.3006 -0.4027 396 GLY A N   
2687  C CA  . GLY A 396 ? 0.9066 1.5502 0.7911 0.3107  -0.3096 -0.3741 396 GLY A CA  
2688  C C   . GLY A 396 ? 0.9476 1.5011 0.7888 0.3186  -0.2973 -0.3285 396 GLY A C   
2689  O O   . GLY A 396 ? 0.9701 1.4635 0.8198 0.2849  -0.2809 -0.3215 396 GLY A O   
2690  N N   . PHE A 397 ? 1.0172 1.5588 0.8106 0.3646  -0.3015 -0.2958 397 PHE A N   
2691  C CA  . PHE A 397 ? 1.0580 1.5226 0.8052 0.3762  -0.2873 -0.2546 397 PHE A CA  
2692  C C   . PHE A 397 ? 1.0807 1.4809 0.8185 0.3788  -0.2716 -0.2148 397 PHE A C   
2693  O O   . PHE A 397 ? 1.0660 1.4854 0.8170 0.3892  -0.2756 -0.2130 397 PHE A O   
2694  C CB  . PHE A 397 ? 1.0649 1.5473 0.7591 0.4232  -0.2948 -0.2437 397 PHE A CB  
2695  C CG  . PHE A 397 ? 1.0558 1.5852 0.7591 0.4176  -0.3008 -0.2758 397 PHE A CG  
2696  C CD1 . PHE A 397 ? 1.0289 1.6012 0.7822 0.3797  -0.3065 -0.3193 397 PHE A CD1 
2697  C CD2 . PHE A 397 ? 1.0895 1.6166 0.7500 0.4500  -0.2981 -0.2624 397 PHE A CD2 
2698  C CE1 . PHE A 397 ? 1.0376 1.6501 0.7987 0.3743  -0.3099 -0.3484 397 PHE A CE1 
2699  C CE2 . PHE A 397 ? 1.1023 1.6734 0.7712 0.4463  -0.3038 -0.2915 397 PHE A CE2 
2700  C CZ  . PHE A 397 ? 1.0761 1.6906 0.7962 0.4083  -0.3100 -0.3347 397 PHE A CZ  
2701  N N   . LEU A 398 ? 1.0501 1.3762 0.7651 0.3689  -0.2532 -0.1847 398 LEU A N   
2702  C CA  . LEU A 398 ? 1.0670 1.3320 0.7662 0.3734  -0.2368 -0.1476 398 LEU A CA  
2703  C C   . LEU A 398 ? 1.0898 1.3477 0.7327 0.4232  -0.2373 -0.1223 398 LEU A C   
2704  O O   . LEU A 398 ? 1.1081 1.3773 0.7114 0.4496  -0.2420 -0.1209 398 LEU A O   
2705  C CB  . LEU A 398 ? 1.0968 1.2933 0.7906 0.3470  -0.2162 -0.1276 398 LEU A CB  
2706  C CG  . LEU A 398 ? 1.0916 1.2737 0.8317 0.3023  -0.2099 -0.1419 398 LEU A CG  
2707  C CD1 . LEU A 398 ? 1.1147 1.2310 0.8490 0.2864  -0.1891 -0.1139 398 LEU A CD1 
2708  C CD2 . LEU A 398 ? 1.0652 1.2817 0.8492 0.2874  -0.2175 -0.1625 398 LEU A CD2 
2709  N N   . PRO A 399 ? 1.1690 1.4053 0.8033 0.4386  -0.2312 -0.1021 399 PRO A N   
2710  C CA  . PRO A 399 ? 1.1889 1.4062 0.7621 0.4887  -0.2276 -0.0753 399 PRO A CA  
2711  C C   . PRO A 399 ? 1.2360 1.3734 0.7606 0.4898  -0.2026 -0.0416 399 PRO A C   
2712  O O   . PRO A 399 ? 1.2513 1.3434 0.7942 0.4518  -0.1861 -0.0342 399 PRO A O   
2713  C CB  . PRO A 399 ? 1.1801 1.3898 0.7637 0.4979  -0.2250 -0.0651 399 PRO A CB  
2714  C CG  . PRO A 399 ? 1.1608 1.3729 0.8077 0.4490  -0.2231 -0.0807 399 PRO A CG  
2715  C CD  . PRO A 399 ? 1.1536 1.3870 0.8330 0.4135  -0.2282 -0.1059 399 PRO A CD  
2716  N N   . ASP A 400 ? 1.3035 1.4256 0.7632 0.5357  -0.1989 -0.0219 400 ASP A N   
2717  C CA  . ASP A 400 ? 1.3539 1.3992 0.7606 0.5390  -0.1716 0.0097  400 ASP A CA  
2718  C C   . ASP A 400 ? 1.3826 1.3519 0.7766 0.5289  -0.1443 0.0386  400 ASP A C   
2719  O O   . ASP A 400 ? 1.4258 1.3289 0.7849 0.5202  -0.1171 0.0613  400 ASP A O   
2720  C CB  . ASP A 400 ? 1.3807 1.4250 0.7345 0.5798  -0.1642 0.0182  400 ASP A CB  
2721  C CG  . ASP A 400 ? 1.3662 1.4744 0.7325 0.5826  -0.1828 -0.0096 400 ASP A CG  
2722  O OD1 . ASP A 400 ? 1.3789 1.4658 0.7261 0.5716  -0.1760 -0.0052 400 ASP A OD1 
2723  O OD2 . ASP A 400 ? 1.3447 1.5257 0.7405 0.5945  -0.2030 -0.0374 400 ASP A OD2 
2724  N N   . THR A 401 ? 1.3001 1.2788 0.7217 0.5284  -0.1495 0.0362  401 THR A N   
2725  C CA  . THR A 401 ? 1.3210 1.2328 0.7372 0.5156  -0.1250 0.0590  401 THR A CA  
2726  C C   . THR A 401 ? 1.3127 1.2093 0.7848 0.4590  -0.1162 0.0510  401 THR A C   
2727  O O   . THR A 401 ? 1.3194 1.1743 0.7995 0.4437  -0.0999 0.0631  401 THR A O   
2728  C CB  . THR A 401 ? 1.2990 1.2313 0.7192 0.5432  -0.1353 0.0590  401 THR A CB  
2729  O OG1 . THR A 401 ? 1.2483 1.2575 0.7354 0.5245  -0.1618 0.0264  401 THR A OG1 
2730  C CG2 . THR A 401 ? 1.3210 1.2651 0.6961 0.5894  -0.1330 0.0626  401 THR A CG2 
2731  N N   . ILE A 402 ? 1.2542 1.1813 0.7601 0.4306  -0.1255 0.0314  402 ILE A N   
2732  C CA  . ILE A 402 ? 1.2345 1.1668 0.7993 0.3843  -0.1255 0.0173  402 ILE A CA  
2733  C C   . ILE A 402 ? 1.2617 1.1300 0.8217 0.3595  -0.0975 0.0367  402 ILE A C   
2734  O O   . ILE A 402 ? 1.2440 1.1075 0.8426 0.3335  -0.0948 0.0327  402 ILE A O   
2735  C CB  . ILE A 402 ? 1.2234 1.1911 0.8132 0.3644  -0.1375 -0.0051 402 ILE A CB  
2736  C CG1 . ILE A 402 ? 1.2062 1.1742 0.8499 0.3219  -0.1361 -0.0180 402 ILE A CG1 
2737  C CG2 . ILE A 402 ? 1.2599 1.1995 0.8073 0.3707  -0.1240 0.0069  402 ILE A CG2 
2738  C CD1 . ILE A 402 ? 1.1713 1.1749 0.8582 0.3140  -0.1506 -0.0349 402 ILE A CD1 
2739  N N   . CYS A 403 ? 1.2258 1.0466 0.7391 0.3657  -0.0752 0.0558  403 CYS A N   
2740  C CA  . CYS A 403 ? 1.2566 1.0204 0.7643 0.3400  -0.0457 0.0703  403 CYS A CA  
2741  C C   . CYS A 403 ? 1.3030 1.0054 0.7448 0.3649  -0.0195 0.0967  403 CYS A C   
2742  O O   . CYS A 403 ? 1.3465 1.0042 0.7597 0.3523  0.0076  0.1079  403 CYS A O   
2743  C CB  . CYS A 403 ? 1.2712 1.0364 0.7968 0.3081  -0.0377 0.0619  403 CYS A CB  
2744  S SG  . CYS A 403 ? 1.2981 1.0175 0.8373 0.2690  -0.0065 0.0686  403 CYS A SG  
2745  N N   . ARG A 404 ? 1.3448 1.0438 0.7593 0.4020  -0.0259 0.1061  404 ARG A N   
2746  C CA  . ARG A 404 ? 1.3904 1.0262 0.7317 0.4347  -0.0011 0.1329  404 ARG A CA  
2747  C C   . ARG A 404 ? 1.4284 0.9892 0.7547 0.4071  0.0374  0.1478  404 ARG A C   
2748  O O   . ARG A 404 ? 1.4791 0.9807 0.7513 0.4107  0.0681  0.1651  404 ARG A O   
2749  C CB  . ARG A 404 ? 1.3721 1.0217 0.6930 0.4802  -0.0162 0.1383  404 ARG A CB  
2750  C CG  . ARG A 404 ? 1.4215 1.0048 0.6575 0.5245  0.0077  0.1673  404 ARG A CG  
2751  C CD  . ARG A 404 ? 1.4044 1.0287 0.6371 0.5655  -0.0098 0.1606  404 ARG A CD  
2752  N NE  . ARG A 404 ? 1.3978 1.0012 0.6446 0.5631  -0.0028 0.1642  404 ARG A NE  
2753  C CZ  . ARG A 404 ? 1.4094 1.0364 0.6501 0.5948  -0.0098 0.1600  404 ARG A CZ  
2754  N NH1 . ARG A 404 ? 1.4402 1.1138 0.6618 0.6323  -0.0237 0.1513  404 ARG A NH1 
2755  N NH2 . ARG A 404 ? 1.4064 1.0109 0.6592 0.5897  -0.0017 0.1637  404 ARG A NH2 
2756  N N   . GLY A 405 ? 1.3570 0.9194 0.7296 0.3783  0.0381  0.1398  405 GLY A N   
2757  C CA  . GLY A 405 ? 1.3886 0.8860 0.7502 0.3508  0.0741  0.1495  405 GLY A CA  
2758  C C   . GLY A 405 ? 1.4089 0.9025 0.7930 0.3058  0.0915  0.1399  405 GLY A C   
2759  O O   . GLY A 405 ? 1.4425 0.8821 0.8104 0.2822  0.1260  0.1460  405 GLY A O   
2760  N N   . GLY A 406 ? 1.2988 0.8491 0.7190 0.2934  0.0699  0.1233  406 GLY A N   
2761  C CA  . GLY A 406 ? 1.3179 0.8732 0.7620 0.2543  0.0840  0.1122  406 GLY A CA  
2762  C C   . GLY A 406 ? 1.2954 0.8657 0.7938 0.2178  0.0849  0.0979  406 GLY A C   
2763  O O   . GLY A 406 ? 1.3206 0.8820 0.8300 0.1856  0.1063  0.0908  406 GLY A O   
2764  N N   . LYS A 407 ? 1.2660 0.8630 0.7986 0.2226  0.0623  0.0920  407 LYS A N   
2765  C CA  . LYS A 407 ? 1.2383 0.8509 0.8197 0.1924  0.0614  0.0792  407 LYS A CA  
2766  C C   . LYS A 407 ? 1.1842 0.8564 0.8169 0.1890  0.0285  0.0627  407 LYS A C   
2767  O O   . LYS A 407 ? 1.1552 0.8417 0.8260 0.1686  0.0255  0.0531  407 LYS A O   
2768  C CB  . LYS A 407 ? 1.2318 0.8058 0.8028 0.1964  0.0741  0.0886  407 LYS A CB  
2769  C CG  . LYS A 407 ? 1.2833 0.7859 0.7938 0.2057  0.1088  0.1072  407 LYS A CG  
2770  C CD  . LYS A 407 ? 1.2804 0.7409 0.7867 0.1984  0.1276  0.1119  407 LYS A CD  
2771  C CE  . LYS A 407 ? 1.3291 0.7090 0.7652 0.2175  0.1614  0.1335  407 LYS A CE  
2772  N NZ  . LYS A 407 ? 1.3236 0.6613 0.7527 0.2170  0.1767  0.1383  407 LYS A NZ  
2773  N N   . LEU A 408 ? 1.1188 0.8240 0.7513 0.2076  0.0060  0.0583  408 LEU A N   
2774  C CA  . LEU A 408 ? 1.0695 0.8234 0.7458 0.2037  -0.0214 0.0420  408 LEU A CA  
2775  C C   . LEU A 408 ? 1.0642 0.8371 0.7717 0.1766  -0.0207 0.0287  408 LEU A C   
2776  O O   . LEU A 408 ? 1.0936 0.8694 0.7895 0.1727  -0.0147 0.0264  408 LEU A O   
2777  C CB  . LEU A 408 ? 1.0605 0.8446 0.7264 0.2284  -0.0426 0.0372  408 LEU A CB  
2778  C CG  . LEU A 408 ? 1.0152 0.8455 0.7223 0.2252  -0.0682 0.0187  408 LEU A CG  
2779  C CD1 . LEU A 408 ? 0.9890 0.8252 0.7101 0.2332  -0.0754 0.0194  408 LEU A CD1 
2780  C CD2 . LEU A 408 ? 1.0144 0.8779 0.7129 0.2418  -0.0858 0.0080  408 LEU A CD2 
2781  N N   . GLU A 409 ? 0.9781 0.7646 0.7226 0.1605  -0.0262 0.0202  409 GLU A N   
2782  C CA  . GLU A 409 ? 0.9665 0.7723 0.7384 0.1404  -0.0265 0.0080  409 GLU A CA  
2783  C C   . GLU A 409 ? 0.9307 0.7669 0.7253 0.1431  -0.0479 -0.0047 409 GLU A C   
2784  O O   . GLU A 409 ? 0.9374 0.7869 0.7331 0.1406  -0.0505 -0.0125 409 GLU A O   
2785  C CB  . GLU A 409 ? 0.9501 0.7503 0.7435 0.1227  -0.0172 0.0061  409 GLU A CB  
2786  C CG  . GLU A 409 ? 0.9847 0.7500 0.7572 0.1169  0.0062  0.0161  409 GLU A CG  
2787  C CD  . GLU A 409 ? 0.9792 0.7477 0.7739 0.0938  0.0185  0.0080  409 GLU A CD  
2788  O OE1 . GLU A 409 ? 0.9393 0.7339 0.7645 0.0887  0.0054  -0.0012 409 GLU A OE1 
2789  O OE2 . GLU A 409 ? 1.0149 0.7591 0.7948 0.0806  0.0427  0.0098  409 GLU A OE2 
2790  N N   . ASN A 410 ? 0.8954 0.7409 0.7071 0.1474  -0.0612 -0.0080 410 ASN A N   
2791  C CA  . ASN A 410 ? 0.8702 0.7374 0.7047 0.1443  -0.0762 -0.0219 410 ASN A CA  
2792  C C   . ASN A 410 ? 0.8726 0.7570 0.7052 0.1582  -0.0910 -0.0276 410 ASN A C   
2793  O O   . ASN A 410 ? 0.8686 0.7532 0.6981 0.1682  -0.0932 -0.0221 410 ASN A O   
2794  C CB  . ASN A 410 ? 0.8373 0.7036 0.6983 0.1314  -0.0754 -0.0249 410 ASN A CB  
2795  C CG  . ASN A 410 ? 0.8349 0.6932 0.6982 0.1200  -0.0618 -0.0218 410 ASN A CG  
2796  O OD1 . ASN A 410 ? 0.8548 0.7162 0.7083 0.1182  -0.0558 -0.0236 410 ASN A OD1 
2797  N ND2 . ASN A 410 ? 0.8156 0.6685 0.6926 0.1121  -0.0568 -0.0195 410 ASN A ND2 
2798  N N   . LEU A 411 ? 0.8481 0.7496 0.6820 0.1596  -0.1007 -0.0406 411 LEU A N   
2799  C CA  . LEU A 411 ? 0.8571 0.7847 0.6916 0.1707  -0.1152 -0.0521 411 LEU A CA  
2800  C C   . LEU A 411 ? 0.8455 0.7863 0.7010 0.1577  -0.1221 -0.0723 411 LEU A C   
2801  O O   . LEU A 411 ? 0.8518 0.7846 0.7024 0.1523  -0.1189 -0.0766 411 LEU A O   
2802  C CB  . LEU A 411 ? 0.8871 0.8209 0.6894 0.1901  -0.1178 -0.0483 411 LEU A CB  
2803  C CG  . LEU A 411 ? 0.8981 0.8688 0.7001 0.2029  -0.1347 -0.0652 411 LEU A CG  
2804  C CD1 . LEU A 411 ? 0.8997 0.8914 0.7107 0.2143  -0.1431 -0.0671 411 LEU A CD1 
2805  C CD2 . LEU A 411 ? 0.9298 0.9042 0.6959 0.2228  -0.1359 -0.0607 411 LEU A CD2 
2806  N N   . THR A 412 ? 0.9502 0.9096 0.8277 0.1523  -0.1294 -0.0856 412 THR A N   
2807  C CA  . THR A 412 ? 0.9500 0.9132 0.8467 0.1356  -0.1305 -0.1056 412 THR A CA  
2808  C C   . THR A 412 ? 0.9379 0.9406 0.8456 0.1371  -0.1426 -0.1282 412 THR A C   
2809  O O   . THR A 412 ? 0.9285 0.9564 0.8456 0.1444  -0.1490 -0.1298 412 THR A O   
2810  C CB  . THR A 412 ? 0.9423 0.8860 0.8588 0.1202  -0.1219 -0.1026 412 THR A CB  
2811  O OG1 . THR A 412 ? 0.9328 0.8471 0.8402 0.1176  -0.1118 -0.0899 412 THR A OG1 
2812  C CG2 . THR A 412 ? 0.9271 0.8735 0.8614 0.1033  -0.1205 -0.1240 412 THR A CG2 
2813  N N   . LEU A 413 ? 0.9286 0.9398 0.8354 0.1305  -0.1453 -0.1479 413 LEU A N   
2814  C CA  . LEU A 413 ? 0.9145 0.9706 0.8328 0.1297  -0.1566 -0.1752 413 LEU A CA  
2815  C C   . LEU A 413 ? 0.9086 0.9591 0.8429 0.1046  -0.1502 -0.2020 413 LEU A C   
2816  O O   . LEU A 413 ? 0.8983 0.9845 0.8390 0.1008  -0.1577 -0.2293 413 LEU A O   
2817  C CB  . LEU A 413 ? 0.9158 0.9976 0.8092 0.1524  -0.1679 -0.1762 413 LEU A CB  
2818  C CG  . LEU A 413 ? 0.9235 1.0017 0.7900 0.1796  -0.1703 -0.1493 413 LEU A CG  
2819  C CD1 . LEU A 413 ? 0.9338 1.0088 0.7675 0.1956  -0.1719 -0.1436 413 LEU A CD1 
2820  C CD2 . LEU A 413 ? 0.9075 1.0278 0.7784 0.1977  -0.1822 -0.1542 413 LEU A CD2 
2821  N N   . ASP A 414 ? 0.9645 0.9702 0.9028 0.0881  -0.1353 -0.1961 414 ASP A N   
2822  C CA  . ASP A 414 ? 0.9669 0.9492 0.9083 0.0673  -0.1240 -0.2169 414 ASP A CA  
2823  C C   . ASP A 414 ? 0.9549 0.9701 0.9221 0.0467  -0.1240 -0.2504 414 ASP A C   
2824  O O   . ASP A 414 ? 0.9422 0.9860 0.9311 0.0431  -0.1273 -0.2539 414 ASP A O   
2825  C CB  . ASP A 414 ? 0.9727 0.9000 0.9098 0.0584  -0.1070 -0.2018 414 ASP A CB  
2826  C CG  . ASP A 414 ? 0.9764 0.8787 0.8914 0.0762  -0.1060 -0.1749 414 ASP A CG  
2827  O OD1 . ASP A 414 ? 0.9797 0.9028 0.8829 0.0925  -0.1162 -0.1670 414 ASP A OD1 
2828  O OD2 . ASP A 414 ? 0.9749 0.8390 0.8834 0.0745  -0.0942 -0.1626 414 ASP A OD2 
2829  N N   . ASP A 415 ? 1.0154 1.0280 0.9808 0.0322  -0.1190 -0.2772 415 ASP A N   
2830  C CA  . ASP A 415 ? 1.0055 1.0366 0.9952 0.0033  -0.1108 -0.3141 415 ASP A CA  
2831  C C   . ASP A 415 ? 0.9767 1.0864 0.9930 0.0062  -0.1277 -0.3341 415 ASP A C   
2832  O O   . ASP A 415 ? 0.9627 1.0920 1.0050 -0.0075 -0.1236 -0.3433 415 ASP A O   
2833  C CB  . ASP A 415 ? 1.0152 0.9946 1.0115 -0.0193 -0.0878 -0.3104 415 ASP A CB  
2834  C CG  . ASP A 415 ? 1.0433 0.9473 1.0094 -0.0184 -0.0706 -0.2943 415 ASP A CG  
2835  O OD1 . ASP A 415 ? 1.0575 0.9430 1.0086 -0.0238 -0.0646 -0.3107 415 ASP A OD1 
2836  O OD2 . ASP A 415 ? 1.0504 0.9160 1.0066 -0.0102 -0.0633 -0.2662 415 ASP A OD2 
2837  N N   . ASN A 416 ? 0.9699 1.1267 0.9773 0.0270  -0.1467 -0.3412 416 ASN A N   
2838  C CA  . ASN A 416 ? 0.9403 1.1781 0.9655 0.0393  -0.1658 -0.3602 416 ASN A CA  
2839  C C   . ASN A 416 ? 0.9281 1.2096 0.9480 0.0421  -0.1768 -0.3912 416 ASN A C   
2840  O O   . ASN A 416 ? 0.9428 1.1899 0.9517 0.0266  -0.1662 -0.4028 416 ASN A O   
2841  C CB  . ASN A 416 ? 0.9419 1.1910 0.9517 0.0758  -0.1800 -0.3253 416 ASN A CB  
2842  C CG  . ASN A 416 ? 0.9388 1.1822 0.9673 0.0720  -0.1748 -0.3113 416 ASN A CG  
2843  O OD1 . ASN A 416 ? 0.9141 1.2141 0.9666 0.0733  -0.1829 -0.3294 416 ASN A OD1 
2844  N ND2 . ASN A 416 ? 0.9615 1.1406 0.9791 0.0685  -0.1614 -0.2807 416 ASN A ND2 
2845  N N   . HIS A 417 ? 0.9744 1.3334 1.0003 0.0637  -0.1978 -0.4060 417 HIS A N   
2846  C CA  . HIS A 417 ? 0.9579 1.3700 0.9776 0.0711  -0.2113 -0.4368 417 HIS A CA  
2847  C C   . HIS A 417 ? 0.9581 1.3965 0.9440 0.1185  -0.2319 -0.4129 417 HIS A C   
2848  O O   . HIS A 417 ? 0.9314 1.4436 0.9161 0.1385  -0.2507 -0.4362 417 HIS A O   
2849  C CB  . HIS A 417 ? 0.9173 1.4109 0.9762 0.0510  -0.2166 -0.4888 417 HIS A CB  
2850  C CG  . HIS A 417 ? 0.9179 1.3822 1.0078 0.0018  -0.1919 -0.5136 417 HIS A CG  
2851  N ND1 . HIS A 417 ? 0.9377 1.3491 1.0222 -0.0299 -0.1717 -0.5303 417 HIS A ND1 
2852  C CD2 . HIS A 417 ? 0.9036 1.3792 1.0263 -0.0204 -0.1816 -0.5236 417 HIS A CD2 
2853  C CE1 . HIS A 417 ? 0.9370 1.3239 1.0469 -0.0695 -0.1484 -0.5487 417 HIS A CE1 
2854  N NE2 . HIS A 417 ? 0.9153 1.3424 1.0500 -0.0657 -0.1541 -0.5455 417 HIS A NE2 
2855  N N   . PHE A 418 ? 0.9273 1.3055 0.8832 0.1373  -0.2271 -0.3671 418 PHE A N   
2856  C CA  . PHE A 418 ? 0.9348 1.3207 0.8513 0.1787  -0.2398 -0.3421 418 PHE A CA  
2857  C C   . PHE A 418 ? 0.9417 1.3358 0.8369 0.1827  -0.2442 -0.3577 418 PHE A C   
2858  O O   . PHE A 418 ? 0.9494 1.3149 0.8527 0.1543  -0.2328 -0.3745 418 PHE A O   
2859  C CB  . PHE A 418 ? 0.9643 1.2799 0.8563 0.1897  -0.2285 -0.2939 418 PHE A CB  
2860  C CG  . PHE A 418 ? 0.9611 1.2727 0.8633 0.1971  -0.2272 -0.2740 418 PHE A CG  
2861  C CD1 . PHE A 418 ? 0.9459 1.3035 0.8377 0.2305  -0.2416 -0.2700 418 PHE A CD1 
2862  C CD2 . PHE A 418 ? 0.9745 1.2354 0.8933 0.1737  -0.2113 -0.2590 418 PHE A CD2 
2863  C CE1 . PHE A 418 ? 0.9436 1.2945 0.8430 0.2386  -0.2393 -0.2519 418 PHE A CE1 
2864  C CE2 . PHE A 418 ? 0.9722 1.2296 0.9001 0.1802  -0.2098 -0.2418 418 PHE A CE2 
2865  C CZ  . PHE A 418 ? 0.9569 1.2579 0.8757 0.2118  -0.2234 -0.2384 418 PHE A CZ  
2866  N N   . GLU A 419 ? 1.0099 1.4408 0.8742 0.2205  -0.2599 -0.3516 419 GLU A N   
2867  C CA  . GLU A 419 ? 1.0152 1.4554 0.8534 0.2301  -0.2650 -0.3627 419 GLU A CA  
2868  C C   . GLU A 419 ? 1.0307 1.4635 0.8193 0.2749  -0.2714 -0.3277 419 GLU A C   
2869  O O   . GLU A 419 ? 1.0373 1.4566 0.8127 0.2964  -0.2708 -0.2979 419 GLU A O   
2870  C CB  . GLU A 419 ? 0.9804 1.5015 0.8404 0.2225  -0.2792 -0.4154 419 GLU A CB  
2871  C CG  . GLU A 419 ? 0.9604 1.5523 0.8028 0.2649  -0.2982 -0.4184 419 GLU A CG  
2872  C CD  . GLU A 419 ? 0.9585 1.6283 0.8407 0.2529  -0.3011 -0.4615 419 GLU A CD  
2873  O OE1 . GLU A 419 ? 0.9490 1.6261 0.8723 0.2098  -0.2922 -0.4951 419 GLU A OE1 
2874  O OE2 . GLU A 419 ? 0.9843 1.7062 0.8548 0.2874  -0.3100 -0.4619 419 GLU A OE2 
2875  N N   . GLY A 420 ? 1.0525 1.4889 0.8106 0.2883  -0.2749 -0.3313 420 GLY A N   
2876  C CA  . GLY A 420 ? 1.0703 1.4971 0.7763 0.3298  -0.2778 -0.3004 420 GLY A CA  
2877  C C   . GLY A 420 ? 1.1079 1.4545 0.7900 0.3249  -0.2576 -0.2617 420 GLY A C   
2878  O O   . GLY A 420 ? 1.1180 1.4202 0.8237 0.2925  -0.2436 -0.2589 420 GLY A O   
2879  N N   . PRO A 421 ? 1.0876 1.4156 0.7204 0.3580  -0.2545 -0.2322 421 PRO A N   
2880  C CA  . PRO A 421 ? 1.1215 1.3813 0.7310 0.3523  -0.2339 -0.1996 421 PRO A CA  
2881  C C   . PRO A 421 ? 1.1373 1.3502 0.7473 0.3503  -0.2197 -0.1666 421 PRO A C   
2882  O O   . PRO A 421 ? 1.1234 1.3527 0.7462 0.3578  -0.2260 -0.1651 421 PRO A O   
2883  C CB  . PRO A 421 ? 1.1397 1.4051 0.6931 0.3887  -0.2353 -0.1870 421 PRO A CB  
2884  C CG  . PRO A 421 ? 1.1236 1.4397 0.6614 0.4243  -0.2527 -0.1922 421 PRO A CG  
2885  C CD  . PRO A 421 ? 1.0868 1.4578 0.6795 0.4035  -0.2686 -0.2298 421 PRO A CD  
2886  N N   . VAL A 422 ? 1.1361 1.2938 0.7325 0.3398  -0.2001 -0.1421 422 VAL A N   
2887  C CA  . VAL A 422 ? 1.1538 1.2651 0.7493 0.3348  -0.1839 -0.1127 422 VAL A CA  
2888  C C   . VAL A 422 ? 1.1772 1.2727 0.7211 0.3705  -0.1777 -0.0857 422 VAL A C   
2889  O O   . VAL A 422 ? 1.1982 1.2878 0.6995 0.3899  -0.1731 -0.0777 422 VAL A O   
2890  C CB  . VAL A 422 ? 1.1733 1.2400 0.7762 0.3092  -0.1650 -0.1016 422 VAL A CB  
2891  C CG1 . VAL A 422 ? 1.1793 1.2115 0.8010 0.2935  -0.1521 -0.0836 422 VAL A CG1 
2892  C CG2 . VAL A 422 ? 1.1562 1.2370 0.7904 0.2857  -0.1709 -0.1286 422 VAL A CG2 
2893  N N   . PRO A 423 ? 1.2337 1.3193 0.7759 0.3816  -0.1760 -0.0713 423 PRO A N   
2894  C CA  . PRO A 423 ? 1.2610 1.3206 0.7470 0.4182  -0.1664 -0.0436 423 PRO A CA  
2895  C C   . PRO A 423 ? 1.3070 1.3015 0.7601 0.4102  -0.1373 -0.0159 423 PRO A C   
2896  O O   . PRO A 423 ? 1.3144 1.2842 0.7951 0.3759  -0.1243 -0.0152 423 PRO A O   
2897  C CB  . PRO A 423 ? 1.2475 1.3057 0.7483 0.4245  -0.1689 -0.0367 423 PRO A CB  
2898  C CG  . PRO A 423 ? 1.2062 1.3118 0.7690 0.3985  -0.1869 -0.0677 423 PRO A CG  
2899  C CD  . PRO A 423 ? 1.2080 1.3052 0.7964 0.3636  -0.1822 -0.0804 423 PRO A CD  
2900  N N   . LYS A 424 ? 1.3393 1.3073 0.7302 0.4439  -0.1256 0.0062  424 LYS A N   
2901  C CA  . LYS A 424 ? 1.3882 1.2962 0.7422 0.4361  -0.0947 0.0298  424 LYS A CA  
2902  C C   . LYS A 424 ? 1.4094 1.2641 0.7725 0.4143  -0.0710 0.0482  424 LYS A C   
2903  O O   . LYS A 424 ? 1.4384 1.2573 0.8028 0.3872  -0.0473 0.0557  424 LYS A O   
2904  C CB  . LYS A 424 ? 1.4213 1.3085 0.6997 0.4792  -0.0852 0.0494  424 LYS A CB  
2905  C CG  . LYS A 424 ? 1.3976 1.3453 0.6600 0.5109  -0.1120 0.0308  424 LYS A CG  
2906  C CD  . LYS A 424 ? 1.3545 1.3587 0.6734 0.4827  -0.1338 -0.0043 424 LYS A CD  
2907  C CE  . LYS A 424 ? 1.3529 1.3905 0.6430 0.5022  -0.1441 -0.0173 424 LYS A CE  
2908  N NZ  . LYS A 424 ? 1.3134 1.4011 0.6582 0.4742  -0.1637 -0.0534 424 LYS A NZ  
2909  N N   . SER A 425 ? 1.3628 1.2163 0.7337 0.4255  -0.0771 0.0530  425 SER A N   
2910  C CA  . SER A 425 ? 1.3774 1.1841 0.7603 0.4042  -0.0563 0.0671  425 SER A CA  
2911  C C   . SER A 425 ? 1.3588 1.1780 0.8044 0.3586  -0.0576 0.0511  425 SER A C   
2912  O O   . SER A 425 ? 1.3810 1.1615 0.8339 0.3336  -0.0349 0.0605  425 SER A O   
2913  C CB  . SER A 425 ? 1.3570 1.1681 0.7388 0.4278  -0.0662 0.0722  425 SER A CB  
2914  O OG  . SER A 425 ? 1.3579 1.1856 0.6919 0.4767  -0.0776 0.0777  425 SER A OG  
2915  N N   . LEU A 426 ? 1.2658 1.1380 0.7550 0.3480  -0.0825 0.0258  426 LEU A N   
2916  C CA  . LEU A 426 ? 1.2496 1.1302 0.7909 0.3101  -0.0831 0.0118  426 LEU A CA  
2917  C C   . LEU A 426 ? 1.2740 1.1446 0.8101 0.2933  -0.0697 0.0101  426 LEU A C   
2918  O O   . LEU A 426 ? 1.2770 1.1390 0.8419 0.2653  -0.0599 0.0068  426 LEU A O   
2919  C CB  . LEU A 426 ? 1.2032 1.1346 0.7880 0.3043  -0.1100 -0.0144 426 LEU A CB  
2920  C CG  . LEU A 426 ? 1.1828 1.1168 0.8185 0.2710  -0.1109 -0.0263 426 LEU A CG  
2921  C CD1 . LEU A 426 ? 1.1960 1.0924 0.8374 0.2564  -0.0920 -0.0096 426 LEU A CD1 
2922  C CD2 . LEU A 426 ? 1.1449 1.1170 0.8161 0.2682  -0.1317 -0.0471 426 LEU A CD2 
2923  N N   . ARG A 427 ? 1.2521 1.1282 0.7518 0.3117  -0.0696 0.0110  427 ARG A N   
2924  C CA  . ARG A 427 ? 1.2748 1.1420 0.7663 0.2976  -0.0547 0.0101  427 ARG A CA  
2925  C C   . ARG A 427 ? 1.3181 1.1378 0.7899 0.2837  -0.0220 0.0291  427 ARG A C   
2926  O O   . ARG A 427 ? 1.3244 1.1425 0.8176 0.2573  -0.0093 0.0235  427 ARG A O   
2927  C CB  . ARG A 427 ? 1.2812 1.1636 0.7337 0.3224  -0.0607 0.0077  427 ARG A CB  
2928  C CG  . ARG A 427 ? 1.3116 1.1776 0.7425 0.3131  -0.0397 0.0120  427 ARG A CG  
2929  C CD  . ARG A 427 ? 1.3204 1.1979 0.7059 0.3412  -0.0442 0.0122  427 ARG A CD  
2930  N NE  . ARG A 427 ? 1.3652 1.1981 0.6894 0.3613  -0.0199 0.0384  427 ARG A NE  
2931  C CZ  . ARG A 427 ? 1.3737 1.2074 0.6474 0.3997  -0.0259 0.0473  427 ARG A CZ  
2932  N NH1 . ARG A 427 ? 1.3383 1.2235 0.6194 0.4205  -0.0569 0.0290  427 ARG A NH1 
2933  N NH2 . ARG A 427 ? 1.4189 1.2004 0.6311 0.4180  0.0013  0.0739  427 ARG A NH2 
2934  N N   . ASP A 428 ? 1.3303 1.1114 0.7605 0.3013  -0.0070 0.0501  428 ASP A N   
2935  C CA  . ASP A 428 ? 1.3749 1.1032 0.7794 0.2872  0.0289  0.0673  428 ASP A CA  
2936  C C   . ASP A 428 ? 1.3724 1.0837 0.8088 0.2646  0.0371  0.0686  428 ASP A C   
2937  O O   . ASP A 428 ? 1.4068 1.0735 0.8245 0.2497  0.0684  0.0800  428 ASP A O   
2938  C CB  . ASP A 428 ? 1.4107 1.0937 0.7443 0.3194  0.0464  0.0910  428 ASP A CB  
2939  C CG  . ASP A 428 ? 1.4086 1.1145 0.7071 0.3500  0.0330  0.0896  428 ASP A CG  
2940  O OD1 . ASP A 428 ? 1.3947 1.1361 0.7146 0.3381  0.0234  0.0730  428 ASP A OD1 
2941  O OD2 . ASP A 428 ? 1.4199 1.1091 0.6670 0.3884  0.0319  0.1046  428 ASP A OD2 
2942  N N   . CYS A 429 ? 1.2887 1.0332 0.7714 0.2603  0.0119  0.0560  429 CYS A N   
2943  C CA  . CYS A 429 ? 1.2807 1.0132 0.7942 0.2413  0.0170  0.0564  429 CYS A CA  
2944  C C   . CYS A 429 ? 1.2835 1.0288 0.8356 0.2061  0.0261  0.0434  429 CYS A C   
2945  O O   . CYS A 429 ? 1.2512 1.0357 0.8403 0.1980  0.0070  0.0267  429 CYS A O   
2946  C CB  . CYS A 429 ? 1.2295 0.9944 0.7745 0.2518  -0.0125 0.0474  429 CYS A CB  
2947  S SG  . CYS A 429 ? 1.2044 0.9594 0.7869 0.2328  -0.0102 0.0473  429 CYS A SG  
2948  N N   . LYS A 430 ? 1.2202 0.9328 0.7626 0.1860  0.0564  0.0495  430 LYS A N   
2949  C CA  . LYS A 430 ? 1.2123 0.9434 0.7855 0.1549  0.0682  0.0353  430 LYS A CA  
2950  C C   . LYS A 430 ? 1.1857 0.9303 0.8033 0.1350  0.0640  0.0258  430 LYS A C   
2951  O O   . LYS A 430 ? 1.1672 0.9360 0.8132 0.1125  0.0706  0.0117  430 LYS A O   
2952  C CB  . LYS A 430 ? 1.2511 0.9472 0.7917 0.1396  0.1063  0.0416  430 LYS A CB  
2953  C CG  . LYS A 430 ? 1.2825 0.9515 0.7674 0.1619  0.1166  0.0559  430 LYS A CG  
2954  C CD  . LYS A 430 ? 1.3189 0.9513 0.7724 0.1416  0.1588  0.0602  430 LYS A CD  
2955  C CE  . LYS A 430 ? 1.3196 0.9763 0.7632 0.1414  0.1621  0.0531  430 LYS A CE  
2956  N NZ  . LYS A 430 ? 1.3622 0.9730 0.7585 0.1297  0.2054  0.0622  430 LYS A NZ  
2957  N N   . SER A 431 ? 1.1669 0.9007 0.7909 0.1443  0.0528  0.0322  431 SER A N   
2958  C CA  . SER A 431 ? 1.1376 0.8806 0.7993 0.1268  0.0504  0.0246  431 SER A CA  
2959  C C   . SER A 431 ? 1.0851 0.8690 0.7864 0.1299  0.0207  0.0123  431 SER A C   
2960  O O   . SER A 431 ? 1.0541 0.8457 0.7842 0.1197  0.0161  0.0073  431 SER A O   
2961  C CB  . SER A 431 ? 1.1472 0.8513 0.7926 0.1333  0.0592  0.0382  431 SER A CB  
2962  O OG  . SER A 431 ? 1.1221 0.8261 0.7535 0.1628  0.0391  0.0468  431 SER A OG  
2963  N N   . LEU A 432 ? 1.0622 0.8692 0.7632 0.1430  0.0028  0.0067  432 LEU A N   
2964  C CA  . LEU A 432 ? 1.0161 0.8518 0.7483 0.1455  -0.0214 -0.0049 432 LEU A CA  
2965  C C   . LEU A 432 ? 0.9843 0.8395 0.7476 0.1282  -0.0199 -0.0168 432 LEU A C   
2966  O O   . LEU A 432 ? 0.9930 0.8571 0.7553 0.1181  -0.0068 -0.0220 432 LEU A O   
2967  C CB  . LEU A 432 ? 1.0110 0.8642 0.7334 0.1603  -0.0366 -0.0114 432 LEU A CB  
2968  C CG  . LEU A 432 ? 1.0182 0.8659 0.7142 0.1826  -0.0453 -0.0040 432 LEU A CG  
2969  C CD1 . LEU A 432 ? 1.0154 0.8854 0.7028 0.1942  -0.0589 -0.0144 432 LEU A CD1 
2970  C CD2 . LEU A 432 ? 0.9800 0.8327 0.6937 0.1877  -0.0589 -0.0047 432 LEU A CD2 
2971  N N   . ILE A 433 ? 0.9337 0.7976 0.7233 0.1262  -0.0327 -0.0218 433 ILE A N   
2972  C CA  . ILE A 433 ? 0.9000 0.7818 0.7149 0.1164  -0.0338 -0.0320 433 ILE A CA  
2973  C C   . ILE A 433 ? 0.8655 0.7574 0.6917 0.1246  -0.0513 -0.0403 433 ILE A C   
2974  O O   . ILE A 433 ? 0.8562 0.7613 0.6844 0.1271  -0.0532 -0.0491 433 ILE A O   
2975  C CB  . ILE A 433 ? 0.8848 0.7610 0.7161 0.1055  -0.0276 -0.0297 433 ILE A CB  
2976  C CG1 . ILE A 433 ? 0.9256 0.7852 0.7429 0.0946  -0.0062 -0.0235 433 ILE A CG1 
2977  C CG2 . ILE A 433 ? 0.8535 0.7522 0.7069 0.1001  -0.0298 -0.0404 433 ILE A CG2 
2978  C CD1 . ILE A 433 ? 0.9154 0.7722 0.7491 0.0810  0.0024  -0.0251 433 ILE A CD1 
2979  N N   . ARG A 434 ? 0.8934 0.7781 0.7262 0.1284  -0.0622 -0.0390 434 ARG A N   
2980  C CA  . ARG A 434 ? 0.8739 0.7624 0.7151 0.1323  -0.0750 -0.0489 434 ARG A CA  
2981  C C   . ARG A 434 ? 0.8956 0.7875 0.7265 0.1409  -0.0848 -0.0512 434 ARG A C   
2982  O O   . ARG A 434 ? 0.8995 0.7899 0.7278 0.1449  -0.0868 -0.0448 434 ARG A O   
2983  C CB  . ARG A 434 ? 0.8404 0.7233 0.7018 0.1263  -0.0777 -0.0503 434 ARG A CB  
2984  C CG  . ARG A 434 ? 0.8178 0.7012 0.6864 0.1245  -0.0735 -0.0540 434 ARG A CG  
2985  C CD  . ARG A 434 ? 0.7912 0.6645 0.6742 0.1204  -0.0748 -0.0541 434 ARG A CD  
2986  N NE  . ARG A 434 ? 0.7918 0.6531 0.6749 0.1212  -0.0796 -0.0626 434 ARG A NE  
2987  C CZ  . ARG A 434 ? 0.7862 0.6346 0.6632 0.1259  -0.0766 -0.0674 434 ARG A CZ  
2988  N NH1 . ARG A 434 ? 0.7777 0.6316 0.6491 0.1340  -0.0720 -0.0650 434 ARG A NH1 
2989  N NH2 . ARG A 434 ? 0.7951 0.6248 0.6700 0.1231  -0.0768 -0.0761 434 ARG A NH2 
2990  N N   . VAL A 435 ? 0.8967 0.7957 0.7206 0.1456  -0.0910 -0.0619 435 VAL A N   
2991  C CA  . VAL A 435 ? 0.9165 0.8272 0.7320 0.1538  -0.1018 -0.0696 435 VAL A CA  
2992  C C   . VAL A 435 ? 0.9011 0.8138 0.7287 0.1481  -0.1085 -0.0876 435 VAL A C   
2993  O O   . VAL A 435 ? 0.8923 0.7974 0.7156 0.1473  -0.1049 -0.0935 435 VAL A O   
2994  C CB  . VAL A 435 ? 0.9376 0.8538 0.7262 0.1650  -0.0999 -0.0665 435 VAL A CB  
2995  C CG1 . VAL A 435 ? 0.9400 0.8727 0.7161 0.1783  -0.1115 -0.0714 435 VAL A CG1 
2996  C CG2 . VAL A 435 ? 0.9541 0.8578 0.7284 0.1650  -0.0852 -0.0498 435 VAL A CG2 
2997  N N   . ARG A 436 ? 0.9603 0.8824 0.8022 0.1440  -0.1162 -0.0975 436 ARG A N   
2998  C CA  . ARG A 436 ? 0.9460 0.8652 0.7998 0.1335  -0.1181 -0.1170 436 ARG A CA  
2999  C C   . ARG A 436 ? 0.9477 0.8965 0.8028 0.1358  -0.1296 -0.1351 436 ARG A C   
3000  O O   . ARG A 436 ? 0.9440 0.9149 0.8098 0.1377  -0.1365 -0.1373 436 ARG A O   
3001  C CB  . ARG A 436 ? 0.9309 0.8359 0.8050 0.1208  -0.1128 -0.1167 436 ARG A CB  
3002  C CG  . ARG A 436 ? 0.9166 0.7976 0.7889 0.1204  -0.1027 -0.1024 436 ARG A CG  
3003  C CD  . ARG A 436 ? 0.9014 0.7596 0.7844 0.1097  -0.0954 -0.1074 436 ARG A CD  
3004  N NE  . ARG A 436 ? 0.9106 0.7534 0.7881 0.1037  -0.0920 -0.1249 436 ARG A NE  
3005  C CZ  . ARG A 436 ? 0.9105 0.7193 0.7770 0.1038  -0.0811 -0.1260 436 ARG A CZ  
3006  N NH1 . ARG A 436 ? 0.8962 0.6902 0.7572 0.1117  -0.0750 -0.1114 436 ARG A NH1 
3007  N NH2 . ARG A 436 ? 0.9277 0.7165 0.7859 0.0973  -0.0754 -0.1432 436 ARG A NH2 
3008  N N   . PHE A 437 ? 0.9616 0.9143 0.8058 0.1370  -0.1318 -0.1499 437 PHE A N   
3009  C CA  . PHE A 437 ? 0.9581 0.9447 0.8028 0.1392  -0.1431 -0.1717 437 PHE A CA  
3010  C C   . PHE A 437 ? 0.9531 0.9341 0.8113 0.1199  -0.1396 -0.1995 437 PHE A C   
3011  O O   . PHE A 437 ? 0.9479 0.9599 0.8092 0.1175  -0.1477 -0.2240 437 PHE A O   
3012  C CB  . PHE A 437 ? 0.9672 0.9657 0.7848 0.1564  -0.1480 -0.1694 437 PHE A CB  
3013  C CG  . PHE A 437 ? 0.9732 0.9883 0.7732 0.1769  -0.1533 -0.1511 437 PHE A CG  
3014  C CD1 . PHE A 437 ? 0.9773 0.9791 0.7800 0.1794  -0.1481 -0.1295 437 PHE A CD1 
3015  C CD2 . PHE A 437 ? 0.9763 1.0162 0.7526 0.1950  -0.1618 -0.1555 437 PHE A CD2 
3016  C CE1 . PHE A 437 ? 0.9858 0.9924 0.7659 0.1992  -0.1490 -0.1120 437 PHE A CE1 
3017  C CE2 . PHE A 437 ? 0.9848 1.0312 0.7367 0.2172  -0.1635 -0.1367 437 PHE A CE2 
3018  C CZ  . PHE A 437 ? 0.9906 1.0171 0.7432 0.2191  -0.1560 -0.1146 437 PHE A CZ  
3019  N N   . LYS A 438 ? 0.9656 0.9070 0.8297 0.1065  -0.1261 -0.1972 438 LYS A N   
3020  C CA  . LYS A 438 ? 0.9722 0.8895 0.8378 0.0895  -0.1162 -0.2200 438 LYS A CA  
3021  C C   . LYS A 438 ? 0.9647 0.9122 0.8522 0.0714  -0.1194 -0.2502 438 LYS A C   
3022  O O   . LYS A 438 ? 0.9517 0.9255 0.8598 0.0672  -0.1243 -0.2505 438 LYS A O   
3023  C CB  . LYS A 438 ? 0.9767 0.8438 0.8409 0.0824  -0.0998 -0.2082 438 LYS A CB  
3024  C CG  . LYS A 438 ? 0.9957 0.8187 0.8468 0.0721  -0.0843 -0.2240 438 LYS A CG  
3025  C CD  . LYS A 438 ? 1.0019 0.7760 0.8487 0.0680  -0.0677 -0.2115 438 LYS A CD  
3026  C CE  . LYS A 438 ? 1.0268 0.7466 0.8451 0.0730  -0.0517 -0.2141 438 LYS A CE  
3027  N NZ  . LYS A 438 ? 1.0522 0.7516 0.8680 0.0522  -0.0401 -0.2444 438 LYS A NZ  
3028  N N   . GLY A 439 ? 1.0031 0.9503 0.8869 0.0603  -0.1161 -0.2782 439 GLY A N   
3029  C CA  . GLY A 439 ? 0.9935 0.9690 0.9000 0.0371  -0.1151 -0.3137 439 GLY A CA  
3030  C C   . GLY A 439 ? 0.9682 1.0188 0.8905 0.0455  -0.1358 -0.3279 439 GLY A C   
3031  O O   . GLY A 439 ? 0.9509 1.0327 0.8979 0.0381  -0.1392 -0.3345 439 GLY A O   
3032  N N   . ASN A 440 ? 0.9889 1.0704 0.8948 0.0636  -0.1495 -0.3330 440 ASN A N   
3033  C CA  . ASN A 440 ? 0.9654 1.1196 0.8779 0.0788  -0.1701 -0.3465 440 ASN A CA  
3034  C C   . ASN A 440 ? 0.9640 1.1435 0.8614 0.0839  -0.1776 -0.3707 440 ASN A C   
3035  O O   . ASN A 440 ? 0.9805 1.1225 0.8692 0.0691  -0.1651 -0.3832 440 ASN A O   
3036  C CB  . ASN A 440 ? 0.9655 1.1288 0.8630 0.1101  -0.1810 -0.3099 440 ASN A CB  
3037  C CG  . ASN A 440 ? 0.9585 1.1212 0.8767 0.1063  -0.1787 -0.2962 440 ASN A CG  
3038  O OD1 . ASN A 440 ? 0.9364 1.1503 0.8756 0.1063  -0.1881 -0.3134 440 ASN A OD1 
3039  N ND2 . ASN A 440 ? 0.9748 1.0840 0.8872 0.1045  -0.1665 -0.2665 440 ASN A ND2 
3040  N N   . SER A 441 ? 1.0020 1.2444 0.8933 0.1072  -0.1975 -0.3778 441 SER A N   
3041  C CA  . SER A 441 ? 0.9982 1.2725 0.8716 0.1178  -0.2074 -0.3990 441 SER A CA  
3042  C C   . SER A 441 ? 1.0052 1.2879 0.8425 0.1571  -0.2193 -0.3682 441 SER A C   
3043  O O   . SER A 441 ? 0.9919 1.3269 0.8143 0.1782  -0.2350 -0.3821 441 SER A O   
3044  C CB  . SER A 441 ? 0.9649 1.3168 0.8628 0.1083  -0.2197 -0.4463 441 SER A CB  
3045  O OG  . SER A 441 ? 0.9635 1.2999 0.8888 0.0667  -0.2033 -0.4809 441 SER A OG  
3046  N N   . PHE A 442 ? 1.0022 1.2333 0.8233 0.1670  -0.2104 -0.3272 442 PHE A N   
3047  C CA  . PHE A 442 ? 1.0143 1.2417 0.7986 0.1995  -0.2151 -0.2968 442 PHE A CA  
3048  C C   . PHE A 442 ? 1.0245 1.2501 0.7829 0.2066  -0.2155 -0.3058 442 PHE A C   
3049  O O   . PHE A 442 ? 1.0305 1.2352 0.7965 0.1856  -0.2073 -0.3252 442 PHE A O   
3050  C CB  . PHE A 442 ? 1.0341 1.2055 0.8108 0.2007  -0.2014 -0.2572 442 PHE A CB  
3051  C CG  . PHE A 442 ? 1.0270 1.2011 0.8197 0.2022  -0.2021 -0.2425 442 PHE A CG  
3052  C CD1 . PHE A 442 ? 1.0159 1.2300 0.7985 0.2278  -0.2149 -0.2380 442 PHE A CD1 
3053  C CD2 . PHE A 442 ? 1.0316 1.1675 0.8462 0.1811  -0.1896 -0.2327 442 PHE A CD2 
3054  C CE1 . PHE A 442 ? 1.0100 1.2248 0.8059 0.2309  -0.2148 -0.2246 442 PHE A CE1 
3055  C CE2 . PHE A 442 ? 1.0256 1.1640 0.8546 0.1824  -0.1899 -0.2198 442 PHE A CE2 
3056  C CZ  . PHE A 442 ? 1.0151 1.1923 0.8355 0.2067  -0.2023 -0.2160 442 PHE A CZ  
3057  N N   . SER A 443 ? 0.7778 1.3417 0.9035 0.2325  -0.3899 -0.3069 443 SER A N   
3058  C CA  . SER A 443 ? 0.8230 1.3749 0.8889 0.2292  -0.3981 -0.3186 443 SER A CA  
3059  C C   . SER A 443 ? 0.8740 1.3533 0.8187 0.2650  -0.3987 -0.2704 443 SER A C   
3060  O O   . SER A 443 ? 0.8794 1.3194 0.7890 0.2919  -0.3929 -0.2304 443 SER A O   
3061  C CB  . SER A 443 ? 0.8731 1.4961 0.9674 0.2402  -0.4231 -0.3586 443 SER A CB  
3062  O OG  . SER A 443 ? 0.9106 1.5626 0.9984 0.2839  -0.4420 -0.3463 443 SER A OG  
3063  N N   . GLY A 444 ? 0.9363 1.3925 0.8179 0.2650  -0.4008 -0.2742 444 GLY A N   
3064  C CA  . GLY A 444 ? 0.9981 1.3824 0.7656 0.2981  -0.3946 -0.2314 444 GLY A CA  
3065  C C   . GLY A 444 ? 1.0197 1.3365 0.7483 0.2683  -0.3676 -0.2164 444 GLY A C   
3066  O O   . GLY A 444 ? 0.9883 1.3059 0.7802 0.2190  -0.3456 -0.2336 444 GLY A O   
3067  N N   . ASP A 445 ? 1.0868 1.3328 0.7162 0.2958  -0.3548 -0.1772 445 ASP A N   
3068  C CA  . ASP A 445 ? 1.1202 1.2902 0.7166 0.2663  -0.3159 -0.1541 445 ASP A CA  
3069  C C   . ASP A 445 ? 1.1170 1.2312 0.7449 0.2405  -0.2793 -0.1198 445 ASP A C   
3070  O O   . ASP A 445 ? 1.1369 1.2192 0.7409 0.2661  -0.2738 -0.0885 445 ASP A O   
3071  C CB  . ASP A 445 ? 1.1923 1.3061 0.6747 0.3070  -0.3112 -0.1262 445 ASP A CB  
3072  C CG  . ASP A 445 ? 1.2257 1.2754 0.6804 0.2769  -0.2743 -0.1116 445 ASP A CG  
3073  O OD1 . ASP A 445 ? 1.2413 1.2288 0.7034 0.2566  -0.2370 -0.0774 445 ASP A OD1 
3074  O OD2 . ASP A 445 ? 1.2361 1.3002 0.6648 0.2736  -0.2830 -0.1367 445 ASP A OD2 
3075  N N   . ILE A 446 ? 1.0876 1.1892 0.7661 0.1922  -0.2539 -0.1270 446 ILE A N   
3076  C CA  . ILE A 446 ? 1.0770 1.1393 0.7924 0.1689  -0.2257 -0.1031 446 ILE A CA  
3077  C C   . ILE A 446 ? 1.1335 1.1164 0.7882 0.1801  -0.2007 -0.0603 446 ILE A C   
3078  O O   . ILE A 446 ? 1.1358 1.0867 0.8037 0.1787  -0.1870 -0.0389 446 ILE A O   
3079  C CB  . ILE A 446 ? 1.0396 1.1085 0.8162 0.1221  -0.2044 -0.1208 446 ILE A CB  
3080  C CG1 . ILE A 446 ? 1.0179 1.0654 0.8395 0.1056  -0.1846 -0.1051 446 ILE A CG1 
3081  C CG2 . ILE A 446 ? 1.0711 1.0986 0.8103 0.1052  -0.1824 -0.1125 446 ILE A CG2 
3082  C CD1 . ILE A 446 ? 0.9790 1.0731 0.8573 0.1118  -0.1982 -0.1212 446 ILE A CD1 
3083  N N   . SER A 447 ? 1.2135 1.1609 0.8023 0.1918  -0.1917 -0.0488 447 SER A N   
3084  C CA  . SER A 447 ? 1.2712 1.1405 0.8076 0.2024  -0.1615 -0.0093 447 SER A CA  
3085  C C   . SER A 447 ? 1.3075 1.1535 0.7835 0.2527  -0.1685 0.0138  447 SER A C   
3086  O O   . SER A 447 ? 1.3477 1.1262 0.7950 0.2604  -0.1391 0.0465  447 SER A O   
3087  C CB  . SER A 447 ? 1.3130 1.1454 0.8030 0.1965  -0.1406 -0.0025 447 SER A CB  
3088  O OG  . SER A 447 ? 1.3427 1.1855 0.7614 0.2362  -0.1600 -0.0085 447 SER A OG  
3089  N N   . GLU A 448 ? 1.3464 1.2474 0.8051 0.2880  -0.2051 -0.0039 448 GLU A N   
3090  C CA  . GLU A 448 ? 1.3762 1.2624 0.7774 0.3428  -0.2139 0.0180  448 GLU A CA  
3091  C C   . GLU A 448 ? 1.3367 1.2517 0.7913 0.3463  -0.2260 0.0168  448 GLU A C   
3092  O O   . GLU A 448 ? 1.3639 1.2480 0.7762 0.3866  -0.2212 0.0432  448 GLU A O   
3093  C CB  . GLU A 448 ? 1.3868 1.3216 0.7321 0.3892  -0.2508 -0.0007 448 GLU A CB  
3094  C CG  . GLU A 448 ? 1.4612 1.3306 0.6984 0.4370  -0.2313 0.0313  448 GLU A CG  
3095  C CD  . GLU A 448 ? 1.4718 1.3936 0.6855 0.4625  -0.2576 0.0028  448 GLU A CD  
3096  O OE1 . GLU A 448 ? 1.4274 1.4389 0.7005 0.4586  -0.2968 -0.0367 448 GLU A OE1 
3097  O OE2 . GLU A 448 ? 1.5377 1.4102 0.6772 0.4861  -0.2374 0.0185  448 GLU A OE2 
3098  N N   . ALA A 449 ? 1.1900 1.1582 0.7328 0.3080  -0.2371 -0.0115 449 ALA A N   
3099  C CA  . ALA A 449 ? 1.1520 1.1510 0.7470 0.3130  -0.2478 -0.0149 449 ALA A CA  
3100  C C   . ALA A 449 ? 1.1663 1.0968 0.7669 0.2994  -0.2155 0.0144  449 ALA A C   
3101  O O   . ALA A 449 ? 1.1700 1.0879 0.7627 0.3263  -0.2156 0.0302  449 ALA A O   
3102  C CB  . ALA A 449 ? 1.0879 1.1607 0.7735 0.2786  -0.2637 -0.0549 449 ALA A CB  
3103  N N   . PHE A 450 ? 1.1214 1.0091 0.7363 0.2595  -0.1885 0.0196  450 PHE A N   
3104  C CA  . PHE A 450 ? 1.1238 0.9611 0.7605 0.2392  -0.1637 0.0353  450 PHE A CA  
3105  C C   . PHE A 450 ? 1.1809 0.9384 0.7699 0.2373  -0.1310 0.0624  450 PHE A C   
3106  O O   . PHE A 450 ? 1.2068 0.9497 0.7716 0.2285  -0.1202 0.0644  450 PHE A O   
3107  C CB  . PHE A 450 ? 1.0797 0.9410 0.7847 0.1951  -0.1602 0.0145  450 PHE A CB  
3108  C CG  . PHE A 450 ? 1.0266 0.9571 0.7865 0.1936  -0.1816 -0.0115 450 PHE A CG  
3109  C CD1 . PHE A 450 ? 1.0048 0.9420 0.7944 0.2027  -0.1838 -0.0102 450 PHE A CD1 
3110  C CD2 . PHE A 450 ? 1.0016 0.9881 0.7854 0.1834  -0.1961 -0.0388 450 PHE A CD2 
3111  C CE1 . PHE A 450 ? 0.9633 0.9621 0.8098 0.2014  -0.1973 -0.0337 450 PHE A CE1 
3112  C CE2 . PHE A 450 ? 0.9564 1.0059 0.8013 0.1792  -0.2102 -0.0658 450 PHE A CE2 
3113  C CZ  . PHE A 450 ? 0.9397 0.9955 0.8179 0.1885  -0.2095 -0.0622 450 PHE A CZ  
3114  N N   . GLY A 451 ? 1.1561 0.8600 0.7353 0.2448  -0.1119 0.0819  451 GLY A N   
3115  C CA  . GLY A 451 ? 1.2073 0.8318 0.7533 0.2404  -0.0747 0.1050  451 GLY A CA  
3116  C C   . GLY A 451 ? 1.1935 0.7963 0.7916 0.1937  -0.0566 0.0964  451 GLY A C   
3117  O O   . GLY A 451 ? 1.1682 0.8054 0.8035 0.1636  -0.0632 0.0791  451 GLY A O   
3118  N N   . VAL A 452 ? 1.2016 0.7481 0.8027 0.1892  -0.0337 0.1064  452 VAL A N   
3119  C CA  . VAL A 452 ? 1.1832 0.7122 0.8354 0.1483  -0.0202 0.0936  452 VAL A CA  
3120  C C   . VAL A 452 ? 1.1580 0.6826 0.8332 0.1482  -0.0286 0.0849  452 VAL A C   
3121  O O   . VAL A 452 ? 1.1798 0.6721 0.8228 0.1766  -0.0223 0.0992  452 VAL A O   
3122  C CB  . VAL A 452 ? 1.2246 0.6840 0.8667 0.1360  0.0212  0.1073  452 VAL A CB  
3123  C CG1 . VAL A 452 ? 1.2342 0.7029 0.8714 0.1244  0.0309  0.1100  452 VAL A CG1 
3124  C CG2 . VAL A 452 ? 1.2768 0.6713 0.8591 0.1729  0.0469  0.1346  452 VAL A CG2 
3125  N N   . TYR A 453 ? 1.1469 0.7015 0.8723 0.1203  -0.0415 0.0624  453 TYR A N   
3126  C CA  . TYR A 453 ? 1.1194 0.6738 0.8628 0.1222  -0.0521 0.0513  453 TYR A CA  
3127  C C   . TYR A 453 ? 1.1016 0.6437 0.8849 0.0899  -0.0473 0.0313  453 TYR A C   
3128  O O   . TYR A 453 ? 1.0595 0.6442 0.8750 0.0738  -0.0621 0.0144  453 TYR A O   
3129  C CB  . TYR A 453 ? 1.0740 0.6897 0.8322 0.1337  -0.0788 0.0421  453 TYR A CB  
3130  C CG  . TYR A 453 ? 1.0843 0.7308 0.8166 0.1610  -0.0895 0.0529  453 TYR A CG  
3131  C CD1 . TYR A 453 ? 1.1056 0.7342 0.8025 0.1965  -0.0892 0.0693  453 TYR A CD1 
3132  C CD2 . TYR A 453 ? 1.0730 0.7674 0.8152 0.1534  -0.1004 0.0447  453 TYR A CD2 
3133  C CE1 . TYR A 453 ? 1.1101 0.7754 0.7840 0.2259  -0.1042 0.0754  453 TYR A CE1 
3134  C CE2 . TYR A 453 ? 1.0795 0.8076 0.7998 0.1787  -0.1148 0.0478  453 TYR A CE2 
3135  C CZ  . TYR A 453 ? 1.0957 0.8128 0.7826 0.2160  -0.1188 0.0623  453 TYR A CZ  
3136  O OH  . TYR A 453 ? 1.0969 0.8562 0.7626 0.2456  -0.1383 0.0619  453 TYR A OH  
3137  N N   . PRO A 454 ? 1.0994 0.5840 0.8823 0.0813  -0.0257 0.0309  454 PRO A N   
3138  C CA  . PRO A 454 ? 1.0840 0.5640 0.9116 0.0500  -0.0250 0.0048  454 PRO A CA  
3139  C C   . PRO A 454 ? 1.0441 0.5507 0.8867 0.0522  -0.0506 -0.0166 454 PRO A C   
3140  O O   . PRO A 454 ? 1.0199 0.5461 0.8978 0.0320  -0.0607 -0.0412 454 PRO A O   
3141  C CB  . PRO A 454 ? 1.1346 0.5417 0.9575 0.0434  0.0072  0.0075  454 PRO A CB  
3142  C CG  . PRO A 454 ? 1.1766 0.5469 0.9450 0.0737  0.0281  0.0414  454 PRO A CG  
3143  C CD  . PRO A 454 ? 1.1505 0.5718 0.8934 0.1024  -0.0009 0.0513  454 PRO A CD  
3144  N N   . THR A 455 ? 1.1107 0.6181 0.9262 0.0793  -0.0602 -0.0082 455 THR A N   
3145  C CA  . THR A 455 ? 1.0801 0.6009 0.9006 0.0872  -0.0782 -0.0249 455 THR A CA  
3146  C C   . THR A 455 ? 1.0340 0.6108 0.8590 0.1001  -0.0949 -0.0228 455 THR A C   
3147  O O   . THR A 455 ? 1.0105 0.5946 0.8329 0.1136  -0.1043 -0.0312 455 THR A O   
3148  C CB  . THR A 455 ? 1.1064 0.5801 0.8970 0.1088  -0.0704 -0.0178 455 THR A CB  
3149  O OG1 . THR A 455 ? 1.1203 0.5926 0.8827 0.1340  -0.0631 0.0101  455 THR A OG1 
3150  C CG2 . THR A 455 ? 1.1518 0.5640 0.9449 0.0917  -0.0510 -0.0288 455 THR A CG2 
3151  N N   . LEU A 456 ? 1.0057 0.6175 0.8365 0.0969  -0.0951 -0.0127 456 LEU A N   
3152  C CA  . LEU A 456 ? 0.9673 0.6291 0.8085 0.1063  -0.1053 -0.0132 456 LEU A CA  
3153  C C   . LEU A 456 ? 0.9318 0.6156 0.7941 0.0971  -0.1113 -0.0306 456 LEU A C   
3154  O O   . LEU A 456 ? 0.9306 0.6190 0.8083 0.0776  -0.1109 -0.0398 456 LEU A O   
3155  C CB  . LEU A 456 ? 0.9758 0.6671 0.8180 0.1022  -0.1039 -0.0039 456 LEU A CB  
3156  C CG  . LEU A 456 ? 0.9480 0.6899 0.8056 0.1109  -0.1115 -0.0070 456 LEU A CG  
3157  C CD1 . LEU A 456 ? 0.9430 0.6888 0.7948 0.1373  -0.1164 -0.0016 456 LEU A CD1 
3158  C CD2 . LEU A 456 ? 0.9670 0.7344 0.8221 0.1044  -0.1119 -0.0036 456 LEU A CD2 
3159  N N   . ASN A 457 ? 0.9388 0.6356 0.8011 0.1147  -0.1143 -0.0339 457 ASN A N   
3160  C CA  . ASN A 457 ? 0.9113 0.6229 0.7815 0.1170  -0.1163 -0.0467 457 ASN A CA  
3161  C C   . ASN A 457 ? 0.8815 0.6313 0.7687 0.1204  -0.1079 -0.0438 457 ASN A C   
3162  O O   . ASN A 457 ? 0.8679 0.6348 0.7645 0.1138  -0.1044 -0.0498 457 ASN A O   
3163  C CB  . ASN A 457 ? 0.9111 0.5951 0.7606 0.1387  -0.1191 -0.0532 457 ASN A CB  
3164  C CG  . ASN A 457 ? 0.8878 0.5845 0.7334 0.1536  -0.1171 -0.0616 457 ASN A CG  
3165  O OD1 . ASN A 457 ? 0.8636 0.5701 0.7107 0.1707  -0.1043 -0.0543 457 ASN A OD1 
3166  N ND2 . ASN A 457 ? 0.9001 0.5965 0.7416 0.1496  -0.1279 -0.0777 457 ASN A ND2 
3167  N N   . PHE A 458 ? 0.8711 0.6355 0.7660 0.1311  -0.1027 -0.0364 458 PHE A N   
3168  C CA  . PHE A 458 ? 0.8508 0.6491 0.7710 0.1326  -0.0902 -0.0385 458 PHE A CA  
3169  C C   . PHE A 458 ? 0.8684 0.6956 0.8061 0.1301  -0.0939 -0.0356 458 PHE A C   
3170  O O   . PHE A 458 ? 0.8830 0.7025 0.8109 0.1431  -0.1022 -0.0288 458 PHE A O   
3171  C CB  . PHE A 458 ? 0.8292 0.6172 0.7487 0.1558  -0.0768 -0.0394 458 PHE A CB  
3172  C CG  . PHE A 458 ? 0.8122 0.6254 0.7617 0.1570  -0.0539 -0.0426 458 PHE A CG  
3173  C CD1 . PHE A 458 ? 0.8186 0.6650 0.8059 0.1530  -0.0476 -0.0456 458 PHE A CD1 
3174  C CD2 . PHE A 458 ? 0.7957 0.5986 0.7363 0.1649  -0.0367 -0.0444 458 PHE A CD2 
3175  C CE1 . PHE A 458 ? 0.8078 0.6742 0.8313 0.1504  -0.0214 -0.0528 458 PHE A CE1 
3176  C CE2 . PHE A 458 ? 0.7845 0.6005 0.7518 0.1669  -0.0070 -0.0461 458 PHE A CE2 
3177  C CZ  . PHE A 458 ? 0.7906 0.6370 0.8031 0.1567  0.0025  -0.0515 458 PHE A CZ  
3178  N N   . ILE A 459 ? 0.8084 0.6692 0.7696 0.1159  -0.0884 -0.0423 459 ILE A N   
3179  C CA  . ILE A 459 ? 0.8315 0.7287 0.8113 0.1152  -0.0960 -0.0466 459 ILE A CA  
3180  C C   . ILE A 459 ? 0.8251 0.7581 0.8448 0.1026  -0.0810 -0.0619 459 ILE A C   
3181  O O   . ILE A 459 ? 0.8129 0.7410 0.8326 0.0879  -0.0685 -0.0647 459 ILE A O   
3182  C CB  . ILE A 459 ? 0.8612 0.7539 0.8133 0.1086  -0.1107 -0.0401 459 ILE A CB  
3183  C CG1 . ILE A 459 ? 0.8707 0.8063 0.8351 0.1143  -0.1232 -0.0479 459 ILE A CG1 
3184  C CG2 . ILE A 459 ? 0.8676 0.7498 0.8115 0.0870  -0.1038 -0.0405 459 ILE A CG2 
3185  C CD1 . ILE A 459 ? 0.8914 0.8134 0.8166 0.1321  -0.1386 -0.0344 459 ILE A CD1 
3186  N N   . ASP A 460 ? 0.8237 0.7927 0.8819 0.1087  -0.0798 -0.0732 460 ASP A N   
3187  C CA  . ASP A 460 ? 0.8151 0.8193 0.9225 0.0939  -0.0620 -0.0933 460 ASP A CA  
3188  C C   . ASP A 460 ? 0.8305 0.8887 0.9689 0.0934  -0.0820 -0.1113 460 ASP A C   
3189  O O   . ASP A 460 ? 0.8201 0.9023 0.9854 0.1098  -0.0887 -0.1149 460 ASP A O   
3190  C CB  . ASP A 460 ? 0.7793 0.7737 0.9185 0.1024  -0.0304 -0.0950 460 ASP A CB  
3191  C CG  . ASP A 460 ? 0.7604 0.7779 0.9512 0.0845  -0.0007 -0.1151 460 ASP A CG  
3192  O OD1 . ASP A 460 ? 0.7725 0.8153 0.9735 0.0639  -0.0077 -0.1301 460 ASP A OD1 
3193  O OD2 . ASP A 460 ? 0.7332 0.7387 0.9527 0.0919  0.0336  -0.1161 460 ASP A OD2 
3194  N N   . LEU A 461 ? 0.8117 0.8912 0.9452 0.0775  -0.0926 -0.1238 461 LEU A N   
3195  C CA  . LEU A 461 ? 0.7894 0.9248 0.9454 0.0794  -0.1169 -0.1461 461 LEU A CA  
3196  C C   . LEU A 461 ? 0.7626 0.9403 0.9821 0.0562  -0.1017 -0.1807 461 LEU A C   
3197  O O   . LEU A 461 ? 0.7392 0.9644 0.9739 0.0516  -0.1233 -0.2065 461 LEU A O   
3198  C CB  . LEU A 461 ? 0.7930 0.9197 0.8894 0.0834  -0.1413 -0.1377 461 LEU A CB  
3199  C CG  . LEU A 461 ? 0.8196 0.8909 0.8530 0.0980  -0.1456 -0.1042 461 LEU A CG  
3200  C CD1 . LEU A 461 ? 0.8325 0.8785 0.8160 0.0896  -0.1484 -0.0954 461 LEU A CD1 
3201  C CD2 . LEU A 461 ? 0.8291 0.9077 0.8464 0.1293  -0.1661 -0.0938 461 LEU A CD2 
3202  N N   . SER A 462 ? 0.7571 0.9162 1.0120 0.0435  -0.0631 -0.1832 462 SER A N   
3203  C CA  . SER A 462 ? 0.7287 0.9112 1.0393 0.0175  -0.0373 -0.2139 462 SER A CA  
3204  C C   . SER A 462 ? 0.6965 0.9479 1.0855 0.0136  -0.0465 -0.2511 462 SER A C   
3205  O O   . SER A 462 ? 0.6961 0.9734 1.1063 0.0340  -0.0624 -0.2490 462 SER A O   
3206  C CB  . SER A 462 ? 0.7300 0.8680 1.0545 0.0126  0.0129  -0.2030 462 SER A CB  
3207  O OG  . SER A 462 ? 0.7328 0.8168 0.9902 0.0208  0.0161  -0.1715 462 SER A OG  
3208  N N   . ASN A 463 ? 0.6907 0.9738 1.1266 -0.0132 -0.0359 -0.2881 463 ASN A N   
3209  C CA  . ASN A 463 ? 0.6490 1.0054 1.1754 -0.0242 -0.0423 -0.3345 463 ASN A CA  
3210  C C   . ASN A 463 ? 0.6404 1.0568 1.1567 -0.0002 -0.1006 -0.3443 463 ASN A C   
3211  O O   . ASN A 463 ? 0.6292 1.0858 1.1917 0.0170  -0.1116 -0.3497 463 ASN A O   
3212  C CB  . ASN A 463 ? 0.6398 0.9947 1.2431 -0.0257 0.0015  -0.3381 463 ASN A CB  
3213  C CG  . ASN A 463 ? 0.6517 0.9392 1.2515 -0.0391 0.0629  -0.3227 463 ASN A CG  
3214  O OD1 . ASN A 463 ? 0.6470 0.9143 1.2323 -0.0605 0.0798  -0.3318 463 ASN A OD1 
3215  N ND2 . ASN A 463 ? 0.6560 0.9051 1.2631 -0.0222 0.0980  -0.2979 463 ASN A ND2 
3216  N N   . ASN A 464 ? 0.6925 1.1109 1.1425 0.0048  -0.1354 -0.3437 464 ASN A N   
3217  C CA  . ASN A 464 ? 0.6912 1.1593 1.1130 0.0342  -0.1896 -0.3505 464 ASN A CA  
3218  C C   . ASN A 464 ? 0.6825 1.1762 1.0771 0.0242  -0.2145 -0.3810 464 ASN A C   
3219  O O   . ASN A 464 ? 0.6695 1.1519 1.0857 -0.0091 -0.1888 -0.4031 464 ASN A O   
3220  C CB  . ASN A 464 ? 0.7326 1.1493 1.0670 0.0678  -0.2034 -0.2984 464 ASN A CB  
3221  C CG  . ASN A 464 ? 0.7380 1.1553 1.1021 0.0887  -0.1966 -0.2796 464 ASN A CG  
3222  O OD1 . ASN A 464 ? 0.7180 1.1973 1.1235 0.1091  -0.2215 -0.2968 464 ASN A OD1 
3223  N ND2 . ASN A 464 ? 0.7653 1.1148 1.1069 0.0863  -0.1638 -0.2455 464 ASN A ND2 
3224  N N   . ASN A 465 ? 0.7656 1.2897 1.1067 0.0566  -0.2624 -0.3815 465 ASN A N   
3225  C CA  . ASN A 465 ? 0.7659 1.3199 1.0731 0.0565  -0.2922 -0.4132 465 ASN A CA  
3226  C C   . ASN A 465 ? 0.8177 1.3171 1.0029 0.0865  -0.3087 -0.3722 465 ASN A C   
3227  O O   . ASN A 465 ? 0.8332 1.3635 0.9677 0.1148  -0.3480 -0.3859 465 ASN A O   
3228  C CB  . ASN A 465 ? 0.7470 1.3881 1.1033 0.0720  -0.3272 -0.4553 465 ASN A CB  
3229  C CG  . ASN A 465 ? 0.7720 1.4298 1.1136 0.0600  -0.3355 -0.4898 465 ASN A CG  
3230  O OD1 . ASN A 465 ? 0.7632 1.3941 1.1176 0.0230  -0.3069 -0.5052 465 ASN A OD1 
3231  N ND2 . ASN A 465 ? 0.8220 1.5217 1.1337 0.0937  -0.3731 -0.5014 465 ASN A ND2 
3232  N N   . PHE A 466 ? 0.8105 1.2279 0.9477 0.0823  -0.2772 -0.3230 466 PHE A N   
3233  C CA  . PHE A 466 ? 0.8606 1.2195 0.8931 0.1046  -0.2825 -0.2851 466 PHE A CA  
3234  C C   . PHE A 466 ? 0.8748 1.2160 0.8721 0.0850  -0.2755 -0.3005 466 PHE A C   
3235  O O   . PHE A 466 ? 0.8511 1.1888 0.8951 0.0469  -0.2481 -0.3204 466 PHE A O   
3236  C CB  . PHE A 466 ? 0.8830 1.1663 0.8886 0.1019  -0.2510 -0.2350 466 PHE A CB  
3237  C CG  . PHE A 466 ? 0.8848 1.1694 0.8995 0.1279  -0.2580 -0.2133 466 PHE A CG  
3238  C CD1 . PHE A 466 ? 0.9102 1.2001 0.8709 0.1713  -0.2860 -0.1976 466 PHE A CD1 
3239  C CD2 . PHE A 466 ? 0.8667 1.1414 0.9374 0.1129  -0.2334 -0.2067 466 PHE A CD2 
3240  C CE1 . PHE A 466 ? 0.9125 1.1989 0.8796 0.1963  -0.2890 -0.1766 466 PHE A CE1 
3241  C CE2 . PHE A 466 ? 0.8729 1.1441 0.9482 0.1375  -0.2379 -0.1870 466 PHE A CE2 
3242  C CZ  . PHE A 466 ? 0.8930 1.1705 0.9186 0.1778  -0.2655 -0.1722 466 PHE A CZ  
3243  N N   . HIS A 467 ? 0.9080 1.2331 0.8185 0.1142  -0.2964 -0.2897 467 HIS A N   
3244  C CA  . HIS A 467 ? 0.9361 1.2348 0.7963 0.1029  -0.2890 -0.2984 467 HIS A CA  
3245  C C   . HIS A 467 ? 0.9967 1.2133 0.7661 0.1201  -0.2700 -0.2459 467 HIS A C   
3246  O O   . HIS A 467 ? 1.0123 1.1933 0.7647 0.1360  -0.2615 -0.2069 467 HIS A O   
3247  C CB  . HIS A 467 ? 0.9384 1.2993 0.7788 0.1235  -0.3318 -0.3446 467 HIS A CB  
3248  C CG  . HIS A 467 ? 0.9798 1.3404 0.7403 0.1801  -0.3621 -0.3223 467 HIS A CG  
3249  N ND1 . HIS A 467 ? 0.9716 1.3822 0.7637 0.2085  -0.3857 -0.3246 467 HIS A ND1 
3250  C CD2 . HIS A 467 ? 1.0441 1.3510 0.6974 0.2137  -0.3613 -0.2916 467 HIS A CD2 
3251  C CE1 . HIS A 467 ? 1.0424 1.4298 0.7491 0.2577  -0.3983 -0.2966 467 HIS A CE1 
3252  N NE2 . HIS A 467 ? 1.0794 1.4023 0.7015 0.2618  -0.3824 -0.2755 467 HIS A NE2 
3253  N N   . GLY A 468 ? 1.0039 1.1887 0.7184 0.1157  -0.2602 -0.2470 468 GLY A N   
3254  C CA  . GLY A 468 ? 1.0644 1.1716 0.7003 0.1295  -0.2364 -0.2004 468 GLY A CA  
3255  C C   . GLY A 468 ? 1.0610 1.1184 0.7256 0.0915  -0.1925 -0.1775 468 GLY A C   
3256  O O   . GLY A 468 ? 1.0158 1.0923 0.7489 0.0566  -0.1776 -0.1968 468 GLY A O   
3257  N N   . GLN A 469 ? 1.1175 1.1094 0.7288 0.1014  -0.1691 -0.1358 469 GLN A N   
3258  C CA  . GLN A 469 ? 1.1210 1.0678 0.7539 0.0714  -0.1303 -0.1129 469 GLN A CA  
3259  C C   . GLN A 469 ? 1.1269 1.0422 0.7711 0.0762  -0.1196 -0.0792 469 GLN A C   
3260  O O   . GLN A 469 ? 1.1535 1.0556 0.7608 0.1070  -0.1315 -0.0623 469 GLN A O   
3261  C CB  . GLN A 469 ? 1.1750 1.0725 0.7477 0.0729  -0.1066 -0.0976 469 GLN A CB  
3262  C CG  . GLN A 469 ? 1.2373 1.0860 0.7313 0.1099  -0.1027 -0.0650 469 GLN A CG  
3263  C CD  . GLN A 469 ? 1.2811 1.0656 0.7441 0.1018  -0.0616 -0.0358 469 GLN A CD  
3264  O OE1 . GLN A 469 ? 1.3142 1.0786 0.7239 0.1100  -0.0524 -0.0390 469 GLN A OE1 
3265  N NE2 . GLN A 469 ? 1.2797 1.0333 0.7783 0.0860  -0.0363 -0.0096 469 GLN A NE2 
3266  N N   . LEU A 470 ? 1.0433 0.9461 0.7368 0.0477  -0.0965 -0.0710 470 LEU A N   
3267  C CA  . LEU A 470 ? 1.0411 0.9224 0.7560 0.0482  -0.0900 -0.0487 470 LEU A CA  
3268  C C   . LEU A 470 ? 1.1023 0.9255 0.7699 0.0612  -0.0723 -0.0166 470 LEU A C   
3269  O O   . LEU A 470 ? 1.1316 0.9236 0.7803 0.0519  -0.0484 -0.0057 470 LEU A O   
3270  C CB  . LEU A 470 ? 1.0004 0.8853 0.7729 0.0195  -0.0720 -0.0510 470 LEU A CB  
3271  C CG  . LEU A 470 ? 0.9390 0.8694 0.7640 0.0095  -0.0802 -0.0768 470 LEU A CG  
3272  C CD1 . LEU A 470 ? 0.9053 0.8289 0.7709 -0.0104 -0.0572 -0.0736 470 LEU A CD1 
3273  C CD2 . LEU A 470 ? 0.9238 0.8747 0.7613 0.0280  -0.1026 -0.0792 470 LEU A CD2 
3274  N N   . SER A 471 ? 1.0986 0.9044 0.7498 0.0828  -0.0794 -0.0012 471 SER A N   
3275  C CA  . SER A 471 ? 1.1510 0.8948 0.7661 0.0935  -0.0553 0.0289  471 SER A CA  
3276  C C   . SER A 471 ? 1.1391 0.8624 0.8055 0.0636  -0.0332 0.0360  471 SER A C   
3277  O O   . SER A 471 ? 1.0994 0.8505 0.8166 0.0486  -0.0436 0.0236  471 SER A O   
3278  C CB  . SER A 471 ? 1.1690 0.8978 0.7509 0.1276  -0.0667 0.0420  471 SER A CB  
3279  O OG  . SER A 471 ? 1.2097 0.8721 0.7679 0.1338  -0.0362 0.0701  471 SER A OG  
3280  N N   . ALA A 472 ? 1.1513 0.8269 0.8049 0.0570  -0.0020 0.0546  472 ALA A N   
3281  C CA  . ALA A 472 ? 1.1204 0.7812 0.8276 0.0305  0.0166  0.0576  472 ALA A CA  
3282  C C   . ALA A 472 ? 1.1165 0.7545 0.8367 0.0356  0.0152  0.0631  472 ALA A C   
3283  O O   . ALA A 472 ? 1.0879 0.7147 0.8539 0.0144  0.0275  0.0606  472 ALA A O   
3284  C CB  . ALA A 472 ? 1.1320 0.7515 0.8326 0.0206  0.0536  0.0733  472 ALA A CB  
3285  N N   . ASN A 473 ? 1.1843 0.8173 0.8667 0.0639  -0.0001 0.0682  473 ASN A N   
3286  C CA  . ASN A 473 ? 1.1829 0.7909 0.8734 0.0708  0.0003  0.0734  473 ASN A CA  
3287  C C   . ASN A 473 ? 1.1292 0.7726 0.8772 0.0517  -0.0184 0.0535  473 ASN A C   
3288  O O   . ASN A 473 ? 1.1221 0.7411 0.8863 0.0489  -0.0145 0.0535  473 ASN A O   
3289  C CB  . ASN A 473 ? 1.2127 0.8159 0.8496 0.1103  -0.0141 0.0833  473 ASN A CB  
3290  C CG  . ASN A 473 ? 1.2705 0.8189 0.8381 0.1392  0.0108  0.1089  473 ASN A CG  
3291  O OD1 . ASN A 473 ? 1.2903 0.7944 0.8536 0.1270  0.0452  0.1211  473 ASN A OD1 
3292  N ND2 . ASN A 473 ? 1.2927 0.8439 0.8049 0.1811  -0.0045 0.1175  473 ASN A ND2 
3293  N N   . TRP A 474 ? 1.0989 0.7943 0.8733 0.0412  -0.0360 0.0364  474 TRP A N   
3294  C CA  . TRP A 474 ? 1.0481 0.7720 0.8660 0.0311  -0.0505 0.0204  474 TRP A CA  
3295  C C   . TRP A 474 ? 1.0183 0.7279 0.8743 0.0093  -0.0390 0.0154  474 TRP A C   
3296  O O   . TRP A 474 ? 0.9856 0.7020 0.8656 0.0074  -0.0497 0.0043  474 TRP A O   
3297  C CB  . TRP A 474 ? 1.0218 0.7956 0.8584 0.0258  -0.0619 0.0053  474 TRP A CB  
3298  C CG  . TRP A 474 ? 1.0315 0.8325 0.8485 0.0443  -0.0783 0.0002  474 TRP A CG  
3299  C CD1 . TRP A 474 ? 1.0362 0.8561 0.8331 0.0473  -0.0811 -0.0050 474 TRP A CD1 
3300  C CD2 . TRP A 474 ? 1.0095 0.8265 0.8293 0.0629  -0.0955 -0.0039 474 TRP A CD2 
3301  N NE1 . TRP A 474 ? 1.0152 0.8680 0.8073 0.0658  -0.1021 -0.0155 474 TRP A NE1 
3302  C CE2 . TRP A 474 ? 0.9996 0.8521 0.8080 0.0758  -0.1099 -0.0134 474 TRP A CE2 
3303  C CE3 . TRP A 474 ? 0.9947 0.8003 0.8265 0.0707  -0.0999 -0.0021 474 TRP A CE3 
3304  C CZ2 . TRP A 474 ? 0.9780 0.8605 0.7945 0.0959  -0.1285 -0.0209 474 TRP A CZ2 
3305  C CZ3 . TRP A 474 ? 0.9774 0.8053 0.8105 0.0916  -0.1149 -0.0056 474 TRP A CZ3 
3306  C CH2 . TRP A 474 ? 0.9697 0.8383 0.7991 0.1038  -0.1290 -0.0148 474 TRP A CH2 
3307  N N   . GLU A 475 ? 1.0796 0.7716 0.9428 -0.0058 -0.0175 0.0215  475 GLU A N   
3308  C CA  . GLU A 475 ? 1.0532 0.7415 0.9638 -0.0274 -0.0084 0.0119  475 GLU A CA  
3309  C C   . GLU A 475 ? 1.0688 0.7213 0.9878 -0.0280 -0.0055 0.0089  475 GLU A C   
3310  O O   . GLU A 475 ? 1.0422 0.7056 1.0028 -0.0412 -0.0130 -0.0097 475 GLU A O   
3311  C CB  . GLU A 475 ? 1.0659 0.7402 0.9872 -0.0425 0.0189  0.0203  475 GLU A CB  
3312  C CG  . GLU A 475 ? 1.0340 0.7251 1.0180 -0.0655 0.0242  0.0052  475 GLU A CG  
3313  C CD  . GLU A 475 ? 1.0570 0.7076 1.0637 -0.0810 0.0573  0.0115  475 GLU A CD  
3314  O OE1 . GLU A 475 ? 1.0851 0.7020 1.0583 -0.0760 0.0841  0.0324  475 GLU A OE1 
3315  O OE2 . GLU A 475 ? 1.0421 0.6930 1.1006 -0.0975 0.0580  -0.0062 475 GLU A OE2 
3316  N N   . GLN A 476 ? 1.1182 0.7275 0.9956 -0.0113 0.0054  0.0254  476 GLN A N   
3317  C CA  . GLN A 476 ? 1.1397 0.7048 1.0211 -0.0113 0.0153  0.0240  476 GLN A CA  
3318  C C   . GLN A 476 ? 1.1127 0.6956 1.0003 -0.0031 -0.0118 0.0090  476 GLN A C   
3319  O O   . GLN A 476 ? 1.1215 0.6750 1.0241 -0.0091 -0.0075 -0.0013 476 GLN A O   
3320  C CB  . GLN A 476 ? 1.1971 0.7067 1.0228 0.0119  0.0385  0.0502  476 GLN A CB  
3321  C CG  . GLN A 476 ? 1.2259 0.7037 1.0381 0.0075  0.0728  0.0673  476 GLN A CG  
3322  C CD  . GLN A 476 ? 1.2851 0.6992 1.0329 0.0375  0.1005  0.0955  476 GLN A CD  
3323  O OE1 . GLN A 476 ? 1.3065 0.6847 1.0365 0.0522  0.1057  0.1009  476 GLN A OE1 
3324  N NE2 . GLN A 476 ? 1.3141 0.7095 1.0204 0.0507  0.1207  0.1150  476 GLN A NE2 
3325  N N   . SER A 477 ? 1.0827 0.7098 0.9605 0.0102  -0.0362 0.0062  477 SER A N   
3326  C CA  . SER A 477 ? 1.0519 0.6955 0.9363 0.0196  -0.0575 -0.0070 477 SER A CA  
3327  C C   . SER A 477 ? 1.0102 0.6809 0.9358 0.0032  -0.0679 -0.0298 477 SER A C   
3328  O O   . SER A 477 ? 0.9746 0.6834 0.9069 0.0092  -0.0818 -0.0371 477 SER A O   
3329  C CB  . SER A 477 ? 1.0396 0.7179 0.9050 0.0398  -0.0729 -0.0020 477 SER A CB  
3330  O OG  . SER A 477 ? 1.0756 0.7357 0.9033 0.0615  -0.0702 0.0150  477 SER A OG  
3331  N N   . GLN A 478 ? 1.0282 0.6780 0.9828 -0.0159 -0.0589 -0.0422 478 GLN A N   
3332  C CA  . GLN A 478 ? 0.9942 0.6762 0.9924 -0.0304 -0.0705 -0.0668 478 GLN A CA  
3333  C C   . GLN A 478 ? 0.9661 0.6677 0.9591 -0.0144 -0.0958 -0.0841 478 GLN A C   
3334  O O   . GLN A 478 ? 0.9406 0.6757 0.9596 -0.0169 -0.1098 -0.1038 478 GLN A O   
3335  C CB  . GLN A 478 ? 1.0123 0.6690 1.0509 -0.0550 -0.0563 -0.0823 478 GLN A CB  
3336  C CG  . GLN A 478 ? 1.0276 0.6788 1.0890 -0.0738 -0.0291 -0.0709 478 GLN A CG  
3337  C CD  . GLN A 478 ? 0.9886 0.6948 1.0881 -0.0833 -0.0374 -0.0811 478 GLN A CD  
3338  O OE1 . GLN A 478 ? 0.9630 0.6980 1.1123 -0.0955 -0.0494 -0.1086 478 GLN A OE1 
3339  N NE2 . GLN A 478 ? 0.9875 0.7099 1.0637 -0.0759 -0.0313 -0.0610 478 GLN A NE2 
3340  N N   . LYS A 479 ? 0.9685 0.6504 0.9267 0.0058  -0.1010 -0.0766 479 LYS A N   
3341  C CA  . LYS A 479 ? 0.9486 0.6413 0.8945 0.0253  -0.1195 -0.0896 479 LYS A CA  
3342  C C   . LYS A 479 ? 0.9247 0.6466 0.8537 0.0447  -0.1216 -0.0772 479 LYS A C   
3343  O O   . LYS A 479 ? 0.9116 0.6382 0.8266 0.0649  -0.1303 -0.0838 479 LYS A O   
3344  C CB  . LYS A 479 ? 0.9733 0.6215 0.8954 0.0362  -0.1196 -0.0910 479 LYS A CB  
3345  C CG  . LYS A 479 ? 1.0007 0.6133 0.9428 0.0160  -0.1138 -0.1092 479 LYS A CG  
3346  C CD  . LYS A 479 ? 0.9805 0.6237 0.9608 0.0024  -0.1308 -0.1423 479 LYS A CD  
3347  C CE  . LYS A 479 ? 1.0056 0.6157 1.0143 -0.0192 -0.1267 -0.1698 479 LYS A CE  
3348  N NZ  . LYS A 479 ? 1.0277 0.5986 1.0044 -0.0037 -0.1336 -0.1811 479 LYS A NZ  
3349  N N   . LEU A 480 ? 0.8969 0.6357 0.8274 0.0392  -0.1111 -0.0614 480 LEU A N   
3350  C CA  . LEU A 480 ? 0.8775 0.6426 0.8009 0.0528  -0.1088 -0.0538 480 LEU A CA  
3351  C C   . LEU A 480 ? 0.8523 0.6439 0.7860 0.0584  -0.1099 -0.0635 480 LEU A C   
3352  O O   . LEU A 480 ? 0.8491 0.6555 0.8009 0.0461  -0.1098 -0.0696 480 LEU A O   
3353  C CB  . LEU A 480 ? 0.8906 0.6678 0.8136 0.0436  -0.0991 -0.0408 480 LEU A CB  
3354  C CG  . LEU A 480 ? 0.8837 0.6861 0.8053 0.0543  -0.0963 -0.0370 480 LEU A CG  
3355  C CD1 . LEU A 480 ? 0.8928 0.6850 0.8019 0.0727  -0.1022 -0.0329 480 LEU A CD1 
3356  C CD2 . LEU A 480 ? 0.9055 0.7227 0.8260 0.0431  -0.0903 -0.0313 480 LEU A CD2 
3357  N N   . VAL A 481 ? 0.8734 0.6692 0.7951 0.0801  -0.1077 -0.0634 481 VAL A N   
3358  C CA  . VAL A 481 ? 0.8593 0.6729 0.7806 0.0938  -0.1020 -0.0679 481 VAL A CA  
3359  C C   . VAL A 481 ? 0.8427 0.6709 0.7692 0.0982  -0.0805 -0.0586 481 VAL A C   
3360  O O   . VAL A 481 ? 0.8345 0.6752 0.7626 0.1052  -0.0674 -0.0585 481 VAL A O   
3361  C CB  . VAL A 481 ? 0.8609 0.6590 0.7583 0.1212  -0.1113 -0.0777 481 VAL A CB  
3362  C CG1 . VAL A 481 ? 0.8828 0.6708 0.7820 0.1134  -0.1334 -0.0951 481 VAL A CG1 
3363  C CG2 . VAL A 481 ? 0.8510 0.6283 0.7326 0.1377  -0.1039 -0.0701 481 VAL A CG2 
3364  N N   . ALA A 482 ? 0.8396 0.6679 0.7716 0.0954  -0.0750 -0.0529 482 ALA A N   
3365  C CA  . ALA A 482 ? 0.8315 0.6772 0.7800 0.0952  -0.0543 -0.0510 482 ALA A CA  
3366  C C   . ALA A 482 ? 0.8523 0.7140 0.8141 0.0772  -0.0593 -0.0504 482 ALA A C   
3367  O O   . ALA A 482 ? 0.8670 0.7250 0.8249 0.0821  -0.0712 -0.0481 482 ALA A O   
3368  C CB  . ALA A 482 ? 0.8170 0.6532 0.7646 0.1183  -0.0412 -0.0505 482 ALA A CB  
3369  N N   . PHE A 483 ? 0.8194 0.6978 0.7919 0.0604  -0.0501 -0.0524 483 PHE A N   
3370  C CA  . PHE A 483 ? 0.8418 0.7377 0.8205 0.0471  -0.0553 -0.0552 483 PHE A CA  
3371  C C   . PHE A 483 ? 0.8352 0.7549 0.8417 0.0413  -0.0359 -0.0671 483 PHE A C   
3372  O O   . PHE A 483 ? 0.8243 0.7456 0.8359 0.0311  -0.0176 -0.0694 483 PHE A O   
3373  C CB  . PHE A 483 ? 0.8518 0.7415 0.8161 0.0315  -0.0595 -0.0499 483 PHE A CB  
3374  C CG  . PHE A 483 ? 0.8801 0.7782 0.8328 0.0267  -0.0691 -0.0501 483 PHE A CG  
3375  C CD1 . PHE A 483 ? 0.8951 0.8070 0.8488 0.0392  -0.0821 -0.0539 483 PHE A CD1 
3376  C CD2 . PHE A 483 ? 0.8945 0.7874 0.8325 0.0141  -0.0650 -0.0462 483 PHE A CD2 
3377  C CE1 . PHE A 483 ? 0.9141 0.8374 0.8501 0.0422  -0.0945 -0.0551 483 PHE A CE1 
3378  C CE2 . PHE A 483 ? 0.9241 0.8211 0.8400 0.0165  -0.0740 -0.0460 483 PHE A CE2 
3379  C CZ  . PHE A 483 ? 0.9299 0.8437 0.8427 0.0321  -0.0906 -0.0511 483 PHE A CZ  
3380  N N   . ILE A 484 ? 0.8080 0.7465 0.8369 0.0473  -0.0374 -0.0760 484 ILE A N   
3381  C CA  . ILE A 484 ? 0.7999 0.7618 0.8687 0.0397  -0.0153 -0.0928 484 ILE A CA  
3382  C C   . ILE A 484 ? 0.8171 0.8169 0.9041 0.0311  -0.0338 -0.1097 484 ILE A C   
3383  O O   . ILE A 484 ? 0.8334 0.8479 0.9227 0.0442  -0.0547 -0.1097 484 ILE A O   
3384  C CB  . ILE A 484 ? 0.7816 0.7363 0.8731 0.0561  0.0051  -0.0929 484 ILE A CB  
3385  C CG1 . ILE A 484 ? 0.7609 0.6775 0.8199 0.0731  0.0165  -0.0766 484 ILE A CG1 
3386  C CG2 . ILE A 484 ? 0.7671 0.7397 0.9076 0.0451  0.0378  -0.1113 484 ILE A CG2 
3387  C CD1 . ILE A 484 ? 0.7403 0.6396 0.8096 0.0943  0.0445  -0.0741 484 ILE A CD1 
3388  N N   . LEU A 485 ? 0.8284 0.8443 0.9248 0.0122  -0.0270 -0.1247 485 LEU A N   
3389  C CA  . LEU A 485 ? 0.8229 0.8769 0.9274 0.0060  -0.0491 -0.1449 485 LEU A CA  
3390  C C   . LEU A 485 ? 0.7996 0.8802 0.9496 -0.0153 -0.0285 -0.1757 485 LEU A C   
3391  O O   . LEU A 485 ? 0.7894 0.8831 0.9285 -0.0281 -0.0360 -0.1908 485 LEU A O   
3392  C CB  . LEU A 485 ? 0.8321 0.8710 0.8822 0.0066  -0.0689 -0.1322 485 LEU A CB  
3393  C CG  . LEU A 485 ? 0.8427 0.9053 0.8722 0.0232  -0.1028 -0.1359 485 LEU A CG  
3394  C CD1 . LEU A 485 ? 0.8695 0.9026 0.8375 0.0287  -0.1130 -0.1173 485 LEU A CD1 
3395  C CD2 . LEU A 485 ? 0.8224 0.9403 0.8895 0.0183  -0.1145 -0.1714 485 LEU A CD2 
3396  N N   . SER A 486 ? 0.7889 0.8719 0.9887 -0.0193 0.0026  -0.1857 486 SER A N   
3397  C CA  . SER A 486 ? 0.7654 0.8625 1.0104 -0.0428 0.0321  -0.2150 486 SER A CA  
3398  C C   . SER A 486 ? 0.7455 0.9034 1.0462 -0.0525 0.0132  -0.2549 486 SER A C   
3399  O O   . SER A 486 ? 0.7493 0.9397 1.0634 -0.0367 -0.0158 -0.2576 486 SER A O   
3400  C CB  . SER A 486 ? 0.7629 0.8292 1.0377 -0.0422 0.0835  -0.2090 486 SER A CB  
3401  O OG  . SER A 486 ? 0.7671 0.8454 1.0820 -0.0293 0.0894  -0.2110 486 SER A OG  
3402  N N   . ASN A 487 ? 0.7750 0.9501 1.1082 -0.0779 0.0290  -0.2885 487 ASN A N   
3403  C CA  . ASN A 487 ? 0.7449 0.9834 1.1473 -0.0929 0.0167  -0.3377 487 ASN A CA  
3404  C C   . ASN A 487 ? 0.7435 1.0323 1.1223 -0.0752 -0.0443 -0.3476 487 ASN A C   
3405  O O   . ASN A 487 ? 0.7297 1.0700 1.1551 -0.0644 -0.0663 -0.3651 487 ASN A O   
3406  C CB  . ASN A 487 ? 0.7335 0.9873 1.2194 -0.0960 0.0488  -0.3512 487 ASN A CB  
3407  C CG  . ASN A 487 ? 0.6902 1.0074 1.2689 -0.1211 0.0509  -0.4100 487 ASN A CG  
3408  O OD1 . ASN A 487 ? 0.6721 1.0021 1.2581 -0.1448 0.0513  -0.4428 487 ASN A OD1 
3409  N ND2 . ASN A 487 ? 0.6725 1.0309 1.3263 -0.1161 0.0530  -0.4257 487 ASN A ND2 
3410  N N   . ASN A 488 ? 0.7436 1.0155 1.0475 -0.0689 -0.0686 -0.3351 488 ASN A N   
3411  C CA  . ASN A 488 ? 0.7501 1.0608 1.0161 -0.0473 -0.1215 -0.3436 488 ASN A CA  
3412  C C   . ASN A 488 ? 0.7517 1.0718 0.9881 -0.0600 -0.1329 -0.3714 488 ASN A C   
3413  O O   . ASN A 488 ? 0.7406 1.0450 1.0014 -0.0893 -0.0995 -0.3902 488 ASN A O   
3414  C CB  . ASN A 488 ? 0.7850 1.0552 0.9740 -0.0175 -0.1388 -0.2941 488 ASN A CB  
3415  C CG  . ASN A 488 ? 0.7863 1.0726 0.9969 0.0062  -0.1516 -0.2798 488 ASN A CG  
3416  O OD1 . ASN A 488 ? 0.7847 1.1127 0.9888 0.0309  -0.1887 -0.2877 488 ASN A OD1 
3417  N ND2 . ASN A 488 ? 0.7933 1.0446 1.0243 0.0028  -0.1203 -0.2578 488 ASN A ND2 
3418  N N   . SER A 489 ? 0.7692 1.1118 0.9495 -0.0351 -0.1774 -0.3748 489 SER A N   
3419  C CA  . SER A 489 ? 0.7844 1.1315 0.9209 -0.0398 -0.1915 -0.3995 489 SER A CA  
3420  C C   . SER A 489 ? 0.8351 1.1160 0.8706 -0.0242 -0.1876 -0.3547 489 SER A C   
3421  O O   . SER A 489 ? 0.8660 1.1479 0.8385 -0.0088 -0.2105 -0.3634 489 SER A O   
3422  C CB  . SER A 489 ? 0.7752 1.1988 0.9171 -0.0185 -0.2443 -0.4421 489 SER A CB  
3423  O OG  . SER A 489 ? 0.7272 1.2156 0.9725 -0.0305 -0.2470 -0.4793 489 SER A OG  
3424  N N   . ILE A 490 ? 0.8237 1.0473 0.8438 -0.0265 -0.1579 -0.3088 490 ILE A N   
3425  C CA  . ILE A 490 ? 0.8708 1.0356 0.8090 -0.0123 -0.1525 -0.2665 490 ILE A CA  
3426  C C   . ILE A 490 ? 0.8876 1.0184 0.8013 -0.0338 -0.1254 -0.2702 490 ILE A C   
3427  O O   . ILE A 490 ? 0.8601 0.9865 0.8206 -0.0624 -0.0936 -0.2845 490 ILE A O   
3428  C CB  . ILE A 490 ? 0.8748 0.9992 0.8134 -0.0071 -0.1352 -0.2227 490 ILE A CB  
3429  C CG1 . ILE A 490 ? 0.8777 1.0231 0.8118 0.0226  -0.1647 -0.2130 490 ILE A CG1 
3430  C CG2 . ILE A 490 ? 0.9174 0.9816 0.7953 -0.0039 -0.1184 -0.1852 490 ILE A CG2 
3431  C CD1 . ILE A 490 ? 0.8509 1.0014 0.8396 0.0183  -0.1534 -0.2063 490 ILE A CD1 
3432  N N   . THR A 491 ? 0.8779 0.9800 0.7142 -0.0167 -0.1339 -0.2553 491 THR A N   
3433  C CA  . THR A 491 ? 0.9089 0.9758 0.7062 -0.0295 -0.1115 -0.2564 491 THR A CA  
3434  C C   . THR A 491 ? 0.9571 0.9613 0.6998 -0.0191 -0.0908 -0.2061 491 THR A C   
3435  O O   . THR A 491 ? 0.9610 0.9494 0.7037 -0.0069 -0.0920 -0.1746 491 THR A O   
3436  C CB  . THR A 491 ? 0.9326 1.0258 0.6856 -0.0158 -0.1409 -0.2924 491 THR A CB  
3437  O OG1 . THR A 491 ? 0.9825 1.0564 0.6547 0.0245  -0.1635 -0.2661 491 THR A OG1 
3438  C CG2 . THR A 491 ? 0.8843 1.0530 0.6998 -0.0206 -0.1715 -0.3447 491 THR A CG2 
3439  N N   . GLY A 492 ? 0.8945 0.8626 0.5949 -0.0252 -0.0693 -0.2009 492 GLY A N   
3440  C CA  . GLY A 492 ? 0.9260 0.8374 0.5824 -0.0173 -0.0456 -0.1572 492 GLY A CA  
3441  C C   . GLY A 492 ? 0.8992 0.7897 0.6019 -0.0410 -0.0101 -0.1368 492 GLY A C   
3442  O O   . GLY A 492 ? 0.8524 0.7623 0.6090 -0.0619 0.0030  -0.1542 492 GLY A O   
3443  N N   . ALA A 493 ? 0.9193 0.7690 0.6005 -0.0351 0.0079  -0.0998 493 ALA A N   
3444  C CA  . ALA A 493 ? 0.8929 0.7271 0.6143 -0.0516 0.0373  -0.0796 493 ALA A CA  
3445  C C   . ALA A 493 ? 0.8786 0.7168 0.6311 -0.0465 0.0274  -0.0617 493 ALA A C   
3446  O O   . ALA A 493 ? 0.9020 0.7372 0.6332 -0.0292 0.0068  -0.0542 493 ALA A O   
3447  C CB  . ALA A 493 ? 0.9270 0.7182 0.6160 -0.0521 0.0672  -0.0557 493 ALA A CB  
3448  N N   . ILE A 494 ? 0.9039 0.7470 0.7032 -0.0588 0.0430  -0.0552 494 ILE A N   
3449  C CA  . ILE A 494 ? 0.8914 0.7371 0.7193 -0.0543 0.0340  -0.0416 494 ILE A CA  
3450  C C   . ILE A 494 ? 0.9388 0.7517 0.7504 -0.0509 0.0436  -0.0168 494 ILE A C   
3451  O O   . ILE A 494 ? 0.9287 0.7276 0.7476 -0.0597 0.0681  -0.0060 494 ILE A O   
3452  C CB  . ILE A 494 ? 0.8364 0.6970 0.7108 -0.0622 0.0470  -0.0434 494 ILE A CB  
3453  C CG1 . ILE A 494 ? 0.7950 0.6795 0.6892 -0.0661 0.0479  -0.0671 494 ILE A CG1 
3454  C CG2 . ILE A 494 ? 0.8226 0.6848 0.7196 -0.0552 0.0344  -0.0328 494 ILE A CG2 
3455  C CD1 . ILE A 494 ? 0.7494 0.6437 0.6807 -0.0631 0.0570  -0.0661 494 ILE A CD1 
3456  N N   . PRO A 495 ? 0.9704 0.7691 0.7643 -0.0383 0.0293  -0.0072 495 PRO A N   
3457  C CA  . PRO A 495 ? 0.9856 0.7464 0.7696 -0.0369 0.0459  0.0152  495 PRO A CA  
3458  C C   . PRO A 495 ? 0.9250 0.6919 0.7641 -0.0522 0.0584  0.0197  495 PRO A C   
3459  O O   . PRO A 495 ? 0.8886 0.6815 0.7634 -0.0543 0.0439  0.0101  495 PRO A O   
3460  C CB  . PRO A 495 ? 1.0149 0.7621 0.7776 -0.0194 0.0282  0.0210  495 PRO A CB  
3461  C CG  . PRO A 495 ? 1.0171 0.7957 0.7622 -0.0071 0.0012  0.0028  495 PRO A CG  
3462  C CD  . PRO A 495 ? 0.9636 0.7785 0.7497 -0.0239 0.0012  -0.0163 495 PRO A CD  
3463  N N   . PRO A 496 ? 0.9572 0.7026 0.8049 -0.0604 0.0851  0.0331  496 PRO A N   
3464  C CA  . PRO A 496 ? 0.9056 0.6687 0.8134 -0.0736 0.0937  0.0326  496 PRO A CA  
3465  C C   . PRO A 496 ? 0.8957 0.6644 0.8379 -0.0750 0.0771  0.0276  496 PRO A C   
3466  O O   . PRO A 496 ? 0.8616 0.6607 0.8503 -0.0800 0.0694  0.0178  496 PRO A O   
3467  C CB  . PRO A 496 ? 0.9078 0.6427 0.8178 -0.0809 0.1278  0.0484  496 PRO A CB  
3468  C CG  . PRO A 496 ? 0.9489 0.6563 0.7929 -0.0707 0.1380  0.0551  496 PRO A CG  
3469  C CD  . PRO A 496 ? 0.9927 0.6992 0.7963 -0.0556 0.1098  0.0479  496 PRO A CD  
3470  N N   . GLU A 497 ? 0.9792 0.7179 0.8961 -0.0676 0.0721  0.0334  497 GLU A N   
3471  C CA  . GLU A 497 ? 0.9721 0.7082 0.9192 -0.0700 0.0601  0.0273  497 GLU A CA  
3472  C C   . GLU A 497 ? 0.9455 0.7164 0.9049 -0.0635 0.0301  0.0114  497 GLU A C   
3473  O O   . GLU A 497 ? 0.9309 0.7070 0.9202 -0.0660 0.0182  0.0016  497 GLU A O   
3474  C CB  . GLU A 497 ? 1.0178 0.7064 0.9257 -0.0590 0.0667  0.0401  497 GLU A CB  
3475  C CG  . GLU A 497 ? 1.0448 0.6864 0.9360 -0.0611 0.1040  0.0590  497 GLU A CG  
3476  C CD  . GLU A 497 ? 1.0756 0.7055 0.9062 -0.0468 0.1128  0.0705  497 GLU A CD  
3477  O OE1 . GLU A 497 ? 1.0842 0.7425 0.8870 -0.0362 0.0873  0.0611  497 GLU A OE1 
3478  O OE2 . GLU A 497 ? 1.0930 0.6845 0.9051 -0.0462 0.1466  0.0870  497 GLU A OE2 
3479  N N   . ILE A 498 ? 0.9164 0.7085 0.8543 -0.0552 0.0204  0.0069  498 ILE A N   
3480  C CA  . ILE A 498 ? 0.8861 0.7058 0.8361 -0.0472 0.0003  -0.0059 498 ILE A CA  
3481  C C   . ILE A 498 ? 0.8521 0.6962 0.8428 -0.0505 -0.0004 -0.0141 498 ILE A C   
3482  O O   . ILE A 498 ? 0.8331 0.6884 0.8361 -0.0420 -0.0169 -0.0237 498 ILE A O   
3483  C CB  . ILE A 498 ? 0.8867 0.7235 0.8166 -0.0414 -0.0014 -0.0115 498 ILE A CB  
3484  C CG1 . ILE A 498 ? 0.9402 0.7626 0.8298 -0.0332 -0.0082 -0.0082 498 ILE A CG1 
3485  C CG2 . ILE A 498 ? 0.8496 0.7084 0.7950 -0.0323 -0.0133 -0.0227 498 ILE A CG2 
3486  C CD1 . ILE A 498 ? 0.9516 0.7685 0.8329 -0.0194 -0.0275 -0.0083 498 ILE A CD1 
3487  N N   . TRP A 499 ? 0.8715 0.7253 0.8802 -0.0588 0.0170  -0.0106 499 TRP A N   
3488  C CA  . TRP A 499 ? 0.8540 0.7377 0.9001 -0.0560 0.0142  -0.0187 499 TRP A CA  
3489  C C   . TRP A 499 ? 0.8520 0.7392 0.9352 -0.0622 0.0022  -0.0287 499 TRP A C   
3490  O O   . TRP A 499 ? 0.8402 0.7582 0.9520 -0.0545 -0.0109 -0.0418 499 TRP A O   
3491  C CB  . TRP A 499 ? 0.8498 0.7448 0.9075 -0.0609 0.0377  -0.0114 499 TRP A CB  
3492  C CG  . TRP A 499 ? 0.8455 0.7279 0.8665 -0.0609 0.0540  -0.0045 499 TRP A CG  
3493  C CD1 . TRP A 499 ? 0.8520 0.7152 0.8559 -0.0703 0.0759  0.0055  499 TRP A CD1 
3494  C CD2 . TRP A 499 ? 0.8370 0.7239 0.8363 -0.0515 0.0516  -0.0105 499 TRP A CD2 
3495  N NE1 . TRP A 499 ? 0.8533 0.7115 0.8250 -0.0682 0.0830  0.0026  499 TRP A NE1 
3496  C CE2 . TRP A 499 ? 0.8421 0.7161 0.8163 -0.0587 0.0696  -0.0080 499 TRP A CE2 
3497  C CE3 . TRP A 499 ? 0.8271 0.7256 0.8275 -0.0376 0.0389  -0.0188 499 TRP A CE3 
3498  C CZ2 . TRP A 499 ? 0.8391 0.7159 0.7986 -0.0565 0.0744  -0.0178 499 TRP A CZ2 
3499  C CZ3 . TRP A 499 ? 0.8167 0.7144 0.8023 -0.0342 0.0481  -0.0243 499 TRP A CZ3 
3500  C CH2 . TRP A 499 ? 0.8219 0.7111 0.7919 -0.0455 0.0652  -0.0257 499 TRP A CH2 
3501  N N   . ASN A 500 ? 0.9874 0.8427 1.0695 -0.0740 0.0073  -0.0248 500 ASN A N   
3502  C CA  . ASN A 500 ? 0.9814 0.8347 1.1033 -0.0835 -0.0007 -0.0390 500 ASN A CA  
3503  C C   . ASN A 500 ? 0.9755 0.8222 1.0825 -0.0725 -0.0256 -0.0505 500 ASN A C   
3504  O O   . ASN A 500 ? 0.9722 0.8133 1.1088 -0.0806 -0.0336 -0.0664 500 ASN A O   
3505  C CB  . ASN A 500 ? 1.0041 0.8165 1.1338 -0.1006 0.0255  -0.0286 500 ASN A CB  
3506  C CG  . ASN A 500 ? 0.9891 0.8179 1.1763 -0.1179 0.0461  -0.0321 500 ASN A CG  
3507  O OD1 . ASN A 500 ? 0.9654 0.8427 1.1933 -0.1167 0.0340  -0.0464 500 ASN A OD1 
3508  N ND2 . ASN A 500 ? 1.0054 0.7933 1.1954 -0.1306 0.0795  -0.0180 500 ASN A ND2 
3509  N N   . MET A 501 ? 0.8715 0.6692 1.0894 -0.0453 -0.1249 0.0078  501 MET A N   
3510  C CA  . MET A 501 ? 0.8787 0.6346 1.0714 -0.0396 -0.1319 -0.0237 501 MET A CA  
3511  C C   . MET A 501 ? 0.8813 0.6329 1.0320 -0.0398 -0.1562 -0.0618 501 MET A C   
3512  O O   . MET A 501 ? 0.8794 0.6347 0.9677 -0.0252 -0.1531 -0.0713 501 MET A O   
3513  C CB  . MET A 501 ? 0.8783 0.6327 1.0324 -0.0201 -0.1130 -0.0129 501 MET A CB  
3514  C CG  . MET A 501 ? 0.8724 0.6468 1.0473 -0.0147 -0.0951 0.0294  501 MET A CG  
3515  S SD  . MET A 501 ? 0.8740 0.6512 1.0238 0.0068  -0.0826 0.0391  501 MET A SD  
3516  C CE  . MET A 501 ? 0.8943 0.6261 1.0374 0.0138  -0.0834 -0.0003 501 MET A CE  
3517  N N   . THR A 502 ? 0.9342 0.6775 1.1221 -0.0570 -0.1818 -0.0829 502 THR A N   
3518  C CA  . THR A 502 ? 0.9378 0.6863 1.0885 -0.0567 -0.2128 -0.1152 502 THR A CA  
3519  C C   . THR A 502 ? 0.9610 0.6673 1.0317 -0.0399 -0.2161 -0.1505 502 THR A C   
3520  O O   . THR A 502 ? 0.9672 0.6791 0.9770 -0.0288 -0.2317 -0.1674 502 THR A O   
3521  C CB  . THR A 502 ? 0.9391 0.6908 1.1577 -0.0817 -0.2456 -0.1328 502 THR A CB  
3522  O OG1 . THR A 502 ? 0.9606 0.6565 1.2006 -0.0926 -0.2503 -0.1584 502 THR A OG1 
3523  C CG2 . THR A 502 ? 0.9198 0.7164 1.2246 -0.0968 -0.2336 -0.0928 502 THR A CG2 
3524  N N   . GLN A 503 ? 1.0013 0.6643 1.0690 -0.0340 -0.1986 -0.1594 503 GLN A N   
3525  C CA  . GLN A 503 ? 1.0360 0.6555 1.0305 -0.0154 -0.1955 -0.1938 503 GLN A CA  
3526  C C   . GLN A 503 ? 1.0317 0.6657 0.9689 0.0077  -0.1658 -0.1776 503 GLN A C   
3527  O O   . GLN A 503 ? 1.0644 0.6674 0.9387 0.0264  -0.1550 -0.2004 503 GLN A O   
3528  C CB  . GLN A 503 ? 1.0671 0.6309 1.0867 -0.0147 -0.1844 -0.2106 503 GLN A CB  
3529  C CG  . GLN A 503 ? 1.0909 0.6164 1.1438 -0.0366 -0.2176 -0.2470 503 GLN A CG  
3530  C CD  . GLN A 503 ? 1.1140 0.6321 1.1013 -0.0364 -0.2562 -0.2908 503 GLN A CD  
3531  O OE1 . GLN A 503 ? 1.1415 0.6434 1.0367 -0.0114 -0.2485 -0.3088 503 GLN A OE1 
3532  N NE2 . GLN A 503 ? 1.1054 0.6380 1.1414 -0.0632 -0.2978 -0.3059 503 GLN A NE2 
3533  N N   . LEU A 504 ? 0.9967 0.6747 0.9539 0.0065  -0.1512 -0.1403 504 LEU A N   
3534  C CA  . LEU A 504 ? 0.9925 0.6847 0.9125 0.0222  -0.1241 -0.1249 504 LEU A CA  
3535  C C   . LEU A 504 ? 1.0030 0.6927 0.8497 0.0336  -0.1275 -0.1384 504 LEU A C   
3536  O O   . LEU A 504 ? 0.9919 0.6979 0.8273 0.0287  -0.1497 -0.1386 504 LEU A O   
3537  C CB  . LEU A 504 ? 0.9609 0.6957 0.9168 0.0152  -0.1147 -0.0878 504 LEU A CB  
3538  C CG  . LEU A 504 ? 0.9603 0.7096 0.9265 0.0233  -0.0902 -0.0673 504 LEU A CG  
3539  C CD1 . LEU A 504 ? 0.9766 0.7066 0.9838 0.0287  -0.0820 -0.0649 504 LEU A CD1 
3540  C CD2 . LEU A 504 ? 0.9380 0.7252 0.9207 0.0158  -0.0893 -0.0386 504 LEU A CD2 
3541  N N   . SER A 505 ? 0.9911 0.6613 0.7902 0.0514  -0.1026 -0.1457 505 SER A N   
3542  C CA  . SER A 505 ? 1.0095 0.6729 0.7338 0.0657  -0.0967 -0.1506 505 SER A CA  
3543  C C   . SER A 505 ? 1.0012 0.6864 0.7226 0.0696  -0.0647 -0.1231 505 SER A C   
3544  O O   . SER A 505 ? 1.0076 0.6926 0.6812 0.0766  -0.0601 -0.1159 505 SER A O   
3545  C CB  . SER A 505 ? 1.0638 0.6802 0.7215 0.0856  -0.0893 -0.1825 505 SER A CB  
3546  O OG  . SER A 505 ? 1.0902 0.6944 0.6629 0.1012  -0.0927 -0.1888 505 SER A OG  
3547  N N   . GLN A 506 ? 0.9131 0.6167 0.6874 0.0650  -0.0447 -0.1071 506 GLN A N   
3548  C CA  . GLN A 506 ? 0.9112 0.6399 0.6976 0.0624  -0.0207 -0.0842 506 GLN A CA  
3549  C C   . GLN A 506 ? 0.8846 0.6478 0.7376 0.0479  -0.0275 -0.0654 506 GLN A C   
3550  O O   . GLN A 506 ? 0.8866 0.6520 0.7806 0.0492  -0.0303 -0.0648 506 GLN A O   
3551  C CB  . GLN A 506 ? 0.9541 0.6730 0.7290 0.0777  0.0160  -0.0854 506 GLN A CB  
3552  C CG  . GLN A 506 ? 0.9614 0.7139 0.7779 0.0691  0.0385  -0.0624 506 GLN A CG  
3553  C CD  . GLN A 506 ? 1.0051 0.7493 0.8048 0.0834  0.0805  -0.0593 506 GLN A CD  
3554  O OE1 . GLN A 506 ? 1.0296 0.7437 0.7900 0.1044  0.0967  -0.0747 506 GLN A OE1 
3555  N NE2 . GLN A 506 ? 1.0200 0.7884 0.8495 0.0720  0.1003  -0.0401 506 GLN A NE2 
3556  N N   . LEU A 507 ? 0.8544 0.6397 0.7121 0.0367  -0.0295 -0.0500 507 LEU A N   
3557  C CA  . LEU A 507 ? 0.8384 0.6544 0.7410 0.0250  -0.0383 -0.0338 507 LEU A CA  
3558  C C   . LEU A 507 ? 0.8538 0.6870 0.7599 0.0164  -0.0264 -0.0250 507 LEU A C   
3559  O O   . LEU A 507 ? 0.8469 0.6682 0.7200 0.0127  -0.0226 -0.0253 507 LEU A O   
3560  C CB  . LEU A 507 ? 0.8050 0.6254 0.7074 0.0181  -0.0589 -0.0288 507 LEU A CB  
3561  C CG  . LEU A 507 ? 0.7974 0.6439 0.7238 0.0098  -0.0658 -0.0113 507 LEU A CG  
3562  C CD1 . LEU A 507 ? 0.8167 0.6800 0.7834 0.0123  -0.0661 -0.0006 507 LEU A CD1 
3563  C CD2 . LEU A 507 ? 0.7824 0.6306 0.7120 0.0075  -0.0774 -0.0048 507 LEU A CD2 
3564  N N   . ASP A 508 ? 0.7774 0.6380 0.7284 0.0132  -0.0219 -0.0170 508 ASP A N   
3565  C CA  . ASP A 508 ? 0.8093 0.6899 0.7786 0.0003  -0.0139 -0.0121 508 ASP A CA  
3566  C C   . ASP A 508 ? 0.8139 0.7315 0.8216 -0.0087 -0.0359 -0.0033 508 ASP A C   
3567  O O   . ASP A 508 ? 0.8431 0.7886 0.8971 -0.0023 -0.0389 0.0046  508 ASP A O   
3568  C CB  . ASP A 508 ? 0.8617 0.7472 0.8546 0.0059  0.0152  -0.0115 508 ASP A CB  
3569  C CG  . ASP A 508 ? 0.8940 0.7968 0.9140 -0.0123 0.0266  -0.0066 508 ASP A CG  
3570  O OD1 . ASP A 508 ? 0.8760 0.7805 0.8890 -0.0293 0.0087  -0.0083 508 ASP A OD1 
3571  O OD2 . ASP A 508 ? 0.9323 0.8442 0.9822 -0.0100 0.0559  -0.0017 508 ASP A OD2 
3572  N N   . LEU A 509 ? 0.8407 0.7570 0.8244 -0.0202 -0.0510 -0.0043 509 LEU A N   
3573  C CA  . LEU A 509 ? 0.8283 0.7751 0.8287 -0.0282 -0.0743 0.0007  509 LEU A CA  
3574  C C   . LEU A 509 ? 0.8315 0.7824 0.8334 -0.0488 -0.0779 -0.0100 509 LEU A C   
3575  O O   . LEU A 509 ? 0.8110 0.7709 0.7979 -0.0573 -0.0999 -0.0144 509 LEU A O   
3576  C CB  . LEU A 509 ? 0.7867 0.7248 0.7518 -0.0218 -0.0881 0.0070  509 LEU A CB  
3577  C CG  . LEU A 509 ? 0.7825 0.7121 0.7552 -0.0068 -0.0849 0.0175  509 LEU A CG  
3578  C CD1 . LEU A 509 ? 0.7491 0.6738 0.6967 -0.0031 -0.0922 0.0281  509 LEU A CD1 
3579  C CD2 . LEU A 509 ? 0.7993 0.7521 0.8191 0.0027  -0.0886 0.0292  509 LEU A CD2 
3580  N N   . SER A 510 ? 0.8325 0.7730 0.8503 -0.0570 -0.0551 -0.0145 510 SER A N   
3581  C CA  . SER A 510 ? 0.8404 0.7728 0.8640 -0.0800 -0.0531 -0.0249 510 SER A CA  
3582  C C   . SER A 510 ? 0.8340 0.8143 0.9144 -0.0978 -0.0787 -0.0287 510 SER A C   
3583  O O   . SER A 510 ? 0.8262 0.8512 0.9518 -0.0889 -0.0911 -0.0184 510 SER A O   
3584  C CB  . SER A 510 ? 0.8784 0.7882 0.9114 -0.0827 -0.0164 -0.0216 510 SER A CB  
3585  O OG  . SER A 510 ? 0.9031 0.8459 0.9915 -0.0765 -0.0010 -0.0120 510 SER A OG  
3586  N N   . SER A 511 ? 0.8232 0.7921 0.9022 -0.1225 -0.0890 -0.0448 511 SER A N   
3587  C CA  . SER A 511 ? 0.8129 0.8266 0.9502 -0.1461 -0.1186 -0.0547 511 SER A CA  
3588  C C   . SER A 511 ? 0.7855 0.8409 0.9161 -0.1342 -0.1599 -0.0515 511 SER A C   
3589  O O   . SER A 511 ? 0.7688 0.8832 0.9649 -0.1348 -0.1803 -0.0432 511 SER A O   
3590  C CB  . SER A 511 ? 0.8163 0.8698 1.0471 -0.1562 -0.0987 -0.0440 511 SER A CB  
3591  O OG  . SER A 511 ? 0.8374 0.8508 1.0735 -0.1719 -0.0616 -0.0457 511 SER A OG  
3592  N N   . ASN A 512 ? 0.8430 0.8683 0.8944 -0.1205 -0.1700 -0.0545 512 ASN A N   
3593  C CA  . ASN A 512 ? 0.8267 0.8808 0.8529 -0.1060 -0.2042 -0.0474 512 ASN A CA  
3594  C C   . ASN A 512 ? 0.8403 0.8606 0.7857 -0.1107 -0.2222 -0.0681 512 ASN A C   
3595  O O   . ASN A 512 ? 0.8596 0.8380 0.7829 -0.1287 -0.2123 -0.0910 512 ASN A O   
3596  C CB  . ASN A 512 ? 0.8123 0.8652 0.8247 -0.0757 -0.1890 -0.0209 512 ASN A CB  
3597  C CG  . ASN A 512 ? 0.8062 0.9030 0.8933 -0.0645 -0.1867 -0.0013 512 ASN A CG  
3598  O OD1 . ASN A 512 ? 0.7922 0.9336 0.9059 -0.0552 -0.2148 0.0116  512 ASN A OD1 
3599  N ND2 . ASN A 512 ? 0.8231 0.9057 0.9399 -0.0616 -0.1524 0.0018  512 ASN A ND2 
3600  N N   . ARG A 513 ? 0.9068 0.9406 0.8048 -0.0923 -0.2453 -0.0590 513 ARG A N   
3601  C CA  . ARG A 513 ? 0.9345 0.9367 0.7440 -0.0902 -0.2598 -0.0775 513 ARG A CA  
3602  C C   . ARG A 513 ? 0.9328 0.9102 0.6801 -0.0607 -0.2360 -0.0557 513 ARG A C   
3603  O O   . ARG A 513 ? 0.9560 0.9336 0.6387 -0.0445 -0.2503 -0.0508 513 ARG A O   
3604  C CB  . ARG A 513 ? 0.9529 0.9944 0.7499 -0.0949 -0.3118 -0.0883 513 ARG A CB  
3605  C CG  . ARG A 513 ? 0.9536 1.0244 0.8221 -0.1296 -0.3401 -0.1138 513 ARG A CG  
3606  C CD  . ARG A 513 ? 0.9747 0.9871 0.8314 -0.1571 -0.3214 -0.1476 513 ARG A CD  
3607  N NE  . ARG A 513 ? 1.0061 1.0219 0.8628 -0.1877 -0.3656 -0.1870 513 ARG A NE  
3608  C CZ  . ARG A 513 ? 1.0393 0.9969 0.8749 -0.2137 -0.3594 -0.2233 513 ARG A CZ  
3609  N NH1 . ARG A 513 ? 1.0441 0.9376 0.8558 -0.2094 -0.3096 -0.2215 513 ARG A NH1 
3610  N NH2 . ARG A 513 ? 1.0704 1.0328 0.9108 -0.2442 -0.4063 -0.2628 513 ARG A NH2 
3611  N N   . ILE A 514 ? 0.9021 0.8593 0.6691 -0.0532 -0.1994 -0.0417 514 ILE A N   
3612  C CA  . ILE A 514 ? 0.8955 0.8365 0.6275 -0.0296 -0.1760 -0.0194 514 ILE A CA  
3613  C C   . ILE A 514 ? 0.9207 0.8169 0.5843 -0.0255 -0.1594 -0.0356 514 ILE A C   
3614  O O   . ILE A 514 ? 0.9288 0.7931 0.5885 -0.0392 -0.1505 -0.0592 514 ILE A O   
3615  C CB  . ILE A 514 ? 0.8639 0.8039 0.6484 -0.0251 -0.1507 -0.0028 514 ILE A CB  
3616  C CG1 . ILE A 514 ? 0.8517 0.8296 0.7009 -0.0248 -0.1621 0.0112  514 ILE A CG1 
3617  C CG2 . ILE A 514 ? 0.8574 0.7848 0.6220 -0.0063 -0.1295 0.0185  514 ILE A CG2 
3618  C CD1 . ILE A 514 ? 0.8448 0.8170 0.7439 -0.0321 -0.1432 0.0064  514 ILE A CD1 
3619  N N   . THR A 515 ? 0.9070 0.7983 0.5179 -0.0039 -0.1506 -0.0198 515 THR A N   
3620  C CA  . THR A 515 ? 0.9433 0.7959 0.4839 0.0076  -0.1310 -0.0317 515 THR A CA  
3621  C C   . THR A 515 ? 0.9320 0.7811 0.4842 0.0269  -0.0945 -0.0039 515 THR A C   
3622  O O   . THR A 515 ? 0.8964 0.7669 0.5096 0.0266  -0.0884 0.0184  515 THR A O   
3623  C CB  . THR A 515 ? 1.0017 0.8526 0.4610 0.0188  -0.1504 -0.0388 515 THR A CB  
3624  O OG1 . THR A 515 ? 0.9990 0.8855 0.4614 0.0359  -0.1561 -0.0019 515 THR A OG1 
3625  C CG2 . THR A 515 ? 1.0424 0.8953 0.4926 -0.0044 -0.1921 -0.0747 515 THR A CG2 
3626  N N   . GLY A 516 ? 1.0023 0.8239 0.4990 0.0435  -0.0702 -0.0073 516 GLY A N   
3627  C CA  . GLY A 516 ? 0.9984 0.8217 0.5177 0.0603  -0.0348 0.0171  516 GLY A CA  
3628  C C   . GLY A 516 ? 0.9816 0.7865 0.5366 0.0549  -0.0219 0.0047  516 GLY A C   
3629  O O   . GLY A 516 ? 0.9776 0.7590 0.5298 0.0398  -0.0336 -0.0216 516 GLY A O   
3630  N N   . GLU A 517 ? 0.9927 0.8098 0.5853 0.0677  0.0024  0.0266  517 GLU A N   
3631  C CA  . GLU A 517 ? 0.9850 0.7905 0.6102 0.0685  0.0119  0.0205  517 GLU A CA  
3632  C C   . GLU A 517 ? 0.9523 0.7913 0.6520 0.0643  0.0081  0.0411  517 GLU A C   
3633  O O   . GLU A 517 ? 0.9469 0.8139 0.6772 0.0654  0.0105  0.0640  517 GLU A O   
3634  C CB  . GLU A 517 ? 1.0306 0.8149 0.6260 0.0925  0.0433  0.0200  517 GLU A CB  
3635  C CG  . GLU A 517 ? 1.0556 0.8645 0.6557 0.1139  0.0717  0.0481  517 GLU A CG  
3636  C CD  . GLU A 517 ? 1.1027 0.8873 0.6712 0.1412  0.1067  0.0442  517 GLU A CD  
3637  O OE1 . GLU A 517 ? 1.1086 0.9026 0.7270 0.1511  0.1178  0.0522  517 GLU A OE1 
3638  O OE2 . GLU A 517 ? 1.1389 0.8937 0.6298 0.1553  0.1220  0.0321  517 GLU A OE2 
3639  N N   . LEU A 518 ? 0.9172 0.7486 0.6422 0.0596  0.0017  0.0322  518 LEU A N   
3640  C CA  . LEU A 518 ? 0.8885 0.7455 0.6732 0.0544  -0.0089 0.0431  518 LEU A CA  
3641  C C   . LEU A 518 ? 0.9108 0.7937 0.7366 0.0687  0.0055  0.0628  518 LEU A C   
3642  O O   . LEU A 518 ? 0.9401 0.8152 0.7559 0.0857  0.0211  0.0630  518 LEU A O   
3643  C CB  . LEU A 518 ? 0.8699 0.7087 0.6543 0.0492  -0.0199 0.0284  518 LEU A CB  
3644  C CG  . LEU A 518 ? 0.8362 0.6739 0.6283 0.0321  -0.0367 0.0192  518 LEU A CG  
3645  C CD1 . LEU A 518 ? 0.8379 0.6687 0.6041 0.0216  -0.0402 0.0108  518 LEU A CD1 
3646  C CD2 . LEU A 518 ? 0.8316 0.6481 0.6145 0.0319  -0.0387 0.0093  518 LEU A CD2 
3647  N N   . PRO A 519 ? 0.8463 0.7601 0.7260 0.0624  0.0020  0.0804  519 PRO A N   
3648  C CA  . PRO A 519 ? 0.8702 0.8166 0.8067 0.0719  0.0163  0.1012  519 PRO A CA  
3649  C C   . PRO A 519 ? 0.8605 0.8217 0.8398 0.0726  -0.0023 0.0946  519 PRO A C   
3650  O O   . PRO A 519 ? 0.8362 0.7792 0.7958 0.0664  -0.0245 0.0760  519 PRO A O   
3651  C CB  . PRO A 519 ? 0.8663 0.8331 0.8497 0.0588  0.0160  0.1206  519 PRO A CB  
3652  C CG  . PRO A 519 ? 0.8366 0.7854 0.8089 0.0425  -0.0104 0.1036  519 PRO A CG  
3653  C CD  . PRO A 519 ? 0.8229 0.7421 0.7230 0.0461  -0.0138 0.0830  519 PRO A CD  
3654  N N   . GLU A 520 ? 0.8603 0.8583 0.8995 0.0825  0.0077  0.1123  520 GLU A N   
3655  C CA  . GLU A 520 ? 0.8437 0.8682 0.9358 0.0827  -0.0181 0.1086  520 GLU A CA  
3656  C C   . GLU A 520 ? 0.8234 0.8639 0.9697 0.0578  -0.0480 0.1028  520 GLU A C   
3657  O O   . GLU A 520 ? 0.8025 0.8568 0.9751 0.0549  -0.0797 0.0908  520 GLU A O   
3658  C CB  . GLU A 520 ? 0.8493 0.9171 1.0019 0.1020  0.0001  0.1302  520 GLU A CB  
3659  C CG  . GLU A 520 ? 0.8681 0.9136 0.9682 0.1324  0.0278  0.1316  520 GLU A CG  
3660  C CD  . GLU A 520 ? 0.8550 0.8748 0.9162 0.1439  0.0060  0.1158  520 GLU A CD  
3661  O OE1 . GLU A 520 ? 0.8358 0.8526 0.8956 0.1288  -0.0294 0.1022  520 GLU A OE1 
3662  O OE2 . GLU A 520 ? 0.8704 0.8679 0.8983 0.1702  0.0271  0.1180  520 GLU A OE2 
3663  N N   . SER A 521 ? 0.8117 0.8464 0.9703 0.0419  -0.0396 0.1104  521 SER A N   
3664  C CA  . SER A 521 ? 0.8030 0.8348 1.0007 0.0187  -0.0651 0.1004  521 SER A CA  
3665  C C   . SER A 521 ? 0.7819 0.7766 0.9204 0.0149  -0.0890 0.0713  521 SER A C   
3666  O O   . SER A 521 ? 0.7812 0.7652 0.9410 -0.0006 -0.1099 0.0571  521 SER A O   
3667  C CB  . SER A 521 ? 0.8191 0.8466 1.0391 0.0083  -0.0438 0.1216  521 SER A CB  
3668  O OG  . SER A 521 ? 0.8191 0.8368 1.0837 -0.0132 -0.0649 0.1124  521 SER A OG  
3669  N N   . ILE A 522 ? 0.8958 0.8673 0.9628 0.0286  -0.0825 0.0624  522 ILE A N   
3670  C CA  . ILE A 522 ? 0.8743 0.8134 0.8871 0.0277  -0.0968 0.0398  522 ILE A CA  
3671  C C   . ILE A 522 ? 0.8684 0.8111 0.8956 0.0253  -0.1281 0.0226  522 ILE A C   
3672  O O   . ILE A 522 ? 0.8593 0.7758 0.8530 0.0218  -0.1399 0.0035  522 ILE A O   
3673  C CB  . ILE A 522 ? 0.8681 0.7850 0.8183 0.0423  -0.0823 0.0374  522 ILE A CB  
3674  C CG1 . ILE A 522 ? 0.8499 0.7338 0.7514 0.0368  -0.0833 0.0218  522 ILE A CG1 
3675  C CG2 . ILE A 522 ? 0.8752 0.8002 0.8235 0.0595  -0.0897 0.0387  522 ILE A CG2 
3676  C CD1 . ILE A 522 ? 0.8422 0.7241 0.7529 0.0239  -0.0806 0.0220  522 ILE A CD1 
3677  N N   . SER A 523 ? 0.8746 0.8520 0.9520 0.0285  -0.1423 0.0287  523 SER A N   
3678  C CA  . SER A 523 ? 0.8640 0.8503 0.9517 0.0280  -0.1803 0.0104  523 SER A CA  
3679  C C   . SER A 523 ? 0.8607 0.8377 0.9808 0.0056  -0.2028 -0.0094 523 SER A C   
3680  O O   . SER A 523 ? 0.8557 0.8265 0.9620 0.0046  -0.2373 -0.0338 523 SER A O   
3681  C CB  . SER A 523 ? 0.8605 0.8970 1.0093 0.0369  -0.1925 0.0244  523 SER A CB  
3682  O OG  . SER A 523 ? 0.8500 0.8994 1.0017 0.0392  -0.2367 0.0059  523 SER A OG  
3683  N N   . ASN A 524 ? 0.8294 0.7998 0.9852 -0.0100 -0.1843 0.0000  524 ASN A N   
3684  C CA  . ASN A 524 ? 0.8260 0.7825 1.0265 -0.0315 -0.2008 -0.0151 524 ASN A CA  
3685  C C   . ASN A 524 ? 0.8242 0.7328 0.9630 -0.0301 -0.2114 -0.0451 524 ASN A C   
3686  O O   . ASN A 524 ? 0.8247 0.7123 0.9913 -0.0452 -0.2289 -0.0658 524 ASN A O   
3687  C CB  . ASN A 524 ? 0.8394 0.7968 1.0888 -0.0427 -0.1713 0.0114  524 ASN A CB  
3688  C CG  . ASN A 524 ? 0.8379 0.8388 1.1794 -0.0536 -0.1661 0.0350  524 ASN A CG  
3689  O OD1 . ASN A 524 ? 0.8247 0.8642 1.1963 -0.0494 -0.1814 0.0352  524 ASN A OD1 
3690  N ND2 . ASN A 524 ? 0.8448 0.8423 1.2363 -0.0656 -0.1421 0.0591  524 ASN A ND2 
3691  N N   . ILE A 525 ? 0.9018 0.7903 0.9619 -0.0126 -0.1982 -0.0482 525 ILE A N   
3692  C CA  . ILE A 525 ? 0.9040 0.7504 0.9097 -0.0080 -0.1945 -0.0691 525 ILE A CA  
3693  C C   . ILE A 525 ? 0.9126 0.7439 0.8496 0.0070  -0.2129 -0.0912 525 ILE A C   
3694  O O   . ILE A 525 ? 0.9204 0.7232 0.7947 0.0194  -0.1968 -0.0982 525 ILE A O   
3695  C CB  . ILE A 525 ? 0.8982 0.7353 0.8772 -0.0015 -0.1608 -0.0523 525 ILE A CB  
3696  C CG1 . ILE A 525 ? 0.8923 0.7473 0.8452 0.0085  -0.1462 -0.0337 525 ILE A CG1 
3697  C CG2 . ILE A 525 ? 0.9014 0.7416 0.9327 -0.0123 -0.1473 -0.0350 525 ILE A CG2 
3698  C CD1 . ILE A 525 ? 0.8854 0.7343 0.8184 0.0101  -0.1205 -0.0215 525 ILE A CD1 
3699  N N   . ASN A 526 ? 0.9466 0.8002 0.8973 0.0074  -0.2460 -0.0993 526 ASN A N   
3700  C CA  . ASN A 526 ? 0.9619 0.8087 0.8418 0.0276  -0.2656 -0.1112 526 ASN A CA  
3701  C C   . ASN A 526 ? 0.9907 0.7889 0.7910 0.0374  -0.2670 -0.1399 526 ASN A C   
3702  O O   . ASN A 526 ? 1.0133 0.7970 0.7351 0.0593  -0.2700 -0.1430 526 ASN A O   
3703  C CB  . ASN A 526 ? 0.9618 0.8457 0.8833 0.0241  -0.3117 -0.1197 526 ASN A CB  
3704  C CG  . ASN A 526 ? 0.9698 0.8433 0.9292 0.0022  -0.3465 -0.1535 526 ASN A CG  
3705  O OD1 . ASN A 526 ? 0.9729 0.8145 0.9478 -0.0119 -0.3300 -0.1636 526 ASN A OD1 
3706  N ND2 . ASN A 526 ? 0.9752 0.8742 0.9517 -0.0002 -0.3971 -0.1722 526 ASN A ND2 
3707  N N   . ARG A 527 ? 1.0303 0.7999 0.8464 0.0252  -0.2607 -0.1585 527 ARG A N   
3708  C CA  . ARG A 527 ? 1.0659 0.7866 0.8069 0.0387  -0.2513 -0.1843 527 ARG A CA  
3709  C C   . ARG A 527 ? 1.0667 0.7749 0.7628 0.0544  -0.2050 -0.1640 527 ARG A C   
3710  O O   . ARG A 527 ? 1.1015 0.7735 0.7355 0.0696  -0.1879 -0.1794 527 ARG A O   
3711  C CB  . ARG A 527 ? 1.0775 0.7679 0.8571 0.0237  -0.2532 -0.2082 527 ARG A CB  
3712  C CG  . ARG A 527 ? 1.0975 0.7773 0.8962 0.0093  -0.3017 -0.2450 527 ARG A CG  
3713  C CD  . ARG A 527 ? 1.1201 0.7516 0.9446 -0.0021 -0.2967 -0.2717 527 ARG A CD  
3714  N NE  . ARG A 527 ? 1.1240 0.7528 1.0125 -0.0291 -0.3399 -0.2981 527 ARG A NE  
3715  C CZ  . ARG A 527 ? 1.1630 0.7649 1.0111 -0.0310 -0.3795 -0.3436 527 ARG A CZ  
3716  N NH1 . ARG A 527 ? 1.2214 0.7995 0.9580 -0.0036 -0.3747 -0.3620 527 ARG A NH1 
3717  N NH2 . ARG A 527 ? 1.1763 0.7911 1.1035 -0.0601 -0.4080 -0.3564 527 ARG A NH2 
3718  N N   . ILE A 528 ? 1.0311 0.7675 0.7593 0.0506  -0.1834 -0.1313 528 ILE A N   
3719  C CA  . ILE A 528 ? 1.0308 0.7588 0.7335 0.0587  -0.1432 -0.1140 528 ILE A CA  
3720  C C   . ILE A 528 ? 1.0618 0.7702 0.6821 0.0803  -0.1334 -0.1121 528 ILE A C   
3721  O O   . ILE A 528 ? 1.0713 0.7845 0.6597 0.0905  -0.1574 -0.1119 528 ILE A O   
3722  C CB  . ILE A 528 ? 0.9949 0.7536 0.7475 0.0475  -0.1294 -0.0855 528 ILE A CB  
3723  C CG1 . ILE A 528 ? 0.9954 0.7490 0.7414 0.0483  -0.0943 -0.0727 528 ILE A CG1 
3724  C CG2 . ILE A 528 ? 0.9875 0.7645 0.7323 0.0531  -0.1407 -0.0716 528 ILE A CG2 
3725  C CD1 . ILE A 528 ? 0.9704 0.7470 0.7744 0.0340  -0.0873 -0.0585 528 ILE A CD1 
3726  N N   . SER A 529 ? 1.0734 0.7612 0.6620 0.0891  -0.0965 -0.1074 529 SER A N   
3727  C CA  . SER A 529 ? 1.1100 0.7756 0.6232 0.1097  -0.0756 -0.0973 529 SER A CA  
3728  C C   . SER A 529 ? 1.1083 0.7776 0.6413 0.1043  -0.0333 -0.0716 529 SER A C   
3729  O O   . SER A 529 ? 1.1307 0.7857 0.6228 0.1149  -0.0141 -0.0530 529 SER A O   
3730  C CB  . SER A 529 ? 1.1622 0.7910 0.6024 0.1299  -0.0687 -0.1203 529 SER A CB  
3731  O OG  . SER A 529 ? 1.1678 0.7895 0.6404 0.1255  -0.0438 -0.1301 529 SER A OG  
3732  N N   . LYS A 530 ? 1.0132 0.7006 0.6110 0.0878  -0.0203 -0.0698 530 LYS A N   
3733  C CA  . LYS A 530 ? 1.0141 0.7141 0.6481 0.0761  0.0094  -0.0497 530 LYS A CA  
3734  C C   . LYS A 530 ? 0.9697 0.7010 0.6689 0.0557  -0.0085 -0.0447 530 LYS A C   
3735  O O   . LYS A 530 ? 0.9502 0.6962 0.6889 0.0497  -0.0225 -0.0526 530 LYS A O   
3736  C CB  . LYS A 530 ? 1.0472 0.7459 0.6968 0.0796  0.0433  -0.0502 530 LYS A CB  
3737  C CG  . LYS A 530 ? 1.0926 0.7732 0.7086 0.0885  0.0849  -0.0337 530 LYS A CG  
3738  C CD  . LYS A 530 ? 1.1229 0.8134 0.7741 0.0914  0.1226  -0.0310 530 LYS A CD  
3739  C CE  . LYS A 530 ? 1.1665 0.8415 0.7955 0.0980  0.1713  -0.0094 530 LYS A CE  
3740  N NZ  . LYS A 530 ? 1.1864 0.8891 0.8855 0.0929  0.2092  0.0000  530 LYS A NZ  
3741  N N   . LEU A 531 ? 0.9277 0.6635 0.6327 0.0472  -0.0056 -0.0310 531 LEU A N   
3742  C CA  . LEU A 531 ? 0.8920 0.6520 0.6410 0.0318  -0.0197 -0.0268 531 LEU A CA  
3743  C C   . LEU A 531 ? 0.9116 0.6726 0.6771 0.0181  -0.0013 -0.0184 531 LEU A C   
3744  O O   . LEU A 531 ? 0.9336 0.6721 0.6730 0.0192  0.0107  -0.0117 531 LEU A O   
3745  C CB  . LEU A 531 ? 0.8687 0.6300 0.6056 0.0370  -0.0395 -0.0242 531 LEU A CB  
3746  C CG  . LEU A 531 ? 0.8354 0.6231 0.6132 0.0284  -0.0569 -0.0221 531 LEU A CG  
3747  C CD1 . LEU A 531 ? 0.8313 0.6235 0.6028 0.0368  -0.0683 -0.0164 531 LEU A CD1 
3748  C CD2 . LEU A 531 ? 0.8289 0.6278 0.6286 0.0153  -0.0487 -0.0166 531 LEU A CD2 
3749  N N   . GLN A 532 ? 0.8272 0.6134 0.6389 0.0051  -0.0012 -0.0190 532 GLN A N   
3750  C CA  . GLN A 532 ? 0.8541 0.6474 0.6925 -0.0124 0.0097  -0.0157 532 GLN A CA  
3751  C C   . GLN A 532 ? 0.8260 0.6449 0.6903 -0.0243 -0.0137 -0.0181 532 GLN A C   
3752  O O   . GLN A 532 ? 0.8297 0.6795 0.7318 -0.0268 -0.0241 -0.0167 532 GLN A O   
3753  C CB  . GLN A 532 ? 0.9015 0.7092 0.7757 -0.0152 0.0310  -0.0128 532 GLN A CB  
3754  C CG  . GLN A 532 ? 0.9370 0.7168 0.7739 0.0014  0.0598  -0.0089 532 GLN A CG  
3755  C CD  . GLN A 532 ? 0.9762 0.7743 0.8494 0.0066  0.0836  -0.0065 532 GLN A CD  
3756  O OE1 . GLN A 532 ? 0.9717 0.7594 0.8202 0.0266  0.0901  -0.0126 532 GLN A OE1 
3757  N NE2 . GLN A 532 ? 1.0110 0.8369 0.9466 -0.0112 0.0966  0.0008  532 GLN A NE2 
3758  N N   . LEU A 533 ? 0.8494 0.6528 0.6883 -0.0279 -0.0201 -0.0204 533 LEU A N   
3759  C CA  . LEU A 533 ? 0.8338 0.6531 0.6783 -0.0367 -0.0386 -0.0243 533 LEU A CA  
3760  C C   . LEU A 533 ? 0.8589 0.6637 0.7020 -0.0553 -0.0370 -0.0349 533 LEU A C   
3761  O O   . LEU A 533 ? 0.8540 0.6600 0.6818 -0.0606 -0.0523 -0.0433 533 LEU A O   
3762  C CB  . LEU A 533 ? 0.8055 0.6178 0.6206 -0.0235 -0.0454 -0.0208 533 LEU A CB  
3763  C CG  . LEU A 533 ? 0.7819 0.6110 0.6105 -0.0114 -0.0526 -0.0122 533 LEU A CG  
3764  C CD1 . LEU A 533 ? 0.7705 0.5991 0.5849 -0.0015 -0.0554 -0.0058 533 LEU A CD1 
3765  C CD2 . LEU A 533 ? 0.7834 0.6415 0.6466 -0.0146 -0.0635 -0.0070 533 LEU A CD2 
3766  N N   . ASN A 534 ? 0.8509 0.6387 0.7080 -0.0656 -0.0175 -0.0353 534 ASN A N   
3767  C CA  . ASN A 534 ? 0.8764 0.6402 0.7386 -0.0871 -0.0132 -0.0467 534 ASN A CA  
3768  C C   . ASN A 534 ? 0.8787 0.6791 0.7810 -0.1091 -0.0395 -0.0596 534 ASN A C   
3769  O O   . ASN A 534 ? 0.8696 0.7175 0.8060 -0.1063 -0.0549 -0.0537 534 ASN A O   
3770  C CB  . ASN A 534 ? 0.9109 0.6510 0.7906 -0.0940 0.0188  -0.0377 534 ASN A CB  
3771  C CG  . ASN A 534 ? 0.9251 0.7035 0.8521 -0.0934 0.0298  -0.0269 534 ASN A CG  
3772  O OD1 . ASN A 534 ? 0.9179 0.7118 0.8332 -0.0726 0.0289  -0.0200 534 ASN A OD1 
3773  N ND2 . ASN A 534 ? 0.9454 0.7381 0.9309 -0.1166 0.0416  -0.0265 534 ASN A ND2 
3774  N N   . GLY A 535 ? 0.8731 0.6486 0.7702 -0.1301 -0.0468 -0.0783 535 GLY A N   
3775  C CA  . GLY A 535 ? 0.8787 0.6879 0.8128 -0.1543 -0.0782 -0.0953 535 GLY A CA  
3776  C C   . GLY A 535 ? 0.8578 0.7001 0.7646 -0.1421 -0.1122 -0.0984 535 GLY A C   
3777  O O   . GLY A 535 ? 0.8476 0.7447 0.7976 -0.1452 -0.1358 -0.0934 535 GLY A O   
3778  N N   . ASN A 536 ? 0.9176 0.7276 0.7543 -0.1253 -0.1122 -0.1033 536 ASN A N   
3779  C CA  . ASN A 536 ? 0.9053 0.7393 0.7048 -0.1092 -0.1355 -0.1004 536 ASN A CA  
3780  C C   . ASN A 536 ? 0.9349 0.7239 0.6615 -0.1067 -0.1391 -0.1229 536 ASN A C   
3781  O O   . ASN A 536 ? 0.9640 0.7057 0.6788 -0.1215 -0.1298 -0.1444 536 ASN A O   
3782  C CB  . ASN A 536 ? 0.8735 0.7212 0.6688 -0.0820 -0.1203 -0.0728 536 ASN A CB  
3783  C CG  . ASN A 536 ? 0.8564 0.7535 0.7084 -0.0792 -0.1290 -0.0548 536 ASN A CG  
3784  O OD1 . ASN A 536 ? 0.8534 0.7866 0.7132 -0.0762 -0.1543 -0.0493 536 ASN A OD1 
3785  N ND2 . ASN A 536 ? 0.8530 0.7490 0.7397 -0.0765 -0.1072 -0.0449 536 ASN A ND2 
3786  N N   . ARG A 537 ? 0.9784 0.7773 0.6540 -0.0859 -0.1485 -0.1167 537 ARG A N   
3787  C CA  . ARG A 537 ? 1.0180 0.7742 0.6134 -0.0754 -0.1456 -0.1357 537 ARG A CA  
3788  C C   . ARG A 537 ? 1.0091 0.7532 0.5731 -0.0442 -0.1138 -0.1130 537 ARG A C   
3789  O O   . ARG A 537 ? 1.0389 0.7706 0.5400 -0.0252 -0.1090 -0.1144 537 ARG A O   
3790  C CB  . ARG A 537 ? 1.0470 0.8238 0.5984 -0.0764 -0.1831 -0.1497 537 ARG A CB  
3791  C CG  . ARG A 537 ? 1.0443 0.8592 0.6507 -0.1059 -0.2229 -0.1641 537 ARG A CG  
3792  C CD  . ARG A 537 ? 1.0955 0.8979 0.6453 -0.1186 -0.2628 -0.2021 537 ARG A CD  
3793  N NE  . ARG A 537 ? 1.1077 0.9443 0.6020 -0.0953 -0.2890 -0.1892 537 ARG A NE  
3794  C CZ  . ARG A 537 ? 1.1734 0.9921 0.5790 -0.0909 -0.3182 -0.2169 537 ARG A CZ  
3795  N NH1 . ARG A 537 ? 1.2523 1.0169 0.6178 -0.1110 -0.3283 -0.2651 537 ARG A NH1 
3796  N NH2 . ARG A 537 ? 1.2058 1.0560 0.5560 -0.0641 -0.3368 -0.1960 537 ARG A NH2 
3797  N N   . LEU A 538 ? 0.9886 0.7376 0.5968 -0.0383 -0.0918 -0.0922 538 LEU A N   
3798  C CA  . LEU A 538 ? 0.9808 0.7254 0.5774 -0.0125 -0.0656 -0.0716 538 LEU A CA  
3799  C C   . LEU A 538 ? 1.0216 0.7141 0.5703 -0.0004 -0.0431 -0.0866 538 LEU A C   
3800  O O   . LEU A 538 ? 1.0400 0.6914 0.5859 -0.0123 -0.0383 -0.1059 538 LEU A O   
3801  C CB  . LEU A 538 ? 0.9411 0.7016 0.5928 -0.0111 -0.0555 -0.0523 538 LEU A CB  
3802  C CG  . LEU A 538 ? 0.9065 0.7106 0.6062 -0.0180 -0.0711 -0.0376 538 LEU A CG  
3803  C CD1 . LEU A 538 ? 0.8818 0.6869 0.6205 -0.0185 -0.0615 -0.0297 538 LEU A CD1 
3804  C CD2 . LEU A 538 ? 0.9004 0.7328 0.5983 -0.0032 -0.0733 -0.0162 538 LEU A CD2 
3805  N N   . SER A 539 ? 1.0680 0.7609 0.5843 0.0252  -0.0247 -0.0747 539 SER A N   
3806  C CA  . SER A 539 ? 1.1177 0.7625 0.5806 0.0436  -0.0002 -0.0892 539 SER A CA  
3807  C C   . SER A 539 ? 1.1170 0.7722 0.6043 0.0710  0.0305  -0.0627 539 SER A C   
3808  O O   . SER A 539 ? 1.0798 0.7730 0.6265 0.0700  0.0276  -0.0389 539 SER A O   
3809  C CB  . SER A 539 ? 1.1634 0.7962 0.5504 0.0524  -0.0046 -0.1048 539 SER A CB  
3810  O OG  . SER A 539 ? 1.1475 0.8300 0.5381 0.0598  -0.0122 -0.0785 539 SER A OG  
3811  N N   . GLY A 540 ? 1.1338 0.7542 0.5786 0.0958  0.0590  -0.0691 540 GLY A N   
3812  C CA  . GLY A 540 ? 1.1430 0.7793 0.6194 0.1245  0.0888  -0.0433 540 GLY A CA  
3813  C C   . GLY A 540 ? 1.1302 0.7579 0.6531 0.1246  0.0889  -0.0369 540 GLY A C   
3814  O O   . GLY A 540 ? 1.1226 0.7154 0.6396 0.1065  0.0770  -0.0540 540 GLY A O   
3815  N N   . LYS A 541 ? 1.0696 0.7321 0.6415 0.1460  0.1026  -0.0097 541 LYS A N   
3816  C CA  . LYS A 541 ? 1.0681 0.7257 0.6759 0.1529  0.1000  -0.0003 541 LYS A CA  
3817  C C   . LYS A 541 ? 1.0331 0.7343 0.6901 0.1330  0.0706  0.0117  541 LYS A C   
3818  O O   . LYS A 541 ? 1.0047 0.7485 0.6872 0.1204  0.0578  0.0197  541 LYS A O   
3819  C CB  . LYS A 541 ? 1.0926 0.7669 0.7305 0.1896  0.1253  0.0211  541 LYS A CB  
3820  C CG  . LYS A 541 ? 1.0694 0.8196 0.7833 0.1932  0.1156  0.0497  541 LYS A CG  
3821  C CD  . LYS A 541 ? 1.0690 0.8443 0.8248 0.2299  0.1411  0.0716  541 LYS A CD  
3822  C CE  . LYS A 541 ? 1.1086 0.8849 0.8441 0.2486  0.1797  0.0752  541 LYS A CE  
3823  N NZ  . LYS A 541 ? 1.1043 0.9047 0.8856 0.2885  0.2120  0.0974  541 LYS A NZ  
3824  N N   . ILE A 542 ? 1.0723 0.7560 0.7367 0.1326  0.0625  0.0132  542 ILE A N   
3825  C CA  . ILE A 542 ? 1.0236 0.7396 0.7219 0.1196  0.0374  0.0216  542 ILE A CA  
3826  C C   . ILE A 542 ? 0.9928 0.7629 0.7446 0.1360  0.0301  0.0424  542 ILE A C   
3827  O O   . ILE A 542 ? 1.0028 0.7749 0.7672 0.1627  0.0404  0.0550  542 ILE A O   
3828  C CB  . ILE A 542 ? 1.0212 0.6982 0.6996 0.1188  0.0358  0.0198  542 ILE A CB  
3829  C CG1 . ILE A 542 ? 1.0317 0.6648 0.6783 0.0939  0.0406  -0.0006 542 ILE A CG1 
3830  C CG2 . ILE A 542 ? 0.9754 0.6843 0.6773 0.1153  0.0129  0.0291  542 ILE A CG2 
3831  C CD1 . ILE A 542 ? 1.0422 0.6294 0.6718 0.0928  0.0496  0.0019  542 ILE A CD1 
3832  N N   . PRO A 543 ? 0.9705 0.7851 0.7615 0.1210  0.0122  0.0471  543 PRO A N   
3833  C CA  . PRO A 543 ? 0.9553 0.8231 0.8100 0.1308  0.0030  0.0646  543 PRO A CA  
3834  C C   . PRO A 543 ? 0.9386 0.8140 0.8058 0.1431  -0.0183 0.0687  543 PRO A C   
3835  O O   . PRO A 543 ? 0.9263 0.7761 0.7595 0.1356  -0.0325 0.0589  543 PRO A O   
3836  C CB  . PRO A 543 ? 0.9329 0.8295 0.8200 0.1063  -0.0127 0.0639  543 PRO A CB  
3837  C CG  . PRO A 543 ? 0.9145 0.7771 0.7568 0.0880  -0.0208 0.0465  543 PRO A CG  
3838  C CD  . PRO A 543 ? 0.9453 0.7631 0.7316 0.0943  -0.0010 0.0370  543 PRO A CD  
3839  N N   . SER A 544 ? 0.9717 0.8853 0.8878 0.1646  -0.0197 0.0854  544 SER A N   
3840  C CA  . SER A 544 ? 0.9589 0.8903 0.8896 0.1791  -0.0482 0.0912  544 SER A CA  
3841  C C   . SER A 544 ? 0.9370 0.9026 0.9007 0.1578  -0.0876 0.0821  544 SER A C   
3842  O O   . SER A 544 ? 0.9295 0.9070 0.8912 0.1677  -0.1187 0.0815  544 SER A O   
3843  C CB  . SER A 544 ? 0.9644 0.9353 0.9489 0.2104  -0.0417 0.1130  544 SER A CB  
3844  O OG  . SER A 544 ? 0.9543 0.9908 1.0255 0.2010  -0.0484 0.1223  544 SER A OG  
3845  N N   . GLY A 545 ? 0.9502 0.9279 0.9399 0.1310  -0.0874 0.0750  545 GLY A N   
3846  C CA  . GLY A 545 ? 0.9306 0.9256 0.9461 0.1092  -0.1212 0.0615  545 GLY A CA  
3847  C C   . GLY A 545 ? 0.9207 0.8739 0.8675 0.1047  -0.1358 0.0427  545 GLY A C   
3848  O O   . GLY A 545 ? 0.9113 0.8715 0.8653 0.0938  -0.1663 0.0275  545 GLY A O   
3849  N N   . ILE A 546 ? 0.9864 0.8936 0.8679 0.1125  -0.1123 0.0424  546 ILE A N   
3850  C CA  . ILE A 546 ? 0.9867 0.8557 0.8060 0.1124  -0.1178 0.0309  546 ILE A CA  
3851  C C   . ILE A 546 ? 0.9975 0.8730 0.7962 0.1336  -0.1453 0.0332  546 ILE A C   
3852  O O   . ILE A 546 ? 1.0052 0.8578 0.7542 0.1347  -0.1569 0.0222  546 ILE A O   
3853  C CB  . ILE A 546 ? 0.9995 0.8209 0.7689 0.1146  -0.0844 0.0339  546 ILE A CB  
3854  C CG1 . ILE A 546 ? 0.9925 0.8132 0.7786 0.0963  -0.0651 0.0301  546 ILE A CG1 
3855  C CG2 . ILE A 546 ? 1.0064 0.7920 0.7235 0.1109  -0.0812 0.0259  546 ILE A CG2 
3856  C CD1 . ILE A 546 ? 0.9706 0.7980 0.7684 0.0737  -0.0730 0.0182  546 ILE A CD1 
3857  N N   . ARG A 547 ? 0.9966 0.9054 0.8311 0.1535  -0.1560 0.0486  547 ARG A N   
3858  C CA  . ARG A 547 ? 1.0065 0.9301 0.8243 0.1767  -0.1899 0.0530  547 ARG A CA  
3859  C C   . ARG A 547 ? 0.9992 0.9434 0.8240 0.1616  -0.2334 0.0295  547 ARG A C   
3860  O O   . ARG A 547 ? 1.0172 0.9474 0.7829 0.1764  -0.2588 0.0226  547 ARG A O   
3861  C CB  . ARG A 547 ? 1.0059 0.9768 0.8850 0.1996  -0.1971 0.0744  547 ARG A CB  
3862  C CG  . ARG A 547 ? 1.0032 1.0216 0.9056 0.2140  -0.2505 0.0742  547 ARG A CG  
3863  C CD  . ARG A 547 ? 0.9938 1.0757 0.9850 0.2331  -0.2583 0.0963  547 ARG A CD  
3864  N NE  . ARG A 547 ? 0.9876 1.0830 1.0408 0.2206  -0.2177 0.1045  547 ARG A NE  
3865  C CZ  . ARG A 547 ? 0.9699 1.1167 1.1137 0.1966  -0.2244 0.1014  547 ARG A CZ  
3866  N NH1 . ARG A 547 ? 0.9470 1.1375 1.1423 0.1781  -0.2733 0.0867  547 ARG A NH1 
3867  N NH2 . ARG A 547 ? 0.9780 1.1287 1.1589 0.1911  -0.1803 0.1130  547 ARG A NH2 
3868  N N   . LEU A 548 ? 0.9378 0.9083 0.8278 0.1332  -0.2407 0.0166  548 LEU A N   
3869  C CA  . LEU A 548 ? 0.9319 0.9219 0.8463 0.1163  -0.2844 -0.0084 548 LEU A CA  
3870  C C   . LEU A 548 ? 0.9394 0.8816 0.7971 0.1011  -0.2799 -0.0339 548 LEU A C   
3871  O O   . LEU A 548 ? 0.9410 0.8860 0.8115 0.0863  -0.3127 -0.0601 548 LEU A O   
3872  C CB  . LEU A 548 ? 0.9107 0.9514 0.9370 0.0932  -0.2923 -0.0060 548 LEU A CB  
3873  C CG  . LEU A 548 ? 0.9014 1.0034 1.0031 0.1086  -0.3024 0.0172  548 LEU A CG  
3874  C CD1 . LEU A 548 ? 0.8814 1.0303 1.0977 0.0840  -0.2957 0.0254  548 LEU A CD1 
3875  C CD2 . LEU A 548 ? 0.9026 1.0335 0.9983 0.1245  -0.3583 0.0081  548 LEU A CD2 
3876  N N   . LEU A 549 ? 1.0148 0.9132 0.8157 0.1044  -0.2403 -0.0280 549 LEU A N   
3877  C CA  . LEU A 549 ? 1.0230 0.8803 0.7747 0.0952  -0.2301 -0.0480 549 LEU A CA  
3878  C C   . LEU A 549 ? 1.0570 0.8819 0.7143 0.1192  -0.2372 -0.0537 549 LEU A C   
3879  O O   . LEU A 549 ? 1.0724 0.8618 0.6726 0.1300  -0.2033 -0.0425 549 LEU A O   
3880  C CB  . LEU A 549 ? 1.0101 0.8472 0.7638 0.0847  -0.1862 -0.0375 549 LEU A CB  
3881  C CG  . LEU A 549 ? 0.9894 0.8551 0.8148 0.0700  -0.1736 -0.0238 549 LEU A CG  
3882  C CD1 . LEU A 549 ? 0.9815 0.8269 0.7928 0.0641  -0.1370 -0.0146 549 LEU A CD1 
3883  C CD2 . LEU A 549 ? 0.9819 0.8668 0.8691 0.0493  -0.1919 -0.0356 549 LEU A CD2 
3884  N N   . THR A 550 ? 1.1110 0.9492 0.7528 0.1274  -0.2830 -0.0709 550 THR A N   
3885  C CA  . THR A 550 ? 1.1521 0.9660 0.6966 0.1578  -0.2953 -0.0702 550 THR A CA  
3886  C C   . THR A 550 ? 1.1854 0.9454 0.6448 0.1628  -0.2696 -0.0851 550 THR A C   
3887  O O   . THR A 550 ? 1.2219 0.9501 0.5959 0.1890  -0.2505 -0.0700 550 THR A O   
3888  C CB  . THR A 550 ? 1.1645 1.0108 0.7118 0.1651  -0.3591 -0.0887 550 THR A CB  
3889  O OG1 . THR A 550 ? 1.1636 1.0072 0.7367 0.1396  -0.3858 -0.1279 550 THR A OG1 
3890  C CG2 . THR A 550 ? 1.1335 1.0411 0.7732 0.1652  -0.3797 -0.0676 550 THR A CG2 
3891  N N   . ASN A 551 ? 1.2208 0.9681 0.7038 0.1407  -0.2644 -0.1112 551 ASN A N   
3892  C CA  . ASN A 551 ? 1.2568 0.9562 0.6676 0.1481  -0.2380 -0.1276 551 ASN A CA  
3893  C C   . ASN A 551 ? 1.2525 0.9323 0.6568 0.1489  -0.1784 -0.1019 551 ASN A C   
3894  O O   . ASN A 551 ? 1.2798 0.9274 0.6427 0.1543  -0.1474 -0.1099 551 ASN A O   
3895  C CB  . ASN A 551 ? 1.2534 0.9444 0.7014 0.1269  -0.2514 -0.1630 551 ASN A CB  
3896  C CG  . ASN A 551 ? 1.2916 0.9710 0.6950 0.1326  -0.3034 -0.2021 551 ASN A CG  
3897  O OD1 . ASN A 551 ? 1.2730 0.9871 0.7317 0.1191  -0.3515 -0.2128 551 ASN A OD1 
3898  N ND2 . ASN A 551 ? 1.3479 0.9810 0.6548 0.1523  -0.2922 -0.2231 551 ASN A ND2 
3899  N N   . LEU A 552 ? 1.1795 0.8785 0.6259 0.1445  -0.1630 -0.0726 552 LEU A N   
3900  C CA  . LEU A 552 ? 1.1700 0.8572 0.6333 0.1362  -0.1148 -0.0521 552 LEU A CA  
3901  C C   . LEU A 552 ? 1.2164 0.8656 0.6010 0.1582  -0.0805 -0.0341 552 LEU A C   
3902  O O   . LEU A 552 ? 1.2395 0.8788 0.5757 0.1807  -0.0877 -0.0169 552 LEU A O   
3903  C CB  . LEU A 552 ? 1.1346 0.8478 0.6593 0.1257  -0.1142 -0.0330 552 LEU A CB  
3904  C CG  . LEU A 552 ? 1.1224 0.8296 0.6768 0.1129  -0.0778 -0.0155 552 LEU A CG  
3905  C CD1 . LEU A 552 ? 1.1026 0.8178 0.7002 0.0906  -0.0644 -0.0264 552 LEU A CD1 
3906  C CD2 . LEU A 552 ? 1.0986 0.8301 0.6969 0.1109  -0.0895 -0.0047 552 LEU A CD2 
3907  N N   . GLU A 553 ? 1.2698 0.8993 0.6468 0.1535  -0.0411 -0.0343 553 GLU A N   
3908  C CA  . GLU A 553 ? 1.3174 0.9115 0.6329 0.1708  0.0026  -0.0130 553 GLU A CA  
3909  C C   . GLU A 553 ? 1.3118 0.9032 0.6761 0.1536  0.0418  0.0118  553 GLU A C   
3910  O O   . GLU A 553 ? 1.3462 0.9077 0.6715 0.1662  0.0723  0.0382  553 GLU A O   
3911  C CB  . GLU A 553 ? 1.3525 0.9270 0.6295 0.1796  0.0277  -0.0281 553 GLU A CB  
3912  C CG  . GLU A 553 ? 1.3798 0.9404 0.5858 0.1997  -0.0061 -0.0578 553 GLU A CG  
3913  C CD  . GLU A 553 ? 1.4169 0.9532 0.5889 0.2095  0.0245  -0.0764 553 GLU A CD  
3914  O OE1 . GLU A 553 ? 1.4375 0.9626 0.6103 0.2131  0.0799  -0.0550 553 GLU A OE1 
3915  O OE2 . GLU A 553 ? 1.4283 0.9559 0.5786 0.2134  -0.0051 -0.1126 553 GLU A OE2 
3916  N N   . TYR A 554 ? 1.1268 0.7460 0.5734 0.1254  0.0405  0.0039  554 TYR A N   
3917  C CA  . TYR A 554 ? 1.1342 0.7532 0.6308 0.1045  0.0739  0.0182  554 TYR A CA  
3918  C C   . TYR A 554 ? 1.0910 0.7389 0.6539 0.0818  0.0504  0.0110  554 TYR A C   
3919  O O   . TYR A 554 ? 1.0577 0.7347 0.6614 0.0708  0.0309  -0.0049 554 TYR A O   
3920  C CB  . TYR A 554 ? 1.1564 0.7812 0.6766 0.0978  0.1053  0.0147  554 TYR A CB  
3921  C CG  . TYR A 554 ? 1.1744 0.8091 0.7607 0.0727  0.1352  0.0270  554 TYR A CG  
3922  C CD1 . TYR A 554 ? 1.1520 0.8214 0.8122 0.0470  0.1161  0.0169  554 TYR A CD1 
3923  C CD2 . TYR A 554 ? 1.2173 0.8275 0.7934 0.0742  0.1816  0.0492  554 TYR A CD2 
3924  C CE1 . TYR A 554 ? 1.1814 0.8637 0.9031 0.0223  0.1346  0.0236  554 TYR A CE1 
3925  C CE2 . TYR A 554 ? 1.2335 0.8563 0.8834 0.0462  0.2050  0.0578  554 TYR A CE2 
3926  C CZ  . TYR A 554 ? 1.2179 0.8786 0.9405 0.0196  0.1774  0.0424  554 TYR A CZ  
3927  O OH  . TYR A 554 ? 1.2245 0.9020 1.0218 -0.0101 0.1914  0.0463  554 TYR A OH  
3928  N N   . LEU A 555 ? 1.0960 0.7305 0.6642 0.0775  0.0550  0.0236  555 LEU A N   
3929  C CA  . LEU A 555 ? 1.0658 0.7196 0.6803 0.0609  0.0379  0.0172  555 LEU A CA  
3930  C C   . LEU A 555 ? 1.0989 0.7398 0.7452 0.0383  0.0610  0.0204  555 LEU A C   
3931  O O   . LEU A 555 ? 1.1353 0.7383 0.7620 0.0404  0.0868  0.0346  555 LEU A O   
3932  C CB  . LEU A 555 ? 1.0537 0.7011 0.6478 0.0779  0.0212  0.0241  555 LEU A CB  
3933  C CG  . LEU A 555 ? 1.0082 0.6929 0.6270 0.0807  -0.0130 0.0142  555 LEU A CG  
3934  C CD1 . LEU A 555 ? 1.0095 0.6919 0.6248 0.0966  -0.0200 0.0252  555 LEU A CD1 
3935  C CD2 . LEU A 555 ? 0.9761 0.6886 0.6455 0.0578  -0.0189 0.0026  555 LEU A CD2 
3936  N N   . ASP A 556 ? 1.0161 0.6864 0.7115 0.0167  0.0497  0.0078  556 ASP A N   
3937  C CA  . ASP A 556 ? 1.0211 0.6850 0.7506 -0.0083 0.0605  0.0042  556 ASP A CA  
3938  C C   . ASP A 556 ? 0.9784 0.6608 0.7236 -0.0177 0.0350  -0.0091 556 ASP A C   
3939  O O   . ASP A 556 ? 0.9450 0.6656 0.7157 -0.0221 0.0159  -0.0156 556 ASP A O   
3940  C CB  . ASP A 556 ? 1.0377 0.7249 0.8132 -0.0251 0.0740  0.0036  556 ASP A CB  
3941  C CG  . ASP A 556 ? 1.0589 0.7297 0.8692 -0.0509 0.0930  0.0046  556 ASP A CG  
3942  O OD1 . ASP A 556 ? 1.0524 0.6958 0.8534 -0.0602 0.0871  -0.0025 556 ASP A OD1 
3943  O OD2 . ASP A 556 ? 1.0812 0.7653 0.9320 -0.0621 0.1152  0.0116  556 ASP A OD2 
3944  N N   . LEU A 557 ? 1.0126 0.6634 0.7379 -0.0174 0.0380  -0.0115 557 LEU A N   
3945  C CA  . LEU A 557 ? 0.9895 0.6489 0.7156 -0.0227 0.0205  -0.0248 557 LEU A CA  
3946  C C   . LEU A 557 ? 1.0144 0.6431 0.7446 -0.0449 0.0258  -0.0399 557 LEU A C   
3947  O O   . LEU A 557 ? 1.0141 0.6337 0.7261 -0.0456 0.0158  -0.0538 557 LEU A O   
3948  C CB  . LEU A 557 ? 0.9870 0.6374 0.6831 0.0028  0.0182  -0.0183 557 LEU A CB  
3949  C CG  . LEU A 557 ? 0.9659 0.6481 0.6645 0.0216  0.0058  -0.0075 557 LEU A CG  
3950  C CD1 . LEU A 557 ? 0.9832 0.6591 0.6657 0.0457  0.0056  0.0014  557 LEU A CD1 
3951  C CD2 . LEU A 557 ? 0.9203 0.6463 0.6481 0.0130  -0.0130 -0.0123 557 LEU A CD2 
3952  N N   . SER A 558 ? 1.0435 0.6547 0.7979 -0.0636 0.0424  -0.0386 558 SER A N   
3953  C CA  . SER A 558 ? 1.0723 0.6430 0.8352 -0.0876 0.0491  -0.0542 558 SER A CA  
3954  C C   . SER A 558 ? 1.0631 0.6664 0.8539 -0.1135 0.0190  -0.0789 558 SER A C   
3955  O O   . SER A 558 ? 1.0354 0.6941 0.8435 -0.1115 -0.0030 -0.0780 558 SER A O   
3956  C CB  . SER A 558 ? 1.1020 0.6463 0.8939 -0.1021 0.0798  -0.0407 558 SER A CB  
3957  O OG  . SER A 558 ? 1.0941 0.6890 0.9408 -0.1181 0.0780  -0.0368 558 SER A OG  
3958  N N   . SER A 559 ? 1.0960 0.6602 0.8883 -0.1368 0.0165  -0.1015 559 SER A N   
3959  C CA  . SER A 559 ? 1.0998 0.6879 0.9106 -0.1633 -0.0179 -0.1303 559 SER A CA  
3960  C C   . SER A 559 ? 1.0776 0.6988 0.8458 -0.1433 -0.0450 -0.1359 559 SER A C   
3961  O O   . SER A 559 ? 1.0573 0.7364 0.8493 -0.1479 -0.0721 -0.1356 559 SER A O   
3962  C CB  . SER A 559 ? 1.0925 0.7341 0.9843 -0.1908 -0.0272 -0.1266 559 SER A CB  
3963  O OG  . SER A 559 ? 1.1171 0.7240 1.0536 -0.2157 -0.0005 -0.1242 559 SER A OG  
3964  N N   . ASN A 560 ? 1.1089 0.6918 0.8158 -0.1183 -0.0337 -0.1375 560 ASN A N   
3965  C CA  . ASN A 560 ? 1.0933 0.7009 0.7577 -0.0952 -0.0474 -0.1363 560 ASN A CA  
3966  C C   . ASN A 560 ? 1.1358 0.6854 0.7361 -0.0843 -0.0392 -0.1584 560 ASN A C   
3967  O O   . ASN A 560 ? 1.1760 0.6677 0.7680 -0.0998 -0.0311 -0.1803 560 ASN A O   
3968  C CB  . ASN A 560 ? 1.0543 0.6916 0.7253 -0.0674 -0.0341 -0.1045 560 ASN A CB  
3969  C CG  . ASN A 560 ? 1.0171 0.7172 0.7291 -0.0709 -0.0518 -0.0903 560 ASN A CG  
3970  O OD1 . ASN A 560 ? 1.0062 0.7386 0.7090 -0.0667 -0.0714 -0.0899 560 ASN A OD1 
3971  N ND2 . ASN A 560 ? 1.0059 0.7192 0.7594 -0.0756 -0.0418 -0.0769 560 ASN A ND2 
3972  N N   . ARG A 561 ? 1.1374 0.6990 0.6939 -0.0568 -0.0375 -0.1521 561 ARG A N   
3973  C CA  . ARG A 561 ? 1.1861 0.6956 0.6756 -0.0399 -0.0247 -0.1724 561 ARG A CA  
3974  C C   . ARG A 561 ? 1.1820 0.6877 0.6584 -0.0019 0.0067  -0.1471 561 ARG A C   
3975  O O   . ARG A 561 ? 1.2108 0.7051 0.6380 0.0218  0.0188  -0.1514 561 ARG A O   
3976  C CB  . ARG A 561 ? 1.2093 0.7344 0.6478 -0.0406 -0.0504 -0.1924 561 ARG A CB  
3977  C CG  . ARG A 561 ? 1.2086 0.7599 0.6721 -0.0760 -0.0915 -0.2127 561 ARG A CG  
3978  C CD  . ARG A 561 ? 1.2531 0.8017 0.6451 -0.0748 -0.1204 -0.2408 561 ARG A CD  
3979  N NE  . ARG A 561 ? 1.2358 0.8336 0.6007 -0.0475 -0.1225 -0.2127 561 ARG A NE  
3980  C CZ  . ARG A 561 ? 1.2543 0.8820 0.5786 -0.0464 -0.1560 -0.2192 561 ARG A CZ  
3981  N NH1 . ARG A 561 ? 1.2888 0.9091 0.5954 -0.0721 -0.1976 -0.2571 561 ARG A NH1 
3982  N NH2 . ARG A 561 ? 1.2421 0.9076 0.5442 -0.0188 -0.1489 -0.1858 561 ARG A NH2 
3983  N N   . PHE A 562 ? 1.1570 0.6753 0.6771 0.0059  0.0201  -0.1201 562 PHE A N   
3984  C CA  . PHE A 562 ? 1.1608 0.6798 0.6797 0.0407  0.0445  -0.0970 562 PHE A CA  
3985  C C   . PHE A 562 ? 1.2149 0.6632 0.6923 0.0586  0.0708  -0.1122 562 PHE A C   
3986  O O   . PHE A 562 ? 1.2399 0.6308 0.7112 0.0437  0.0763  -0.1286 562 PHE A O   
3987  C CB  . PHE A 562 ? 1.1306 0.6722 0.6957 0.0444  0.0462  -0.0702 562 PHE A CB  
3988  C CG  . PHE A 562 ? 1.0817 0.6870 0.6850 0.0337  0.0250  -0.0562 562 PHE A CG  
3989  C CD1 . PHE A 562 ? 1.0657 0.7177 0.6810 0.0471  0.0205  -0.0416 562 PHE A CD1 
3990  C CD2 . PHE A 562 ? 1.0582 0.6733 0.6889 0.0110  0.0139  -0.0566 562 PHE A CD2 
3991  C CE1 . PHE A 562 ? 1.0232 0.7234 0.6747 0.0372  0.0027  -0.0300 562 PHE A CE1 
3992  C CE2 . PHE A 562 ? 1.0170 0.6832 0.6807 0.0047  -0.0023 -0.0458 562 PHE A CE2 
3993  C CZ  . PHE A 562 ? 0.9973 0.7024 0.6700 0.0175  -0.0091 -0.0337 562 PHE A CZ  
3994  N N   . SER A 563 ? 1.2759 0.7255 0.7288 0.0914  0.0910  -0.1056 563 SER A N   
3995  C CA  . SER A 563 ? 1.3340 0.7142 0.7313 0.1094  0.1156  -0.1293 563 SER A CA  
3996  C C   . SER A 563 ? 1.3554 0.7092 0.7615 0.1488  0.1501  -0.1100 563 SER A C   
3997  O O   . SER A 563 ? 1.4052 0.6855 0.7692 0.1637  0.1739  -0.1309 563 SER A O   
3998  C CB  . SER A 563 ? 1.3594 0.7500 0.7021 0.1207  0.1179  -0.1436 563 SER A CB  
3999  O OG  . SER A 563 ? 1.3632 0.7530 0.6757 0.0883  0.0853  -0.1722 563 SER A OG  
4000  N N   . PHE A 564 ? 1.2959 0.7049 0.7558 0.1669  0.1516  -0.0728 564 PHE A N   
4001  C CA  . PHE A 564 ? 1.3143 0.7126 0.7898 0.2091  0.1803  -0.0511 564 PHE A CA  
4002  C C   . PHE A 564 ? 1.2925 0.6952 0.8080 0.2126  0.1721  -0.0255 564 PHE A C   
4003  O O   . PHE A 564 ? 1.2689 0.6770 0.7945 0.1829  0.1500  -0.0261 564 PHE A O   
4004  C CB  . PHE A 564 ? 1.3080 0.7741 0.8122 0.2360  0.1918  -0.0283 564 PHE A CB  
4005  C CG  . PHE A 564 ? 1.3440 0.7895 0.7935 0.2486  0.2155  -0.0479 564 PHE A CG  
4006  C CD1 . PHE A 564 ? 1.3879 0.7793 0.8030 0.2857  0.2551  -0.0563 564 PHE A CD1 
4007  C CD2 . PHE A 564 ? 1.3363 0.8122 0.7617 0.2273  0.2001  -0.0572 564 PHE A CD2 
4008  C CE1 . PHE A 564 ? 1.4279 0.7947 0.7789 0.3011  0.2803  -0.0766 564 PHE A CE1 
4009  C CE2 . PHE A 564 ? 1.3749 0.8289 0.7348 0.2428  0.2223  -0.0738 564 PHE A CE2 
4010  C CZ  . PHE A 564 ? 1.4231 0.8217 0.7420 0.2796  0.2631  -0.0851 564 PHE A CZ  
4011  N N   . GLU A 565 ? 1.3678 0.7691 0.9038 0.2531  0.1914  -0.0012 565 GLU A N   
4012  C CA  . GLU A 565 ? 1.3556 0.7469 0.9121 0.2659  0.1866  0.0244  565 GLU A CA  
4013  C C   . GLU A 565 ? 1.3072 0.7730 0.9031 0.2511  0.1514  0.0438  565 GLU A C   
4014  O O   . GLU A 565 ? 1.2805 0.8163 0.9082 0.2430  0.1345  0.0464  565 GLU A O   
4015  C CB  . GLU A 565 ? 1.3677 0.7533 0.9427 0.3183  0.2112  0.0491  565 GLU A CB  
4016  C CG  . GLU A 565 ? 1.3490 0.8130 0.9695 0.3421  0.2150  0.0633  565 GLU A CG  
4017  C CD  . GLU A 565 ? 1.3903 0.8188 0.9786 0.3603  0.2533  0.0436  565 GLU A CD  
4018  O OE1 . GLU A 565 ? 1.4269 0.7810 0.9513 0.3408  0.2637  0.0086  565 GLU A OE1 
4019  O OE2 . GLU A 565 ? 1.3854 0.8609 1.0128 0.3945  0.2734  0.0623  565 GLU A OE2 
4020  N N   . ILE A 566 ? 1.2687 0.7128 0.8584 0.2488  0.1431  0.0576  566 ILE A N   
4021  C CA  . ILE A 566 ? 1.2284 0.7275 0.8386 0.2371  0.1114  0.0716  566 ILE A CA  
4022  C C   . ILE A 566 ? 1.1989 0.7684 0.8539 0.2673  0.0936  0.0956  566 ILE A C   
4023  O O   . ILE A 566 ? 1.2120 0.7732 0.8768 0.3063  0.1067  0.1153  566 ILE A O   
4024  C CB  . ILE A 566 ? 1.2422 0.6917 0.8227 0.2356  0.1155  0.0840  566 ILE A CB  
4025  C CG1 . ILE A 566 ? 1.2655 0.6565 0.8219 0.1983  0.1306  0.0603  566 ILE A CG1 
4026  C CG2 . ILE A 566 ? 1.2086 0.7097 0.7964 0.2333  0.0852  0.0983  566 ILE A CG2 
4027  C CD1 . ILE A 566 ? 1.2833 0.6267 0.8185 0.1924  0.1423  0.0755  566 ILE A CD1 
4028  N N   . PRO A 567 ? 1.1760 0.8149 0.8652 0.2513  0.0632  0.0950  567 PRO A N   
4029  C CA  . PRO A 567 ? 1.1478 0.8574 0.8910 0.2742  0.0402  0.1150  567 PRO A CA  
4030  C C   . PRO A 567 ? 1.1518 0.8531 0.8814 0.3053  0.0270  0.1384  567 PRO A C   
4031  O O   . PRO A 567 ? 1.1540 0.8325 0.8424 0.2963  0.0135  0.1388  567 PRO A O   
4032  C CB  . PRO A 567 ? 1.1125 0.8758 0.8826 0.2421  0.0085  0.1036  567 PRO A CB  
4033  C CG  . PRO A 567 ? 1.1209 0.8544 0.8642 0.2097  0.0234  0.0811  567 PRO A CG  
4034  C CD  . PRO A 567 ? 1.1572 0.8133 0.8447 0.2110  0.0484  0.0749  567 PRO A CD  
4035  N N   . PRO A 568 ? 1.1875 0.9071 0.9488 0.3460  0.0327  0.1611  568 PRO A N   
4036  C CA  . PRO A 568 ? 1.1949 0.9108 0.9413 0.3817  0.0160  0.1885  568 PRO A CA  
4037  C C   . PRO A 568 ? 1.1682 0.9506 0.9330 0.3772  -0.0367 0.1919  568 PRO A C   
4038  O O   . PRO A 568 ? 1.1802 0.9577 0.9136 0.4039  -0.0576 0.2118  568 PRO A O   
4039  C CB  . PRO A 568 ? 1.2002 0.9330 0.9933 0.4272  0.0344  0.2113  568 PRO A CB  
4040  C CG  . PRO A 568 ? 1.1844 0.9589 1.0324 0.4126  0.0507  0.1964  568 PRO A CG  
4041  C CD  . PRO A 568 ? 1.1732 0.9515 1.0048 0.3607  0.0402  0.1674  568 PRO A CD  
4042  N N   . THR A 569 ? 1.1803 1.0191 0.9897 0.3450  -0.0587 0.1724  569 THR A N   
4043  C CA  . THR A 569 ? 1.1578 1.0613 0.9967 0.3367  -0.1113 0.1683  569 THR A CA  
4044  C C   . THR A 569 ? 1.1591 1.0332 0.9353 0.3080  -0.1277 0.1475  569 THR A C   
4045  O O   . THR A 569 ? 1.1451 1.0615 0.9347 0.2969  -0.1711 0.1358  569 THR A O   
4046  C CB  . THR A 569 ? 1.1304 1.1071 1.0640 0.3178  -0.1210 0.1610  569 THR A CB  
4047  O OG1 . THR A 569 ? 1.1109 1.1393 1.0740 0.2977  -0.1721 0.1477  569 THR A OG1 
4048  C CG2 . THR A 569 ? 1.1314 1.0787 1.0582 0.2865  -0.0839 0.1434  569 THR A CG2 
4049  N N   . LEU A 570 ? 1.1975 1.0001 0.9098 0.2956  -0.0935 0.1413  570 LEU A N   
4050  C CA  . LEU A 570 ? 1.2014 0.9748 0.8567 0.2733  -0.0998 0.1258  570 LEU A CA  
4051  C C   . LEU A 570 ? 1.2325 0.9766 0.8192 0.3044  -0.1092 0.1457  570 LEU A C   
4052  O O   . LEU A 570 ? 1.2637 0.9430 0.7954 0.3134  -0.0754 0.1597  570 LEU A O   
4053  C CB  . LEU A 570 ? 1.2083 0.9283 0.8406 0.2457  -0.0595 0.1131  570 LEU A CB  
4054  C CG  . LEU A 570 ? 1.1809 0.9260 0.8553 0.2100  -0.0579 0.0898  570 LEU A CG  
4055  C CD1 . LEU A 570 ? 1.1940 0.8887 0.8433 0.1871  -0.0243 0.0788  570 LEU A CD1 
4056  C CD2 . LEU A 570 ? 1.1580 0.9378 0.8415 0.1915  -0.0904 0.0737  570 LEU A CD2 
4057  N N   . ASN A 571 ? 1.2714 1.0638 0.8615 0.3215  -0.1573 0.1479  571 ASN A N   
4058  C CA  . ASN A 571 ? 1.3073 1.0770 0.8212 0.3565  -0.1728 0.1686  571 ASN A CA  
4059  C C   . ASN A 571 ? 1.3105 1.1106 0.7901 0.3527  -0.2236 0.1484  571 ASN A C   
4060  O O   . ASN A 571 ? 1.3508 1.1544 0.7857 0.3750  -0.2429 0.1592  571 ASN A O   
4061  C CB  . ASN A 571 ? 1.3162 1.1071 0.8537 0.4007  -0.1828 0.2014  571 ASN A CB  
4062  C CG  . ASN A 571 ? 1.2800 1.1567 0.9193 0.4017  -0.2186 0.1966  571 ASN A CG  
4063  O OD1 . ASN A 571 ? 1.2563 1.1856 0.9334 0.3762  -0.2580 0.1708  571 ASN A OD1 
4064  N ND2 . ASN A 571 ? 1.2772 1.1677 0.9681 0.4306  -0.2014 0.2218  571 ASN A ND2 
4065  N N   . ASN A 572 ? 1.2971 1.1208 0.8094 0.3146  -0.2378 0.1138  572 ASN A N   
4066  C CA  . ASN A 572 ? 1.3017 1.1517 0.7899 0.3085  -0.2891 0.0870  572 ASN A CA  
4067  C C   . ASN A 572 ? 1.3029 1.1175 0.7567 0.2771  -0.2704 0.0577  572 ASN A C   
4068  O O   . ASN A 572 ? 1.2837 1.1242 0.7742 0.2506  -0.2974 0.0261  572 ASN A O   
4069  C CB  . ASN A 572 ? 1.2673 1.1959 0.8551 0.2965  -0.3390 0.0727  572 ASN A CB  
4070  C CG  . ASN A 572 ? 1.2864 1.2408 0.8508 0.2920  -0.3981 0.0439  572 ASN A CG  
4071  O OD1 . ASN A 572 ? 1.3444 1.2978 0.8557 0.3120  -0.4124 0.0516  572 ASN A OD1 
4072  N ND2 . ASN A 572 ? 1.2568 1.2317 0.8703 0.2574  -0.4224 0.0092  572 ASN A ND2 
4073  N N   . LEU A 573 ? 1.3072 1.0616 0.6985 0.2795  -0.2212 0.0693  573 LEU A N   
4074  C CA  . LEU A 573 ? 1.3124 1.0374 0.6718 0.2563  -0.2020 0.0453  573 LEU A CA  
4075  C C   . LEU A 573 ? 1.3677 1.0506 0.6121 0.2827  -0.1983 0.0492  573 LEU A C   
4076  O O   . LEU A 573 ? 1.3959 1.0305 0.5913 0.2921  -0.1495 0.0723  573 LEU A O   
4077  C CB  . LEU A 573 ? 1.2962 0.9935 0.6869 0.2327  -0.1475 0.0520  573 LEU A CB  
4078  C CG  . LEU A 573 ? 1.2521 0.9823 0.7373 0.2102  -0.1446 0.0494  573 LEU A CG  
4079  C CD1 . LEU A 573 ? 1.2448 0.9453 0.7448 0.1868  -0.0989 0.0498  573 LEU A CD1 
4080  C CD2 . LEU A 573 ? 1.2208 0.9993 0.7660 0.1897  -0.1823 0.0233  573 LEU A CD2 
4081  N N   . PRO A 574 ? 1.3577 1.0620 0.5777 0.2874  -0.2403 0.0250  574 PRO A N   
4082  C CA  . PRO A 574 ? 1.4457 1.1215 0.5790 0.3092  -0.2291 0.0291  574 PRO A CA  
4083  C C   . PRO A 574 ? 1.4708 1.0994 0.5490 0.3030  -0.1854 0.0185  574 PRO A C   
4084  O O   . PRO A 574 ? 1.5601 1.1642 0.5651 0.3223  -0.1728 0.0210  574 PRO A O   
4085  C CB  . PRO A 574 ? 1.4897 1.2065 0.6258 0.3100  -0.2920 0.0003  574 PRO A CB  
4086  C CG  . PRO A 574 ? 1.4111 1.1583 0.6254 0.2774  -0.3208 -0.0320 574 PRO A CG  
4087  C CD  . PRO A 574 ? 1.3318 1.0857 0.6093 0.2694  -0.2976 -0.0087 574 PRO A CD  
4088  N N   . ARG A 575 ? 1.4740 1.0906 0.5849 0.2788  -0.1602 0.0086  575 ARG A N   
4089  C CA  . ARG A 575 ? 1.4968 1.0756 0.5680 0.2739  -0.1152 0.0009  575 ARG A CA  
4090  C C   . ARG A 575 ? 1.4758 1.0327 0.5775 0.2591  -0.0598 0.0243  575 ARG A C   
4091  O O   . ARG A 575 ? 1.4895 1.0263 0.5848 0.2505  -0.0190 0.0197  575 ARG A O   
4092  C CB  . ARG A 575 ? 1.4834 1.0713 0.5707 0.2552  -0.1396 -0.0444 575 ARG A CB  
4093  C CG  . ARG A 575 ? 1.5394 1.1412 0.5977 0.2641  -0.1882 -0.0726 575 ARG A CG  
4094  C CD  . ARG A 575 ? 1.5267 1.1292 0.6110 0.2426  -0.2094 -0.1179 575 ARG A CD  
4095  N NE  . ARG A 575 ? 1.5833 1.2053 0.6620 0.2425  -0.2657 -0.1472 575 ARG A NE  
4096  C CZ  . ARG A 575 ? 1.5455 1.2120 0.6944 0.2263  -0.3183 -0.1579 575 ARG A CZ  
4097  N NH1 . ARG A 575 ? 1.4517 1.1473 0.6789 0.2116  -0.3219 -0.1417 575 ARG A NH1 
4098  N NH2 . ARG A 575 ? 1.6109 1.2943 0.7537 0.2245  -0.3675 -0.1851 575 ARG A NH2 
4099  N N   . LEU A 576 ? 1.4442 1.0130 0.6048 0.2511  -0.0550 0.0466  576 LEU A N   
4100  C CA  . LEU A 576 ? 1.4285 0.9850 0.6463 0.2274  -0.0076 0.0618  576 LEU A CA  
4101  C C   . LEU A 576 ? 1.4791 0.9850 0.6376 0.2451  0.0439  0.0965  576 LEU A C   
4102  O O   . LEU A 576 ? 1.5069 0.9901 0.6155 0.2737  0.0435  0.1247  576 LEU A O   
4103  C CB  . LEU A 576 ? 1.3885 0.9684 0.6802 0.2147  -0.0213 0.0682  576 LEU A CB  
4104  C CG  . LEU A 576 ? 1.3685 0.9437 0.7281 0.1838  0.0120  0.0703  576 LEU A CG  
4105  C CD1 . LEU A 576 ? 1.3272 0.9390 0.7501 0.1540  -0.0016 0.0417  576 LEU A CD1 
4106  C CD2 . LEU A 576 ? 1.3593 0.9306 0.7498 0.1871  0.0120  0.0858  576 LEU A CD2 
4107  N N   . TYR A 577 ? 1.4362 0.9258 0.6053 0.2296  0.0900  0.0979  577 TYR A N   
4108  C CA  . TYR A 577 ? 1.4800 0.9238 0.6186 0.2375  0.1480  0.1339  577 TYR A CA  
4109  C C   . TYR A 577 ? 1.4636 0.9044 0.6930 0.2014  0.1803  0.1416  577 TYR A C   
4110  O O   . TYR A 577 ? 1.4967 0.8986 0.7208 0.2004  0.2298  0.1714  577 TYR A O   
4111  C CB  . TYR A 577 ? 1.5227 0.9472 0.5982 0.2525  0.1843  0.1359  577 TYR A CB  
4112  C CG  . TYR A 577 ? 1.5038 0.9555 0.6412 0.2261  0.1987  0.1095  577 TYR A CG  
4113  C CD1 . TYR A 577 ? 1.4996 0.9555 0.7169 0.1971  0.2433  0.1212  577 TYR A CD1 
4114  C CD2 . TYR A 577 ? 1.4951 0.9672 0.6139 0.2315  0.1668  0.0732  577 TYR A CD2 
4115  C CE1 . TYR A 577 ? 1.4855 0.9728 0.7649 0.1775  0.2541  0.1008  577 TYR A CE1 
4116  C CE2 . TYR A 577 ? 1.4813 0.9748 0.6576 0.2127  0.1821  0.0526  577 TYR A CE2 
4117  C CZ  . TYR A 577 ? 1.4761 0.9806 0.7331 0.1877  0.2254  0.0684  577 TYR A CZ  
4118  O OH  . TYR A 577 ? 1.4648 0.9972 0.7851 0.1731  0.2383  0.0512  577 TYR A OH  
4119  N N   . TYR A 578 ? 1.2979 0.7766 0.6084 0.1715  0.1535  0.1157  578 TYR A N   
4120  C CA  . TYR A 578 ? 1.2894 0.7696 0.6813 0.1356  0.1750  0.1147  578 TYR A CA  
4121  C C   . TYR A 578 ? 1.2498 0.7542 0.6908 0.1210  0.1380  0.0969  578 TYR A C   
4122  O O   . TYR A 578 ? 1.2126 0.7566 0.6685 0.1200  0.1004  0.0748  578 TYR A O   
4123  C CB  . TYR A 578 ? 1.2878 0.7961 0.7298 0.1123  0.1919  0.1000  578 TYR A CB  
4124  C CG  . TYR A 578 ? 1.2878 0.8042 0.8157 0.0743  0.2093  0.0980  578 TYR A CG  
4125  C CD1 . TYR A 578 ? 1.2577 0.8090 0.8457 0.0501  0.1761  0.0740  578 TYR A CD1 
4126  C CD2 . TYR A 578 ? 1.3172 0.8075 0.8666 0.0621  0.2584  0.1202  578 TYR A CD2 
4127  C CE1 . TYR A 578 ? 1.2587 0.8189 0.9175 0.0162  0.1846  0.0683  578 TYR A CE1 
4128  C CE2 . TYR A 578 ? 1.3110 0.8124 0.9460 0.0237  0.2677  0.1142  578 TYR A CE2 
4129  C CZ  . TYR A 578 ? 1.2816 0.8182 0.9671 0.0013  0.2273  0.0862  578 TYR A CZ  
4130  O OH  . TYR A 578 ? 1.2707 0.8193 1.0342 -0.0363 0.2297  0.0767  578 TYR A OH  
4131  N N   . MET A 579 ? 1.3160 0.7924 0.7817 0.1100  0.1523  0.1063  579 MET A N   
4132  C CA  . MET A 579 ? 1.2873 0.7802 0.7939 0.0976  0.1262  0.0893  579 MET A CA  
4133  C C   . MET A 579 ? 1.3039 0.7674 0.8531 0.0683  0.1505  0.0867  579 MET A C   
4134  O O   . MET A 579 ? 1.3342 0.7438 0.8669 0.0730  0.1807  0.1069  579 MET A O   
4135  C CB  . MET A 579 ? 1.2816 0.7646 0.7543 0.1293  0.1079  0.1010  579 MET A CB  
4136  C CG  . MET A 579 ? 1.2621 0.7531 0.7727 0.1215  0.0939  0.0879  579 MET A CG  
4137  S SD  . MET A 579 ? 1.2601 0.7474 0.7474 0.1628  0.0778  0.1057  579 MET A SD  
4138  C CE  . MET A 579 ? 1.2111 0.7737 0.7159 0.1682  0.0299  0.0903  579 MET A CE  
4139  N N   . ASN A 580 ? 1.1872 0.6831 0.7897 0.0384  0.1359  0.0620  580 ASN A N   
4140  C CA  . ASN A 580 ? 1.1929 0.6672 0.8380 0.0062  0.1483  0.0510  580 ASN A CA  
4141  C C   . ASN A 580 ? 1.1658 0.6537 0.8222 -0.0004 0.1196  0.0272  580 ASN A C   
4142  O O   . ASN A 580 ? 1.1327 0.6710 0.8080 -0.0061 0.0928  0.0123  580 ASN A O   
4143  C CB  . ASN A 580 ? 1.1916 0.6963 0.8904 -0.0233 0.1574  0.0446  580 ASN A CB  
4144  C CG  . ASN A 580 ? 1.2016 0.6802 0.9497 -0.0591 0.1729  0.0368  580 ASN A CG  
4145  O OD1 . ASN A 580 ? 1.2094 0.6444 0.9482 -0.0648 0.1720  0.0280  580 ASN A OD1 
4146  N ND2 . ASN A 580 ? 1.2036 0.7087 1.0093 -0.0838 0.1871  0.0382  580 ASN A ND2 
4147  N N   . LEU A 581 ? 1.1891 0.6273 0.8304 0.0031  0.1289  0.0252  581 LEU A N   
4148  C CA  . LEU A 581 ? 1.1752 0.6154 0.8147 0.0018  0.1100  0.0029  581 LEU A CA  
4149  C C   . LEU A 581 ? 1.1974 0.5917 0.8517 -0.0275 0.1185  -0.0192 581 LEU A C   
4150  O O   . LEU A 581 ? 1.2100 0.5739 0.8431 -0.0215 0.1158  -0.0356 581 LEU A O   
4151  C CB  . LEU A 581 ? 1.1833 0.6072 0.7871 0.0400  0.1111  0.0160  581 LEU A CB  
4152  C CG  . LEU A 581 ? 1.1691 0.6310 0.7578 0.0701  0.0989  0.0373  581 LEU A CG  
4153  C CD1 . LEU A 581 ? 1.1735 0.6283 0.7446 0.1054  0.0966  0.0489  581 LEU A CD1 
4154  C CD2 . LEU A 581 ? 1.1313 0.6597 0.7438 0.0598  0.0713  0.0256  581 LEU A CD2 
4155  N N   . SER A 582 ? 1.2443 0.6333 0.9373 -0.0593 0.1290  -0.0217 582 SER A N   
4156  C CA  . SER A 582 ? 1.2719 0.6124 0.9886 -0.0925 0.1363  -0.0433 582 SER A CA  
4157  C C   . SER A 582 ? 1.2603 0.6257 0.9828 -0.1129 0.1006  -0.0818 582 SER A C   
4158  O O   . SER A 582 ? 1.2254 0.6552 0.9501 -0.1081 0.0735  -0.0862 582 SER A O   
4159  C CB  . SER A 582 ? 1.2814 0.6235 1.0547 -0.1232 0.1571  -0.0319 582 SER A CB  
4160  O OG  . SER A 582 ? 1.2868 0.6284 1.1119 -0.1676 0.1424  -0.0624 582 SER A OG  
4161  N N   . ARG A 583 ? 1.2877 0.5956 1.0072 -0.1344 0.1009  -0.1101 583 ARG A N   
4162  C CA  . ARG A 583 ? 1.2916 0.6148 1.0107 -0.1586 0.0648  -0.1513 583 ARG A CA  
4163  C C   . ARG A 583 ? 1.2721 0.6282 0.9377 -0.1281 0.0443  -0.1577 583 ARG A C   
4164  O O   . ARG A 583 ? 1.2404 0.6635 0.9155 -0.1316 0.0154  -0.1611 583 ARG A O   
4165  C CB  . ARG A 583 ? 1.2718 0.6573 1.0610 -0.1965 0.0410  -0.1586 583 ARG A CB  
4166  C CG  . ARG A 583 ? 1.2934 0.6478 1.1489 -0.2328 0.0634  -0.1549 583 ARG A CG  
4167  C CD  . ARG A 583 ? 1.2658 0.6988 1.2049 -0.2602 0.0501  -0.1476 583 ARG A CD  
4168  N NE  . ARG A 583 ? 1.2824 0.6932 1.2991 -0.2974 0.0757  -0.1412 583 ARG A NE  
4169  C CZ  . ARG A 583 ? 1.2940 0.6572 1.3168 -0.2901 0.1268  -0.1078 583 ARG A CZ  
4170  N NH1 . ARG A 583 ? 1.2922 0.6298 1.2470 -0.2450 0.1532  -0.0778 583 ARG A NH1 
4171  N NH2 . ARG A 583 ? 1.3069 0.6502 1.4087 -0.3286 0.1513  -0.1021 583 ARG A NH2 
4172  N N   . ASN A 584 ? 1.3139 0.6211 0.9272 -0.0961 0.0637  -0.1555 584 ASN A N   
4173  C CA  . ASN A 584 ? 1.3025 0.6341 0.8695 -0.0637 0.0560  -0.1563 584 ASN A CA  
4174  C C   . ASN A 584 ? 1.3554 0.6087 0.8695 -0.0446 0.0764  -0.1756 584 ASN A C   
4175  O O   . ASN A 584 ? 1.4001 0.5808 0.9117 -0.0635 0.0872  -0.1971 584 ASN A O   
4176  C CB  . ASN A 584 ? 1.2619 0.6422 0.8390 -0.0322 0.0642  -0.1171 584 ASN A CB  
4177  C CG  . ASN A 584 ? 1.2127 0.6708 0.8268 -0.0440 0.0412  -0.1056 584 ASN A CG  
4178  O OD1 . ASN A 584 ? 1.1906 0.6935 0.7979 -0.0416 0.0205  -0.1112 584 ASN A OD1 
4179  N ND2 . ASN A 584 ? 1.2010 0.6714 0.8513 -0.0533 0.0488  -0.0872 584 ASN A ND2 
4180  N N   . ASP A 585 ? 1.4374 0.7031 0.9136 -0.0069 0.0843  -0.1683 585 ASP A N   
4181  C CA  . ASP A 585 ? 1.4914 0.6887 0.9132 0.0176  0.1065  -0.1882 585 ASP A CA  
4182  C C   . ASP A 585 ? 1.4921 0.6818 0.9129 0.0649  0.1382  -0.1546 585 ASP A C   
4183  O O   . ASP A 585 ? 1.5260 0.6858 0.9075 0.0966  0.1587  -0.1629 585 ASP A O   
4184  C CB  . ASP A 585 ? 1.5072 0.7228 0.8771 0.0230  0.0910  -0.2148 585 ASP A CB  
4185  C CG  . ASP A 585 ? 1.5435 0.7271 0.8880 -0.0155 0.0629  -0.2626 585 ASP A CG  
4186  O OD1 . ASP A 585 ? 1.5313 0.7156 0.9245 -0.0548 0.0458  -0.2687 585 ASP A OD1 
4187  O OD2 . ASP A 585 ? 1.5834 0.7512 0.8665 -0.0058 0.0570  -0.2915 585 ASP A OD2 
4188  N N   . LEU A 586 ? 1.4441 0.6623 0.9062 0.0725  0.1423  -0.1172 586 LEU A N   
4189  C CA  . LEU A 586 ? 1.4444 0.6661 0.9123 0.1175  0.1637  -0.0831 586 LEU A CA  
4190  C C   . LEU A 586 ? 1.5006 0.6278 0.9413 0.1402  0.1974  -0.0889 586 LEU A C   
4191  O O   . LEU A 586 ? 1.5320 0.5873 0.9680 0.1176  0.2071  -0.1026 586 LEU A O   
4192  C CB  . LEU A 586 ? 1.4084 0.6706 0.9130 0.1185  0.1556  -0.0471 586 LEU A CB  
4193  C CG  . LEU A 586 ? 1.3578 0.7011 0.8897 0.0947  0.1249  -0.0451 586 LEU A CG  
4194  C CD1 . LEU A 586 ? 1.3518 0.6846 0.8977 0.0528  0.1156  -0.0591 586 LEU A CD1 
4195  C CD2 . LEU A 586 ? 1.3276 0.7262 0.8838 0.1147  0.1154  -0.0121 586 LEU A CD2 
4196  N N   . ASP A 587 ? 1.5908 0.7178 1.0204 0.1858  0.2179  -0.0770 587 ASP A N   
4197  C CA  . ASP A 587 ? 1.6426 0.6934 1.0407 0.2058  0.2475  -0.0949 587 ASP A CA  
4198  C C   . ASP A 587 ? 1.6492 0.6938 1.0683 0.2531  0.2731  -0.0573 587 ASP A C   
4199  O O   . ASP A 587 ? 1.6948 0.7135 1.1004 0.2778  0.2962  -0.0646 587 ASP A O   
4200  C CB  . ASP A 587 ? 1.6603 0.7246 1.0208 0.2140  0.2500  -0.1237 587 ASP A CB  
4201  C CG  . ASP A 587 ? 1.6335 0.7740 1.0110 0.2500  0.2546  -0.0970 587 ASP A CG  
4202  O OD1 . ASP A 587 ? 1.5868 0.7953 1.0177 0.2532  0.2387  -0.0602 587 ASP A OD1 
4203  O OD2 . ASP A 587 ? 1.6549 0.8020 1.0020 0.2707  0.2710  -0.1096 587 ASP A OD2 
4204  N N   . GLN A 588 ? 1.6425 0.7116 1.0919 0.2679  0.2684  -0.0173 588 GLN A N   
4205  C CA  . GLN A 588 ? 1.6551 0.7260 1.1247 0.3131  0.2868  0.0191  588 GLN A CA  
4206  C C   . GLN A 588 ? 1.6471 0.7123 1.1301 0.3112  0.2807  0.0531  588 GLN A C   
4207  O O   . GLN A 588 ? 1.6423 0.6860 1.1186 0.2728  0.2720  0.0454  588 GLN A O   
4208  C CB  . GLN A 588 ? 1.6211 0.7666 1.1186 0.3561  0.2857  0.0404  588 GLN A CB  
4209  C CG  . GLN A 588 ? 1.6646 0.7953 1.1568 0.3855  0.3161  0.0309  588 GLN A CG  
4210  C CD  . GLN A 588 ? 1.6301 0.8420 1.1595 0.4211  0.3198  0.0487  588 GLN A CD  
4211  O OE1 . GLN A 588 ? 1.6257 0.8583 1.1399 0.4140  0.3238  0.0273  588 GLN A OE1 
4212  N NE2 . GLN A 588 ? 1.6091 0.8729 1.1915 0.4589  0.3183  0.0895  588 GLN A NE2 
4213  N N   . THR A 589 ? 1.5980 0.6857 1.1004 0.3535  0.2862  0.0917  589 THR A N   
4214  C CA  . THR A 589 ? 1.6096 0.6906 1.1132 0.3590  0.2833  0.1264  589 THR A CA  
4215  C C   . THR A 589 ? 1.5477 0.6908 1.0557 0.3529  0.2506  0.1439  589 THR A C   
4216  O O   . THR A 589 ? 1.5012 0.7066 1.0259 0.3599  0.2279  0.1409  589 THR A O   
4217  C CB  . THR A 589 ? 1.6540 0.7449 1.1738 0.4086  0.2945  0.1609  589 THR A CB  
4218  O OG1 . THR A 589 ? 1.5952 0.7761 1.1476 0.4406  0.2697  0.1813  589 THR A OG1 
4219  C CG2 . THR A 589 ? 1.7291 0.7658 1.2458 0.4212  0.3268  0.1424  589 THR A CG2 
4220  N N   . ILE A 590 ? 1.5465 0.6710 1.0391 0.3402  0.2502  0.1626  590 ILE A N   
4221  C CA  . ILE A 590 ? 1.4984 0.6739 0.9840 0.3352  0.2216  0.1788  590 ILE A CA  
4222  C C   . ILE A 590 ? 1.4788 0.7270 0.9802 0.3793  0.1948  0.2078  590 ILE A C   
4223  O O   . ILE A 590 ? 1.5280 0.7711 1.0315 0.4116  0.2031  0.2331  590 ILE A O   
4224  C CB  . ILE A 590 ? 1.5332 0.6700 0.9952 0.3160  0.2360  0.1942  590 ILE A CB  
4225  C CG1 . ILE A 590 ? 1.5606 0.6297 1.0267 0.2705  0.2624  0.1655  590 ILE A CG1 
4226  C CG2 . ILE A 590 ? 1.4905 0.6758 0.9359 0.3086  0.2097  0.2048  590 ILE A CG2 
4227  C CD1 . ILE A 590 ? 1.6149 0.6416 1.0735 0.2543  0.2872  0.1847  590 ILE A CD1 
4228  N N   . PRO A 591 ? 1.4344 0.7529 0.9525 0.3809  0.1601  0.2047  591 PRO A N   
4229  C CA  . PRO A 591 ? 1.4182 0.8159 0.9659 0.4175  0.1280  0.2279  591 PRO A CA  
4230  C C   . PRO A 591 ? 1.4533 0.8659 0.9708 0.4301  0.1083  0.2538  591 PRO A C   
4231  O O   . PRO A 591 ? 1.4615 0.8467 0.9368 0.4077  0.1111  0.2522  591 PRO A O   
4232  C CB  . PRO A 591 ? 1.3297 0.8019 0.9111 0.3985  0.0957  0.2085  591 PRO A CB  
4233  C CG  . PRO A 591 ? 1.3116 0.7588 0.8679 0.3470  0.1008  0.1800  591 PRO A CG  
4234  C CD  . PRO A 591 ? 1.3596 0.7099 0.8864 0.3379  0.1441  0.1732  591 PRO A CD  
4235  N N   . GLU A 592 ? 1.5422 0.8607 1.0117 0.3794  -0.1141 0.3047  592 GLU A N   
4236  C CA  . GLU A 592 ? 1.5968 0.8860 1.0226 0.3832  -0.1209 0.3138  592 GLU A CA  
4237  C C   . GLU A 592 ? 1.5468 0.8924 0.9978 0.3716  -0.1578 0.3074  592 GLU A C   
4238  O O   . GLU A 592 ? 1.5987 0.9054 0.9941 0.3725  -0.1582 0.3079  592 GLU A O   
4239  C CB  . GLU A 592 ? 1.6205 0.9216 1.0706 0.3981  -0.1293 0.3355  592 GLU A CB  
4240  C CG  . GLU A 592 ? 1.7136 0.9465 1.0909 0.4080  -0.1168 0.3450  592 GLU A CG  
4241  C CD  . GLU A 592 ? 1.7032 0.9846 1.1208 0.4126  -0.1539 0.3621  592 GLU A CD  
4242  O OE1 . GLU A 592 ? 1.6224 0.9906 1.1287 0.4043  -0.1869 0.3681  592 GLU A OE1 
4243  O OE2 . GLU A 592 ? 1.7776 1.0092 1.1399 0.4225  -0.1481 0.3706  592 GLU A OE2 
4244  N N   . GLY A 593 ? 1.4961 0.9317 1.0291 0.3601  -0.1862 0.3008  593 GLY A N   
4245  C CA  . GLY A 593 ? 1.4472 0.9393 1.0079 0.3461  -0.2173 0.2927  593 GLY A CA  
4246  C C   . GLY A 593 ? 1.4789 0.9210 0.9681 0.3385  -0.2079 0.2744  593 GLY A C   
4247  O O   . GLY A 593 ? 1.4688 0.9317 0.9532 0.3313  -0.2283 0.2687  593 GLY A O   
4248  N N   . LEU A 594 ? 1.5076 0.8811 0.9411 0.3380  -0.1741 0.2666  594 LEU A N   
4249  C CA  . LEU A 594 ? 1.5419 0.8637 0.9091 0.3259  -0.1594 0.2537  594 LEU A CA  
4250  C C   . LEU A 594 ? 1.6228 0.8792 0.9123 0.3311  -0.1464 0.2609  594 LEU A C   
4251  O O   . LEU A 594 ? 1.6311 0.8806 0.8878 0.3226  -0.1521 0.2526  594 LEU A O   
4252  C CB  . LEU A 594 ? 1.5667 0.8477 0.9196 0.3050  -0.1124 0.2387  594 LEU A CB  
4253  C CG  . LEU A 594 ? 1.5282 0.8916 0.9557 0.2705  -0.1147 0.2074  594 LEU A CG  
4254  C CD1 . LEU A 594 ? 1.3967 0.8450 0.8991 0.2883  -0.1634 0.2142  594 LEU A CD1 
4255  C CD2 . LEU A 594 ? 1.6022 0.9454 1.0407 0.2424  -0.0676 0.1872  594 LEU A CD2 
4256  N N   . THR A 595 ? 1.6879 0.8975 0.9474 0.3459  -0.1284 0.2761  595 THR A N   
4257  C CA  . THR A 595 ? 1.7761 0.9202 0.9600 0.3530  -0.1128 0.2829  595 THR A CA  
4258  C C   . THR A 595 ? 1.7599 0.9513 0.9604 0.3580  -0.1538 0.2833  595 THR A C   
4259  O O   . THR A 595 ? 1.8333 0.9731 0.9695 0.3656  -0.1447 0.2871  595 THR A O   
4260  C CB  . THR A 595 ? 1.8478 0.9372 1.0025 0.3678  -0.0858 0.2982  595 THR A CB  
4261  O OG1 . THR A 595 ? 1.8179 0.9662 1.0306 0.3813  -0.1204 0.3105  595 THR A OG1 
4262  C CG2 . THR A 595 ? 1.8543 0.9085 1.0095 0.3618  -0.0489 0.2965  595 THR A CG2 
4263  N N   . LYS A 596 ? 1.6871 0.9733 0.9735 0.3522  -0.1952 0.2795  596 LYS A N   
4264  C CA  . LYS A 596 ? 1.6706 1.0023 0.9806 0.3520  -0.2309 0.2800  596 LYS A CA  
4265  C C   . LYS A 596 ? 1.6406 0.9929 0.9422 0.3386  -0.2444 0.2612  596 LYS A C   
4266  O O   . LYS A 596 ? 1.6388 1.0163 0.9477 0.3380  -0.2692 0.2591  596 LYS A O   
4267  C CB  . LYS A 596 ? 1.5911 1.0163 1.0055 0.3483  -0.2612 0.2901  596 LYS A CB  
4268  C CG  . LYS A 596 ? 1.6089 1.0261 1.0452 0.3604  -0.2501 0.3099  596 LYS A CG  
4269  C CD  . LYS A 596 ? 1.5294 1.0425 1.0724 0.3537  -0.2757 0.3243  596 LYS A CD  
4270  C CE  . LYS A 596 ? 1.5305 1.0431 1.1062 0.3627  -0.2622 0.3414  596 LYS A CE  
4271  N NZ  . LYS A 596 ? 1.4501 1.0581 1.1345 0.3538  -0.2810 0.3593  596 LYS A NZ  
4272  N N   . LEU A 597 ? 1.6523 0.9915 0.9367 0.3275  -0.2275 0.2482  597 LEU A N   
4273  C CA  . LEU A 597 ? 1.6306 0.9846 0.9011 0.3150  -0.2371 0.2313  597 LEU A CA  
4274  C C   . LEU A 597 ? 1.7356 0.9964 0.9001 0.3234  -0.2083 0.2346  597 LEU A C   
4275  O O   . LEU A 597 ? 1.7914 0.9808 0.8948 0.3212  -0.1658 0.2388  597 LEU A O   
4276  C CB  . LEU A 597 ? 1.5736 0.9530 0.8694 0.2985  -0.2308 0.2183  597 LEU A CB  
4277  C CG  . LEU A 597 ? 1.4980 0.9396 0.8775 0.2937  -0.2403 0.2173  597 LEU A CG  
4278  C CD1 . LEU A 597 ? 1.4444 0.9156 0.8456 0.2761  -0.2411 0.2002  597 LEU A CD1 
4279  C CD2 . LEU A 597 ? 1.4240 0.9594 0.8967 0.2909  -0.2735 0.2197  597 LEU A CD2 
4280  N N   . SER A 598 ? 1.7122 0.9692 0.8550 0.3321  -0.2261 0.2347  598 SER A N   
4281  C CA  . SER A 598 ? 1.8206 0.9881 0.8643 0.3447  -0.1969 0.2406  598 SER A CA  
4282  C C   . SER A 598 ? 1.8461 0.9733 0.8319 0.3342  -0.1660 0.2322  598 SER A C   
4283  O O   . SER A 598 ? 1.9323 0.9790 0.8409 0.3385  -0.1216 0.2405  598 SER A O   
4284  C CB  . SER A 598 ? 1.8524 1.0256 0.8865 0.3572  -0.2261 0.2414  598 SER A CB  
4285  O OG  . SER A 598 ? 1.7913 1.0255 0.8672 0.3461  -0.2582 0.2261  598 SER A OG  
4286  N N   . GLN A 599 ? 1.8062 0.9910 0.8319 0.3187  -0.1853 0.2171  599 GLN A N   
4287  C CA  . GLN A 599 ? 1.8287 0.9867 0.8032 0.3091  -0.1621 0.2095  599 GLN A CA  
4288  C C   . GLN A 599 ? 1.8234 0.9575 0.7823 0.2883  -0.1209 0.2116  599 GLN A C   
4289  O O   . GLN A 599 ? 1.8449 0.9889 0.7977 0.2682  -0.0958 0.1984  599 GLN A O   
4290  C CB  . GLN A 599 ? 1.7587 0.9906 0.7815 0.3018  -0.2027 0.1913  599 GLN A CB  
4291  C CG  . GLN A 599 ? 1.8129 1.0238 0.7976 0.3169  -0.2168 0.1885  599 GLN A CG  
4292  C CD  . GLN A 599 ? 1.8232 1.0467 0.8354 0.3304  -0.2465 0.1956  599 GLN A CD  
4293  O OE1 . GLN A 599 ? 1.9004 1.0641 0.8628 0.3466  -0.2298 0.2095  599 GLN A OE1 
4294  N NE2 . GLN A 599 ? 1.7455 1.0486 0.8399 0.3215  -0.2870 0.1873  599 GLN A NE2 
4295  N N   . LEU A 600 ? 1.7596 0.9057 0.7672 0.2758  -0.1036 0.2111  600 LEU A N   
4296  C CA  . LEU A 600 ? 1.7965 0.9735 0.8588 0.2332  -0.0557 0.1901  600 LEU A CA  
4297  C C   . LEU A 600 ? 1.9046 1.0125 0.9062 0.2213  0.0046  0.1936  600 LEU A C   
4298  O O   . LEU A 600 ? 1.9620 0.9860 0.8888 0.2432  0.0251  0.2144  600 LEU A O   
4299  C CB  . LEU A 600 ? 1.7947 0.9852 0.9113 0.2219  -0.0432 0.1876  600 LEU A CB  
4300  C CG  . LEU A 600 ? 1.7001 0.9624 0.8955 0.2257  -0.0843 0.1830  600 LEU A CG  
4301  C CD1 . LEU A 600 ? 1.6708 0.8951 0.8278 0.2670  -0.1166 0.2100  600 LEU A CD1 
4302  C CD2 . LEU A 600 ? 1.7309 1.0057 0.9778 0.2010  -0.0523 0.1711  600 LEU A CD2 
4303  N N   . GLN A 601 ? 1.7656 0.9111 0.8029 0.1867  0.0332  0.1746  601 GLN A N   
4304  C CA  . GLN A 601 ? 1.8500 0.9447 0.8543 0.1670  0.0955  0.1771  601 GLN A CA  
4305  C C   . GLN A 601 ? 1.8759 0.9853 0.9420 0.1277  0.1344  0.1640  601 GLN A C   
4306  O O   . GLN A 601 ? 1.9349 0.9785 0.9675 0.1202  0.1816  0.1743  601 GLN A O   
4307  C CB  . GLN A 601 ? 1.8516 0.9722 0.8500 0.1561  0.1045  0.1686  601 GLN A CB  
4308  C CG  . GLN A 601 ? 1.8923 1.0200 0.9230 0.1156  0.1624  0.1595  601 GLN A CG  
4309  C CD  . GLN A 601 ? 1.9139 1.0270 0.9009 0.1188  0.1851  0.1646  601 GLN A CD  
4310  O OE1 . GLN A 601 ? 1.8902 1.0060 0.8360 0.1464  0.1507  0.1674  601 GLN A OE1 
4311  N NE2 . GLN A 601 ? 1.9525 1.0474 0.9473 0.0915  0.2433  0.1671  601 GLN A NE2 
4312  N N   . MET A 602 ? 1.7076 0.8994 0.8615 0.1032  0.1142  0.1420  602 MET A N   
4313  C CA  . MET A 602 ? 1.7240 0.9329 0.9379 0.0657  0.1437  0.1266  602 MET A CA  
4314  C C   . MET A 602 ? 1.6761 0.9288 0.9429 0.0714  0.1077  0.1185  602 MET A C   
4315  O O   . MET A 602 ? 1.6106 0.9241 0.9087 0.0861  0.0599  0.1142  602 MET A O   
4316  C CB  . MET A 602 ? 1.7168 0.9861 0.9900 0.0240  0.1630  0.1055  602 MET A CB  
4317  C CG  . MET A 602 ? 1.7590 0.9823 0.9892 0.0134  0.2108  0.1156  602 MET A CG  
4318  S SD  . MET A 602 ? 1.7236 1.0256 1.0112 -0.0200 0.2197  0.0978  602 MET A SD  
4319  C CE  . MET A 602 ? 1.7007 1.0306 1.0717 -0.0754 0.2538  0.0789  602 MET A CE  
4320  N N   . LEU A 603 ? 1.6453 0.8642 0.9208 0.0610  0.1314  0.1178  603 LEU A N   
4321  C CA  . LEU A 603 ? 1.6038 0.8553 0.9249 0.0678  0.1052  0.1118  603 LEU A CA  
4322  C C   . LEU A 603 ? 1.6275 0.8674 0.9824 0.0325  0.1405  0.0958  603 LEU A C   
4323  O O   . LEU A 603 ? 1.6735 0.8354 0.9853 0.0296  0.1776  0.1055  603 LEU A O   
4324  C CB  . LEU A 603 ? 1.5921 0.7914 0.8627 0.1121  0.0872  0.1375  603 LEU A CB  
4325  C CG  . LEU A 603 ? 1.5503 0.7704 0.8608 0.1234  0.0684  0.1368  603 LEU A CG  
4326  C CD1 . LEU A 603 ? 1.4610 0.7753 0.8364 0.1314  0.0175  0.1287  603 LEU A CD1 
4327  C CD2 . LEU A 603 ? 1.5847 0.7332 0.8363 0.1627  0.0672  0.1651  603 LEU A CD2 
4328  N N   . ASP A 604 ? 1.4502 0.7643 0.8799 0.0061  0.1278  0.0714  604 ASP A N   
4329  C CA  . ASP A 604 ? 1.4491 0.7577 0.9144 -0.0302 0.1553  0.0525  604 ASP A CA  
4330  C C   . ASP A 604 ? 1.4060 0.7499 0.9124 -0.0198 0.1288  0.0436  604 ASP A C   
4331  O O   . ASP A 604 ? 1.3526 0.7790 0.9145 -0.0193 0.0949  0.0317  604 ASP A O   
4332  C CB  . ASP A 604 ? 1.4221 0.7841 0.9385 -0.0743 0.1683  0.0309  604 ASP A CB  
4333  C CG  . ASP A 604 ? 1.4048 0.7463 0.9488 -0.1156 0.2001  0.0139  604 ASP A CG  
4334  O OD1 . ASP A 604 ? 1.4205 0.7107 0.9462 -0.1096 0.2090  0.0154  604 ASP A OD1 
4335  O OD2 . ASP A 604 ? 1.3675 0.7430 0.9515 -0.1539 0.2154  -0.0007 604 ASP A OD2 
4336  N N   . LEU A 605 ? 1.4271 0.7072 0.9053 -0.0100 0.1457  0.0504  605 LEU A N   
4337  C CA  . LEU A 605 ? 1.3922 0.6941 0.9019 0.0023  0.1275  0.0440  605 LEU A CA  
4338  C C   . LEU A 605 ? 1.4124 0.6856 0.9364 -0.0312 0.1555  0.0231  605 LEU A C   
4339  O O   . LEU A 605 ? 1.4208 0.6772 0.9461 -0.0175 0.1525  0.0216  605 LEU A O   
4340  C CB  . LEU A 605 ? 1.4429 0.6966 0.9073 0.0500  0.1177  0.0717  605 LEU A CB  
4341  C CG  . LEU A 605 ? 1.4359 0.7067 0.8803 0.0880  0.0849  0.0957  605 LEU A CG  
4342  C CD1 . LEU A 605 ? 1.4891 0.7105 0.8948 0.1323  0.0775  0.1234  605 LEU A CD1 
4343  C CD2 . LEU A 605 ? 1.3298 0.7025 0.8393 0.0901  0.0414  0.0861  605 LEU A CD2 
4344  N N   . SER A 606 ? 1.5240 0.7900 1.0587 -0.0743 0.1819  0.0080  606 SER A N   
4345  C CA  . SER A 606 ? 1.5254 0.7446 1.0620 -0.1077 0.2106  -0.0082 606 SER A CA  
4346  C C   . SER A 606 ? 1.4543 0.7313 1.0494 -0.1240 0.1911  -0.0349 606 SER A C   
4347  O O   . SER A 606 ? 1.3967 0.7591 1.0399 -0.1170 0.1591  -0.0428 606 SER A O   
4348  C CB  . SER A 606 ? 1.5340 0.7336 1.0727 -0.1499 0.2428  -0.0134 606 SER A CB  
4349  O OG  . SER A 606 ? 1.4720 0.7579 1.0677 -0.1734 0.2283  -0.0279 606 SER A OG  
4350  N N   . TYR A 607 ? 1.5994 0.8241 1.1869 -0.1457 0.2107  -0.0489 607 TYR A N   
4351  C CA  . TYR A 607 ? 1.5310 0.7951 1.1654 -0.1669 0.1974  -0.0769 607 TYR A CA  
4352  C C   . TYR A 607 ? 1.5044 0.8178 1.1570 -0.1276 0.1650  -0.0748 607 TYR A C   
4353  O O   . TYR A 607 ? 1.4313 0.8333 1.1398 -0.1307 0.1379  -0.0873 607 TYR A O   
4354  C CB  . TYR A 607 ? 1.4475 0.7831 1.1433 -0.2116 0.1925  -0.0983 607 TYR A CB  
4355  C CG  . TYR A 607 ? 1.4563 0.7429 1.1468 -0.2571 0.2257  -0.1038 607 TYR A CG  
4356  C CD1 . TYR A 607 ? 1.5187 0.7549 1.1696 -0.2557 0.2528  -0.0816 607 TYR A CD1 
4357  C CD2 . TYR A 607 ? 1.3984 0.6884 1.1248 -0.3011 0.2294  -0.1298 607 TYR A CD2 
4358  C CE1 . TYR A 607 ? 1.5249 0.7180 1.1763 -0.2967 0.2848  -0.0833 607 TYR A CE1 
4359  C CE2 . TYR A 607 ? 1.4021 0.6490 1.1307 -0.3442 0.2581  -0.1323 607 TYR A CE2 
4360  C CZ  . TYR A 607 ? 1.4661 0.6660 1.1593 -0.3417 0.2868  -0.1081 607 TYR A CZ  
4361  O OH  . TYR A 607 ? 1.4963 0.6550 1.1967 -0.3838 0.3171  -0.1072 607 TYR A OH  
4362  N N   . ASN A 608 ? 1.4946 0.7488 1.1002 -0.0892 0.1695  -0.0567 608 ASN A N   
4363  C CA  . ASN A 608 ? 1.4747 0.7664 1.0934 -0.0456 0.1429  -0.0466 608 ASN A CA  
4364  C C   . ASN A 608 ? 1.5120 0.7251 1.0867 -0.0253 0.1592  -0.0431 608 ASN A C   
4365  O O   . ASN A 608 ? 1.5485 0.6846 1.0880 -0.0494 0.1870  -0.0535 608 ASN A O   
4366  C CB  . ASN A 608 ? 1.4896 0.8013 1.0963 -0.0066 0.1256  -0.0161 608 ASN A CB  
4367  C CG  . ASN A 608 ? 1.4324 0.8474 1.0971 -0.0078 0.0921  -0.0198 608 ASN A CG  
4368  O OD1 . ASN A 608 ? 1.3754 0.8527 1.0921 -0.0373 0.0828  -0.0446 608 ASN A OD1 
4369  N ND2 . ASN A 608 ? 1.4377 0.8682 1.0913 0.0233  0.0732  0.0050  608 ASN A ND2 
4370  N N   . GLN A 609 ? 1.5964 0.8295 1.1753 0.0197  0.1416  -0.0275 609 GLN A N   
4371  C CA  . GLN A 609 ? 1.6302 0.7885 1.1620 0.0511  0.1570  -0.0160 609 GLN A CA  
4372  C C   . GLN A 609 ? 1.6485 0.7767 1.1442 0.0979  0.1563  0.0221  609 GLN A C   
4373  O O   . GLN A 609 ? 1.6412 0.7447 1.1189 0.1386  0.1566  0.0399  609 GLN A O   
4374  C CB  . GLN A 609 ? 1.5853 0.7846 1.1493 0.0686  0.1414  -0.0264 609 GLN A CB  
4375  C CG  . GLN A 609 ? 1.5717 0.7684 1.1502 0.0273  0.1473  -0.0640 609 GLN A CG  
4376  C CD  . GLN A 609 ? 1.5109 0.7775 1.1362 0.0418  0.1247  -0.0756 609 GLN A CD  
4377  O OE1 . GLN A 609 ? 1.5022 0.7728 1.1237 0.0883  0.1188  -0.0562 609 GLN A OE1 
4378  N NE2 . GLN A 609 ? 1.4577 0.7812 1.1292 0.0030  0.1128  -0.1055 609 GLN A NE2 
4379  N N   . LEU A 610 ? 1.6215 0.7517 1.1058 0.0940  0.1550  0.0360  610 LEU A N   
4380  C CA  . LEU A 610 ? 1.6490 0.7488 1.0964 0.1364  0.1518  0.0720  610 LEU A CA  
4381  C C   . LEU A 610 ? 1.7598 0.7505 1.1388 0.1525  0.1849  0.0846  610 LEU A C   
4382  O O   . LEU A 610 ? 1.8228 0.7469 1.1694 0.1208  0.2153  0.0683  610 LEU A O   
4383  C CB  . LEU A 610 ? 1.6473 0.7560 1.0840 0.1250  0.1481  0.0806  610 LEU A CB  
4384  C CG  . LEU A 610 ? 1.5876 0.7971 1.0813 0.1171  0.1132  0.0748  610 LEU A CG  
4385  C CD1 . LEU A 610 ? 1.6099 0.8052 1.0720 0.1178  0.1125  0.0899  610 LEU A CD1 
4386  C CD2 . LEU A 610 ? 1.5054 0.7838 1.0432 0.1548  0.0759  0.0892  610 LEU A CD2 
4387  N N   . ASP A 611 ? 1.8926 0.8653 1.2521 0.2019  0.1787  0.1150  611 ASP A N   
4388  C CA  . ASP A 611 ? 1.9425 0.8118 1.2348 0.2234  0.2095  0.1315  611 ASP A CA  
4389  C C   . ASP A 611 ? 1.9264 0.7749 1.1874 0.2641  0.2026  0.1704  611 ASP A C   
4390  O O   . ASP A 611 ? 1.8822 0.7895 1.1686 0.2704  0.1745  0.1816  611 ASP A O   
4391  C CB  . ASP A 611 ? 1.9299 0.7818 1.2221 0.2467  0.2154  0.1294  611 ASP A CB  
4392  C CG  . ASP A 611 ? 1.8437 0.7572 1.1727 0.2963  0.1872  0.1568  611 ASP A CG  
4393  O OD1 . ASP A 611 ? 1.7770 0.7780 1.1584 0.2990  0.1536  0.1628  611 ASP A OD1 
4394  O OD2 . ASP A 611 ? 1.8426 0.7166 1.1494 0.3331  0.1987  0.1735  611 ASP A OD2 
4395  N N   . GLY A 612 ? 2.0060 0.7688 1.2099 0.2919  0.2270  0.1909  612 GLY A N   
4396  C CA  . GLY A 612 ? 2.0301 0.7680 1.2011 0.3302  0.2215  0.2282  612 GLY A CA  
4397  C C   . GLY A 612 ? 2.0925 0.7736 1.2128 0.3103  0.2415  0.2305  612 GLY A C   
4398  O O   . GLY A 612 ? 2.1221 0.7691 1.2278 0.2680  0.2659  0.2066  612 GLY A O   
4399  N N   . GLU A 613 ? 2.1578 0.8596 1.2692 0.3353  0.2269  0.2543  613 GLU A N   
4400  C CA  . GLU A 613 ? 2.2245 0.8737 1.2839 0.3258  0.2464  0.2606  613 GLU A CA  
4401  C C   . GLU A 613 ? 2.1871 0.8722 1.2525 0.3200  0.2223  0.2654  613 GLU A C   
4402  O O   . GLU A 613 ? 2.1116 0.8730 1.2224 0.3352  0.1817  0.2717  613 GLU A O   
4403  C CB  . GLU A 613 ? 2.2738 0.9108 1.3104 0.3570  0.2494  0.2818  613 GLU A CB  
4404  C CG  . GLU A 613 ? 2.3300 0.9187 1.3468 0.3628  0.2785  0.2781  613 GLU A CG  
4405  C CD  . GLU A 613 ? 2.4032 0.9576 1.3820 0.3852  0.2920  0.2964  613 GLU A CD  
4406  O OE1 . GLU A 613 ? 2.3805 0.9849 1.3804 0.4127  0.2642  0.3165  613 GLU A OE1 
4407  O OE2 . GLU A 613 ? 2.4836 0.9622 1.4143 0.3734  0.3294  0.2900  613 GLU A OE2 
4408  N N   . ILE A 614 ? 2.2083 0.8396 1.2285 0.2976  0.2480  0.2621  614 ILE A N   
4409  C CA  . ILE A 614 ? 2.1872 0.8405 1.2002 0.2918  0.2315  0.2664  614 ILE A CA  
4410  C C   . ILE A 614 ? 2.1999 0.8803 1.2021 0.3269  0.2052  0.2884  614 ILE A C   
4411  O O   . ILE A 614 ? 2.2742 0.9065 1.2331 0.3358  0.2266  0.2979  614 ILE A O   
4412  C CB  . ILE A 614 ? 2.2408 0.8352 1.2157 0.2546  0.2712  0.2553  614 ILE A CB  
4413  C CG1 . ILE A 614 ? 2.2518 0.8362 1.2541 0.2124  0.2992  0.2254  614 ILE A CG1 
4414  C CG2 . ILE A 614 ? 2.2075 0.8587 1.1998 0.2395  0.2518  0.2481  614 ILE A CG2 
4415  C CD1 . ILE A 614 ? 2.2907 0.8600 1.2912 0.1660  0.3282  0.2079  614 ILE A CD1 
4416  N N   . SER A 615 ? 2.1837 0.9431 1.2296 0.3448  0.1575  0.2953  615 SER A N   
4417  C CA  . SER A 615 ? 2.1855 0.9787 1.2337 0.3726  0.1270  0.3133  615 SER A CA  
4418  C C   . SER A 615 ? 2.2463 0.9956 1.2353 0.3690  0.1388  0.3170  615 SER A C   
4419  O O   . SER A 615 ? 2.2398 0.9805 1.2118 0.3497  0.1437  0.3080  615 SER A O   
4420  C CB  . SER A 615 ? 2.0905 0.9819 1.2062 0.3831  0.0723  0.3161  615 SER A CB  
4421  O OG  . SER A 615 ? 2.0967 1.0190 1.2175 0.4017  0.0414  0.3309  615 SER A OG  
4422  N N   . SER A 616 ? 2.2946 1.0161 1.2520 0.3885  0.1443  0.3311  616 SER A N   
4423  C CA  . SER A 616 ? 2.3590 1.0385 1.2581 0.3906  0.1551  0.3361  616 SER A CA  
4424  C C   . SER A 616 ? 2.3181 1.0508 1.2294 0.3977  0.1108  0.3379  616 SER A C   
4425  O O   . SER A 616 ? 2.3674 1.0671 1.2284 0.3985  0.1187  0.3394  616 SER A O   
4426  C CB  . SER A 616 ? 2.4344 1.0746 1.3001 0.4120  0.1687  0.3509  616 SER A CB  
4427  O OG  . SER A 616 ? 2.5171 1.0880 1.3157 0.4070  0.2038  0.3520  616 SER A OG  
4428  N N   . GLN A 617 ? 2.2822 1.0966 1.2599 0.4022  0.0654  0.3370  617 GLN A N   
4429  C CA  . GLN A 617 ? 2.2416 1.1104 1.2374 0.4063  0.0206  0.3367  617 GLN A CA  
4430  C C   . GLN A 617 ? 2.2213 1.0863 1.1982 0.3866  0.0249  0.3222  617 GLN A C   
4431  O O   . GLN A 617 ? 2.1935 1.0977 1.1777 0.3888  -0.0095 0.3193  617 GLN A O   
4432  C CB  . GLN A 617 ? 2.1523 1.1154 1.2359 0.4130  -0.0282 0.3408  617 GLN A CB  
4433  C CG  . GLN A 617 ? 2.1677 1.1471 1.2793 0.4320  -0.0398 0.3591  617 GLN A CG  
4434  C CD  . GLN A 617 ? 2.2437 1.1865 1.3071 0.4469  -0.0427 0.3716  617 GLN A CD  
4435  O OE1 . GLN A 617 ? 2.2894 1.1930 1.2946 0.4453  -0.0355 0.3665  617 GLN A OE1 
4436  N NE2 . GLN A 617 ? 2.2594 1.2147 1.3472 0.4620  -0.0526 0.3889  617 GLN A NE2 
4437  N N   . PHE A 618 ? 2.2431 1.0629 1.1990 0.3653  0.0663  0.3128  618 PHE A N   
4438  C CA  . PHE A 618 ? 2.2406 1.0463 1.1717 0.3437  0.0790  0.3020  618 PHE A CA  
4439  C C   . PHE A 618 ? 2.3158 1.0722 1.1791 0.3484  0.0963  0.3068  618 PHE A C   
4440  O O   . PHE A 618 ? 2.3129 1.0688 1.1557 0.3366  0.0986  0.3003  618 PHE A O   
4441  C CB  . PHE A 618 ? 2.2508 1.0144 1.1798 0.3136  0.1245  0.2921  618 PHE A CB  
4442  C CG  . PHE A 618 ? 2.1600 0.9940 1.1628 0.2981  0.1029  0.2759  618 PHE A CG  
4443  C CD1 . PHE A 618 ? 2.1230 0.9816 1.1654 0.3161  0.0846  0.2823  618 PHE A CD1 
4444  C CD2 . PHE A 618 ? 2.1410 1.0364 1.1885 0.2629  0.1011  0.2492  618 PHE A CD2 
4445  C CE1 . PHE A 618 ? 2.0428 0.9840 1.1655 0.2997  0.0651  0.2622  618 PHE A CE1 
4446  C CE2 . PHE A 618 ? 2.0844 1.0634 1.2132 0.2452  0.0803  0.2283  618 PHE A CE2 
4447  C CZ  . PHE A 618 ? 2.0300 1.0312 1.1953 0.2638  0.0623  0.2346  618 PHE A CZ  
4448  N N   . ARG A 619 ? 2.3496 1.0650 1.1773 0.3665  0.1096  0.3183  619 ARG A N   
4449  C CA  . ARG A 619 ? 2.4235 1.0966 1.1881 0.3774  0.1203  0.3239  619 ARG A CA  
4450  C C   . ARG A 619 ? 2.3922 1.1148 1.1628 0.3898  0.0711  0.3215  619 ARG A C   
4451  O O   . ARG A 619 ? 2.4427 1.1342 1.1606 0.3941  0.0801  0.3210  619 ARG A O   
4452  C CB  . ARG A 619 ? 2.4953 1.1274 1.2310 0.3981  0.1337  0.3373  619 ARG A CB  
4453  C CG  . ARG A 619 ? 2.5863 1.1617 1.2505 0.4104  0.1542  0.3438  619 ARG A CG  
4454  C CD  . ARG A 619 ? 2.6326 1.1985 1.2836 0.4378  0.1391  0.3575  619 ARG A CD  
4455  N NE  . ARG A 619 ? 2.7264 1.2323 1.3054 0.4514  0.1618  0.3640  619 ARG A NE  
4456  C CZ  . ARG A 619 ? 2.7636 1.2700 1.3198 0.4757  0.1340  0.3723  619 ARG A CZ  
4457  N NH1 . ARG A 619 ? 2.7139 1.2806 1.3187 0.4864  0.0822  0.3763  619 ARG A NH1 
4458  N NH2 . ARG A 619 ? 2.8537 1.2999 1.3402 0.4882  0.1595  0.3774  619 ARG A NH2 
4459  N N   . SER A 620 ? 2.3330 1.1330 1.1698 0.3946  0.0206  0.3192  620 SER A N   
4460  C CA  . SER A 620 ? 2.2980 1.1508 1.1518 0.4017  -0.0283 0.3147  620 SER A CA  
4461  C C   . SER A 620 ? 2.2689 1.1324 1.1120 0.3857  -0.0283 0.3007  620 SER A C   
4462  O O   . SER A 620 ? 2.2714 1.1518 1.1008 0.3919  -0.0550 0.2956  620 SER A O   
4463  C CB  . SER A 620 ? 2.2125 1.1520 1.1541 0.4051  -0.0779 0.3166  620 SER A CB  
4464  O OG  . SER A 620 ? 2.2390 1.1723 1.1937 0.4197  -0.0779 0.3319  620 SER A OG  
4465  N N   . LEU A 621 ? 2.2240 1.0759 1.0725 0.3642  0.0023  0.2944  621 LEU A N   
4466  C CA  . LEU A 621 ? 2.1925 1.0597 1.0367 0.3464  0.0035  0.2826  621 LEU A CA  
4467  C C   . LEU A 621 ? 2.2777 1.0777 1.0441 0.3458  0.0432  0.2852  621 LEU A C   
4468  O O   . LEU A 621 ? 2.3179 1.0663 1.0554 0.3270  0.0968  0.2873  621 LEU A O   
4469  C CB  . LEU A 621 ? 2.1472 1.0221 1.0247 0.3207  0.0249  0.2766  621 LEU A CB  
4470  C CG  . LEU A 621 ? 2.0660 1.0040 1.0203 0.3225  -0.0080 0.2740  621 LEU A CG  
4471  C CD1 . LEU A 621 ? 2.0385 1.0061 1.0466 0.2861  0.0190  0.2538  621 LEU A CD1 
4472  C CD2 . LEU A 621 ? 1.9841 1.0122 0.9953 0.3313  -0.0699 0.2669  621 LEU A CD2 
4473  N N   . GLN A 622 ? 2.2496 1.0523 0.9868 0.3652  0.0173  0.2847  622 GLN A N   
4474  C CA  . GLN A 622 ? 2.3408 1.0780 1.0014 0.3727  0.0527  0.2889  622 GLN A CA  
4475  C C   . GLN A 622 ? 2.3377 1.0672 0.9781 0.3534  0.0811  0.2821  622 GLN A C   
4476  O O   . GLN A 622 ? 2.4114 1.0834 0.9969 0.3527  0.1275  0.2877  622 GLN A O   
4477  C CB  . GLN A 622 ? 2.3760 1.1170 1.0112 0.3991  0.0145  0.2889  622 GLN A CB  
4478  C CG  . GLN A 622 ? 2.4048 1.1386 1.0459 0.4178  -0.0013 0.2999  622 GLN A CG  
4479  C CD  . GLN A 622 ? 2.4447 1.1787 1.0603 0.4400  -0.0375 0.3003  622 GLN A CD  
4480  O OE1 . GLN A 622 ? 2.4768 1.1941 1.0500 0.4454  -0.0394 0.2930  622 GLN A OE1 
4481  N NE2 . GLN A 622 ? 2.4458 1.1974 1.0877 0.4524  -0.0651 0.3093  622 GLN A NE2 
4482  N N   . ASN A 623 ? 2.2710 1.0599 0.9574 0.3376  0.0560  0.2710  623 ASN A N   
4483  C CA  . ASN A 623 ? 2.2627 1.0528 0.9350 0.3176  0.0817  0.2651  623 ASN A CA  
4484  C C   . ASN A 623 ? 2.2459 1.0450 0.9594 0.2796  0.1224  0.2610  623 ASN A C   
4485  O O   . ASN A 623 ? 2.2484 1.0844 0.9920 0.2515  0.1444  0.2456  623 ASN A O   
4486  C CB  . ASN A 623 ? 2.1938 1.0527 0.8956 0.3213  0.0280  0.2505  623 ASN A CB  
4487  C CG  . ASN A 623 ? 2.2050 1.0802 0.9044 0.3495  -0.0223 0.2473  623 ASN A CG  
4488  O OD1 . ASN A 623 ? 2.2070 1.0864 0.9266 0.3617  -0.0426 0.2533  623 ASN A OD1 
4489  N ND2 . ASN A 623 ? 2.2151 1.0994 0.8923 0.3577  -0.0404 0.2379  623 ASN A ND2 
4490  N N   . LEU A 624 ? 2.1758 0.9734 0.9274 0.2707  0.1315  0.2614  624 LEU A N   
4491  C CA  . LEU A 624 ? 2.1105 0.9535 0.9437 0.2265  0.1610  0.2407  624 LEU A CA  
4492  C C   . LEU A 624 ? 2.1704 0.9664 0.9824 0.2005  0.2272  0.2422  624 LEU A C   
4493  O O   . LEU A 624 ? 2.2635 0.9757 1.0116 0.2143  0.2615  0.2621  624 LEU A O   
4494  C CB  . LEU A 624 ? 2.0974 0.9367 0.9618 0.2296  0.1542  0.2432  624 LEU A CB  
4495  C CG  . LEU A 624 ? 2.0732 0.9620 1.0228 0.1893  0.1711  0.2204  624 LEU A CG  
4496  C CD1 . LEU A 624 ? 2.0165 1.0062 1.0426 0.1693  0.1382  0.1965  624 LEU A CD1 
4497  C CD2 . LEU A 624 ? 2.0542 0.9273 1.0173 0.2031  0.1618  0.2272  624 LEU A CD2 
4498  N N   . GLU A 625 ? 2.1145 0.9656 0.9828 0.1631  0.2450  0.2227  625 GLU A N   
4499  C CA  . GLU A 625 ? 2.1640 0.9834 1.0301 0.1334  0.3065  0.2243  625 GLU A CA  
4500  C C   . GLU A 625 ? 2.1612 1.0050 1.1030 0.0893  0.3319  0.2075  625 GLU A C   
4501  O O   . GLU A 625 ? 2.1997 0.9938 1.1320 0.0689  0.3828  0.2148  625 GLU A O   
4502  C CB  . GLU A 625 ? 2.1558 1.0134 1.0287 0.1220  0.3146  0.2179  625 GLU A CB  
4503  C CG  . GLU A 625 ? 2.1901 0.9840 0.9649 0.1587  0.3239  0.2403  625 GLU A CG  
4504  C CD  . GLU A 625 ? 2.1662 1.0065 0.9451 0.1571  0.3149  0.2322  625 GLU A CD  
4505  O OE1 . GLU A 625 ? 2.1633 1.0392 0.9927 0.1217  0.3501  0.2233  625 GLU A OE1 
4506  O OE2 . GLU A 625 ? 2.1443 0.9838 0.8760 0.1912  0.2721  0.2354  625 GLU A OE2 
4507  N N   . ARG A 626 ? 2.0536 0.9699 1.0687 0.0746  0.2971  0.1859  626 ARG A N   
4508  C CA  . ARG A 626 ? 2.0443 0.9878 1.1310 0.0324  0.3156  0.1666  626 ARG A CA  
4509  C C   . ARG A 626 ? 2.0189 0.9771 1.1320 0.0429  0.2838  0.1597  626 ARG A C   
4510  O O   . ARG A 626 ? 1.9779 0.9804 1.1018 0.0680  0.2359  0.1583  626 ARG A O   
4511  C CB  . ARG A 626 ? 2.0041 1.0349 1.1675 -0.0047 0.3114  0.1430  626 ARG A CB  
4512  C CG  . ARG A 626 ? 2.0191 1.0395 1.1694 -0.0212 0.3508  0.1499  626 ARG A CG  
4513  C CD  . ARG A 626 ? 1.9722 1.0661 1.2095 -0.0691 0.3610  0.1274  626 ARG A CD  
4514  N NE  . ARG A 626 ? 1.9831 1.0461 1.2187 -0.0951 0.4153  0.1379  626 ARG A NE  
4515  C CZ  . ARG A 626 ? 1.9397 1.0572 1.2253 -0.1241 0.4299  0.1301  626 ARG A CZ  
4516  N NH1 . ARG A 626 ? 1.8852 1.0903 1.2243 -0.1317 0.3946  0.1099  626 ARG A NH1 
4517  N NH2 . ARG A 626 ? 1.9455 1.0297 1.2296 -0.1454 0.4819  0.1446  626 ARG A NH2 
4518  N N   . LEU A 627 ? 1.9588 0.8777 1.0824 0.0244  0.3112  0.1566  627 LEU A N   
4519  C CA  . LEU A 627 ? 1.9343 0.8658 1.0875 0.0299  0.2889  0.1481  627 LEU A CA  
4520  C C   . LEU A 627 ? 1.9282 0.8696 1.1367 -0.0160 0.3132  0.1260  627 LEU A C   
4521  O O   . LEU A 627 ? 1.9579 0.8514 1.1555 -0.0428 0.3564  0.1282  627 LEU A O   
4522  C CB  . LEU A 627 ? 1.9623 0.8116 1.0492 0.0666  0.2944  0.1721  627 LEU A CB  
4523  C CG  . LEU A 627 ? 1.9188 0.7902 0.9987 0.1097  0.2461  0.1826  627 LEU A CG  
4524  C CD1 . LEU A 627 ? 1.9947 0.7878 1.0238 0.1383  0.2576  0.2034  627 LEU A CD1 
4525  C CD2 . LEU A 627 ? 1.8587 0.8201 1.0189 0.0983  0.2106  0.1605  627 LEU A CD2 
4526  N N   . ASP A 628 ? 1.7678 0.7697 1.0355 -0.0247 0.2847  0.1056  628 ASP A N   
4527  C CA  . ASP A 628 ? 1.7507 0.7581 1.0663 -0.0649 0.3011  0.0832  628 ASP A CA  
4528  C C   . ASP A 628 ? 1.7223 0.7412 1.0543 -0.0466 0.2749  0.0763  628 ASP A C   
4529  O O   . ASP A 628 ? 1.6436 0.7394 1.0206 -0.0379 0.2372  0.0658  628 ASP A O   
4530  C CB  . ASP A 628 ? 1.6703 0.7578 1.0559 -0.1053 0.2968  0.0596  628 ASP A CB  
4531  C CG  . ASP A 628 ? 1.6733 0.7520 1.1002 -0.1519 0.3198  0.0391  628 ASP A CG  
4532  O OD1 . ASP A 628 ? 1.7352 0.7462 1.1361 -0.1522 0.3364  0.0410  628 ASP A OD1 
4533  O OD2 . ASP A 628 ? 1.6163 0.7543 1.1010 -0.1884 0.3201  0.0212  628 ASP A OD2 
4534  N N   . LEU A 629 ? 1.7594 0.7010 1.0549 -0.0402 0.2965  0.0833  629 LEU A N   
4535  C CA  . LEU A 629 ? 1.7483 0.6874 1.0508 -0.0199 0.2787  0.0797  629 LEU A CA  
4536  C C   . LEU A 629 ? 1.7686 0.6777 1.0900 -0.0546 0.2999  0.0582  629 LEU A C   
4537  O O   . LEU A 629 ? 1.7921 0.6689 1.1003 -0.0377 0.2976  0.0578  629 LEU A O   
4538  C CB  . LEU A 629 ? 1.8221 0.6922 1.0588 0.0266  0.2813  0.1090  629 LEU A CB  
4539  C CG  . LEU A 629 ? 1.8220 0.7037 1.0271 0.0675  0.2572  0.1342  629 LEU A CG  
4540  C CD1 . LEU A 629 ? 1.8528 0.7032 1.0273 0.1142  0.2418  0.1562  629 LEU A CD1 
4541  C CD2 . LEU A 629 ? 1.7201 0.7024 0.9790 0.0657  0.2179  0.1234  629 LEU A CD2 
4542  N N   . SER A 630 ? 1.8569 0.7739 1.2078 -0.1020 0.3199  0.0413  630 SER A N   
4543  C CA  . SER A 630 ? 1.8542 0.7313 1.2178 -0.1388 0.3404  0.0221  630 SER A CA  
4544  C C   . SER A 630 ? 1.7979 0.7287 1.2089 -0.1441 0.3122  -0.0031 630 SER A C   
4545  O O   . SER A 630 ? 1.7514 0.7654 1.2008 -0.1291 0.2790  -0.0083 630 SER A O   
4546  C CB  . SER A 630 ? 1.8421 0.7234 1.2347 -0.1892 0.3653  0.0129  630 SER A CB  
4547  O OG  . SER A 630 ? 1.7751 0.7549 1.2322 -0.2092 0.3429  -0.0039 630 SER A OG  
4548  N N   . HIS A 631 ? 1.8961 0.7750 1.3021 -0.1655 0.3259  -0.0187 631 HIS A N   
4549  C CA  . HIS A 631 ? 1.8456 0.7609 1.2885 -0.1735 0.3040  -0.0445 631 HIS A CA  
4550  C C   . HIS A 631 ? 1.8362 0.7854 1.2751 -0.1226 0.2757  -0.0351 631 HIS A C   
4551  O O   . HIS A 631 ? 1.7781 0.8162 1.2668 -0.1164 0.2452  -0.0446 631 HIS A O   
4552  C CB  . HIS A 631 ? 1.7661 0.7670 1.2809 -0.2156 0.2895  -0.0692 631 HIS A CB  
4553  C CG  . HIS A 631 ? 1.7595 0.7270 1.2878 -0.2687 0.3156  -0.0800 631 HIS A CG  
4554  N ND1 . HIS A 631 ? 1.8126 0.7256 1.3107 -0.2784 0.3478  -0.0603 631 HIS A ND1 
4555  C CD2 . HIS A 631 ? 1.7030 0.6820 1.2729 -0.3148 0.3139  -0.1066 631 HIS A CD2 
4556  C CE1 . HIS A 631 ? 1.7889 0.6844 1.3144 -0.3288 0.3656  -0.0729 631 HIS A CE1 
4557  N NE2 . HIS A 631 ? 1.7209 0.6555 1.2904 -0.3525 0.3440  -0.1014 631 HIS A NE2 
4558  N N   . ASN A 632 ? 1.8456 0.7222 1.2261 -0.0854 0.2874  -0.0140 632 ASN A N   
4559  C CA  . ASN A 632 ? 1.8230 0.7183 1.1959 -0.0344 0.2655  0.0006  632 ASN A CA  
4560  C C   . ASN A 632 ? 1.9166 0.7153 1.2330 -0.0142 0.2865  0.0073  632 ASN A C   
4561  O O   . ASN A 632 ? 1.9882 0.7140 1.2783 -0.0437 0.3125  -0.0051 632 ASN A O   
4562  C CB  . ASN A 632 ? 1.8048 0.7264 1.1657 0.0015  0.2520  0.0301  632 ASN A CB  
4563  C CG  . ASN A 632 ? 1.7195 0.7467 1.1390 -0.0064 0.2214  0.0232  632 ASN A CG  
4564  O OD1 . ASN A 632 ? 1.6676 0.7662 1.1324 0.0065  0.1919  0.0160  632 ASN A OD1 
4565  N ND2 . ASN A 632 ? 1.7330 0.7688 1.1507 -0.0263 0.2296  0.0262  632 ASN A ND2 
4566  N N   . ASN A 633 ? 1.9789 0.7765 1.2781 0.0364  0.2745  0.0280  633 ASN A N   
4567  C CA  . ASN A 633 ? 2.0215 0.7265 1.2616 0.0648  0.2955  0.0409  633 ASN A CA  
4568  C C   . ASN A 633 ? 2.0392 0.7111 1.2365 0.1090  0.2997  0.0789  633 ASN A C   
4569  O O   . ASN A 633 ? 2.0412 0.6765 1.2084 0.1511  0.3024  0.0980  633 ASN A O   
4570  C CB  . ASN A 633 ? 1.9924 0.7155 1.2471 0.0882  0.2818  0.0323  633 ASN A CB  
4571  C CG  . ASN A 633 ? 2.0439 0.6595 1.2355 0.1036  0.3090  0.0345  633 ASN A CG  
4572  O OD1 . ASN A 633 ? 2.1004 0.6291 1.2455 0.0826  0.3376  0.0326  633 ASN A OD1 
4573  N ND2 . ASN A 633 ? 2.0247 0.6449 1.2145 0.1415  0.3009  0.0396  633 ASN A ND2 
4574  N N   . LEU A 634 ? 2.0691 0.7536 1.2623 0.1016  0.3001  0.0910  634 LEU A N   
4575  C CA  . LEU A 634 ? 2.0833 0.7303 1.2304 0.1415  0.3035  0.1264  634 LEU A CA  
4576  C C   . LEU A 634 ? 2.1468 0.6767 1.2241 0.1481  0.3417  0.1373  634 LEU A C   
4577  O O   . LEU A 634 ? 2.1912 0.6655 1.2520 0.1099  0.3695  0.1197  634 LEU A O   
4578  C CB  . LEU A 634 ? 2.0858 0.7611 1.2347 0.1300  0.2985  0.1345  634 LEU A CB  
4579  C CG  . LEU A 634 ? 2.0320 0.8167 1.2458 0.1166  0.2642  0.1214  634 LEU A CG  
4580  C CD1 . LEU A 634 ? 2.0572 0.8477 1.2735 0.0781  0.2780  0.1119  634 LEU A CD1 
4581  C CD2 . LEU A 634 ? 1.9788 0.8140 1.2018 0.1619  0.2280  0.1467  634 LEU A CD2 
4582  N N   . SER A 635 ? 2.2193 0.7117 1.2578 0.1968  0.3422  0.1676  635 SER A N   
4583  C CA  . SER A 635 ? 2.3106 0.7258 1.2968 0.2059  0.3722  0.1755  635 SER A CA  
4584  C C   . SER A 635 ? 2.3460 0.7545 1.3002 0.2339  0.3737  0.2044  635 SER A C   
4585  O O   . SER A 635 ? 2.3068 0.7564 1.2717 0.2435  0.3533  0.2177  635 SER A O   
4586  C CB  . SER A 635 ? 2.3164 0.7313 1.3043 0.2337  0.3688  0.1750  635 SER A CB  
4587  O OG  . SER A 635 ? 2.2592 0.7403 1.2753 0.2779  0.3386  0.1974  635 SER A OG  
4588  N N   . GLY A 636 ? 2.4101 0.7672 1.3238 0.2475  0.3962  0.2130  636 GLY A N   
4589  C CA  . GLY A 636 ? 2.4529 0.7975 1.3337 0.2716  0.4004  0.2371  636 GLY A CA  
4590  C C   . GLY A 636 ? 2.4931 0.8006 1.3477 0.2423  0.4228  0.2350  636 GLY A C   
4591  O O   . GLY A 636 ? 2.4996 0.7841 1.3610 0.1999  0.4406  0.2150  636 GLY A O   
4592  N N   . GLN A 637 ? 2.5542 0.8596 1.3815 0.2655  0.4213  0.2563  637 GLN A N   
4593  C CA  . GLN A 637 ? 2.5994 0.8704 1.3969 0.2462  0.4438  0.2590  637 GLN A CA  
4594  C C   . GLN A 637 ? 2.5423 0.8630 1.3549 0.2473  0.4194  0.2650  637 GLN A C   
4595  O O   . GLN A 637 ? 2.4844 0.8629 1.3195 0.2748  0.3819  0.2750  637 GLN A O   
4596  C CB  . GLN A 637 ? 2.6816 0.9086 1.4310 0.2711  0.4618  0.2772  637 GLN A CB  
4597  C CG  . GLN A 637 ? 2.7384 0.9203 1.4697 0.2787  0.4814  0.2747  637 GLN A CG  
4598  C CD  . GLN A 637 ? 2.8299 0.9558 1.5110 0.2923  0.5082  0.2887  637 GLN A CD  
4599  O OE1 . GLN A 637 ? 2.8497 0.9736 1.5094 0.3007  0.5098  0.3017  637 GLN A OE1 
4600  N NE2 . GLN A 637 ? 2.8896 0.9677 1.5490 0.2958  0.5295  0.2861  637 GLN A NE2 
4601  N N   . ILE A 638 ? 2.5779 0.8784 1.3807 0.2162  0.4405  0.2591  638 ILE A N   
4602  C CA  . ILE A 638 ? 2.5412 0.8787 1.3468 0.2174  0.4230  0.2657  638 ILE A CA  
4603  C C   . ILE A 638 ? 2.5747 0.9119 1.3427 0.2578  0.4104  0.2884  638 ILE A C   
4604  O O   . ILE A 638 ? 2.6534 0.9389 1.3805 0.2639  0.4380  0.2966  638 ILE A O   
4605  C CB  . ILE A 638 ? 2.5615 0.8758 1.3654 0.1751  0.4543  0.2558  638 ILE A CB  
4606  C CG1 . ILE A 638 ? 2.5256 0.8473 1.3753 0.1309  0.4627  0.2307  638 ILE A CG1 
4607  C CG2 . ILE A 638 ? 2.5331 0.8817 1.3312 0.1809  0.4383  0.2645  638 ILE A CG2 
4608  C CD1 . ILE A 638 ? 2.5401 0.8491 1.4023 0.0845  0.4932  0.2202  638 ILE A CD1 
4609  N N   . PRO A 639 ? 2.5825 0.9770 1.3652 0.2850  0.3677  0.2980  639 PRO A N   
4610  C CA  . PRO A 639 ? 2.6140 1.0136 1.3678 0.3223  0.3496  0.3173  639 PRO A CA  
4611  C C   . PRO A 639 ? 2.6795 1.0365 1.3829 0.3188  0.3742  0.3234  639 PRO A C   
4612  O O   . PRO A 639 ? 2.6615 1.0274 1.3630 0.3010  0.3766  0.3183  639 PRO A O   
4613  C CB  . PRO A 639 ? 2.5310 1.0091 1.3230 0.3404  0.2960  0.3211  639 PRO A CB  
4614  C CG  . PRO A 639 ? 2.4679 0.9717 1.2931 0.3104  0.2931  0.3049  639 PRO A CG  
4615  C CD  . PRO A 639 ? 2.4904 0.9510 1.3217 0.2818  0.3311  0.2907  639 PRO A CD  
4616  N N   . PRO A 640 ? 2.6896 1.0000 1.3511 0.3364  0.3943  0.3350  640 PRO A N   
4617  C CA  . PRO A 640 ? 2.7596 1.0251 1.3711 0.3350  0.4221  0.3415  640 PRO A CA  
4618  C C   . PRO A 640 ? 2.7458 1.0418 1.3402 0.3542  0.3919  0.3490  640 PRO A C   
4619  O O   . PRO A 640 ? 2.7998 1.0617 1.3529 0.3532  0.4148  0.3533  640 PRO A O   
4620  C CB  . PRO A 640 ? 2.8402 1.0562 1.4154 0.3555  0.4430  0.3529  640 PRO A CB  
4621  C CG  . PRO A 640 ? 2.8215 1.0401 1.4268 0.3524  0.4435  0.3470  640 PRO A CG  
4622  C CD  . PRO A 640 ? 2.7244 1.0141 1.3819 0.3545  0.4005  0.3412  640 PRO A CD  
4623  N N   . SER A 641 ? 2.7500 1.1091 1.3756 0.3719  0.3414  0.3507  641 SER A N   
4624  C CA  . SER A 641 ? 2.7344 1.1247 1.3467 0.3868  0.3086  0.3546  641 SER A CA  
4625  C C   . SER A 641 ? 2.7075 1.1047 1.3201 0.3616  0.3182  0.3442  641 SER A C   
4626  O O   . SER A 641 ? 2.7117 1.1209 1.3008 0.3725  0.3004  0.3465  641 SER A O   
4627  C CB  . SER A 641 ? 2.6626 1.1255 1.3206 0.4066  0.2500  0.3576  641 SER A CB  
4628  O OG  . SER A 641 ? 2.5785 1.0883 1.2930 0.3891  0.2351  0.3466  641 SER A OG  
4629  N N   . PHE A 642 ? 2.7420 1.1319 1.3813 0.3276  0.3458  0.3326  642 PHE A N   
4630  C CA  . PHE A 642 ? 2.7099 1.1129 1.3591 0.2999  0.3557  0.3231  642 PHE A CA  
4631  C C   . PHE A 642 ? 2.7804 1.1367 1.3831 0.2926  0.3958  0.3277  642 PHE A C   
4632  O O   . PHE A 642 ? 2.7596 1.1306 1.3651 0.2756  0.4020  0.3230  642 PHE A O   
4633  C CB  . PHE A 642 ? 2.6687 1.0762 1.3647 0.2618  0.3752  0.3086  642 PHE A CB  
4634  C CG  . PHE A 642 ? 2.5827 1.0501 1.3302 0.2641  0.3333  0.3012  642 PHE A CG  
4635  C CD1 . PHE A 642 ? 2.5466 1.0597 1.3043 0.2992  0.2841  0.3093  642 PHE A CD1 
4636  C CD2 . PHE A 642 ? 2.5369 1.0184 1.3282 0.2295  0.3427  0.2856  642 PHE A CD2 
4637  C CE1 . PHE A 642 ? 2.4650 1.0389 1.2768 0.3023  0.2459  0.3038  642 PHE A CE1 
4638  C CE2 . PHE A 642 ? 2.4594 0.9952 1.2977 0.2339  0.3052  0.2792  642 PHE A CE2 
4639  C CZ  . PHE A 642 ? 2.4228 1.0061 1.2718 0.2718  0.2571  0.2893  642 PHE A CZ  
4640  N N   . LYS A 643 ? 2.7405 1.0430 1.3023 0.3059  0.4239  0.3375  643 LYS A N   
4641  C CA  . LYS A 643 ? 2.8115 1.0714 1.3283 0.3052  0.4604  0.3442  643 LYS A CA  
4642  C C   . LYS A 643 ? 2.8135 1.0926 1.2967 0.3306  0.4323  0.3489  643 LYS A C   
4643  O O   . LYS A 643 ? 2.8543 1.1108 1.3080 0.3270  0.4597  0.3519  643 LYS A O   
4644  C CB  . LYS A 643 ? 2.9005 1.1010 1.3790 0.3198  0.4907  0.3547  643 LYS A CB  
4645  C CG  . LYS A 643 ? 2.9271 1.1277 1.3743 0.3619  0.4576  0.3655  643 LYS A CG  
4646  C CD  . LYS A 643 ? 3.0132 1.1548 1.4257 0.3735  0.4904  0.3754  643 LYS A CD  
4647  C CE  . LYS A 643 ? 3.0415 1.1849 1.4248 0.4138  0.4583  0.3868  643 LYS A CE  
4648  N NZ  . LYS A 643 ? 3.0573 1.2100 1.4041 0.4361  0.4349  0.3911  643 LYS A NZ  
4649  N N   . ASP A 644 ? 2.8071 1.1289 1.2976 0.3558  0.3780  0.3493  644 ASP A N   
4650  C CA  . ASP A 644 ? 2.8108 1.1518 1.2712 0.3805  0.3439  0.3513  644 ASP A CA  
4651  C C   . ASP A 644 ? 2.7358 1.1291 1.2251 0.3665  0.3187  0.3407  644 ASP A C   
4652  O O   . ASP A 644 ? 2.7221 1.1438 1.1983 0.3863  0.2781  0.3392  644 ASP A O   
4653  C CB  . ASP A 644 ? 2.8067 1.1709 1.2670 0.4127  0.2950  0.3571  644 ASP A CB  
4654  C CG  . ASP A 644 ? 2.8804 1.1962 1.3115 0.4289  0.3169  0.3687  644 ASP A CG  
4655  O OD1 . ASP A 644 ? 2.9529 1.2103 1.3454 0.4237  0.3665  0.3732  644 ASP A OD1 
4656  O OD2 . ASP A 644 ? 2.8655 1.2042 1.3158 0.4464  0.2848  0.3739  644 ASP A OD2 
4657  N N   . MET A 645 ? 2.7406 1.1480 1.2701 0.3317  0.3401  0.3324  645 MET A N   
4658  C CA  . MET A 645 ? 2.6683 1.1264 1.2265 0.3166  0.3184  0.3226  645 MET A CA  
4659  C C   . MET A 645 ? 2.7047 1.1382 1.2374 0.2999  0.3616  0.3230  645 MET A C   
4660  O O   . MET A 645 ? 2.6944 1.1219 1.2554 0.2638  0.4019  0.3191  645 MET A O   
4661  C CB  . MET A 645 ? 2.5908 1.0856 1.2127 0.2897  0.3106  0.3131  645 MET A CB  
4662  C CG  . MET A 645 ? 2.5415 1.0787 1.1948 0.3124  0.2578  0.3132  645 MET A CG  
4663  S SD  . MET A 645 ? 2.4623 1.0381 1.1874 0.2911  0.2465  0.3037  645 MET A SD  
4664  C CE  . MET A 645 ? 2.4606 1.0177 1.2005 0.2409  0.2970  0.2927  645 MET A CE  
4665  N N   . LEU A 646 ? 2.5915 1.0128 1.0738 0.3262  0.3525  0.3274  646 LEU A N   
4666  C CA  . LEU A 646 ? 2.6394 1.0337 1.0914 0.3187  0.3953  0.3306  646 LEU A CA  
4667  C C   . LEU A 646 ? 2.5731 1.0125 1.0604 0.2911  0.3973  0.3216  646 LEU A C   
4668  O O   . LEU A 646 ? 2.5934 1.0208 1.0848 0.2691  0.4444  0.3238  646 LEU A O   
4669  C CB  . LEU A 646 ? 2.7060 1.0752 1.0925 0.3576  0.3804  0.3359  646 LEU A CB  
4670  C CG  . LEU A 646 ? 2.7824 1.1061 1.1232 0.3891  0.3772  0.3454  646 LEU A CG  
4671  C CD1 . LEU A 646 ? 2.7420 1.1002 1.1007 0.4078  0.3172  0.3425  646 LEU A CD1 
4672  C CD2 . LEU A 646 ? 2.8635 1.1490 1.1368 0.4171  0.3869  0.3505  646 LEU A CD2 
4673  N N   . ALA A 647 ? 2.5639 1.0595 1.0813 0.2918  0.3468  0.3121  647 ALA A N   
4674  C CA  . ALA A 647 ? 2.4991 1.0415 1.0507 0.2654  0.3467  0.3031  647 ALA A CA  
4675  C C   . ALA A 647 ? 2.4608 1.0173 1.0725 0.2198  0.3777  0.2981  647 ALA A C   
4676  O O   . ALA A 647 ? 2.4419 1.0469 1.1007 0.1882  0.3912  0.2853  647 ALA A O   
4677  C CB  . ALA A 647 ? 2.4308 1.0311 0.9967 0.2819  0.2795  0.2937  647 ALA A CB  
4678  N N   . LEU A 648 ? 2.4433 0.9774 1.0739 0.2132  0.3850  0.2993  648 LEU A N   
4679  C CA  . LEU A 648 ? 2.4239 0.9895 1.1323 0.1679  0.4056  0.2826  648 LEU A CA  
4680  C C   . LEU A 648 ? 2.4603 0.9983 1.1775 0.1337  0.4681  0.2857  648 LEU A C   
4681  O O   . LEU A 648 ? 2.5134 0.9879 1.1844 0.1449  0.5043  0.3014  648 LEU A O   
4682  C CB  . LEU A 648 ? 2.4257 0.9591 1.1378 0.1745  0.4011  0.2858  648 LEU A CB  
4683  C CG  . LEU A 648 ? 2.4038 0.9791 1.2007 0.1327  0.4079  0.2624  648 LEU A CG  
4684  C CD1 . LEU A 648 ? 2.3419 1.0168 1.2111 0.1243  0.3580  0.2385  648 LEU A CD1 
4685  C CD2 . LEU A 648 ? 2.4222 0.9370 1.1997 0.1423  0.4195  0.2714  648 LEU A CD2 
4686  N N   . THR A 649 ? 2.3745 0.9821 1.1714 0.0913  0.4747  0.2642  649 THR A N   
4687  C CA  . THR A 649 ? 2.3908 0.9845 1.2126 0.0541  0.5305  0.2671  649 THR A CA  
4688  C C   . THR A 649 ? 2.3641 0.9928 1.2737 0.0038  0.5418  0.2457  649 THR A C   
4689  O O   . THR A 649 ? 2.3789 0.9738 1.3036 -0.0262 0.5897  0.2526  649 THR A O   
4690  C CB  . THR A 649 ? 2.3738 1.0123 1.2048 0.0484  0.5371  0.2659  649 THR A CB  
4691  O OG1 . THR A 649 ? 2.3175 1.0518 1.2417 0.0126  0.5145  0.2377  649 THR A OG1 
4692  C CG2 . THR A 649 ? 2.3797 1.0089 1.1374 0.0973  0.5034  0.2761  649 THR A CG2 
4693  N N   . HIS A 650 ? 2.2938 0.9866 1.2607 -0.0060 0.4990  0.2212  650 HIS A N   
4694  C CA  . HIS A 650 ? 2.2623 0.9906 1.3097 -0.0524 0.5044  0.1983  650 HIS A CA  
4695  C C   . HIS A 650 ? 2.2529 0.9822 1.3085 -0.0397 0.4705  0.1873  650 HIS A C   
4696  O O   . HIS A 650 ? 2.2316 1.0003 1.2836 -0.0105 0.4250  0.1835  650 HIS A O   
4697  C CB  . HIS A 650 ? 2.2044 1.0307 1.3312 -0.0846 0.4887  0.1752  650 HIS A CB  
4698  C CG  . HIS A 650 ? 2.2001 1.0335 1.3324 -0.1019 0.5252  0.1852  650 HIS A CG  
4699  N ND1 . HIS A 650 ? 2.2454 1.0267 1.3034 -0.0713 0.5490  0.2119  650 HIS A ND1 
4700  C CD2 . HIS A 650 ? 2.1485 1.0361 1.3525 -0.1451 0.5424  0.1735  650 HIS A CD2 
4701  C CE1 . HIS A 650 ? 2.2262 1.0284 1.3095 -0.0938 0.5817  0.2171  650 HIS A CE1 
4702  N NE2 . HIS A 650 ? 2.1643 1.0328 1.3387 -0.1394 0.5780  0.1947  650 HIS A NE2 
4703  N N   . VAL A 651 ? 2.2527 0.9376 1.3199 -0.0612 0.4928  0.1834  651 VAL A N   
4704  C CA  . VAL A 651 ? 2.2426 0.9230 1.3184 -0.0513 0.4674  0.1730  651 VAL A CA  
4705  C C   . VAL A 651 ? 2.2186 0.9104 1.3568 -0.0990 0.4798  0.1497  651 VAL A C   
4706  O O   . VAL A 651 ? 2.2281 0.8890 1.3793 -0.1342 0.5185  0.1512  651 VAL A O   
4707  C CB  . VAL A 651 ? 2.2898 0.8769 1.2892 -0.0152 0.4805  0.1969  651 VAL A CB  
4708  C CG1 . VAL A 651 ? 2.2668 0.8669 1.2699 0.0111  0.4426  0.1913  651 VAL A CG1 
4709  C CG2 . VAL A 651 ? 2.3190 0.8696 1.2467 0.0226  0.4856  0.2239  651 VAL A CG2 
4710  N N   . ASP A 652 ? 2.1144 0.8487 1.2908 -0.0994 0.4461  0.1294  652 ASP A N   
4711  C CA  . ASP A 652 ? 2.0931 0.8232 1.3138 -0.1369 0.4531  0.1073  652 ASP A CA  
4712  C C   . ASP A 652 ? 2.0925 0.8072 1.2985 -0.1090 0.4287  0.1032  652 ASP A C   
4713  O O   . ASP A 652 ? 2.0626 0.8355 1.2828 -0.0819 0.3898  0.0998  652 ASP A O   
4714  C CB  . ASP A 652 ? 2.0273 0.8475 1.3298 -0.1769 0.4376  0.0803  652 ASP A CB  
4715  C CG  . ASP A 652 ? 2.0022 0.8053 1.3459 -0.2240 0.4529  0.0599  652 ASP A CG  
4716  O OD1 . ASP A 652 ? 2.0334 0.7666 1.3467 -0.2202 0.4630  0.0604  652 ASP A OD1 
4717  O OD2 . ASP A 652 ? 1.9471 0.8052 1.3530 -0.2646 0.4537  0.0436  652 ASP A OD2 
4718  N N   . VAL A 653 ? 2.0921 0.7274 1.2702 -0.1148 0.4524  0.1051  653 VAL A N   
4719  C CA  . VAL A 653 ? 2.1112 0.7141 1.2634 -0.0843 0.4378  0.1062  653 VAL A CA  
4720  C C   . VAL A 653 ? 2.1270 0.7026 1.3043 -0.1194 0.4478  0.0827  653 VAL A C   
4721  O O   . VAL A 653 ? 2.1526 0.6917 1.3092 -0.1008 0.4419  0.0801  653 VAL A O   
4722  C CB  . VAL A 653 ? 2.2070 0.7228 1.2796 -0.0450 0.4576  0.1376  653 VAL A CB  
4723  C CG1 . VAL A 653 ? 2.2265 0.7121 1.2727 -0.0092 0.4433  0.1429  653 VAL A CG1 
4724  C CG2 . VAL A 653 ? 2.1950 0.7365 1.2414 -0.0136 0.4452  0.1586  653 VAL A CG2 
4725  N N   . SER A 654 ? 2.1671 0.7623 1.3903 -0.1700 0.4611  0.0656  654 SER A N   
4726  C CA  . SER A 654 ? 2.1581 0.7201 1.4037 -0.2096 0.4710  0.0434  654 SER A CA  
4727  C C   . SER A 654 ? 2.1210 0.7187 1.3897 -0.2006 0.4379  0.0205  654 SER A C   
4728  O O   . SER A 654 ? 2.0826 0.7578 1.3764 -0.1771 0.4054  0.0169  654 SER A O   
4729  C CB  . SER A 654 ? 2.1177 0.7176 1.4230 -0.2650 0.4820  0.0293  654 SER A CB  
4730  O OG  . SER A 654 ? 2.0508 0.7578 1.4147 -0.2715 0.4517  0.0142  654 SER A OG  
4731  N N   . HIS A 655 ? 2.1701 0.7066 1.4281 -0.2189 0.4470  0.0057  655 HIS A N   
4732  C CA  . HIS A 655 ? 2.1382 0.6958 1.4138 -0.2148 0.4208  -0.0182 655 HIS A CA  
4733  C C   . HIS A 655 ? 2.1439 0.7176 1.3922 -0.1559 0.4001  -0.0043 655 HIS A C   
4734  O O   . HIS A 655 ? 2.0938 0.7517 1.3810 -0.1408 0.3683  -0.0124 655 HIS A O   
4735  C CB  . HIS A 655 ? 2.0586 0.7114 1.4105 -0.2509 0.3963  -0.0457 655 HIS A CB  
4736  C CG  . HIS A 655 ? 2.0395 0.6764 1.4250 -0.3105 0.4131  -0.0608 655 HIS A CG  
4737  N ND1 . HIS A 655 ? 2.0496 0.6941 1.4493 -0.3315 0.4353  -0.0456 655 HIS A ND1 
4738  C CD2 . HIS A 655 ? 2.0163 0.6732 1.4395 -0.3422 0.3995  -0.0865 655 HIS A CD2 
4739  C CE1 . HIS A 655 ? 2.0358 0.7065 1.4847 -0.3736 0.4348  -0.0604 655 HIS A CE1 
4740  N NE2 . HIS A 655 ? 2.0233 0.7016 1.4867 -0.3811 0.4114  -0.0853 655 HIS A NE2 
4741  N N   . ASN A 656 ? 2.1847 0.6762 1.3677 -0.1225 0.4192  0.0190  656 ASN A N   
4742  C CA  . ASN A 656 ? 2.1879 0.6832 1.3421 -0.0653 0.4034  0.0377  656 ASN A CA  
4743  C C   . ASN A 656 ? 2.2429 0.6301 1.3326 -0.0450 0.4266  0.0470  656 ASN A C   
4744  O O   . ASN A 656 ? 2.3002 0.6377 1.3809 -0.0760 0.4448  0.0326  656 ASN A O   
4745  C CB  . ASN A 656 ? 2.1890 0.7150 1.3313 -0.0353 0.3976  0.0658  656 ASN A CB  
4746  C CG  . ASN A 656 ? 2.1293 0.7669 1.3249 -0.0218 0.3583  0.0618  656 ASN A CG  
4747  O OD1 . ASN A 656 ? 2.1037 0.7713 1.3042 0.0160  0.3342  0.0688  656 ASN A OD1 
4748  N ND2 . ASN A 656 ? 2.1042 0.8039 1.3419 -0.0523 0.3524  0.0518  656 ASN A ND2 
4749  N N   . ASN A 657 ? 2.3043 0.6776 1.3591 0.0087  0.4203  0.0711  657 ASN A N   
4750  C CA  . ASN A 657 ? 2.3757 0.6833 1.3816 0.0360  0.4349  0.0805  657 ASN A CA  
4751  C C   . ASN A 657 ? 2.4273 0.7058 1.3883 0.0703  0.4484  0.1133  657 ASN A C   
4752  O O   . ASN A 657 ? 2.4596 0.7191 1.3905 0.1110  0.4485  0.1294  657 ASN A O   
4753  C CB  . ASN A 657 ? 2.3444 0.6728 1.3566 0.0712  0.4143  0.0779  657 ASN A CB  
4754  C CG  . ASN A 657 ? 2.4189 0.6911 1.3903 0.0888  0.4289  0.0783  657 ASN A CG  
4755  O OD1 . ASN A 657 ? 2.4697 0.6988 1.4303 0.0556  0.4435  0.0581  657 ASN A OD1 
4756  N ND2 . ASN A 657 ? 2.4264 0.7021 1.3771 0.1410  0.4237  0.1025  657 ASN A ND2 
4757  N N   . LEU A 658 ? 2.4322 0.7104 1.3893 0.0549  0.4600  0.1235  658 LEU A N   
4758  C CA  . LEU A 658 ? 2.4765 0.7336 1.3917 0.0883  0.4695  0.1533  658 LEU A CA  
4759  C C   . LEU A 658 ? 2.5707 0.7589 1.4474 0.0767  0.5033  0.1556  658 LEU A C   
4760  O O   . LEU A 658 ? 2.6021 0.7598 1.4867 0.0401  0.5183  0.1351  658 LEU A O   
4761  C CB  . LEU A 658 ? 2.4410 0.7330 1.3648 0.0851  0.4631  0.1654  658 LEU A CB  
4762  C CG  . LEU A 658 ? 2.3501 0.7097 1.3124 0.0966  0.4274  0.1634  658 LEU A CG  
4763  C CD1 . LEU A 658 ? 2.3141 0.7321 1.3180 0.0597  0.4222  0.1497  658 LEU A CD1 
4764  C CD2 . LEU A 658 ? 2.3318 0.7211 1.2784 0.1501  0.4020  0.1916  658 LEU A CD2 
4765  N N   . GLN A 659 ? 2.5824 0.7483 1.4185 0.1088  0.5129  0.1809  659 GLN A N   
4766  C CA  . GLN A 659 ? 2.6777 0.7778 1.4730 0.1064  0.5444  0.1872  659 GLN A CA  
4767  C C   . GLN A 659 ? 2.7083 0.8023 1.4696 0.1348  0.5513  0.2138  659 GLN A C   
4768  O O   . GLN A 659 ? 2.6634 0.8007 1.4265 0.1663  0.5270  0.2287  659 GLN A O   
4769  C CB  . GLN A 659 ? 2.7236 0.7879 1.4943 0.1286  0.5474  0.1858  659 GLN A CB  
4770  C CG  . GLN A 659 ? 2.7086 0.7976 1.4644 0.1833  0.5286  0.2076  659 GLN A CG  
4771  C CD  . GLN A 659 ? 2.7357 0.8037 1.4786 0.2039  0.5285  0.2039  659 GLN A CD  
4772  O OE1 . GLN A 659 ? 2.7645 0.7978 1.5063 0.1779  0.5395  0.1830  659 GLN A OE1 
4773  N NE2 . GLN A 659 ? 2.7276 0.8190 1.4623 0.2507  0.5147  0.2242  659 GLN A NE2 
4774  N N   . GLY A 660 ? 2.7805 0.8212 1.5118 0.1235  0.5831  0.2193  660 GLY A N   
4775  C CA  . GLY A 660 ? 2.8240 0.8494 1.5166 0.1517  0.5931  0.2432  660 GLY A CA  
4776  C C   . GLY A 660 ? 2.8277 0.8563 1.5240 0.1285  0.6090  0.2469  660 GLY A C   
4777  O O   . GLY A 660 ? 2.7806 0.8370 1.5163 0.0925  0.6073  0.2326  660 GLY A O   
4778  N N   . PRO A 661 ? 2.8852 0.8867 1.5409 0.1499  0.6253  0.2664  661 PRO A N   
4779  C CA  . PRO A 661 ? 2.8972 0.8989 1.5513 0.1331  0.6437  0.2726  661 PRO A CA  
4780  C C   . PRO A 661 ? 2.8270 0.8861 1.4928 0.1450  0.6164  0.2775  661 PRO A C   
4781  O O   . PRO A 661 ? 2.7891 0.8808 1.4487 0.1795  0.5836  0.2849  661 PRO A O   
4782  C CB  . PRO A 661 ? 2.9854 0.9374 1.5864 0.1598  0.6672  0.2922  661 PRO A CB  
4783  C CG  . PRO A 661 ? 2.9896 0.9424 1.5666 0.2021  0.6457  0.3008  661 PRO A CG  
4784  C CD  . PRO A 661 ? 2.9478 0.9146 1.5572 0.1896  0.6306  0.2833  661 PRO A CD  
4785  N N   . ILE A 662 ? 2.8563 0.9300 1.5421 0.1158  0.6297  0.2741  662 ILE A N   
4786  C CA  . ILE A 662 ? 2.7945 0.9194 1.4901 0.1224  0.6073  0.2777  662 ILE A CA  
4787  C C   . ILE A 662 ? 2.8365 0.9505 1.4810 0.1599  0.6077  0.2991  662 ILE A C   
4788  O O   . ILE A 662 ? 2.9076 0.9800 1.5245 0.1583  0.6413  0.3086  662 ILE A O   
4789  C CB  . ILE A 662 ? 2.7586 0.9078 1.4992 0.0755  0.6221  0.2651  662 ILE A CB  
4790  C CG1 . ILE A 662 ? 2.8300 0.9393 1.5627 0.0545  0.6658  0.2715  662 ILE A CG1 
4791  C CG2 . ILE A 662 ? 2.7050 0.8759 1.4994 0.0401  0.6119  0.2411  662 ILE A CG2 
4792  C CD1 . ILE A 662 ? 2.7962 0.9368 1.5782 0.0107  0.6811  0.2628  662 ILE A CD1 
4793  N N   . PRO A 663 ? 2.8465 0.9956 1.4773 0.1955  0.5697  0.3072  663 PRO A N   
4794  C CA  . PRO A 663 ? 2.8711 1.0222 1.4612 0.2234  0.5640  0.3226  663 PRO A CA  
4795  C C   . PRO A 663 ? 2.8766 1.0285 1.4703 0.1981  0.5898  0.3219  663 PRO A C   
4796  O O   . PRO A 663 ? 2.8241 1.0046 1.4633 0.1620  0.5935  0.3089  663 PRO A O   
4797  C CB  . PRO A 663 ? 2.8015 1.0092 1.4016 0.2507  0.5108  0.3241  663 PRO A CB  
4798  C CG  . PRO A 663 ? 2.7324 0.9712 1.3858 0.2304  0.4950  0.3086  663 PRO A CG  
4799  C CD  . PRO A 663 ? 2.7866 0.9753 1.4378 0.2156  0.5283  0.3040  663 PRO A CD  
4800  N N   . ASP A 664 ? 2.8966 1.0184 1.4439 0.2177  0.6085  0.3362  664 ASP A N   
4801  C CA  . ASP A 664 ? 2.9229 1.0351 1.4691 0.1976  0.6430  0.3393  664 ASP A CA  
4802  C C   . ASP A 664 ? 2.8900 1.0388 1.4203 0.2149  0.6195  0.3430  664 ASP A C   
4803  O O   . ASP A 664 ? 2.9231 1.0626 1.4035 0.2543  0.6019  0.3538  664 ASP A O   
4804  C CB  . ASP A 664 ? 3.0229 1.0749 1.5264 0.2101  0.6817  0.3531  664 ASP A CB  
4805  C CG  . ASP A 664 ? 3.0597 1.1025 1.5487 0.2060  0.7125  0.3622  664 ASP A CG  
4806  O OD1 . ASP A 664 ? 3.0178 1.0912 1.5500 0.1730  0.7236  0.3552  664 ASP A OD1 
4807  O OD2 . ASP A 664 ? 3.1324 1.1382 1.5676 0.2368  0.7261  0.3766  664 ASP A OD2 
4808  N N   . ASN A 665 ? 2.9031 1.0938 1.4761 0.1849  0.6177  0.3330  665 ASN A N   
4809  C CA  . ASN A 665 ? 2.8778 1.1004 1.4364 0.1968  0.6021  0.3360  665 ASN A CA  
4810  C C   . ASN A 665 ? 2.8583 1.0995 1.4582 0.1562  0.6355  0.3312  665 ASN A C   
4811  O O   . ASN A 665 ? 2.8586 1.0930 1.5035 0.1178  0.6648  0.3244  665 ASN A O   
4812  C CB  . ASN A 665 ? 2.7992 1.0734 1.3695 0.2113  0.5465  0.3289  665 ASN A CB  
4813  C CG  . ASN A 665 ? 2.7210 1.0319 1.3559 0.1759  0.5362  0.3131  665 ASN A CG  
4814  O OD1 . ASN A 665 ? 2.7033 1.0225 1.3812 0.1339  0.5651  0.3042  665 ASN A OD1 
4815  N ND2 . ASN A 665 ? 2.6746 1.0115 1.3209 0.1929  0.4935  0.3092  665 ASN A ND2 
4816  N N   . ALA A 666 ? 2.8545 1.1218 1.4411 0.1650  0.6294  0.3343  666 ALA A N   
4817  C CA  . ALA A 666 ? 2.8318 1.1258 1.4619 0.1288  0.6601  0.3312  666 ALA A CA  
4818  C C   . ALA A 666 ? 2.7478 1.0881 1.4534 0.0828  0.6526  0.3134  666 ALA A C   
4819  O O   . ALA A 666 ? 2.7389 1.0918 1.4990 0.0412  0.6845  0.3080  666 ALA A O   
4820  C CB  . ALA A 666 ? 2.8247 1.1423 1.4245 0.1505  0.6491  0.3363  666 ALA A CB  
4821  N N   . ALA A 667 ? 2.6931 1.0612 1.4078 0.0889  0.6094  0.3036  667 ALA A N   
4822  C CA  . ALA A 667 ? 2.6174 1.0303 1.4032 0.0453  0.6027  0.2854  667 ALA A CA  
4823  C C   . ALA A 667 ? 2.6349 1.0226 1.4597 0.0129  0.6257  0.2757  667 ALA A C   
4824  O O   . ALA A 667 ? 2.6032 1.0174 1.4918 -0.0337 0.6436  0.2626  667 ALA A O   
4825  C CB  . ALA A 667 ? 2.5651 1.0128 1.3520 0.0620  0.5510  0.2785  667 ALA A CB  
4826  N N   . PHE A 668 ? 2.6527 0.9916 1.4414 0.0369  0.6242  0.2813  668 PHE A N   
4827  C CA  . PHE A 668 ? 2.6739 0.9852 1.4925 0.0099  0.6418  0.2712  668 PHE A CA  
4828  C C   . PHE A 668 ? 2.7275 1.0153 1.5649 -0.0185 0.6880  0.2752  668 PHE A C   
4829  O O   . PHE A 668 ? 2.7177 1.0102 1.6093 -0.0604 0.7011  0.2611  668 PHE A O   
4830  C CB  . PHE A 668 ? 2.7185 0.9858 1.4907 0.0465  0.6288  0.2778  668 PHE A CB  
4831  C CG  . PHE A 668 ? 2.6598 0.9538 1.4412 0.0614  0.5856  0.2691  668 PHE A CG  
4832  C CD1 . PHE A 668 ? 2.6091 0.9240 1.4442 0.0287  0.5774  0.2486  668 PHE A CD1 
4833  C CD2 . PHE A 668 ? 2.6564 0.9574 1.3964 0.1089  0.5513  0.2810  668 PHE A CD2 
4834  C CE1 . PHE A 668 ? 2.5572 0.8968 1.4022 0.0454  0.5392  0.2419  668 PHE A CE1 
4835  C CE2 . PHE A 668 ? 2.6010 0.9325 1.3572 0.1243  0.5108  0.2753  668 PHE A CE2 
4836  C CZ  . PHE A 668 ? 2.5520 0.9014 1.3597 0.0938  0.5064  0.2566  668 PHE A CZ  
4837  N N   . ARG A 669 ? 2.7079 0.9707 1.5023 0.0050  0.7109  0.2944  669 ARG A N   
4838  C CA  . ARG A 669 ? 2.7674 1.0050 1.5781 -0.0163 0.7553  0.3023  669 ARG A CA  
4839  C C   . ARG A 669 ? 2.7168 1.0062 1.6046 -0.0648 0.7689  0.2925  669 ARG A C   
4840  O O   . ARG A 669 ? 2.7334 1.0179 1.6703 -0.1018 0.7904  0.2871  669 ARG A O   
4841  C CB  . ARG A 669 ? 2.8386 1.0433 1.5868 0.0225  0.7753  0.3249  669 ARG A CB  
4842  C CG  . ARG A 669 ? 2.9027 1.0532 1.5806 0.0666  0.7679  0.3352  669 ARG A CG  
4843  C CD  . ARG A 669 ? 2.9852 1.0975 1.6078 0.0983  0.7950  0.3559  669 ARG A CD  
4844  N NE  . ARG A 669 ? 3.0011 1.1028 1.5552 0.1491  0.7658  0.3634  669 ARG A NE  
4845  C CZ  . ARG A 669 ? 3.0113 1.1220 1.5286 0.1754  0.7609  0.3717  669 ARG A CZ  
4846  N NH1 . ARG A 669 ? 3.0071 1.1378 1.5473 0.1587  0.7862  0.3753  669 ARG A NH1 
4847  N NH2 . ARG A 669 ? 3.0273 1.1283 1.4854 0.2200  0.7283  0.3762  669 ARG A NH2 
4848  N N   . ASN A 670 ? 2.7390 1.0811 1.6407 -0.0651 0.7544  0.2900  670 ASN A N   
4849  C CA  . ASN A 670 ? 2.6838 1.0852 1.6618 -0.1086 0.7647  0.2810  670 ASN A CA  
4850  C C   . ASN A 670 ? 2.6035 1.0498 1.6480 -0.1482 0.7392  0.2548  670 ASN A C   
4851  O O   . ASN A 670 ? 2.5483 1.0530 1.6632 -0.1859 0.7418  0.2442  670 ASN A O   
4852  C CB  . ASN A 670 ? 2.6567 1.0953 1.6178 -0.0896 0.7617  0.2899  670 ASN A CB  
4853  C CG  . ASN A 670 ? 2.7365 1.1267 1.6166 -0.0406 0.7766  0.3128  670 ASN A CG  
4854  O OD1 . ASN A 670 ? 2.7780 1.1220 1.5943 -0.0041 0.7626  0.3186  670 ASN A OD1 
4855  N ND2 . ASN A 670 ? 2.7585 1.1618 1.6421 -0.0380 0.8036  0.3256  670 ASN A ND2 
4856  N N   . ALA A 671 ? 2.5418 0.9648 1.5681 -0.1395 0.7144  0.2440  671 ALA A N   
4857  C CA  . ALA A 671 ? 2.4690 0.9312 1.5540 -0.1736 0.6893  0.2179  671 ALA A CA  
4858  C C   . ALA A 671 ? 2.4802 0.9473 1.6312 -0.2215 0.7062  0.2048  671 ALA A C   
4859  O O   . ALA A 671 ? 2.5563 0.9706 1.6897 -0.2205 0.7287  0.2137  671 ALA A O   
4860  C CB  . ALA A 671 ? 2.4681 0.8993 1.5144 -0.1474 0.6606  0.2118  671 ALA A CB  
4861  N N   . PRO A 672 ? 2.3958 0.9272 1.6237 -0.2633 0.6930  0.1838  672 PRO A N   
4862  C CA  . PRO A 672 ? 2.4018 0.9430 1.6955 -0.3085 0.7003  0.1703  672 PRO A CA  
4863  C C   . PRO A 672 ? 2.4199 0.9220 1.7041 -0.3130 0.6828  0.1528  672 PRO A C   
4864  O O   . PRO A 672 ? 2.4132 0.8929 1.6509 -0.2834 0.6633  0.1494  672 PRO A O   
4865  C CB  . PRO A 672 ? 2.3096 0.9410 1.6852 -0.3449 0.6838  0.1526  672 PRO A CB  
4866  C CG  . PRO A 672 ? 2.2518 0.9157 1.6036 -0.3216 0.6625  0.1501  672 PRO A CG  
4867  C CD  . PRO A 672 ? 2.3078 0.9073 1.5652 -0.2696 0.6665  0.1709  672 PRO A CD  
4868  N N   . PRO A 673 ? 2.4041 0.8957 1.7299 -0.3471 0.6878  0.1429  673 PRO A N   
4869  C CA  . PRO A 673 ? 2.4261 0.8785 1.7395 -0.3506 0.6704  0.1249  673 PRO A CA  
4870  C C   . PRO A 673 ? 2.3452 0.8406 1.6810 -0.3564 0.6327  0.0980  673 PRO A C   
4871  O O   . PRO A 673 ? 2.3623 0.8201 1.6668 -0.3425 0.6176  0.0870  673 PRO A O   
4872  C CB  . PRO A 673 ? 2.4660 0.9124 1.8313 -0.3920 0.6795  0.1197  673 PRO A CB  
4873  C CG  . PRO A 673 ? 2.5009 0.9502 1.8765 -0.3941 0.7127  0.1456  673 PRO A CG  
4874  C CD  . PRO A 673 ? 2.4358 0.9392 1.8119 -0.3781 0.7114  0.1524  673 PRO A CD  
4875  N N   . ASP A 674 ? 2.3742 0.9485 1.7639 -0.3751 0.6174  0.0873  674 ASP A N   
4876  C CA  . ASP A 674 ? 2.2982 0.9172 1.7105 -0.3790 0.5815  0.0618  674 ASP A CA  
4877  C C   . ASP A 674 ? 2.3010 0.8895 1.6472 -0.3332 0.5705  0.0695  674 ASP A C   
4878  O O   . ASP A 674 ? 2.2760 0.8675 1.6203 -0.3263 0.5441  0.0515  674 ASP A O   
4879  C CB  . ASP A 674 ? 2.2088 0.9225 1.6910 -0.4050 0.5686  0.0512  674 ASP A CB  
4880  C CG  . ASP A 674 ? 2.2130 0.9593 1.7540 -0.4387 0.5857  0.0572  674 ASP A CG  
4881  O OD1 . ASP A 674 ? 2.2523 0.9799 1.8197 -0.4635 0.5856  0.0502  674 ASP A OD1 
4882  O OD2 . ASP A 674 ? 2.1832 0.9736 1.7440 -0.4389 0.5981  0.0703  674 ASP A OD2 
4883  N N   . ALA A 675 ? 2.2617 0.8215 1.5533 -0.2987 0.5882  0.0972  675 ALA A N   
4884  C CA  . ALA A 675 ? 2.2529 0.7930 1.4858 -0.2521 0.5722  0.1087  675 ALA A CA  
4885  C C   . ALA A 675 ? 2.3101 0.7840 1.4899 -0.2209 0.5673  0.1117  675 ALA A C   
4886  O O   . ALA A 675 ? 2.2994 0.7699 1.4388 -0.1771 0.5475  0.1213  675 ALA A O   
4887  C CB  . ALA A 675 ? 2.2782 0.8089 1.4653 -0.2218 0.5886  0.1380  675 ALA A CB  
4888  N N   . PHE A 676 ? 2.3116 0.7462 1.4957 -0.2384 0.5800  0.1035  676 PHE A N   
4889  C CA  . PHE A 676 ? 2.3668 0.7408 1.5021 -0.2097 0.5766  0.1052  676 PHE A CA  
4890  C C   . PHE A 676 ? 2.3684 0.7372 1.5352 -0.2382 0.5652  0.0778  676 PHE A C   
4891  O O   . PHE A 676 ? 2.4267 0.7402 1.5549 -0.2199 0.5676  0.0784  676 PHE A O   
4892  C CB  . PHE A 676 ? 2.4625 0.7718 1.5452 -0.1892 0.6075  0.1296  676 PHE A CB  
4893  C CG  . PHE A 676 ? 2.4725 0.7824 1.5172 -0.1580 0.6183  0.1565  676 PHE A CG  
4894  C CD1 . PHE A 676 ? 2.4768 0.7720 1.4668 -0.1070 0.6030  0.1726  676 PHE A CD1 
4895  C CD2 . PHE A 676 ? 2.4800 0.8073 1.5441 -0.1774 0.6419  0.1663  676 PHE A CD2 
4896  C CE1 . PHE A 676 ? 2.4907 0.7863 1.4422 -0.0768 0.6084  0.1961  676 PHE A CE1 
4897  C CE2 . PHE A 676 ? 2.4956 0.8203 1.5184 -0.1459 0.6514  0.1902  676 PHE A CE2 
4898  C CZ  . PHE A 676 ? 2.5023 0.8098 1.4665 -0.0959 0.6332  0.2041  676 PHE A CZ  
4899  N N   . GLU A 677 ? 2.3331 0.7600 1.5672 -0.2803 0.5513  0.0541  677 GLU A N   
4900  C CA  . GLU A 677 ? 2.3369 0.7618 1.6020 -0.3094 0.5381  0.0278  677 GLU A CA  
4901  C C   . GLU A 677 ? 2.3236 0.7347 1.5628 -0.2825 0.5139  0.0145  677 GLU A C   
4902  O O   . GLU A 677 ? 2.2760 0.7120 1.5046 -0.2541 0.4977  0.0178  677 GLU A O   
4903  C CB  . GLU A 677 ? 2.2657 0.7687 1.6121 -0.3564 0.5235  0.0067  677 GLU A CB  
4904  C CG  . GLU A 677 ? 2.2977 0.8055 1.6824 -0.3921 0.5442  0.0136  677 GLU A CG  
4905  C CD  . GLU A 677 ? 2.2608 0.8206 1.7189 -0.4370 0.5225  -0.0115 677 GLU A CD  
4906  O OE1 . GLU A 677 ? 2.1765 0.8040 1.6744 -0.4456 0.4949  -0.0312 677 GLU A OE1 
4907  O OE2 . GLU A 677 ? 2.3174 0.8514 1.7940 -0.4625 0.5309  -0.0107 677 GLU A OE2 
4908  N N   . GLY A 678 ? 2.3497 0.7200 1.5789 -0.2903 0.5109  0.0006  678 GLY A N   
4909  C CA  . GLY A 678 ? 2.3351 0.6989 1.5490 -0.2703 0.4875  -0.0159 678 GLY A CA  
4910  C C   . GLY A 678 ? 2.3494 0.6804 1.5043 -0.2135 0.4874  0.0033  678 GLY A C   
4911  O O   . GLY A 678 ? 2.3013 0.6562 1.4578 -0.1914 0.4647  -0.0054 678 GLY A O   
4912  N N   . ASN A 679 ? 2.4131 0.6947 1.5190 -0.1873 0.5107  0.0306  679 ASN A N   
4913  C CA  . ASN A 679 ? 2.4384 0.6877 1.4888 -0.1317 0.5095  0.0509  679 ASN A CA  
4914  C C   . ASN A 679 ? 2.5247 0.7060 1.5335 -0.1204 0.5210  0.0496  679 ASN A C   
4915  O O   . ASN A 679 ? 2.5626 0.7208 1.5847 -0.1556 0.5263  0.0318  679 ASN A O   
4916  C CB  . ASN A 679 ? 2.4531 0.6965 1.4737 -0.1054 0.5239  0.0818  679 ASN A CB  
4917  C CG  . ASN A 679 ? 2.3716 0.6723 1.4078 -0.0859 0.5020  0.0896  679 ASN A CG  
4918  O OD1 . ASN A 679 ? 2.3454 0.6572 1.3669 -0.0457 0.4814  0.0973  679 ASN A OD1 
4919  N ND2 . ASN A 679 ? 2.3318 0.6713 1.4000 -0.1135 0.5057  0.0890  679 ASN A ND2 
4920  N N   . LYS A 680 ? 2.5566 0.7080 1.5161 -0.0703 0.5226  0.0693  680 LYS A N   
4921  C CA  . LYS A 680 ? 2.6373 0.7259 1.5552 -0.0565 0.5333  0.0683  680 LYS A CA  
4922  C C   . LYS A 680 ? 2.7269 0.7566 1.6045 -0.0530 0.5637  0.0871  680 LYS A C   
4923  O O   . LYS A 680 ? 2.7898 0.7757 1.6637 -0.0824 0.5784  0.0769  680 LYS A O   
4924  C CB  . LYS A 680 ? 2.6246 0.7170 1.5158 -0.0033 0.5189  0.0789  680 LYS A CB  
4925  C CG  . LYS A 680 ? 2.6437 0.7157 1.5274 -0.0006 0.5100  0.0594  680 LYS A CG  
4926  C CD  . LYS A 680 ? 2.6605 0.7216 1.5070 0.0570  0.5070  0.0789  680 LYS A CD  
4927  C CE  . LYS A 680 ? 2.6671 0.7186 1.5085 0.0654  0.4961  0.0609  680 LYS A CE  
4928  N NZ  . LYS A 680 ? 2.6704 0.7264 1.4863 0.1233  0.4923  0.0825  680 LYS A NZ  
4929  N N   . ASP A 681 ? 2.7351 0.7640 1.5834 -0.0170 0.5714  0.1146  681 ASP A N   
4930  C CA  . ASP A 681 ? 2.8228 0.7949 1.6274 -0.0060 0.5998  0.1334  681 ASP A CA  
4931  C C   . ASP A 681 ? 2.8140 0.8037 1.6123 0.0046  0.6094  0.1558  681 ASP A C   
4932  O O   . ASP A 681 ? 2.8586 0.8233 1.6139 0.0405  0.6200  0.1784  681 ASP A O   
4933  C CB  . ASP A 681 ? 2.8739 0.8077 1.6293 0.0390  0.6020  0.1456  681 ASP A CB  
4934  C CG  . ASP A 681 ? 2.9772 0.8376 1.6949 0.0321  0.6301  0.1486  681 ASP A CG  
4935  O OD1 . ASP A 681 ? 3.0079 0.8420 1.7414 -0.0090 0.6369  0.1293  681 ASP A OD1 
4936  O OD2 . ASP A 681 ? 3.0280 0.8588 1.7025 0.0672  0.6436  0.1701  681 ASP A OD2 
4937  N N   . LEU A 682 ? 2.7592 0.7925 1.5983 -0.0249 0.6058  0.1501  682 LEU A N   
4938  C CA  . LEU A 682 ? 2.7542 0.8029 1.5826 -0.0126 0.6148  0.1714  682 LEU A CA  
4939  C C   . LEU A 682 ? 2.8399 0.8370 1.6449 -0.0241 0.6500  0.1828  682 LEU A C   
4940  O O   . LEU A 682 ? 2.8591 0.8464 1.6946 -0.0675 0.6653  0.1712  682 LEU A O   
4941  C CB  . LEU A 682 ? 2.6739 0.7836 1.5517 -0.0405 0.6029  0.1624  682 LEU A CB  
4942  C CG  . LEU A 682 ? 2.5858 0.7521 1.4819 -0.0205 0.5680  0.1589  682 LEU A CG  
4943  C CD1 . LEU A 682 ? 2.5139 0.7365 1.4578 -0.0522 0.5604  0.1498  682 LEU A CD1 
4944  C CD2 . LEU A 682 ? 2.5893 0.7584 1.4434 0.0347  0.5555  0.1846  682 LEU A CD2 
4945  N N   . CYS A 683 ? 2.8909 0.8584 1.6455 0.0151  0.6612  0.2061  683 CYS A N   
4946  C CA  . CYS A 683 ? 2.9758 0.8926 1.7035 0.0106  0.6954  0.2194  683 CYS A CA  
4947  C C   . CYS A 683 ? 2.9628 0.9028 1.7105 -0.0090 0.7101  0.2273  683 CYS A C   
4948  O O   . CYS A 683 ? 2.9824 0.9146 1.7622 -0.0497 0.7294  0.2205  683 CYS A O   
4949  C CB  . CYS A 683 ? 3.0311 0.9140 1.6993 0.0605  0.7010  0.2413  683 CYS A CB  
4950  S SG  . CYS A 683 ? 3.1315 0.9575 1.7620 0.0633  0.7425  0.2615  683 CYS A SG  
4951  N N   . ASN B 26  ? 1.1069 0.7784 1.0975 0.1798  0.2838  0.0562  26  ASN B N   
4952  C CA  . ASN B 26  ? 1.1406 0.7864 1.1398 0.1758  0.3242  0.0574  26  ASN B CA  
4953  C C   . ASN B 26  ? 1.2176 0.8160 1.1122 0.1720  0.3432  0.0467  26  ASN B C   
4954  O O   . ASN B 26  ? 1.2401 0.8258 1.0670 0.1718  0.3312  0.0355  26  ASN B O   
4955  C CB  . ASN B 26  ? 1.1207 0.7902 1.1683 0.1720  0.3090  0.0705  26  ASN B CB  
4956  C CG  . ASN B 26  ? 1.1320 0.8036 1.1224 0.1704  0.2731  0.0695  26  ASN B CG  
4957  O OD1 . ASN B 26  ? 1.1402 0.8087 1.0723 0.1740  0.2497  0.0629  26  ASN B OD1 
4958  N ND2 . ASN B 26  ? 1.1283 0.8049 1.1444 0.1643  0.2712  0.0751  26  ASN B ND2 
4959  N N   . ALA B 27  ? 1.1998 0.7737 1.0830 0.1674  0.3715  0.0524  27  ALA B N   
4960  C CA  . ALA B 27  ? 1.2718 0.7982 1.0521 0.1615  0.3928  0.0483  27  ALA B CA  
4961  C C   . ALA B 27  ? 1.2695 0.7973 0.9782 0.1646  0.3476  0.0539  27  ALA B C   
4962  O O   . ALA B 27  ? 1.3151 0.8203 0.9376 0.1609  0.3424  0.0480  27  ALA B O   
4963  C CB  . ALA B 27  ? 1.3144 0.8137 1.1039 0.1557  0.4351  0.0578  27  ALA B CB  
4964  N N   . GLU B 28  ? 1.3591 0.9140 1.1063 0.1695  0.3152  0.0644  28  GLU B N   
4965  C CA  . GLU B 28  ? 1.3746 0.9316 1.0724 0.1741  0.2767  0.0699  28  GLU B CA  
4966  C C   . GLU B 28  ? 1.3582 0.9350 1.0376 0.1774  0.2452  0.0581  28  GLU B C   
4967  O O   . GLU B 28  ? 1.3926 0.9608 1.0115 0.1791  0.2234  0.0593  28  GLU B O   
4968  C CB  . GLU B 28  ? 1.3208 0.8986 1.0714 0.1758  0.2577  0.0776  28  GLU B CB  
4969  C CG  . GLU B 28  ? 1.3395 0.8928 1.1025 0.1719  0.2870  0.0903  28  GLU B CG  
4970  C CD  . GLU B 28  ? 1.2826 0.8542 1.1001 0.1699  0.2707  0.0922  28  GLU B CD  
4971  O OE1 . GLU B 28  ? 1.2445 0.8379 1.0650 0.1726  0.2366  0.0857  28  GLU B OE1 
4972  O OE2 . GLU B 28  ? 1.2800 0.8421 1.1374 0.1637  0.2953  0.0979  28  GLU B OE2 
4973  N N   . GLY B 29  ? 1.3059 0.9106 1.0423 0.1782  0.2416  0.0494  29  GLY B N   
4974  C CA  . GLY B 29  ? 1.2773 0.8987 1.0022 0.1806  0.2168  0.0389  29  GLY B CA  
4975  C C   . GLY B 29  ? 1.3161 0.9108 0.9817 0.1756  0.2330  0.0252  29  GLY B C   
4976  O O   . GLY B 29  ? 1.3261 0.9243 0.9519 0.1752  0.2085  0.0174  29  GLY B O   
4977  N N   . ASP B 30  ? 1.3061 0.8735 0.9673 0.1693  0.2768  0.0196  30  ASP B N   
4978  C CA  . ASP B 30  ? 1.3443 0.8799 0.9375 0.1588  0.2981  0.0010  30  ASP B CA  
4979  C C   . ASP B 30  ? 1.4080 0.9217 0.9010 0.1524  0.2806  0.0058  30  ASP B C   
4980  O O   . ASP B 30  ? 1.4335 0.9379 0.8635 0.1433  0.2685  -0.0083 30  ASP B O   
4981  C CB  . ASP B 30  ? 1.3515 0.8576 0.9621 0.1514  0.3573  -0.0081 30  ASP B CB  
4982  C CG  . ASP B 30  ? 1.2851 0.8144 1.0053 0.1585  0.3741  -0.0091 30  ASP B CG  
4983  O OD1 . ASP B 30  ? 1.2474 0.7985 0.9972 0.1628  0.3531  -0.0146 30  ASP B OD1 
4984  O OD2 . ASP B 30  ? 1.2703 0.7963 1.0520 0.1597  0.4086  -0.0018 30  ASP B OD2 
4985  N N   . ALA B 31  ? 1.3879 0.8941 0.8690 0.1561  0.2774  0.0275  31  ALA B N   
4986  C CA  . ALA B 31  ? 1.4448 0.9319 0.8390 0.1521  0.2573  0.0416  31  ALA B CA  
4987  C C   . ALA B 31  ? 1.4184 0.9346 0.8103 0.1595  0.2032  0.0455  31  ALA B C   
4988  O O   . ALA B 31  ? 1.4603 0.9697 0.7825 0.1522  0.1805  0.0458  31  ALA B O   
4989  C CB  . ALA B 31  ? 1.4636 0.9349 0.8619 0.1563  0.2697  0.0673  31  ALA B CB  
4990  N N   . LEU B 32  ? 1.3926 0.9422 0.8610 0.1719  0.1827  0.0479  32  LEU B N   
4991  C CA  . LEU B 32  ? 1.3752 0.9520 0.8528 0.1785  0.1391  0.0485  32  LEU B CA  
4992  C C   . LEU B 32  ? 1.3628 0.9519 0.8345 0.1725  0.1307  0.0255  32  LEU B C   
4993  O O   . LEU B 32  ? 1.3665 0.9698 0.8217 0.1726  0.0978  0.0236  32  LEU B O   
4994  C CB  . LEU B 32  ? 1.3322 0.9362 0.8851 0.1890  0.1270  0.0532  32  LEU B CB  
4995  C CG  . LEU B 32  ? 1.3166 0.9120 0.8809 0.1954  0.1242  0.0739  32  LEU B CG  
4996  C CD1 . LEU B 32  ? 1.2465 0.8640 0.8825 0.1982  0.1239  0.0692  32  LEU B CD1 
4997  C CD2 . LEU B 32  ? 1.3212 0.9166 0.8585 0.2017  0.0928  0.0888  32  LEU B CD2 
4998  N N   . SER B 33  ? 1.3200 0.9035 0.8130 0.1671  0.1616  0.0088  33  SER B N   
4999  C CA  . SER B 33  ? 1.3183 0.9046 0.8008 0.1590  0.1600  -0.0141 33  SER B CA  
5000  C C   . SER B 33  ? 1.3915 0.9527 0.7816 0.1432  0.1569  -0.0236 33  SER B C   
5001  O O   . SER B 33  ? 1.3987 0.9725 0.7679 0.1373  0.1280  -0.0343 33  SER B O   
5002  C CB  . SER B 33  ? 1.2911 0.8723 0.8243 0.1574  0.1988  -0.0271 33  SER B CB  
5003  O OG  . SER B 33  ? 1.2209 0.8319 0.8360 0.1692  0.1918  -0.0152 33  SER B OG  
5004  N N   . ALA B 34  ? 1.4183 0.9472 0.7493 0.1353  0.1797  -0.0155 34  ALA B N   
5005  C CA  . ALA B 34  ? 1.5135 1.0169 0.7412 0.1151  0.1760  -0.0235 34  ALA B CA  
5006  C C   . ALA B 34  ? 1.5214 1.0473 0.7199 0.1174  0.1183  -0.0062 34  ALA B C   
5007  O O   . ALA B 34  ? 1.5666 1.0956 0.7141 0.1015  0.0951  -0.0209 34  ALA B O   
5008  C CB  . ALA B 34  ? 1.5901 1.0526 0.7550 0.1056  0.2129  -0.0130 34  ALA B CB  
5009  N N   . LEU B 35  ? 1.5096 1.0524 0.7481 0.1360  0.0951  0.0241  35  LEU B N   
5010  C CA  . LEU B 35  ? 1.5117 1.0800 0.7505 0.1425  0.0424  0.0432  35  LEU B CA  
5011  C C   . LEU B 35  ? 1.4803 1.0822 0.7661 0.1432  0.0177  0.0216  35  LEU B C   
5012  O O   . LEU B 35  ? 1.5024 1.1198 0.7617 0.1351  -0.0200 0.0211  35  LEU B O   
5013  C CB  . LEU B 35  ? 1.4819 1.0590 0.7769 0.1635  0.0343  0.0737  35  LEU B CB  
5014  C CG  . LEU B 35  ? 1.4908 1.0789 0.7834 0.1728  -0.0075 0.1079  35  LEU B CG  
5015  C CD1 . LEU B 35  ? 1.4427 1.0345 0.8090 0.1924  -0.0007 0.1272  35  LEU B CD1 
5016  C CD2 . LEU B 35  ? 1.4814 1.1040 0.7950 0.1727  -0.0512 0.1016  35  LEU B CD2 
5017  N N   . LYS B 36  ? 1.4085 1.0232 0.7662 0.1518  0.0372  0.0061  36  LYS B N   
5018  C CA  . LYS B 36  ? 1.3720 1.0152 0.7773 0.1526  0.0199  -0.0122 36  LYS B CA  
5019  C C   . LYS B 36  ? 1.4060 1.0425 0.7640 0.1316  0.0175  -0.0393 36  LYS B C   
5020  O O   . LYS B 36  ? 1.3968 1.0577 0.7761 0.1283  -0.0105 -0.0496 36  LYS B O   
5021  C CB  . LYS B 36  ? 1.3153 0.9675 0.7919 0.1619  0.0457  -0.0202 36  LYS B CB  
5022  C CG  . LYS B 36  ? 1.2768 0.9520 0.8001 0.1612  0.0377  -0.0378 36  LYS B CG  
5023  C CD  . LYS B 36  ? 1.2158 0.8944 0.7950 0.1668  0.0654  -0.0405 36  LYS B CD  
5024  C CE  . LYS B 36  ? 1.1729 0.8704 0.7953 0.1657  0.0606  -0.0531 36  LYS B CE  
5025  N NZ  . LYS B 36  ? 1.1457 0.8703 0.8032 0.1745  0.0359  -0.0436 36  LYS B NZ  
5026  N N   . ASN B 37  ? 1.4980 1.1002 0.7931 0.1149  0.0491  -0.0539 37  ASN B N   
5027  C CA  . ASN B 37  ? 1.5346 1.1245 0.7769 0.0897  0.0522  -0.0859 37  ASN B CA  
5028  C C   . ASN B 37  ? 1.5996 1.1887 0.7528 0.0712  0.0133  -0.0796 37  ASN B C   
5029  O O   . ASN B 37  ? 1.6326 1.2214 0.7452 0.0473  0.0021  -0.1072 37  ASN B O   
5030  C CB  . ASN B 37  ? 1.5478 1.0969 0.7623 0.0761  0.1107  -0.1105 37  ASN B CB  
5031  C CG  . ASN B 37  ? 1.4813 1.0338 0.7907 0.0920  0.1471  -0.1153 37  ASN B CG  
5032  O OD1 . ASN B 37  ? 1.4488 1.0068 0.8042 0.1103  0.1573  -0.0922 37  ASN B OD1 
5033  N ND2 . ASN B 37  ? 1.4626 1.0122 0.8036 0.0834  0.1656  -0.1442 37  ASN B ND2 
5034  N N   . SER B 38  ? 1.6515 1.2400 0.7734 0.0795  -0.0081 -0.0431 38  SER B N   
5035  C CA  . SER B 38  ? 1.7110 1.3021 0.7493 0.0628  -0.0514 -0.0269 38  SER B CA  
5036  C C   . SER B 38  ? 1.6913 1.3285 0.7838 0.0760  -0.1119 -0.0024 38  SER B C   
5037  O O   . SER B 38  ? 1.7348 1.3835 0.7726 0.0630  -0.1577 0.0158  38  SER B O   
5038  C CB  . SER B 38  ? 1.7508 1.3099 0.7180 0.0622  -0.0381 0.0044  38  SER B CB  
5039  O OG  . SER B 38  ? 1.7905 1.3623 0.7049 0.0571  -0.0912 0.0400  38  SER B OG  
5040  N N   . LEU B 39  ? 1.6110 1.2749 0.8096 0.1000  -0.1130 -0.0002 39  LEU B N   
5041  C CA  . LEU B 39  ? 1.5777 1.2833 0.8427 0.1139  -0.1607 0.0203  39  LEU B CA  
5042  C C   . LEU B 39  ? 1.5466 1.2795 0.8698 0.1086  -0.1681 -0.0116 39  LEU B C   
5043  O O   . LEU B 39  ? 1.5088 1.2337 0.8683 0.1113  -0.1305 -0.0370 39  LEU B O   
5044  C CB  . LEU B 39  ? 1.5216 1.2338 0.8631 0.1438  -0.1532 0.0483  39  LEU B CB  
5045  C CG  . LEU B 39  ? 1.5424 1.2357 0.8549 0.1540  -0.1558 0.0890  39  LEU B CG  
5046  C CD1 . LEU B 39  ? 1.4785 1.1864 0.8871 0.1807  -0.1545 0.1086  39  LEU B CD1 
5047  C CD2 . LEU B 39  ? 1.6323 1.3321 0.8816 0.1421  -0.2032 0.1174  39  LEU B CD2 
5048  N N   . ALA B 40  ? 1.5429 1.3088 0.8780 0.1002  -0.2173 -0.0076 40  ALA B N   
5049  C CA  . ALA B 40  ? 1.5171 1.3144 0.9262 0.0982  -0.2278 -0.0318 40  ALA B CA  
5050  C C   . ALA B 40  ? 1.4634 1.2844 0.9775 0.1273  -0.2279 -0.0127 40  ALA B C   
5051  O O   . ALA B 40  ? 1.4547 1.2923 0.9986 0.1419  -0.2567 0.0217  40  ALA B O   
5052  C CB  . ALA B 40  ? 1.5530 1.3800 0.9423 0.0756  -0.2817 -0.0355 40  ALA B CB  
5053  N N   . ASP B 41  ? 1.4251 1.2452 0.9946 0.1346  -0.1933 -0.0340 41  ASP B N   
5054  C CA  . ASP B 41  ? 1.3804 1.2150 1.0352 0.1575  -0.1820 -0.0227 41  ASP B CA  
5055  C C   . ASP B 41  ? 1.3654 1.2289 1.0904 0.1537  -0.1883 -0.0425 41  ASP B C   
5056  O O   . ASP B 41  ? 1.3486 1.2045 1.0873 0.1487  -0.1583 -0.0661 41  ASP B O   
5057  C CB  . ASP B 41  ? 1.3547 1.1630 1.0063 0.1666  -0.1360 -0.0265 41  ASP B CB  
5058  C CG  . ASP B 41  ? 1.3133 1.1328 1.0367 0.1845  -0.1230 -0.0181 41  ASP B CG  
5059  O OD1 . ASP B 41  ? 1.2976 1.1430 1.0837 0.1885  -0.1361 -0.0201 41  ASP B OD1 
5060  O OD2 . ASP B 41  ? 1.2941 1.0958 1.0116 0.1923  -0.0974 -0.0115 41  ASP B OD2 
5061  N N   . PRO B 42  ? 1.3307 1.1557 0.9765 0.0591  -0.3184 -0.1725 42  PRO B N   
5062  C CA  . PRO B 42  ? 1.3447 1.2351 1.0869 0.0554  -0.3220 -0.1728 42  PRO B CA  
5063  C C   . PRO B 42  ? 1.3494 1.2773 1.1322 0.0626  -0.2935 -0.1557 42  PRO B C   
5064  O O   . PRO B 42  ? 1.3699 1.3429 1.2251 0.0536  -0.2772 -0.1497 42  PRO B O   
5065  C CB  . PRO B 42  ? 1.3569 1.2600 1.1109 0.0725  -0.3651 -0.1855 42  PRO B CB  
5066  C CG  . PRO B 42  ? 1.3525 1.2064 1.0186 0.0934  -0.3753 -0.1825 42  PRO B CG  
5067  C CD  . PRO B 42  ? 1.3404 1.1369 0.9321 0.0813  -0.3496 -0.1777 42  PRO B CD  
5068  N N   . ASN B 43  ? 1.2904 1.1960 1.0241 0.0796  -0.2865 -0.1476 43  ASN B N   
5069  C CA  . ASN B 43  ? 1.2961 1.2311 1.0560 0.0923  -0.2642 -0.1342 43  ASN B CA  
5070  C C   . ASN B 43  ? 1.2818 1.2033 1.0276 0.0821  -0.2309 -0.1245 43  ASN B C   
5071  O O   . ASN B 43  ? 1.2859 1.2237 1.0409 0.0948  -0.2132 -0.1146 43  ASN B O   
5072  C CB  . ASN B 43  ? 1.2861 1.2035 1.0043 0.1182  -0.2775 -0.1329 43  ASN B CB  
5073  C CG  . ASN B 43  ? 1.3099 1.2671 1.0743 0.1361  -0.3025 -0.1377 43  ASN B CG  
5074  O OD1 . ASN B 43  ? 1.3103 1.2514 1.0548 0.1429  -0.3359 -0.1484 43  ASN B OD1 
5075  N ND2 . ASN B 43  ? 1.3345 1.3428 1.1606 0.1456  -0.2863 -0.1300 43  ASN B ND2 
5076  N N   . LYS B 44  ? 1.2924 1.1834 1.0151 0.0619  -0.2235 -0.1285 44  LYS B N   
5077  C CA  . LYS B 44  ? 1.2774 1.1571 0.9950 0.0513  -0.1955 -0.1216 44  LYS B CA  
5078  C C   . LYS B 44  ? 1.2471 1.0993 0.9200 0.0651  -0.1866 -0.1173 44  LYS B C   
5079  O O   . LYS B 44  ? 1.2400 1.0992 0.9216 0.0682  -0.1682 -0.1104 44  LYS B O   
5080  C CB  . LYS B 44  ? 1.3133 1.2380 1.0938 0.0473  -0.1766 -0.1116 44  LYS B CB  
5081  C CG  . LYS B 44  ? 1.3432 1.2914 1.1769 0.0288  -0.1814 -0.1160 44  LYS B CG  
5082  C CD  . LYS B 44  ? 1.3169 1.2265 1.1175 0.0119  -0.1944 -0.1302 44  LYS B CD  
5083  C CE  . LYS B 44  ? 1.3361 1.2668 1.1892 -0.0039 -0.2074 -0.1393 44  LYS B CE  
5084  N NZ  . LYS B 44  ? 1.3305 1.2482 1.1953 -0.0252 -0.1910 -0.1403 44  LYS B NZ  
5085  N N   . VAL B 45  ? 1.3060 1.1232 0.9296 0.0744  -0.2013 -0.1219 45  VAL B N   
5086  C CA  . VAL B 45  ? 1.2832 1.0690 0.8678 0.0858  -0.1943 -0.1193 45  VAL B CA  
5087  C C   . VAL B 45  ? 1.2625 1.0150 0.8295 0.0691  -0.1755 -0.1211 45  VAL B C   
5088  O O   . VAL B 45  ? 1.2453 0.9943 0.8153 0.0733  -0.1635 -0.1190 45  VAL B O   
5089  C CB  . VAL B 45  ? 1.2904 1.0429 0.8276 0.0997  -0.2134 -0.1219 45  VAL B CB  
5090  C CG1 . VAL B 45  ? 1.2798 0.9810 0.7710 0.1001  -0.2025 -0.1211 45  VAL B CG1 
5091  C CG2 . VAL B 45  ? 1.3032 1.0879 0.8604 0.1238  -0.2279 -0.1194 45  VAL B CG2 
5092  N N   . LEU B 46  ? 1.2597 0.9870 0.8093 0.0515  -0.1740 -0.1266 46  LEU B N   
5093  C CA  . LEU B 46  ? 1.2473 0.9396 0.7806 0.0361  -0.1549 -0.1295 46  LEU B CA  
5094  C C   . LEU B 46  ? 1.2346 0.9507 0.8113 0.0229  -0.1399 -0.1292 46  LEU B C   
5095  O O   . LEU B 46  ? 1.2257 0.9177 0.7982 0.0085  -0.1252 -0.1336 46  LEU B O   
5096  C CB  . LEU B 46  ? 1.2666 0.9179 0.7566 0.0256  -0.1563 -0.1355 46  LEU B CB  
5097  C CG  . LEU B 46  ? 1.2908 0.8978 0.7213 0.0379  -0.1645 -0.1339 46  LEU B CG  
5098  C CD1 . LEU B 46  ? 1.3180 0.8711 0.6987 0.0261  -0.1507 -0.1374 46  LEU B CD1 
5099  C CD2 . LEU B 46  ? 1.2832 0.8801 0.7108 0.0500  -0.1588 -0.1283 46  LEU B CD2 
5100  N N   . GLN B 47  ? 1.1496 0.9100 0.7674 0.0287  -0.1413 -0.1233 47  GLN B N   
5101  C CA  . GLN B 47  ? 1.1515 0.9303 0.8063 0.0175  -0.1276 -0.1208 47  GLN B CA  
5102  C C   . GLN B 47  ? 1.1269 0.8867 0.7778 0.0174  -0.1149 -0.1220 47  GLN B C   
5103  O O   . GLN B 47  ? 1.1197 0.8712 0.7849 0.0032  -0.1041 -0.1252 47  GLN B O   
5104  C CB  . GLN B 47  ? 1.1833 1.0083 0.8779 0.0270  -0.1270 -0.1108 47  GLN B CB  
5105  C CG  . GLN B 47  ? 1.1966 1.0339 0.9167 0.0252  -0.1108 -0.1035 47  GLN B CG  
5106  C CD  . GLN B 47  ? 1.2500 1.1222 1.0159 0.0190  -0.1043 -0.0947 47  GLN B CD  
5107  O OE1 . GLN B 47  ? 1.2844 1.1857 1.0720 0.0261  -0.1092 -0.0903 47  GLN B OE1 
5108  N NE2 . GLN B 47  ? 1.2632 1.1324 1.0494 0.0058  -0.0924 -0.0922 47  GLN B NE2 
5109  N N   . SER B 48  ? 1.1218 0.8740 0.7567 0.0338  -0.1183 -0.1215 48  SER B N   
5110  C CA  . SER B 48  ? 1.1034 0.8402 0.7414 0.0363  -0.1121 -0.1255 48  SER B CA  
5111  C C   . SER B 48  ? 1.0916 0.7918 0.7233 0.0190  -0.1026 -0.1346 48  SER B C   
5112  O O   . SER B 48  ? 1.0790 0.7697 0.7274 0.0173  -0.0974 -0.1402 48  SER B O   
5113  C CB  . SER B 48  ? 1.0973 0.8299 0.7186 0.0583  -0.1213 -0.1262 48  SER B CB  
5114  O OG  . SER B 48  ? 1.1017 0.8155 0.6944 0.0624  -0.1289 -0.1273 48  SER B OG  
5115  N N   . TRP B 49  ? 1.1541 0.8325 0.7621 0.0079  -0.1001 -0.1366 49  TRP B N   
5116  C CA  . TRP B 49  ? 1.1564 0.7952 0.7516 -0.0066 -0.0853 -0.1435 49  TRP B CA  
5117  C C   . TRP B 49  ? 1.1464 0.7899 0.7699 -0.0230 -0.0725 -0.1480 49  TRP B C   
5118  O O   . TRP B 49  ? 1.1552 0.7905 0.7679 -0.0349 -0.0674 -0.1505 49  TRP B O   
5119  C CB  . TRP B 49  ? 1.1822 0.7905 0.7299 -0.0083 -0.0865 -0.1427 49  TRP B CB  
5120  C CG  . TRP B 49  ? 1.1962 0.7891 0.7145 0.0078  -0.0968 -0.1386 49  TRP B CG  
5121  C CD1 . TRP B 49  ? 1.1843 0.7983 0.7149 0.0251  -0.1093 -0.1360 49  TRP B CD1 
5122  C CD2 . TRP B 49  ? 1.2314 0.7797 0.6991 0.0099  -0.0945 -0.1364 49  TRP B CD2 
5123  N NE1 . TRP B 49  ? 1.2054 0.7928 0.7015 0.0370  -0.1163 -0.1334 49  TRP B NE1 
5124  C CE2 . TRP B 49  ? 1.2373 0.7832 0.6940 0.0279  -0.1074 -0.1324 49  TRP B CE2 
5125  C CE3 . TRP B 49  ? 1.2658 0.7722 0.6913 0.0004  -0.0818 -0.1368 49  TRP B CE3 
5126  C CZ2 . TRP B 49  ? 1.2777 0.7805 0.6858 0.0356  -0.1088 -0.1277 49  TRP B CZ2 
5127  C CZ3 . TRP B 49  ? 1.3102 0.7719 0.6815 0.0091  -0.0818 -0.1311 49  TRP B CZ3 
5128  C CH2 . TRP B 49  ? 1.3163 0.7765 0.6809 0.0262  -0.0956 -0.1261 49  TRP B CH2 
5129  N N   . ASP B 50  ? 1.0610 0.7159 0.7200 -0.0216 -0.0696 -0.1505 50  ASP B N   
5130  C CA  . ASP B 50  ? 1.0482 0.7083 0.7395 -0.0339 -0.0592 -0.1548 50  ASP B CA  
5131  C C   . ASP B 50  ? 1.0411 0.6681 0.7375 -0.0473 -0.0405 -0.1647 50  ASP B C   
5132  O O   . ASP B 50  ? 1.0330 0.6484 0.7465 -0.0445 -0.0378 -0.1701 50  ASP B O   
5133  C CB  . ASP B 50  ? 1.0396 0.7236 0.7622 -0.0225 -0.0671 -0.1527 50  ASP B CB  
5134  C CG  . ASP B 50  ? 1.0291 0.7172 0.7854 -0.0324 -0.0588 -0.1560 50  ASP B CG  
5135  O OD1 . ASP B 50  ? 1.0246 0.7015 0.7822 -0.0486 -0.0467 -0.1600 50  ASP B OD1 
5136  O OD2 . ASP B 50  ? 1.0280 0.7279 0.8060 -0.0219 -0.0656 -0.1551 50  ASP B OD2 
5137  N N   . ALA B 51  ? 1.0749 0.6864 0.7603 -0.0616 -0.0268 -0.1682 51  ALA B N   
5138  C CA  . ALA B 51  ? 1.0802 0.6562 0.7617 -0.0736 -0.0027 -0.1759 51  ALA B CA  
5139  C C   . ALA B 51  ? 1.0495 0.6295 0.7865 -0.0796 0.0087  -0.1847 51  ALA B C   
5140  O O   . ALA B 51  ? 1.0506 0.6055 0.8003 -0.0871 0.0294  -0.1912 51  ALA B O   
5141  C CB  . ALA B 51  ? 1.1014 0.6577 0.7483 -0.0837 0.0079  -0.1786 51  ALA B CB  
5142  N N   . THR B 52  ? 1.0288 0.6382 0.8010 -0.0755 -0.0035 -0.1846 52  THR B N   
5143  C CA  . THR B 52  ? 0.9994 0.6128 0.8251 -0.0787 0.0027  -0.1940 52  THR B CA  
5144  C C   . THR B 52  ? 0.9890 0.6074 0.8451 -0.0676 -0.0097 -0.1989 52  THR B C   
5145  O O   . THR B 52  ? 0.9657 0.5914 0.8703 -0.0660 -0.0127 -0.2079 52  THR B O   
5146  C CB  . THR B 52  ? 0.9895 0.6260 0.8355 -0.0770 -0.0061 -0.1910 52  THR B CB  
5147  O OG1 . THR B 52  ? 1.0028 0.6635 0.8438 -0.0606 -0.0283 -0.1809 52  THR B OG1 
5148  C CG2 . THR B 52  ? 1.0016 0.6334 0.8213 -0.0877 0.0014  -0.1885 52  THR B CG2 
5149  N N   . LEU B 53  ? 0.9937 0.6074 0.8236 -0.0584 -0.0198 -0.1947 53  LEU B N   
5150  C CA  . LEU B 53  ? 0.9914 0.6043 0.8489 -0.0481 -0.0330 -0.2027 53  LEU B CA  
5151  C C   . LEU B 53  ? 1.0112 0.5960 0.8963 -0.0615 -0.0113 -0.2126 53  LEU B C   
5152  O O   . LEU B 53  ? 1.0351 0.5958 0.8965 -0.0749 0.0146  -0.2090 53  LEU B O   
5153  C CB  . LEU B 53  ? 0.9959 0.6136 0.8154 -0.0315 -0.0524 -0.1952 53  LEU B CB  
5154  C CG  . LEU B 53  ? 0.9804 0.6261 0.7884 -0.0111 -0.0761 -0.1886 53  LEU B CG  
5155  C CD1 . LEU B 53  ? 0.9648 0.6298 0.7769 -0.0146 -0.0726 -0.1810 53  LEU B CD1 
5156  C CD2 . LEU B 53  ? 0.9895 0.6387 0.7522 0.0011  -0.0850 -0.1787 53  LEU B CD2 
5157  N N   . VAL B 54  ? 1.0608 0.6470 0.9972 -0.0569 -0.0219 -0.2256 54  VAL B N   
5158  C CA  . VAL B 54  ? 1.0551 0.6167 1.0327 -0.0703 -0.0001 -0.2355 54  VAL B CA  
5159  C C   . VAL B 54  ? 1.0969 0.6291 1.0298 -0.0726 0.0112  -0.2265 54  VAL B C   
5160  O O   . VAL B 54  ? 1.1177 0.6205 1.0359 -0.0871 0.0442  -0.2215 54  VAL B O   
5161  C CB  . VAL B 54  ? 1.0173 0.5892 1.0663 -0.0632 -0.0213 -0.2541 54  VAL B CB  
5162  C CG1 . VAL B 54  ? 1.0199 0.5661 1.1105 -0.0744 -0.0046 -0.2629 54  VAL B CG1 
5163  C CG2 . VAL B 54  ? 0.9726 0.5629 1.0768 -0.0657 -0.0218 -0.2646 54  VAL B CG2 
5164  N N   . THR B 55  ? 1.1366 0.6730 1.0424 -0.0564 -0.0151 -0.2235 55  THR B N   
5165  C CA  . THR B 55  ? 1.1743 0.6831 1.0348 -0.0546 -0.0098 -0.2143 55  THR B CA  
5166  C C   . THR B 55  ? 1.1865 0.7105 0.9842 -0.0384 -0.0303 -0.2018 55  THR B C   
5167  O O   . THR B 55  ? 1.1639 0.7201 0.9629 -0.0254 -0.0525 -0.2023 55  THR B O   
5168  C CB  . THR B 55  ? 1.1763 0.6703 1.0735 -0.0497 -0.0211 -0.2254 55  THR B CB  
5169  O OG1 . THR B 55  ? 1.1526 0.6709 1.0483 -0.0277 -0.0596 -0.2320 55  THR B OG1 
5170  C CG2 . THR B 55  ? 1.1484 0.6365 1.1272 -0.0644 -0.0063 -0.2411 55  THR B CG2 
5171  N N   . PRO B 56  ? 1.1890 0.6894 0.9324 -0.0378 -0.0224 -0.1900 56  PRO B N   
5172  C CA  . PRO B 56  ? 1.1976 0.7144 0.8904 -0.0217 -0.0426 -0.1796 56  PRO B CA  
5173  C C   . PRO B 56  ? 1.1969 0.7189 0.8862 -0.0016 -0.0675 -0.1823 56  PRO B C   
5174  O O   . PRO B 56  ? 1.2085 0.7379 0.8566 0.0123  -0.0802 -0.1735 56  PRO B O   
5175  C CB  . PRO B 56  ? 1.2421 0.7258 0.8798 -0.0280 -0.0254 -0.1682 56  PRO B CB  
5176  C CG  . PRO B 56  ? 1.2700 0.7116 0.9230 -0.0405 0.0003  -0.1708 56  PRO B CG  
5177  C CD  . PRO B 56  ? 1.2299 0.6862 0.9532 -0.0519 0.0088  -0.1843 56  PRO B CD  
5178  N N   . CYS B 57  ? 1.2000 0.7177 0.9333 0.0013  -0.0761 -0.1960 57  CYS B N   
5179  C CA  . CYS B 57  ? 1.2031 0.7175 0.9305 0.0211  -0.0997 -0.2016 57  CYS B CA  
5180  C C   . CYS B 57  ? 1.1834 0.7339 0.8942 0.0442  -0.1249 -0.2011 57  CYS B C   
5181  O O   . CYS B 57  ? 1.1908 0.7398 0.8807 0.0643  -0.1428 -0.2031 57  CYS B O   
5182  C CB  . CYS B 57  ? 1.1903 0.6876 0.9748 0.0171  -0.1042 -0.2199 57  CYS B CB  
5183  S SG  . CYS B 57  ? 1.2240 0.6733 1.0336 -0.0091 -0.0682 -0.2185 57  CYS B SG  
5184  N N   . THR B 58  ? 1.1091 0.6890 0.8278 0.0429  -0.1244 -0.1980 58  THR B N   
5185  C CA  . THR B 58  ? 1.1031 0.7145 0.8015 0.0640  -0.1406 -0.1926 58  THR B CA  
5186  C C   . THR B 58  ? 1.1136 0.7421 0.7759 0.0648  -0.1333 -0.1755 58  THR B C   
5187  O O   . THR B 58  ? 1.1128 0.7690 0.7619 0.0807  -0.1408 -0.1683 58  THR B O   
5188  C CB  . THR B 58  ? 1.0865 0.7176 0.8134 0.0645  -0.1446 -0.1968 58  THR B CB  
5189  O OG1 . THR B 58  ? 1.0821 0.7178 0.8224 0.0424  -0.1242 -0.1904 58  THR B OG1 
5190  C CG2 . THR B 58  ? 1.0700 0.6871 0.8387 0.0667  -0.1581 -0.2168 58  THR B CG2 
5191  N N   . TRP B 59  ? 1.1174 0.7292 0.7642 0.0490  -0.1188 -0.1692 59  TRP B N   
5192  C CA  . TRP B 59  ? 1.1261 0.7526 0.7423 0.0511  -0.1180 -0.1565 59  TRP B CA  
5193  C C   . TRP B 59  ? 1.1361 0.7622 0.7248 0.0725  -0.1320 -0.1535 59  TRP B C   
5194  O O   . TRP B 59  ? 1.1438 0.7476 0.7301 0.0816  -0.1393 -0.1609 59  TRP B O   
5195  C CB  . TRP B 59  ? 1.1432 0.7454 0.7419 0.0318  -0.1024 -0.1528 59  TRP B CB  
5196  C CG  . TRP B 59  ? 1.1357 0.7330 0.7579 0.0109  -0.0852 -0.1567 59  TRP B CG  
5197  C CD1 . TRP B 59  ? 1.1133 0.7283 0.7744 0.0071  -0.0839 -0.1624 59  TRP B CD1 
5198  C CD2 . TRP B 59  ? 1.1542 0.7242 0.7586 -0.0067 -0.0665 -0.1556 59  TRP B CD2 
5199  N NE1 . TRP B 59  ? 1.1108 0.7140 0.7858 -0.0126 -0.0653 -0.1657 59  TRP B NE1 
5200  C CE2 . TRP B 59  ? 1.1364 0.7115 0.7753 -0.0212 -0.0531 -0.1618 59  TRP B CE2 
5201  C CE3 . TRP B 59  ? 1.1888 0.7272 0.7466 -0.0090 -0.0603 -0.1502 59  TRP B CE3 
5202  C CZ2 . TRP B 59  ? 1.1493 0.7004 0.7787 -0.0383 -0.0313 -0.1635 59  TRP B CZ2 
5203  C CZ3 . TRP B 59  ? 1.2085 0.7199 0.7500 -0.0249 -0.0395 -0.1510 59  TRP B CZ3 
5204  C CH2 . TRP B 59  ? 1.1877 0.7063 0.7655 -0.0396 -0.0240 -0.1581 59  TRP B CH2 
5205  N N   . PHE B 60  ? 1.1242 0.7757 0.6974 0.0806  -0.1364 -0.1438 60  PHE B N   
5206  C CA  . PHE B 60  ? 1.1330 0.7861 0.6828 0.1015  -0.1488 -0.1408 60  PHE B CA  
5207  C C   . PHE B 60  ? 1.1571 0.7768 0.6767 0.0959  -0.1486 -0.1379 60  PHE B C   
5208  O O   . PHE B 60  ? 1.1677 0.7702 0.6788 0.0773  -0.1383 -0.1358 60  PHE B O   
5209  C CB  . PHE B 60  ? 1.1298 0.8273 0.6850 0.1145  -0.1528 -0.1322 60  PHE B CB  
5210  C CG  . PHE B 60  ? 1.1226 0.8478 0.6974 0.1233  -0.1495 -0.1312 60  PHE B CG  
5211  C CD1 . PHE B 60  ? 1.1165 0.8297 0.6883 0.1376  -0.1558 -0.1399 60  PHE B CD1 
5212  C CD2 . PHE B 60  ? 1.1318 0.8912 0.7263 0.1184  -0.1411 -0.1216 60  PHE B CD2 
5213  C CE1 . PHE B 60  ? 1.1177 0.8501 0.6966 0.1493  -0.1544 -0.1384 60  PHE B CE1 
5214  C CE2 . PHE B 60  ? 1.1392 0.9176 0.7447 0.1281  -0.1355 -0.1177 60  PHE B CE2 
5215  C CZ  . PHE B 60  ? 1.1310 0.8946 0.7239 0.1449  -0.1424 -0.1256 60  PHE B CZ  
5216  N N   . HIS B 61  ? 1.2633 0.8698 0.7619 0.1145  -0.1601 -0.1378 61  HIS B N   
5217  C CA  . HIS B 61  ? 1.2979 0.8668 0.7605 0.1156  -0.1627 -0.1335 61  HIS B CA  
5218  C C   . HIS B 61  ? 1.3299 0.8472 0.7840 0.0983  -0.1473 -0.1356 61  HIS B C   
5219  O O   . HIS B 61  ? 1.3728 0.8499 0.7902 0.0974  -0.1442 -0.1294 61  HIS B O   
5220  C CB  . HIS B 61  ? 1.3018 0.8836 0.7471 0.1124  -0.1673 -0.1260 61  HIS B CB  
5221  C CG  . HIS B 61  ? 1.2783 0.9159 0.7492 0.1231  -0.1766 -0.1238 61  HIS B CG  
5222  N ND1 . HIS B 61  ? 1.2778 0.9385 0.7532 0.1477  -0.1886 -0.1230 61  HIS B ND1 
5223  C CD2 . HIS B 61  ? 1.2655 0.9392 0.7627 0.1123  -0.1729 -0.1220 61  HIS B CD2 
5224  C CE1 . HIS B 61  ? 1.2696 0.9796 0.7749 0.1512  -0.1891 -0.1196 61  HIS B CE1 
5225  N NE2 . HIS B 61  ? 1.2641 0.9822 0.7842 0.1293  -0.1804 -0.1187 61  HIS B NE2 
5226  N N   . VAL B 62  ? 1.1073 1.0036 0.7992 0.1761  0.0307  0.2160  62  VAL B N   
5227  C CA  . VAL B 62  ? 1.1444 0.9702 0.8318 0.1682  0.0568  0.2086  62  VAL B CA  
5228  C C   . VAL B 62  ? 1.1519 0.9867 0.8717 0.1628  0.0619  0.1983  62  VAL B C   
5229  O O   . VAL B 62  ? 1.1211 1.0107 0.8852 0.1519  0.0488  0.1996  62  VAL B O   
5230  C CB  . VAL B 62  ? 1.1411 0.9553 0.8550 0.1473  0.0626  0.2107  62  VAL B CB  
5231  C CG1 . VAL B 62  ? 1.1797 0.9484 0.9057 0.1347  0.0915  0.1985  62  VAL B CG1 
5232  C CG2 . VAL B 62  ? 1.1491 0.9431 0.8262 0.1569  0.0577  0.2158  62  VAL B CG2 
5233  N N   . THR B 63  ? 1.1857 0.9623 0.8813 0.1693  0.0784  0.1889  63  THR B N   
5234  C CA  . THR B 63  ? 1.2096 0.9861 0.9383 0.1644  0.0818  0.1750  63  THR B CA  
5235  C C   . THR B 63  ? 1.2651 0.9804 1.0033 0.1419  0.1120  0.1687  63  THR B C   
5236  O O   . THR B 63  ? 1.2920 0.9461 0.9845 0.1391  0.1314  0.1756  63  THR B O   
5237  C CB  . THR B 63  ? 1.2365 1.0061 0.9350 0.1927  0.0666  0.1652  63  THR B CB  
5238  O OG1 . THR B 63  ? 1.3018 0.9799 0.9500 0.1974  0.0799  0.1646  63  THR B OG1 
5239  C CG2 . THR B 63  ? 1.1996 1.0280 0.8744 0.2181  0.0422  0.1692  63  THR B CG2 
5240  N N   . CYS B 64  ? 1.1993 0.9364 0.9964 0.1253  0.1160  0.1550  64  CYS B N   
5241  C CA  . CYS B 64  ? 1.2507 0.9521 1.0745 0.1000  0.1450  0.1434  64  CYS B CA  
5242  C C   . CYS B 64  ? 1.2984 0.9777 1.1427 0.0967  0.1462  0.1275  64  CYS B C   
5243  O O   . CYS B 64  ? 1.2914 0.9964 1.1422 0.1167  0.1207  0.1204  64  CYS B O   
5244  C CB  . CYS B 64  ? 1.2432 0.9896 1.1282 0.0841  0.1455  0.1322  64  CYS B CB  
5245  S SG  . CYS B 64  ? 1.2072 0.9681 1.0785 0.0844  0.1413  0.1440  64  CYS B SG  
5246  N N   . ASN B 65  ? 1.2735 0.9088 1.1296 0.0702  0.1760  0.1204  65  ASN B N   
5247  C CA  . ASN B 65  ? 1.3127 0.9270 1.2030 0.0590  0.1775  0.1022  65  ASN B CA  
5248  C C   . ASN B 65  ? 1.2909 0.9664 1.2664 0.0472  0.1750  0.0766  65  ASN B C   
5249  O O   . ASN B 65  ? 1.2569 0.9857 1.2569 0.0525  0.1653  0.0753  65  ASN B O   
5250  C CB  . ASN B 65  ? 1.3726 0.9076 1.2321 0.0305  0.2099  0.1101  65  ASN B CB  
5251  C CG  . ASN B 65  ? 1.3749 0.9184 1.2479 -0.0009 0.2496  0.1120  65  ASN B CG  
5252  O OD1 . ASN B 65  ? 1.3432 0.9517 1.2723 -0.0046 0.2515  0.0959  65  ASN B OD1 
5253  N ND2 . ASN B 65  ? 1.4207 0.8974 1.2379 -0.0221 0.2796  0.1308  65  ASN B ND2 
5254  N N   . SER B 66  ? 1.2659 0.9302 1.2876 0.0318  0.1794  0.0545  66  SER B N   
5255  C CA  . SER B 66  ? 1.2393 0.9615 1.3426 0.0263  0.1712  0.0246  66  SER B CA  
5256  C C   . SER B 66  ? 1.2388 0.9912 1.3811 0.0036  0.1965  0.0146  66  SER B C   
5257  O O   . SER B 66  ? 1.2022 1.0086 1.4037 0.0081  0.1816  -0.0090 66  SER B O   
5258  C CB  . SER B 66  ? 1.2594 0.9610 1.4066 0.0141  0.1695  -0.0007 66  SER B CB  
5259  O OG  . SER B 66  ? 1.3176 0.9500 1.4406 -0.0172 0.2003  0.0093  66  SER B OG  
5260  N N   . ASP B 67  ? 1.2572 0.9771 1.3647 -0.0173 0.2315  0.0294  67  ASP B N   
5261  C CA  . ASP B 67  ? 1.2684 1.0238 1.4098 -0.0354 0.2569  0.0153  67  ASP B CA  
5262  C C   . ASP B 67  ? 1.2476 1.0250 1.3596 -0.0144 0.2434  0.0282  67  ASP B C   
5263  O O   . ASP B 67  ? 1.2526 1.0546 1.3806 -0.0231 0.2615  0.0163  67  ASP B O   
5264  C CB  . ASP B 67  ? 1.2978 1.0144 1.4166 -0.0716 0.3051  0.0230  67  ASP B CB  
5265  C CG  . ASP B 67  ? 1.3142 1.0149 1.4791 -0.1030 0.3203  0.0063  67  ASP B CG  
5266  O OD1 . ASP B 67  ? 1.2969 1.0334 1.5292 -0.0954 0.2959  -0.0225 67  ASP B OD1 
5267  O OD2 . ASP B 67  ? 1.3505 1.0008 1.4830 -0.1365 0.3551  0.0223  67  ASP B OD2 
5268  N N   . ASN B 68  ? 1.2311 1.0044 1.3032 0.0126  0.2109  0.0496  68  ASN B N   
5269  C CA  . ASN B 68  ? 1.2038 0.9936 1.2490 0.0294  0.1928  0.0645  68  ASN B CA  
5270  C C   . ASN B 68  ? 1.2195 0.9754 1.2076 0.0247  0.2195  0.0808  68  ASN B C   
5271  O O   . ASN B 68  ? 1.2136 0.9859 1.1955 0.0325  0.2124  0.0813  68  ASN B O   
5272  C CB  . ASN B 68  ? 1.1840 1.0234 1.2890 0.0325  0.1730  0.0410  68  ASN B CB  
5273  C CG  . ASN B 68  ? 1.1493 1.0196 1.3024 0.0404  0.1430  0.0258  68  ASN B CG  
5274  O OD1 . ASN B 68  ? 1.1495 1.0304 1.3522 0.0303  0.1529  -0.0011 68  ASN B OD1 
5275  N ND2 . ASN B 68  ? 1.1167 1.0037 1.2546 0.0572  0.1060  0.0433  68  ASN B ND2 
5276  N N   . SER B 69  ? 1.3393 1.0427 1.2812 0.0133  0.2467  0.0941  69  SER B N   
5277  C CA  . SER B 69  ? 1.3404 1.0019 1.2109 0.0130  0.2690  0.1143  69  SER B CA  
5278  C C   . SER B 69  ? 1.3075 0.9316 1.1097 0.0381  0.2459  0.1402  69  SER B C   
5279  O O   . SER B 69  ? 1.3108 0.9142 1.1050 0.0450  0.2319  0.1437  69  SER B O   
5280  C CB  . SER B 69  ? 1.3824 1.0030 1.2354 -0.0187 0.3141  0.1159  69  SER B CB  
5281  O OG  . SER B 69  ? 1.4009 0.9825 1.1779 -0.0183 0.3365  0.1361  69  SER B OG  
5282  N N   . VAL B 70  ? 1.4248 1.0443 1.1802 0.0548  0.2391  0.1536  70  VAL B N   
5283  C CA  . VAL B 70  ? 1.3813 0.9822 1.0816 0.0819  0.2127  0.1721  70  VAL B CA  
5284  C C   . VAL B 70  ? 1.4211 0.9459 1.0523 0.0841  0.2256  0.1859  70  VAL B C   
5285  O O   . VAL B 70  ? 1.4633 0.9382 1.0519 0.0689  0.2571  0.1942  70  VAL B O   
5286  C CB  . VAL B 70  ? 1.3375 0.9519 1.0102 0.0976  0.2008  0.1792  70  VAL B CB  
5287  C CG1 . VAL B 70  ? 1.3020 0.8941 0.9121 0.1248  0.1792  0.1953  70  VAL B CG1 
5288  C CG2 . VAL B 70  ? 1.3000 0.9784 1.0363 0.0972  0.1749  0.1692  70  VAL B CG2 
5289  N N   . THR B 71  ? 1.4375 0.9525 1.0533 0.1042  0.1993  0.1883  71  THR B N   
5290  C CA  . THR B 71  ? 1.4860 0.9206 1.0333 0.1136  0.1988  0.1986  71  THR B CA  
5291  C C   . THR B 71  ? 1.4566 0.8817 0.9441 0.1532  0.1676  0.2057  71  THR B C   
5292  O O   . THR B 71  ? 1.5020 0.8485 0.9154 0.1667  0.1644  0.2153  71  THR B O   
5293  C CB  . THR B 71  ? 1.5320 0.9524 1.1122 0.1070  0.1907  0.1863  71  THR B CB  
5294  O OG1 . THR B 71  ? 1.4921 0.9790 1.1091 0.1326  0.1558  0.1732  71  THR B OG1 
5295  C CG2 . THR B 71  ? 1.5620 0.9980 1.2093 0.0674  0.2198  0.1744  71  THR B CG2 
5296  N N   . ARG B 72  ? 1.4541 0.9559 0.9711 0.1712  0.1429  0.2007  72  ARG B N   
5297  C CA  . ARG B 72  ? 1.4233 0.9349 0.8953 0.2074  0.1134  0.2024  72  ARG B CA  
5298  C C   . ARG B 72  ? 1.3522 0.9263 0.8428 0.2098  0.1042  0.2062  72  ARG B C   
5299  O O   . ARG B 72  ? 1.3167 0.9461 0.8692 0.1893  0.1066  0.2046  72  ARG B O   
5300  C CB  . ARG B 72  ? 1.4199 0.9727 0.9126 0.2294  0.0843  0.1882  72  ARG B CB  
5301  C CG  . ARG B 72  ? 1.4133 0.9736 0.8569 0.2708  0.0536  0.1825  72  ARG B CG  
5302  C CD  . ARG B 72  ? 1.4258 1.0214 0.8848 0.2958  0.0270  0.1626  72  ARG B CD  
5303  N NE  . ARG B 72  ? 1.4641 1.0119 0.8553 0.3381  0.0003  0.1517  72  ARG B NE  
5304  C CZ  . ARG B 72  ? 1.5393 1.0016 0.8911 0.3529  -0.0111 0.1432  72  ARG B CZ  
5305  N NH1 . ARG B 72  ? 1.5839 1.0051 0.9632 0.3262  0.0034  0.1436  72  ARG B NH1 
5306  N NH2 . ARG B 72  ? 1.5779 0.9918 0.8620 0.3960  -0.0416 0.1322  72  ARG B NH2 
5307  N N   . VAL B 73  ? 1.4600 1.0191 0.8958 0.2356  0.0899  0.2099  73  VAL B N   
5308  C CA  . VAL B 73  ? 1.3987 1.0179 0.8509 0.2419  0.0721  0.2111  73  VAL B CA  
5309  C C   . VAL B 73  ? 1.3872 1.0296 0.8066 0.2781  0.0416  0.2036  73  VAL B C   
5310  O O   . VAL B 73  ? 1.4208 1.0046 0.7702 0.3048  0.0357  0.2024  73  VAL B O   
5311  C CB  . VAL B 73  ? 1.4056 0.9868 0.8271 0.2377  0.0863  0.2170  73  VAL B CB  
5312  C CG1 . VAL B 73  ? 1.3518 0.9915 0.7955 0.2441  0.0611  0.2157  73  VAL B CG1 
5313  C CG2 . VAL B 73  ? 1.4271 0.9958 0.8831 0.2056  0.1169  0.2175  73  VAL B CG2 
5314  N N   . ASP B 74  ? 1.3674 1.0979 0.8341 0.2809  0.0215  0.1969  74  ASP B N   
5315  C CA  . ASP B 74  ? 1.3587 1.1341 0.8056 0.3162  -0.0072 0.1829  74  ASP B CA  
5316  C C   . ASP B 74  ? 1.3080 1.1562 0.7772 0.3143  -0.0239 0.1849  74  ASP B C   
5317  O O   . ASP B 74  ? 1.2637 1.2074 0.7883 0.2977  -0.0339 0.1876  74  ASP B O   
5318  C CB  . ASP B 74  ? 1.3509 1.1913 0.8341 0.3216  -0.0177 0.1711  74  ASP B CB  
5319  C CG  . ASP B 74  ? 1.4101 1.1795 0.8787 0.3230  -0.0068 0.1659  74  ASP B CG  
5320  O OD1 . ASP B 74  ? 1.4659 1.1655 0.8760 0.3534  -0.0174 0.1555  74  ASP B OD1 
5321  O OD2 . ASP B 74  ? 1.4076 1.1870 0.9232 0.2935  0.0094  0.1716  74  ASP B OD2 
5322  N N   . LEU B 75  ? 1.4089 1.2092 0.8320 0.3297  -0.0279 0.1846  75  LEU B N   
5323  C CA  . LEU B 75  ? 1.3742 1.2319 0.8175 0.3284  -0.0466 0.1839  75  LEU B CA  
5324  C C   . LEU B 75  ? 1.3871 1.2554 0.7863 0.3725  -0.0728 0.1637  75  LEU B C   
5325  O O   . LEU B 75  ? 1.3830 1.2601 0.7739 0.3812  -0.0878 0.1592  75  LEU B O   
5326  C CB  . LEU B 75  ? 1.3775 1.1828 0.8138 0.3114  -0.0350 0.1946  75  LEU B CB  
5327  C CG  . LEU B 75  ? 1.3497 1.1842 0.8518 0.2687  -0.0260 0.2082  75  LEU B CG  
5328  C CD1 . LEU B 75  ? 1.3629 1.1435 0.8516 0.2622  -0.0180 0.2103  75  LEU B CD1 
5329  C CD2 . LEU B 75  ? 1.3099 1.2446 0.8729 0.2491  -0.0498 0.2132  75  LEU B CD2 
5330  N N   . GLY B 76  ? 1.4456 1.3119 0.8168 0.4043  -0.0830 0.1473  76  GLY B N   
5331  C CA  . GLY B 76  ? 1.4780 1.3539 0.8062 0.4531  -0.1133 0.1219  76  GLY B CA  
5332  C C   . GLY B 76  ? 1.4269 1.4431 0.8154 0.4521  -0.1348 0.1072  76  GLY B C   
5333  O O   . GLY B 76  ? 1.3787 1.4912 0.8298 0.4262  -0.1301 0.1113  76  GLY B O   
5334  N N   . ASN B 77  ? 1.4600 1.4896 0.8277 0.4796  -0.1586 0.0899  77  ASN B N   
5335  C CA  . ASN B 77  ? 1.4227 1.5892 0.8465 0.4802  -0.1810 0.0713  77  ASN B CA  
5336  C C   . ASN B 77  ? 1.3862 1.6328 0.8911 0.4183  -0.1684 0.0976  77  ASN B C   
5337  O O   . ASN B 77  ? 1.3580 1.7249 0.9218 0.3962  -0.1696 0.0976  77  ASN B O   
5338  C CB  . ASN B 77  ? 1.4154 1.6673 0.8484 0.5128  -0.1967 0.0413  77  ASN B CB  
5339  C CG  . ASN B 77  ? 1.4015 1.7457 0.8434 0.5498  -0.2299 0.0033  77  ASN B CG  
5340  O OD1 . ASN B 77  ? 1.4276 1.6999 0.8197 0.5922  -0.2463 -0.0238 77  ASN B OD1 
5341  N ND2 . ASN B 77  ? 1.3602 1.8593 0.8801 0.5216  -0.2319 -0.0012 77  ASN B ND2 
5342  N N   . ALA B 78  ? 1.3970 1.5744 0.9006 0.3910  -0.1580 0.1201  78  ALA B N   
5343  C CA  . ALA B 78  ? 1.3753 1.5990 0.9462 0.3342  -0.1521 0.1464  78  ALA B CA  
5344  C C   . ALA B 78  ? 1.3747 1.6310 0.9738 0.3222  -0.1756 0.1434  78  ALA B C   
5345  O O   . ALA B 78  ? 1.3691 1.6492 1.0201 0.2749  -0.1779 0.1655  78  ALA B O   
5346  C CB  . ALA B 78  ? 1.3823 1.5105 0.9426 0.3104  -0.1273 0.1700  78  ALA B CB  
5347  N N   . ASN B 79  ? 1.3819 1.6350 0.9474 0.3649  -0.1974 0.1151  79  ASN B N   
5348  C CA  . ASN B 79  ? 1.3839 1.6624 0.9741 0.3600  -0.2241 0.1059  79  ASN B CA  
5349  C C   . ASN B 79  ? 1.3975 1.5886 0.9832 0.3385  -0.2211 0.1244  79  ASN B C   
5350  O O   . ASN B 79  ? 1.4002 1.6209 1.0331 0.3110  -0.2422 0.1279  79  ASN B O   
5351  C CB  . ASN B 79  ? 1.3662 1.7871 1.0418 0.3189  -0.2385 0.1085  79  ASN B CB  
5352  C CG  . ASN B 79  ? 1.3488 1.8776 1.0322 0.3499  -0.2490 0.0768  79  ASN B CG  
5353  O OD1 . ASN B 79  ? 1.3540 1.8466 0.9799 0.4101  -0.2604 0.0449  79  ASN B OD1 
5354  N ND2 . ASN B 79  ? 1.3301 1.9935 1.0822 0.3098  -0.2469 0.0845  79  ASN B ND2 
5355  N N   . LEU B 80  ? 1.5083 1.5946 1.0393 0.3505  -0.1965 0.1340  80  LEU B N   
5356  C CA  . LEU B 80  ? 1.5224 1.5308 1.0438 0.3379  -0.1915 0.1447  80  LEU B CA  
5357  C C   . LEU B 80  ? 1.5427 1.4982 1.0113 0.3792  -0.2110 0.1226  80  LEU B C   
5358  O O   . LEU B 80  ? 1.5514 1.4766 0.9549 0.4259  -0.2145 0.1047  80  LEU B O   
5359  C CB  . LEU B 80  ? 1.5226 1.4525 1.0075 0.3348  -0.1549 0.1595  80  LEU B CB  
5360  C CG  . LEU B 80  ? 1.5016 1.4709 1.0371 0.2955  -0.1366 0.1799  80  LEU B CG  
5361  C CD1 . LEU B 80  ? 1.5047 1.3992 0.9999 0.3006  -0.1020 0.1868  80  LEU B CD1 
5362  C CD2 . LEU B 80  ? 1.5021 1.5010 1.1054 0.2493  -0.1489 0.1962  80  LEU B CD2 
5363  N N   . SER B 81  ? 1.5581 1.4983 1.0514 0.3649  -0.2279 0.1221  81  SER B N   
5364  C CA  . SER B 81  ? 1.5820 1.4693 1.0249 0.4047  -0.2472 0.1000  81  SER B CA  
5365  C C   . SER B 81  ? 1.6045 1.4224 1.0336 0.3972  -0.2361 0.1061  81  SER B C   
5366  O O   . SER B 81  ? 1.5992 1.4316 1.0871 0.3559  -0.2344 0.1212  81  SER B O   
5367  C CB  . SER B 81  ? 1.5820 1.5373 1.0761 0.4036  -0.2918 0.0805  81  SER B CB  
5368  O OG  . SER B 81  ? 1.6115 1.5137 1.0535 0.4478  -0.3134 0.0554  81  SER B OG  
5369  N N   . GLY B 82  ? 1.7106 1.4551 1.0588 0.4393  -0.2302 0.0927  82  GLY B N   
5370  C CA  . GLY B 82  ? 1.7465 1.4339 1.0734 0.4391  -0.2160 0.0928  82  GLY B CA  
5371  C C   . GLY B 82  ? 1.7966 1.4039 1.0165 0.4748  -0.1824 0.0935  82  GLY B C   
5372  O O   . GLY B 82  ? 1.8075 1.3893 0.9608 0.5105  -0.1862 0.0878  82  GLY B O   
5373  N N   . GLN B 83  ? 1.7826 1.3519 0.9867 0.4638  -0.1513 0.1002  83  GLN B N   
5374  C CA  . GLN B 83  ? 1.8474 1.3440 0.9516 0.4871  -0.1138 0.1055  83  GLN B CA  
5375  C C   . GLN B 83  ? 1.8591 1.3437 0.9756 0.4515  -0.0667 0.1263  83  GLN B C   
5376  O O   . GLN B 83  ? 1.8405 1.3651 1.0372 0.4172  -0.0647 0.1281  83  GLN B O   
5377  C CB  . GLN B 83  ? 1.9167 1.3844 0.9761 0.5158  -0.1193 0.0855  83  GLN B CB  
5378  C CG  . GLN B 83  ? 1.8978 1.3952 0.9883 0.5389  -0.1743 0.0582  83  GLN B CG  
5379  C CD  . GLN B 83  ? 1.9709 1.4242 0.9765 0.5875  -0.1818 0.0365  83  GLN B CD  
5380  O OE1 . GLN B 83  ? 2.0403 1.4563 0.9849 0.5945  -0.1446 0.0400  83  GLN B OE1 
5381  N NE2 . GLN B 83  ? 1.9600 1.4230 0.9611 0.6212  -0.2295 0.0124  83  GLN B NE2 
5382  N N   . LEU B 84  ? 1.8486 1.2732 0.8832 0.4600  -0.0319 0.1416  84  LEU B N   
5383  C CA  . LEU B 84  ? 1.8657 1.2746 0.9073 0.4260  0.0144  0.1595  84  LEU B CA  
5384  C C   . LEU B 84  ? 1.9260 1.3423 0.9802 0.4150  0.0371  0.1495  84  LEU B C   
5385  O O   . LEU B 84  ? 1.9658 1.3855 1.0029 0.4399  0.0195  0.1297  84  LEU B O   
5386  C CB  . LEU B 84  ? 1.8966 1.2288 0.8407 0.4355  0.0429  0.1792  84  LEU B CB  
5387  C CG  . LEU B 84  ? 1.8526 1.1798 0.8121 0.4226  0.0434  0.1932  84  LEU B CG  
5388  C CD1 . LEU B 84  ? 1.7905 1.1687 0.7896 0.4420  -0.0030 0.1800  84  LEU B CD1 
5389  C CD2 . LEU B 84  ? 1.9227 1.1631 0.7899 0.4298  0.0651  0.2076  84  LEU B CD2 
5390  N N   . VAL B 85  ? 1.7421 1.1667 0.8305 0.3799  0.0741  0.1587  85  VAL B N   
5391  C CA  . VAL B 85  ? 1.7885 1.2402 0.9118 0.3661  0.0941  0.1434  85  VAL B CA  
5392  C C   . VAL B 85  ? 1.8191 1.2418 0.9007 0.3440  0.1523  0.1574  85  VAL B C   
5393  O O   . VAL B 85  ? 1.7907 1.1930 0.8742 0.3207  0.1712  0.1781  85  VAL B O   
5394  C CB  . VAL B 85  ? 1.7558 1.2673 0.9938 0.3403  0.0697  0.1339  85  VAL B CB  
5395  C CG1 . VAL B 85  ? 1.7976 1.3341 1.0791 0.3180  0.0985  0.1220  85  VAL B CG1 
5396  C CG2 . VAL B 85  ? 1.7512 1.2882 1.0236 0.3595  0.0172  0.1143  85  VAL B CG2 
5397  N N   . MET B 86  ? 1.9083 1.3331 0.9531 0.3504  0.1802  0.1449  86  MET B N   
5398  C CA  . MET B 86  ? 1.9319 1.3317 0.9286 0.3249  0.2395  0.1612  86  MET B CA  
5399  C C   . MET B 86  ? 1.9039 1.3403 0.9873 0.2810  0.2632  0.1620  86  MET B C   
5400  O O   . MET B 86  ? 1.9100 1.3182 0.9654 0.2515  0.3066  0.1819  86  MET B O   
5401  C CB  . MET B 86  ? 1.9876 1.3998 0.9290 0.3393  0.2684  0.1452  86  MET B CB  
5402  C CG  . MET B 86  ? 1.9985 1.4907 1.0161 0.3417  0.2663  0.1045  86  MET B CG  
5403  S SD  . MET B 86  ? 1.9723 1.5359 1.1041 0.2979  0.2948  0.0864  86  MET B SD  
5404  C CE  . MET B 86  ? 1.9753 1.5051 1.0567 0.2509  0.3661  0.1221  86  MET B CE  
5405  N N   . GLN B 87  ? 1.7638 1.2573 0.9495 0.2754  0.2328  0.1413  87  GLN B N   
5406  C CA  . GLN B 87  ? 1.7403 1.2726 1.0118 0.2397  0.2485  0.1363  87  GLN B CA  
5407  C C   . GLN B 87  ? 1.6969 1.1971 0.9714 0.2173  0.2549  0.1637  87  GLN B C   
5408  O O   . GLN B 87  ? 1.6761 1.2025 1.0169 0.1886  0.2669  0.1610  87  GLN B O   
5409  C CB  . GLN B 87  ? 1.7358 1.3231 1.1031 0.2439  0.2045  0.1107  87  GLN B CB  
5410  C CG  . GLN B 87  ? 1.7771 1.4010 1.1598 0.2669  0.1909  0.0743  87  GLN B CG  
5411  C CD  . GLN B 87  ? 1.8085 1.4090 1.1285 0.3060  0.1633  0.0690  87  GLN B CD  
5412  O OE1 . GLN B 87  ? 1.8108 1.3650 1.0458 0.3182  0.1767  0.0900  87  GLN B OE1 
5413  N NE2 . GLN B 87  ? 1.8312 1.4592 1.1927 0.3280  0.1195  0.0385  87  GLN B NE2 
5414  N N   . LEU B 88  ? 1.8260 1.2707 1.0304 0.2343  0.2425  0.1858  88  LEU B N   
5415  C CA  . LEU B 88  ? 1.7916 1.2023 0.9914 0.2194  0.2455  0.2071  88  LEU B CA  
5416  C C   . LEU B 88  ? 1.8240 1.1983 0.9970 0.1864  0.2955  0.2213  88  LEU B C   
5417  O O   . LEU B 88  ? 1.8055 1.1599 0.9973 0.1680  0.2981  0.2325  88  LEU B O   
5418  C CB  . LEU B 88  ? 1.7796 1.1376 0.9039 0.2512  0.2181  0.2216  88  LEU B CB  
5419  C CG  . LEU B 88  ? 1.7309 1.1310 0.8923 0.2767  0.1669  0.2099  88  LEU B CG  
5420  C CD1 . LEU B 88  ? 1.7294 1.0823 0.8093 0.3138  0.1424  0.2166  88  LEU B CD1 
5421  C CD2 . LEU B 88  ? 1.6681 1.1163 0.9149 0.2576  0.1504  0.2095  88  LEU B CD2 
5422  N N   . GLY B 89  ? 1.8440 1.2121 0.9737 0.1775  0.3347  0.2202  89  GLY B N   
5423  C CA  . GLY B 89  ? 1.8765 1.2203 0.9869 0.1374  0.3865  0.2343  89  GLY B CA  
5424  C C   . GLY B 89  ? 1.8595 1.2728 1.0747 0.1022  0.4082  0.2133  89  GLY B C   
5425  O O   . GLY B 89  ? 1.8837 1.2892 1.0966 0.0636  0.4529  0.2213  89  GLY B O   
5426  N N   . GLN B 90  ? 1.6710 1.1504 0.9778 0.1132  0.3757  0.1865  90  GLN B N   
5427  C CA  . GLN B 90  ? 1.6561 1.2027 1.0646 0.0876  0.3870  0.1610  90  GLN B CA  
5428  C C   . GLN B 90  ? 1.6248 1.1651 1.0886 0.0696  0.3732  0.1676  90  GLN B C   
5429  O O   . GLN B 90  ? 1.6083 1.2043 1.1616 0.0565  0.3685  0.1442  90  GLN B O   
5430  C CB  . GLN B 90  ? 1.6480 1.2605 1.1197 0.1112  0.3536  0.1276  90  GLN B CB  
5431  C CG  . GLN B 90  ? 1.6802 1.2975 1.0977 0.1405  0.3519  0.1166  90  GLN B CG  
5432  C CD  . GLN B 90  ? 1.7006 1.3736 1.1341 0.1306  0.3916  0.0880  90  GLN B CD  
5433  O OE1 . GLN B 90  ? 1.6907 1.4274 1.1984 0.1395  0.3742  0.0502  90  GLN B OE1 
5434  N NE2 . GLN B 90  ? 1.7294 1.3798 1.0908 0.1124  0.4438  0.1050  90  GLN B NE2 
5435  N N   . LEU B 91  ? 1.6645 1.1395 1.0761 0.0737  0.3622  0.1950  91  LEU B N   
5436  C CA  . LEU B 91  ? 1.6421 1.1111 1.0995 0.0608  0.3486  0.1983  91  LEU B CA  
5437  C C   . LEU B 91  ? 1.6832 1.0883 1.0999 0.0302  0.3827  0.2175  91  LEU B C   
5438  O O   . LEU B 91  ? 1.6977 1.0280 1.0434 0.0412  0.3707  0.2408  91  LEU B O   
5439  C CB  . LEU B 91  ? 1.6016 1.0556 1.0416 0.0925  0.3017  0.2083  91  LEU B CB  
5440  C CG  . LEU B 91  ? 1.5577 1.0697 1.0409 0.1159  0.2616  0.1957  91  LEU B CG  
5441  C CD1 . LEU B 91  ? 1.5598 1.1375 1.1304 0.1013  0.2624  0.1708  91  LEU B CD1 
5442  C CD2 . LEU B 91  ? 1.5667 1.0616 0.9866 0.1436  0.2504  0.2000  91  LEU B CD2 
5443  N N   . PRO B 92  ? 1.6658 1.0969 1.1266 -0.0088 0.4224  0.2068  92  PRO B N   
5444  C CA  . PRO B 92  ? 1.7153 1.0799 1.1332 -0.0464 0.4575  0.2292  92  PRO B CA  
5445  C C   . PRO B 92  ? 1.7240 1.0277 1.1381 -0.0460 0.4304  0.2415  92  PRO B C   
5446  O O   . PRO B 92  ? 1.7738 0.9861 1.1131 -0.0599 0.4398  0.2690  92  PRO B O   
5447  C CB  . PRO B 92  ? 1.7190 1.1531 1.2179 -0.0883 0.4984  0.2051  92  PRO B CB  
5448  C CG  . PRO B 92  ? 1.6707 1.1934 1.2686 -0.0674 0.4687  0.1683  92  PRO B CG  
5449  C CD  . PRO B 92  ? 1.6470 1.1699 1.2068 -0.0210 0.4313  0.1716  92  PRO B CD  
5450  N N   . ASN B 93  ? 1.6684 1.0171 1.1556 -0.0284 0.3940  0.2217  93  ASN B N   
5451  C CA  . ASN B 93  ? 1.6787 0.9859 1.1726 -0.0239 0.3664  0.2251  93  ASN B CA  
5452  C C   . ASN B 93  ? 1.6503 0.9321 1.0939 0.0234  0.3208  0.2335  93  ASN B C   
5453  O O   . ASN B 93  ? 1.6515 0.9152 1.1045 0.0371  0.2913  0.2297  93  ASN B O   
5454  C CB  . ASN B 93  ? 1.6613 1.0397 1.2658 -0.0342 0.3562  0.1957  93  ASN B CB  
5455  C CG  . ASN B 93  ? 1.6915 1.0914 1.3523 -0.0822 0.3977  0.1825  93  ASN B CG  
5456  O OD1 . ASN B 93  ? 1.7398 1.0783 1.3790 -0.1147 0.4178  0.1956  93  ASN B OD1 
5457  N ND2 . ASN B 93  ? 1.6624 1.1496 1.3968 -0.0876 0.4084  0.1551  93  ASN B ND2 
5458  N N   . LEU B 94  ? 1.7626 1.0472 1.1546 0.0500  0.3134  0.2414  94  LEU B N   
5459  C CA  . LEU B 94  ? 1.7266 1.0051 1.0809 0.0945  0.2705  0.2444  94  LEU B CA  
5460  C C   . LEU B 94  ? 1.7749 0.9520 1.0406 0.1085  0.2576  0.2621  94  LEU B C   
5461  O O   . LEU B 94  ? 1.8317 0.9363 1.0088 0.1092  0.2719  0.2822  94  LEU B O   
5462  C CB  . LEU B 94  ? 1.6965 1.0042 1.0245 0.1160  0.2661  0.2450  94  LEU B CB  
5463  C CG  . LEU B 94  ? 1.6705 0.9650 0.9424 0.1595  0.2291  0.2495  94  LEU B CG  
5464  C CD1 . LEU B 94  ? 1.6010 0.9709 0.9374 0.1773  0.1917  0.2354  94  LEU B CD1 
5465  C CD2 . LEU B 94  ? 1.6713 0.9738 0.9083 0.1704  0.2367  0.2509  94  LEU B CD2 
5466  N N   . GLN B 95  ? 1.8075 0.9776 1.0929 0.1228  0.2270  0.2530  95  GLN B N   
5467  C CA  . GLN B 95  ? 1.8644 0.9343 1.0734 0.1395  0.2057  0.2633  95  GLN B CA  
5468  C C   . GLN B 95  ? 1.8432 0.9044 0.9926 0.1936  0.1644  0.2603  95  GLN B C   
5469  O O   . GLN B 95  ? 1.8990 0.8620 0.9540 0.2122  0.1507  0.2737  95  GLN B O   
5470  C CB  . GLN B 95  ? 1.8845 0.9520 1.1461 0.1332  0.1882  0.2479  95  GLN B CB  
5471  C CG  . GLN B 95  ? 1.9065 0.9884 1.2371 0.0806  0.2248  0.2450  95  GLN B CG  
5472  C CD  . GLN B 95  ? 1.9169 1.0145 1.3130 0.0794  0.2028  0.2229  95  GLN B CD  
5473  O OE1 . GLN B 95  ? 1.9226 1.0007 1.2987 0.1167  0.1608  0.2122  95  GLN B OE1 
5474  N NE2 . GLN B 95  ? 1.9219 1.0582 1.3973 0.0395  0.2289  0.2118  95  GLN B NE2 
5475  N N   . TYR B 96  ? 1.8265 0.8143 0.9957 0.4999  -0.0357 0.0682  96  TYR B N   
5476  C CA  . TYR B 96  ? 1.8286 0.8710 0.9605 0.5367  -0.0650 0.0792  96  TYR B CA  
5477  C C   . TYR B 96  ? 1.7818 0.8924 0.9397 0.5224  -0.0945 0.0826  96  TYR B C   
5478  O O   . TYR B 96  ? 1.7158 0.8781 0.9398 0.4864  -0.1135 0.0779  96  TYR B O   
5479  C CB  . TYR B 96  ? 1.7953 0.8976 0.9514 0.5449  -0.0841 0.0767  96  TYR B CB  
5480  C CG  . TYR B 96  ? 1.8537 0.8819 0.9733 0.5619  -0.0574 0.0718  96  TYR B CG  
5481  C CD1 . TYR B 96  ? 1.8455 0.8331 1.0035 0.5258  -0.0376 0.0601  96  TYR B CD1 
5482  C CD2 . TYR B 96  ? 1.9255 0.9220 0.9700 0.6150  -0.0542 0.0769  96  TYR B CD2 
5483  C CE1 . TYR B 96  ? 1.9081 0.8214 1.0279 0.5354  -0.0132 0.0538  96  TYR B CE1 
5484  C CE2 . TYR B 96  ? 1.9938 0.9070 0.9939 0.6305  -0.0300 0.0718  96  TYR B CE2 
5485  C CZ  . TYR B 96  ? 1.9852 0.8550 1.0218 0.5870  -0.0085 0.0603  96  TYR B CZ  
5486  O OH  . TYR B 96  ? 2.0616 0.8428 1.0497 0.5966  0.0156  0.0535  96  TYR B OH  
5487  N N   . LEU B 97  ? 1.8514 0.9548 0.9503 0.5504  -0.1004 0.0903  97  LEU B N   
5488  C CA  . LEU B 97  ? 1.8528 1.0115 0.9627 0.5369  -0.1281 0.0920  97  LEU B CA  
5489  C C   . LEU B 97  ? 1.8468 1.0828 0.9293 0.5707  -0.1598 0.0975  97  LEU B C   
5490  O O   . LEU B 97  ? 1.8801 1.0840 0.8920 0.6142  -0.1577 0.1028  97  LEU B O   
5491  C CB  . LEU B 97  ? 1.8977 0.9796 0.9632 0.5351  -0.1062 0.0918  97  LEU B CB  
5492  C CG  . LEU B 97  ? 1.9065 1.0167 0.9953 0.5060  -0.1250 0.0876  97  LEU B CG  
5493  C CD1 . LEU B 97  ? 1.9492 0.9760 1.0166 0.4947  -0.0913 0.0808  97  LEU B CD1 
5494  C CD2 . LEU B 97  ? 1.9223 1.0788 0.9633 0.5302  -0.1553 0.0941  97  LEU B CD2 
5495  N N   . GLU B 98  ? 1.7957 1.1348 0.9321 0.5507  -0.1893 0.0951  98  GLU B N   
5496  C CA  . GLU B 98  ? 1.7738 1.2116 0.9033 0.5775  -0.2175 0.0950  98  GLU B CA  
5497  C C   . GLU B 98  ? 1.7603 1.2711 0.9069 0.5473  -0.2486 0.0938  98  GLU B C   
5498  O O   . GLU B 98  ? 1.7350 1.3082 0.9331 0.5018  -0.2652 0.0915  98  GLU B O   
5499  C CB  . GLU B 98  ? 1.7432 1.2485 0.9163 0.5736  -0.2221 0.0906  98  GLU B CB  
5500  C CG  . GLU B 98  ? 1.7595 1.1863 0.9252 0.5860  -0.1924 0.0891  98  GLU B CG  
5501  C CD  . GLU B 98  ? 1.7958 1.1409 0.8864 0.6433  -0.1727 0.0920  98  GLU B CD  
5502  O OE1 . GLU B 98  ? 1.8237 1.2114 0.8779 0.6907  -0.1893 0.0925  98  GLU B OE1 
5503  O OE2 . GLU B 98  ? 1.8256 1.0629 0.8913 0.6405  -0.1414 0.0928  98  GLU B OE2 
5504  N N   . LEU B 99  ? 1.7956 1.2919 0.8906 0.5710  -0.2576 0.0951  99  LEU B N   
5505  C CA  . LEU B 99  ? 1.7911 1.3573 0.8929 0.5449  -0.2897 0.0914  99  LEU B CA  
5506  C C   . LEU B 99  ? 1.7849 1.4473 0.8677 0.5846  -0.3182 0.0869  99  LEU B C   
5507  O O   . LEU B 99  ? 1.7969 1.5071 0.8687 0.5725  -0.3451 0.0822  99  LEU B O   
5508  C CB  . LEU B 99  ? 1.8412 1.3210 0.9021 0.5316  -0.2826 0.0922  99  LEU B CB  
5509  C CG  . LEU B 99  ? 1.8510 1.2829 0.9475 0.4784  -0.2733 0.0898  99  LEU B CG  
5510  C CD1 . LEU B 99  ? 1.9141 1.2323 0.9651 0.4869  -0.2444 0.0890  99  LEU B CD1 
5511  C CD2 . LEU B 99  ? 1.8444 1.3399 0.9623 0.4329  -0.3068 0.0851  99  LEU B CD2 
5512  N N   . TYR B 100 ? 1.7784 1.4723 0.8578 0.6333  -0.3146 0.0857  100 TYR B N   
5513  C CA  . TYR B 100 ? 1.8155 1.5947 0.8740 0.6865  -0.3415 0.0790  100 TYR B CA  
5514  C C   . TYR B 100 ? 1.7615 1.7060 0.8862 0.6529  -0.3727 0.0660  100 TYR B C   
5515  O O   . TYR B 100 ? 1.6995 1.6868 0.8806 0.5928  -0.3695 0.0645  100 TYR B O   
5516  C CB  . TYR B 100 ? 1.8527 1.6094 0.8861 0.7527  -0.3275 0.0792  100 TYR B CB  
5517  C CG  . TYR B 100 ? 1.7939 1.6029 0.8877 0.7361  -0.3142 0.0737  100 TYR B CG  
5518  C CD1 . TYR B 100 ? 1.7563 1.7180 0.9045 0.7387  -0.3340 0.0599  100 TYR B CD1 
5519  C CD2 . TYR B 100 ? 1.7821 1.4912 0.8772 0.7167  -0.2812 0.0802  100 TYR B CD2 
5520  C CE1 . TYR B 100 ? 1.7122 1.7172 0.9061 0.7227  -0.3196 0.0542  100 TYR B CE1 
5521  C CE2 . TYR B 100 ? 1.7372 1.4890 0.8789 0.7018  -0.2716 0.0745  100 TYR B CE2 
5522  C CZ  . TYR B 100 ? 1.7046 1.5999 0.8911 0.7054  -0.2900 0.0623  100 TYR B CZ  
5523  O OH  . TYR B 100 ? 1.6967 1.6308 0.9209 0.6895  -0.2782 0.0560  100 TYR B OH  
5524  N N   . SER B 101 ? 1.7949 1.8316 0.9085 0.6915  -0.4039 0.0559  101 SER B N   
5525  C CA  . SER B 101 ? 1.7556 1.9697 0.9335 0.6667  -0.4331 0.0387  101 SER B CA  
5526  C C   . SER B 101 ? 1.7149 1.9571 0.9258 0.5763  -0.4430 0.0376  101 SER B C   
5527  O O   . SER B 101 ? 1.6613 1.9691 0.9278 0.5194  -0.4383 0.0343  101 SER B O   
5528  C CB  . SER B 101 ? 1.7152 2.0190 0.9478 0.6786  -0.4209 0.0301  101 SER B CB  
5529  O OG  . SER B 101 ? 1.6690 2.1374 0.9711 0.6296  -0.4382 0.0142  101 SER B OG  
5530  N N   . ASN B 102 ? 1.7536 1.9346 0.9192 0.5640  -0.4567 0.0403  102 ASN B N   
5531  C CA  . ASN B 102 ? 1.7367 1.9290 0.9177 0.4844  -0.4701 0.0374  102 ASN B CA  
5532  C C   . ASN B 102 ? 1.7937 2.0042 0.9318 0.4939  -0.5029 0.0284  102 ASN B C   
5533  O O   . ASN B 102 ? 1.8425 2.0699 0.9443 0.5623  -0.5179 0.0246  102 ASN B O   
5534  C CB  . ASN B 102 ? 1.7238 1.7718 0.8899 0.4457  -0.4426 0.0516  102 ASN B CB  
5535  C CG  . ASN B 102 ? 1.6667 1.7171 0.8819 0.4181  -0.4205 0.0575  102 ASN B CG  
5536  O OD1 . ASN B 102 ? 1.6329 1.7660 0.8918 0.3633  -0.4301 0.0530  102 ASN B OD1 
5537  N ND2 . ASN B 102 ? 1.6645 1.6197 0.8670 0.4524  -0.3907 0.0671  102 ASN B ND2 
5538  N N   . ASN B 103 ? 1.7976 1.9977 0.9329 0.4259  -0.5165 0.0243  103 ASN B N   
5539  C CA  . ASN B 103 ? 1.8560 2.0642 0.9468 0.4215  -0.5486 0.0138  103 ASN B CA  
5540  C C   . ASN B 103 ? 1.8965 1.9398 0.9222 0.4059  -0.5334 0.0229  103 ASN B C   
5541  O O   . ASN B 103 ? 1.9296 1.9572 0.9302 0.3606  -0.5528 0.0143  103 ASN B O   
5542  C CB  . ASN B 103 ? 1.8424 2.1870 0.9799 0.3515  -0.5801 -0.0043 103 ASN B CB  
5543  C CG  . ASN B 103 ? 1.9059 2.2921 1.0044 0.3542  -0.6206 -0.0205 103 ASN B CG  
5544  O OD1 . ASN B 103 ? 1.9462 2.3549 1.0186 0.4229  -0.6353 -0.0243 103 ASN B OD1 
5545  N ND2 . ASN B 103 ? 1.9243 2.3106 1.0170 0.2766  -0.6375 -0.0299 103 ASN B ND2 
5546  N N   . ILE B 104 ? 1.8994 1.8201 0.8980 0.4420  -0.4968 0.0380  104 ILE B N   
5547  C CA  . ILE B 104 ? 1.9367 1.7073 0.8813 0.4318  -0.4747 0.0439  104 ILE B CA  
5548  C C   . ILE B 104 ? 2.0241 1.7441 0.8821 0.4767  -0.4862 0.0414  104 ILE B C   
5549  O O   . ILE B 104 ? 2.0580 1.8048 0.8867 0.5394  -0.4950 0.0439  104 ILE B O   
5550  C CB  . ILE B 104 ? 1.9196 1.5921 0.8750 0.4491  -0.4295 0.0576  104 ILE B CB  
5551  C CG1 . ILE B 104 ? 1.8631 1.5968 0.8983 0.4125  -0.4242 0.0601  104 ILE B CG1 
5552  C CG2 . ILE B 104 ? 1.9791 1.5160 0.8972 0.4313  -0.4041 0.0589  104 ILE B CG2 
5553  C CD1 . ILE B 104 ? 1.8514 1.5215 0.9041 0.4380  -0.3871 0.0706  104 ILE B CD1 
5554  N N   . THR B 105 ? 2.0704 1.7116 0.8801 0.4471  -0.4878 0.0358  105 THR B N   
5555  C CA  . THR B 105 ? 2.1648 1.7498 0.8812 0.4800  -0.5003 0.0318  105 THR B CA  
5556  C C   . THR B 105 ? 2.2100 1.6325 0.8664 0.4857  -0.4565 0.0380  105 THR B C   
5557  O O   . THR B 105 ? 2.1706 1.5359 0.8658 0.4705  -0.4188 0.0444  105 THR B O   
5558  C CB  . THR B 105 ? 2.1969 1.8474 0.9009 0.4373  -0.5459 0.0134  105 THR B CB  
5559  O OG1 . THR B 105 ? 2.2182 1.7726 0.8984 0.3866  -0.5333 0.0074  105 THR B OG1 
5560  C CG2 . THR B 105 ? 2.1306 1.9420 0.9227 0.3970  -0.5766 0.0040  105 THR B CG2 
5561  N N   . GLY B 106 ? 2.3165 1.6702 0.8778 0.5078  -0.4619 0.0341  106 GLY B N   
5562  C CA  . GLY B 106 ? 2.3740 1.5801 0.8699 0.5136  -0.4177 0.0367  106 GLY B CA  
5563  C C   . GLY B 106 ? 2.4192 1.5475 0.8610 0.5718  -0.3820 0.0531  106 GLY B C   
5564  O O   . GLY B 106 ? 2.4329 1.6081 0.8660 0.6167  -0.3976 0.0609  106 GLY B O   
5565  N N   . THR B 107 ? 2.5244 1.5337 0.9383 0.5668  -0.3291 0.0554  107 THR B N   
5566  C CA  . THR B 107 ? 2.5720 1.4842 0.9212 0.6100  -0.2866 0.0698  107 THR B CA  
5567  C C   . THR B 107 ? 2.5372 1.4325 0.9645 0.5984  -0.2426 0.0757  107 THR B C   
5568  O O   . THR B 107 ? 2.4897 1.4390 1.0160 0.5594  -0.2442 0.0687  107 THR B O   
5569  C CB  . THR B 107 ? 2.6872 1.4709 0.9275 0.6131  -0.2538 0.0660  107 THR B CB  
5570  O OG1 . THR B 107 ? 2.7458 1.4310 0.9081 0.6524  -0.2135 0.0820  107 THR B OG1 
5571  C CG2 . THR B 107 ? 2.7218 1.4625 1.0102 0.5658  -0.2160 0.0510  107 THR B CG2 
5572  N N   . ILE B 108 ? 2.5933 1.4057 0.9655 0.6326  -0.2049 0.0887  108 ILE B N   
5573  C CA  . ILE B 108 ? 2.5771 1.3572 1.0067 0.6227  -0.1587 0.0929  108 ILE B CA  
5574  C C   . ILE B 108 ? 2.6638 1.3465 1.0763 0.5946  -0.1035 0.0830  108 ILE B C   
5575  O O   . ILE B 108 ? 2.7559 1.3389 1.0606 0.6109  -0.0754 0.0863  108 ILE B O   
5576  C CB  . ILE B 108 ? 2.5830 1.3185 0.9556 0.6712  -0.1464 0.1102  108 ILE B CB  
5577  C CG1 . ILE B 108 ? 2.5076 1.3540 0.9090 0.7043  -0.2008 0.1150  108 ILE B CG1 
5578  C CG2 . ILE B 108 ? 2.5727 1.2610 0.9904 0.6568  -0.0962 0.1125  108 ILE B CG2 
5579  C CD1 . ILE B 108 ? 2.5596 1.3811 0.9310 0.7476  -0.1882 0.1194  108 ILE B CD1 
5580  N N   . PRO B 109 ? 2.5751 1.2832 1.0861 0.5543  -0.0873 0.0697  109 PRO B N   
5581  C CA  . PRO B 109 ? 2.6489 1.2797 1.1544 0.5311  -0.0354 0.0548  109 PRO B CA  
5582  C C   . PRO B 109 ? 2.6523 1.2099 1.1439 0.5360  0.0246  0.0596  109 PRO B C   
5583  O O   . PRO B 109 ? 2.5678 1.1575 1.1322 0.5313  0.0314  0.0634  109 PRO B O   
5584  C CB  . PRO B 109 ? 2.5914 1.2853 1.2140 0.4944  -0.0486 0.0390  109 PRO B CB  
5585  C CG  . PRO B 109 ? 2.4904 1.2762 1.1861 0.4947  -0.0867 0.0502  109 PRO B CG  
5586  C CD  . PRO B 109 ? 2.4810 1.2917 1.1077 0.5295  -0.1194 0.0660  109 PRO B CD  
5587  N N   . GLU B 110 ? 2.7844 1.2413 1.1838 0.5385  0.0717  0.0567  110 GLU B N   
5588  C CA  . GLU B 110 ? 2.7968 1.1734 1.1622 0.5389  0.1307  0.0628  110 GLU B CA  
5589  C C   . GLU B 110 ? 2.6978 1.1058 1.1860 0.5049  0.1663  0.0467  110 GLU B C   
5590  O O   . GLU B 110 ? 2.6912 1.0497 1.1716 0.4985  0.2107  0.0503  110 GLU B O   
5591  C CB  . GLU B 110 ? 2.9260 1.1869 1.1651 0.5397  0.1796  0.0608  110 GLU B CB  
5592  C CG  . GLU B 110 ? 2.9325 1.1857 1.2099 0.5066  0.2191  0.0329  110 GLU B CG  
5593  C CD  . GLU B 110 ? 3.0669 1.2089 1.2058 0.5086  0.2640  0.0309  110 GLU B CD  
5594  O OE1 . GLU B 110 ? 3.1446 1.1941 1.1855 0.5166  0.3018  0.0472  110 GLU B OE1 
5595  O OE2 . GLU B 110 ? 3.1064 1.2452 1.2253 0.5017  0.2617  0.0132  110 GLU B OE2 
5596  N N   . GLN B 111 ? 2.6564 1.1418 1.2535 0.4831  0.1451  0.0287  111 GLN B N   
5597  C CA  . GLN B 111 ? 2.5542 1.0791 1.2727 0.4563  0.1685  0.0121  111 GLN B CA  
5598  C C   . GLN B 111 ? 2.4713 1.0425 1.2492 0.4593  0.1494  0.0249  111 GLN B C   
5599  O O   . GLN B 111 ? 2.3935 0.9929 1.2651 0.4377  0.1684  0.0118  111 GLN B O   
5600  C CB  . GLN B 111 ? 2.5051 1.0909 1.3108 0.4400  0.1416  -0.0084 111 GLN B CB  
5601  C CG  . GLN B 111 ? 2.5733 1.1108 1.3333 0.4352  0.1687  -0.0282 111 GLN B CG  
5602  C CD  . GLN B 111 ? 2.6213 1.0837 1.3337 0.4277  0.2444  -0.0379 111 GLN B CD  
5603  O OE1 . GLN B 111 ? 2.7282 1.1135 1.3174 0.4386  0.2665  -0.0284 111 GLN B OE1 
5604  N NE2 . GLN B 111 ? 2.5574 1.0424 1.3645 0.4070  0.2843  -0.0575 111 GLN B NE2 
5605  N N   . LEU B 112 ? 2.5133 1.0978 1.2416 0.4870  0.1110  0.0472  112 LEU B N   
5606  C CA  . LEU B 112 ? 2.4421 1.0581 1.2129 0.4933  0.1005  0.0575  112 LEU B CA  
5607  C C   . LEU B 112 ? 2.4623 0.9939 1.1931 0.4903  0.1564  0.0599  112 LEU B C   
5608  O O   . LEU B 112 ? 2.4033 0.9517 1.1800 0.4866  0.1576  0.0619  112 LEU B O   
5609  C CB  . LEU B 112 ? 2.4457 1.1025 1.1756 0.5283  0.0488  0.0769  112 LEU B CB  
5610  C CG  . LEU B 112 ? 2.4338 1.1790 1.1910 0.5288  -0.0095 0.0765  112 LEU B CG  
5611  C CD1 . LEU B 112 ? 2.5045 1.2291 1.1569 0.5627  -0.0323 0.0875  112 LEU B CD1 
5612  C CD2 . LEU B 112 ? 2.3499 1.1916 1.1862 0.5267  -0.0484 0.0806  112 LEU B CD2 
5613  N N   . GLY B 113 ? 2.5624 0.9981 1.2011 0.4886  0.2035  0.0592  113 GLY B N   
5614  C CA  . GLY B 113 ? 2.6091 0.9571 1.2092 0.4727  0.2648  0.0585  113 GLY B CA  
5615  C C   . GLY B 113 ? 2.5463 0.9297 1.2638 0.4283  0.3026  0.0327  113 GLY B C   
5616  O O   . GLY B 113 ? 2.5868 0.9121 1.2901 0.4067  0.3519  0.0290  113 GLY B O   
5617  N N   . ASN B 114 ? 2.4724 0.9472 1.3022 0.4143  0.2789  0.0138  114 ASN B N   
5618  C CA  . ASN B 114 ? 2.4049 0.9309 1.3593 0.3798  0.3025  -0.0132 114 ASN B CA  
5619  C C   . ASN B 114 ? 2.3123 0.8969 1.3499 0.3753  0.2724  -0.0109 114 ASN B C   
5620  O O   . ASN B 114 ? 2.2587 0.8909 1.4022 0.3487  0.2846  -0.0334 114 ASN B O   
5621  C CB  . ASN B 114 ? 2.3645 0.9529 1.3945 0.3744  0.2845  -0.0347 114 ASN B CB  
5622  C CG  . ASN B 114 ? 2.4499 0.9850 1.4278 0.3667  0.3345  -0.0508 114 ASN B CG  
5623  O OD1 . ASN B 114 ? 2.5443 0.9981 1.4377 0.3578  0.3892  -0.0474 114 ASN B OD1 
5624  N ND2 . ASN B 114 ? 2.4321 1.0052 1.4521 0.3694  0.3171  -0.0686 114 ASN B ND2 
5625  N N   . LEU B 115 ? 1.9003 1.3434 1.1969 0.1772  0.5200  0.1623  115 LEU B N   
5626  C CA  . LEU B 115 ? 1.8664 1.3054 1.2047 0.1681  0.4987  0.1741  115 LEU B CA  
5627  C C   . LEU B 115 ? 1.8753 1.2538 1.1790 0.1592  0.5239  0.1995  115 LEU B C   
5628  O O   . LEU B 115 ? 1.8884 1.2270 1.1240 0.1779  0.5168  0.2182  115 LEU B O   
5629  C CB  . LEU B 115 ? 1.8501 1.3076 1.1626 0.1931  0.4590  0.1769  115 LEU B CB  
5630  C CG  . LEU B 115 ? 1.8460 1.3634 1.1953 0.1993  0.4280  0.1561  115 LEU B CG  
5631  C CD1 . LEU B 115 ? 1.8334 1.3685 1.1433 0.2269  0.3939  0.1633  115 LEU B CD1 
5632  C CD2 . LEU B 115 ? 1.8268 1.3851 1.2802 0.1716  0.4115  0.1436  115 LEU B CD2 
5633  N N   . THR B 116 ? 1.9147 1.2861 1.2713 0.1297  0.5512  0.2001  116 THR B N   
5634  C CA  . THR B 116 ? 1.9286 1.2427 1.2587 0.1156  0.5769  0.2258  116 THR B CA  
5635  C C   . THR B 116 ? 1.9180 1.1944 1.2323 0.1220  0.5512  0.2424  116 THR B C   
5636  O O   . THR B 116 ? 1.9494 1.1704 1.1917 0.1338  0.5547  0.2642  116 THR B O   
5637  C CB  . THR B 116 ? 1.9129 1.2369 1.3241 0.0806  0.6033  0.2224  116 THR B CB  
5638  O OG1 . THR B 116 ? 1.9339 1.2884 1.3483 0.0783  0.6341  0.2069  116 THR B OG1 
5639  C CG2 . THR B 116 ? 1.9214 1.1857 1.3151 0.0621  0.6227  0.2523  116 THR B CG2 
5640  N N   . GLU B 117 ? 1.8947 1.1999 1.2733 0.1152  0.5233  0.2317  117 GLU B N   
5641  C CA  . GLU B 117 ? 1.8870 1.1665 1.2490 0.1258  0.4968  0.2412  117 GLU B CA  
5642  C C   . GLU B 117 ? 1.8820 1.1985 1.2138 0.1577  0.4671  0.2317  117 GLU B C   
5643  O O   . GLU B 117 ? 1.8560 1.2331 1.2346 0.1555  0.4510  0.2147  117 GLU B O   
5644  C CB  . GLU B 117 ? 1.8470 1.1361 1.2894 0.0988  0.4834  0.2372  117 GLU B CB  
5645  C CG  . GLU B 117 ? 1.8590 1.0922 1.2750 0.1016  0.4710  0.2519  117 GLU B CG  
5646  C CD  . GLU B 117 ? 1.8764 1.1096 1.2362 0.1383  0.4430  0.2503  117 GLU B CD  
5647  O OE1 . GLU B 117 ? 1.8647 1.1507 1.2173 0.1585  0.4284  0.2390  117 GLU B OE1 
5648  O OE2 . GLU B 117 ? 1.9044 1.0840 1.2291 0.1474  0.4344  0.2601  117 GLU B OE2 
5649  N N   . LEU B 118 ? 1.9389 1.2189 1.1964 0.1868  0.4575  0.2436  118 LEU B N   
5650  C CA  . LEU B 118 ? 1.9352 1.2487 1.1564 0.2204  0.4331  0.2372  118 LEU B CA  
5651  C C   . LEU B 118 ? 1.9652 1.2352 1.1223 0.2512  0.4181  0.2487  118 LEU B C   
5652  O O   . LEU B 118 ? 2.0107 1.2138 1.1099 0.2567  0.4313  0.2653  118 LEU B O   
5653  C CB  . LEU B 118 ? 1.9511 1.2759 1.1353 0.2292  0.4459  0.2337  118 LEU B CB  
5654  C CG  . LEU B 118 ? 1.9424 1.3090 1.0992 0.2587  0.4205  0.2256  118 LEU B CG  
5655  C CD1 . LEU B 118 ? 1.9748 1.2971 1.0480 0.2927  0.4109  0.2407  118 LEU B CD1 
5656  C CD2 . LEU B 118 ? 1.8968 1.3291 1.1241 0.2541  0.3911  0.2132  118 LEU B CD2 
5657  N N   . VAL B 119 ? 1.9221 1.2299 1.0887 0.2718  0.3899  0.2406  119 VAL B N   
5658  C CA  . VAL B 119 ? 1.9585 1.2303 1.0721 0.3048  0.3740  0.2463  119 VAL B CA  
5659  C C   . VAL B 119 ? 1.9553 1.2641 1.0323 0.3431  0.3534  0.2425  119 VAL B C   
5660  O O   . VAL B 119 ? 2.0007 1.2639 1.0102 0.3717  0.3493  0.2519  119 VAL B O   
5661  C CB  . VAL B 119 ? 1.9537 1.2323 1.1046 0.3002  0.3600  0.2392  119 VAL B CB  
5662  C CG1 . VAL B 119 ? 1.9902 1.2599 1.0956 0.3429  0.3381  0.2360  119 VAL B CG1 
5663  C CG2 . VAL B 119 ? 1.9772 1.1900 1.1407 0.2708  0.3760  0.2483  119 VAL B CG2 
5664  N N   . SER B 120 ? 1.9571 1.3481 1.0803 0.3427  0.3375  0.2306  120 SER B N   
5665  C CA  . SER B 120 ? 1.9457 1.3835 1.0477 0.3767  0.3144  0.2276  120 SER B CA  
5666  C C   . SER B 120 ? 1.9166 1.4012 1.0348 0.3681  0.3109  0.2235  120 SER B C   
5667  O O   . SER B 120 ? 1.8835 1.4093 1.0637 0.3378  0.3121  0.2157  120 SER B O   
5668  C CB  . SER B 120 ? 1.9156 1.4169 1.0571 0.3871  0.2929  0.2189  120 SER B CB  
5669  O OG  . SER B 120 ? 1.9198 1.4532 1.0321 0.4271  0.2725  0.2183  120 SER B OG  
5670  N N   . LEU B 121 ? 1.9470 1.4239 1.0104 0.3958  0.3021  0.2279  121 LEU B N   
5671  C CA  . LEU B 121 ? 1.9327 1.4508 1.0010 0.3946  0.2919  0.2228  121 LEU B CA  
5672  C C   . LEU B 121 ? 1.9228 1.4863 0.9773 0.4291  0.2605  0.2242  121 LEU B C   
5673  O O   . LEU B 121 ? 1.9603 1.4858 0.9499 0.4599  0.2547  0.2323  121 LEU B O   
5674  C CB  . LEU B 121 ? 1.9767 1.4377 0.9856 0.3918  0.3128  0.2275  121 LEU B CB  
5675  C CG  . LEU B 121 ? 1.9752 1.4378 1.0179 0.3570  0.3361  0.2181  121 LEU B CG  
5676  C CD1 . LEU B 121 ? 1.9559 1.4839 1.0431 0.3504  0.3159  0.2028  121 LEU B CD1 
5677  C CD2 . LEU B 121 ? 1.9510 1.4154 1.0552 0.3296  0.3483  0.2159  121 LEU B CD2 
5678  N N   . ASP B 122 ? 1.9099 1.5559 1.0276 0.4228  0.2385  0.2181  122 ASP B N   
5679  C CA  . ASP B 122 ? 1.8931 1.5976 1.0130 0.4524  0.2087  0.2206  122 ASP B CA  
5680  C C   . ASP B 122 ? 1.8731 1.6352 1.0244 0.4423  0.1857  0.2180  122 ASP B C   
5681  O O   . ASP B 122 ? 1.8359 1.6631 1.0571 0.4177  0.1724  0.2147  122 ASP B O   
5682  C CB  . ASP B 122 ? 1.8609 1.6195 1.0268 0.4550  0.2011  0.2188  122 ASP B CB  
5683  C CG  . ASP B 122 ? 1.8988 1.5982 1.0250 0.4752  0.2158  0.2188  122 ASP B CG  
5684  O OD1 . ASP B 122 ? 1.9205 1.5551 1.0353 0.4553  0.2388  0.2190  122 ASP B OD1 
5685  O OD2 . ASP B 122 ? 1.9143 1.6317 1.0232 0.5114  0.2026  0.2183  122 ASP B OD2 
5686  N N   . LEU B 123 ? 1.8870 1.6216 0.9844 0.4604  0.1778  0.2202  123 LEU B N   
5687  C CA  . LEU B 123 ? 1.8831 1.6619 0.9987 0.4560  0.1510  0.2170  123 LEU B CA  
5688  C C   . LEU B 123 ? 1.8794 1.6901 0.9725 0.4909  0.1196  0.2255  123 LEU B C   
5689  O O   . LEU B 123 ? 1.8896 1.7165 0.9752 0.4939  0.0954  0.2248  123 LEU B O   
5690  C CB  . LEU B 123 ? 1.9305 1.6538 1.0039 0.4448  0.1658  0.2092  123 LEU B CB  
5691  C CG  . LEU B 123 ? 1.9445 1.6333 1.0362 0.4124  0.1989  0.1992  123 LEU B CG  
5692  C CD1 . LEU B 123 ? 1.9075 1.6546 1.0934 0.3815  0.1908  0.1927  123 LEU B CD1 
5693  C CD2 . LEU B 123 ? 1.9609 1.5786 1.0063 0.4148  0.2346  0.2069  123 LEU B CD2 
5694  N N   . TYR B 124 ? 1.8783 1.6996 0.9636 0.5181  0.1173  0.2321  124 TYR B N   
5695  C CA  . TYR B 124 ? 1.8815 1.7278 0.9446 0.5554  0.0894  0.2398  124 TYR B CA  
5696  C C   . TYR B 124 ? 1.8278 1.7785 0.9612 0.5497  0.0559  0.2431  124 TYR B C   
5697  O O   . TYR B 124 ? 1.7876 1.7942 0.9884 0.5184  0.0543  0.2410  124 TYR B O   
5698  C CB  . TYR B 124 ? 1.8998 1.7271 0.9386 0.5890  0.0968  0.2422  124 TYR B CB  
5699  C CG  . TYR B 124 ? 1.8674 1.7465 0.9631 0.5819  0.1066  0.2371  124 TYR B CG  
5700  C CD1 . TYR B 124 ? 1.8776 1.7100 0.9728 0.5612  0.1359  0.2315  124 TYR B CD1 
5701  C CD2 . TYR B 124 ? 1.8295 1.8054 0.9772 0.5962  0.0865  0.2385  124 TYR B CD2 
5702  C CE1 . TYR B 124 ? 1.8542 1.7302 0.9946 0.5549  0.1429  0.2260  124 TYR B CE1 
5703  C CE2 . TYR B 124 ? 1.8075 1.8331 0.9998 0.5899  0.0968  0.2332  124 TYR B CE2 
5704  C CZ  . TYR B 124 ? 1.8218 1.7942 1.0075 0.5696  0.1240  0.2263  124 TYR B CZ  
5705  O OH  . TYR B 124 ? 1.8043 1.8222 1.0283 0.5630  0.1323  0.2203  124 TYR B OH  
5706  N N   . LEU B 125 ? 1.8635 1.8393 0.9814 0.5788  0.0263  0.2506  125 LEU B N   
5707  C CA  . LEU B 125 ? 1.8096 1.8865 0.9917 0.5771  -0.0097 0.2583  125 LEU B CA  
5708  C C   . LEU B 125 ? 1.7910 1.8940 1.0151 0.5382  -0.0269 0.2563  125 LEU B C   
5709  O O   . LEU B 125 ? 1.7421 1.9161 1.0402 0.5097  -0.0355 0.2593  125 LEU B O   
5710  C CB  . LEU B 125 ? 1.7628 1.9230 1.0059 0.5803  -0.0062 0.2612  125 LEU B CB  
5711  C CG  . LEU B 125 ? 1.7851 1.9435 1.0011 0.6264  -0.0007 0.2608  125 LEU B CG  
5712  C CD1 . LEU B 125 ? 1.7574 1.9861 1.0254 0.6249  0.0129  0.2574  125 LEU B CD1 
5713  C CD2 . LEU B 125 ? 1.7777 1.9741 0.9905 0.6596  -0.0353 0.2701  125 LEU B CD2 
5714  N N   . ASN B 126 ? 1.8021 1.8453 0.9758 0.5376  -0.0341 0.2511  126 ASN B N   
5715  C CA  . ASN B 126 ? 1.8065 1.8618 1.0114 0.5062  -0.0533 0.2443  126 ASN B CA  
5716  C C   . ASN B 126 ? 1.8478 1.8699 0.9989 0.5228  -0.0816 0.2432  126 ASN B C   
5717  O O   . ASN B 126 ? 1.8580 1.8641 0.9614 0.5562  -0.0925 0.2518  126 ASN B O   
5718  C CB  . ASN B 126 ? 1.8417 1.8446 1.0437 0.4775  -0.0188 0.2291  126 ASN B CB  
5719  C CG  . ASN B 126 ? 1.7960 1.8576 1.0847 0.4429  -0.0176 0.2292  126 ASN B CG  
5720  O OD1 . ASN B 126 ? 1.7727 1.8877 1.1220 0.4193  -0.0495 0.2305  126 ASN B OD1 
5721  N ND2 . ASN B 126 ? 1.7843 1.8332 1.0783 0.4385  0.0158  0.2288  126 ASN B ND2 
5722  N N   . ASN B 127 ? 1.8897 1.9013 1.0505 0.4996  -0.0967 0.2312  127 ASN B N   
5723  C CA  . ASN B 127 ? 1.9386 1.9174 1.0500 0.5100  -0.1262 0.2255  127 ASN B CA  
5724  C C   . ASN B 127 ? 2.0222 1.9167 1.0687 0.5028  -0.0955 0.2047  127 ASN B C   
5725  O O   . ASN B 127 ? 2.0752 1.9461 1.0972 0.4986  -0.1149 0.1904  127 ASN B O   
5726  C CB  . ASN B 127 ? 1.9023 1.9506 1.0871 0.4908  -0.1780 0.2284  127 ASN B CB  
5727  C CG  . ASN B 127 ? 1.9574 1.9712 1.0977 0.4977  -0.2147 0.2187  127 ASN B CG  
5728  O OD1 . ASN B 127 ? 2.0260 1.9876 1.1345 0.4873  -0.2065 0.1964  127 ASN B OD1 
5729  N ND2 . ASN B 127 ? 1.9303 1.9754 1.0688 0.5168  -0.2563 0.2344  127 ASN B ND2 
5730  N N   . LEU B 128 ? 2.0261 1.8739 1.0407 0.5025  -0.0469 0.2025  128 LEU B N   
5731  C CA  . LEU B 128 ? 2.0946 1.8722 1.0539 0.4933  -0.0128 0.1848  128 LEU B CA  
5732  C C   . LEU B 128 ? 2.1517 1.8658 1.0054 0.5183  -0.0157 0.1857  128 LEU B C   
5733  O O   . LEU B 128 ? 2.1406 1.8450 0.9536 0.5448  -0.0294 0.2031  128 LEU B O   
5734  C CB  . LEU B 128 ? 2.0836 1.8305 1.0422 0.4833  0.0382  0.1861  128 LEU B CB  
5735  C CG  . LEU B 128 ? 2.0610 1.8409 1.1045 0.4498  0.0535  0.1762  128 LEU B CG  
5736  C CD1 . LEU B 128 ? 2.0027 1.8679 1.1379 0.4380  0.0163  0.1837  128 LEU B CD1 
5737  C CD2 . LEU B 128 ? 2.0426 1.7886 1.0804 0.4431  0.0998  0.1810  128 LEU B CD2 
5738  N N   . SER B 129 ? 2.2108 1.8820 1.0195 0.5099  -0.0031 0.1659  129 SER B N   
5739  C CA  . SER B 129 ? 2.2720 1.8826 0.9742 0.5292  -0.0053 0.1646  129 SER B CA  
5740  C C   . SER B 129 ? 2.3220 1.8736 0.9651 0.5181  0.0464  0.1510  129 SER B C   
5741  O O   . SER B 129 ? 2.3087 1.8691 1.0010 0.4960  0.0800  0.1407  129 SER B O   
5742  C CB  . SER B 129 ? 2.3062 1.9334 1.0048 0.5341  -0.0559 0.1520  129 SER B CB  
5743  O OG  . SER B 129 ? 2.3438 1.9811 1.0801 0.5129  -0.0543 0.1235  129 SER B OG  
5744  N N   . GLY B 130 ? 2.4640 1.9579 1.0011 0.5327  0.0517  0.1522  130 GLY B N   
5745  C CA  . GLY B 130 ? 2.5092 1.9510 0.9798 0.5229  0.1013  0.1425  130 GLY B CA  
5746  C C   . GLY B 130 ? 2.4955 1.8925 0.9219 0.5240  0.1398  0.1682  130 GLY B C   
5747  O O   . GLY B 130 ? 2.4617 1.8597 0.8969 0.5380  0.1246  0.1915  130 GLY B O   
5748  N N   . PRO B 131 ? 2.5206 1.8787 0.9012 0.5094  0.1894  0.1641  131 PRO B N   
5749  C CA  . PRO B 131 ? 2.5227 1.8292 0.8519 0.5074  0.2242  0.1912  131 PRO B CA  
5750  C C   . PRO B 131 ? 2.4633 1.7901 0.8780 0.4914  0.2472  0.1973  131 PRO B C   
5751  O O   . PRO B 131 ? 2.4196 1.8014 0.9313 0.4807  0.2382  0.1817  131 PRO B O   
5752  C CB  . PRO B 131 ? 2.5790 1.8467 0.8305 0.4942  0.2673  0.1831  131 PRO B CB  
5753  C CG  . PRO B 131 ? 2.5759 1.8900 0.8896 0.4814  0.2726  0.1456  131 PRO B CG  
5754  C CD  . PRO B 131 ? 2.5597 1.9193 0.9299 0.4951  0.2143  0.1338  131 PRO B CD  
5755  N N   . ILE B 132 ? 2.4975 1.7751 0.8716 0.4895  0.2731  0.2221  132 ILE B N   
5756  C CA  . ILE B 132 ? 2.4424 1.7222 0.8784 0.4718  0.3013  0.2289  132 ILE B CA  
5757  C C   . ILE B 132 ? 2.4718 1.7308 0.8923 0.4442  0.3534  0.2229  132 ILE B C   
5758  O O   . ILE B 132 ? 2.5647 1.7708 0.9006 0.4409  0.3764  0.2400  132 ILE B O   
5759  C CB  . ILE B 132 ? 2.4766 1.7116 0.8809 0.4867  0.2945  0.2586  132 ILE B CB  
5760  C CG1 . ILE B 132 ? 2.4151 1.6927 0.8740 0.5104  0.2510  0.2589  132 ILE B CG1 
5761  C CG2 . ILE B 132 ? 2.4647 1.6732 0.8945 0.4646  0.3325  0.2691  132 ILE B CG2 
5762  C CD1 . ILE B 132 ? 2.4500 1.7373 0.8688 0.5374  0.2076  0.2598  132 ILE B CD1 
5763  N N   . PRO B 133 ? 2.4286 1.7310 0.9306 0.4232  0.3710  0.1993  133 PRO B N   
5764  C CA  . PRO B 133 ? 2.4488 1.7402 0.9438 0.3986  0.4214  0.1910  133 PRO B CA  
5765  C C   . PRO B 133 ? 2.4614 1.6995 0.9179 0.3855  0.4561  0.2218  133 PRO B C   
5766  O O   . PRO B 133 ? 2.4327 1.6579 0.9229 0.3848  0.4486  0.2392  133 PRO B O   
5767  C CB  . PRO B 133 ? 2.4031 1.7502 1.0158 0.3802  0.4243  0.1657  133 PRO B CB  
5768  C CG  . PRO B 133 ? 2.3709 1.7619 1.0393 0.3949  0.3719  0.1579  133 PRO B CG  
5769  C CD  . PRO B 133 ? 2.3921 1.7593 0.9844 0.4234  0.3395  0.1753  133 PRO B CD  
5770  N N   . SER B 134 ? 2.5657 1.7744 0.9531 0.3737  0.4920  0.2281  134 SER B N   
5771  C CA  . SER B 134 ? 2.5764 1.7452 0.9517 0.3513  0.5186  0.2561  134 SER B CA  
5772  C C   . SER B 134 ? 2.5461 1.7266 0.9943 0.3265  0.5554  0.2555  134 SER B C   
5773  O O   . SER B 134 ? 2.5519 1.6974 1.0017 0.3082  0.5717  0.2812  134 SER B O   
5774  C CB  . SER B 134 ? 2.6514 1.8070 0.9612 0.3375  0.5405  0.2600  134 SER B CB  
5775  O OG  . SER B 134 ? 2.6406 1.8380 0.9732 0.3250  0.5754  0.2309  134 SER B OG  
5776  N N   . THR B 135 ? 2.4590 1.6939 0.9892 0.3213  0.5587  0.2241  135 THR B N   
5777  C CA  . THR B 135 ? 2.3995 1.6555 1.0241 0.2944  0.5837  0.2188  135 THR B CA  
5778  C C   . THR B 135 ? 2.3551 1.5982 1.0318 0.2931  0.5613  0.2352  135 THR B C   
5779  O O   . THR B 135 ? 2.3287 1.5753 1.0720 0.2692  0.5810  0.2378  135 THR B O   
5780  C CB  . THR B 135 ? 2.3643 1.6838 1.0742 0.2893  0.5815  0.1784  135 THR B CB  
5781  O OG1 . THR B 135 ? 2.3534 1.6997 1.0717 0.3128  0.5333  0.1616  135 THR B OG1 
5782  C CG2 . THR B 135 ? 2.4021 1.7352 1.0809 0.2819  0.6215  0.1593  135 THR B CG2 
5783  N N   . LEU B 136 ? 2.4263 1.6567 1.0768 0.3188  0.5205  0.2447  136 LEU B N   
5784  C CA  . LEU B 136 ? 2.3935 1.6138 1.0893 0.3203  0.5013  0.2569  136 LEU B CA  
5785  C C   . LEU B 136 ? 2.4239 1.5790 1.0841 0.3077  0.5224  0.2881  136 LEU B C   
5786  O O   . LEU B 136 ? 2.4038 1.5453 1.1046 0.3052  0.5114  0.2959  136 LEU B O   
5787  C CB  . LEU B 136 ? 2.3819 1.6097 1.0594 0.3536  0.4545  0.2584  136 LEU B CB  
5788  C CG  . LEU B 136 ? 2.3749 1.6514 1.0537 0.3712  0.4264  0.2371  136 LEU B CG  
5789  C CD1 . LEU B 136 ? 2.3804 1.6480 1.0160 0.4047  0.3864  0.2485  136 LEU B CD1 
5790  C CD2 . LEU B 136 ? 2.3251 1.6694 1.1079 0.3587  0.4143  0.2116  136 LEU B CD2 
5791  N N   . GLY B 137 ? 2.4486 1.5629 1.0325 0.2987  0.5506  0.3066  137 GLY B N   
5792  C CA  . GLY B 137 ? 2.4839 1.5374 1.0404 0.2801  0.5710  0.3390  137 GLY B CA  
5793  C C   . GLY B 137 ? 2.4569 1.5239 1.0946 0.2456  0.6018  0.3370  137 GLY B C   
5794  O O   . GLY B 137 ? 2.4806 1.4974 1.1100 0.2284  0.6127  0.3644  137 GLY B O   
5795  N N   . ARG B 138 ? 2.3829 1.5136 1.1008 0.2349  0.6122  0.3063  138 ARG B N   
5796  C CA  . ARG B 138 ? 2.3549 1.5014 1.1600 0.2030  0.6365  0.3029  138 ARG B CA  
5797  C C   . ARG B 138 ? 2.3145 1.4598 1.1877 0.2032  0.6071  0.3010  138 ARG B C   
5798  O O   . ARG B 138 ? 2.2987 1.4382 1.2330 0.1766  0.6215  0.3062  138 ARG B O   
5799  C CB  . ARG B 138 ? 2.3317 1.5445 1.1989 0.1920  0.6570  0.2696  138 ARG B CB  
5800  C CG  . ARG B 138 ? 2.3665 1.5945 1.1645 0.2042  0.6732  0.2581  138 ARG B CG  
5801  C CD  . ARG B 138 ? 2.3760 1.6389 1.2064 0.1815  0.7206  0.2431  138 ARG B CD  
5802  N NE  . ARG B 138 ? 2.3323 1.6544 1.2686 0.1768  0.7134  0.2061  138 ARG B NE  
5803  C CZ  . ARG B 138 ? 2.3089 1.6533 1.3367 0.1503  0.7349  0.2002  138 ARG B CZ  
5804  N NH1 . ARG B 138 ? 2.3215 1.6374 1.3515 0.1247  0.7666  0.2287  138 ARG B NH1 
5805  N NH2 . ARG B 138 ? 2.2747 1.6698 1.3964 0.1481  0.7211  0.1663  138 ARG B NH2 
5806  N N   . LEU B 139 ? 2.3018 1.4555 1.1664 0.2322  0.5665  0.2934  139 LEU B N   
5807  C CA  . LEU B 139 ? 2.2683 1.4245 1.1872 0.2357  0.5386  0.2907  139 LEU B CA  
5808  C C   . LEU B 139 ? 2.3069 1.3887 1.1740 0.2426  0.5305  0.3188  139 LEU B C   
5809  O O   . LEU B 139 ? 2.3204 1.3825 1.1463 0.2731  0.5000  0.3231  139 LEU B O   
5810  C CB  . LEU B 139 ? 2.2356 1.4403 1.1687 0.2634  0.5008  0.2715  139 LEU B CB  
5811  C CG  . LEU B 139 ? 2.2197 1.4838 1.1690 0.2680  0.4970  0.2477  139 LEU B CG  
5812  C CD1 . LEU B 139 ? 2.1963 1.4971 1.1447 0.2971  0.4554  0.2386  139 LEU B CD1 
5813  C CD2 . LEU B 139 ? 2.1893 1.4996 1.2322 0.2394  0.5099  0.2273  139 LEU B CD2 
5814  N N   . LYS B 140 ? 2.3181 1.3586 1.1925 0.2134  0.5565  0.3380  140 LYS B N   
5815  C CA  . LYS B 140 ? 2.3643 1.3256 1.1888 0.2163  0.5471  0.3668  140 LYS B CA  
5816  C C   . LYS B 140 ? 2.3490 1.2971 1.2079 0.2297  0.5139  0.3598  140 LYS B C   
5817  O O   . LYS B 140 ? 2.3931 1.2757 1.2058 0.2436  0.4952  0.3774  140 LYS B O   
5818  C CB  . LYS B 140 ? 2.3874 1.3104 1.2180 0.1778  0.5811  0.3915  140 LYS B CB  
5819  C CG  . LYS B 140 ? 2.4023 1.3476 1.2094 0.1588  0.6223  0.3970  140 LYS B CG  
5820  C CD  . LYS B 140 ? 2.4547 1.3726 1.1561 0.1796  0.6201  0.4121  140 LYS B CD  
5821  C CE  . LYS B 140 ? 2.4710 1.4158 1.1572 0.1552  0.6596  0.4157  140 LYS B CE  
5822  N NZ  . LYS B 140 ? 2.4896 1.4142 1.2069 0.1154  0.6833  0.4395  140 LYS B NZ  
5823  N N   . LYS B 141 ? 2.2525 1.2597 1.1899 0.2253  0.5051  0.3347  141 LYS B N   
5824  C CA  . LYS B 141 ? 2.2144 1.2190 1.1846 0.2364  0.4760  0.3256  141 LYS B CA  
5825  C C   . LYS B 141 ? 2.1990 1.2333 1.1435 0.2782  0.4437  0.3119  141 LYS B C   
5826  O O   . LYS B 141 ? 2.1732 1.2124 1.1375 0.2928  0.4198  0.3023  141 LYS B O   
5827  C CB  . LYS B 141 ? 2.1227 1.1785 1.1895 0.2088  0.4792  0.3078  141 LYS B CB  
5828  C CG  . LYS B 141 ? 2.1028 1.1642 1.2301 0.1648  0.5110  0.3114  141 LYS B CG  
5829  C CD  . LYS B 141 ? 2.1810 1.1718 1.2801 0.1428  0.5337  0.3402  141 LYS B CD  
5830  C CE  . LYS B 141 ? 2.2406 1.2282 1.2868 0.1394  0.5652  0.3534  141 LYS B CE  
5831  N NZ  . LYS B 141 ? 2.3099 1.2473 1.3428 0.1080  0.5950  0.3835  141 LYS B NZ  
5832  N N   . LEU B 142 ? 2.2213 1.2770 1.1222 0.2974  0.4427  0.3107  142 LEU B N   
5833  C CA  . LEU B 142 ? 2.2086 1.3045 1.0949 0.3346  0.4128  0.2980  142 LEU B CA  
5834  C C   . LEU B 142 ? 2.2568 1.3011 1.0957 0.3677  0.3874  0.3060  142 LEU B C   
5835  O O   . LEU B 142 ? 2.3162 1.2860 1.0915 0.3735  0.3890  0.3268  142 LEU B O   
5836  C CB  . LEU B 142 ? 2.2128 1.3275 1.0541 0.3455  0.4168  0.2986  142 LEU B CB  
5837  C CG  . LEU B 142 ? 2.2265 1.3505 1.0178 0.3869  0.3870  0.2978  142 LEU B CG  
5838  C CD1 . LEU B 142 ? 2.1783 1.3728 1.0249 0.4041  0.3604  0.2786  142 LEU B CD1 
5839  C CD2 . LEU B 142 ? 2.2322 1.3709 0.9823 0.3892  0.3935  0.2981  142 LEU B CD2 
5840  N N   . ARG B 143 ? 2.2088 1.2939 1.0800 0.3890  0.3632  0.2892  143 ARG B N   
5841  C CA  . ARG B 143 ? 2.2560 1.3094 1.0900 0.4286  0.3360  0.2886  143 ARG B CA  
5842  C C   . ARG B 143 ? 2.2480 1.3484 1.0598 0.4677  0.3133  0.2811  143 ARG B C   
5843  O O   . ARG B 143 ? 2.3011 1.3555 1.0532 0.4997  0.2965  0.2901  143 ARG B O   
5844  C CB  . ARG B 143 ? 2.2504 1.3204 1.1323 0.4293  0.3252  0.2731  143 ARG B CB  
5845  C CG  . ARG B 143 ? 2.2542 1.2813 1.1665 0.3911  0.3415  0.2787  143 ARG B CG  
5846  C CD  . ARG B 143 ? 2.2881 1.2978 1.2110 0.4069  0.3216  0.2661  143 ARG B CD  
5847  N NE  . ARG B 143 ? 2.2749 1.2653 1.2435 0.3691  0.3315  0.2661  143 ARG B NE  
5848  C CZ  . ARG B 143 ? 2.3123 1.2718 1.2863 0.3755  0.3158  0.2567  143 ARG B CZ  
5849  N NH1 . ARG B 143 ? 2.3703 1.3153 1.3074 0.4198  0.2916  0.2444  143 ARG B NH1 
5850  N NH2 . ARG B 143 ? 2.2937 1.2361 1.3114 0.3377  0.3234  0.2583  143 ARG B NH2 
5851  N N   . PHE B 144 ? 2.1649 1.3558 1.0272 0.4649  0.3092  0.2662  144 PHE B N   
5852  C CA  . PHE B 144 ? 2.1479 1.3968 1.0051 0.4999  0.2844  0.2585  144 PHE B CA  
5853  C C   . PHE B 144 ? 2.1104 1.4060 0.9747 0.4871  0.2880  0.2584  144 PHE B C   
5854  O O   . PHE B 144 ? 2.0549 1.3958 0.9738 0.4553  0.2997  0.2507  144 PHE B O   
5855  C CB  . PHE B 144 ? 2.1123 1.4357 1.0272 0.5109  0.2693  0.2410  144 PHE B CB  
5856  C CG  . PHE B 144 ? 2.1501 1.4355 1.0729 0.5110  0.2708  0.2354  144 PHE B CG  
5857  C CD1 . PHE B 144 ? 2.2277 1.4483 1.1006 0.5459  0.2575  0.2366  144 PHE B CD1 
5858  C CD2 . PHE B 144 ? 2.1145 1.4249 1.0941 0.4767  0.2820  0.2283  144 PHE B CD2 
5859  C CE1 . PHE B 144 ? 2.2728 1.4535 1.1503 0.5475  0.2555  0.2289  144 PHE B CE1 
5860  C CE2 . PHE B 144 ? 2.1565 1.4283 1.1395 0.4766  0.2807  0.2223  144 PHE B CE2 
5861  C CZ  . PHE B 144 ? 2.2380 1.4444 1.1689 0.5125  0.2676  0.2217  144 PHE B CZ  
5862  N N   . LEU B 145 ? 2.2057 1.4887 1.0157 0.5130  0.2741  0.2659  145 LEU B N   
5863  C CA  . LEU B 145 ? 2.1789 1.5010 0.9857 0.5067  0.2714  0.2642  145 LEU B CA  
5864  C C   . LEU B 145 ? 2.1784 1.5387 0.9700 0.5459  0.2378  0.2632  145 LEU B C   
5865  O O   . LEU B 145 ? 2.2477 1.5570 0.9775 0.5753  0.2247  0.2739  145 LEU B O   
5866  C CB  . LEU B 145 ? 2.2328 1.4888 0.9761 0.4916  0.2929  0.2776  145 LEU B CB  
5867  C CG  . LEU B 145 ? 2.2294 1.5165 0.9596 0.4851  0.2921  0.2727  145 LEU B CG  
5868  C CD1 . LEU B 145 ? 2.2516 1.5061 0.9672 0.4509  0.3284  0.2749  145 LEU B CD1 
5869  C CD2 . LEU B 145 ? 2.3012 1.5648 0.9588 0.5177  0.2679  0.2830  145 LEU B CD2 
5870  N N   . ARG B 146 ? 2.1444 1.5940 0.9949 0.5450  0.2216  0.2520  146 ARG B N   
5871  C CA  . ARG B 146 ? 2.1351 1.6365 0.9866 0.5789  0.1887  0.2515  146 ARG B CA  
5872  C C   . ARG B 146 ? 2.1022 1.6558 0.9737 0.5652  0.1761  0.2483  146 ARG B C   
5873  O O   . ARG B 146 ? 2.0554 1.6670 0.9919 0.5375  0.1780  0.2396  146 ARG B O   
5874  C CB  . ARG B 146 ? 2.1041 1.6744 1.0138 0.5942  0.1760  0.2427  146 ARG B CB  
5875  C CG  . ARG B 146 ? 2.1495 1.6682 1.0402 0.6111  0.1846  0.2409  146 ARG B CG  
5876  C CD  . ARG B 146 ? 2.1187 1.7107 1.0715 0.6157  0.1803  0.2281  146 ARG B CD  
5877  N NE  . ARG B 146 ? 2.1653 1.7025 1.1051 0.6210  0.1923  0.2226  146 ARG B NE  
5878  C CZ  . ARG B 146 ? 2.1533 1.6702 1.1171 0.5860  0.2129  0.2198  146 ARG B CZ  
5879  N NH1 . ARG B 146 ? 2.0957 1.6428 1.1005 0.5439  0.2250  0.2213  146 ARG B NH1 
5880  N NH2 . ARG B 146 ? 2.2063 1.6692 1.1543 0.5944  0.2184  0.2146  146 ARG B NH2 
5881  N N   . LEU B 147 ? 2.5786 1.4016 1.2229 0.4018  -0.0732 0.0697  147 LEU B N   
5882  C CA  . LEU B 147 ? 2.5482 1.4091 1.1428 0.3981  -0.1171 0.0530  147 LEU B CA  
5883  C C   . LEU B 147 ? 2.5300 1.4206 1.1217 0.4206  -0.1710 0.0867  147 LEU B C   
5884  O O   . LEU B 147 ? 2.5176 1.4340 1.0519 0.4191  -0.2077 0.0841  147 LEU B O   
5885  C CB  . LEU B 147 ? 2.5879 1.4286 1.0842 0.3881  -0.1000 0.0539  147 LEU B CB  
5886  C CG  . LEU B 147 ? 2.5962 1.4045 1.0753 0.3680  -0.0426 0.0336  147 LEU B CG  
5887  C CD1 . LEU B 147 ? 2.6238 1.4221 1.0004 0.3615  -0.0345 0.0390  147 LEU B CD1 
5888  C CD2 . LEU B 147 ? 2.4759 1.3075 1.0098 0.3483  -0.0317 -0.0221 147 LEU B CD2 
5889  N N   . ASN B 148 ? 2.5961 1.4867 1.2484 0.4410  -0.1767 0.1168  148 ASN B N   
5890  C CA  . ASN B 148 ? 2.5691 1.4868 1.2142 0.4657  -0.2227 0.1581  148 ASN B CA  
5891  C C   . ASN B 148 ? 2.4898 1.4695 1.1573 0.4599  -0.2777 0.1321  148 ASN B C   
5892  O O   . ASN B 148 ? 2.4476 1.4464 1.1481 0.4391  -0.2794 0.0835  148 ASN B O   
5893  C CB  . ASN B 148 ? 2.5346 1.4358 1.2432 0.4913  -0.2112 0.1954  148 ASN B CB  
5894  C CG  . ASN B 148 ? 2.4459 1.3624 1.2526 0.4851  -0.2010 0.1627  148 ASN B CG  
5895  O OD1 . ASN B 148 ? 2.4487 1.3413 1.2788 0.4655  -0.1594 0.1303  148 ASN B OD1 
5896  N ND2 . ASN B 148 ? 2.3544 1.3166 1.2192 0.5010  -0.2392 0.1714  148 ASN B ND2 
5897  N N   . ASN B 149 ? 2.5506 1.5631 1.1998 0.4782  -0.3232 0.1673  149 ASN B N   
5898  C CA  . ASN B 149 ? 2.4691 1.5427 1.1344 0.4734  -0.3803 0.1515  149 ASN B CA  
5899  C C   . ASN B 149 ? 2.4630 1.5469 1.0812 0.4447  -0.3926 0.1021  149 ASN B C   
5900  O O   . ASN B 149 ? 2.3930 1.4996 1.0565 0.4274  -0.4044 0.0589  149 ASN B O   
5901  C CB  . ASN B 149 ? 2.3725 1.4770 1.1421 0.4776  -0.3905 0.1394  149 ASN B CB  
5902  C CG  . ASN B 149 ? 2.3604 1.4805 1.1687 0.5100  -0.4053 0.1908  149 ASN B CG  
5903  O OD1 . ASN B 149 ? 2.4160 1.4960 1.2062 0.5307  -0.3774 0.2309  149 ASN B OD1 
5904  N ND2 . ASN B 149 ? 2.2902 1.4757 1.1614 0.5109  -0.4453 0.1885  149 ASN B ND2 
5905  N N   . ASN B 150 ? 2.5393 1.6062 1.0644 0.4405  -0.3894 0.1099  150 ASN B N   
5906  C CA  . ASN B 150 ? 2.5336 1.6044 1.0019 0.4162  -0.3973 0.0645  150 ASN B CA  
5907  C C   . ASN B 150 ? 2.6078 1.6993 0.9986 0.4147  -0.4193 0.0864  150 ASN B C   
5908  O O   . ASN B 150 ? 2.6537 1.7597 1.0398 0.4312  -0.4271 0.1369  150 ASN B O   
5909  C CB  . ASN B 150 ? 2.5579 1.5850 1.0152 0.4016  -0.3416 0.0330  150 ASN B CB  
5910  C CG  . ASN B 150 ? 2.4782 1.5122 1.0105 0.3860  -0.3305 -0.0151 150 ASN B CG  
5911  O OD1 . ASN B 150 ? 2.4064 1.4557 0.9280 0.3684  -0.3468 -0.0588 150 ASN B OD1 
5912  N ND2 . ASN B 150 ? 2.4829 1.5059 1.0921 0.3923  -0.3024 -0.0072 150 ASN B ND2 
5913  N N   . SER B 151 ? 2.5550 1.6619 0.9128 0.3891  -0.4212 0.0456  151 SER B N   
5914  C CA  . SER B 151 ? 2.6286 1.7690 0.9334 0.3780  -0.4337 0.0563  151 SER B CA  
5915  C C   . SER B 151 ? 2.6955 1.7959 0.9196 0.3751  -0.3943 0.0543  151 SER B C   
5916  O O   . SER B 151 ? 2.7406 1.8674 0.9230 0.3575  -0.3982 0.0387  151 SER B O   
5917  C CB  . SER B 151 ? 2.6004 1.7947 0.9327 0.3497  -0.4644 0.0150  151 SER B CB  
5918  O OG  . SER B 151 ? 2.6710 1.9070 0.9579 0.3394  -0.4821 0.0299  151 SER B OG  
5919  N N   . LEU B 152 ? 2.7409 1.7807 0.9450 0.3904  -0.3544 0.0699  152 LEU B N   
5920  C CA  . LEU B 152 ? 2.7990 1.8031 0.9338 0.3851  -0.3116 0.0693  152 LEU B CA  
5921  C C   . LEU B 152 ? 2.8896 1.9106 0.9698 0.3915  -0.3163 0.1182  152 LEU B C   
5922  O O   . LEU B 152 ? 2.9099 1.9439 1.0072 0.4098  -0.3357 0.1676  152 LEU B O   
5923  C CB  . LEU B 152 ? 2.7805 1.7263 0.9341 0.3934  -0.2623 0.0775  152 LEU B CB  
5924  C CG  . LEU B 152 ? 2.7155 1.6480 0.9133 0.3755  -0.2304 0.0222  152 LEU B CG  
5925  C CD1 . LEU B 152 ? 2.6283 1.5942 0.8762 0.3673  -0.2681 -0.0205 152 LEU B CD1 
5926  C CD2 . LEU B 152 ? 2.7281 1.6276 0.9948 0.3793  -0.1855 0.0362  152 LEU B CD2 
5927  N N   . SER B 153 ? 2.8751 1.9022 0.8966 0.3759  -0.2972 0.1050  153 SER B N   
5928  C CA  . SER B 153 ? 2.9637 2.0160 0.9303 0.3773  -0.3020 0.1468  153 SER B CA  
5929  C C   . SER B 153 ? 3.0151 2.0394 0.9215 0.3688  -0.2562 0.1453  153 SER B C   
5930  O O   . SER B 153 ? 2.9930 2.0197 0.8933 0.3501  -0.2377 0.0949  153 SER B O   
5931  C CB  . SER B 153 ? 2.9804 2.1043 0.9418 0.3600  -0.3439 0.1295  153 SER B CB  
5932  O OG  . SER B 153 ? 2.9497 2.0860 0.9138 0.3366  -0.3395 0.0666  153 SER B OG  
5933  N N   . GLY B 154 ? 3.1108 2.1137 0.9823 0.3814  -0.2370 0.2012  154 GLY B N   
5934  C CA  . GLY B 154 ? 3.1641 2.1456 0.9812 0.3718  -0.1936 0.2071  154 GLY B CA  
5935  C C   . GLY B 154 ? 3.2085 2.1393 1.0161 0.3896  -0.1642 0.2695  154 GLY B C   
5936  O O   . GLY B 154 ? 3.2229 2.1541 1.0556 0.4098  -0.1844 0.3175  154 GLY B O   
5937  N N   . GLU B 155 ? 3.1947 2.0865 0.9739 0.3801  -0.1151 0.2679  155 GLU B N   
5938  C CA  . GLU B 155 ? 3.2378 2.0742 1.0110 0.3911  -0.0788 0.3224  155 GLU B CA  
5939  C C   . GLU B 155 ? 3.1897 1.9658 0.9831 0.3841  -0.0320 0.2968  155 GLU B C   
5940  O O   . GLU B 155 ? 3.1420 1.9295 0.9376 0.3659  -0.0190 0.2395  155 GLU B O   
5941  C CB  . GLU B 155 ? 3.3263 2.1813 1.0413 0.3808  -0.0620 0.3561  155 GLU B CB  
5942  C CG  . GLU B 155 ? 3.3802 2.1817 1.0932 0.3899  -0.0269 0.4174  155 GLU B CG  
5943  C CD  . GLU B 155 ? 3.4688 2.2990 1.1265 0.3791  -0.0174 0.4537  155 GLU B CD  
5944  O OE1 . GLU B 155 ? 3.4793 2.3445 1.0966 0.3571  -0.0073 0.4192  155 GLU B OE1 
5945  O OE2 . GLU B 155 ? 3.5273 2.3490 1.1871 0.3927  -0.0200 0.5169  155 GLU B OE2 
5946  N N   . ILE B 156 ? 3.1971 1.9136 1.0149 0.3972  -0.0052 0.3389  156 ILE B N   
5947  C CA  . ILE B 156 ? 3.1546 1.8313 1.0322 0.3836  0.0412  0.3134  156 ILE B CA  
5948  C C   . ILE B 156 ? 3.1923 1.8514 1.0109 0.3611  0.0883  0.3090  156 ILE B C   
5949  O O   . ILE B 156 ? 3.2659 1.9081 1.0357 0.3622  0.1033  0.3582  156 ILE B O   
5950  C CB  . ILE B 156 ? 3.1676 1.7973 1.1141 0.4003  0.0552  0.3548  156 ILE B CB  
5951  C CG1 . ILE B 156 ? 3.1267 1.7805 1.1405 0.4217  0.0108  0.3523  156 ILE B CG1 
5952  C CG2 . ILE B 156 ? 3.1540 1.7417 1.1514 0.3819  0.1076  0.3303  156 ILE B CG2 
5953  C CD1 . ILE B 156 ? 3.1528 1.8264 1.1380 0.4481  -0.0311 0.4073  156 ILE B CD1 
5954  N N   . PRO B 157 ? 3.1536 1.8233 0.9803 0.3398  0.1117  0.2519  157 PRO B N   
5955  C CA  . PRO B 157 ? 3.1744 1.8416 0.9560 0.3166  0.1556  0.2446  157 PRO B CA  
5956  C C   . PRO B 157 ? 3.2198 1.8245 1.0066 0.3109  0.2034  0.2866  157 PRO B C   
5957  O O   . PRO B 157 ? 3.1947 1.7647 1.0576 0.3151  0.2152  0.2921  157 PRO B O   
5958  C CB  . PRO B 157 ? 3.0828 1.7777 0.9019 0.2984  0.1685  0.1739  157 PRO B CB  
5959  C CG  . PRO B 157 ? 3.0300 1.7428 0.8814 0.3126  0.1248  0.1440  157 PRO B CG  
5960  C CD  . PRO B 157 ? 3.0659 1.7679 0.9412 0.3362  0.0901  0.1908  157 PRO B CD  
5961  N N   . ARG B 158 ? 3.2321 1.8468 0.9804 0.2950  0.2275  0.3084  158 ARG B N   
5962  C CA  . ARG B 158 ? 3.2682 1.8293 1.0226 0.2822  0.2757  0.3424  158 ARG B CA  
5963  C C   . ARG B 158 ? 3.1977 1.7391 0.9942 0.2603  0.3181  0.2993  158 ARG B C   
5964  O O   . ARG B 158 ? 3.2075 1.6915 1.0284 0.2521  0.3555  0.3218  158 ARG B O   
5965  C CB  . ARG B 158 ? 3.3455 1.9363 1.0520 0.2661  0.2887  0.3687  158 ARG B CB  
5966  C CG  . ARG B 158 ? 3.3837 1.9297 1.0965 0.2455  0.3393  0.3977  158 ARG B CG  
5967  C CD  . ARG B 158 ? 3.3430 1.9224 1.0642 0.2133  0.3745  0.3507  158 ARG B CD  
5968  N NE  . ARG B 158 ? 3.3483 1.8772 1.0978 0.1922  0.4231  0.3642  158 ARG B NE  
5969  C CZ  . ARG B 158 ? 3.3031 1.8538 1.0788 0.1634  0.4572  0.3266  158 ARG B CZ  
5970  N NH1 . ARG B 158 ? 3.2449 1.8672 1.0298 0.1543  0.4492  0.2738  158 ARG B NH1 
5971  N NH2 . ARG B 158 ? 3.3148 1.8191 1.1168 0.1429  0.4987  0.3423  158 ARG B NH2 
5972  N N   . SER B 159 ? 3.1869 1.7792 1.0024 0.2498  0.3122  0.2371  159 SER B N   
5973  C CA  . SER B 159 ? 3.1122 1.7032 0.9801 0.2274  0.3502  0.1944  159 SER B CA  
5974  C C   . SER B 159 ? 3.0890 1.6303 1.0186 0.2350  0.3586  0.1949  159 SER B C   
5975  O O   . SER B 159 ? 3.0596 1.5772 1.0300 0.2147  0.4006  0.1844  159 SER B O   
5976  C CB  . SER B 159 ? 3.0248 1.6906 0.9242 0.2188  0.3335  0.1302  159 SER B CB  
5977  O OG  . SER B 159 ? 2.9866 1.6636 0.8976 0.2401  0.2893  0.1101  159 SER B OG  
5978  N N   . LEU B 160 ? 3.0833 1.6274 1.0510 0.2605  0.3146  0.2033  160 LEU B N   
5979  C CA  . LEU B 160 ? 3.0683 1.5882 1.1296 0.2676  0.3144  0.1996  160 LEU B CA  
5980  C C   . LEU B 160 ? 3.1292 1.5832 1.2072 0.2649  0.3493  0.2455  160 LEU B C   
5981  O O   . LEU B 160 ? 3.1152 1.5438 1.2698 0.2646  0.3623  0.2378  160 LEU B O   
5982  C CB  . LEU B 160 ? 3.0758 1.6166 1.1668 0.2968  0.2582  0.2053  160 LEU B CB  
5983  C CG  . LEU B 160 ? 3.0049 1.6053 1.0963 0.2994  0.2196  0.1565  160 LEU B CG  
5984  C CD1 . LEU B 160 ? 3.0197 1.6389 1.1324 0.3264  0.1638  0.1718  160 LEU B CD1 
5985  C CD2 . LEU B 160 ? 2.9099 1.5286 1.0684 0.2822  0.2381  0.1003  160 LEU B CD2 
5986  N N   . THR B 161 ? 3.0646 1.4901 1.0729 0.2626  0.3647  0.2928  161 THR B N   
5987  C CA  . THR B 161 ? 3.1242 1.4804 1.1425 0.2597  0.3981  0.3397  161 THR B CA  
5988  C C   . THR B 161 ? 3.1160 1.4473 1.1411 0.2235  0.4556  0.3222  161 THR B C   
5989  O O   . THR B 161 ? 3.1566 1.4254 1.2006 0.2165  0.4871  0.3529  161 THR B O   
5990  C CB  . THR B 161 ? 3.2412 1.5770 1.1829 0.2723  0.3893  0.4033  161 THR B CB  
5991  O OG1 . THR B 161 ? 3.2856 1.6470 1.1496 0.2495  0.4083  0.3992  161 THR B OG1 
5992  C CG2 . THR B 161 ? 3.2514 1.6216 1.1810 0.3057  0.3315  0.4207  161 THR B CG2 
5993  N N   . ALA B 162 ? 3.0917 1.4698 1.1027 0.2005  0.4703  0.2740  162 ALA B N   
5994  C CA  . ALA B 162 ? 3.0763 1.4415 1.0859 0.1642  0.5246  0.2588  162 ALA B CA  
5995  C C   . ALA B 162 ? 2.9773 1.3560 1.0707 0.1489  0.5424  0.2075  162 ALA B C   
5996  O O   . ALA B 162 ? 2.9558 1.3333 1.0556 0.1167  0.5867  0.1899  162 ALA B O   
5997  C CB  . ALA B 162 ? 3.0835 1.5176 1.0546 0.1461  0.5258  0.2373  162 ALA B CB  
5998  N N   . VAL B 163 ? 2.9704 1.3670 1.1298 0.1696  0.5087  0.1843  163 VAL B N   
5999  C CA  . VAL B 163 ? 2.8817 1.3036 1.1199 0.1552  0.5219  0.1337  163 VAL B CA  
6000  C C   . VAL B 163 ? 2.8964 1.2638 1.1882 0.1387  0.5613  0.1438  163 VAL B C   
6001  O O   . VAL B 163 ? 2.8206 1.2019 1.1502 0.1101  0.5960  0.1097  163 VAL B O   
6002  C CB  . VAL B 163 ? 2.8541 1.3142 1.1450 0.1815  0.4720  0.1085  163 VAL B CB  
6003  C CG1 . VAL B 163 ? 2.9446 1.3692 1.2463 0.2139  0.4387  0.1520  163 VAL B CG1 
6004  C CG2 . VAL B 163 ? 2.7617 1.2446 1.1418 0.1682  0.4849  0.0632  163 VAL B CG2 
6005  N N   . LEU B 164 ? 2.9556 1.2626 1.2552 0.1574  0.5552  0.1890  164 LEU B N   
6006  C CA  . LEU B 164 ? 2.9686 1.2070 1.3051 0.1455  0.5922  0.2087  164 LEU B CA  
6007  C C   . LEU B 164 ? 2.9002 1.1493 1.3329 0.1413  0.5974  0.1687  164 LEU B C   
6008  O O   . LEU B 164 ? 2.8851 1.0795 1.3590 0.1341  0.6246  0.1783  164 LEU B O   
6009  C CB  . LEU B 164 ? 2.9731 1.1836 1.2645 0.1063  0.6456  0.2175  164 LEU B CB  
6010  C CG  . LEU B 164 ? 2.8929 1.1354 1.2070 0.0645  0.6876  0.1714  164 LEU B CG  
6011  C CD1 . LEU B 164 ? 2.8576 1.0620 1.2457 0.0448  0.7211  0.1563  164 LEU B CD1 
6012  C CD2 . LEU B 164 ? 2.9163 1.1741 1.1746 0.0362  0.7126  0.1807  164 LEU B CD2 
6013  N N   . THR B 165 ? 2.8556 1.1739 1.3247 0.1464  0.5705  0.1246  165 THR B N   
6014  C CA  . THR B 165 ? 2.7832 1.1226 1.3448 0.1451  0.5689  0.0879  165 THR B CA  
6015  C C   . THR B 165 ? 2.7619 1.1126 1.3650 0.1840  0.5184  0.0955  165 THR B C   
6016  O O   . THR B 165 ? 2.6591 1.0111 1.3397 0.1886  0.5171  0.0789  165 THR B O   
6017  C CB  . THR B 165 ? 2.6856 1.0978 1.2703 0.1217  0.5760  0.0330  165 THR B CB  
6018  O OG1 . THR B 165 ? 2.6554 1.0723 1.1789 0.0926  0.6115  0.0311  165 THR B OG1 
6019  C CG2 . THR B 165 ? 2.5669 0.9911 1.2406 0.1040  0.5979  -0.0013 165 THR B CG2 
6020  N N   . LEU B 166 ? 2.7242 1.0872 1.2763 0.2105  0.4774  0.1201  166 LEU B N   
6021  C CA  . LEU B 166 ? 2.7035 1.0864 1.2879 0.2464  0.4259  0.1288  166 LEU B CA  
6022  C C   . LEU B 166 ? 2.6680 0.9961 1.2998 0.2662  0.4304  0.1598  166 LEU B C   
6023  O O   . LEU B 166 ? 2.7581 1.0205 1.3567 0.2690  0.4536  0.2021  166 LEU B O   
6024  C CB  . LEU B 166 ? 2.7851 1.1819 1.2930 0.2671  0.3881  0.1578  166 LEU B CB  
6025  C CG  . LEU B 166 ? 2.7923 1.2020 1.3051 0.3054  0.3339  0.1848  166 LEU B CG  
6026  C CD1 . LEU B 166 ? 2.7038 1.1593 1.2985 0.3157  0.3038  0.1508  166 LEU B CD1 
6027  C CD2 . LEU B 166 ? 2.8450 1.2873 1.2771 0.3124  0.3022  0.1946  166 LEU B CD2 
6028  N N   . GLN B 167 ? 2.7170 1.0725 1.4273 0.2801  0.4089  0.1386  167 GLN B N   
6029  C CA  . GLN B 167 ? 2.6605 0.9731 1.4248 0.3023  0.4106  0.1615  167 GLN B CA  
6030  C C   . GLN B 167 ? 2.6458 0.9854 1.4299 0.3433  0.3558  0.1825  167 GLN B C   
6031  O O   . GLN B 167 ? 2.6665 0.9609 1.4540 0.3716  0.3507  0.2255  167 GLN B O   
6032  C CB  . GLN B 167 ? 2.5226 0.8450 1.3711 0.2821  0.4384  0.1187  167 GLN B CB  
6033  C CG  . GLN B 167 ? 2.5204 0.8209 1.3626 0.2395  0.4951  0.1009  167 GLN B CG  
6034  C CD  . GLN B 167 ? 2.5314 0.8101 1.4169 0.2319  0.5216  0.1195  167 GLN B CD  
6035  O OE1 . GLN B 167 ? 2.6316 0.8508 1.4741 0.2485  0.5247  0.1649  167 GLN B OE1 
6036  N NE2 . GLN B 167 ? 2.4508 0.7841 1.4233 0.2063  0.5385  0.0852  167 GLN B NE2 
6037  N N   . VAL B 168 ? 2.6158 1.0279 1.4121 0.3471  0.3145  0.1545  168 VAL B N   
6038  C CA  . VAL B 168 ? 2.5894 1.0380 1.4100 0.3814  0.2604  0.1693  168 VAL B CA  
6039  C C   . VAL B 168 ? 2.6724 1.1657 1.4290 0.3845  0.2203  0.1700  168 VAL B C   
6040  O O   . VAL B 168 ? 2.6747 1.2074 1.4182 0.3610  0.2204  0.1300  168 VAL B O   
6041  C CB  . VAL B 168 ? 2.4377 0.9360 1.3520 0.3819  0.2457  0.1303  168 VAL B CB  
6042  C CG1 . VAL B 168 ? 2.4141 0.9501 1.3533 0.4173  0.1903  0.1501  168 VAL B CG1 
6043  C CG2 . VAL B 168 ? 2.3607 0.8185 1.3371 0.3738  0.2895  0.1216  168 VAL B CG2 
6044  N N   . LEU B 169 ? 2.6299 1.1196 1.3486 0.4141  0.1858  0.2147  169 LEU B N   
6045  C CA  . LEU B 169 ? 2.7114 1.2338 1.3557 0.4168  0.1515  0.2229  169 LEU B CA  
6046  C C   . LEU B 169 ? 2.6926 1.2478 1.3445 0.4506  0.0963  0.2521  169 LEU B C   
6047  O O   . LEU B 169 ? 2.6752 1.2025 1.3521 0.4777  0.0937  0.2926  169 LEU B O   
6048  C CB  . LEU B 169 ? 2.8117 1.2862 1.3706 0.4092  0.1804  0.2569  169 LEU B CB  
6049  C CG  . LEU B 169 ? 2.8843 1.3825 1.3516 0.4014  0.1645  0.2608  169 LEU B CG  
6050  C CD1 . LEU B 169 ? 2.8947 1.4203 1.3335 0.4307  0.1123  0.2961  169 LEU B CD1 
6051  C CD2 . LEU B 169 ? 2.8646 1.4125 1.3313 0.3765  0.1604  0.2011  169 LEU B CD2 
6052  N N   . ASP B 170 ? 2.7710 1.3857 1.4027 0.4487  0.0526  0.2311  170 ASP B N   
6053  C CA  . ASP B 170 ? 2.7397 1.3966 1.3804 0.4759  -0.0031 0.2536  170 ASP B CA  
6054  C C   . ASP B 170 ? 2.7738 1.4777 1.3506 0.4673  -0.0416 0.2386  170 ASP B C   
6055  O O   . ASP B 170 ? 2.7528 1.4898 1.3405 0.4458  -0.0481 0.1882  170 ASP B O   
6056  C CB  . ASP B 170 ? 2.6269 1.3198 1.3644 0.4828  -0.0214 0.2289  170 ASP B CB  
6057  C CG  . ASP B 170 ? 2.5846 1.3174 1.3405 0.5139  -0.0741 0.2602  170 ASP B CG  
6058  O OD1 . ASP B 170 ? 2.6388 1.3611 1.3412 0.5346  -0.0899 0.3089  170 ASP B OD1 
6059  O OD2 . ASP B 170 ? 2.4914 1.2708 1.3155 0.5170  -0.1002 0.2373  170 ASP B OD2 
6060  N N   . LEU B 171 ? 2.7521 1.4598 1.2631 0.4840  -0.0672 0.2820  171 LEU B N   
6061  C CA  . LEU B 171 ? 2.7696 1.5260 1.2205 0.4790  -0.1106 0.2718  171 LEU B CA  
6062  C C   . LEU B 171 ? 2.7933 1.5892 1.2462 0.5060  -0.1638 0.3093  171 LEU B C   
6063  O O   . LEU B 171 ? 2.8556 1.6762 1.2385 0.5092  -0.1934 0.3289  171 LEU B O   
6064  C CB  . LEU B 171 ? 2.8558 1.5935 1.2081 0.4673  -0.0937 0.2840  171 LEU B CB  
6065  C CG  . LEU B 171 ? 2.8678 1.5760 1.1878 0.4393  -0.0452 0.2528  171 LEU B CG  
6066  C CD1 . LEU B 171 ? 2.8093 1.5377 1.1827 0.4176  -0.0365 0.1884  171 LEU B CD1 
6067  C CD2 . LEU B 171 ? 2.9180 1.5631 1.2380 0.4411  0.0050  0.2878  171 LEU B CD2 
6068  N N   . SER B 172 ? 2.8289 1.6358 1.3608 0.5255  -0.1767 0.3202  172 SER B N   
6069  C CA  . SER B 172 ? 2.7923 1.6415 1.3294 0.5525  -0.2262 0.3588  172 SER B CA  
6070  C C   . SER B 172 ? 2.7521 1.6682 1.2712 0.5394  -0.2789 0.3282  172 SER B C   
6071  O O   . SER B 172 ? 2.7320 1.6609 1.2555 0.5127  -0.2778 0.2734  172 SER B O   
6072  C CB  . SER B 172 ? 2.7284 1.5789 1.3582 0.5766  -0.2269 0.3735  172 SER B CB  
6073  O OG  . SER B 172 ? 2.7220 1.6352 1.3768 0.5953  -0.2713 0.4056  172 SER B OG  
6074  N N   . ASN B 173 ? 2.7803 1.7468 1.2887 0.5541  -0.3226 0.3624  173 ASN B N   
6075  C CA  . ASN B 173 ? 2.7347 1.7797 1.2548 0.5373  -0.3731 0.3348  173 ASN B CA  
6076  C C   . ASN B 173 ? 2.7590 1.8030 1.1973 0.5105  -0.3793 0.2960  173 ASN B C   
6077  O O   . ASN B 173 ? 2.7049 1.7834 1.1561 0.4905  -0.4055 0.2502  173 ASN B O   
6078  C CB  . ASN B 173 ? 2.6348 1.7075 1.2415 0.5360  -0.3904 0.3026  173 ASN B CB  
6079  C CG  . ASN B 173 ? 2.5977 1.7607 1.2718 0.5362  -0.4329 0.3172  173 ASN B CG  
6080  O OD1 . ASN B 173 ? 2.6336 1.8501 1.2795 0.5241  -0.4618 0.3273  173 ASN B OD1 
6081  N ND2 . ASN B 173 ? 2.5288 1.7132 1.2943 0.5474  -0.4347 0.3178  173 ASN B ND2 
6082  N N   . ASN B 174 ? 2.8006 1.8079 1.1597 0.5080  -0.3531 0.3129  174 ASN B N   
6083  C CA  . ASN B 174 ? 2.8276 1.8395 1.1112 0.4824  -0.3541 0.2767  174 ASN B CA  
6084  C C   . ASN B 174 ? 2.9171 1.9543 1.1429 0.4806  -0.3579 0.3142  174 ASN B C   
6085  O O   . ASN B 174 ? 2.9729 1.9802 1.1866 0.4978  -0.3334 0.3642  174 ASN B O   
6086  C CB  . ASN B 174 ? 2.8265 1.7790 1.0905 0.4688  -0.3037 0.2432  174 ASN B CB  
6087  C CG  . ASN B 174 ? 2.7597 1.7191 1.0964 0.4531  -0.2995 0.1870  174 ASN B CG  
6088  O OD1 . ASN B 174 ? 2.7150 1.6997 1.0365 0.4341  -0.3200 0.1410  174 ASN B OD1 
6089  N ND2 . ASN B 174 ? 2.7480 1.6843 1.1639 0.4605  -0.2718 0.1903  174 ASN B ND2 
6090  N N   . PRO B 175 ? 2.8915 1.9845 1.0848 0.4591  -0.3868 0.2926  175 PRO B N   
6091  C CA  . PRO B 175 ? 2.9795 2.1043 1.1157 0.4551  -0.3917 0.3279  175 PRO B CA  
6092  C C   . PRO B 175 ? 3.0391 2.1205 1.0957 0.4455  -0.3526 0.3219  175 PRO B C   
6093  O O   . PRO B 175 ? 3.0653 2.1731 1.0722 0.4229  -0.3572 0.2909  175 PRO B O   
6094  C CB  . PRO B 175 ? 2.9671 2.1698 1.1081 0.4322  -0.4365 0.3001  175 PRO B CB  
6095  C CG  . PRO B 175 ? 2.8903 2.0800 1.0576 0.4163  -0.4391 0.2353  175 PRO B CG  
6096  C CD  . PRO B 175 ? 2.8311 1.9690 1.0512 0.4368  -0.4196 0.2390  175 PRO B CD  
6097  N N   . LEU B 176 ? 3.0739 2.0898 1.1216 0.4611  -0.3107 0.3516  176 LEU B N   
6098  C CA  . LEU B 176 ? 3.1360 2.1166 1.1130 0.4510  -0.2711 0.3555  176 LEU B CA  
6099  C C   . LEU B 176 ? 3.2252 2.2294 1.1689 0.4576  -0.2725 0.4162  176 LEU B C   
6100  O O   . LEU B 176 ? 3.2399 2.2905 1.2134 0.4693  -0.3045 0.4540  176 LEU B O   
6101  C CB  . LEU B 176 ? 3.1208 2.0187 1.1016 0.4572  -0.2199 0.3551  176 LEU B CB  
6102  C CG  . LEU B 176 ? 3.0395 1.9005 1.0497 0.4500  -0.2021 0.3022  176 LEU B CG  
6103  C CD1 . LEU B 176 ? 3.0120 1.9024 0.9930 0.4243  -0.2104 0.2374  176 LEU B CD1 
6104  C CD2 . LEU B 176 ? 2.9627 1.8355 1.0656 0.4637  -0.2246 0.3002  176 LEU B CD2 
6105  N N   . THR B 177 ? 3.2219 2.1983 1.1061 0.4483  -0.2364 0.4263  177 THR B N   
6106  C CA  . THR B 177 ? 3.3109 2.3082 1.1573 0.4508  -0.2334 0.4827  177 THR B CA  
6107  C C   . THR B 177 ? 3.3532 2.2837 1.1711 0.4503  -0.1794 0.5052  177 THR B C   
6108  O O   . THR B 177 ? 3.3156 2.1925 1.1340 0.4431  -0.1449 0.4710  177 THR B O   
6109  C CB  . THR B 177 ? 3.3525 2.4205 1.1424 0.4282  -0.2574 0.4651  177 THR B CB  
6110  O OG1 . THR B 177 ? 3.3216 2.3823 1.0827 0.4061  -0.2426 0.3991  177 THR B OG1 
6111  C CG2 . THR B 177 ? 3.3342 2.4755 1.1539 0.4282  -0.3115 0.4647  177 THR B CG2 
6112  N N   . GLY B 178 ? 3.3941 2.3314 1.1898 0.4554  -0.1719 0.5644  178 GLY B N   
6113  C CA  . GLY B 178 ? 3.4443 2.3252 1.2142 0.4515  -0.1228 0.5919  178 GLY B CA  
6114  C C   . GLY B 178 ? 3.4441 2.2604 1.2720 0.4738  -0.0992 0.6346  178 GLY B C   
6115  O O   . GLY B 178 ? 3.3905 2.1973 1.2829 0.4929  -0.1147 0.6330  178 GLY B O   
6116  N N   . ASP B 179 ? 3.4777 2.2509 1.2859 0.4695  -0.0599 0.6720  179 ASP B N   
6117  C CA  . ASP B 179 ? 3.4904 2.1986 1.3537 0.4870  -0.0325 0.7130  179 ASP B CA  
6118  C C   . ASP B 179 ? 3.4284 2.0654 1.3211 0.4814  0.0061  0.6728  179 ASP B C   
6119  O O   . ASP B 179 ? 3.3965 2.0266 1.2528 0.4596  0.0237  0.6231  179 ASP B O   
6120  C CB  . ASP B 179 ? 3.5850 2.2751 1.4187 0.4810  -0.0065 0.7689  179 ASP B CB  
6121  C CG  . ASP B 179 ? 3.6498 2.4138 1.4520 0.4838  -0.0433 0.8112  179 ASP B CG  
6122  O OD1 . ASP B 179 ? 3.6603 2.4476 1.5077 0.5063  -0.0717 0.8501  179 ASP B OD1 
6123  O OD2 . ASP B 179 ? 3.6896 2.4929 1.4241 0.4621  -0.0436 0.8046  179 ASP B OD2 
6124  N N   . ILE B 180 ? 3.4113 1.9996 1.3748 0.5003  0.0198  0.6936  180 ILE B N   
6125  C CA  . ILE B 180 ? 3.3493 1.8738 1.3534 0.4958  0.0546  0.6579  180 ILE B CA  
6126  C C   . ILE B 180 ? 3.3874 1.8580 1.3541 0.4694  0.1090  0.6562  180 ILE B C   
6127  O O   . ILE B 180 ? 3.4583 1.8998 1.4257 0.4688  0.1316  0.7028  180 ILE B O   
6128  C CB  . ILE B 180 ? 3.3267 1.8205 1.4223 0.5216  0.0558  0.6806  180 ILE B CB  
6129  C CG1 . ILE B 180 ? 3.2602 1.8092 1.4018 0.5421  0.0062  0.6640  180 ILE B CG1 
6130  C CG2 . ILE B 180 ? 3.2883 1.7078 1.4237 0.5110  0.1044  0.6545  180 ILE B CG2 
6131  C CD1 . ILE B 180 ? 3.3023 1.9201 1.4436 0.5591  -0.0392 0.7066  180 ILE B CD1 
6132  N N   . PRO B 181 ? 3.3890 1.8492 1.3258 0.4456  0.1308  0.6038  181 PRO B N   
6133  C CA  . PRO B 181 ? 3.4203 1.8453 1.3190 0.4152  0.1815  0.5968  181 PRO B CA  
6134  C C   . PRO B 181 ? 3.4078 1.7562 1.3589 0.4072  0.2302  0.5982  181 PRO B C   
6135  O O   . PRO B 181 ? 3.3524 1.6756 1.3205 0.3914  0.2562  0.5539  181 PRO B O   
6136  C CB  . PRO B 181 ? 3.3668 1.8282 1.2228 0.3946  0.1790  0.5343  181 PRO B CB  
6137  C CG  . PRO B 181 ? 3.2917 1.7741 1.2036 0.4098  0.1458  0.4981  181 PRO B CG  
6138  C CD  . PRO B 181 ? 3.3059 1.7962 1.2437 0.4441  0.1067  0.5465  181 PRO B CD  
6139  N N   . VAL B 182 ? 3.4230 1.7358 1.4044 0.4165  0.2436  0.6492  182 VAL B N   
6140  C CA  . VAL B 182 ? 3.4257 1.6675 1.4558 0.4041  0.2917  0.6513  182 VAL B CA  
6141  C C   . VAL B 182 ? 3.4809 1.7095 1.4567 0.3697  0.3306  0.6569  182 VAL B C   
6142  O O   . VAL B 182 ? 3.5636 1.7804 1.5252 0.3677  0.3389  0.7048  182 VAL B O   
6143  C CB  . VAL B 182 ? 3.4640 1.6762 1.5597 0.4299  0.2868  0.6977  182 VAL B CB  
6144  C CG1 . VAL B 182 ? 3.4714 1.6126 1.6172 0.4134  0.3368  0.6941  182 VAL B CG1 
6145  C CG2 . VAL B 182 ? 3.4037 1.6441 1.5565 0.4628  0.2462  0.6894  182 VAL B CG2 
6146  N N   . ASN B 183 ? 3.4336 1.6704 1.3812 0.3416  0.3537  0.6072  183 ASN B N   
6147  C CA  . ASN B 183 ? 3.4698 1.7042 1.3754 0.3054  0.3926  0.6027  183 ASN B CA  
6148  C C   . ASN B 183 ? 3.4458 1.6229 1.3972 0.2798  0.4436  0.5828  183 ASN B C   
6149  O O   . ASN B 183 ? 3.4666 1.6441 1.3929 0.2463  0.4783  0.5743  183 ASN B O   
6150  C CB  . ASN B 183 ? 3.4348 1.7339 1.2826 0.2888  0.3838  0.5580  183 ASN B CB  
6151  C CG  . ASN B 183 ? 3.4970 1.8269 1.2895 0.2625  0.4017  0.5713  183 ASN B CG  
6152  O OD1 . ASN B 183 ? 3.4655 1.8250 1.2393 0.2349  0.4239  0.5300  183 ASN B OD1 
6153  N ND2 . ASN B 183 ? 3.5836 1.9134 1.3554 0.2712  0.3910  0.6293  183 ASN B ND2 
6154  N N   . GLY B 184 ? 3.4220 1.5577 1.4442 0.2933  0.4476  0.5730  184 GLY B N   
6155  C CA  . GLY B 184 ? 3.3955 1.4815 1.4704 0.2689  0.4934  0.5505  184 GLY B CA  
6156  C C   . GLY B 184 ? 3.2920 1.3873 1.3975 0.2605  0.5005  0.4920  184 GLY B C   
6157  O O   . GLY B 184 ? 3.2547 1.3836 1.3245 0.2353  0.5146  0.4547  184 GLY B O   
6158  N N   . SER B 185 ? 3.3263 1.3981 1.5057 0.2811  0.4913  0.4840  185 SER B N   
6159  C CA  . SER B 185 ? 3.2408 1.3370 1.4807 0.2820  0.4837  0.4310  185 SER B CA  
6160  C C   . SER B 185 ? 3.2241 1.3425 1.4997 0.3249  0.4322  0.4445  185 SER B C   
6161  O O   . SER B 185 ? 3.1663 1.2769 1.5193 0.3381  0.4273  0.4277  185 SER B O   
6162  C CB  . SER B 185 ? 3.2067 1.3775 1.4306 0.2583  0.4795  0.3741  185 SER B CB  
6163  O OG  . SER B 185 ? 3.1859 1.3443 1.4079 0.2178  0.5297  0.3480  185 SER B OG  
6164  N N   . PHE B 186 ? 2.9479 1.7772 1.3131 0.8385  0.2965  0.4514  186 PHE B N   
6165  C CA  . PHE B 186 ? 2.9332 1.7856 1.3094 0.8532  0.2843  0.4652  186 PHE B CA  
6166  C C   . PHE B 186 ? 2.9442 1.7825 1.3306 0.8698  0.3088  0.4991  186 PHE B C   
6167  O O   . PHE B 186 ? 2.9406 1.7992 1.3396 0.8838  0.3022  0.5159  186 PHE B O   
6168  C CB  . PHE B 186 ? 2.9309 1.8338 1.2933 0.8645  0.2565  0.4645  186 PHE B CB  
6169  C CG  . PHE B 186 ? 2.9225 1.8391 1.2809 0.8522  0.2244  0.4301  186 PHE B CG  
6170  C CD1 . PHE B 186 ? 2.9319 1.8331 1.2830 0.8372  0.2256  0.4042  186 PHE B CD1 
6171  C CD2 . PHE B 186 ? 2.9101 1.8548 1.2745 0.8554  0.1909  0.4253  186 PHE B CD2 
6172  C CE1 . PHE B 186 ? 2.9308 1.8423 1.2818 0.8274  0.1950  0.3730  186 PHE B CE1 
6173  C CE2 . PHE B 186 ? 2.9101 1.8626 1.2738 0.8441  0.1579  0.3940  186 PHE B CE2 
6174  C CZ  . PHE B 186 ? 2.9214 1.8565 1.2787 0.8310  0.1604  0.3671  186 PHE B CZ  
6175  N N   . SER B 187 ? 2.9605 1.7648 1.3442 0.8684  0.3352  0.5113  187 SER B N   
6176  C CA  . SER B 187 ? 2.9888 1.7763 1.3911 0.8817  0.3572  0.5396  187 SER B CA  
6177  C C   . SER B 187 ? 2.9911 1.7446 1.4094 0.8851  0.3679  0.5355  187 SER B C   
6178  O O   . SER B 187 ? 3.0082 1.7639 1.4504 0.9001  0.3798  0.5548  187 SER B O   
6179  C CB  . SER B 187 ? 3.0157 1.7728 1.4154 0.8748  0.3780  0.5515  187 SER B CB  
6180  O OG  . SER B 187 ? 3.0128 1.7243 1.3990 0.8558  0.3838  0.5299  187 SER B OG  
6181  N N   . LEU B 188 ? 2.9595 1.6913 1.3730 0.8689  0.3637  0.5074  188 LEU B N   
6182  C CA  . LEU B 188 ? 2.9634 1.6668 1.3895 0.8702  0.3757  0.4995  188 LEU B CA  
6183  C C   . LEU B 188 ? 2.9394 1.6850 1.3809 0.8782  0.3590  0.5012  188 LEU B C   
6184  O O   . LEU B 188 ? 2.9447 1.6790 1.3985 0.8845  0.3703  0.5000  188 LEU B O   
6185  C CB  . LEU B 188 ? 2.9541 1.6201 1.3716 0.8444  0.3790  0.4684  188 LEU B CB  
6186  C CG  . LEU B 188 ? 2.9765 1.5972 1.3809 0.8300  0.3933  0.4645  188 LEU B CG  
6187  C CD1 . LEU B 188 ? 2.9583 1.6069 1.3513 0.8180  0.3788  0.4611  188 LEU B CD1 
6188  C CD2 . LEU B 188 ? 2.9795 1.5546 1.3795 0.8098  0.4014  0.4385  188 LEU B CD2 
6189  N N   . PHE B 189 ? 2.9017 1.6965 1.3427 0.8783  0.3316  0.5043  189 PHE B N   
6190  C CA  . PHE B 189 ? 2.8770 1.7127 1.3347 0.8796  0.3091  0.5057  189 PHE B CA  
6191  C C   . PHE B 189 ? 2.8894 1.7590 1.3672 0.9032  0.3105  0.5382  189 PHE B C   
6192  O O   . PHE B 189 ? 2.9083 1.7856 1.3919 0.9134  0.3205  0.5548  189 PHE B O   
6193  C CB  . PHE B 189 ? 2.8484 1.7155 1.2986 0.8637  0.2730  0.4873  189 PHE B CB  
6194  C CG  . PHE B 189 ? 2.8294 1.6725 1.2717 0.8383  0.2682  0.4543  189 PHE B CG  
6195  C CD1 . PHE B 189 ? 2.8454 1.6633 1.2681 0.8304  0.2786  0.4422  189 PHE B CD1 
6196  C CD2 . PHE B 189 ? 2.8104 1.6593 1.2675 0.8215  0.2535  0.4391  189 PHE B CD2 
6197  C CE1 . PHE B 189 ? 2.8449 1.6428 1.2633 0.8069  0.2741  0.4145  189 PHE B CE1 
6198  C CE2 . PHE B 189 ? 2.8111 1.6391 1.2634 0.7973  0.2486  0.4114  189 PHE B CE2 
6199  C CZ  . PHE B 189 ? 2.8284 1.6299 1.2614 0.7903  0.2588  0.3986  189 PHE B CZ  
6200  N N   . THR B 190 ? 2.9308 1.8316 1.4303 0.9061  0.2986  0.5453  190 THR B N   
6201  C CA  . THR B 190 ? 2.9327 1.8724 1.4665 0.9232  0.3023  0.5719  190 THR B CA  
6202  C C   . THR B 190 ? 2.9078 1.9091 1.4587 0.9164  0.2635  0.5808  190 THR B C   
6203  O O   . THR B 190 ? 2.8865 1.8943 1.4256 0.8993  0.2346  0.5639  190 THR B O   
6204  C CB  . THR B 190 ? 2.9389 1.8627 1.4828 0.9327  0.3232  0.5739  190 THR B CB  
6205  O OG1 . THR B 190 ? 2.9764 1.8358 1.5012 0.9405  0.3571  0.5649  190 THR B OG1 
6206  C CG2 . THR B 190 ? 2.9429 1.9121 1.5245 0.9527  0.3281  0.6027  190 THR B CG2 
6207  N N   . PRO B 191 ? 2.8536 1.8989 1.4329 0.9286  0.2594  0.6079  191 PRO B N   
6208  C CA  . PRO B 191 ? 2.8363 1.9370 1.4298 0.9200  0.2190  0.6172  191 PRO B CA  
6209  C C   . PRO B 191 ? 2.8092 1.9335 1.4163 0.9051  0.1899  0.6128  191 PRO B C   
6210  O O   . PRO B 191 ? 2.7982 1.9553 1.4089 0.8932  0.1497  0.6135  191 PRO B O   
6211  C CB  . PRO B 191 ? 2.8494 1.9890 1.4780 0.9363  0.2277  0.6513  191 PRO B CB  
6212  C CG  . PRO B 191 ? 2.8731 1.9752 1.5076 0.9557  0.2730  0.6580  191 PRO B CG  
6213  C CD  . PRO B 191 ? 2.8811 1.9236 1.4768 0.9486  0.2876  0.6305  191 PRO B CD  
6214  N N   . ILE B 192 ? 2.7992 1.9086 1.4134 0.9053  0.2070  0.6097  192 ILE B N   
6215  C CA  . ILE B 192 ? 2.7729 1.9085 1.4016 0.8882  0.1776  0.6083  192 ILE B CA  
6216  C C   . ILE B 192 ? 2.7609 1.8729 1.3603 0.8674  0.1471  0.5795  192 ILE B C   
6217  O O   . ILE B 192 ? 2.7423 1.8805 1.3544 0.8504  0.1071  0.5791  192 ILE B O   
6218  C CB  . ILE B 192 ? 2.7723 1.8988 1.4092 0.8949  0.2056  0.6121  192 ILE B CB  
6219  C CG1 . ILE B 192 ? 2.7904 1.9405 1.4551 0.9214  0.2356  0.6404  192 ILE B CG1 
6220  C CG2 . ILE B 192 ? 2.7444 1.9057 1.4000 0.8751  0.1745  0.6156  192 ILE B CG2 
6221  C CD1 . ILE B 192 ? 2.7970 1.9448 1.4664 0.9344  0.2634  0.6461  192 ILE B CD1 
6222  N N   . SER B 193 ? 2.7779 1.8411 1.3400 0.8687  0.1636  0.5568  193 SER B N   
6223  C CA  . SER B 193 ? 2.7672 1.8136 1.3071 0.8497  0.1366  0.5258  193 SER B CA  
6224  C C   . SER B 193 ? 2.7740 1.8469 1.3045 0.8513  0.0972  0.5280  193 SER B C   
6225  O O   . SER B 193 ? 2.7631 1.8365 1.2886 0.8343  0.0620  0.5037  193 SER B O   
6226  C CB  . SER B 193 ? 2.7786 1.7769 1.2897 0.8492  0.1663  0.5026  193 SER B CB  
6227  O OG  . SER B 193 ? 2.7774 1.7460 1.2936 0.8456  0.1988  0.4967  193 SER B OG  
6228  N N   . PHE B 194 ? 2.8212 1.9224 1.3603 0.8657  0.1015  0.5505  194 PHE B N   
6229  C CA  . PHE B 194 ? 2.8335 1.9618 1.3614 0.8670  0.0667  0.5509  194 PHE B CA  
6230  C C   . PHE B 194 ? 2.8301 2.0119 1.3972 0.8656  0.0435  0.5804  194 PHE B C   
6231  O O   . PHE B 194 ? 2.8472 2.0547 1.4078 0.8699  0.0232  0.5885  194 PHE B O   
6232  C CB  . PHE B 194 ? 2.8586 1.9778 1.3577 0.8818  0.0892  0.5499  194 PHE B CB  
6233  C CG  . PHE B 194 ? 2.8647 1.9375 1.3264 0.8821  0.1097  0.5244  194 PHE B CG  
6234  C CD1 . PHE B 194 ? 2.8654 1.9036 1.3303 0.8843  0.1522  0.5262  194 PHE B CD1 
6235  C CD2 . PHE B 194 ? 2.8829 1.9497 1.3105 0.8786  0.0857  0.4967  194 PHE B CD2 
6236  C CE1 . PHE B 194 ? 2.8797 1.8796 1.3171 0.8796  0.1692  0.5042  194 PHE B CE1 
6237  C CE2 . PHE B 194 ? 2.8927 1.9297 1.3008 0.8732  0.1054  0.4712  194 PHE B CE2 
6238  C CZ  . PHE B 194 ? 2.8890 1.8934 1.3031 0.8721  0.1467  0.4768  194 PHE B CZ  
6239  N N   . ALA B 195 ? 2.7839 1.9864 1.3907 0.8594  0.0457  0.5984  195 ALA B N   
6240  C CA  . ALA B 195 ? 2.7806 2.0384 1.4301 0.8578  0.0274  0.6314  195 ALA B CA  
6241  C C   . ALA B 195 ? 2.7780 2.0603 1.4329 0.8394  -0.0326 0.6297  195 ALA B C   
6242  O O   . ALA B 195 ? 2.7696 2.0306 1.4111 0.8255  -0.0597 0.6072  195 ALA B O   
6243  C CB  . ALA B 195 ? 2.7636 2.0409 1.4530 0.8595  0.0503  0.6526  195 ALA B CB  
6244  N N   . ASN B 196 ? 2.7367 2.0621 1.4125 0.8388  -0.0555 0.6547  196 ASN B N   
6245  C CA  . ASN B 196 ? 2.7408 2.0920 1.4272 0.8204  -0.1162 0.6588  196 ASN B CA  
6246  C C   . ASN B 196 ? 2.7615 2.0762 1.3959 0.8190  -0.1488 0.6210  196 ASN B C   
6247  O O   . ASN B 196 ? 2.7655 2.0809 1.4016 0.8030  -0.2011 0.6115  196 ASN B O   
6248  C CB  . ASN B 196 ? 2.7140 2.0888 1.4450 0.7999  -0.1392 0.6735  196 ASN B CB  
6249  C CG  . ASN B 196 ? 2.7194 2.1387 1.4838 0.7807  -0.1954 0.6979  196 ASN B CG  
6250  O OD1 . ASN B 196 ? 2.7377 2.1851 1.5088 0.7849  -0.2036 0.7179  196 ASN B OD1 
6251  N ND2 . ASN B 196 ? 2.7054 2.1312 1.4927 0.7576  -0.2366 0.6983  196 ASN B ND2 
6252  N N   . THR B 197 ? 2.8750 2.1581 1.4638 0.8365  -0.1191 0.5995  197 THR B N   
6253  C CA  . THR B 197 ? 2.8966 2.1440 1.4312 0.8407  -0.1408 0.5609  197 THR B CA  
6254  C C   . THR B 197 ? 2.9346 2.1990 1.4367 0.8503  -0.1662 0.5577  197 THR B C   
6255  O O   . THR B 197 ? 2.9600 2.2012 1.4152 0.8557  -0.1931 0.5243  197 THR B O   
6256  C CB  . THR B 197 ? 2.8930 2.0989 1.3963 0.8529  -0.0929 0.5403  197 THR B CB  
6257  O OG1 . THR B 197 ? 2.8625 2.0576 1.3970 0.8458  -0.0630 0.5489  197 THR B OG1 
6258  C CG2 . THR B 197 ? 2.9049 2.0746 1.3650 0.8523  -0.1145 0.4982  197 THR B CG2 
6259  N N   . LYS B 198 ? 2.9055 2.2110 1.4306 0.8531  -0.1599 0.5911  198 LYS B N   
6260  C CA  . LYS B 198 ? 2.9437 2.2711 1.4383 0.8615  -0.1813 0.5925  198 LYS B CA  
6261  C C   . LYS B 198 ? 2.9669 2.2725 1.4042 0.8814  -0.1550 0.5675  198 LYS B C   
6262  O O   . LYS B 198 ? 3.0043 2.3167 1.3969 0.8898  -0.1809 0.5507  198 LYS B O   
6263  C CB  . LYS B 198 ? 2.9672 2.2999 1.4513 0.8492  -0.2495 0.5789  198 LYS B CB  
6264  C CG  . LYS B 198 ? 2.9431 2.2971 1.4867 0.8252  -0.2807 0.6037  198 LYS B CG  
6265  C CD  . LYS B 198 ? 2.9680 2.3134 1.5008 0.8107  -0.3516 0.5837  198 LYS B CD  
6266  C CE  . LYS B 198 ? 2.9399 2.3061 1.5370 0.7834  -0.3821 0.6098  198 LYS B CE  
6267  N NZ  . LYS B 198 ? 2.9663 2.3202 1.5595 0.7659  -0.4553 0.5912  198 LYS B NZ  
6268  N N   . LEU B 199 ? 3.0128 2.2939 1.4506 0.8887  -0.1043 0.5653  199 LEU B N   
6269  C CA  . LEU B 199 ? 3.0320 2.2964 1.4223 0.9048  -0.0769 0.5468  199 LEU B CA  
6270  C C   . LEU B 199 ? 3.0555 2.3568 1.4410 0.9156  -0.0601 0.5723  199 LEU B C   
6271  O O   . LEU B 199 ? 3.0885 2.4020 1.4279 0.9264  -0.0701 0.5585  199 LEU B O   
6272  C CB  . LEU B 199 ? 3.0067 2.2340 1.4045 0.9055  -0.0302 0.5413  199 LEU B CB  
6273  C CG  . LEU B 199 ? 2.9912 2.1772 1.3759 0.8975  -0.0425 0.5089  199 LEU B CG  
6274  C CD1 . LEU B 199 ? 2.9735 2.1239 1.3598 0.8981  0.0054  0.5050  199 LEU B CD1 
6275  C CD2 . LEU B 199 ? 3.0165 2.1956 1.3548 0.9012  -0.0772 0.4701  199 LEU B CD2 
6276  N N   . THR B 200 ? 3.0086 2.3304 1.4415 0.9138  -0.0350 0.6097  200 THR B N   
6277  C CA  . THR B 200 ? 3.0297 2.3862 1.4661 0.9225  -0.0186 0.6387  200 THR B CA  
6278  C C   . THR B 200 ? 3.0239 2.4178 1.5114 0.9153  -0.0296 0.6766  200 THR B C   
6279  O O   . THR B 200 ? 3.0231 2.4333 1.5219 0.9037  -0.0713 0.6777  200 THR B O   
6280  C CB  . THR B 200 ? 3.0251 2.3636 1.4674 0.9319  0.0352  0.6489  200 THR B CB  
6281  O OG1 . THR B 200 ? 3.0300 2.3373 1.4278 0.9366  0.0456  0.6166  200 THR B OG1 
6282  C CG2 . THR B 200 ? 3.0495 2.4258 1.4971 0.9396  0.0481  0.6807  200 THR B CG2 
6283  N N   . PRO C 1   ? 1.1389 0.7951 1.0332 0.3882  -0.2845 -0.0349 1   PRO C N   
6284  C CA  . PRO C 1   ? 1.0825 0.7537 1.1006 0.3256  -0.2833 -0.0457 1   PRO C CA  
6285  C C   . PRO C 1   ? 1.1520 0.7400 1.1339 0.2907  -0.2259 -0.0373 1   PRO C C   
6286  O O   . PRO C 1   ? 1.1654 0.7285 1.0939 0.2929  -0.2036 -0.0117 1   PRO C O   
6287  C CB  . PRO C 1   ? 0.9514 0.7375 1.1202 0.2929  -0.3340 -0.0278 1   PRO C CB  
6288  C CG  . PRO C 1   ? 0.9622 0.7683 1.0716 0.3243  -0.3416 0.0026  1   PRO C CG  
6289  C CD  . PRO C 1   ? 1.0802 0.8087 1.0169 0.3870  -0.3142 -0.0039 1   PRO C CD  
6290  N N   . VAL C 2   ? 1.0947 0.6423 1.1082 0.2591  -0.2023 -0.0614 2   VAL C N   
6291  C CA  . VAL C 2   ? 1.1169 0.5881 1.1064 0.2235  -0.1465 -0.0614 2   VAL C CA  
6292  C C   . VAL C 2   ? 1.0195 0.5531 1.1216 0.1743  -0.1616 -0.0406 2   VAL C C   
6293  O O   . VAL C 2   ? 0.9257 0.5452 1.1648 0.1428  -0.2046 -0.0410 2   VAL C O   
6294  C CB  . VAL C 2   ? 1.1378 0.5616 1.1469 0.2008  -0.1222 -0.0949 2   VAL C CB  
6295  C CG1 . VAL C 2   ? 1.1233 0.5033 1.1652 0.1485  -0.0782 -0.0988 2   VAL C CG1 
6296  C CG2 . VAL C 2   ? 1.2590 0.5926 1.1230 0.2531  -0.0877 -0.1117 2   VAL C CG2 
6297  N N   . ARG C 3   ? 1.0904 0.5813 1.1338 0.1701  -0.1258 -0.0225 3   ARG C N   
6298  C CA  . ARG C 3   ? 1.0151 0.5603 1.1489 0.1300  -0.1363 -0.0033 3   ARG C CA  
6299  C C   . ARG C 3   ? 1.0190 0.4914 1.1301 0.0969  -0.0789 -0.0158 3   ARG C C   
6300  O O   . ARG C 3   ? 1.1043 0.4769 1.1149 0.1087  -0.0261 -0.0336 3   ARG C O   
6301  C CB  . ARG C 3   ? 1.0143 0.5975 1.1123 0.1576  -0.1554 0.0312  3   ARG C CB  
6302  C CG  . ARG C 3   ? 1.0112 0.6311 1.0710 0.2074  -0.1933 0.0387  3   ARG C CG  
6303  C CD  . ARG C 3   ? 1.0146 0.6357 0.9922 0.2428  -0.1931 0.0683  3   ARG C CD  
6304  N NE  . ARG C 3   ? 1.0676 0.6743 0.9459 0.3025  -0.2037 0.0657  3   ARG C NE  
6305  C CZ  . ARG C 3   ? 1.1799 0.6884 0.9090 0.3432  -0.1604 0.0581  3   ARG C CZ  
6306  N NH1 . ARG C 3   ? 1.2395 0.6502 0.9016 0.3284  -0.0994 0.0521  3   ARG C NH1 
6307  N NH2 . ARG C 3   ? 1.2372 0.7456 0.8826 0.4019  -0.1770 0.0554  3   ARG C NH2 
6308  N N   . SER C 4   ? 0.9257 0.4498 1.1327 0.0565  -0.0884 -0.0078 4   SER C N   
6309  C CA  . SER C 4   ? 0.9347 0.4060 1.1332 0.0243  -0.0387 -0.0216 4   SER C CA  
6310  C C   . SER C 4   ? 0.9658 0.4148 1.0884 0.0409  -0.0167 0.0007  4   SER C C   
6311  O O   . SER C 4   ? 0.9766 0.4819 1.0972 0.0643  -0.0522 0.0314  4   SER C O   
6312  C CB  . SER C 4   ? 0.8388 0.3808 1.1823 -0.0257 -0.0608 -0.0299 4   SER C CB  
6313  O OG  . SER C 4   ? 0.7707 0.3921 1.1703 -0.0290 -0.0942 -0.0001 4   SER C OG  
6314  N N   . SER C 5   ? 1.0256 0.3924 1.0895 0.0275  0.0438  -0.0166 5   SER C N   
6315  C CA  . SER C 5   ? 1.0620 0.3994 1.0519 0.0418  0.0705  0.0004  5   SER C CA  
6316  C C   . SER C 5   ? 0.9689 0.3974 1.0593 0.0153  0.0388  0.0148  5   SER C C   
6317  O O   . SER C 5   ? 0.8975 0.3801 1.1029 -0.0237 0.0216  0.0005  5   SER C O   
6318  C CB  . SER C 5   ? 1.1559 0.3769 1.0615 0.0327  0.1488  -0.0258 5   SER C CB  
6319  O OG  . SER C 5   ? 1.1225 0.3453 1.1170 -0.0176 0.1679  -0.0592 5   SER C OG  
6320  N N   . GLN C 6   ? 1.0711 0.5168 1.1138 0.0401  0.0307  0.0438  6   GLN C N   
6321  C CA  . GLN C 6   ? 1.0167 0.5466 1.1370 0.0242  0.0015  0.0620  6   GLN C CA  
6322  C C   . GLN C 6   ? 1.0565 0.5329 1.1195 0.0180  0.0511  0.0530  6   GLN C C   
6323  O O   . GLN C 6   ? 1.1147 0.5118 1.0563 0.0471  0.0891  0.0580  6   GLN C O   
6324  C CB  . GLN C 6   ? 1.0064 0.6102 1.1290 0.0571  -0.0512 0.1031  6   GLN C CB  
6325  C CG  . GLN C 6   ? 0.9416 0.6102 1.1379 0.0609  -0.1029 0.1105  6   GLN C CG  
6326  C CD  . GLN C 6   ? 0.8176 0.5883 1.1609 0.0289  -0.1460 0.1189  6   GLN C CD  
6327  O OE1 . GLN C 6   ? 0.7574 0.5637 1.1834 0.0128  -0.1715 0.1094  6   GLN C OE1 
6328  N NE2 . GLN C 6   ? 0.7809 0.5980 1.1552 0.0219  -0.1533 0.1369  6   GLN C NE2 
6329  N N   . SER C 7   ? 0.9761 0.4966 1.1264 -0.0179 0.0511  0.0384  7   SER C N   
6330  C CA  . SER C 7   ? 0.9980 0.4780 1.1089 -0.0267 0.0961  0.0241  7   SER C CA  
6331  C C   . SER C 7   ? 1.0530 0.5653 1.1169 0.0047  0.0771  0.0611  7   SER C C   
6332  O O   . SER C 7   ? 1.0214 0.6294 1.1471 0.0130  0.0213  0.0917  7   SER C O   
6333  C CB  . SER C 7   ? 0.9060 0.4356 1.1288 -0.0704 0.0964  -0.0060 7   SER C CB  
6334  O OG  . SER C 7   ? 0.9345 0.3994 1.1173 -0.0855 0.1556  -0.0377 7   SER C OG  
6335  N N   . SER C 8   ? 1.0449 0.4747 0.9991 0.0224  0.1261  0.0586  8   SER C N   
6336  C CA  . SER C 8   ? 1.0805 0.5295 0.9788 0.0529  0.1152  0.0907  8   SER C CA  
6337  C C   . SER C 8   ? 1.0757 0.5718 1.0327 0.0298  0.1181  0.0800  8   SER C C   
6338  O O   . SER C 8   ? 1.0535 0.5222 1.0459 -0.0040 0.1555  0.0397  8   SER C O   
6339  C CB  . SER C 8   ? 1.1484 0.4842 0.8966 0.0865  0.1674  0.0939  8   SER C CB  
6340  O OG  . SER C 8   ? 1.1514 0.5147 0.8403 0.1273  0.1403  0.1334  8   SER C OG  
6341  N N   . GLN C 9   ? 0.9899 0.5610 0.9593 0.0496  0.0778  0.1145  9   GLN C N   
6342  C CA  . GLN C 9   ? 0.9790 0.6095 1.0070 0.0339  0.0718  0.1077  9   GLN C CA  
6343  C C   . GLN C 9   ? 1.0395 0.5893 0.9879 0.0337  0.1326  0.0843  9   GLN C C   
6344  O O   . GLN C 9   ? 1.0911 0.5496 0.9236 0.0582  0.1706  0.0906  9   GLN C O   
6345  C CB  . GLN C 9   ? 0.9380 0.6666 0.9932 0.0590  0.0143  0.1540  9   GLN C CB  
6346  C CG  . GLN C 9   ? 0.8986 0.7257 1.0612 0.0401  -0.0152 0.1508  9   GLN C CG  
6347  C CD  . GLN C 9   ? 0.7798 0.7113 0.9969 0.0600  -0.0781 0.1983  9   GLN C CD  
6348  O OE1 . GLN C 9   ? 0.6850 0.6785 0.9926 0.0483  -0.1148 0.2065  9   GLN C OE1 
6349  N NE2 . GLN C 9   ? 0.7659 0.7157 0.9286 0.0904  -0.0885 0.2301  9   GLN C NE2 
6350  N N   . ALA C 10  ? 0.9486 0.5341 0.9613 0.0077  0.1423  0.0556  10  ALA C N   
6351  C CA  . ALA C 10  ? 1.0031 0.5218 0.9582 0.0032  0.1996  0.0278  10  ALA C CA  
6352  C C   . ALA C 10  ? 1.0342 0.5578 0.9109 0.0411  0.1908  0.0649  10  ALA C C   
6353  O O   . ALA C 10  ? 0.9871 0.5952 0.8860 0.0637  0.1341  0.1065  10  ALA C O   
6354  C CB  . ALA C 10  ? 0.9660 0.5373 1.0213 -0.0326 0.2055  -0.0165 10  ALA C CB  
6355  N N   . GLY C 11  ? 1.1242 0.5542 0.9095 0.0478  0.2503  0.0490  11  GLY C N   
6356  C CA  . GLY C 11  ? 1.1570 0.5830 0.8620 0.0836  0.2478  0.0806  11  GLY C CA  
6357  C C   . GLY C 11  ? 1.1460 0.6741 0.9235 0.0790  0.2143  0.0813  11  GLY C C   
6358  O O   . GLY C 11  ? 1.1377 0.6934 0.9913 0.0471  0.2277  0.0390  11  GLY C O   
6359  N N   . GLY C 12  ? 1.0856 0.6733 0.8393 0.1133  0.1695  0.1285  12  GLY C N   
6360  C CA  . GLY C 12  ? 1.0678 0.7515 0.8764 0.1171  0.1364  0.1360  12  GLY C CA  
6361  C C   . GLY C 12  ? 1.1136 0.7579 0.8353 0.1401  0.1649  0.1411  12  GLY C C   
6362  O O   . GLY C 12  ? 1.1438 0.6950 0.7530 0.1630  0.1994  0.1538  12  GLY C O   
6363  N N   . ARG C 13  ? 1.1210 0.8355 0.8919 0.1370  0.1510  0.1307  13  ARG C N   
6364  C CA  . ARG C 13  ? 1.1542 0.8418 0.8518 0.1586  0.1742  0.1344  13  ARG C CA  
6365  C C   . ARG C 13  ? 1.0670 0.8482 0.7640 0.1938  0.1156  0.1868  13  ARG C C   
6366  O O   . ARG C 13  ? 1.0446 0.7917 0.6478 0.2270  0.1209  0.2173  13  ARG C O   
6367  C CB  . ARG C 13  ? 1.1996 0.8902 0.9454 0.1307  0.2091  0.0773  13  ARG C CB  
6368  C CG  . ARG C 13  ? 1.2159 0.8814 0.8939 0.1509  0.2343  0.0762  13  ARG C CG  
6369  C CD  . ARG C 13  ? 1.2524 0.7839 0.8594 0.1361  0.3178  0.0345  13  ARG C CD  
6370  N NE  . ARG C 13  ? 1.2695 0.7863 0.8368 0.1472  0.3447  0.0206  13  ARG C NE  
6371  C CZ  . ARG C 13  ? 1.2616 0.7882 0.8860 0.1201  0.3754  -0.0374 13  ARG C CZ  
6372  N NH1 . ARG C 13  ? 1.2309 0.7825 0.9540 0.0805  0.3840  -0.0884 13  ARG C NH1 
6373  N NH2 . ARG C 13  ? 1.2793 0.7933 0.8634 0.1336  0.3974  -0.0469 13  ARG C NH2 
6374  N N   . THR D 47  ? 0.6838 0.5598 0.8489 -0.0120 0.0021  0.0731  47  THR D N   
6375  C CA  . THR D 47  ? 0.6987 0.5860 0.8727 -0.0124 0.0077  0.0789  47  THR D CA  
6376  C C   . THR D 47  ? 0.7100 0.6277 0.8974 -0.0168 -0.0012 0.0790  47  THR D C   
6377  O O   . THR D 47  ? 0.7053 0.6349 0.8940 -0.0183 -0.0121 0.0758  47  THR D O   
6378  C CB  . THR D 47  ? 0.6850 0.5649 0.8512 0.0044  0.0115  0.0878  47  THR D CB  
6379  O OG1 . THR D 47  ? 0.6687 0.5626 0.8340 0.0149  0.0021  0.0889  47  THR D OG1 
6380  C CG2 . THR D 47  ? 0.6661 0.5213 0.8191 0.0120  0.0159  0.0906  47  THR D CG2 
6381  N N   . VAL D 48  ? 0.7030 0.6343 0.9020 -0.0186 0.0041  0.0842  48  VAL D N   
6382  C CA  . VAL D 48  ? 0.7080 0.6701 0.9239 -0.0205 -0.0028 0.0876  48  VAL D CA  
6383  C C   . VAL D 48  ? 0.7019 0.6688 0.9180 -0.0024 -0.0056 0.0931  48  VAL D C   
6384  O O   . VAL D 48  ? 0.6902 0.6775 0.9178 0.0002  -0.0139 0.0954  48  VAL D O   
6385  C CB  . VAL D 48  ? 0.7151 0.6917 0.9464 -0.0314 0.0050  0.0910  48  VAL D CB  
6386  C CG1 . VAL D 48  ? 0.7036 0.7163 0.9561 -0.0363 -0.0030 0.0957  48  VAL D CG1 
6387  C CG2 . VAL D 48  ? 0.7168 0.6813 0.9449 -0.0495 0.0115  0.0840  48  VAL D CG2 
6388  N N   . GLU D 49  ? 0.7880 0.7367 0.9914 0.0095  0.0016  0.0953  49  GLU D N   
6389  C CA  . GLU D 49  ? 0.7583 0.7087 0.9583 0.0247  0.0002  0.0978  49  GLU D CA  
6390  C C   . GLU D 49  ? 0.7236 0.6697 0.9154 0.0303  -0.0107 0.0937  49  GLU D C   
6391  O O   . GLU D 49  ? 0.6985 0.6556 0.8972 0.0376  -0.0153 0.0947  49  GLU D O   
6392  C CB  . GLU D 49  ? 0.7574 0.6908 0.9421 0.0333  0.0100  0.1005  49  GLU D CB  
6393  C CG  . GLU D 49  ? 0.7897 0.7242 0.9804 0.0276  0.0220  0.1051  49  GLU D CG  
6394  C CD  . GLU D 49  ? 0.8001 0.7180 0.9848 0.0185  0.0267  0.1048  49  GLU D CD  
6395  O OE1 . GLU D 49  ? 0.7830 0.6830 0.9534 0.0218  0.0243  0.1035  49  GLU D OE1 
6396  O OE2 . GLU D 49  ? 0.8210 0.7437 1.0169 0.0079  0.0338  0.1063  49  GLU D OE2 
6397  N N   . GLU D 50  ? 0.7134 0.6429 0.8920 0.0272  -0.0137 0.0896  50  GLU D N   
6398  C CA  . GLU D 50  ? 0.6836 0.6096 0.8553 0.0310  -0.0239 0.0856  50  GLU D CA  
6399  C C   . GLU D 50  ? 0.6835 0.6315 0.8702 0.0247  -0.0331 0.0849  50  GLU D C   
6400  O O   . GLU D 50  ? 0.6505 0.6057 0.8401 0.0323  -0.0398 0.0858  50  GLU D O   
6401  C CB  . GLU D 50  ? 0.6850 0.5912 0.8442 0.0269  -0.0235 0.0818  50  GLU D CB  
6402  C CG  . GLU D 50  ? 0.6704 0.5568 0.8143 0.0365  -0.0180 0.0851  50  GLU D CG  
6403  C CD  . GLU D 50  ? 0.6731 0.5407 0.8108 0.0321  -0.0144 0.0837  50  GLU D CD  
6404  O OE1 . GLU D 50  ? 0.6927 0.5602 0.8370 0.0196  -0.0133 0.0784  50  GLU D OE1 
6405  O OE2 . GLU D 50  ? 0.6576 0.5111 0.7843 0.0405  -0.0120 0.0882  50  GLU D OE2 
6406  N N   . ALA D 51  ? 0.6594 0.6194 0.8560 0.0099  -0.0333 0.0840  51  ALA D N   
6407  C CA  . ALA D 51  ? 0.6616 0.6465 0.8715 0.0015  -0.0431 0.0848  51  ALA D CA  
6408  C C   . ALA D 51  ? 0.6290 0.6367 0.8576 0.0098  -0.0452 0.0935  51  ALA D C   
6409  O O   . ALA D 51  ? 0.5933 0.6143 0.8292 0.0134  -0.0539 0.0965  51  ALA D O   
6410  C CB  . ALA D 51  ? 0.6953 0.6909 0.9113 -0.0183 -0.0417 0.0819  51  ALA D CB  
6411  N N   . ASN D 52  ? 0.6632 0.6753 0.9012 0.0133  -0.0360 0.0983  52  ASN D N   
6412  C CA  . ASN D 52  ? 0.6334 0.6663 0.8923 0.0218  -0.0351 0.1069  52  ASN D CA  
6413  C C   . ASN D 52  ? 0.5933 0.6143 0.8462 0.0381  -0.0351 0.1063  52  ASN D C   
6414  O O   . ASN D 52  ? 0.5617 0.5984 0.8316 0.0446  -0.0380 0.1125  52  ASN D O   
6415  C CB  . ASN D 52  ? 0.6566 0.6943 0.9257 0.0221  -0.0232 0.1112  52  ASN D CB  
6416  C CG  . ASN D 52  ? 0.6793 0.7409 0.9651 0.0057  -0.0243 0.1150  52  ASN D CG  
6417  O OD1 . ASN D 52  ? 0.6499 0.7414 0.9566 0.0010  -0.0315 0.1223  52  ASN D OD1 
6418  N ND2 . ASN D 52  ? 0.7206 0.7705 0.9980 -0.0036 -0.0170 0.1109  52  ASN D ND2 
6419  N N   . ALA D 53  ? 0.6585 0.6525 0.8880 0.0443  -0.0319 0.0996  53  ALA D N   
6420  C CA  . ALA D 53  ? 0.6268 0.6093 0.8482 0.0573  -0.0319 0.0973  53  ALA D CA  
6421  C C   . ALA D 53  ? 0.5960 0.5829 0.8190 0.0577  -0.0436 0.0965  53  ALA D C   
6422  O O   . ALA D 53  ? 0.5685 0.5602 0.8009 0.0664  -0.0442 0.0990  53  ALA D O   
6423  C CB  . ALA D 53  ? 0.6351 0.5923 0.8307 0.0614  -0.0272 0.0915  53  ALA D CB  
6424  N N   . LEU D 54  ? 0.6208 0.6052 0.8351 0.0481  -0.0515 0.0930  54  LEU D N   
6425  C CA  . LEU D 54  ? 0.5964 0.5881 0.8128 0.0463  -0.0626 0.0929  54  LEU D CA  
6426  C C   . LEU D 54  ? 0.5819 0.6036 0.8240 0.0440  -0.0670 0.1025  54  LEU D C   
6427  O O   . LEU D 54  ? 0.5482 0.5776 0.7986 0.0499  -0.0726 0.1066  54  LEU D O   
6428  C CB  . LEU D 54  ? 0.6194 0.6045 0.8230 0.0342  -0.0678 0.0869  54  LEU D CB  
6429  C CG  . LEU D 54  ? 0.6111 0.5707 0.7931 0.0380  -0.0686 0.0797  54  LEU D CG  
6430  C CD1 . LEU D 54  ? 0.5682 0.5245 0.7474 0.0487  -0.0741 0.0796  54  LEU D CD1 
6431  C CD2 . LEU D 54  ? 0.6231 0.5637 0.7931 0.0426  -0.0591 0.0782  54  LEU D CD2 
6432  N N   . LEU D 55  ? 0.6000 0.6405 0.8564 0.0353  -0.0645 0.1076  55  LEU D N   
6433  C CA  . LEU D 55  ? 0.5805 0.6549 0.8639 0.0320  -0.0694 0.1193  55  LEU D CA  
6434  C C   . LEU D 55  ? 0.5478 0.6274 0.8502 0.0480  -0.0636 0.1278  55  LEU D C   
6435  O O   . LEU D 55  ? 0.5158 0.6175 0.8389 0.0509  -0.0690 0.1385  55  LEU D O   
6436  C CB  . LEU D 55  ? 0.6102 0.7032 0.9047 0.0189  -0.0666 0.1226  55  LEU D CB  
6437  C CG  . LEU D 55  ? 0.6032 0.7289 0.9097 0.0018  -0.0773 0.1282  55  LEU D CG  
6438  C CD1 . LEU D 55  ? 0.6022 0.7211 0.8900 -0.0068 -0.0872 0.1204  55  LEU D CD1 
6439  C CD2 . LEU D 55  ? 0.6356 0.7703 0.9446 -0.0137 -0.0729 0.1262  55  LEU D CD2 
6440  N N   . LYS D 56  ? 0.6429 0.7026 0.9389 0.0582  -0.0515 0.1235  56  LYS D N   
6441  C CA  . LYS D 56  ? 0.6202 0.6793 0.9315 0.0730  -0.0429 0.1283  56  LYS D CA  
6442  C C   . LYS D 56  ? 0.5914 0.6381 0.8960 0.0810  -0.0475 0.1254  56  LYS D C   
6443  O O   . LYS D 56  ? 0.5646 0.6223 0.8909 0.0892  -0.0461 0.1341  56  LYS D O   
6444  C CB  . LYS D 56  ? 0.6443 0.6839 0.9453 0.0794  -0.0283 0.1220  56  LYS D CB  
6445  C CG  . LYS D 56  ? 0.6370 0.6858 0.9630 0.0897  -0.0153 0.1293  56  LYS D CG  
6446  C CD  . LYS D 56  ? 0.6632 0.6889 0.9728 0.0958  -0.0004 0.1203  56  LYS D CD  
6447  C CE  . LYS D 56  ? 0.6525 0.6589 0.9548 0.1067  0.0061  0.1136  56  LYS D CE  
6448  N NZ  . LYS D 56  ? 0.6809 0.6724 0.9754 0.1124  0.0239  0.1070  56  LYS D NZ  
6449  N N   . TRP D 57  ? 0.6419 0.6662 0.9183 0.0788  -0.0523 0.1143  57  TRP D N   
6450  C CA  . TRP D 57  ? 0.6163 0.6292 0.8850 0.0847  -0.0575 0.1110  57  TRP D CA  
6451  C C   . TRP D 57  ? 0.5905 0.6258 0.8756 0.0809  -0.0689 0.1204  57  TRP D C   
6452  O O   . TRP D 57  ? 0.5639 0.6012 0.8608 0.0890  -0.0693 0.1253  57  TRP D O   
6453  C CB  . TRP D 57  ? 0.6256 0.6148 0.8632 0.0816  -0.0614 0.0992  57  TRP D CB  
6454  C CG  . TRP D 57  ? 0.6012 0.5793 0.8299 0.0862  -0.0672 0.0952  57  TRP D CG  
6455  C CD1 . TRP D 57  ? 0.5862 0.5576 0.8207 0.0960  -0.0626 0.0948  57  TRP D CD1 
6456  C CD2 . TRP D 57  ? 0.5929 0.5643 0.8057 0.0807  -0.0774 0.0905  57  TRP D CD2 
6457  N NE1 . TRP D 57  ? 0.5683 0.5302 0.7915 0.0966  -0.0702 0.0906  57  TRP D NE1 
6458  C CE2 . TRP D 57  ? 0.5699 0.5323 0.7800 0.0877  -0.0796 0.0883  57  TRP D CE2 
6459  C CE3 . TRP D 57  ? 0.6069 0.5778 0.8084 0.0703  -0.0834 0.0875  57  TRP D CE3 
6460  C CZ2 . TRP D 57  ? 0.5560 0.5111 0.7528 0.0851  -0.0884 0.0840  57  TRP D CZ2 
6461  C CZ3 . TRP D 57  ? 0.5948 0.5571 0.7832 0.0680  -0.0910 0.0828  57  TRP D CZ3 
6462  C CH2 . TRP D 57  ? 0.5674 0.5229 0.7538 0.0756  -0.0939 0.0816  57  TRP D CH2 
6463  N N   . LYS D 58  ? 0.5549 0.6074 0.8403 0.0676  -0.0775 0.1230  58  LYS D N   
6464  C CA  . LYS D 58  ? 0.5341 0.6107 0.8312 0.0611  -0.0894 0.1317  58  LYS D CA  
6465  C C   . LYS D 58  ? 0.5074 0.6112 0.8387 0.0680  -0.0878 0.1488  58  LYS D C   
6466  O O   . LYS D 58  ? 0.4840 0.6027 0.8271 0.0695  -0.0954 0.1582  58  LYS D O   
6467  C CB  . LYS D 58  ? 0.5598 0.6507 0.8498 0.0428  -0.0967 0.1297  58  LYS D CB  
6468  C CG  . LYS D 58  ? 0.5424 0.6600 0.8390 0.0323  -0.1097 0.1370  58  LYS D CG  
6469  C CD  . LYS D 58  ? 0.5311 0.6886 0.8556 0.0257  -0.1129 0.1527  58  LYS D CD  
6470  C CE  . LYS D 58  ? 0.5180 0.7056 0.8442 0.0102  -0.1267 0.1590  58  LYS D CE  
6471  N NZ  . LYS D 58  ? 0.5537 0.7405 0.8597 -0.0104 -0.1293 0.1467  58  LYS D NZ  
6472  N N   . SER D 59  ? 0.5590 0.6694 0.9077 0.0732  -0.0773 0.1541  59  SER D N   
6473  C CA  . SER D 59  ? 0.5330 0.6709 0.9185 0.0805  -0.0740 0.1723  59  SER D CA  
6474  C C   . SER D 59  ? 0.5077 0.6325 0.9051 0.0970  -0.0665 0.1759  59  SER D C   
6475  O O   . SER D 59  ? 0.4814 0.6287 0.9120 0.1043  -0.0641 0.1932  59  SER D O   
6476  C CB  . SER D 59  ? 0.5502 0.6967 0.9513 0.0818  -0.0628 0.1762  59  SER D CB  
6477  O OG  . SER D 59  ? 0.5632 0.6800 0.9564 0.0938  -0.0475 0.1666  59  SER D OG  
6478  N N   . THR D 60  ? 0.5530 0.6432 0.9258 0.1026  -0.0621 0.1607  60  THR D N   
6479  C CA  . THR D 60  ? 0.5353 0.6096 0.9161 0.1161  -0.0541 0.1610  60  THR D CA  
6480  C C   . THR D 60  ? 0.5095 0.5875 0.8893 0.1153  -0.0658 0.1653  60  THR D C   
6481  O O   . THR D 60  ? 0.4944 0.5608 0.8837 0.1258  -0.0595 0.1672  60  THR D O   
6482  C CB  . THR D 60  ? 0.5590 0.5964 0.9129 0.1206  -0.0437 0.1423  60  THR D CB  
6483  O OG1 . THR D 60  ? 0.5606 0.5815 0.8843 0.1147  -0.0542 0.1306  60  THR D OG1 
6484  C CG2 . THR D 60  ? 0.5903 0.6232 0.9350 0.1173  -0.0356 0.1359  60  THR D CG2 
6485  N N   . PHE D 61  ? 0.5452 0.6380 0.9135 0.1026  -0.0813 0.1663  61  PHE D N   
6486  C CA  . PHE D 61  ? 0.5247 0.6192 0.8872 0.1006  -0.0922 0.1684  61  PHE D CA  
6487  C C   . PHE D 61  ? 0.4921 0.6141 0.8894 0.1068  -0.0939 0.1902  61  PHE D C   
6488  O O   . PHE D 61  ? 0.4835 0.6355 0.9080 0.1063  -0.0934 0.2063  61  PHE D O   
6489  C CB  . PHE D 61  ? 0.5361 0.6398 0.8771 0.0840  -0.1063 0.1629  61  PHE D CB  
6490  C CG  . PHE D 61  ? 0.5653 0.6404 0.8734 0.0790  -0.1046 0.1434  61  PHE D CG  
6491  C CD1 . PHE D 61  ? 0.5728 0.6177 0.8684 0.0886  -0.0945 0.1321  61  PHE D CD1 
6492  C CD2 . PHE D 61  ? 0.5868 0.6664 0.8774 0.0641  -0.1122 0.1369  61  PHE D CD2 
6493  C CE1 . PHE D 61  ? 0.5956 0.6179 0.8632 0.0845  -0.0934 0.1174  61  PHE D CE1 
6494  C CE2 . PHE D 61  ? 0.6128 0.6663 0.8770 0.0609  -0.1092 0.1215  61  PHE D CE2 
6495  C CZ  . PHE D 61  ? 0.6138 0.6400 0.8673 0.0717  -0.1005 0.1131  61  PHE D CZ  
6496  N N   . THR D 62  ? 0.6522 0.7648 1.0500 0.1127  -0.0957 0.1921  62  THR D N   
6497  C CA  . THR D 62  ? 0.6208 0.7541 1.0520 0.1211  -0.0953 0.2135  62  THR D CA  
6498  C C   . THR D 62  ? 0.6030 0.7611 1.0312 0.1109  -0.1125 0.2235  62  THR D C   
6499  O O   . THR D 62  ? 0.6141 0.7608 1.0115 0.1008  -0.1216 0.2097  62  THR D O   
6500  C CB  . THR D 62  ? 0.6155 0.7187 1.0519 0.1354  -0.0823 0.2090  62  THR D CB  
6501  O OG1 . THR D 62  ? 0.6410 0.7152 1.0661 0.1404  -0.0677 0.1924  62  THR D OG1 
6502  C CG2 . THR D 62  ? 0.5874 0.7090 1.0671 0.1478  -0.0748 0.2330  62  THR D CG2 
6503  N N   . ASN D 63  ? 0.6952 0.8885 1.1567 0.1137  -0.1160 0.2487  63  ASN D N   
6504  C CA  . ASN D 63  ? 0.6750 0.8970 1.1376 0.1046  -0.1316 0.2624  63  ASN D CA  
6505  C C   . ASN D 63  ? 0.6924 0.9303 1.1275 0.0834  -0.1461 0.2532  63  ASN D C   
6506  O O   . ASN D 63  ? 0.6888 0.9344 1.1072 0.0730  -0.1578 0.2522  63  ASN D O   
6507  C CB  . ASN D 63  ? 0.6704 0.8669 1.1182 0.1091  -0.1306 0.2553  63  ASN D CB  
6508  C CG  . ASN D 63  ? 0.6700 0.8528 1.1365 0.1231  -0.1135 0.2618  63  ASN D CG  
6509  O OD1 . ASN D 63  ? 0.6772 0.8771 1.1702 0.1281  -0.1045 0.2766  63  ASN D OD1 
6510  N ND2 . ASN D 63  ? 0.6733 0.8252 1.1267 0.1285  -0.1088 0.2507  63  ASN D ND2 
6511  N N   . GLN D 64  ? 0.5859 0.8278 1.0158 0.0760  -0.1443 0.2458  64  GLN D N   
6512  C CA  . GLN D 64  ? 0.6099 0.8599 1.0122 0.0553  -0.1546 0.2334  64  GLN D CA  
6513  C C   . GLN D 64  ? 0.5926 0.8940 1.0093 0.0404  -0.1680 0.2525  64  GLN D C   
6514  O O   . GLN D 64  ? 0.5726 0.9062 1.0223 0.0442  -0.1672 0.2732  64  GLN D O   
6515  C CB  . GLN D 64  ? 0.6423 0.8757 1.0341 0.0527  -0.1464 0.2184  64  GLN D CB  
6516  C CG  . GLN D 64  ? 0.6767 0.8795 1.0293 0.0425  -0.1473 0.1934  64  GLN D CG  
6517  C CD  . GLN D 64  ? 0.6743 0.8424 1.0081 0.0513  -0.1452 0.1817  64  GLN D CD  
6518  O OE1 . GLN D 64  ? 0.6656 0.8125 1.0070 0.0674  -0.1359 0.1811  64  GLN D OE1 
6519  N NE2 . GLN D 64  ? 0.6831 0.8459 0.9924 0.0398  -0.1532 0.1719  64  GLN D NE2 
6520  N N   . THR D 65  ? 0.5682 0.8787 0.9607 0.0231  -0.1798 0.2461  65  THR D N   
6521  C CA  . THR D 65  ? 0.5543 0.9147 0.9536 0.0044  -0.1935 0.2612  65  THR D CA  
6522  C C   . THR D 65  ? 0.5837 0.9536 0.9677 -0.0159 -0.1956 0.2485  65  THR D C   
6523  O O   . THR D 65  ? 0.6193 0.9536 0.9809 -0.0174 -0.1878 0.2258  65  THR D O   
6524  C CB  . THR D 65  ? 0.5471 0.9151 0.9271 -0.0062 -0.2045 0.2608  65  THR D CB  
6525  O OG1 . THR D 65  ? 0.5274 0.9499 0.9174 -0.0239 -0.2180 0.2795  65  THR D OG1 
6526  C CG2 . THR D 65  ? 0.5858 0.9204 0.9241 -0.0189 -0.2036 0.2314  65  THR D CG2 
6527  N N   . SER D 66  ? 0.5549 0.9753 0.9521 -0.0323 -0.2063 0.2645  66  SER D N   
6528  C CA  . SER D 66  ? 0.5794 1.0139 0.9638 -0.0548 -0.2087 0.2535  66  SER D CA  
6529  C C   . SER D 66  ? 0.6115 1.0271 0.9543 -0.0755 -0.2117 0.2285  66  SER D C   
6530  O O   . SER D 66  ? 0.6405 1.0534 0.9677 -0.0931 -0.2095 0.2131  66  SER D O   
6531  C CB  . SER D 66  ? 0.5481 1.0462 0.9579 -0.0690 -0.2205 0.2782  66  SER D CB  
6532  O OG  . SER D 66  ? 0.5691 1.0806 0.9720 -0.0890 -0.2207 0.2685  66  SER D OG  
6533  N N   . SER D 67  ? 0.5731 0.9744 0.8987 -0.0737 -0.2150 0.2240  67  SER D N   
6534  C CA  . SER D 67  ? 0.6007 0.9876 0.8893 -0.0936 -0.2172 0.2023  67  SER D CA  
6535  C C   . SER D 67  ? 0.6392 0.9682 0.9042 -0.0844 -0.2049 0.1770  67  SER D C   
6536  O O   . SER D 67  ? 0.6661 0.9777 0.9020 -0.0989 -0.2036 0.1579  67  SER D O   
6537  C CB  . SER D 67  ? 0.5764 0.9831 0.8593 -0.0983 -0.2276 0.2123  67  SER D CB  
6538  O OG  . SER D 67  ? 0.5790 0.9452 0.8519 -0.0807 -0.2219 0.2041  67  SER D OG  
6539  N N   . SER D 68  ? 0.5172 0.8169 0.7940 -0.0614 -0.1952 0.1768  68  SER D N   
6540  C CA  . SER D 68  ? 0.5307 0.7796 0.7862 -0.0518 -0.1851 0.1561  68  SER D CA  
6541  C C   . SER D 68  ? 0.5601 0.7918 0.7949 -0.0673 -0.1786 0.1361  68  SER D C   
6542  O O   . SER D 68  ? 0.5668 0.8206 0.8081 -0.0811 -0.1792 0.1379  68  SER D O   
6543  C CB  . SER D 68  ? 0.5212 0.7461 0.7926 -0.0264 -0.1760 0.1601  68  SER D CB  
6544  O OG  . SER D 68  ? 0.5294 0.7535 0.8100 -0.0257 -0.1690 0.1588  68  SER D OG  
6545  N N   . LYS D 69  ? 0.5375 0.7300 0.7486 -0.0655 -0.1718 0.1176  69  LYS D N   
6546  C CA  . LYS D 69  ? 0.5824 0.7533 0.7748 -0.0784 -0.1632 0.0988  69  LYS D CA  
6547  C C   . LYS D 69  ? 0.6001 0.7592 0.8028 -0.0704 -0.1544 0.0984  69  LYS D C   
6548  O O   . LYS D 69  ? 0.6330 0.7837 0.8266 -0.0836 -0.1477 0.0870  69  LYS D O   
6549  C CB  . LYS D 69  ? 0.6081 0.7398 0.7775 -0.0746 -0.1567 0.0825  69  LYS D CB  
6550  C CG  . LYS D 69  ? 0.6068 0.7468 0.7594 -0.0905 -0.1619 0.0763  69  LYS D CG  
6551  C CD  . LYS D 69  ? 0.6032 0.7178 0.7470 -0.0760 -0.1609 0.0730  69  LYS D CD  
6552  C CE  . LYS D 69  ? 0.6109 0.7281 0.7354 -0.0921 -0.1630 0.0640  69  LYS D CE  
6553  N NZ  . LYS D 69  ? 0.6116 0.7024 0.7277 -0.0784 -0.1607 0.0597  69  LYS D NZ  
6554  N N   . LEU D 70  ? 0.5239 0.6815 0.7453 -0.0498 -0.1529 0.1100  70  LEU D N   
6555  C CA  . LEU D 70  ? 0.5404 0.6876 0.7711 -0.0418 -0.1438 0.1100  70  LEU D CA  
6556  C C   . LEU D 70  ? 0.5363 0.7188 0.7849 -0.0544 -0.1461 0.1193  70  LEU D C   
6557  O O   . LEU D 70  ? 0.5485 0.7262 0.8076 -0.0481 -0.1384 0.1210  70  LEU D O   
6558  C CB  . LEU D 70  ? 0.5155 0.6498 0.7593 -0.0173 -0.1399 0.1180  70  LEU D CB  
6559  C CG  . LEU D 70  ? 0.5119 0.6118 0.7400 -0.0039 -0.1370 0.1093  70  LEU D CG  
6560  C CD1 . LEU D 70  ? 0.4978 0.5804 0.7342 0.0155  -0.1289 0.1118  70  LEU D CD1 
6561  C CD2 . LEU D 70  ? 0.5531 0.6257 0.7562 -0.0119 -0.1324 0.0926  70  LEU D CD2 
6562  N N   . SER D 71  ? 0.4979 0.7167 0.7496 -0.0728 -0.1563 0.1254  71  SER D N   
6563  C CA  . SER D 71  ? 0.4984 0.7530 0.7651 -0.0884 -0.1591 0.1330  71  SER D CA  
6564  C C   . SER D 71  ? 0.5240 0.7598 0.7770 -0.1020 -0.1495 0.1164  71  SER D C   
6565  O O   . SER D 71  ? 0.5257 0.7827 0.7933 -0.1102 -0.1482 0.1218  71  SER D O   
6566  C CB  . SER D 71  ? 0.5021 0.7994 0.7690 -0.1094 -0.1726 0.1405  71  SER D CB  
6567  O OG  . SER D 71  ? 0.4916 0.8037 0.7693 -0.0972 -0.1810 0.1559  71  SER D OG  
6568  N N   . SER D 72  ? 0.5353 0.7325 0.7625 -0.1046 -0.1421 0.0975  72  SER D N   
6569  C CA  . SER D 72  ? 0.5744 0.7506 0.7891 -0.1176 -0.1311 0.0820  72  SER D CA  
6570  C C   . SER D 72  ? 0.5960 0.7508 0.8197 -0.1017 -0.1201 0.0834  72  SER D C   
6571  O O   . SER D 72  ? 0.6253 0.7653 0.8427 -0.1116 -0.1104 0.0736  72  SER D O   
6572  C CB  . SER D 72  ? 0.6015 0.7424 0.7893 -0.1233 -0.1247 0.0634  72  SER D CB  
6573  O OG  . SER D 72  ? 0.6042 0.7172 0.7873 -0.1004 -0.1231 0.0640  72  SER D OG  
6574  N N   . TRP D 73  ? 0.5730 0.7251 0.8105 -0.0783 -0.1204 0.0949  73  TRP D N   
6575  C CA  . TRP D 73  ? 0.5930 0.7261 0.8371 -0.0638 -0.1096 0.0961  73  TRP D CA  
6576  C C   . TRP D 73  ? 0.5802 0.7464 0.8484 -0.0695 -0.1098 0.1077  73  TRP D C   
6577  O O   . TRP D 73  ? 0.5506 0.7369 0.8410 -0.0568 -0.1124 0.1227  73  TRP D O   
6578  C CB  . TRP D 73  ? 0.5777 0.6936 0.8245 -0.0387 -0.1082 0.1014  73  TRP D CB  
6579  C CG  . TRP D 73  ? 0.5897 0.6724 0.8141 -0.0319 -0.1069 0.0906  73  TRP D CG  
6580  C CD1 . TRP D 73  ? 0.6069 0.6785 0.8128 -0.0444 -0.1085 0.0793  73  TRP D CD1 
6581  C CD2 . TRP D 73  ? 0.5792 0.6367 0.7983 -0.0117 -0.1032 0.0901  73  TRP D CD2 
6582  N NE1 . TRP D 73  ? 0.6124 0.6547 0.8040 -0.0319 -0.1063 0.0734  73  TRP D NE1 
6583  C CE2 . TRP D 73  ? 0.5915 0.6258 0.7903 -0.0126 -0.1039 0.0799  73  TRP D CE2 
6584  C CE3 . TRP D 73  ? 0.5553 0.6082 0.7845 0.0058  -0.0986 0.0966  73  TRP D CE3 
6585  C CZ2 . TRP D 73  ? 0.5738 0.5836 0.7630 0.0032  -0.1017 0.0774  73  TRP D CZ2 
6586  C CZ3 . TRP D 73  ? 0.5380 0.5650 0.7551 0.0200  -0.0959 0.0922  73  TRP D CZ3 
6587  C CH2 . TRP D 73  ? 0.5434 0.5506 0.7411 0.0184  -0.0983 0.0833  73  TRP D CH2 
6588  N N   . VAL D 74  ? 0.6206 0.7921 0.8861 -0.0887 -0.1057 0.1010  74  VAL D N   
6589  C CA  . VAL D 74  ? 0.6033 0.8123 0.8928 -0.0972 -0.1077 0.1128  74  VAL D CA  
6590  C C   . VAL D 74  ? 0.6324 0.8264 0.9258 -0.0958 -0.0946 0.1096  74  VAL D C   
6591  O O   . VAL D 74  ? 0.6248 0.8277 0.9381 -0.0819 -0.0906 0.1211  74  VAL D O   
6592  C CB  . VAL D 74  ? 0.5875 0.8307 0.8757 -0.1258 -0.1171 0.1111  74  VAL D CB  
6593  C CG1 . VAL D 74  ? 0.5637 0.8518 0.8798 -0.1345 -0.1210 0.1260  74  VAL D CG1 
6594  C CG2 . VAL D 74  ? 0.5594 0.8182 0.8422 -0.1276 -0.1299 0.1150  74  VAL D CG2 
6595  N N   . ASN D 75  ? 0.6865 0.8565 0.9617 -0.1098 -0.0864 0.0944  75  ASN D N   
6596  C CA  . ASN D 75  ? 0.7080 0.8677 0.9907 -0.1066 -0.0742 0.0951  75  ASN D CA  
6597  C C   . ASN D 75  ? 0.7421 0.8550 1.0073 -0.0906 -0.0625 0.0872  75  ASN D C   
6598  O O   . ASN D 75  ? 0.7562 0.8421 1.0007 -0.0921 -0.0611 0.0761  75  ASN D O   
6599  C CB  . ASN D 75  ? 0.7151 0.8868 0.9988 -0.1331 -0.0702 0.0883  75  ASN D CB  
6600  C CG  . ASN D 75  ? 0.7440 0.8793 1.0032 -0.1454 -0.0609 0.0699  75  ASN D CG  
6601  O OD1 . ASN D 75  ? 0.7482 0.8633 0.9898 -0.1426 -0.0628 0.0618  75  ASN D OD1 
6602  N ND2 . ASN D 75  ? 0.7625 0.8886 1.0221 -0.1587 -0.0494 0.0635  75  ASN D ND2 
6603  N N   . PRO D 76  ? 0.7148 0.8191 0.9881 -0.0747 -0.0542 0.0937  76  PRO D N   
6604  C CA  . PRO D 76  ? 0.7437 0.8085 1.0001 -0.0585 -0.0450 0.0888  76  PRO D CA  
6605  C C   . PRO D 76  ? 0.7690 0.8064 1.0120 -0.0680 -0.0332 0.0794  76  PRO D C   
6606  O O   . PRO D 76  ? 0.7867 0.7929 1.0156 -0.0557 -0.0260 0.0769  76  PRO D O   
6607  C CB  . PRO D 76  ? 0.7443 0.8147 1.0147 -0.0413 -0.0396 0.0993  76  PRO D CB  
6608  C CG  . PRO D 76  ? 0.7070 0.8178 1.0027 -0.0434 -0.0480 0.1106  76  PRO D CG  
6609  C CD  . PRO D 76  ? 0.6968 0.8296 0.9958 -0.0680 -0.0540 0.1075  76  PRO D CD  
6610  N N   . ASN D 77  ? 0.7932 0.8416 1.0407 -0.0897 -0.0306 0.0747  77  ASN D N   
6611  C CA  . ASN D 77  ? 0.8130 0.8330 1.0498 -0.0993 -0.0172 0.0657  77  ASN D CA  
6612  C C   . ASN D 77  ? 0.8184 0.8093 1.0354 -0.1012 -0.0155 0.0546  77  ASN D C   
6613  O O   . ASN D 77  ? 0.8075 0.8080 1.0193 -0.1077 -0.0252 0.0498  77  ASN D O   
6614  C CB  . ASN D 77  ? 0.8102 0.8497 1.0571 -0.1246 -0.0142 0.0618  77  ASN D CB  
6615  C CG  . ASN D 77  ? 0.8120 0.8650 1.0762 -0.1222 -0.0078 0.0713  77  ASN D CG  
6616  O OD1 . ASN D 77  ? 0.8218 0.8601 1.0861 -0.1031 -0.0012 0.0780  77  ASN D OD1 
6617  N ND2 . ASN D 77  ? 0.8020 0.8845 1.0806 -0.1427 -0.0093 0.0717  77  ASN D ND2 
6618  N N   . THR D 78  ? 0.8979 0.8538 1.1049 -0.0951 -0.0024 0.0517  78  THR D N   
6619  C CA  . THR D 78  ? 0.8996 0.8269 1.0919 -0.1000 0.0034  0.0412  78  THR D CA  
6620  C C   . THR D 78  ? 0.9017 0.8360 1.0938 -0.1281 0.0063  0.0286  78  THR D C   
6621  O O   . THR D 78  ? 0.9015 0.8611 1.1047 -0.1437 0.0047  0.0290  78  THR D O   
6622  C CB  . THR D 78  ? 0.9049 0.7967 1.0915 -0.0892 0.0186  0.0436  78  THR D CB  
6623  O OG1 . THR D 78  ? 0.9036 0.7965 1.0912 -0.0676 0.0164  0.0558  78  THR D OG1 
6624  C CG2 . THR D 78  ? 0.8985 0.7613 1.0724 -0.0857 0.0232  0.0371  78  THR D CG2 
6625  N N   . SER D 79  ? 0.8694 0.7823 1.0488 -0.1353 0.0108  0.0171  79  SER D N   
6626  C CA  . SER D 79  ? 0.8704 0.7867 1.0442 -0.1625 0.0137  0.0020  79  SER D CA  
6627  C C   . SER D 79  ? 0.8610 0.8149 1.0346 -0.1718 -0.0046 0.0017  79  SER D C   
6628  O O   . SER D 79  ? 0.8555 0.8174 1.0216 -0.1955 -0.0048 -0.0110 79  SER D O   
6629  C CB  . SER D 79  ? 0.8754 0.7947 1.0564 -0.1848 0.0248  -0.0039 79  SER D CB  
6630  O OG  . SER D 79  ? 0.8726 0.8318 1.0680 -0.1896 0.0140  0.0052  79  SER D OG  
6631  N N   . SER D 80  ? 0.7786 0.7567 0.9606 -0.1549 -0.0191 0.0154  80  SER D N   
6632  C CA  . SER D 80  ? 0.7577 0.7651 0.9388 -0.1577 -0.0357 0.0176  80  SER D CA  
6633  C C   . SER D 80  ? 0.7516 0.7485 0.9301 -0.1306 -0.0421 0.0260  80  SER D C   
6634  O O   . SER D 80  ? 0.7404 0.7410 0.9110 -0.1293 -0.0506 0.0238  80  SER D O   
6635  C CB  . SER D 80  ? 0.7365 0.7904 0.9350 -0.1671 -0.0472 0.0276  80  SER D CB  
6636  O OG  . SER D 80  ? 0.7096 0.7942 0.9082 -0.1721 -0.0629 0.0312  80  SER D OG  
6637  N N   . PHE D 81  ? 0.6904 0.6748 0.8749 -0.1101 -0.0376 0.0352  81  PHE D N   
6638  C CA  . PHE D 81  ? 0.6879 0.6591 0.8680 -0.0858 -0.0416 0.0414  81  PHE D CA  
6639  C C   . PHE D 81  ? 0.6912 0.6310 0.8550 -0.0831 -0.0363 0.0325  81  PHE D C   
6640  O O   . PHE D 81  ? 0.6816 0.6207 0.8394 -0.0741 -0.0444 0.0329  81  PHE D O   
6641  C CB  . PHE D 81  ? 0.6981 0.6591 0.8837 -0.0681 -0.0351 0.0505  81  PHE D CB  
6642  C CG  . PHE D 81  ? 0.6959 0.6434 0.8751 -0.0453 -0.0382 0.0557  81  PHE D CG  
6643  C CD1 . PHE D 81  ? 0.6857 0.6512 0.8697 -0.0356 -0.0500 0.0613  81  PHE D CD1 
6644  C CD2 . PHE D 81  ? 0.6952 0.6131 0.8644 -0.0340 -0.0290 0.0560  81  PHE D CD2 
6645  C CE1 . PHE D 81  ? 0.6793 0.6319 0.8568 -0.0167 -0.0520 0.0646  81  PHE D CE1 
6646  C CE2 . PHE D 81  ? 0.6754 0.5840 0.8378 -0.0154 -0.0325 0.0606  81  PHE D CE2 
6647  C CZ  . PHE D 81  ? 0.6621 0.5873 0.8278 -0.0075 -0.0438 0.0638  81  PHE D CZ  
6648  N N   . CYS D 82  ? 0.7834 0.6968 0.9418 -0.0905 -0.0216 0.0250  82  CYS D N   
6649  C CA  . CYS D 82  ? 0.7818 0.6630 0.9285 -0.0863 -0.0132 0.0184  82  CYS D CA  
6650  C C   . CYS D 82  ? 0.7836 0.6626 0.9218 -0.1063 -0.0113 0.0040  82  CYS D C   
6651  O O   . CYS D 82  ? 0.7817 0.6330 0.9119 -0.1043 -0.0018 -0.0025 82  CYS D O   
6652  C CB  . CYS D 82  ? 0.7863 0.6379 0.9341 -0.0822 0.0041  0.0197  82  CYS D CB  
6653  S SG  . CYS D 82  ? 0.7789 0.6270 0.9307 -0.0566 0.0035  0.0362  82  CYS D SG  
6654  N N   . THR D 83  ? 0.7261 0.6342 0.8659 -0.1260 -0.0193 -0.0007 83  THR D N   
6655  C CA  . THR D 83  ? 0.7276 0.6355 0.8562 -0.1473 -0.0174 -0.0154 83  THR D CA  
6656  C C   . THR D 83  ? 0.7110 0.6546 0.8376 -0.1541 -0.0355 -0.0134 83  THR D C   
6657  O O   . THR D 83  ? 0.7061 0.6470 0.8205 -0.1637 -0.0364 -0.0230 83  THR D O   
6658  C CB  . THR D 83  ? 0.7336 0.6392 0.8618 -0.1737 -0.0052 -0.0274 83  THR D CB  
6659  O OG1 . THR D 83  ? 0.7347 0.6679 0.8762 -0.1778 -0.0110 -0.0187 83  THR D OG1 
6660  C CG2 . THR D 83  ? 0.7386 0.6007 0.8654 -0.1702 0.0165  -0.0332 83  THR D CG2 
6661  N N   . SER D 84  ? 0.6637 0.6411 0.8031 -0.1494 -0.0490 -0.0003 84  SER D N   
6662  C CA  . SER D 84  ? 0.6480 0.6639 0.7889 -0.1593 -0.0652 0.0037  84  SER D CA  
6663  C C   . SER D 84  ? 0.6258 0.6563 0.7754 -0.1366 -0.0787 0.0191  84  SER D C   
6664  O O   . SER D 84  ? 0.6115 0.6700 0.7618 -0.1419 -0.0916 0.0237  84  SER D O   
6665  C CB  . SER D 84  ? 0.6489 0.7014 0.8007 -0.1799 -0.0699 0.0066  84  SER D CB  
6666  O OG  . SER D 84  ? 0.6299 0.7057 0.8017 -0.1648 -0.0780 0.0242  84  SER D OG  
6667  N N   . TRP D 85  ? 0.6559 0.6690 0.8117 -0.1126 -0.0756 0.0271  85  TRP D N   
6668  C CA  . TRP D 85  ? 0.6369 0.6608 0.8008 -0.0919 -0.0861 0.0398  85  TRP D CA  
6669  C C   . TRP D 85  ? 0.6331 0.6400 0.7840 -0.0839 -0.0888 0.0355  85  TRP D C   
6670  O O   . TRP D 85  ? 0.6515 0.6257 0.7913 -0.0779 -0.0794 0.0280  85  TRP D O   
6671  C CB  . TRP D 85  ? 0.6489 0.6595 0.8212 -0.0716 -0.0806 0.0478  85  TRP D CB  
6672  C CG  . TRP D 85  ? 0.6449 0.6786 0.8346 -0.0744 -0.0804 0.0564  85  TRP D CG  
6673  C CD1 . TRP D 85  ? 0.6424 0.6973 0.8387 -0.0951 -0.0798 0.0546  85  TRP D CD1 
6674  C CD2 . TRP D 85  ? 0.6418 0.6802 0.8451 -0.0565 -0.0796 0.0677  85  TRP D CD2 
6675  N NE1 . TRP D 85  ? 0.6370 0.7106 0.8520 -0.0901 -0.0793 0.0655  85  TRP D NE1 
6676  C CE2 . TRP D 85  ? 0.6371 0.7000 0.8566 -0.0662 -0.0784 0.0733  85  TRP D CE2 
6677  C CE3 . TRP D 85  ? 0.6398 0.6644 0.8428 -0.0345 -0.0791 0.0727  85  TRP D CE3 
6678  C CZ2 . TRP D 85  ? 0.6324 0.7051 0.8685 -0.0533 -0.0758 0.0842  85  TRP D CZ2 
6679  C CZ3 . TRP D 85  ? 0.6312 0.6645 0.8487 -0.0230 -0.0760 0.0820  85  TRP D CZ3 
6680  C CH2 . TRP D 85  ? 0.6305 0.6871 0.8649 -0.0318 -0.0740 0.0878  85  TRP D CH2 
6681  N N   . TYR D 86  ? 0.6538 0.6840 0.8077 -0.0833 -0.1014 0.0417  86  TYR D N   
6682  C CA  . TYR D 86  ? 0.6471 0.6645 0.7896 -0.0768 -0.1046 0.0382  86  TYR D CA  
6683  C C   . TYR D 86  ? 0.6540 0.6453 0.7960 -0.0528 -0.1012 0.0414  86  TYR D C   
6684  O O   . TYR D 86  ? 0.6416 0.6386 0.7951 -0.0384 -0.1034 0.0513  86  TYR D O   
6685  C CB  . TYR D 86  ? 0.6089 0.6587 0.7575 -0.0794 -0.1189 0.0474  86  TYR D CB  
6686  C CG  . TYR D 86  ? 0.5990 0.6372 0.7369 -0.0725 -0.1225 0.0447  86  TYR D CG  
6687  C CD1 . TYR D 86  ? 0.5794 0.6081 0.7226 -0.0507 -0.1255 0.0522  86  TYR D CD1 
6688  C CD2 . TYR D 86  ? 0.6064 0.6432 0.7288 -0.0890 -0.1220 0.0339  86  TYR D CD2 
6689  C CE1 . TYR D 86  ? 0.5677 0.5867 0.7022 -0.0452 -0.1287 0.0500  86  TYR D CE1 
6690  C CE2 . TYR D 86  ? 0.5989 0.6257 0.7124 -0.0829 -0.1246 0.0318  86  TYR D CE2 
6691  C CZ  . TYR D 86  ? 0.5803 0.5987 0.7004 -0.0608 -0.1284 0.0403  86  TYR D CZ  
6692  O OH  . TYR D 86  ? 0.5711 0.5803 0.6830 -0.0556 -0.1309 0.0382  86  TYR D OH  
6693  N N   . GLY D 87  ? 0.6235 0.5870 0.7522 -0.0494 -0.0950 0.0329  87  GLY D N   
6694  C CA  . GLY D 87  ? 0.6260 0.5688 0.7528 -0.0289 -0.0936 0.0362  87  GLY D CA  
6695  C C   . GLY D 87  ? 0.6418 0.5646 0.7692 -0.0193 -0.0837 0.0375  87  GLY D C   
6696  O O   . GLY D 87  ? 0.6043 0.5140 0.7296 -0.0031 -0.0834 0.0414  87  GLY D O   
6697  N N   . VAL D 88  ? 0.6292 0.5506 0.7592 -0.0296 -0.0755 0.0349  88  VAL D N   
6698  C CA  . VAL D 88  ? 0.6287 0.5308 0.7590 -0.0210 -0.0652 0.0373  88  VAL D CA  
6699  C C   . VAL D 88  ? 0.6352 0.5143 0.7592 -0.0310 -0.0518 0.0287  88  VAL D C   
6700  O O   . VAL D 88  ? 0.6471 0.5294 0.7685 -0.0493 -0.0490 0.0195  88  VAL D O   
6701  C CB  . VAL D 88  ? 0.6415 0.5590 0.7831 -0.0211 -0.0645 0.0439  88  VAL D CB  
6702  C CG1 . VAL D 88  ? 0.6294 0.5725 0.7811 -0.0148 -0.0759 0.0519  88  VAL D CG1 
6703  C CG2 . VAL D 88  ? 0.6568 0.5818 0.8018 -0.0410 -0.0591 0.0385  88  VAL D CG2 
6704  N N   . ALA D 89  ? 0.6642 0.5201 0.7860 -0.0194 -0.0428 0.0320  89  ALA D N   
6705  C CA  . ALA D 89  ? 0.6703 0.5013 0.7899 -0.0258 -0.0274 0.0266  89  ALA D CA  
6706  C C   . ALA D 89  ? 0.6617 0.4798 0.7848 -0.0146 -0.0189 0.0358  89  ALA D C   
6707  O O   . ALA D 89  ? 0.6386 0.4590 0.7606 0.0015  -0.0244 0.0450  89  ALA D O   
6708  C CB  . ALA D 89  ? 0.6573 0.4703 0.7708 -0.0223 -0.0239 0.0222  89  ALA D CB  
6709  N N   . CYS D 90  ? 0.6724 0.4772 0.7990 -0.0241 -0.0050 0.0330  90  CYS D N   
6710  C CA  . CYS D 90  ? 0.6679 0.4625 0.7984 -0.0153 0.0037  0.0428  90  CYS D CA  
6711  C C   . CYS D 90  ? 0.6592 0.4242 0.7909 -0.0117 0.0197  0.0449  90  CYS D C   
6712  O O   . CYS D 90  ? 0.6645 0.4144 0.7959 -0.0213 0.0285  0.0354  90  CYS D O   
6713  C CB  . CYS D 90  ? 0.6923 0.4966 0.8294 -0.0277 0.0081  0.0414  90  CYS D CB  
6714  S SG  . CYS D 90  ? 0.7058 0.5468 0.8474 -0.0336 -0.0076 0.0411  90  CYS D SG  
6715  N N   . SER D 91  ? 0.6695 0.4269 0.8030 0.0022  0.0243  0.0582  91  SER D N   
6716  C CA  . SER D 91  ? 0.6649 0.3968 0.8042 0.0057  0.0418  0.0647  91  SER D CA  
6717  C C   . SER D 91  ? 0.6760 0.4091 0.8194 0.0056  0.0485  0.0729  91  SER D C   
6718  O O   . SER D 91  ? 0.6713 0.4206 0.8110 0.0145  0.0393  0.0812  91  SER D O   
6719  C CB  . SER D 91  ? 0.6411 0.3650 0.7794 0.0239  0.0407  0.0769  91  SER D CB  
6720  O OG  . SER D 91  ? 0.6506 0.3512 0.7978 0.0287  0.0582  0.0864  91  SER D OG  
6721  N N   . LEU D 92  ? 0.6584 0.3738 0.8093 -0.0056 0.0655  0.0695  92  LEU D N   
6722  C CA  . LEU D 92  ? 0.6683 0.3830 0.8244 -0.0075 0.0740  0.0769  92  LEU D CA  
6723  C C   . LEU D 92  ? 0.6521 0.3947 0.8059 -0.0124 0.0615  0.0745  92  LEU D C   
6724  O O   . LEU D 92  ? 0.6506 0.4009 0.8050 -0.0059 0.0618  0.0846  92  LEU D O   
6725  C CB  . LEU D 92  ? 0.6741 0.3800 0.8314 0.0107  0.0793  0.0966  92  LEU D CB  
6726  C CG  . LEU D 92  ? 0.6908 0.3712 0.8549 0.0186  0.0926  0.1041  92  LEU D CG  
6727  C CD1 . LEU D 92  ? 0.6944 0.3747 0.8595 0.0367  0.0943  0.1267  92  LEU D CD1 
6728  C CD2 . LEU D 92  ? 0.7174 0.3717 0.8925 0.0046  0.1142  0.0964  92  LEU D CD2 
6729  N N   . GLY D 93  ? 0.6744 0.4333 0.8264 -0.0241 0.0512  0.0617  93  GLY D N   
6730  C CA  . GLY D 93  ? 0.6891 0.4757 0.8433 -0.0296 0.0407  0.0603  93  GLY D CA  
6731  C C   . GLY D 93  ? 0.6772 0.4831 0.8270 -0.0145 0.0257  0.0673  93  GLY D C   
6732  O O   . GLY D 93  ? 0.6884 0.5166 0.8427 -0.0169 0.0189  0.0679  93  GLY D O   
6733  N N   . SER D 94  ? 0.7215 0.5202 0.8636 0.0002  0.0209  0.0723  94  SER D N   
6734  C CA  . SER D 94  ? 0.7037 0.5181 0.8403 0.0134  0.0082  0.0774  94  SER D CA  
6735  C C   . SER D 94  ? 0.6847 0.5015 0.8162 0.0165  -0.0027 0.0721  94  SER D C   
6736  O O   . SER D 94  ? 0.6771 0.4779 0.8065 0.0161  0.0013  0.0696  94  SER D O   
6737  C CB  . SER D 94  ? 0.6875 0.4946 0.8178 0.0281  0.0119  0.0900  94  SER D CB  
6738  O OG  . SER D 94  ? 0.6659 0.4849 0.7882 0.0392  0.0004  0.0924  94  SER D OG  
6739  N N   . ILE D 95  ? 0.6837 0.5198 0.8146 0.0201  -0.0151 0.0709  95  ILE D N   
6740  C CA  . ILE D 95  ? 0.6649 0.5052 0.7920 0.0223  -0.0257 0.0662  95  ILE D CA  
6741  C C   . ILE D 95  ? 0.6321 0.4601 0.7505 0.0359  -0.0269 0.0715  95  ILE D C   
6742  O O   . ILE D 95  ? 0.6174 0.4470 0.7309 0.0465  -0.0276 0.0790  95  ILE D O   
6743  C CB  . ILE D 95  ? 0.6594 0.5229 0.7908 0.0234  -0.0370 0.0655  95  ILE D CB  
6744  C CG1 . ILE D 95  ? 0.6384 0.5058 0.7664 0.0252  -0.0474 0.0614  95  ILE D CG1 
6745  C CG2 . ILE D 95  ? 0.6405 0.5094 0.7703 0.0354  -0.0375 0.0724  95  ILE D CG2 
6746  C CD1 . ILE D 95  ? 0.6310 0.5208 0.7664 0.0253  -0.0574 0.0618  95  ILE D CD1 
6747  N N   . ILE D 96  ? 0.6424 0.4591 0.7588 0.0347  -0.0264 0.0678  96  ILE D N   
6748  C CA  . ILE D 96  ? 0.6326 0.4411 0.7432 0.0467  -0.0288 0.0733  96  ILE D CA  
6749  C C   . ILE D 96  ? 0.6202 0.4344 0.7282 0.0474  -0.0392 0.0674  96  ILE D C   
6750  O O   . ILE D 96  ? 0.6167 0.4282 0.7202 0.0572  -0.0434 0.0718  96  ILE D O   
6751  C CB  . ILE D 96  ? 0.6497 0.4370 0.7632 0.0481  -0.0158 0.0780  96  ILE D CB  
6752  C CG1 . ILE D 96  ? 0.6584 0.4347 0.7765 0.0350  -0.0085 0.0670  96  ILE D CG1 
6753  C CG2 . ILE D 96  ? 0.6629 0.4442 0.7789 0.0496  -0.0054 0.0869  96  ILE D CG2 
6754  C CD1 . ILE D 96  ? 0.6743 0.4280 0.7968 0.0382  0.0044  0.0702  96  ILE D CD1 
6755  N N   . ARG D 97  ? 0.6939 0.5184 0.8047 0.0369  -0.0441 0.0588  97  ARG D N   
6756  C CA  . ARG D 97  ? 0.6829 0.5124 0.7915 0.0353  -0.0526 0.0532  97  ARG D CA  
6757  C C   . ARG D 97  ? 0.6916 0.5427 0.8040 0.0292  -0.0622 0.0502  97  ARG D C   
6758  O O   . ARG D 97  ? 0.7269 0.5866 0.8445 0.0174  -0.0599 0.0471  97  ARG D O   
6759  C CB  . ARG D 97  ? 0.7042 0.5200 0.8127 0.0256  -0.0447 0.0457  97  ARG D CB  
6760  C CG  . ARG D 97  ? 0.7000 0.5208 0.8053 0.0225  -0.0522 0.0395  97  ARG D CG  
6761  C CD  . ARG D 97  ? 0.7172 0.5199 0.8213 0.0148  -0.0410 0.0321  97  ARG D CD  
6762  N NE  . ARG D 97  ? 0.7006 0.4829 0.8077 0.0251  -0.0301 0.0388  97  ARG D NE  
6763  C CZ  . ARG D 97  ? 0.7087 0.4710 0.8184 0.0220  -0.0166 0.0350  97  ARG D CZ  
6764  N NH1 . ARG D 97  ? 0.7327 0.4911 0.8395 0.0074  -0.0117 0.0220  97  ARG D NH1 
6765  N NH2 . ARG D 97  ? 0.6919 0.4385 0.8077 0.0334  -0.0069 0.0449  97  ARG D NH2 
6766  N N   . LEU D 98  ? 0.6432 0.5040 0.7546 0.0369  -0.0724 0.0520  98  LEU D N   
6767  C CA  . LEU D 98  ? 0.6418 0.5233 0.7597 0.0337  -0.0812 0.0519  98  LEU D CA  
6768  C C   . LEU D 98  ? 0.6216 0.5062 0.7368 0.0346  -0.0894 0.0495  98  LEU D C   
6769  O O   . LEU D 98  ? 0.5831 0.4624 0.6943 0.0452  -0.0929 0.0515  98  LEU D O   
6770  C CB  . LEU D 98  ? 0.6157 0.5053 0.7377 0.0434  -0.0830 0.0578  98  LEU D CB  
6771  C CG  . LEU D 98  ? 0.6062 0.5170 0.7397 0.0424  -0.0897 0.0605  98  LEU D CG  
6772  C CD1 . LEU D 98  ? 0.6460 0.5720 0.7895 0.0303  -0.0879 0.0614  98  LEU D CD1 
6773  C CD2 . LEU D 98  ? 0.5776 0.4901 0.7139 0.0541  -0.0890 0.0647  98  LEU D CD2 
6774  N N   . ASN D 99  ? 0.6588 0.5530 0.7754 0.0223  -0.0922 0.0451  99  ASN D N   
6775  C CA  . ASN D 99  ? 0.6502 0.5472 0.7631 0.0206  -0.0987 0.0424  99  ASN D CA  
6776  C C   . ASN D 99  ? 0.6481 0.5705 0.7689 0.0148  -0.1080 0.0459  99  ASN D C   
6777  O O   . ASN D 99  ? 0.6899 0.6257 0.8121 0.0001  -0.1087 0.0434  99  ASN D O   
6778  C CB  . ASN D 99  ? 0.6925 0.5770 0.7980 0.0098  -0.0919 0.0339  99  ASN D CB  
6779  C CG  . ASN D 99  ? 0.6831 0.5663 0.7834 0.0100  -0.0964 0.0308  99  ASN D CG  
6780  O OD1 . ASN D 99  ? 0.6393 0.5286 0.7413 0.0194  -0.1047 0.0355  99  ASN D OD1 
6781  N ND2 . ASN D 99  ? 0.7187 0.5929 0.8128 -0.0012 -0.0896 0.0222  99  ASN D ND2 
6782  N N   . LEU D 100 ? 0.6157 0.5458 0.7424 0.0255  -0.1147 0.0522  100 LEU D N   
6783  C CA  . LEU D 100 ? 0.5971 0.5517 0.7353 0.0228  -0.1226 0.0590  100 LEU D CA  
6784  C C   . LEU D 100 ? 0.5620 0.5188 0.6996 0.0277  -0.1296 0.0609  100 LEU D C   
6785  O O   . LEU D 100 ? 0.5275 0.4966 0.6764 0.0342  -0.1344 0.0689  100 LEU D O   
6786  C CB  . LEU D 100 ? 0.5751 0.5386 0.7267 0.0310  -0.1214 0.0667  100 LEU D CB  
6787  C CG  . LEU D 100 ? 0.6091 0.5766 0.7649 0.0251  -0.1152 0.0669  100 LEU D CG  
6788  C CD1 . LEU D 100 ? 0.5858 0.5605 0.7552 0.0351  -0.1127 0.0744  100 LEU D CD1 
6789  C CD2 . LEU D 100 ? 0.6411 0.6295 0.8009 0.0078  -0.1186 0.0670  100 LEU D CD2 
6790  N N   . THR D 101 ? 0.5870 0.5309 0.7127 0.0251  -0.1290 0.0541  101 THR D N   
6791  C CA  . THR D 101 ? 0.5593 0.5057 0.6837 0.0279  -0.1353 0.0555  101 THR D CA  
6792  C C   . THR D 101 ? 0.5568 0.5293 0.6882 0.0184  -0.1428 0.0615  101 THR D C   
6793  O O   . THR D 101 ? 0.5903 0.5749 0.7190 0.0038  -0.1427 0.0592  101 THR D O   
6794  C CB  . THR D 101 ? 0.5821 0.5118 0.6936 0.0248  -0.1318 0.0470  101 THR D CB  
6795  O OG1 . THR D 101 ? 0.5844 0.4935 0.6912 0.0319  -0.1243 0.0437  101 THR D OG1 
6796  C CG2 . THR D 101 ? 0.5480 0.4772 0.6586 0.0305  -0.1374 0.0487  101 THR D CG2 
6797  N N   . ASN D 102 ? 0.5769 0.5587 0.7174 0.0259  -0.1488 0.0698  102 ASN D N   
6798  C CA  . ASN D 102 ? 0.5655 0.5729 0.7130 0.0184  -0.1567 0.0783  102 ASN D CA  
6799  C C   . ASN D 102 ? 0.5781 0.6111 0.7344 0.0074  -0.1589 0.0845  102 ASN D C   
6800  O O   . ASN D 102 ? 0.5899 0.6433 0.7425 -0.0076 -0.1638 0.0858  102 ASN D O   
6801  C CB  . ASN D 102 ? 0.5830 0.5888 0.7162 0.0085  -0.1588 0.0719  102 ASN D CB  
6802  C CG  . ASN D 102 ? 0.5569 0.5845 0.6966 0.0061  -0.1672 0.0823  102 ASN D CG  
6803  O OD1 . ASN D 102 ? 0.5604 0.5854 0.6901 0.0017  -0.1689 0.0787  102 ASN D OD1 
6804  N ND2 . ASN D 102 ? 0.5316 0.5815 0.6895 0.0093  -0.1718 0.0966  102 ASN D ND2 
6805  N N   . THR D 103 ? 0.5600 0.5936 0.7277 0.0142  -0.1551 0.0885  103 THR D N   
6806  C CA  . THR D 103 ? 0.5682 0.6274 0.7475 0.0051  -0.1569 0.0957  103 THR D CA  
6807  C C   . THR D 103 ? 0.5296 0.6158 0.7326 0.0112  -0.1625 0.1137  103 THR D C   
6808  O O   . THR D 103 ? 0.5288 0.6435 0.7446 0.0030  -0.1659 0.1232  103 THR D O   
6809  C CB  . THR D 103 ? 0.5898 0.6362 0.7703 0.0085  -0.1485 0.0910  103 THR D CB  
6810  O OG1 . THR D 103 ? 0.6171 0.6331 0.7793 0.0098  -0.1418 0.0774  103 THR D OG1 
6811  C CG2 . THR D 103 ? 0.6139 0.6825 0.7987 -0.0072 -0.1492 0.0925  103 THR D CG2 
6812  N N   . GLY D 104 ? 0.5781 0.6566 0.7888 0.0252  -0.1628 0.1194  104 GLY D N   
6813  C CA  . GLY D 104 ? 0.5453 0.6456 0.7818 0.0333  -0.1653 0.1376  104 GLY D CA  
6814  C C   . GLY D 104 ? 0.5383 0.6340 0.7927 0.0459  -0.1569 0.1423  104 GLY D C   
6815  O O   . GLY D 104 ? 0.5180 0.6364 0.7979 0.0508  -0.1572 0.1588  104 GLY D O   
6816  N N   . ILE D 105 ? 0.5820 0.6498 0.8245 0.0514  -0.1487 0.1291  105 ILE D N   
6817  C CA  . ILE D 105 ? 0.5817 0.6439 0.8376 0.0616  -0.1393 0.1314  105 ILE D CA  
6818  C C   . ILE D 105 ? 0.5573 0.6076 0.8257 0.0770  -0.1336 0.1356  105 ILE D C   
6819  O O   . ILE D 105 ? 0.5488 0.5811 0.8058 0.0807  -0.1346 0.1291  105 ILE D O   
6820  C CB  . ILE D 105 ? 0.6095 0.6476 0.8460 0.0606  -0.1327 0.1163  105 ILE D CB  
6821  C CG1 . ILE D 105 ? 0.6408 0.6869 0.8651 0.0446  -0.1364 0.1109  105 ILE D CG1 
6822  C CG2 . ILE D 105 ? 0.6134 0.6474 0.8619 0.0696  -0.1225 0.1183  105 ILE D CG2 
6823  C CD1 . ILE D 105 ? 0.6710 0.6971 0.8817 0.0437  -0.1287 0.1000  105 ILE D CD1 
6824  N N   . GLU D 106 ? 0.6645 0.7245 0.9577 0.0856  -0.1266 0.1465  106 GLU D N   
6825  C CA  . GLU D 106 ? 0.6498 0.6959 0.9572 0.0999  -0.1173 0.1494  106 GLU D CA  
6826  C C   . GLU D 106 ? 0.6648 0.6997 0.9787 0.1073  -0.1039 0.1455  106 GLU D C   
6827  O O   . GLU D 106 ? 0.6669 0.7216 0.9995 0.1070  -0.1012 0.1554  106 GLU D O   
6828  C CB  . GLU D 106 ? 0.6228 0.6933 0.9603 0.1046  -0.1196 0.1701  106 GLU D CB  
6829  C CG  . GLU D 106 ? 0.6106 0.6639 0.9635 0.1187  -0.1088 0.1729  106 GLU D CG  
6830  C CD  . GLU D 106 ? 0.5836 0.6624 0.9718 0.1251  -0.1088 0.1969  106 GLU D CD  
6831  O OE1 . GLU D 106 ? 0.5682 0.6677 0.9575 0.1187  -0.1210 0.2075  106 GLU D OE1 
6832  O OE2 . GLU D 106 ? 0.5782 0.6567 0.9937 0.1365  -0.0958 0.2060  106 GLU D OE2 
6833  N N   . GLY D 107 ? 0.5467 0.5519 0.8452 0.1130  -0.0955 0.1313  107 GLY D N   
6834  C CA  . GLY D 107 ? 0.5664 0.5599 0.8667 0.1185  -0.0821 0.1257  107 GLY D CA  
6835  C C   . GLY D 107 ? 0.5852 0.5481 0.8618 0.1211  -0.0750 0.1085  107 GLY D C   
6836  O O   . GLY D 107 ? 0.5789 0.5280 0.8489 0.1234  -0.0757 0.1035  107 GLY D O   
6837  N N   . THR D 108 ? 0.5342 0.4883 0.7978 0.1197  -0.0685 0.1001  108 THR D N   
6838  C CA  . THR D 108 ? 0.5583 0.4877 0.7998 0.1212  -0.0609 0.0853  108 THR D CA  
6839  C C   . THR D 108 ? 0.5813 0.5074 0.8021 0.1155  -0.0616 0.0789  108 THR D C   
6840  O O   . THR D 108 ? 0.5833 0.5237 0.8118 0.1122  -0.0629 0.0852  108 THR D O   
6841  C CB  . THR D 108 ? 0.5721 0.4918 0.8283 0.1295  -0.0439 0.0838  108 THR D CB  
6842  O OG1 . THR D 108 ? 0.5500 0.4704 0.8259 0.1351  -0.0428 0.0905  108 THR D OG1 
6843  C CG2 . THR D 108 ? 0.6078 0.5042 0.8389 0.1285  -0.0352 0.0672  108 THR D CG2 
6844  N N   . PHE D 109 ? 0.6047 0.5132 0.7998 0.1138  -0.0608 0.0671  109 PHE D N   
6845  C CA  . PHE D 109 ? 0.6290 0.5332 0.8047 0.1097  -0.0597 0.0624  109 PHE D CA  
6846  C C   . PHE D 109 ? 0.6644 0.5623 0.8383 0.1125  -0.0451 0.0581  109 PHE D C   
6847  O O   . PHE D 109 ? 0.6925 0.5838 0.8462 0.1095  -0.0428 0.0529  109 PHE D O   
6848  C CB  . PHE D 109 ? 0.6321 0.5248 0.7821 0.1062  -0.0671 0.0550  109 PHE D CB  
6849  C CG  . PHE D 109 ? 0.6000 0.4969 0.7507 0.1034  -0.0796 0.0579  109 PHE D CG  
6850  C CD1 . PHE D 109 ? 0.5853 0.4950 0.7454 0.0992  -0.0857 0.0648  109 PHE D CD1 
6851  C CD2 . PHE D 109 ? 0.5902 0.4789 0.7317 0.1038  -0.0846 0.0530  109 PHE D CD2 
6852  C CE1 . PHE D 109 ? 0.5638 0.4771 0.7228 0.0955  -0.0958 0.0663  109 PHE D CE1 
6853  C CE2 . PHE D 109 ? 0.5628 0.4554 0.7050 0.1013  -0.0950 0.0556  109 PHE D CE2 
6854  C CZ  . PHE D 109 ? 0.5506 0.4550 0.7009 0.0972  -0.1002 0.0620  109 PHE D CZ  
6855  N N   . GLU D 110 ? 0.7053 0.6054 0.9007 0.1184  -0.0342 0.0609  110 GLU D N   
6856  C CA  . GLU D 110 ? 0.7410 0.6336 0.9350 0.1209  -0.0178 0.0555  110 GLU D CA  
6857  C C   . GLU D 110 ? 0.7530 0.6560 0.9493 0.1187  -0.0151 0.0607  110 GLU D C   
6858  O O   . GLU D 110 ? 0.7898 0.6853 0.9689 0.1167  -0.0072 0.0543  110 GLU D O   
6859  C CB  . GLU D 110 ? 0.7338 0.6252 0.9543 0.1286  -0.0046 0.0581  110 GLU D CB  
6860  C CG  . GLU D 110 ? 0.7708 0.6526 0.9910 0.1311  0.0152  0.0511  110 GLU D CG  
6861  C CD  . GLU D 110 ? 0.8039 0.6638 1.0051 0.1295  0.0249  0.0353  110 GLU D CD  
6862  O OE1 . GLU D 110 ? 0.7894 0.6425 0.9912 0.1299  0.0200  0.0328  110 GLU D OE1 
6863  O OE2 . GLU D 110 ? 0.8475 0.6978 1.0323 0.1267  0.0378  0.0250  110 GLU D OE2 
6864  N N   . ASP D 111 ? 0.6546 0.5760 0.8714 0.1179  -0.0215 0.0724  111 ASP D N   
6865  C CA  . ASP D 111 ? 0.6667 0.5993 0.8871 0.1141  -0.0199 0.0776  111 ASP D CA  
6866  C C   . ASP D 111 ? 0.6632 0.5981 0.8681 0.1058  -0.0329 0.0780  111 ASP D C   
6867  O O   . ASP D 111 ? 0.6646 0.6131 0.8789 0.1008  -0.0354 0.0844  111 ASP D O   
6868  C CB  . ASP D 111 ? 0.6490 0.6029 0.9039 0.1171  -0.0167 0.0904  111 ASP D CB  
6869  C CG  . ASP D 111 ? 0.6586 0.6090 0.9306 0.1257  0.0010  0.0906  111 ASP D CG  
6870  O OD1 . ASP D 111 ? 0.6909 0.6327 0.9525 0.1258  0.0130  0.0844  111 ASP D OD1 
6871  O OD2 . ASP D 111 ? 0.6351 0.5907 0.9311 0.1325  0.0041  0.0972  111 ASP D OD2 
6872  N N   . PHE D 112 ? 0.6284 0.5505 0.8113 0.1040  -0.0403 0.0712  112 PHE D N   
6873  C CA  . PHE D 112 ? 0.6286 0.5488 0.7963 0.0972  -0.0490 0.0709  112 PHE D CA  
6874  C C   . PHE D 112 ? 0.6617 0.5769 0.8170 0.0951  -0.0414 0.0699  112 PHE D C   
6875  O O   . PHE D 112 ? 0.6875 0.5938 0.8306 0.0983  -0.0331 0.0650  112 PHE D O   
6876  C CB  . PHE D 112 ? 0.6162 0.5247 0.7656 0.0971  -0.0572 0.0653  112 PHE D CB  
6877  C CG  . PHE D 112 ? 0.6080 0.5154 0.7483 0.0911  -0.0657 0.0664  112 PHE D CG  
6878  C CD1 . PHE D 112 ? 0.5912 0.5090 0.7432 0.0860  -0.0730 0.0702  112 PHE D CD1 
6879  C CD2 . PHE D 112 ? 0.6221 0.5186 0.7427 0.0900  -0.0653 0.0642  112 PHE D CD2 
6880  C CE1 . PHE D 112 ? 0.5926 0.5069 0.7362 0.0797  -0.0781 0.0694  112 PHE D CE1 
6881  C CE2 . PHE D 112 ? 0.6158 0.5091 0.7310 0.0855  -0.0704 0.0657  112 PHE D CE2 
6882  C CZ  . PHE D 112 ? 0.6032 0.5038 0.7295 0.0801  -0.0759 0.0671  112 PHE D CZ  
6883  N N   . PRO D 113 ? 0.6219 0.5425 0.7791 0.0890  -0.0431 0.0740  113 PRO D N   
6884  C CA  . PRO D 113 ? 0.6542 0.5705 0.8022 0.0873  -0.0346 0.0747  113 PRO D CA  
6885  C C   . PRO D 113 ? 0.6655 0.5677 0.7886 0.0869  -0.0363 0.0722  113 PRO D C   
6886  O O   . PRO D 113 ? 0.6701 0.5686 0.7879 0.0826  -0.0378 0.0752  113 PRO D O   
6887  C CB  . PRO D 113 ? 0.6581 0.5860 0.8204 0.0798  -0.0359 0.0802  113 PRO D CB  
6888  C CG  . PRO D 113 ? 0.6349 0.5659 0.8000 0.0754  -0.0475 0.0798  113 PRO D CG  
6889  C CD  . PRO D 113 ? 0.6076 0.5388 0.7755 0.0821  -0.0518 0.0779  113 PRO D CD  
6890  N N   . PHE D 114 ? 0.6734 0.5682 0.7820 0.0912  -0.0351 0.0672  114 PHE D N   
6891  C CA  . PHE D 114 ? 0.6870 0.5728 0.7728 0.0909  -0.0378 0.0668  114 PHE D CA  
6892  C C   . PHE D 114 ? 0.7173 0.6018 0.7949 0.0888  -0.0307 0.0723  114 PHE D C   
6893  O O   . PHE D 114 ? 0.7163 0.5961 0.7844 0.0875  -0.0338 0.0772  114 PHE D O   
6894  C CB  . PHE D 114 ? 0.7079 0.5895 0.7792 0.0934  -0.0365 0.0599  114 PHE D CB  
6895  C CG  . PHE D 114 ? 0.6788 0.5596 0.7576 0.0955  -0.0426 0.0549  114 PHE D CG  
6896  C CD1 . PHE D 114 ? 0.6496 0.5280 0.7236 0.0949  -0.0536 0.0551  114 PHE D CD1 
6897  C CD2 . PHE D 114 ? 0.6801 0.5623 0.7723 0.0984  -0.0361 0.0508  114 PHE D CD2 
6898  C CE1 . PHE D 114 ? 0.6240 0.5018 0.7050 0.0966  -0.0589 0.0511  114 PHE D CE1 
6899  C CE2 . PHE D 114 ? 0.6535 0.5344 0.7542 0.1006  -0.0408 0.0477  114 PHE D CE2 
6900  C CZ  . PHE D 114 ? 0.6264 0.5053 0.7206 0.0994  -0.0526 0.0477  114 PHE D CZ  
6901  N N   . SER D 115 ? 0.7355 0.6241 0.8182 0.0888  -0.0203 0.0725  115 SER D N   
6902  C CA  . SER D 115 ? 0.7667 0.6546 0.8416 0.0868  -0.0123 0.0781  115 SER D CA  
6903  C C   . SER D 115 ? 0.7545 0.6434 0.8419 0.0825  -0.0123 0.0846  115 SER D C   
6904  O O   . SER D 115 ? 0.7750 0.6605 0.8554 0.0807  -0.0067 0.0907  115 SER D O   
6905  C CB  . SER D 115 ? 0.7998 0.6918 0.8770 0.0879  0.0003  0.0755  115 SER D CB  
6906  O OG  . SER D 115 ? 0.8242 0.7130 0.8872 0.0900  0.0030  0.0677  115 SER D OG  
6907  N N   . SER D 116 ? 0.7066 0.6000 0.8113 0.0798  -0.0181 0.0835  116 SER D N   
6908  C CA  . SER D 116 ? 0.7099 0.6061 0.8274 0.0729  -0.0164 0.0874  116 SER D CA  
6909  C C   . SER D 116 ? 0.6965 0.5838 0.8106 0.0690  -0.0224 0.0880  116 SER D C   
6910  O O   . SER D 116 ? 0.7099 0.5953 0.8309 0.0619  -0.0187 0.0901  116 SER D O   
6911  C CB  . SER D 116 ? 0.7028 0.6142 0.8429 0.0698  -0.0177 0.0865  116 SER D CB  
6912  O OG  . SER D 116 ? 0.7064 0.6249 0.8526 0.0757  -0.0121 0.0856  116 SER D OG  
6913  N N   . LEU D 117 ? 0.7045 0.5857 0.8089 0.0727  -0.0302 0.0857  117 LEU D N   
6914  C CA  . LEU D 117 ? 0.6904 0.5631 0.7937 0.0697  -0.0349 0.0856  117 LEU D CA  
6915  C C   . LEU D 117 ? 0.6870 0.5490 0.7750 0.0750  -0.0350 0.0904  117 LEU D C   
6916  O O   . LEU D 117 ? 0.6655 0.5248 0.7481 0.0782  -0.0424 0.0888  117 LEU D O   
6917  C CB  . LEU D 117 ? 0.6646 0.5424 0.7739 0.0687  -0.0447 0.0799  117 LEU D CB  
6918  C CG  . LEU D 117 ? 0.6651 0.5584 0.7906 0.0651  -0.0464 0.0779  117 LEU D CG  
6919  C CD1 . LEU D 117 ? 0.6393 0.5379 0.7693 0.0645  -0.0564 0.0744  117 LEU D CD1 
6920  C CD2 . LEU D 117 ? 0.6935 0.5919 0.8299 0.0552  -0.0414 0.0794  117 LEU D CD2 
6921  N N   . PRO D 118 ? 0.7112 0.5688 0.7933 0.0760  -0.0269 0.0979  118 PRO D N   
6922  C CA  . PRO D 118 ? 0.7108 0.5633 0.7792 0.0817  -0.0277 0.1057  118 PRO D CA  
6923  C C   . PRO D 118 ? 0.6911 0.5336 0.7629 0.0823  -0.0297 0.1090  118 PRO D C   
6924  O O   . PRO D 118 ? 0.6833 0.5250 0.7465 0.0878  -0.0330 0.1157  118 PRO D O   
6925  C CB  . PRO D 118 ? 0.7391 0.5908 0.8034 0.0815  -0.0174 0.1146  118 PRO D CB  
6926  C CG  . PRO D 118 ? 0.7474 0.5969 0.8270 0.0746  -0.0106 0.1121  118 PRO D CG  
6927  C CD  . PRO D 118 ? 0.7366 0.5946 0.8256 0.0715  -0.0168 0.1014  118 PRO D CD  
6928  N N   . ASN D 119 ? 0.7128 0.5485 0.7969 0.0761  -0.0273 0.1046  119 ASN D N   
6929  C CA  . ASN D 119 ? 0.7030 0.5257 0.7914 0.0759  -0.0247 0.1074  119 ASN D CA  
6930  C C   . ASN D 119 ? 0.6815 0.5043 0.7721 0.0747  -0.0333 0.0990  119 ASN D C   
6931  O O   . ASN D 119 ? 0.6783 0.4897 0.7743 0.0726  -0.0297 0.0984  119 ASN D O   
6932  C CB  . ASN D 119 ? 0.7233 0.5352 0.8223 0.0679  -0.0130 0.1074  119 ASN D CB  
6933  C CG  . ASN D 119 ? 0.7396 0.5473 0.8372 0.0705  -0.0027 0.1191  119 ASN D CG  
6934  O OD1 . ASN D 119 ? 0.7333 0.5411 0.8235 0.0790  -0.0027 0.1307  119 ASN D OD1 
6935  N ND2 . ASN D 119 ? 0.7622 0.5682 0.8672 0.0626  0.0058  0.1172  119 ASN D ND2 
6936  N N   . LEU D 120 ? 0.6905 0.5248 0.7777 0.0760  -0.0430 0.0928  120 LEU D N   
6937  C CA  . LEU D 120 ? 0.6685 0.5038 0.7573 0.0752  -0.0513 0.0860  120 LEU D CA  
6938  C C   . LEU D 120 ? 0.6518 0.4802 0.7362 0.0816  -0.0531 0.0916  120 LEU D C   
6939  O O   . LEU D 120 ? 0.6493 0.4810 0.7257 0.0885  -0.0547 0.0994  120 LEU D O   
6940  C CB  . LEU D 120 ? 0.6541 0.5021 0.7407 0.0771  -0.0600 0.0807  120 LEU D CB  
6941  C CG  . LEU D 120 ? 0.6635 0.5216 0.7598 0.0712  -0.0600 0.0758  120 LEU D CG  
6942  C CD1 . LEU D 120 ? 0.6452 0.5133 0.7417 0.0752  -0.0668 0.0724  120 LEU D CD1 
6943  C CD2 . LEU D 120 ? 0.6721 0.5299 0.7770 0.0618  -0.0605 0.0711  120 LEU D CD2 
6944  N N   . THR D 121 ? 0.6626 0.4829 0.7528 0.0787  -0.0524 0.0880  121 THR D N   
6945  C CA  . THR D 121 ? 0.6450 0.4600 0.7345 0.0849  -0.0539 0.0930  121 THR D CA  
6946  C C   . THR D 121 ? 0.6276 0.4441 0.7184 0.0828  -0.0611 0.0846  121 THR D C   
6947  O O   . THR D 121 ? 0.6094 0.4255 0.6994 0.0887  -0.0647 0.0886  121 THR D O   
6948  C CB  . THR D 121 ? 0.6570 0.4561 0.7543 0.0853  -0.0411 0.0998  121 THR D CB  
6949  O OG1 . THR D 121 ? 0.6716 0.4608 0.7756 0.0756  -0.0350 0.0895  121 THR D OG1 
6950  C CG2 . THR D 121 ? 0.6754 0.4718 0.7729 0.0862  -0.0324 0.1086  121 THR D CG2 
6951  N N   . PHE D 122 ? 0.6597 0.4800 0.7533 0.0743  -0.0635 0.0746  122 PHE D N   
6952  C CA  . PHE D 122 ? 0.6469 0.4709 0.7410 0.0714  -0.0707 0.0674  122 PHE D CA  
6953  C C   . PHE D 122 ? 0.6431 0.4817 0.7376 0.0679  -0.0786 0.0625  122 PHE D C   
6954  O O   . PHE D 122 ? 0.6664 0.5097 0.7653 0.0602  -0.0760 0.0596  122 PHE D O   
6955  C CB  . PHE D 122 ? 0.6704 0.4839 0.7689 0.0624  -0.0633 0.0610  122 PHE D CB  
6956  C CG  . PHE D 122 ? 0.6660 0.4846 0.7638 0.0578  -0.0700 0.0535  122 PHE D CG  
6957  C CD1 . PHE D 122 ? 0.6774 0.5098 0.7755 0.0495  -0.0768 0.0477  122 PHE D CD1 
6958  C CD2 . PHE D 122 ? 0.6533 0.4643 0.7513 0.0617  -0.0691 0.0538  122 PHE D CD2 
6959  C CE1 . PHE D 122 ? 0.6772 0.5157 0.7743 0.0450  -0.0830 0.0425  122 PHE D CE1 
6960  C CE2 . PHE D 122 ? 0.6527 0.4684 0.7493 0.0571  -0.0747 0.0472  122 PHE D CE2 
6961  C CZ  . PHE D 122 ? 0.6655 0.4949 0.7608 0.0485  -0.0818 0.0416  122 PHE D CZ  
6962  N N   . VAL D 123 ? 0.6098 0.4559 0.7016 0.0730  -0.0877 0.0620  123 VAL D N   
6963  C CA  . VAL D 123 ? 0.6016 0.4606 0.6969 0.0714  -0.0939 0.0591  123 VAL D CA  
6964  C C   . VAL D 123 ? 0.5803 0.4434 0.6763 0.0714  -0.1017 0.0560  123 VAL D C   
6965  O O   . VAL D 123 ? 0.5590 0.4189 0.6503 0.0774  -0.1053 0.0570  123 VAL D O   
6966  C CB  . VAL D 123 ? 0.5936 0.4568 0.6856 0.0781  -0.0943 0.0618  123 VAL D CB  
6967  C CG1 . VAL D 123 ? 0.5821 0.4565 0.6810 0.0781  -0.0989 0.0596  123 VAL D CG1 
6968  C CG2 . VAL D 123 ? 0.6183 0.4795 0.7100 0.0773  -0.0863 0.0652  123 VAL D CG2 
6969  N N   . ASP D 124 ? 0.6012 0.4732 0.7032 0.0639  -0.1047 0.0531  124 ASP D N   
6970  C CA  . ASP D 124 ? 0.5829 0.4615 0.6867 0.0633  -0.1123 0.0515  124 ASP D CA  
6971  C C   . ASP D 124 ? 0.5806 0.4758 0.6941 0.0605  -0.1165 0.0537  124 ASP D C   
6972  O O   . ASP D 124 ? 0.6076 0.5126 0.7260 0.0512  -0.1161 0.0536  124 ASP D O   
6973  C CB  . ASP D 124 ? 0.6031 0.4776 0.7042 0.0557  -0.1114 0.0472  124 ASP D CB  
6974  C CG  . ASP D 124 ? 0.5827 0.4625 0.6839 0.0562  -0.1189 0.0463  124 ASP D CG  
6975  O OD1 . ASP D 124 ? 0.5630 0.4550 0.6699 0.0575  -0.1251 0.0491  124 ASP D OD1 
6976  O OD2 . ASP D 124 ? 0.5865 0.4582 0.6835 0.0556  -0.1175 0.0436  124 ASP D OD2 
6977  N N   . LEU D 125 ? 0.5684 0.4673 0.6857 0.0680  -0.1198 0.0561  125 LEU D N   
6978  C CA  . LEU D 125 ? 0.5598 0.4740 0.6902 0.0679  -0.1227 0.0607  125 LEU D CA  
6979  C C   . LEU D 125 ? 0.5351 0.4538 0.6692 0.0698  -0.1292 0.0622  125 LEU D C   
6980  O O   . LEU D 125 ? 0.5203 0.4480 0.6665 0.0737  -0.1304 0.0673  125 LEU D O   
6981  C CB  . LEU D 125 ? 0.5566 0.4701 0.6918 0.0751  -0.1176 0.0627  125 LEU D CB  
6982  C CG  . LEU D 125 ? 0.5815 0.4909 0.7129 0.0734  -0.1108 0.0621  125 LEU D CG  
6983  C CD1 . LEU D 125 ? 0.5830 0.4888 0.7147 0.0807  -0.1048 0.0624  125 LEU D CD1 
6984  C CD2 . LEU D 125 ? 0.6040 0.5274 0.7451 0.0645  -0.1104 0.0650  125 LEU D CD2 
6985  N N   . SER D 126 ? 0.5758 0.4881 0.7014 0.0675  -0.1322 0.0586  126 SER D N   
6986  C CA  . SER D 126 ? 0.5535 0.4678 0.6810 0.0697  -0.1377 0.0597  126 SER D CA  
6987  C C   . SER D 126 ? 0.5542 0.4869 0.6915 0.0633  -0.1427 0.0655  126 SER D C   
6988  O O   . SER D 126 ? 0.5772 0.5217 0.7166 0.0546  -0.1429 0.0669  126 SER D O   
6989  C CB  . SER D 126 ? 0.5535 0.4567 0.6699 0.0689  -0.1385 0.0547  126 SER D CB  
6990  O OG  . SER D 126 ? 0.5834 0.4870 0.6952 0.0598  -0.1366 0.0518  126 SER D OG  
6991  N N   . MET D 127 ? 0.5451 0.4817 0.6886 0.0671  -0.1467 0.0694  127 MET D N   
6992  C CA  . MET D 127 ? 0.5404 0.4962 0.6937 0.0620  -0.1523 0.0776  127 MET D CA  
6993  C C   . MET D 127 ? 0.5418 0.5163 0.7108 0.0611  -0.1521 0.0869  127 MET D C   
6994  O O   . MET D 127 ? 0.5557 0.5493 0.7273 0.0510  -0.1558 0.0913  127 MET D O   
6995  C CB  . MET D 127 ? 0.5627 0.5237 0.7051 0.0503  -0.1555 0.0738  127 MET D CB  
6996  C CG  . MET D 127 ? 0.5563 0.5055 0.6895 0.0517  -0.1568 0.0688  127 MET D CG  
6997  S SD  . MET D 127 ? 0.5880 0.5470 0.7111 0.0370  -0.1594 0.0658  127 MET D SD  
6998  C CE  . MET D 127 ? 0.6322 0.5765 0.7427 0.0304  -0.1512 0.0543  127 MET D CE  
6999  N N   . ASN D 128 ? 0.5292 0.4989 0.7090 0.0710  -0.1470 0.0898  128 ASN D N   
7000  C CA  . ASN D 128 ? 0.5276 0.5138 0.7266 0.0731  -0.1448 0.1000  128 ASN D CA  
7001  C C   . ASN D 128 ? 0.5084 0.4893 0.7230 0.0849  -0.1399 0.1054  128 ASN D C   
7002  O O   . ASN D 128 ? 0.4979 0.4658 0.7082 0.0891  -0.1400 0.1019  128 ASN D O   
7003  C CB  . ASN D 128 ? 0.5488 0.5315 0.7443 0.0717  -0.1392 0.0954  128 ASN D CB  
7004  C CG  . ASN D 128 ? 0.5752 0.5654 0.7602 0.0586  -0.1423 0.0917  128 ASN D CG  
7005  O OD1 . ASN D 128 ? 0.5808 0.5941 0.7736 0.0496  -0.1474 0.0989  128 ASN D OD1 
7006  N ND2 . ASN D 128 ? 0.5939 0.5654 0.7617 0.0567  -0.1388 0.0809  128 ASN D ND2 
7007  N N   . ARG D 129 ? 0.6193 0.6096 0.8530 0.0901  -0.1343 0.1138  129 ARG D N   
7008  C CA  . ARG D 129 ? 0.6084 0.5924 0.8601 0.1013  -0.1263 0.1190  129 ARG D CA  
7009  C C   . ARG D 129 ? 0.6249 0.5946 0.8764 0.1072  -0.1148 0.1120  129 ARG D C   
7010  O O   . ARG D 129 ? 0.6241 0.5985 0.8970 0.1143  -0.1061 0.1197  129 ARG D O   
7011  C CB  . ARG D 129 ? 0.5910 0.6006 0.8713 0.1037  -0.1278 0.1384  129 ARG D CB  
7012  C CG  . ARG D 129 ? 0.5806 0.6119 0.8592 0.0945  -0.1404 0.1468  129 ARG D CG  
7013  C CD  . ARG D 129 ? 0.5579 0.6110 0.8648 0.0994  -0.1415 0.1675  129 ARG D CD  
7014  N NE  . ARG D 129 ? 0.5476 0.5818 0.8622 0.1096  -0.1350 0.1678  129 ARG D NE  
7015  C CZ  . ARG D 129 ? 0.5397 0.5702 0.8804 0.1215  -0.1238 0.1771  129 ARG D CZ  
7016  N NH1 . ARG D 129 ? 0.5372 0.5828 0.9003 0.1259  -0.1180 0.1882  129 ARG D NH1 
7017  N NH2 . ARG D 129 ? 0.5359 0.5467 0.8814 0.1287  -0.1172 0.1751  129 ARG D NH2 
7018  N N   . PHE D 130 ? 0.5382 0.4914 0.7662 0.1043  -0.1141 0.0983  130 PHE D N   
7019  C CA  . PHE D 130 ? 0.5582 0.4970 0.7812 0.1087  -0.1033 0.0904  130 PHE D CA  
7020  C C   . PHE D 130 ? 0.5628 0.4830 0.7854 0.1152  -0.0956 0.0840  130 PHE D C   
7021  O O   . PHE D 130 ? 0.5563 0.4675 0.7686 0.1139  -0.1003 0.0790  130 PHE D O   
7022  C CB  . PHE D 130 ? 0.5743 0.5035 0.7726 0.1033  -0.1054 0.0801  130 PHE D CB  
7023  C CG  . PHE D 130 ? 0.5826 0.5255 0.7818 0.0967  -0.1082 0.0840  130 PHE D CG  
7024  C CD1 . PHE D 130 ? 0.5944 0.5465 0.8071 0.0983  -0.1014 0.0891  130 PHE D CD1 
7025  C CD2 . PHE D 130 ? 0.5835 0.5295 0.7707 0.0883  -0.1163 0.0820  130 PHE D CD2 
7026  C CE1 . PHE D 130 ? 0.6068 0.5720 0.8207 0.0908  -0.1038 0.0922  130 PHE D CE1 
7027  C CE2 . PHE D 130 ? 0.6004 0.5574 0.7880 0.0804  -0.1175 0.0839  130 PHE D CE2 
7028  C CZ  . PHE D 130 ? 0.6121 0.5792 0.8128 0.0813  -0.1117 0.0891  130 PHE D CZ  
7029  N N   . SER D 131 ? 0.5344 0.4488 0.7686 0.1212  -0.0826 0.0836  131 SER D N   
7030  C CA  . SER D 131 ? 0.5490 0.4443 0.7834 0.1258  -0.0720 0.0757  131 SER D CA  
7031  C C   . SER D 131 ? 0.5847 0.4670 0.8071 0.1261  -0.0602 0.0645  131 SER D C   
7032  O O   . SER D 131 ? 0.5941 0.4831 0.8115 0.1242  -0.0600 0.0652  131 SER D O   
7033  C CB  . SER D 131 ? 0.5339 0.4337 0.7997 0.1336  -0.0642 0.0874  131 SER D CB  
7034  O OG  . SER D 131 ? 0.5333 0.4454 0.8206 0.1383  -0.0563 0.0971  131 SER D OG  
7035  N N   . GLY D 132 ? 0.5461 0.4098 0.7634 0.1274  -0.0495 0.0538  132 GLY D N   
7036  C CA  . GLY D 132 ? 0.5737 0.4248 0.7747 0.1254  -0.0382 0.0413  132 GLY D CA  
7037  C C   . GLY D 132 ? 0.5884 0.4300 0.7574 0.1176  -0.0447 0.0283  132 GLY D C   
7038  O O   . GLY D 132 ? 0.5832 0.4207 0.7467 0.1152  -0.0517 0.0255  132 GLY D O   
7039  N N   . THR D 133 ? 0.5790 0.4192 0.7278 0.1136  -0.0425 0.0218  133 THR D N   
7040  C CA  . THR D 133 ? 0.6096 0.4441 0.7289 0.1062  -0.0479 0.0114  133 THR D CA  
7041  C C   . THR D 133 ? 0.6046 0.4492 0.7097 0.1037  -0.0578 0.0164  133 THR D C   
7042  O O   . THR D 133 ? 0.5865 0.4399 0.7023 0.1065  -0.0581 0.0249  133 THR D O   
7043  C CB  . THR D 133 ? 0.6685 0.4901 0.7735 0.1019  -0.0333 -0.0027 133 THR D CB  
7044  O OG1 . THR D 133 ? 0.6859 0.5083 0.7971 0.1049  -0.0210 -0.0016 133 THR D OG1 
7045  C CG2 . THR D 133 ? 0.6736 0.4814 0.7899 0.1026  -0.0231 -0.0099 133 THR D CG2 
7046  N N   . ILE D 134 ? 0.6412 0.4852 0.7238 0.0982  -0.0656 0.0118  134 ILE D N   
7047  C CA  . ILE D 134 ? 0.6397 0.4913 0.7087 0.0962  -0.0731 0.0170  134 ILE D CA  
7048  C C   . ILE D 134 ? 0.6954 0.5454 0.7481 0.0931  -0.0640 0.0120  134 ILE D C   
7049  O O   . ILE D 134 ? 0.7436 0.5900 0.7779 0.0874  -0.0613 0.0030  134 ILE D O   
7050  C CB  . ILE D 134 ? 0.6281 0.4823 0.6844 0.0929  -0.0855 0.0176  134 ILE D CB  
7051  C CG1 . ILE D 134 ? 0.5781 0.4334 0.6497 0.0954  -0.0931 0.0217  134 ILE D CG1 
7052  C CG2 . ILE D 134 ? 0.6238 0.4847 0.6697 0.0922  -0.0910 0.0249  134 ILE D CG2 
7053  C CD1 . ILE D 134 ? 0.5661 0.4235 0.6279 0.0927  -0.1038 0.0219  134 ILE D CD1 
7054  N N   . SER D 135 ? 0.6532 0.5072 0.7117 0.0955  -0.0592 0.0177  135 SER D N   
7055  C CA  . SER D 135 ? 0.7079 0.5609 0.7525 0.0928  -0.0490 0.0137  135 SER D CA  
7056  C C   . SER D 135 ? 0.7374 0.5953 0.7570 0.0876  -0.0557 0.0152  135 SER D C   
7057  O O   . SER D 135 ? 0.7027 0.5657 0.7218 0.0884  -0.0668 0.0232  135 SER D O   
7058  C CB  . SER D 135 ? 0.6979 0.5553 0.7568 0.0967  -0.0426 0.0208  135 SER D CB  
7059  O OG  . SER D 135 ? 0.7527 0.6093 0.7975 0.0940  -0.0323 0.0174  135 SER D OG  
7060  N N   . PRO D 136 ? 0.7077 0.5651 0.7069 0.0819  -0.0484 0.0082  136 PRO D N   
7061  C CA  . PRO D 136 ? 0.7171 0.5835 0.6941 0.0773  -0.0545 0.0134  136 PRO D CA  
7062  C C   . PRO D 136 ? 0.7079 0.5795 0.6904 0.0813  -0.0560 0.0265  136 PRO D C   
7063  O O   . PRO D 136 ? 0.7095 0.5886 0.6808 0.0800  -0.0632 0.0353  136 PRO D O   
7064  C CB  . PRO D 136 ? 0.7962 0.6618 0.7516 0.0694  -0.0435 0.0027  136 PRO D CB  
7065  C CG  . PRO D 136 ? 0.8012 0.6548 0.7648 0.0686  -0.0344 -0.0110 136 PRO D CG  
7066  C CD  . PRO D 136 ? 0.7300 0.5788 0.7246 0.0785  -0.0340 -0.0050 136 PRO D CD  
7067  N N   . GLU D 137 ? 0.7956 0.6641 0.7963 0.0859  -0.0489 0.0287  137 GLU D N   
7068  C CA  . GLU D 137 ? 0.7784 0.6506 0.7852 0.0882  -0.0486 0.0396  137 GLU D CA  
7069  C C   . GLU D 137 ? 0.7255 0.5996 0.7387 0.0902  -0.0601 0.0486  137 GLU D C   
7070  O O   . GLU D 137 ? 0.7216 0.5977 0.7338 0.0906  -0.0603 0.0579  137 GLU D O   
7071  C CB  . GLU D 137 ? 0.7653 0.6363 0.7932 0.0916  -0.0399 0.0398  137 GLU D CB  
7072  C CG  . GLU D 137 ? 0.8122 0.6801 0.8387 0.0911  -0.0258 0.0313  137 GLU D CG  
7073  C CD  . GLU D 137 ? 0.8630 0.7336 0.8757 0.0883  -0.0169 0.0335  137 GLU D CD  
7074  O OE1 . GLU D 137 ? 0.8989 0.7720 0.8872 0.0835  -0.0191 0.0331  137 GLU D OE1 
7075  O OE2 . GLU D 137 ? 0.8651 0.7374 0.8918 0.0906  -0.0080 0.0366  137 GLU D OE2 
7076  N N   . TRP D 138 ? 0.7149 0.5871 0.7356 0.0913  -0.0681 0.0460  138 TRP D N   
7077  C CA  . TRP D 138 ? 0.6690 0.5417 0.6963 0.0928  -0.0771 0.0532  138 TRP D CA  
7078  C C   . TRP D 138 ? 0.6802 0.5566 0.6934 0.0921  -0.0809 0.0613  138 TRP D C   
7079  O O   . TRP D 138 ? 0.6533 0.5285 0.6730 0.0939  -0.0836 0.0695  138 TRP D O   
7080  C CB  . TRP D 138 ? 0.6357 0.5068 0.6699 0.0934  -0.0846 0.0485  138 TRP D CB  
7081  C CG  . TRP D 138 ? 0.6095 0.4796 0.6629 0.0951  -0.0829 0.0460  138 TRP D CG  
7082  C CD1 . TRP D 138 ? 0.6153 0.4834 0.6755 0.0961  -0.0790 0.0394  138 TRP D CD1 
7083  C CD2 . TRP D 138 ? 0.5784 0.4509 0.6475 0.0953  -0.0846 0.0510  138 TRP D CD2 
7084  N NE1 . TRP D 138 ? 0.5846 0.4559 0.6653 0.0981  -0.0791 0.0424  138 TRP D NE1 
7085  C CE2 . TRP D 138 ? 0.5648 0.4400 0.6498 0.0966  -0.0832 0.0489  138 TRP D CE2 
7086  C CE3 . TRP D 138 ? 0.5671 0.4397 0.6384 0.0936  -0.0863 0.0569  138 TRP D CE3 
7087  C CZ2 . TRP D 138 ? 0.5423 0.4243 0.6439 0.0954  -0.0853 0.0534  138 TRP D CZ2 
7088  C CZ3 . TRP D 138 ? 0.5499 0.4263 0.6362 0.0913  -0.0872 0.0586  138 TRP D CZ3 
7089  C CH2 . TRP D 138 ? 0.5385 0.4214 0.6391 0.0917  -0.0877 0.0572  138 TRP D CH2 
7090  N N   . GLY D 139 ? 0.7161 0.5977 0.7106 0.0890  -0.0803 0.0597  139 GLY D N   
7091  C CA  . GLY D 139 ? 0.7287 0.6185 0.7103 0.0882  -0.0844 0.0701  139 GLY D CA  
7092  C C   . GLY D 139 ? 0.7471 0.6385 0.7261 0.0892  -0.0779 0.0804  139 GLY D C   
7093  O O   . GLY D 139 ? 0.7580 0.6577 0.7274 0.0891  -0.0803 0.0919  139 GLY D O   
7094  N N   . ARG D 140 ? 0.7550 0.6402 0.7438 0.0901  -0.0694 0.0780  140 ARG D N   
7095  C CA  . ARG D 140 ? 0.7748 0.6605 0.7627 0.0905  -0.0620 0.0874  140 ARG D CA  
7096  C C   . ARG D 140 ? 0.7374 0.6168 0.7411 0.0936  -0.0619 0.0967  140 ARG D C   
7097  O O   . ARG D 140 ? 0.7504 0.6294 0.7536 0.0942  -0.0561 0.1069  140 ARG D O   
7098  C CB  . ARG D 140 ? 0.8043 0.6877 0.7950 0.0890  -0.0516 0.0803  140 ARG D CB  
7099  C CG  . ARG D 140 ? 0.8560 0.7430 0.8300 0.0851  -0.0473 0.0704  140 ARG D CG  
7100  C CD  . ARG D 140 ? 0.8980 0.7851 0.8694 0.0836  -0.0344 0.0690  140 ARG D CD  
7101  N NE  . ARG D 140 ? 0.8784 0.7604 0.8716 0.0862  -0.0283 0.0640  140 ARG D NE  
7102  C CZ  . ARG D 140 ? 0.8755 0.7575 0.8801 0.0870  -0.0209 0.0692  140 ARG D CZ  
7103  N NH1 . ARG D 140 ? 0.8905 0.7748 0.8870 0.0858  -0.0175 0.0790  140 ARG D NH1 
7104  N NH2 . ARG D 140 ? 0.8548 0.7360 0.8805 0.0888  -0.0167 0.0655  140 ARG D NH2 
7105  N N   . PHE D 141 ? 0.7288 0.6027 0.7459 0.0948  -0.0670 0.0931  141 PHE D N   
7106  C CA  . PHE D 141 ? 0.7029 0.5690 0.7341 0.0958  -0.0651 0.0991  141 PHE D CA  
7107  C C   . PHE D 141 ? 0.6960 0.5628 0.7239 0.0993  -0.0676 0.1115  141 PHE D C   
7108  O O   . PHE D 141 ? 0.6700 0.5360 0.7016 0.1013  -0.0739 0.1118  141 PHE D O   
7109  C CB  . PHE D 141 ? 0.6692 0.5311 0.7135 0.0944  -0.0693 0.0906  141 PHE D CB  
7110  C CG  . PHE D 141 ? 0.6723 0.5365 0.7242 0.0917  -0.0668 0.0822  141 PHE D CG  
7111  C CD1 . PHE D 141 ? 0.6876 0.5511 0.7473 0.0889  -0.0590 0.0838  141 PHE D CD1 
7112  C CD2 . PHE D 141 ? 0.6606 0.5283 0.7137 0.0921  -0.0715 0.0740  141 PHE D CD2 
7113  C CE1 . PHE D 141 ? 0.6899 0.5588 0.7597 0.0869  -0.0567 0.0783  141 PHE D CE1 
7114  C CE2 . PHE D 141 ? 0.6618 0.5331 0.7256 0.0910  -0.0683 0.0691  141 PHE D CE2 
7115  C CZ  . PHE D 141 ? 0.6758 0.5491 0.7485 0.0885  -0.0612 0.0717  141 PHE D CZ  
7116  N N   . SER D 142 ? 0.7070 0.5763 0.7294 0.1005  -0.0619 0.1232  142 SER D N   
7117  C CA  . SER D 142 ? 0.7018 0.5761 0.7217 0.1047  -0.0639 0.1387  142 SER D CA  
7118  C C   . SER D 142 ? 0.6715 0.5342 0.7086 0.1083  -0.0611 0.1447  142 SER D C   
7119  O O   . SER D 142 ? 0.6594 0.5262 0.6990 0.1131  -0.0631 0.1577  142 SER D O   
7120  C CB  . SER D 142 ? 0.7297 0.6097 0.7412 0.1051  -0.0573 0.1519  142 SER D CB  
7121  O OG  . SER D 142 ? 0.7307 0.5985 0.7539 0.1047  -0.0463 0.1543  142 SER D OG  
7122  N N   . LYS D 143 ? 0.6757 0.5251 0.7251 0.1053  -0.0556 0.1361  143 LYS D N   
7123  C CA  . LYS D 143 ? 0.6573 0.4935 0.7217 0.1066  -0.0507 0.1387  143 LYS D CA  
7124  C C   . LYS D 143 ? 0.6343 0.4685 0.7028 0.1052  -0.0578 0.1273  143 LYS D C   
7125  O O   . LYS D 143 ? 0.6240 0.4469 0.7037 0.1051  -0.0532 0.1271  143 LYS D O   
7126  C CB  . LYS D 143 ? 0.6704 0.4932 0.7445 0.1018  -0.0389 0.1361  143 LYS D CB  
7127  C CG  . LYS D 143 ? 0.6894 0.5108 0.7631 0.1037  -0.0293 0.1498  143 LYS D CG  
7128  C CD  . LYS D 143 ? 0.7022 0.5086 0.7874 0.0976  -0.0168 0.1462  143 LYS D CD  
7129  C CE  . LYS D 143 ? 0.7177 0.5203 0.8046 0.1002  -0.0059 0.1615  143 LYS D CE  
7130  N NZ  . LYS D 143 ? 0.7311 0.5174 0.8304 0.0931  0.0076  0.1577  143 LYS D NZ  
7131  N N   . LEU D 144 ? 0.6744 0.5184 0.7345 0.1037  -0.0675 0.1180  144 LEU D N   
7132  C CA  . LEU D 144 ? 0.6512 0.4939 0.7153 0.1017  -0.0740 0.1073  144 LEU D CA  
7133  C C   . LEU D 144 ? 0.6325 0.4751 0.7003 0.1064  -0.0775 0.1135  144 LEU D C   
7134  O O   . LEU D 144 ? 0.6328 0.4855 0.6945 0.1108  -0.0821 0.1228  144 LEU D O   
7135  C CB  . LEU D 144 ? 0.6486 0.5010 0.7043 0.1000  -0.0819 0.0979  144 LEU D CB  
7136  C CG  . LEU D 144 ? 0.6259 0.4778 0.6874 0.0971  -0.0875 0.0869  144 LEU D CG  
7137  C CD1 . LEU D 144 ? 0.6307 0.4775 0.7019 0.0914  -0.0825 0.0816  144 LEU D CD1 
7138  C CD2 . LEU D 144 ? 0.6241 0.4841 0.6786 0.0969  -0.0935 0.0800  144 LEU D CD2 
7139  N N   . GLU D 145 ? 0.6510 0.4838 0.7289 0.1047  -0.0749 0.1087  145 GLU D N   
7140  C CA  . GLU D 145 ? 0.6338 0.4653 0.7179 0.1090  -0.0767 0.1133  145 GLU D CA  
7141  C C   . GLU D 145 ? 0.6150 0.4485 0.6991 0.1061  -0.0844 0.1020  145 GLU D C   
7142  O O   . GLU D 145 ? 0.5992 0.4374 0.6850 0.1099  -0.0895 0.1054  145 GLU D O   
7143  C CB  . GLU D 145 ? 0.6413 0.4569 0.7385 0.1101  -0.0636 0.1184  145 GLU D CB  
7144  C CG  . GLU D 145 ? 0.6596 0.4695 0.7593 0.1117  -0.0533 0.1287  145 GLU D CG  
7145  C CD  . GLU D 145 ? 0.6662 0.4573 0.7807 0.1125  -0.0378 0.1333  145 GLU D CD  
7146  O OE1 . GLU D 145 ? 0.6681 0.4481 0.7882 0.1073  -0.0335 0.1222  145 GLU D OE1 
7147  O OE2 . GLU D 145 ? 0.6713 0.4584 0.7919 0.1178  -0.0290 0.1479  145 GLU D OE2 
7148  N N   . TYR D 146 ? 0.5760 0.4080 0.6594 0.0993  -0.0856 0.0900  146 TYR D N   
7149  C CA  . TYR D 146 ? 0.5601 0.3948 0.6443 0.0959  -0.0924 0.0806  146 TYR D CA  
7150  C C   . TYR D 146 ? 0.5566 0.4000 0.6359 0.0930  -0.0985 0.0740  146 TYR D C   
7151  O O   . TYR D 146 ? 0.5718 0.4150 0.6525 0.0889  -0.0947 0.0713  146 TYR D O   
7152  C CB  . TYR D 146 ? 0.5729 0.3976 0.6640 0.0893  -0.0858 0.0742  146 TYR D CB  
7153  C CG  . TYR D 146 ? 0.5619 0.3897 0.6536 0.0856  -0.0919 0.0664  146 TYR D CG  
7154  C CD1 . TYR D 146 ? 0.5504 0.3755 0.6451 0.0890  -0.0923 0.0681  146 TYR D CD1 
7155  C CD2 . TYR D 146 ? 0.5650 0.4002 0.6558 0.0789  -0.0968 0.0589  146 TYR D CD2 
7156  C CE1 . TYR D 146 ? 0.5434 0.3717 0.6382 0.0853  -0.0973 0.0614  146 TYR D CE1 
7157  C CE2 . TYR D 146 ? 0.5578 0.3974 0.6492 0.0754  -0.1023 0.0537  146 TYR D CE2 
7158  C CZ  . TYR D 146 ? 0.5477 0.3831 0.6402 0.0784  -0.1025 0.0544  146 TYR D CZ  
7159  O OH  . TYR D 146 ? 0.5432 0.3834 0.6358 0.0745  -0.1076 0.0495  146 TYR D OH  
7160  N N   . PHE D 147 ? 0.5609 0.4118 0.6361 0.0951  -0.1069 0.0717  147 PHE D N   
7161  C CA  . PHE D 147 ? 0.5593 0.4168 0.6317 0.0939  -0.1107 0.0663  147 PHE D CA  
7162  C C   . PHE D 147 ? 0.5388 0.3994 0.6148 0.0925  -0.1173 0.0608  147 PHE D C   
7163  O O   . PHE D 147 ? 0.5265 0.3886 0.5999 0.0948  -0.1223 0.0612  147 PHE D O   
7164  C CB  . PHE D 147 ? 0.5708 0.4332 0.6330 0.0970  -0.1120 0.0688  147 PHE D CB  
7165  C CG  . PHE D 147 ? 0.5821 0.4478 0.6420 0.0958  -0.1111 0.0631  147 PHE D CG  
7166  C CD1 . PHE D 147 ? 0.5852 0.4507 0.6533 0.0935  -0.1069 0.0608  147 PHE D CD1 
7167  C CD2 . PHE D 147 ? 0.5958 0.4653 0.6462 0.0962  -0.1134 0.0599  147 PHE D CD2 
7168  C CE1 . PHE D 147 ? 0.5960 0.4646 0.6655 0.0936  -0.1045 0.0569  147 PHE D CE1 
7169  C CE2 . PHE D 147 ? 0.6133 0.4833 0.6631 0.0953  -0.1097 0.0538  147 PHE D CE2 
7170  C CZ  . PHE D 147 ? 0.6103 0.4796 0.6710 0.0950  -0.1049 0.0531  147 PHE D CZ  
7171  N N   . ASP D 148 ? 0.5885 0.4518 0.6712 0.0885  -0.1176 0.0569  148 ASP D N   
7172  C CA  . ASP D 148 ? 0.5711 0.4384 0.6586 0.0869  -0.1234 0.0536  148 ASP D CA  
7173  C C   . ASP D 148 ? 0.5695 0.4440 0.6638 0.0862  -0.1241 0.0524  148 ASP D C   
7174  O O   . ASP D 148 ? 0.5808 0.4600 0.6813 0.0823  -0.1216 0.0534  148 ASP D O   
7175  C CB  . ASP D 148 ? 0.5759 0.4418 0.6670 0.0815  -0.1229 0.0524  148 ASP D CB  
7176  C CG  . ASP D 148 ? 0.5592 0.4290 0.6529 0.0804  -0.1291 0.0505  148 ASP D CG  
7177  O OD1 . ASP D 148 ? 0.5441 0.4188 0.6402 0.0828  -0.1334 0.0503  148 ASP D OD1 
7178  O OD2 . ASP D 148 ? 0.5655 0.4322 0.6589 0.0770  -0.1283 0.0490  148 ASP D OD2 
7179  N N   . LEU D 149 ? 0.5426 0.4182 0.6372 0.0894  -0.1268 0.0507  149 LEU D N   
7180  C CA  . LEU D 149 ? 0.5402 0.4211 0.6447 0.0903  -0.1259 0.0508  149 LEU D CA  
7181  C C   . LEU D 149 ? 0.5214 0.4049 0.6323 0.0906  -0.1310 0.0507  149 LEU D C   
7182  O O   . LEU D 149 ? 0.5193 0.4045 0.6389 0.0932  -0.1293 0.0512  149 LEU D O   
7183  C CB  . LEU D 149 ? 0.5575 0.4348 0.6582 0.0939  -0.1205 0.0482  149 LEU D CB  
7184  C CG  . LEU D 149 ? 0.5802 0.4568 0.6768 0.0940  -0.1141 0.0491  149 LEU D CG  
7185  C CD1 . LEU D 149 ? 0.6040 0.4776 0.6975 0.0966  -0.1076 0.0453  149 LEU D CD1 
7186  C CD2 . LEU D 149 ? 0.5803 0.4643 0.6885 0.0912  -0.1122 0.0533  149 LEU D CD2 
7187  N N   . SER D 150 ? 0.5669 0.4502 0.6750 0.0881  -0.1358 0.0507  150 SER D N   
7188  C CA  . SER D 150 ? 0.5510 0.4356 0.6630 0.0884  -0.1404 0.0506  150 SER D CA  
7189  C C   . SER D 150 ? 0.5441 0.4391 0.6697 0.0868  -0.1419 0.0557  150 SER D C   
7190  O O   . SER D 150 ? 0.5518 0.4554 0.6835 0.0841  -0.1406 0.0594  150 SER D O   
7191  C CB  . SER D 150 ? 0.5455 0.4280 0.6516 0.0859  -0.1439 0.0497  150 SER D CB  
7192  O OG  . SER D 150 ? 0.5527 0.4288 0.6496 0.0877  -0.1419 0.0484  150 SER D OG  
7193  N N   . ILE D 151 ? 0.5284 0.4242 0.6598 0.0883  -0.1447 0.0571  151 ILE D N   
7194  C CA  . ILE D 151 ? 0.5196 0.4270 0.6650 0.0874  -0.1469 0.0647  151 ILE D CA  
7195  C C   . ILE D 151 ? 0.5245 0.4396 0.6830 0.0898  -0.1425 0.0704  151 ILE D C   
7196  O O   . ILE D 151 ? 0.5299 0.4580 0.6930 0.0854  -0.1440 0.0754  151 ILE D O   
7197  C CB  . ILE D 151 ? 0.5211 0.4387 0.6638 0.0799  -0.1522 0.0672  151 ILE D CB  
7198  C CG1 . ILE D 151 ? 0.5201 0.4286 0.6508 0.0783  -0.1542 0.0612  151 ILE D CG1 
7199  C CG2 . ILE D 151 ? 0.5117 0.4439 0.6676 0.0784  -0.1558 0.0768  151 ILE D CG2 
7200  C CD1 . ILE D 151 ? 0.5340 0.4489 0.6594 0.0701  -0.1565 0.0609  151 ILE D CD1 
7201  N N   . ASN D 152 ? 0.5491 0.4562 0.7137 0.0960  -0.1362 0.0690  152 ASN D N   
7202  C CA  . ASN D 152 ? 0.5560 0.4676 0.7351 0.1001  -0.1292 0.0739  152 ASN D CA  
7203  C C   . ASN D 152 ? 0.5578 0.4599 0.7478 0.1063  -0.1224 0.0736  152 ASN D C   
7204  O O   . ASN D 152 ? 0.5513 0.4475 0.7397 0.1062  -0.1248 0.0719  152 ASN D O   
7205  C CB  . ASN D 152 ? 0.5747 0.4811 0.7441 0.0999  -0.1243 0.0681  152 ASN D CB  
7206  C CG  . ASN D 152 ? 0.5782 0.4965 0.7462 0.0942  -0.1276 0.0716  152 ASN D CG  
7207  O OD1 . ASN D 152 ? 0.5747 0.5094 0.7570 0.0923  -0.1292 0.0806  152 ASN D OD1 
7208  N ND2 . ASN D 152 ? 0.5887 0.4995 0.7400 0.0909  -0.1283 0.0652  152 ASN D ND2 
7209  N N   . GLN D 153 ? 0.5654 0.4651 0.7672 0.1113  -0.1124 0.0749  153 GLN D N   
7210  C CA  . GLN D 153 ? 0.5770 0.4630 0.7879 0.1165  -0.1022 0.0717  153 GLN D CA  
7211  C C   . GLN D 153 ? 0.6094 0.4814 0.8098 0.1172  -0.0917 0.0602  153 GLN D C   
7212  O O   . GLN D 153 ? 0.6242 0.4898 0.8381 0.1221  -0.0789 0.0600  153 GLN D O   
7213  C CB  . GLN D 153 ? 0.5630 0.4586 0.8037 0.1228  -0.0969 0.0860  153 GLN D CB  
7214  C CG  . GLN D 153 ? 0.5364 0.4513 0.7863 0.1206  -0.1081 0.0995  153 GLN D CG  
7215  C CD  . GLN D 153 ? 0.5256 0.4645 0.7904 0.1202  -0.1112 0.1132  153 GLN D CD  
7216  O OE1 . GLN D 153 ? 0.5338 0.4748 0.8101 0.1244  -0.1028 0.1157  153 GLN D OE1 
7217  N NE2 . GLN D 153 ? 0.5104 0.4687 0.7748 0.1142  -0.1229 0.1219  153 GLN D NE2 
7218  N N   . LEU D 154 ? 0.5618 0.4296 0.7383 0.1123  -0.0962 0.0510  154 LEU D N   
7219  C CA  . LEU D 154 ? 0.5988 0.4553 0.7613 0.1112  -0.0874 0.0401  154 LEU D CA  
7220  C C   . LEU D 154 ? 0.6259 0.4668 0.7815 0.1093  -0.0812 0.0291  154 LEU D C   
7221  O O   . LEU D 154 ? 0.6149 0.4536 0.7696 0.1075  -0.0871 0.0283  154 LEU D O   
7222  C CB  . LEU D 154 ? 0.6055 0.4645 0.7457 0.1065  -0.0946 0.0364  154 LEU D CB  
7223  C CG  . LEU D 154 ? 0.5834 0.4553 0.7268 0.1059  -0.1009 0.0449  154 LEU D CG  
7224  C CD1 . LEU D 154 ? 0.5952 0.4654 0.7180 0.1023  -0.1044 0.0411  154 LEU D CD1 
7225  C CD2 . LEU D 154 ? 0.5861 0.4654 0.7470 0.1093  -0.0934 0.0514  154 LEU D CD2 
7226  N N   . VAL D 155 ? 0.5909 0.4212 0.7409 0.1086  -0.0685 0.0197  155 VAL D N   
7227  C CA  . VAL D 155 ? 0.6282 0.4428 0.7699 0.1044  -0.0599 0.0065  155 VAL D CA  
7228  C C   . VAL D 155 ? 0.6793 0.4895 0.7960 0.0978  -0.0552 -0.0056 155 VAL D C   
7229  O O   . VAL D 155 ? 0.6827 0.5011 0.7910 0.0981  -0.0579 -0.0024 155 VAL D O   
7230  C CB  . VAL D 155 ? 0.6302 0.4334 0.7960 0.1098  -0.0438 0.0069  155 VAL D CB  
7231  C CG1 . VAL D 155 ? 0.5900 0.3970 0.7771 0.1144  -0.0490 0.0183  155 VAL D CG1 
7232  C CG2 . VAL D 155 ? 0.6275 0.4348 0.8088 0.1164  -0.0335 0.0134  155 VAL D CG2 
7233  N N   . GLY D 156 ? 0.6468 0.4443 0.7510 0.0908  -0.0474 -0.0197 156 GLY D N   
7234  C CA  . GLY D 156 ? 0.6807 0.4762 0.7587 0.0823  -0.0430 -0.0318 156 GLY D CA  
7235  C C   . GLY D 156 ? 0.6954 0.5023 0.7499 0.0751  -0.0587 -0.0323 156 GLY D C   
7236  O O   . GLY D 156 ? 0.6606 0.4746 0.7189 0.0764  -0.0720 -0.0251 156 GLY D O   
7237  N N   . GLU D 157 ? 0.6870 0.4967 0.7174 0.0672  -0.0565 -0.0401 157 GLU D N   
7238  C CA  . GLU D 157 ? 0.7140 0.5369 0.7222 0.0597  -0.0700 -0.0394 157 GLU D CA  
7239  C C   . GLU D 157 ? 0.6882 0.5246 0.6951 0.0654  -0.0799 -0.0253 157 GLU D C   
7240  O O   . GLU D 157 ? 0.6589 0.4944 0.6779 0.0729  -0.0755 -0.0187 157 GLU D O   
7241  C CB  . GLU D 157 ? 0.7893 0.6117 0.7710 0.0466  -0.0633 -0.0536 157 GLU D CB  
7242  C CG  . GLU D 157 ? 0.8069 0.6129 0.7889 0.0390  -0.0502 -0.0702 157 GLU D CG  
7243  C CD  . GLU D 157 ? 0.8664 0.6762 0.8180 0.0219  -0.0479 -0.0852 157 GLU D CD  
7244  O OE1 . GLU D 157 ? 0.8903 0.7193 0.8223 0.0165  -0.0601 -0.0796 157 GLU D OE1 
7245  O OE2 . GLU D 157 ? 0.8852 0.6796 0.8330 0.0131  -0.0336 -0.1020 157 GLU D OE2 
7246  N N   . ILE D 158 ? 0.6846 0.5339 0.6783 0.0616  -0.0926 -0.0203 158 ILE D N   
7247  C CA  . ILE D 158 ? 0.6563 0.5168 0.6476 0.0661  -0.1003 -0.0072 158 ILE D CA  
7248  C C   . ILE D 158 ? 0.7218 0.5887 0.6919 0.0603  -0.0958 -0.0093 158 ILE D C   
7249  O O   . ILE D 158 ? 0.7880 0.6609 0.7387 0.0500  -0.0967 -0.0166 158 ILE D O   
7250  C CB  . ILE D 158 ? 0.6192 0.4905 0.6107 0.0665  -0.1144 0.0015  158 ILE D CB  
7251  C CG1 . ILE D 158 ? 0.5595 0.4253 0.5720 0.0730  -0.1182 0.0053  158 ILE D CG1 
7252  C CG2 . ILE D 158 ? 0.5991 0.4816 0.5850 0.0694  -0.1197 0.0141  158 ILE D CG2 
7253  C CD1 . ILE D 158 ? 0.5440 0.4175 0.5571 0.0717  -0.1294 0.0096  158 ILE D CD1 
7254  N N   . PRO D 159 ? 0.6710 0.5381 0.6434 0.0652  -0.0908 -0.0032 159 PRO D N   
7255  C CA  . PRO D 159 ? 0.7292 0.6024 0.6810 0.0594  -0.0855 -0.0048 159 PRO D CA  
7256  C C   . PRO D 159 ? 0.7313 0.6219 0.6674 0.0554  -0.0970 0.0050  159 PRO D C   
7257  O O   . PRO D 159 ? 0.6768 0.5731 0.6230 0.0611  -0.1070 0.0171  159 PRO D O   
7258  C CB  . PRO D 159 ? 0.7010 0.5705 0.6643 0.0671  -0.0783 0.0019  159 PRO D CB  
7259  C CG  . PRO D 159 ? 0.6570 0.5249 0.6424 0.0756  -0.0854 0.0112  159 PRO D CG  
7260  C CD  . PRO D 159 ? 0.6505 0.5137 0.6438 0.0749  -0.0898 0.0055  159 PRO D CD  
7261  N N   . PRO D 160 ? 0.7360 0.6366 0.6478 0.0451  -0.0954 0.0008  160 PRO D N   
7262  C CA  . PRO D 160 ? 0.7405 0.6619 0.6389 0.0420  -0.1063 0.0142  160 PRO D CA  
7263  C C   . PRO D 160 ? 0.7326 0.6579 0.6372 0.0505  -0.1063 0.0306  160 PRO D C   
7264  O O   . PRO D 160 ? 0.7309 0.6713 0.6334 0.0521  -0.1152 0.0461  160 PRO D O   
7265  C CB  . PRO D 160 ? 0.7710 0.7027 0.6404 0.0271  -0.1025 0.0042  160 PRO D CB  
7266  C CG  . PRO D 160 ? 0.7913 0.7041 0.6600 0.0221  -0.0894 -0.0168 160 PRO D CG  
7267  C CD  . PRO D 160 ? 0.7808 0.6752 0.6763 0.0356  -0.0825 -0.0155 160 PRO D CD  
7268  N N   . GLU D 161 ? 0.8183 0.7309 0.7316 0.0560  -0.0957 0.0285  161 GLU D N   
7269  C CA  . GLU D 161 ? 0.7896 0.7039 0.7095 0.0631  -0.0940 0.0427  161 GLU D CA  
7270  C C   . GLU D 161 ? 0.7135 0.6261 0.6536 0.0720  -0.1016 0.0549  161 GLU D C   
7271  O O   . GLU D 161 ? 0.6928 0.6089 0.6368 0.0766  -0.1018 0.0687  161 GLU D O   
7272  C CB  . GLU D 161 ? 0.8100 0.7116 0.7373 0.0660  -0.0809 0.0364  161 GLU D CB  
7273  C CG  . GLU D 161 ? 0.8903 0.7949 0.7966 0.0584  -0.0706 0.0293  161 GLU D CG  
7274  C CD  . GLU D 161 ? 0.9552 0.8530 0.8519 0.0504  -0.0636 0.0101  161 GLU D CD  
7275  O OE1 . GLU D 161 ? 0.9369 0.8290 0.8424 0.0505  -0.0680 0.0035  161 GLU D OE1 
7276  O OE2 . GLU D 161 ? 1.0275 0.9246 0.9077 0.0434  -0.0523 0.0012  161 GLU D OE2 
7277  N N   . LEU D 162 ? 0.7541 0.6606 0.7069 0.0741  -0.1067 0.0498  162 LEU D N   
7278  C CA  . LEU D 162 ? 0.6894 0.5940 0.6595 0.0812  -0.1128 0.0597  162 LEU D CA  
7279  C C   . LEU D 162 ? 0.6792 0.5977 0.6445 0.0820  -0.1198 0.0747  162 LEU D C   
7280  O O   . LEU D 162 ? 0.6416 0.5578 0.6200 0.0885  -0.1203 0.0861  162 LEU D O   
7281  C CB  . LEU D 162 ? 0.6585 0.5572 0.6394 0.0817  -0.1175 0.0519  162 LEU D CB  
7282  C CG  . LEU D 162 ? 0.6498 0.5357 0.6428 0.0834  -0.1112 0.0417  162 LEU D CG  
7283  C CD1 . LEU D 162 ? 0.6037 0.4854 0.6109 0.0856  -0.1169 0.0398  162 LEU D CD1 
7284  C CD2 . LEU D 162 ? 0.6360 0.5170 0.6385 0.0876  -0.1043 0.0462  162 LEU D CD2 
7285  N N   . GLY D 163 ? 0.7001 0.6340 0.6475 0.0750  -0.1244 0.0755  163 GLY D N   
7286  C CA  . GLY D 163 ? 0.6903 0.6424 0.6342 0.0756  -0.1314 0.0927  163 GLY D CA  
7287  C C   . GLY D 163 ? 0.6950 0.6500 0.6389 0.0801  -0.1262 0.1078  163 GLY D C   
7288  O O   . GLY D 163 ? 0.6786 0.6468 0.6262 0.0836  -0.1306 0.1260  163 GLY D O   
7289  N N   . LYS D 164 ? 0.7103 0.6538 0.6523 0.0804  -0.1164 0.1020  164 LYS D N   
7290  C CA  . LYS D 164 ? 0.7187 0.6630 0.6612 0.0841  -0.1099 0.1153  164 LYS D CA  
7291  C C   . LYS D 164 ? 0.6737 0.6050 0.6390 0.0933  -0.1064 0.1244  164 LYS D C   
7292  O O   . LYS D 164 ? 0.6782 0.6084 0.6468 0.0967  -0.1001 0.1366  164 LYS D O   
7293  C CB  . LYS D 164 ? 0.7629 0.7001 0.6954 0.0802  -0.0998 0.1048  164 LYS D CB  
7294  C CG  . LYS D 164 ? 0.8216 0.7728 0.7277 0.0700  -0.0994 0.0996  164 LYS D CG  
7295  C CD  . LYS D 164 ? 0.8657 0.8120 0.7634 0.0679  -0.0874 0.0957  164 LYS D CD  
7296  C CE  . LYS D 164 ? 0.8741 0.8019 0.7817 0.0690  -0.0789 0.0780  164 LYS D CE  
7297  N NZ  . LYS D 164 ? 0.9132 0.8360 0.8175 0.0684  -0.0661 0.0755  164 LYS D NZ  
7298  N N   . LEU D 165 ? 0.7222 0.6436 0.7026 0.0965  -0.1093 0.1186  165 LEU D N   
7299  C CA  . LEU D 165 ? 0.6859 0.5938 0.6863 0.1029  -0.1047 0.1239  165 LEU D CA  
7300  C C   . LEU D 165 ? 0.6647 0.5794 0.6740 0.1084  -0.1076 0.1413  165 LEU D C   
7301  O O   . LEU D 165 ? 0.6342 0.5457 0.6552 0.1113  -0.1110 0.1412  165 LEU D O   
7302  C CB  . LEU D 165 ? 0.6567 0.5525 0.6676 0.1024  -0.1059 0.1097  165 LEU D CB  
7303  C CG  . LEU D 165 ? 0.6718 0.5621 0.6789 0.0984  -0.1026 0.0949  165 LEU D CG  
7304  C CD1 . LEU D 165 ? 0.6388 0.5215 0.6572 0.0983  -0.1055 0.0844  165 LEU D CD1 
7305  C CD2 . LEU D 165 ? 0.6873 0.5714 0.6975 0.0987  -0.0930 0.0969  165 LEU D CD2 
7306  N N   . SER D 166 ? 0.7116 0.6363 0.7166 0.1103  -0.1050 0.1578  166 SER D N   
7307  C CA  . SER D 166 ? 0.6920 0.6280 0.7062 0.1162  -0.1075 0.1783  166 SER D CA  
7308  C C   . SER D 166 ? 0.6595 0.5786 0.6973 0.1237  -0.1003 0.1836  166 SER D C   
7309  O O   . SER D 166 ? 0.6388 0.5652 0.6888 0.1296  -0.1018 0.1985  166 SER D O   
7310  C CB  . SER D 166 ? 0.7112 0.6605 0.7180 0.1171  -0.1044 0.1967  166 SER D CB  
7311  O OG  . SER D 166 ? 0.7161 0.6482 0.7305 0.1197  -0.0921 0.1985  166 SER D OG  
7312  N N   . ASN D 167 ? 0.7069 0.6048 0.7521 0.1230  -0.0917 0.1724  167 ASN D N   
7313  C CA  . ASN D 167 ? 0.6853 0.5654 0.7505 0.1274  -0.0831 0.1741  167 ASN D CA  
7314  C C   . ASN D 167 ? 0.6669 0.5383 0.7366 0.1247  -0.0868 0.1575  167 ASN D C   
7315  O O   . ASN D 167 ? 0.6559 0.5117 0.7396 0.1259  -0.0791 0.1550  167 ASN D O   
7316  C CB  . ASN D 167 ? 0.6982 0.5615 0.7689 0.1263  -0.0701 0.1734  167 ASN D CB  
7317  C CG  . ASN D 167 ? 0.7056 0.5717 0.7815 0.1318  -0.0623 0.1949  167 ASN D CG  
7318  O OD1 . ASN D 167 ? 0.6896 0.5557 0.7799 0.1391  -0.0583 0.2108  167 ASN D OD1 
7319  N ND2 . ASN D 167 ? 0.7295 0.5984 0.7950 0.1289  -0.0590 0.1968  167 ASN D ND2 
7320  N N   . LEU D 168 ? 0.6704 0.5510 0.7286 0.1203  -0.0972 0.1459  168 LEU D N   
7321  C CA  . LEU D 168 ? 0.6500 0.5239 0.7123 0.1177  -0.1009 0.1317  168 LEU D CA  
7322  C C   . LEU D 168 ? 0.6285 0.5036 0.7028 0.1223  -0.1026 0.1384  168 LEU D C   
7323  O O   . LEU D 168 ? 0.6263 0.5158 0.7013 0.1263  -0.1071 0.1517  168 LEU D O   
7324  C CB  . LEU D 168 ? 0.6537 0.5365 0.7025 0.1126  -0.1102 0.1196  168 LEU D CB  
7325  C CG  . LEU D 168 ? 0.6349 0.5100 0.6874 0.1091  -0.1126 0.1043  168 LEU D CG  
7326  C CD1 . LEU D 168 ? 0.6421 0.5077 0.6963 0.1058  -0.1063 0.0962  168 LEU D CD1 
7327  C CD2 . LEU D 168 ? 0.6356 0.5203 0.6784 0.1060  -0.1215 0.0965  168 LEU D CD2 
7328  N N   . ASP D 169 ? 0.6777 0.5393 0.7617 0.1213  -0.0986 0.1298  169 ASP D N   
7329  C CA  . ASP D 169 ? 0.6605 0.5208 0.7566 0.1251  -0.0982 0.1335  169 ASP D CA  
7330  C C   . ASP D 169 ? 0.6446 0.5068 0.7377 0.1209  -0.1064 0.1201  169 ASP D C   
7331  O O   . ASP D 169 ? 0.6310 0.5015 0.7285 0.1235  -0.1118 0.1239  169 ASP D O   
7332  C CB  . ASP D 169 ? 0.6661 0.5071 0.7762 0.1266  -0.0837 0.1348  169 ASP D CB  
7333  C CG  . ASP D 169 ? 0.6547 0.4889 0.7755 0.1274  -0.0809 0.1308  169 ASP D CG  
7334  O OD1 . ASP D 169 ? 0.6398 0.4852 0.7661 0.1325  -0.0862 0.1390  169 ASP D OD1 
7335  O OD2 . ASP D 169 ? 0.6642 0.4830 0.7874 0.1217  -0.0733 0.1190  169 ASP D OD2 
7336  N N   . THR D 170 ? 0.5831 0.4397 0.6699 0.1146  -0.1077 0.1060  170 THR D N   
7337  C CA  . THR D 170 ? 0.5679 0.4257 0.6533 0.1108  -0.1144 0.0947  170 THR D CA  
7338  C C   . THR D 170 ? 0.5700 0.4330 0.6450 0.1066  -0.1203 0.0862  170 THR D C   
7339  O O   . THR D 170 ? 0.5831 0.4424 0.6552 0.1045  -0.1160 0.0837  170 THR D O   
7340  C CB  . THR D 170 ? 0.5697 0.4149 0.6622 0.1069  -0.1078 0.0870  170 THR D CB  
7341  O OG1 . THR D 170 ? 0.5728 0.4108 0.6759 0.1108  -0.0999 0.0938  170 THR D OG1 
7342  C CG2 . THR D 170 ? 0.5556 0.4042 0.6464 0.1027  -0.1151 0.0771  170 THR D CG2 
7343  N N   . LEU D 171 ? 0.5423 0.4132 0.6130 0.1055  -0.1286 0.0818  171 LEU D N   
7344  C CA  . LEU D 171 ? 0.5477 0.4213 0.6109 0.1019  -0.1321 0.0733  171 LEU D CA  
7345  C C   . LEU D 171 ? 0.5295 0.4022 0.5971 0.0996  -0.1365 0.0655  171 LEU D C   
7346  O O   . LEU D 171 ? 0.5225 0.3995 0.5914 0.1001  -0.1416 0.0664  171 LEU D O   
7347  C CB  . LEU D 171 ? 0.5675 0.4513 0.6191 0.1014  -0.1362 0.0753  171 LEU D CB  
7348  C CG  . LEU D 171 ? 0.5843 0.4690 0.6278 0.0973  -0.1376 0.0651  171 LEU D CG  
7349  C CD1 . LEU D 171 ? 0.5928 0.4708 0.6377 0.0968  -0.1309 0.0611  171 LEU D CD1 
7350  C CD2 . LEU D 171 ? 0.6169 0.5123 0.6464 0.0942  -0.1408 0.0660  171 LEU D CD2 
7351  N N   . HIS D 172 ? 0.5887 0.4575 0.6598 0.0970  -0.1347 0.0595  172 HIS D N   
7352  C CA  . HIS D 172 ? 0.5733 0.4426 0.6498 0.0948  -0.1384 0.0542  172 HIS D CA  
7353  C C   . HIS D 172 ? 0.5795 0.4499 0.6559 0.0939  -0.1380 0.0496  172 HIS D C   
7354  O O   . HIS D 172 ? 0.5868 0.4567 0.6661 0.0932  -0.1338 0.0495  172 HIS D O   
7355  C CB  . HIS D 172 ? 0.5684 0.4347 0.6519 0.0920  -0.1361 0.0536  172 HIS D CB  
7356  C CG  . HIS D 172 ? 0.5684 0.4309 0.6540 0.0927  -0.1341 0.0566  172 HIS D CG  
7357  N ND1 . HIS D 172 ? 0.5789 0.4369 0.6684 0.0885  -0.1296 0.0546  172 HIS D ND1 
7358  C CD2 . HIS D 172 ? 0.5646 0.4279 0.6498 0.0967  -0.1347 0.0617  172 HIS D CD2 
7359  C CE1 . HIS D 172 ? 0.5815 0.4347 0.6735 0.0907  -0.1260 0.0574  172 HIS D CE1 
7360  N NE2 . HIS D 172 ? 0.5694 0.4268 0.6604 0.0964  -0.1295 0.0630  172 HIS D NE2 
7361  N N   . LEU D 173 ? 0.5464 0.4181 0.6211 0.0936  -0.1413 0.0458  173 LEU D N   
7362  C CA  . LEU D 173 ? 0.5586 0.4289 0.6351 0.0932  -0.1385 0.0409  173 LEU D CA  
7363  C C   . LEU D 173 ? 0.5452 0.4149 0.6294 0.0926  -0.1415 0.0386  173 LEU D C   
7364  O O   . LEU D 173 ? 0.5617 0.4286 0.6447 0.0917  -0.1403 0.0336  173 LEU D O   
7365  C CB  . LEU D 173 ? 0.5933 0.4632 0.6578 0.0922  -0.1362 0.0371  173 LEU D CB  
7366  C CG  . LEU D 173 ? 0.6140 0.4846 0.6714 0.0928  -0.1313 0.0394  173 LEU D CG  
7367  C CD1 . LEU D 173 ? 0.6564 0.5295 0.6986 0.0898  -0.1303 0.0358  173 LEU D CD1 
7368  C CD2 . LEU D 173 ? 0.6150 0.4830 0.6811 0.0941  -0.1248 0.0387  173 LEU D CD2 
7369  N N   . VAL D 174 ? 0.5836 0.4557 0.6755 0.0922  -0.1445 0.0419  174 VAL D N   
7370  C CA  . VAL D 174 ? 0.5699 0.4428 0.6671 0.0912  -0.1486 0.0415  174 VAL D CA  
7371  C C   . VAL D 174 ? 0.5631 0.4375 0.6726 0.0917  -0.1471 0.0432  174 VAL D C   
7372  O O   . VAL D 174 ? 0.5623 0.4406 0.6782 0.0921  -0.1446 0.0466  174 VAL D O   
7373  C CB  . VAL D 174 ? 0.5553 0.4306 0.6526 0.0899  -0.1519 0.0445  174 VAL D CB  
7374  C CG1 . VAL D 174 ? 0.5458 0.4220 0.6456 0.0890  -0.1560 0.0439  174 VAL D CG1 
7375  C CG2 . VAL D 174 ? 0.5621 0.4362 0.6517 0.0911  -0.1510 0.0460  174 VAL D CG2 
7376  N N   . GLU D 175 ? 0.5886 0.4612 0.7030 0.0915  -0.1486 0.0422  175 GLU D N   
7377  C CA  . GLU D 175 ? 0.5796 0.4548 0.7084 0.0927  -0.1474 0.0468  175 GLU D CA  
7378  C C   . GLU D 175 ? 0.5910 0.4647 0.7283 0.0959  -0.1402 0.0479  175 GLU D C   
7379  O O   . GLU D 175 ? 0.5818 0.4638 0.7312 0.0971  -0.1394 0.0554  175 GLU D O   
7380  C CB  . GLU D 175 ? 0.5624 0.4476 0.6959 0.0903  -0.1519 0.0536  175 GLU D CB  
7381  C CG  . GLU D 175 ? 0.5539 0.4397 0.6834 0.0877  -0.1568 0.0530  175 GLU D CG  
7382  C CD  . GLU D 175 ? 0.5470 0.4430 0.6810 0.0839  -0.1601 0.0591  175 GLU D CD  
7383  O OE1 . GLU D 175 ? 0.5457 0.4506 0.6894 0.0836  -0.1598 0.0658  175 GLU D OE1 
7384  O OE2 . GLU D 175 ? 0.5466 0.4432 0.6747 0.0808  -0.1626 0.0576  175 GLU D OE2 
7385  N N   . ASN D 176 ? 0.5549 0.4196 0.6857 0.0964  -0.1346 0.0404  176 ASN D N   
7386  C CA  . ASN D 176 ? 0.5742 0.4339 0.7126 0.0994  -0.1250 0.0390  176 ASN D CA  
7387  C C   . ASN D 176 ? 0.6004 0.4480 0.7384 0.0982  -0.1189 0.0309  176 ASN D C   
7388  O O   . ASN D 176 ? 0.5995 0.4452 0.7334 0.0951  -0.1237 0.0282  176 ASN D O   
7389  C CB  . ASN D 176 ? 0.5926 0.4521 0.7199 0.0991  -0.1218 0.0356  176 ASN D CB  
7390  C CG  . ASN D 176 ? 0.5744 0.4440 0.7067 0.0999  -0.1241 0.0433  176 ASN D CG  
7391  O OD1 . ASN D 176 ? 0.5681 0.4436 0.7160 0.1026  -0.1206 0.0498  176 ASN D OD1 
7392  N ND2 . ASN D 176 ? 0.5691 0.4416 0.6896 0.0973  -0.1294 0.0433  176 ASN D ND2 
7393  N N   . LYS D 177 ? 0.5937 0.4327 0.7361 0.0999  -0.1075 0.0263  177 LYS D N   
7394  C CA  . LYS D 177 ? 0.6273 0.4523 0.7689 0.0971  -0.0989 0.0163  177 LYS D CA  
7395  C C   . LYS D 177 ? 0.6760 0.4941 0.7990 0.0922  -0.0923 0.0038  177 LYS D C   
7396  O O   . LYS D 177 ? 0.7092 0.5147 0.8345 0.0909  -0.0790 -0.0047 177 LYS D O   
7397  C CB  . LYS D 177 ? 0.6209 0.4390 0.7872 0.1030  -0.0876 0.0215  177 LYS D CB  
7398  C CG  . LYS D 177 ? 0.5835 0.4083 0.7675 0.1063  -0.0934 0.0338  177 LYS D CG  
7399  C CD  . LYS D 177 ? 0.5759 0.4034 0.7473 0.1007  -0.1051 0.0312  177 LYS D CD  
7400  C CE  . LYS D 177 ? 0.5361 0.3763 0.7199 0.1032  -0.1139 0.0451  177 LYS D CE  
7401  N NZ  . LYS D 177 ? 0.5128 0.3677 0.6863 0.1015  -0.1255 0.0496  177 LYS D NZ  
7402  N N   . LEU D 178 ? 0.5779 0.4044 0.6823 0.0888  -0.1007 0.0028  178 LEU D N   
7403  C CA  . LEU D 178 ? 0.6289 0.4529 0.7133 0.0830  -0.0962 -0.0072 178 LEU D CA  
7404  C C   . LEU D 178 ? 0.6743 0.4919 0.7465 0.0738  -0.0946 -0.0195 178 LEU D C   
7405  O O   . LEU D 178 ? 0.6626 0.4832 0.7353 0.0713  -0.1028 -0.0184 178 LEU D O   
7406  C CB  . LEU D 178 ? 0.6228 0.4591 0.6929 0.0823  -0.1059 -0.0020 178 LEU D CB  
7407  C CG  . LEU D 178 ? 0.5800 0.4232 0.6596 0.0889  -0.1086 0.0091  178 LEU D CG  
7408  C CD1 . LEU D 178 ? 0.5745 0.4267 0.6406 0.0877  -0.1167 0.0136  178 LEU D CD1 
7409  C CD2 . LEU D 178 ? 0.5922 0.4315 0.6799 0.0925  -0.0971 0.0089  178 LEU D CD2 
7410  N N   . ASN D 179 ? 0.6952 0.5043 0.7559 0.0677  -0.0832 -0.0318 179 ASN D N   
7411  C CA  . ASN D 179 ? 0.7443 0.5473 0.7914 0.0560  -0.0799 -0.0459 179 ASN D CA  
7412  C C   . ASN D 179 ? 0.8047 0.6148 0.8243 0.0460  -0.0800 -0.0543 179 ASN D C   
7413  O O   . ASN D 179 ? 0.8114 0.6284 0.8243 0.0492  -0.0804 -0.0494 179 ASN D O   
7414  C CB  . ASN D 179 ? 0.7513 0.5338 0.8117 0.0554  -0.0623 -0.0556 179 ASN D CB  
7415  C CG  . ASN D 179 ? 0.7677 0.5400 0.8311 0.0584  -0.0455 -0.0603 179 ASN D CG  
7416  O OD1 . ASN D 179 ? 0.7691 0.5502 0.8267 0.0621  -0.0476 -0.0549 179 ASN D OD1 
7417  N ND2 . ASN D 179 ? 0.7794 0.5321 0.8535 0.0569  -0.0273 -0.0703 179 ASN D ND2 
7418  N N   . GLY D 180 ? 0.7141 0.5244 0.7176 0.0328  -0.0800 -0.0666 180 GLY D N   
7419  C CA  . GLY D 180 ? 0.7684 0.5899 0.7438 0.0206  -0.0820 -0.0740 180 GLY D CA  
7420  C C   . GLY D 180 ? 0.7770 0.6210 0.7418 0.0164  -0.1006 -0.0654 180 GLY D C   
7421  O O   . GLY D 180 ? 0.7478 0.5964 0.7260 0.0216  -0.1107 -0.0564 180 GLY D O   
7422  N N   . SER D 181 ? 0.7996 0.6592 0.7405 0.0067  -0.1045 -0.0672 181 SER D N   
7423  C CA  . SER D 181 ? 0.7872 0.6718 0.7185 0.0031  -0.1213 -0.0563 181 SER D CA  
7424  C C   . SER D 181 ? 0.7667 0.6621 0.7012 0.0147  -0.1278 -0.0387 181 SER D C   
7425  O O   . SER D 181 ? 0.7877 0.6760 0.7210 0.0197  -0.1194 -0.0384 181 SER D O   
7426  C CB  . SER D 181 ? 0.8091 0.7089 0.7125 -0.0159 -0.1229 -0.0664 181 SER D CB  
7427  O OG  . SER D 181 ? 0.8119 0.7073 0.7133 -0.0284 -0.1214 -0.0801 181 SER D OG  
7428  N N   . ILE D 182 ? 0.7865 0.6985 0.7266 0.0189  -0.1416 -0.0241 182 ILE D N   
7429  C CA  . ILE D 182 ? 0.7431 0.6649 0.6870 0.0291  -0.1468 -0.0070 182 ILE D CA  
7430  C C   . ILE D 182 ? 0.7717 0.7100 0.6928 0.0210  -0.1475 -0.0048 182 ILE D C   
7431  O O   . ILE D 182 ? 0.7804 0.7375 0.6864 0.0090  -0.1546 -0.0057 182 ILE D O   
7432  C CB  . ILE D 182 ? 0.6751 0.6088 0.6326 0.0356  -0.1588 0.0077  182 ILE D CB  
7433  C CG1 . ILE D 182 ? 0.6461 0.5650 0.6230 0.0413  -0.1579 0.0044  182 ILE D CG1 
7434  C CG2 . ILE D 182 ? 0.6312 0.5702 0.5949 0.0464  -0.1609 0.0243  182 ILE D CG2 
7435  C CD1 . ILE D 182 ? 0.5871 0.5158 0.5775 0.0472  -0.1676 0.0170  182 ILE D CD1 
7436  N N   . PRO D 183 ? 0.7393 0.6732 0.6568 0.0261  -0.1408 -0.0014 183 PRO D N   
7437  C CA  . PRO D 183 ? 0.7696 0.7196 0.6641 0.0176  -0.1406 0.0010  183 PRO D CA  
7438  C C   . PRO D 183 ? 0.7321 0.7090 0.6242 0.0180  -0.1542 0.0201  183 PRO D C   
7439  O O   . PRO D 183 ? 0.7064 0.6849 0.6173 0.0296  -0.1601 0.0348  183 PRO D O   
7440  C CB  . PRO D 183 ? 0.7828 0.7206 0.6807 0.0263  -0.1304 0.0035  183 PRO D CB  
7441  C CG  . PRO D 183 ? 0.7721 0.6869 0.6920 0.0358  -0.1236 -0.0024 183 PRO D CG  
7442  C CD  . PRO D 183 ? 0.7214 0.6378 0.6559 0.0389  -0.1332 0.0015  183 PRO D CD  
7443  N N   . SER D 184 ? 0.8402 0.8392 0.7090 0.0045  -0.1583 0.0204  184 SER D N   
7444  C CA  . SER D 184 ? 0.8075 0.8365 0.6746 0.0044  -0.1712 0.0414  184 SER D CA  
7445  C C   . SER D 184 ? 0.7822 0.8122 0.6594 0.0183  -0.1699 0.0610  184 SER D C   
7446  O O   . SER D 184 ? 0.7409 0.7875 0.6298 0.0253  -0.1784 0.0817  184 SER D O   
7447  C CB  . SER D 184 ? 0.8400 0.8953 0.6780 -0.0147 -0.1755 0.0381  184 SER D CB  
7448  O OG  . SER D 184 ? 0.8759 0.9217 0.7002 -0.0297 -0.1702 0.0135  184 SER D OG  
7449  N N   . GLU D 185 ? 0.8100 0.8221 0.6844 0.0225  -0.1584 0.0554  185 GLU D N   
7450  C CA  . GLU D 185 ? 0.7908 0.8021 0.6735 0.0340  -0.1554 0.0723  185 GLU D CA  
7451  C C   . GLU D 185 ? 0.7319 0.7306 0.6430 0.0493  -0.1564 0.0826  185 GLU D C   
7452  O O   . GLU D 185 ? 0.7096 0.7088 0.6300 0.0586  -0.1545 0.0985  185 GLU D O   
7453  C CB  . GLU D 185 ? 0.8336 0.8284 0.7075 0.0336  -0.1421 0.0617  185 GLU D CB  
7454  C CG  . GLU D 185 ? 0.8904 0.8989 0.7342 0.0189  -0.1389 0.0549  185 GLU D CG  
7455  C CD  . GLU D 185 ? 0.9292 0.9339 0.7576 0.0043  -0.1362 0.0318  185 GLU D CD  
7456  O OE1 . GLU D 185 ? 0.9221 0.9086 0.7652 0.0074  -0.1341 0.0201  185 GLU D OE1 
7457  O OE2 . GLU D 185 ? 0.9642 0.9842 0.7655 -0.0111 -0.1353 0.0252  185 GLU D OE2 
7458  N N   . ILE D 186 ? 0.7870 0.7739 0.7116 0.0515  -0.1583 0.0736  186 ILE D N   
7459  C CA  . ILE D 186 ? 0.7293 0.7066 0.6783 0.0640  -0.1595 0.0828  186 ILE D CA  
7460  C C   . ILE D 186 ? 0.6992 0.6967 0.6561 0.0684  -0.1672 0.1043  186 ILE D C   
7461  O O   . ILE D 186 ? 0.6618 0.6525 0.6369 0.0794  -0.1647 0.1162  186 ILE D O   
7462  C CB  . ILE D 186 ? 0.7112 0.6756 0.6708 0.0637  -0.1607 0.0697  186 ILE D CB  
7463  C CG1 . ILE D 186 ? 0.7452 0.6910 0.7000 0.0603  -0.1517 0.0512  186 ILE D CG1 
7464  C CG2 . ILE D 186 ? 0.6540 0.6081 0.6363 0.0749  -0.1606 0.0772  186 ILE D CG2 
7465  C CD1 . ILE D 186 ? 0.7357 0.6667 0.6980 0.0680  -0.1427 0.0524  186 ILE D CD1 
7466  N N   . GLY D 187 ? 0.7191 0.7426 0.6631 0.0595  -0.1758 0.1101  187 GLY D N   
7467  C CA  . GLY D 187 ? 0.6922 0.7398 0.6449 0.0637  -0.1834 0.1335  187 GLY D CA  
7468  C C   . GLY D 187 ? 0.6894 0.7425 0.6441 0.0709  -0.1790 0.1528  187 GLY D C   
7469  O O   . GLY D 187 ? 0.6697 0.7426 0.6353 0.0763  -0.1837 0.1755  187 GLY D O   
7470  N N   . ARG D 188 ? 0.7253 0.7624 0.6716 0.0714  -0.1696 0.1456  188 ARG D N   
7471  C CA  . ARG D 188 ? 0.7226 0.7609 0.6725 0.0787  -0.1637 0.1630  188 ARG D CA  
7472  C C   . ARG D 188 ? 0.6863 0.7019 0.6614 0.0923  -0.1555 0.1689  188 ARG D C   
7473  O O   . ARG D 188 ? 0.6805 0.6946 0.6627 0.0991  -0.1492 0.1844  188 ARG D O   
7474  C CB  . ARG D 188 ? 0.7699 0.8020 0.6990 0.0721  -0.1564 0.1525  188 ARG D CB  
7475  C CG  . ARG D 188 ? 0.8108 0.8665 0.7117 0.0570  -0.1620 0.1481  188 ARG D CG  
7476  C CD  . ARG D 188 ? 0.8562 0.9066 0.7385 0.0523  -0.1526 0.1421  188 ARG D CD  
7477  N NE  . ARG D 188 ? 0.8984 0.9686 0.7506 0.0357  -0.1557 0.1336  188 ARG D NE  
7478  C CZ  . ARG D 188 ? 0.9343 1.0116 0.7655 0.0289  -0.1500 0.1340  188 ARG D CZ  
7479  N NH1 . ARG D 188 ? 0.9358 1.0025 0.7737 0.0378  -0.1411 0.1433  188 ARG D NH1 
7480  N NH2 . ARG D 188 ? 0.9682 1.0637 0.7703 0.0116  -0.1525 0.1240  188 ARG D NH2 
7481  N N   . LEU D 189 ? 0.7254 0.7235 0.7136 0.0954  -0.1549 0.1569  189 LEU D N   
7482  C CA  . LEU D 189 ? 0.6933 0.6698 0.7031 0.1055  -0.1466 0.1593  189 LEU D CA  
7483  C C   . LEU D 189 ? 0.6622 0.6481 0.6915 0.1140  -0.1477 0.1800  189 LEU D C   
7484  O O   . LEU D 189 ? 0.6358 0.6179 0.6791 0.1173  -0.1495 0.1785  189 LEU D O   
7485  C CB  . LEU D 189 ? 0.6780 0.6355 0.6925 0.1041  -0.1457 0.1394  189 LEU D CB  
7486  C CG  . LEU D 189 ? 0.7037 0.6510 0.7043 0.0974  -0.1429 0.1205  189 LEU D CG  
7487  C CD1 . LEU D 189 ? 0.6789 0.6095 0.6891 0.0979  -0.1419 0.1059  189 LEU D CD1 
7488  C CD2 . LEU D 189 ? 0.7221 0.6613 0.7197 0.0991  -0.1338 0.1229  189 LEU D CD2 
7489  N N   . THR D 190 ? 0.7178 0.7166 0.7490 0.1181  -0.1456 0.2009  190 THR D N   
7490  C CA  . THR D 190 ? 0.6906 0.7041 0.7412 0.1266  -0.1465 0.2250  190 THR D CA  
7491  C C   . THR D 190 ? 0.6629 0.6528 0.7392 0.1368  -0.1358 0.2267  190 THR D C   
7492  O O   . THR D 190 ? 0.6387 0.6368 0.7342 0.1436  -0.1362 0.2406  190 THR D O   
7493  C CB  . THR D 190 ? 0.6997 0.7304 0.7477 0.1291  -0.1447 0.2482  190 THR D CB  
7494  O OG1 . THR D 190 ? 0.7202 0.7798 0.7446 0.1182  -0.1565 0.2491  190 THR D OG1 
7495  C CG2 . THR D 190 ? 0.6715 0.7127 0.7460 0.1410  -0.1414 0.2765  190 THR D CG2 
7496  N N   . LYS D 191 ? 0.6920 0.6539 0.7693 0.1370  -0.1257 0.2124  191 LYS D N   
7497  C CA  . LYS D 191 ? 0.6733 0.6120 0.7719 0.1440  -0.1138 0.2120  191 LYS D CA  
7498  C C   . LYS D 191 ? 0.6626 0.5871 0.7624 0.1404  -0.1153 0.1912  191 LYS D C   
7499  O O   . LYS D 191 ? 0.6514 0.5571 0.7664 0.1440  -0.1054 0.1883  191 LYS D O   
7500  C CB  . LYS D 191 ? 0.6861 0.6043 0.7867 0.1453  -0.1005 0.2114  191 LYS D CB  
7501  C CG  . LYS D 191 ? 0.6894 0.6160 0.7976 0.1520  -0.0942 0.2361  191 LYS D CG  
7502  C CD  . LYS D 191 ? 0.7006 0.6032 0.8144 0.1532  -0.0789 0.2347  191 LYS D CD  
7503  C CE  . LYS D 191 ? 0.7059 0.6175 0.8253 0.1593  -0.0727 0.2600  191 LYS D CE  
7504  N NZ  . LYS D 191 ? 0.7198 0.6079 0.8437 0.1591  -0.0574 0.2578  191 LYS D NZ  
7505  N N   . VAL D 192 ? 0.6563 0.5889 0.7406 0.1327  -0.1263 0.1768  192 VAL D N   
7506  C CA  . VAL D 192 ? 0.6439 0.5633 0.7291 0.1291  -0.1275 0.1581  192 VAL D CA  
7507  C C   . VAL D 192 ? 0.6217 0.5435 0.7233 0.1337  -0.1281 0.1635  192 VAL D C   
7508  O O   . VAL D 192 ? 0.6154 0.5565 0.7236 0.1373  -0.1331 0.1789  192 VAL D O   
7509  C CB  . VAL D 192 ? 0.6542 0.5806 0.7210 0.1204  -0.1373 0.1429  192 VAL D CB  
7510  C CG1 . VAL D 192 ? 0.6518 0.5995 0.7152 0.1177  -0.1486 0.1465  192 VAL D CG1 
7511  C CG2 . VAL D 192 ? 0.6431 0.5522 0.7103 0.1170  -0.1353 0.1246  192 VAL D CG2 
7512  N N   . THR D 193 ? 0.6099 0.5136 0.7190 0.1333  -0.1223 0.1517  193 THR D N   
7513  C CA  . THR D 193 ? 0.5932 0.4967 0.7170 0.1368  -0.1213 0.1541  193 THR D CA  
7514  C C   . THR D 193 ? 0.5832 0.4845 0.7014 0.1306  -0.1280 0.1374  193 THR D C   
7515  O O   . THR D 193 ? 0.5708 0.4787 0.6980 0.1324  -0.1308 0.1399  193 THR D O   
7516  C CB  . THR D 193 ? 0.5941 0.4775 0.7347 0.1419  -0.1053 0.1569  193 THR D CB  
7517  O OG1 . THR D 193 ? 0.6046 0.4685 0.7381 0.1355  -0.0994 0.1402  193 THR D OG1 
7518  C CG2 . THR D 193 ? 0.5996 0.4840 0.7505 0.1495  -0.0967 0.1761  193 THR D CG2 
7519  N N   . GLU D 194 ? 0.5806 0.4735 0.6861 0.1240  -0.1299 0.1221  194 GLU D N   
7520  C CA  . GLU D 194 ? 0.5700 0.4616 0.6710 0.1186  -0.1360 0.1083  194 GLU D CA  
7521  C C   . GLU D 194 ? 0.5776 0.4724 0.6635 0.1129  -0.1422 0.0991  194 GLU D C   
7522  O O   . GLU D 194 ? 0.5898 0.4788 0.6698 0.1118  -0.1381 0.0971  194 GLU D O   
7523  C CB  . GLU D 194 ? 0.5673 0.4422 0.6739 0.1166  -0.1284 0.0990  194 GLU D CB  
7524  C CG  . GLU D 194 ? 0.5572 0.4317 0.6592 0.1109  -0.1346 0.0866  194 GLU D CG  
7525  C CD  . GLU D 194 ? 0.5592 0.4227 0.6672 0.1083  -0.1282 0.0801  194 GLU D CD  
7526  O OE1 . GLU D 194 ? 0.5583 0.4207 0.6756 0.1111  -0.1243 0.0839  194 GLU D OE1 
7527  O OE2 . GLU D 194 ? 0.5658 0.4231 0.6692 0.1028  -0.1268 0.0714  194 GLU D OE2 
7528  N N   . ILE D 195 ? 0.5449 0.4482 0.6256 0.1090  -0.1507 0.0933  195 ILE D N   
7529  C CA  . ILE D 195 ? 0.5571 0.4606 0.6256 0.1034  -0.1543 0.0828  195 ILE D CA  
7530  C C   . ILE D 195 ? 0.5436 0.4431 0.6151 0.1001  -0.1574 0.0729  195 ILE D C   
7531  O O   . ILE D 195 ? 0.5353 0.4415 0.6113 0.0997  -0.1621 0.0744  195 ILE D O   
7532  C CB  . ILE D 195 ? 0.5810 0.4999 0.6380 0.1000  -0.1603 0.0857  195 ILE D CB  
7533  C CG1 . ILE D 195 ? 0.5975 0.5213 0.6499 0.1027  -0.1569 0.0964  195 ILE D CG1 
7534  C CG2 . ILE D 195 ? 0.6016 0.5179 0.6475 0.0933  -0.1619 0.0722  195 ILE D CG2 
7535  C CD1 . ILE D 195 ? 0.6246 0.5678 0.6645 0.0982  -0.1633 0.1017  195 ILE D CD1 
7536  N N   . ALA D 196 ? 0.5785 0.4686 0.6491 0.0980  -0.1548 0.0643  196 ALA D N   
7537  C CA  . ALA D 196 ? 0.5666 0.4533 0.6413 0.0954  -0.1570 0.0569  196 ALA D CA  
7538  C C   . ALA D 196 ? 0.5814 0.4650 0.6511 0.0925  -0.1562 0.0492  196 ALA D C   
7539  O O   . ALA D 196 ? 0.5851 0.4639 0.6548 0.0932  -0.1515 0.0481  196 ALA D O   
7540  C CB  . ALA D 196 ? 0.5504 0.4302 0.6335 0.0960  -0.1535 0.0566  196 ALA D CB  
7541  N N   . ILE D 197 ? 0.5396 0.4259 0.6061 0.0891  -0.1595 0.0440  197 ILE D N   
7542  C CA  . ILE D 197 ? 0.5617 0.4426 0.6257 0.0864  -0.1562 0.0359  197 ILE D CA  
7543  C C   . ILE D 197 ? 0.5557 0.4334 0.6270 0.0844  -0.1578 0.0316  197 ILE D C   
7544  O O   . ILE D 197 ? 0.5836 0.4568 0.6532 0.0811  -0.1549 0.0244  197 ILE D O   
7545  C CB  . ILE D 197 ? 0.6068 0.4915 0.6568 0.0821  -0.1554 0.0319  197 ILE D CB  
7546  C CG1 . ILE D 197 ? 0.6096 0.5026 0.6524 0.0839  -0.1567 0.0402  197 ILE D CG1 
7547  C CG2 . ILE D 197 ? 0.6345 0.5109 0.6824 0.0812  -0.1476 0.0247  197 ILE D CG2 
7548  C CD1 . ILE D 197 ? 0.6560 0.5579 0.6833 0.0780  -0.1579 0.0381  197 ILE D CD1 
7549  N N   . TYR D 198 ? 0.5914 0.4706 0.6709 0.0859  -0.1611 0.0356  198 TYR D N   
7550  C CA  . TYR D 198 ? 0.5882 0.4660 0.6741 0.0836  -0.1630 0.0327  198 TYR D CA  
7551  C C   . TYR D 198 ? 0.5833 0.4541 0.6782 0.0846  -0.1586 0.0312  198 TYR D C   
7552  O O   . TYR D 198 ? 0.5754 0.4449 0.6733 0.0872  -0.1553 0.0335  198 TYR D O   
7553  C CB  . TYR D 198 ? 0.5626 0.4450 0.6542 0.0845  -0.1672 0.0377  198 TYR D CB  
7554  C CG  . TYR D 198 ? 0.5397 0.4208 0.6363 0.0871  -0.1654 0.0422  198 TYR D CG  
7555  C CD1 . TYR D 198 ? 0.5286 0.4080 0.6324 0.0864  -0.1646 0.0427  198 TYR D CD1 
7556  C CD2 . TYR D 198 ? 0.5361 0.4187 0.6307 0.0893  -0.1640 0.0464  198 TYR D CD2 
7557  C CE1 . TYR D 198 ? 0.5202 0.4007 0.6262 0.0860  -0.1631 0.0457  198 TYR D CE1 
7558  C CE2 . TYR D 198 ? 0.5291 0.4091 0.6269 0.0895  -0.1608 0.0483  198 TYR D CE2 
7559  C CZ  . TYR D 198 ? 0.5239 0.4037 0.6262 0.0869  -0.1608 0.0471  198 TYR D CZ  
7560  O OH  . TYR D 198 ? 0.5293 0.4086 0.6324 0.0845  -0.1577 0.0478  198 TYR D OH  
7561  N N   . ASP D 199 ? 0.6236 0.4911 0.7243 0.0825  -0.1584 0.0283  199 ASP D N   
7562  C CA  . ASP D 199 ? 0.6202 0.4818 0.7328 0.0841  -0.1535 0.0291  199 ASP D CA  
7563  C C   . ASP D 199 ? 0.6435 0.4986 0.7559 0.0854  -0.1456 0.0252  199 ASP D C   
7564  O O   . ASP D 199 ? 0.6300 0.4858 0.7507 0.0893  -0.1422 0.0301  199 ASP D O   
7565  C CB  . ASP D 199 ? 0.5867 0.4538 0.7085 0.0868  -0.1557 0.0377  199 ASP D CB  
7566  C CG  . ASP D 199 ? 0.5811 0.4465 0.7177 0.0883  -0.1526 0.0421  199 ASP D CG  
7567  O OD1 . ASP D 199 ? 0.6011 0.4579 0.7426 0.0883  -0.1470 0.0381  199 ASP D OD1 
7568  O OD2 . ASP D 199 ? 0.5608 0.4339 0.7044 0.0890  -0.1551 0.0501  199 ASP D OD2 
7569  N N   . ASN D 200 ? 0.5808 0.4309 0.6834 0.0812  -0.1424 0.0162  200 ASN D N   
7570  C CA  . ASN D 200 ? 0.6145 0.4572 0.7141 0.0809  -0.1331 0.0100  200 ASN D CA  
7571  C C   . ASN D 200 ? 0.6591 0.4915 0.7569 0.0748  -0.1266 -0.0007 200 ASN D C   
7572  O O   . ASN D 200 ? 0.6571 0.4879 0.7599 0.0721  -0.1290 -0.0015 200 ASN D O   
7573  C CB  . ASN D 200 ? 0.6318 0.4801 0.7157 0.0797  -0.1348 0.0088  200 ASN D CB  
7574  C CG  . ASN D 200 ? 0.6013 0.4532 0.6902 0.0856  -0.1341 0.0165  200 ASN D CG  
7575  O OD1 . ASN D 200 ? 0.6087 0.4563 0.7037 0.0883  -0.1263 0.0161  200 ASN D OD1 
7576  N ND2 . ASN D 200 ? 0.5705 0.4302 0.6579 0.0871  -0.1413 0.0233  200 ASN D ND2 
7577  N N   . LEU D 201 ? 0.5765 0.4009 0.6675 0.0720  -0.1168 -0.0098 201 LEU D N   
7578  C CA  . LEU D 201 ? 0.6052 0.4178 0.6919 0.0639  -0.1080 -0.0229 201 LEU D CA  
7579  C C   . LEU D 201 ? 0.6528 0.4707 0.7150 0.0535  -0.1096 -0.0334 201 LEU D C   
7580  O O   . LEU D 201 ? 0.6990 0.5067 0.7527 0.0459  -0.0987 -0.0465 201 LEU D O   
7581  C CB  . LEU D 201 ? 0.6127 0.4095 0.7132 0.0678  -0.0917 -0.0263 201 LEU D CB  
7582  C CG  . LEU D 201 ? 0.5984 0.3919 0.7257 0.0775  -0.0888 -0.0143 201 LEU D CG  
7583  C CD1 . LEU D 201 ? 0.6064 0.3913 0.7482 0.0842  -0.0744 -0.0126 201 LEU D CD1 
7584  C CD2 . LEU D 201 ? 0.6052 0.3893 0.7418 0.0741  -0.0859 -0.0171 201 LEU D CD2 
7585  N N   . LEU D 202 ? 0.6079 0.4422 0.6590 0.0527  -0.1222 -0.0271 202 LEU D N   
7586  C CA  . LEU D 202 ? 0.6679 0.5125 0.6966 0.0434  -0.1254 -0.0329 202 LEU D CA  
7587  C C   . LEU D 202 ? 0.7199 0.5645 0.7389 0.0299  -0.1252 -0.0449 202 LEU D C   
7588  O O   . LEU D 202 ? 0.7033 0.5457 0.7324 0.0286  -0.1281 -0.0449 202 LEU D O   
7589  C CB  . LEU D 202 ? 0.6393 0.5022 0.6634 0.0470  -0.1386 -0.0202 202 LEU D CB  
7590  C CG  . LEU D 202 ? 0.6153 0.4824 0.6362 0.0539  -0.1383 -0.0122 202 LEU D CG  
7591  C CD1 . LEU D 202 ? 0.5835 0.4377 0.6185 0.0623  -0.1294 -0.0109 202 LEU D CD1 
7592  C CD2 . LEU D 202 ? 0.5693 0.4496 0.5936 0.0594  -0.1491 0.0015  202 LEU D CD2 
7593  N N   . THR D 203 ? 0.7151 0.5629 0.7134 0.0185  -0.1214 -0.0558 203 THR D N   
7594  C CA  . THR D 203 ? 0.7394 0.5896 0.7240 0.0020  -0.1207 -0.0694 203 THR D CA  
7595  C C   . THR D 203 ? 0.7554 0.6301 0.7169 -0.0081 -0.1309 -0.0677 203 THR D C   
7596  O O   . THR D 203 ? 0.7492 0.6362 0.7066 -0.0011 -0.1369 -0.0558 203 THR D O   
7597  C CB  . THR D 203 ? 0.7575 0.5854 0.7384 -0.0059 -0.1019 -0.0879 203 THR D CB  
7598  O OG1 . THR D 203 ? 0.7830 0.6102 0.7491 -0.0074 -0.0943 -0.0925 203 THR D OG1 
7599  C CG2 . THR D 203 ? 0.7239 0.5295 0.7312 0.0057  -0.0911 -0.0859 203 THR D CG2 
7600  N N   . GLY D 204 ? 0.7903 0.6734 0.7370 -0.0253 -0.1327 -0.0790 204 GLY D N   
7601  C CA  . GLY D 204 ? 0.7964 0.7063 0.7202 -0.0375 -0.1424 -0.0774 204 GLY D CA  
7602  C C   . GLY D 204 ? 0.7554 0.6916 0.6859 -0.0321 -0.1604 -0.0579 204 GLY D C   
7603  O O   . GLY D 204 ? 0.7228 0.6554 0.6745 -0.0200 -0.1650 -0.0476 204 GLY D O   
7604  N N   . PRO D 205 ? 0.7668 0.7313 0.6799 -0.0414 -0.1702 -0.0519 205 PRO D N   
7605  C CA  . PRO D 205 ? 0.7211 0.7129 0.6428 -0.0365 -0.1862 -0.0319 205 PRO D CA  
7606  C C   . PRO D 205 ? 0.6856 0.6779 0.6198 -0.0172 -0.1887 -0.0129 205 PRO D C   
7607  O O   . PRO D 205 ? 0.7003 0.6785 0.6316 -0.0101 -0.1804 -0.0140 205 PRO D O   
7608  C CB  . PRO D 205 ? 0.7339 0.7572 0.6318 -0.0546 -0.1943 -0.0318 205 PRO D CB  
7609  C CG  . PRO D 205 ? 0.7775 0.7900 0.6538 -0.0617 -0.1830 -0.0450 205 PRO D CG  
7610  C CD  . PRO D 205 ? 0.8030 0.7774 0.6877 -0.0579 -0.1665 -0.0627 205 PRO D CD  
7611  N N   . ILE D 206 ? 0.7363 0.7447 0.6858 -0.0093 -0.1992 0.0043  206 ILE D N   
7612  C CA  . ILE D 206 ? 0.6971 0.7115 0.6561 0.0059  -0.2019 0.0237  206 ILE D CA  
7613  C C   . ILE D 206 ? 0.7114 0.7500 0.6524 -0.0005 -0.2064 0.0323  206 ILE D C   
7614  O O   . ILE D 206 ? 0.7178 0.7839 0.6485 -0.0135 -0.2155 0.0350  206 ILE D O   
7615  C CB  . ILE D 206 ? 0.6432 0.6679 0.6239 0.0153  -0.2097 0.0392  206 ILE D CB  
7616  C CG1 . ILE D 206 ? 0.6233 0.6228 0.6213 0.0238  -0.2041 0.0329  206 ILE D CG1 
7617  C CG2 . ILE D 206 ? 0.6079 0.6432 0.5966 0.0278  -0.2121 0.0599  206 ILE D CG2 
7618  C CD1 . ILE D 206 ? 0.5844 0.5934 0.6002 0.0274  -0.2106 0.0418  206 ILE D CD1 
7619  N N   . PRO D 207 ? 0.7211 0.7528 0.6572 0.0068  -0.2007 0.0370  207 PRO D N   
7620  C CA  . PRO D 207 ? 0.7398 0.7948 0.6569 -0.0004 -0.2042 0.0451  207 PRO D CA  
7621  C C   . PRO D 207 ? 0.7013 0.7890 0.6270 0.0026  -0.2166 0.0692  207 PRO D C   
7622  O O   . PRO D 207 ? 0.6585 0.7439 0.6062 0.0181  -0.2176 0.0852  207 PRO D O   
7623  C CB  . PRO D 207 ? 0.7463 0.7832 0.6634 0.0106  -0.1945 0.0474  207 PRO D CB  
7624  C CG  . PRO D 207 ? 0.7485 0.7526 0.6776 0.0174  -0.1847 0.0331  207 PRO D CG  
7625  C CD  . PRO D 207 ? 0.7131 0.7167 0.6599 0.0202  -0.1905 0.0345  207 PRO D CD  
7626  N N   . SER D 208 ? 0.7372 0.8563 0.6458 -0.0132 -0.2255 0.0719  208 SER D N   
7627  C CA  . SER D 208 ? 0.7002 0.8557 0.6183 -0.0111 -0.2379 0.0974  208 SER D CA  
7628  C C   . SER D 208 ? 0.6823 0.8446 0.6061 0.0022  -0.2364 0.1198  208 SER D C   
7629  O O   . SER D 208 ? 0.6445 0.8305 0.5852 0.0103  -0.2435 0.1447  208 SER D O   
7630  C CB  . SER D 208 ? 0.7157 0.9071 0.6122 -0.0333 -0.2482 0.0955  208 SER D CB  
7631  O OG  . SER D 208 ? 0.7587 0.9488 0.6250 -0.0469 -0.2429 0.0817  208 SER D OG  
7632  N N   . SER D 209 ? 0.7337 0.8757 0.6457 0.0050  -0.2263 0.1123  209 SER D N   
7633  C CA  . SER D 209 ? 0.7179 0.8611 0.6371 0.0183  -0.2228 0.1323  209 SER D CA  
7634  C C   . SER D 209 ? 0.6757 0.7991 0.6255 0.0383  -0.2180 0.1429  209 SER D C   
7635  O O   . SER D 209 ? 0.6570 0.7813 0.6174 0.0500  -0.2145 0.1614  209 SER D O   
7636  C CB  . SER D 209 ? 0.7599 0.8847 0.6595 0.0155  -0.2122 0.1196  209 SER D CB  
7637  O OG  . SER D 209 ? 0.7732 0.8611 0.6781 0.0201  -0.2018 0.0990  209 SER D OG  
7638  N N   . PHE D 210 ? 0.7008 0.8061 0.6642 0.0414  -0.2168 0.1312  210 PHE D N   
7639  C CA  . PHE D 210 ? 0.6589 0.7467 0.6492 0.0578  -0.2120 0.1394  210 PHE D CA  
7640  C C   . PHE D 210 ? 0.6233 0.7352 0.6332 0.0665  -0.2172 0.1667  210 PHE D C   
7641  O O   . PHE D 210 ? 0.5998 0.6977 0.6311 0.0809  -0.2103 0.1768  210 PHE D O   
7642  C CB  . PHE D 210 ? 0.6477 0.7180 0.6469 0.0571  -0.2115 0.1232  210 PHE D CB  
7643  C CG  . PHE D 210 ? 0.6601 0.6976 0.6550 0.0583  -0.2018 0.1033  210 PHE D CG  
7644  C CD1 . PHE D 210 ? 0.6952 0.7238 0.6729 0.0545  -0.1957 0.0949  210 PHE D CD1 
7645  C CD2 . PHE D 210 ? 0.6361 0.6535 0.6449 0.0632  -0.1987 0.0945  210 PHE D CD2 
7646  C CE1 . PHE D 210 ? 0.7051 0.7062 0.6822 0.0563  -0.1867 0.0788  210 PHE D CE1 
7647  C CE2 . PHE D 210 ? 0.6431 0.6344 0.6501 0.0644  -0.1905 0.0791  210 PHE D CE2 
7648  C CZ  . PHE D 210 ? 0.6772 0.6606 0.6695 0.0614  -0.1845 0.0717  210 PHE D CZ  
7649  N N   . GLY D 211 ? 0.6272 0.7756 0.6312 0.0576  -0.2284 0.1789  211 GLY D N   
7650  C CA  . GLY D 211 ? 0.6275 0.8031 0.6522 0.0665  -0.2330 0.2084  211 GLY D CA  
7651  C C   . GLY D 211 ? 0.6320 0.8057 0.6634 0.0782  -0.2259 0.2280  211 GLY D C   
7652  O O   . GLY D 211 ? 0.6296 0.8152 0.6856 0.0905  -0.2247 0.2529  211 GLY D O   
7653  N N   . ASN D 212 ? 0.7087 0.8673 0.7202 0.0749  -0.2199 0.2177  212 ASN D N   
7654  C CA  . ASN D 212 ? 0.7053 0.8589 0.7219 0.0852  -0.2117 0.2343  212 ASN D CA  
7655  C C   . ASN D 212 ? 0.6869 0.8039 0.7244 0.1001  -0.1981 0.2315  212 ASN D C   
7656  O O   . ASN D 212 ? 0.6778 0.7896 0.7265 0.1104  -0.1899 0.2480  212 ASN D O   
7657  C CB  . ASN D 212 ? 0.7469 0.8993 0.7336 0.0747  -0.2100 0.2235  212 ASN D CB  
7658  C CG  . ASN D 212 ? 0.7649 0.9568 0.7289 0.0586  -0.2223 0.2291  212 ASN D CG  
7659  O OD1 . ASN D 212 ? 0.7419 0.9660 0.7144 0.0562  -0.2330 0.2455  212 ASN D OD1 
7660  N ND2 . ASN D 212 ? 0.8062 0.9971 0.7410 0.0466  -0.2203 0.2157  212 ASN D ND2 
7661  N N   . LEU D 213 ? 0.6769 0.7697 0.7199 0.1007  -0.1951 0.2118  213 LEU D N   
7662  C CA  . LEU D 213 ? 0.6597 0.7192 0.7193 0.1118  -0.1827 0.2066  213 LEU D CA  
7663  C C   . LEU D 213 ? 0.6246 0.6877 0.7137 0.1237  -0.1794 0.2249  213 LEU D C   
7664  O O   . LEU D 213 ? 0.6078 0.6593 0.7091 0.1262  -0.1778 0.2166  213 LEU D O   
7665  C CB  . LEU D 213 ? 0.6648 0.7005 0.7175 0.1067  -0.1813 0.1797  213 LEU D CB  
7666  C CG  . LEU D 213 ? 0.7007 0.7314 0.7279 0.0953  -0.1829 0.1602  213 LEU D CG  
7667  C CD1 . LEU D 213 ? 0.6975 0.7103 0.7235 0.0911  -0.1828 0.1382  213 LEU D CD1 
7668  C CD2 . LEU D 213 ? 0.7158 0.7311 0.7370 0.0984  -0.1734 0.1594  213 LEU D CD2 
7669  N N   . THR D 214 ? 0.6904 0.7694 0.7917 0.1315  -0.1770 0.2510  214 THR D N   
7670  C CA  . THR D 214 ? 0.6634 0.7478 0.7901 0.1408  -0.1700 0.2652  214 THR D CA  
7671  C C   . THR D 214 ? 0.6521 0.7015 0.7961 0.1497  -0.1541 0.2561  214 THR D C   
7672  O O   . THR D 214 ? 0.6414 0.6893 0.8021 0.1538  -0.1485 0.2565  214 THR D O   
7673  C CB  . THR D 214 ? 0.6714 0.7741 0.8037 0.1447  -0.1649 0.2873  214 THR D CB  
7674  O OG1 . THR D 214 ? 0.6781 0.7619 0.8066 0.1489  -0.1555 0.2897  214 THR D OG1 
7675  C CG2 . THR D 214 ? 0.6827 0.8253 0.7985 0.1341  -0.1807 0.2968  214 THR D CG2 
7676  N N   . LYS D 215 ? 0.6633 0.6856 0.8032 0.1515  -0.1466 0.2478  215 LYS D N   
7677  C CA  . LYS D 215 ? 0.6557 0.6458 0.8095 0.1573  -0.1312 0.2383  215 LYS D CA  
7678  C C   . LYS D 215 ? 0.6519 0.6273 0.8038 0.1530  -0.1353 0.2182  215 LYS D C   
7679  O O   . LYS D 215 ? 0.6480 0.5984 0.8095 0.1559  -0.1236 0.2092  215 LYS D O   
7680  C CB  . LYS D 215 ? 0.6695 0.6379 0.8207 0.1595  -0.1209 0.2377  215 LYS D CB  
7681  C CG  . LYS D 215 ? 0.6722 0.6504 0.8279 0.1642  -0.1136 0.2574  215 LYS D CG  
7682  C CD  . LYS D 215 ? 0.6712 0.6366 0.8498 0.1718  -0.0958 0.2643  215 LYS D CD  
7683  C CE  . LYS D 215 ? 0.6879 0.6745 0.8758 0.1761  -0.0924 0.2877  215 LYS D CE  
7684  N NZ  . LYS D 215 ? 0.6975 0.6763 0.9114 0.1834  -0.0760 0.2958  215 LYS D NZ  
7685  N N   . LEU D 216 ? 0.6014 0.5907 0.7370 0.1438  -0.1489 0.2069  216 LEU D N   
7686  C CA  . LEU D 216 ? 0.5888 0.5638 0.7181 0.1378  -0.1510 0.1847  216 LEU D CA  
7687  C C   . LEU D 216 ? 0.5826 0.5541 0.7323 0.1432  -0.1468 0.1873  216 LEU D C   
7688  O O   . LEU D 216 ? 0.5859 0.5777 0.7486 0.1471  -0.1493 0.2026  216 LEU D O   
7689  C CB  . LEU D 216 ? 0.5871 0.5787 0.6972 0.1270  -0.1651 0.1746  216 LEU D CB  
7690  C CG  . LEU D 216 ? 0.5767 0.5537 0.6766 0.1196  -0.1674 0.1515  216 LEU D CG  
7691  C CD1 . LEU D 216 ? 0.5753 0.5304 0.6652 0.1181  -0.1605 0.1386  216 LEU D CD1 
7692  C CD2 . LEU D 216 ? 0.5795 0.5746 0.6645 0.1094  -0.1794 0.1448  216 LEU D CD2 
7693  N N   . VAL D 217 ? 0.6148 0.5621 0.7663 0.1422  -0.1391 0.1717  217 VAL D N   
7694  C CA  . VAL D 217 ? 0.6024 0.5446 0.7693 0.1451  -0.1347 0.1701  217 VAL D CA  
7695  C C   . VAL D 217 ? 0.5988 0.5374 0.7548 0.1368  -0.1420 0.1513  217 VAL D C   
7696  O O   . VAL D 217 ? 0.5891 0.5368 0.7533 0.1366  -0.1458 0.1522  217 VAL D O   
7697  C CB  . VAL D 217 ? 0.6061 0.5239 0.7873 0.1510  -0.1167 0.1700  217 VAL D CB  
7698  C CG1 . VAL D 217 ? 0.6097 0.5289 0.7994 0.1582  -0.1063 0.1865  217 VAL D CG1 
7699  C CG2 . VAL D 217 ? 0.6180 0.5127 0.7856 0.1440  -0.1118 0.1501  217 VAL D CG2 
7700  N N   . ASN D 218 ? 0.5754 0.5016 0.7148 0.1301  -0.1434 0.1356  218 ASN D N   
7701  C CA  . ASN D 218 ? 0.5701 0.4913 0.7009 0.1230  -0.1488 0.1194  218 ASN D CA  
7702  C C   . ASN D 218 ? 0.5776 0.5065 0.6912 0.1162  -0.1585 0.1123  218 ASN D C   
7703  O O   . ASN D 218 ? 0.5893 0.5145 0.6934 0.1153  -0.1569 0.1112  218 ASN D O   
7704  C CB  . ASN D 218 ? 0.5726 0.4721 0.7020 0.1209  -0.1400 0.1074  218 ASN D CB  
7705  C CG  . ASN D 218 ? 0.5751 0.4645 0.7192 0.1250  -0.1287 0.1102  218 ASN D CG  
7706  O OD1 . ASN D 218 ? 0.5700 0.4681 0.7279 0.1306  -0.1271 0.1212  218 ASN D OD1 
7707  N ND2 . ASN D 218 ? 0.5868 0.4588 0.7284 0.1214  -0.1201 0.1001  218 ASN D ND2 
7708  N N   . LEU D 219 ? 0.5134 0.4518 0.6234 0.1109  -0.1671 0.1067  219 LEU D N   
7709  C CA  . LEU D 219 ? 0.5181 0.4602 0.6122 0.1032  -0.1738 0.0970  219 LEU D CA  
7710  C C   . LEU D 219 ? 0.5111 0.4451 0.6047 0.0985  -0.1756 0.0842  219 LEU D C   
7711  O O   . LEU D 219 ? 0.5065 0.4480 0.6067 0.0969  -0.1797 0.0848  219 LEU D O   
7712  C CB  . LEU D 219 ? 0.5305 0.4957 0.6192 0.0991  -0.1825 0.1042  219 LEU D CB  
7713  C CG  . LEU D 219 ? 0.5488 0.5174 0.6187 0.0896  -0.1871 0.0934  219 LEU D CG  
7714  C CD1 . LEU D 219 ? 0.5551 0.5092 0.6158 0.0907  -0.1806 0.0879  219 LEU D CD1 
7715  C CD2 . LEU D 219 ? 0.5652 0.5593 0.6274 0.0841  -0.1950 0.1020  219 LEU D CD2 
7716  N N   . TYR D 220 ? 0.5717 0.4918 0.6590 0.0964  -0.1725 0.0739  220 TYR D N   
7717  C CA  . TYR D 220 ? 0.5653 0.4776 0.6538 0.0928  -0.1732 0.0640  220 TYR D CA  
7718  C C   . TYR D 220 ? 0.5881 0.4987 0.6664 0.0872  -0.1748 0.0549  220 TYR D C   
7719  O O   . TYR D 220 ? 0.5970 0.5006 0.6698 0.0876  -0.1708 0.0518  220 TYR D O   
7720  C CB  . TYR D 220 ? 0.5507 0.4501 0.6441 0.0950  -0.1671 0.0616  220 TYR D CB  
7721  C CG  . TYR D 220 ? 0.5418 0.4394 0.6444 0.0992  -0.1623 0.0680  220 TYR D CG  
7722  C CD1 . TYR D 220 ? 0.5360 0.4412 0.6469 0.1007  -0.1641 0.0731  220 TYR D CD1 
7723  C CD2 . TYR D 220 ? 0.5451 0.4329 0.6487 0.1009  -0.1548 0.0683  220 TYR D CD2 
7724  C CE1 . TYR D 220 ? 0.5343 0.4361 0.6552 0.1049  -0.1572 0.0785  220 TYR D CE1 
7725  C CE2 . TYR D 220 ? 0.5477 0.4310 0.6597 0.1037  -0.1478 0.0724  220 TYR D CE2 
7726  C CZ  . TYR D 220 ? 0.5424 0.4320 0.6634 0.1063  -0.1484 0.0775  220 TYR D CZ  
7727  O OH  . TYR D 220 ? 0.5500 0.4334 0.6809 0.1095  -0.1390 0.0812  220 TYR D OH  
7728  N N   . LEU D 221 ? 0.4983 0.4144 0.5748 0.0815  -0.1794 0.0502  221 LEU D N   
7729  C CA  . LEU D 221 ? 0.5076 0.4199 0.5747 0.0751  -0.1786 0.0401  221 LEU D CA  
7730  C C   . LEU D 221 ? 0.5064 0.4127 0.5788 0.0710  -0.1787 0.0326  221 LEU D C   
7731  O O   . LEU D 221 ? 0.5174 0.4221 0.5834 0.0639  -0.1779 0.0239  221 LEU D O   
7732  C CB  . LEU D 221 ? 0.5212 0.4475 0.5759 0.0688  -0.1826 0.0402  221 LEU D CB  
7733  C CG  . LEU D 221 ? 0.5262 0.4601 0.5740 0.0719  -0.1823 0.0486  221 LEU D CG  
7734  C CD1 . LEU D 221 ? 0.5413 0.4935 0.5759 0.0636  -0.1878 0.0496  221 LEU D CD1 
7735  C CD2 . LEU D 221 ? 0.5274 0.4477 0.5707 0.0746  -0.1749 0.0441  221 LEU D CD2 
7736  N N   . PHE D 222 ? 0.5657 0.4680 0.6495 0.0746  -0.1785 0.0355  222 PHE D N   
7737  C CA  . PHE D 222 ? 0.5712 0.4696 0.6612 0.0708  -0.1789 0.0307  222 PHE D CA  
7738  C C   . PHE D 222 ? 0.5816 0.4664 0.6737 0.0707  -0.1727 0.0247  222 PHE D C   
7739  O O   . PHE D 222 ? 0.5795 0.4592 0.6695 0.0740  -0.1685 0.0246  222 PHE D O   
7740  C CB  . PHE D 222 ? 0.5377 0.4385 0.6384 0.0738  -0.1807 0.0367  222 PHE D CB  
7741  C CG  . PHE D 222 ? 0.5100 0.4063 0.6144 0.0797  -0.1774 0.0415  222 PHE D CG  
7742  C CD1 . PHE D 222 ? 0.5011 0.4013 0.6044 0.0837  -0.1767 0.0473  222 PHE D CD1 
7743  C CD2 . PHE D 222 ? 0.4986 0.3878 0.6082 0.0803  -0.1747 0.0408  222 PHE D CD2 
7744  C CE1 . PHE D 222 ? 0.4897 0.3844 0.5954 0.0869  -0.1724 0.0496  222 PHE D CE1 
7745  C CE2 . PHE D 222 ? 0.4857 0.3732 0.5968 0.0830  -0.1721 0.0442  222 PHE D CE2 
7746  C CZ  . PHE D 222 ? 0.4841 0.3733 0.5926 0.0856  -0.1705 0.0473  222 PHE D CZ  
7747  N N   . ILE D 223 ? 0.5650 0.4446 0.6633 0.0671  -0.1714 0.0205  223 ILE D N   
7748  C CA  . ILE D 223 ? 0.5744 0.4413 0.6793 0.0676  -0.1642 0.0168  223 ILE D CA  
7749  C C   . ILE D 223 ? 0.6136 0.4740 0.7099 0.0655  -0.1581 0.0092  223 ILE D C   
7750  O O   . ILE D 223 ? 0.6016 0.4580 0.6996 0.0705  -0.1537 0.0111  223 ILE D O   
7751  C CB  . ILE D 223 ? 0.5326 0.3978 0.6476 0.0744  -0.1629 0.0248  223 ILE D CB  
7752  C CG1 . ILE D 223 ? 0.5041 0.3765 0.6238 0.0753  -0.1682 0.0313  223 ILE D CG1 
7753  C CG2 . ILE D 223 ? 0.5374 0.3928 0.6639 0.0758  -0.1559 0.0247  223 ILE D CG2 
7754  C CD1 . ILE D 223 ? 0.4852 0.3595 0.6108 0.0792  -0.1677 0.0385  223 ILE D CD1 
7755  N N   . ASN D 224 ? 0.5995 0.4601 0.6866 0.0570  -0.1574 0.0000  224 ASN D N   
7756  C CA  . ASN D 224 ? 0.6520 0.5067 0.7278 0.0524  -0.1505 -0.0095 224 ASN D CA  
7757  C C   . ASN D 224 ? 0.7143 0.5648 0.7847 0.0406  -0.1473 -0.0217 224 ASN D C   
7758  O O   . ASN D 224 ? 0.7101 0.5596 0.7887 0.0377  -0.1491 -0.0219 224 ASN D O   
7759  C CB  . ASN D 224 ? 0.6594 0.5264 0.7209 0.0524  -0.1554 -0.0066 224 ASN D CB  
7760  C CG  . ASN D 224 ? 0.6224 0.4864 0.6870 0.0615  -0.1523 -0.0003 224 ASN D CG  
7761  O OD1 . ASN D 224 ? 0.6398 0.4939 0.7047 0.0627  -0.1435 -0.0049 224 ASN D OD1 
7762  N ND2 . ASN D 224 ? 0.5735 0.4459 0.6412 0.0673  -0.1585 0.0101  224 ASN D ND2 
7763  N N   . SER D 225 ? 0.6607 0.5084 0.7163 0.0326  -0.1416 -0.0327 225 SER D N   
7764  C CA  . SER D 225 ? 0.7141 0.5587 0.7606 0.0182  -0.1379 -0.0467 225 SER D CA  
7765  C C   . SER D 225 ? 0.7541 0.6160 0.7781 0.0072  -0.1439 -0.0515 225 SER D C   
7766  O O   . SER D 225 ? 0.7789 0.6366 0.7887 -0.0062 -0.1371 -0.0662 225 SER D O   
7767  C CB  . SER D 225 ? 0.7177 0.5387 0.7689 0.0158  -0.1208 -0.0590 225 SER D CB  
7768  O OG  . SER D 225 ? 0.6823 0.4900 0.7549 0.0215  -0.1157 -0.0552 225 SER D OG  
7769  N N   . LEU D 226 ? 0.7185 0.6002 0.7390 0.0121  -0.1558 -0.0387 226 LEU D N   
7770  C CA  . LEU D 226 ? 0.7185 0.6218 0.7201 0.0023  -0.1635 -0.0386 226 LEU D CA  
7771  C C   . LEU D 226 ? 0.7247 0.6388 0.7205 -0.0132 -0.1681 -0.0464 226 LEU D C   
7772  O O   . LEU D 226 ? 0.7108 0.6223 0.7204 -0.0127 -0.1703 -0.0451 226 LEU D O   
7773  C CB  . LEU D 226 ? 0.6635 0.5855 0.6688 0.0122  -0.1746 -0.0204 226 LEU D CB  
7774  C CG  . LEU D 226 ? 0.6386 0.5521 0.6497 0.0263  -0.1709 -0.0119 226 LEU D CG  
7775  C CD1 . LEU D 226 ? 0.6000 0.5286 0.6184 0.0354  -0.1798 0.0052  226 LEU D CD1 
7776  C CD2 . LEU D 226 ? 0.6801 0.5911 0.6751 0.0227  -0.1643 -0.0180 226 LEU D CD2 
7777  N N   . SER D 227 ? 0.7280 0.6559 0.7026 -0.0283 -0.1697 -0.0544 227 SER D N   
7778  C CA  . SER D 227 ? 0.7399 0.6776 0.7058 -0.0471 -0.1723 -0.0655 227 SER D CA  
7779  C C   . SER D 227 ? 0.7357 0.7088 0.6853 -0.0578 -0.1857 -0.0584 227 SER D C   
7780  O O   . SER D 227 ? 0.7247 0.7119 0.6695 -0.0502 -0.1912 -0.0453 227 SER D O   
7781  C CB  . SER D 227 ? 0.7808 0.6959 0.7351 -0.0606 -0.1564 -0.0886 227 SER D CB  
7782  O OG  . SER D 227 ? 0.8051 0.7184 0.7412 -0.0632 -0.1498 -0.0942 227 SER D OG  
7783  N N   . GLY D 228 ? 0.8318 0.8207 0.7741 -0.0759 -0.1910 -0.0658 228 GLY D N   
7784  C CA  . GLY D 228 ? 0.8229 0.8501 0.7506 -0.0885 -0.2046 -0.0582 228 GLY D CA  
7785  C C   . GLY D 228 ? 0.7742 0.8271 0.7207 -0.0775 -0.2193 -0.0346 228 GLY D C   
7786  O O   . GLY D 228 ? 0.7479 0.7883 0.7171 -0.0625 -0.2188 -0.0268 228 GLY D O   
7787  N N   . SER D 229 ? 0.8286 0.9191 0.7656 -0.0854 -0.2319 -0.0224 229 SER D N   
7788  C CA  . SER D 229 ? 0.7815 0.9004 0.7375 -0.0757 -0.2451 0.0017  229 SER D CA  
7789  C C   . SER D 229 ? 0.7518 0.8684 0.7186 -0.0536 -0.2451 0.0212  229 SER D C   
7790  O O   . SER D 229 ? 0.7685 0.8741 0.7227 -0.0498 -0.2390 0.0190  229 SER D O   
7791  C CB  . SER D 229 ? 0.7752 0.9393 0.7196 -0.0939 -0.2589 0.0093  229 SER D CB  
7792  O OG  . SER D 229 ? 0.8007 0.9669 0.7331 -0.1171 -0.2582 -0.0108 229 SER D OG  
7793  N N   . ILE D 230 ? 0.7985 0.9245 0.7894 -0.0395 -0.2506 0.0398  230 ILE D N   
7794  C CA  . ILE D 230 ? 0.7649 0.8895 0.7682 -0.0195 -0.2497 0.0589  230 ILE D CA  
7795  C C   . ILE D 230 ? 0.7604 0.9193 0.7542 -0.0231 -0.2581 0.0756  230 ILE D C   
7796  O O   . ILE D 230 ? 0.7518 0.9467 0.7457 -0.0339 -0.2694 0.0851  230 ILE D O   
7797  C CB  . ILE D 230 ? 0.7200 0.8448 0.7516 -0.0051 -0.2512 0.0728  230 ILE D CB  
7798  C CG1 . ILE D 230 ? 0.7260 0.8254 0.7652 -0.0063 -0.2454 0.0570  230 ILE D CG1 
7799  C CG2 . ILE D 230 ? 0.6887 0.8007 0.7326 0.0149  -0.2455 0.0864  230 ILE D CG2 
7800  C CD1 . ILE D 230 ? 0.6850 0.7839 0.7499 0.0063  -0.2458 0.0687  230 ILE D CD1 
7801  N N   . PRO D 231 ? 0.7325 0.8841 0.7183 -0.0152 -0.2534 0.0808  231 PRO D N   
7802  C CA  . PRO D 231 ? 0.7271 0.9126 0.7044 -0.0182 -0.2612 0.0992  231 PRO D CA  
7803  C C   . PRO D 231 ? 0.6795 0.8910 0.6830 -0.0059 -0.2687 0.1273  231 PRO D C   
7804  O O   . PRO D 231 ? 0.6509 0.8446 0.6771 0.0121  -0.2628 0.1356  231 PRO D O   
7805  C CB  . PRO D 231 ? 0.7407 0.9047 0.7087 -0.0088 -0.2517 0.0982  231 PRO D CB  
7806  C CG  . PRO D 231 ? 0.7618 0.8844 0.7280 -0.0062 -0.2399 0.0753  231 PRO D CG  
7807  C CD  . PRO D 231 ? 0.7404 0.8547 0.7256 -0.0034 -0.2410 0.0717  231 PRO D CD  
7808  N N   . SER D 232 ? 0.7766 1.0318 0.7772 -0.0165 -0.2811 0.1425  232 SER D N   
7809  C CA  . SER D 232 ? 0.7323 1.0161 0.7612 -0.0051 -0.2878 0.1715  232 SER D CA  
7810  C C   . SER D 232 ? 0.7097 0.9903 0.7526 0.0148  -0.2822 0.1939  232 SER D C   
7811  O O   . SER D 232 ? 0.6738 0.9647 0.7458 0.0296  -0.2821 0.2162  232 SER D O   
7812  C CB  . SER D 232 ? 0.7263 1.0625 0.7495 -0.0223 -0.3033 0.1843  232 SER D CB  
7813  O OG  . SER D 232 ? 0.7571 1.1060 0.7468 -0.0405 -0.3067 0.1748  232 SER D OG  
7814  N N   . GLU D 233 ? 0.7242 0.9898 0.7479 0.0153  -0.2763 0.1886  233 GLU D N   
7815  C CA  . GLU D 233 ? 0.7060 0.9649 0.7423 0.0333  -0.2693 0.2083  233 GLU D CA  
7816  C C   . GLU D 233 ? 0.6854 0.9069 0.7449 0.0521  -0.2570 0.2059  233 GLU D C   
7817  O O   . GLU D 233 ? 0.6615 0.8801 0.7404 0.0682  -0.2508 0.2255  233 GLU D O   
7818  C CB  . GLU D 233 ? 0.7383 0.9866 0.7480 0.0285  -0.2647 0.2000  233 GLU D CB  
7819  C CG  . GLU D 233 ? 0.7546 1.0426 0.7409 0.0115  -0.2753 0.2076  233 GLU D CG  
7820  C CD  . GLU D 233 ? 0.7845 1.0808 0.7465 -0.0121 -0.2816 0.1836  233 GLU D CD  
7821  O OE1 . GLU D 233 ? 0.8158 1.0769 0.7651 -0.0166 -0.2730 0.1555  233 GLU D OE1 
7822  O OE2 . GLU D 233 ? 0.7766 1.1151 0.7330 -0.0265 -0.2946 0.1934  233 GLU D OE2 
7823  N N   . ILE D 234 ? 0.6967 0.8899 0.7543 0.0496  -0.2527 0.1824  234 ILE D N   
7824  C CA  . ILE D 234 ? 0.6755 0.8355 0.7523 0.0648  -0.2417 0.1788  234 ILE D CA  
7825  C C   . ILE D 234 ? 0.6379 0.8122 0.7458 0.0774  -0.2414 0.2015  234 ILE D C   
7826  O O   . ILE D 234 ? 0.6187 0.7732 0.7441 0.0925  -0.2306 0.2087  234 ILE D O   
7827  C CB  . ILE D 234 ? 0.6877 0.8228 0.7581 0.0581  -0.2393 0.1530  234 ILE D CB  
7828  C CG1 . ILE D 234 ? 0.7280 0.8482 0.7706 0.0466  -0.2372 0.1316  234 ILE D CG1 
7829  C CG2 . ILE D 234 ? 0.6623 0.7666 0.7504 0.0718  -0.2287 0.1496  234 ILE D CG2 
7830  C CD1 . ILE D 234 ? 0.7297 0.8178 0.7695 0.0559  -0.2258 0.1244  234 ILE D CD1 
7831  N N   . GLY D 235 ? 0.7064 0.9160 0.8223 0.0709  -0.2523 0.2132  235 GLY D N   
7832  C CA  . GLY D 235 ? 0.6803 0.8996 0.8231 0.0820  -0.2448 0.2282  235 GLY D CA  
7833  C C   . GLY D 235 ? 0.6828 0.9095 0.8361 0.0933  -0.2349 0.2482  235 GLY D C   
7834  O O   . GLY D 235 ? 0.6827 0.9114 0.8595 0.1033  -0.2255 0.2597  235 GLY D O   
7835  N N   . ASN D 236 ? 0.7058 0.9361 0.8433 0.0914  -0.2364 0.2530  236 ASN D N   
7836  C CA  . ASN D 236 ? 0.7179 0.9548 0.8655 0.1011  -0.2273 0.2728  236 ASN D CA  
7837  C C   . ASN D 236 ? 0.7122 0.9130 0.8644 0.1143  -0.2127 0.2711  236 ASN D C   
7838  O O   . ASN D 236 ? 0.7233 0.9255 0.8828 0.1218  -0.2042 0.2863  236 ASN D O   
7839  C CB  . ASN D 236 ? 0.7371 1.0063 0.8649 0.0894  -0.2379 0.2820  236 ASN D CB  
7840  C CG  . ASN D 236 ? 0.7479 1.0569 0.8750 0.0765  -0.2498 0.2878  236 ASN D CG  
7841  O OD1 . ASN D 236 ? 0.7593 1.0907 0.8620 0.0592  -0.2626 0.2817  236 ASN D OD1 
7842  N ND2 . ASN D 236 ? 0.7464 1.0645 0.9000 0.0835  -0.2449 0.2990  236 ASN D ND2 
7843  N N   . LEU D 237 ? 0.7019 0.8710 0.8509 0.1163  -0.2094 0.2533  237 LEU D N   
7844  C CA  . LEU D 237 ? 0.6979 0.8327 0.8517 0.1271  -0.1951 0.2501  237 LEU D CA  
7845  C C   . LEU D 237 ? 0.6969 0.8188 0.8766 0.1393  -0.1790 0.2570  237 LEU D C   
7846  O O   . LEU D 237 ? 0.6873 0.8029 0.8777 0.1403  -0.1770 0.2497  237 LEU D O   
7847  C CB  . LEU D 237 ? 0.6988 0.8059 0.8420 0.1237  -0.1973 0.2291  237 LEU D CB  
7848  C CG  . LEU D 237 ? 0.7266 0.8409 0.8418 0.1102  -0.2089 0.2178  237 LEU D CG  
7849  C CD1 . LEU D 237 ? 0.7393 0.8255 0.8405 0.1034  -0.2067 0.1889  237 LEU D CD1 
7850  C CD2 . LEU D 237 ? 0.7402 0.8528 0.8453 0.1127  -0.2046 0.2259  237 LEU D CD2 
7851  N N   . PRO D 238 ? 0.7284 0.8456 0.9191 0.1480  -0.1667 0.2709  238 PRO D N   
7852  C CA  . PRO D 238 ? 0.7325 0.8426 0.9497 0.1580  -0.1515 0.2800  238 PRO D CA  
7853  C C   . PRO D 238 ? 0.7233 0.7957 0.9478 0.1638  -0.1373 0.2653  238 PRO D C   
7854  O O   . PRO D 238 ? 0.7225 0.7893 0.9654 0.1685  -0.1280 0.2661  238 PRO D O   
7855  C CB  . PRO D 238 ? 0.7502 0.8680 0.9754 0.1636  -0.1436 0.2997  238 PRO D CB  
7856  C CG  . PRO D 238 ? 0.7506 0.8592 0.9534 0.1597  -0.1480 0.2939  238 PRO D CG  
7857  C CD  . PRO D 238 ? 0.7397 0.8586 0.9200 0.1484  -0.1657 0.2797  238 PRO D CD  
7858  N N   . ASN D 239 ? 0.7278 0.7750 0.9383 0.1627  -0.1350 0.2525  239 ASN D N   
7859  C CA  . ASN D 239 ? 0.7220 0.7344 0.9378 0.1663  -0.1213 0.2388  239 ASN D CA  
7860  C C   . ASN D 239 ? 0.7059 0.7080 0.9119 0.1601  -0.1289 0.2194  239 ASN D C   
7861  O O   . ASN D 239 ? 0.7023 0.6774 0.9110 0.1612  -0.1192 0.2071  239 ASN D O   
7862  C CB  . ASN D 239 ? 0.7281 0.7185 0.9380 0.1685  -0.1122 0.2371  239 ASN D CB  
7863  C CG  . ASN D 239 ? 0.7454 0.7459 0.9647 0.1740  -0.1047 0.2569  239 ASN D CG  
7864  O OD1 . ASN D 239 ? 0.7539 0.7752 0.9882 0.1773  -0.1036 0.2723  239 ASN D OD1 
7865  N ND2 . ASN D 239 ? 0.7515 0.7381 0.9638 0.1747  -0.0994 0.2576  239 ASN D ND2 
7866  N N   . LEU D 240 ? 0.6344 0.6573 0.8295 0.1525  -0.1459 0.2166  240 LEU D N   
7867  C CA  . LEU D 240 ? 0.6296 0.6429 0.8164 0.1459  -0.1537 0.1989  240 LEU D CA  
7868  C C   . LEU D 240 ? 0.6217 0.6240 0.8236 0.1491  -0.1446 0.1937  240 LEU D C   
7869  O O   . LEU D 240 ? 0.6193 0.6362 0.8366 0.1531  -0.1408 0.2045  240 LEU D O   
7870  C CB  . LEU D 240 ? 0.6315 0.6709 0.8070 0.1364  -0.1724 0.1984  240 LEU D CB  
7871  C CG  . LEU D 240 ? 0.6363 0.6648 0.7990 0.1272  -0.1809 0.1780  240 LEU D CG  
7872  C CD1 . LEU D 240 ? 0.6506 0.6581 0.7931 0.1231  -0.1780 0.1628  240 LEU D CD1 
7873  C CD2 . LEU D 240 ? 0.6430 0.6976 0.7970 0.1167  -0.1955 0.1766  240 LEU D CD2 
7874  N N   . ARG D 241 ? 0.6776 0.6548 0.8757 0.1470  -0.1410 0.1777  241 ARG D N   
7875  C CA  . ARG D 241 ? 0.6738 0.6392 0.8836 0.1485  -0.1329 0.1712  241 ARG D CA  
7876  C C   . ARG D 241 ? 0.6711 0.6348 0.8724 0.1405  -0.1442 0.1568  241 ARG D C   
7877  O O   . ARG D 241 ? 0.6652 0.6369 0.8757 0.1400  -0.1451 0.1570  241 ARG D O   
7878  C CB  . ARG D 241 ? 0.6842 0.6200 0.8991 0.1523  -0.1161 0.1655  241 ARG D CB  
7879  C CG  . ARG D 241 ? 0.6886 0.6209 0.9109 0.1594  -0.1036 0.1779  241 ARG D CG  
7880  C CD  . ARG D 241 ? 0.6942 0.6146 0.9365 0.1659  -0.0845 0.1821  241 ARG D CD  
7881  N NE  . ARG D 241 ? 0.6997 0.6008 0.9446 0.1630  -0.0785 0.1679  241 ARG D NE  
7882  C CZ  . ARG D 241 ? 0.7023 0.5986 0.9636 0.1666  -0.0661 0.1689  241 ARG D CZ  
7883  N NH1 . ARG D 241 ? 0.7016 0.6107 0.9800 0.1736  -0.0581 0.1838  241 ARG D NH1 
7884  N NH2 . ARG D 241 ? 0.7140 0.5930 0.9756 0.1626  -0.0618 0.1553  241 ARG D NH2 
7885  N N   . GLU D 242 ? 0.5968 0.5503 0.7778 0.1332  -0.1495 0.1423  242 GLU D N   
7886  C CA  . GLU D 242 ? 0.5947 0.5451 0.7642 0.1246  -0.1566 0.1267  242 GLU D CA  
7887  C C   . GLU D 242 ? 0.5991 0.5612 0.7523 0.1173  -0.1690 0.1225  242 GLU D C   
7888  O O   . GLU D 242 ? 0.6077 0.5669 0.7500 0.1167  -0.1692 0.1220  242 GLU D O   
7889  C CB  . GLU D 242 ? 0.5996 0.5261 0.7613 0.1216  -0.1490 0.1121  242 GLU D CB  
7890  C CG  . GLU D 242 ? 0.6085 0.5198 0.7817 0.1268  -0.1338 0.1140  242 GLU D CG  
7891  C CD  . GLU D 242 ? 0.6185 0.5129 0.7848 0.1208  -0.1282 0.0991  242 GLU D CD  
7892  O OE1 . GLU D 242 ? 0.6196 0.5081 0.7716 0.1149  -0.1323 0.0893  242 GLU D OE1 
7893  O OE2 . GLU D 242 ? 0.6280 0.5165 0.8037 0.1218  -0.1193 0.0980  242 GLU D OE2 
7894  N N   . LEU D 243 ? 0.4985 0.4731 0.6500 0.1112  -0.1781 0.1188  243 LEU D N   
7895  C CA  . LEU D 243 ? 0.5018 0.4859 0.6375 0.1021  -0.1881 0.1121  243 LEU D CA  
7896  C C   . LEU D 243 ? 0.4961 0.4715 0.6271 0.0952  -0.1905 0.0976  243 LEU D C   
7897  O O   . LEU D 243 ? 0.4930 0.4767 0.6331 0.0933  -0.1933 0.0987  243 LEU D O   
7898  C CB  . LEU D 243 ? 0.5086 0.5216 0.6477 0.0995  -0.1971 0.1245  243 LEU D CB  
7899  C CG  . LEU D 243 ? 0.5166 0.5414 0.6374 0.0876  -0.2066 0.1166  243 LEU D CG  
7900  C CD1 . LEU D 243 ? 0.5222 0.5350 0.6260 0.0863  -0.2038 0.1099  243 LEU D CD1 
7901  C CD2 . LEU D 243 ? 0.5251 0.5830 0.6491 0.0835  -0.2161 0.1305  243 LEU D CD2 
7902  N N   . CYS D 244 ? 0.5468 0.5064 0.6655 0.0917  -0.1887 0.0854  244 CYS D N   
7903  C CA  . CYS D 244 ? 0.5486 0.4984 0.6644 0.0862  -0.1895 0.0733  244 CYS D CA  
7904  C C   . CYS D 244 ? 0.5757 0.5258 0.6777 0.0781  -0.1934 0.0640  244 CYS D C   
7905  O O   . CYS D 244 ? 0.5842 0.5233 0.6776 0.0783  -0.1899 0.0585  244 CYS D O   
7906  C CB  . CYS D 244 ? 0.5353 0.4665 0.6520 0.0894  -0.1824 0.0682  244 CYS D CB  
7907  S SG  . CYS D 244 ? 0.5201 0.4471 0.6500 0.0959  -0.1750 0.0748  244 CYS D SG  
7908  N N   . LEU D 245 ? 0.5068 0.4691 0.6074 0.0703  -0.1994 0.0616  245 LEU D N   
7909  C CA  . LEU D 245 ? 0.5239 0.4850 0.6113 0.0605  -0.2011 0.0504  245 LEU D CA  
7910  C C   . LEU D 245 ? 0.5299 0.4814 0.6207 0.0548  -0.2000 0.0404  245 LEU D C   
7911  O O   . LEU D 245 ? 0.5659 0.5184 0.6487 0.0446  -0.2010 0.0310  245 LEU D O   
7912  C CB  . LEU D 245 ? 0.5409 0.5251 0.6208 0.0528  -0.2085 0.0543  245 LEU D CB  
7913  C CG  . LEU D 245 ? 0.5368 0.5352 0.6155 0.0584  -0.2104 0.0680  245 LEU D CG  
7914  C CD1 . LEU D 245 ? 0.5558 0.5806 0.6250 0.0484  -0.2188 0.0718  245 LEU D CD1 
7915  C CD2 . LEU D 245 ? 0.5393 0.5217 0.6093 0.0631  -0.2038 0.0648  245 LEU D CD2 
7916  N N   . ASP D 246 ? 0.5706 0.5128 0.6728 0.0603  -0.1970 0.0422  246 ASP D N   
7917  C CA  . ASP D 246 ? 0.5803 0.5149 0.6881 0.0557  -0.1958 0.0358  246 ASP D CA  
7918  C C   . ASP D 246 ? 0.6071 0.5246 0.7095 0.0531  -0.1900 0.0257  246 ASP D C   
7919  O O   . ASP D 246 ? 0.6080 0.5180 0.7042 0.0565  -0.1863 0.0243  246 ASP D O   
7920  C CB  . ASP D 246 ? 0.5438 0.4742 0.6637 0.0620  -0.1936 0.0415  246 ASP D CB  
7921  C CG  . ASP D 246 ? 0.5178 0.4382 0.6372 0.0699  -0.1888 0.0444  246 ASP D CG  
7922  O OD1 . ASP D 246 ? 0.5083 0.4333 0.6256 0.0744  -0.1885 0.0498  246 ASP D OD1 
7923  O OD2 . ASP D 246 ? 0.5092 0.4185 0.6311 0.0710  -0.1851 0.0421  246 ASP D OD2 
7924  N N   . ARG D 247 ? 0.6056 0.5166 0.7122 0.0470  -0.1881 0.0192  247 ARG D N   
7925  C CA  . ARG D 247 ? 0.6320 0.5252 0.7390 0.0456  -0.1804 0.0113  247 ARG D CA  
7926  C C   . ARG D 247 ? 0.6788 0.5680 0.7727 0.0411  -0.1769 0.0027  247 ARG D C   
7927  O O   . ARG D 247 ? 0.6721 0.5516 0.7644 0.0463  -0.1714 0.0021  247 ARG D O   
7928  C CB  . ARG D 247 ? 0.5866 0.4702 0.7020 0.0550  -0.1765 0.0174  247 ARG D CB  
7929  C CG  . ARG D 247 ? 0.5579 0.4425 0.6850 0.0569  -0.1777 0.0234  247 ARG D CG  
7930  C CD  . ARG D 247 ? 0.5179 0.3990 0.6500 0.0643  -0.1756 0.0306  247 ARG D CD  
7931  N NE  . ARG D 247 ? 0.4917 0.3810 0.6200 0.0685  -0.1786 0.0358  247 ARG D NE  
7932  C CZ  . ARG D 247 ? 0.4661 0.3552 0.5966 0.0727  -0.1774 0.0410  247 ARG D CZ  
7933  N NH1 . ARG D 247 ? 0.4585 0.3433 0.5948 0.0734  -0.1749 0.0437  247 ARG D NH1 
7934  N NH2 . ARG D 247 ? 0.4534 0.3475 0.5807 0.0755  -0.1780 0.0441  247 ARG D NH2 
7935  N N   . ASN D 248 ? 0.6456 0.5441 0.7298 0.0302  -0.1799 -0.0040 248 ASN D N   
7936  C CA  . ASN D 248 ? 0.7044 0.6004 0.7733 0.0226  -0.1759 -0.0143 248 ASN D CA  
7937  C C   . ASN D 248 ? 0.7565 0.6536 0.8198 0.0071  -0.1748 -0.0265 248 ASN D C   
7938  O O   . ASN D 248 ? 0.7535 0.6501 0.8271 0.0040  -0.1760 -0.0266 248 ASN D O   
7939  C CB  . ASN D 248 ? 0.6834 0.5962 0.7408 0.0242  -0.1822 -0.0078 248 ASN D CB  
7940  C CG  . ASN D 248 ? 0.6650 0.5682 0.7210 0.0343  -0.1772 -0.0043 248 ASN D CG  
7941  O OD1 . ASN D 248 ? 0.7093 0.6022 0.7570 0.0317  -0.1697 -0.0129 248 ASN D OD1 
7942  N ND2 . ASN D 248 ? 0.6022 0.5088 0.6666 0.0451  -0.1803 0.0076  248 ASN D ND2 
7943  N N   . ASN D 249 ? 0.8248 0.7231 0.8712 -0.0038 -0.1717 -0.0376 249 ASN D N   
7944  C CA  . ASN D 249 ? 0.8485 0.7487 0.8861 -0.0217 -0.1699 -0.0517 249 ASN D CA  
7945  C C   . ASN D 249 ? 0.8428 0.7719 0.8638 -0.0333 -0.1809 -0.0504 249 ASN D C   
7946  O O   . ASN D 249 ? 0.8698 0.8027 0.8736 -0.0501 -0.1784 -0.0641 249 ASN D O   
7947  C CB  . ASN D 249 ? 0.8806 0.7560 0.9119 -0.0283 -0.1541 -0.0687 249 ASN D CB  
7948  C CG  . ASN D 249 ? 0.8766 0.7290 0.9254 -0.0272 -0.1437 -0.0736 249 ASN D CG  
7949  O OD1 . ASN D 249 ? 0.8840 0.7346 0.9332 -0.0402 -0.1418 -0.0829 249 ASN D OD1 
7950  N ND2 . ASN D 249 ? 0.8576 0.6935 0.9218 -0.0120 -0.1369 -0.0662 249 ASN D ND2 
7951  N N   . LEU D 250 ? 0.7818 0.7327 0.8084 -0.0250 -0.1927 -0.0335 250 LEU D N   
7952  C CA  . LEU D 250 ? 0.7700 0.7528 0.7853 -0.0342 -0.2042 -0.0274 250 LEU D CA  
7953  C C   . LEU D 250 ? 0.7770 0.7747 0.7920 -0.0509 -0.2095 -0.0337 250 LEU D C   
7954  O O   . LEU D 250 ? 0.7690 0.7589 0.7996 -0.0494 -0.2084 -0.0339 250 LEU D O   
7955  C CB  . LEU D 250 ? 0.7180 0.7183 0.7450 -0.0194 -0.2132 -0.0060 250 LEU D CB  
7956  C CG  . LEU D 250 ? 0.7031 0.6923 0.7296 -0.0045 -0.2089 0.0011  250 LEU D CG  
7957  C CD1 . LEU D 250 ? 0.6460 0.6464 0.6879 0.0100  -0.2146 0.0204  250 LEU D CD1 
7958  C CD2 . LEU D 250 ? 0.7309 0.7290 0.7363 -0.0119 -0.2088 -0.0023 250 LEU D CD2 
7959  N N   . THR D 251 ? 0.7677 0.7885 0.7645 -0.0680 -0.2153 -0.0384 251 THR D N   
7960  C CA  . THR D 251 ? 0.7733 0.8143 0.7671 -0.0873 -0.2218 -0.0443 251 THR D CA  
7961  C C   . THR D 251 ? 0.7460 0.8308 0.7373 -0.0911 -0.2379 -0.0269 251 THR D C   
7962  O O   . THR D 251 ? 0.7221 0.8182 0.7158 -0.0776 -0.2426 -0.0101 251 THR D O   
7963  C CB  . THR D 251 ? 0.8189 0.8482 0.7915 -0.1094 -0.2124 -0.0691 251 THR D CB  
7964  O OG1 . THR D 251 ? 0.8330 0.8791 0.7814 -0.1187 -0.2151 -0.0711 251 THR D OG1 
7965  C CG2 . THR D 251 ? 0.8429 0.8285 0.8203 -0.1024 -0.1945 -0.0831 251 THR D CG2 
7966  N N   . GLY D 252 ? 0.7879 0.8984 0.7760 -0.1101 -0.2459 -0.0300 252 GLY D N   
7967  C CA  . GLY D 252 ? 0.7623 0.9193 0.7486 -0.1163 -0.2616 -0.0127 252 GLY D CA  
7968  C C   . GLY D 252 ? 0.7158 0.8908 0.7305 -0.0997 -0.2701 0.0115  252 GLY D C   
7969  O O   . GLY D 252 ? 0.7025 0.8550 0.7368 -0.0854 -0.2645 0.0133  252 GLY D O   
7970  N N   . LYS D 253 ? 0.7693 0.9868 0.7863 -0.1018 -0.2834 0.0312  253 LYS D N   
7971  C CA  . LYS D 253 ? 0.7245 0.9650 0.7698 -0.0876 -0.2911 0.0559  253 LYS D CA  
7972  C C   . LYS D 253 ? 0.6972 0.9262 0.7547 -0.0619 -0.2870 0.0733  253 LYS D C   
7973  O O   . LYS D 253 ? 0.7087 0.9260 0.7512 -0.0575 -0.2828 0.0713  253 LYS D O   
7974  C CB  . LYS D 253 ? 0.7060 1.0007 0.7517 -0.1015 -0.3068 0.0717  253 LYS D CB  
7975  C CG  . LYS D 253 ? 0.7165 1.0290 0.7611 -0.1246 -0.3124 0.0603  253 LYS D CG  
7976  C CD  . LYS D 253 ? 0.6911 1.0630 0.7384 -0.1380 -0.3293 0.0794  253 LYS D CD  
7977  C CE  . LYS D 253 ? 0.6572 1.0524 0.7383 -0.1305 -0.3357 0.0981  253 LYS D CE  
7978  N NZ  . LYS D 253 ? 0.6656 1.0798 0.7458 -0.1552 -0.3415 0.0861  253 LYS D NZ  
7979  N N   . ILE D 254 ? 0.6859 0.9177 0.7710 -0.0458 -0.2872 0.0895  254 ILE D N   
7980  C CA  . ILE D 254 ? 0.6554 0.8804 0.7546 -0.0229 -0.2829 0.1076  254 ILE D CA  
7981  C C   . ILE D 254 ? 0.6373 0.9033 0.7389 -0.0224 -0.2928 0.1311  254 ILE D C   
7982  O O   . ILE D 254 ? 0.6239 0.9287 0.7369 -0.0299 -0.3033 0.1447  254 ILE D O   
7983  C CB  . ILE D 254 ? 0.6249 0.8394 0.7521 -0.0074 -0.2780 0.1162  254 ILE D CB  
7984  C CG1 . ILE D 254 ? 0.6390 0.8124 0.7632 -0.0059 -0.2677 0.0956  254 ILE D CG1 
7985  C CG2 . ILE D 254 ? 0.5926 0.8055 0.7360 0.0138  -0.2733 0.1362  254 ILE D CG2 
7986  C CD1 . ILE D 254 ? 0.6125 0.7773 0.7609 0.0058  -0.2630 0.1019  254 ILE D CD1 
7987  N N   . PRO D 255 ? 0.6872 0.9483 0.7798 -0.0140 -0.2899 0.1380  255 PRO D N   
7988  C CA  . PRO D 255 ? 0.6707 0.9723 0.7648 -0.0142 -0.2992 0.1620  255 PRO D CA  
7989  C C   . PRO D 255 ? 0.6292 0.9521 0.7573 0.0018  -0.3000 0.1893  255 PRO D C   
7990  O O   . PRO D 255 ? 0.6104 0.9080 0.7575 0.0211  -0.2890 0.1943  255 PRO D O   
7991  C CB  . PRO D 255 ? 0.6811 0.9623 0.7607 -0.0055 -0.2920 0.1614  255 PRO D CB  
7992  C CG  . PRO D 255 ? 0.7133 0.9505 0.7757 -0.0089 -0.2818 0.1324  255 PRO D CG  
7993  C CD  . PRO D 255 ? 0.7035 0.9238 0.7831 -0.0056 -0.2783 0.1244  255 PRO D CD  
7994  N N   . SER D 256 ? 0.6550 1.0162 0.7871 -0.0062 -0.3047 0.2007  256 SER D N   
7995  C CA  . SER D 256 ? 0.6462 1.0212 0.8072 0.0090  -0.2973 0.2221  256 SER D CA  
7996  C C   . SER D 256 ? 0.6460 1.0113 0.8150 0.0279  -0.2865 0.2386  256 SER D C   
7997  O O   . SER D 256 ? 0.6421 1.0074 0.8369 0.0434  -0.2765 0.2545  256 SER D O   
7998  C CB  . SER D 256 ? 0.6652 1.0848 0.8275 -0.0053 -0.3059 0.2321  256 SER D CB  
7999  O OG  . SER D 256 ? 0.6869 1.1278 0.8236 -0.0196 -0.3135 0.2324  256 SER D OG  
8000  N N   . SER D 257 ? 0.7002 1.0566 0.8477 0.0261  -0.2875 0.2348  257 SER D N   
8001  C CA  . SER D 257 ? 0.6999 1.0423 0.8539 0.0433  -0.2765 0.2481  257 SER D CA  
8002  C C   . SER D 257 ? 0.6802 0.9837 0.8522 0.0620  -0.2624 0.2449  257 SER D C   
8003  O O   . SER D 257 ? 0.6805 0.9726 0.8657 0.0774  -0.2502 0.2574  257 SER D O   
8004  C CB  . SER D 257 ? 0.7091 1.0474 0.8345 0.0359  -0.2809 0.2417  257 SER D CB  
8005  O OG  . SER D 257 ? 0.7269 1.0949 0.8287 0.0131  -0.2944 0.2347  257 SER D OG  
8006  N N   . PHE D 258 ? 0.6469 0.9295 0.8194 0.0597  -0.2634 0.2280  258 PHE D N   
8007  C CA  . PHE D 258 ? 0.6306 0.8769 0.8180 0.0752  -0.2500 0.2234  258 PHE D CA  
8008  C C   . PHE D 258 ? 0.6301 0.8803 0.8454 0.0888  -0.2377 0.2389  258 PHE D C   
8009  O O   . PHE D 258 ? 0.6224 0.8442 0.8491 0.1024  -0.2234 0.2382  258 PHE D O   
8010  C CB  . PHE D 258 ? 0.6294 0.8574 0.8139 0.0682  -0.2546 0.2043  258 PHE D CB  
8011  C CG  . PHE D 258 ? 0.6527 0.8533 0.8130 0.0619  -0.2562 0.1844  258 PHE D CG  
8012  C CD1 . PHE D 258 ? 0.6731 0.8800 0.8108 0.0547  -0.2602 0.1825  258 PHE D CD1 
8013  C CD2 . PHE D 258 ? 0.6575 0.8232 0.8146 0.0629  -0.2484 0.1643  258 PHE D CD2 
8014  C CE1 . PHE D 258 ? 0.7001 0.8777 0.8140 0.0492  -0.2553 0.1604  258 PHE D CE1 
8015  C CE2 . PHE D 258 ? 0.6803 0.8186 0.8146 0.0577  -0.2445 0.1439  258 PHE D CE2 
8016  C CZ  . PHE D 258 ? 0.7027 0.8464 0.8162 0.0512  -0.2475 0.1417  258 PHE D CZ  
8017  N N   . GLY D 259 ? 0.6340 0.9189 0.8605 0.0845  -0.2424 0.2527  259 GLY D N   
8018  C CA  . GLY D 259 ? 0.6364 0.9267 0.8912 0.0970  -0.2306 0.2694  259 GLY D CA  
8019  C C   . GLY D 259 ? 0.6442 0.9242 0.9075 0.1106  -0.2176 0.2834  259 GLY D C   
8020  O O   . GLY D 259 ? 0.6459 0.9209 0.9337 0.1226  -0.2041 0.2947  259 GLY D O   
8021  N N   . ASN D 260 ? 0.6547 0.9316 0.8990 0.1086  -0.2206 0.2829  260 ASN D N   
8022  C CA  . ASN D 260 ? 0.6629 0.9281 0.9143 0.1206  -0.2081 0.2954  260 ASN D CA  
8023  C C   . ASN D 260 ? 0.6518 0.8731 0.9027 0.1310  -0.1944 0.2829  260 ASN D C   
8024  O O   . ASN D 260 ? 0.6584 0.8658 0.9196 0.1416  -0.1808 0.2921  260 ASN D O   
8025  C CB  . ASN D 260 ? 0.6763 0.9597 0.9079 0.1132  -0.2171 0.3019  260 ASN D CB  
8026  C CG  . ASN D 260 ? 0.6904 1.0189 0.9186 0.1000  -0.2313 0.3129  260 ASN D CG  
8027  O OD1 . ASN D 260 ? 0.6963 1.0470 0.9463 0.1019  -0.2298 0.3274  260 ASN D OD1 
8028  N ND2 . ASN D 260 ? 0.6977 1.0408 0.8983 0.0854  -0.2448 0.3058  260 ASN D ND2 
8029  N N   . LEU D 261 ? 0.6450 0.8450 0.8850 0.1272  -0.1972 0.2626  261 LEU D N   
8030  C CA  . LEU D 261 ? 0.6356 0.7956 0.8729 0.1346  -0.1854 0.2497  261 LEU D CA  
8031  C C   . LEU D 261 ? 0.6339 0.7787 0.8954 0.1452  -0.1691 0.2528  261 LEU D C   
8032  O O   . LEU D 261 ? 0.6232 0.7554 0.8891 0.1448  -0.1669 0.2417  261 LEU D O   
8033  C CB  . LEU D 261 ? 0.6223 0.7673 0.8418 0.1260  -0.1945 0.2289  261 LEU D CB  
8034  C CG  . LEU D 261 ? 0.6251 0.7792 0.8201 0.1147  -0.2090 0.2229  261 LEU D CG  
8035  C CD1 . LEU D 261 ? 0.6256 0.7694 0.8095 0.1047  -0.2188 0.2040  261 LEU D CD1 
8036  C CD2 . LEU D 261 ? 0.6297 0.7641 0.8150 0.1202  -0.2023 0.2228  261 LEU D CD2 
8037  N N   . LYS D 262 ? 0.6518 0.7981 0.9297 0.1545  -0.1568 0.2688  262 LYS D N   
8038  C CA  . LYS D 262 ? 0.6546 0.7898 0.9579 0.1641  -0.1398 0.2743  262 LYS D CA  
8039  C C   . LYS D 262 ? 0.6507 0.7452 0.9534 0.1700  -0.1241 0.2608  262 LYS D C   
8040  O O   . LYS D 262 ? 0.6532 0.7349 0.9747 0.1764  -0.1092 0.2614  262 LYS D O   
8041  C CB  . LYS D 262 ? 0.6721 0.8259 0.9964 0.1710  -0.1317 0.2980  262 LYS D CB  
8042  C CG  . LYS D 262 ? 0.6792 0.8765 1.0061 0.1644  -0.1465 0.3138  262 LYS D CG  
8043  C CD  . LYS D 262 ? 0.6747 0.8893 1.0174 0.1623  -0.1494 0.3158  262 LYS D CD  
8044  C CE  . LYS D 262 ? 0.6796 0.8802 1.0514 0.1740  -0.1290 0.3231  262 LYS D CE  
8045  N NZ  . LYS D 262 ? 0.6848 0.9166 1.0802 0.1739  -0.1306 0.3386  262 LYS D NZ  
8046  N N   . ASN D 263 ? 0.7512 0.8261 1.0337 0.1675  -0.1262 0.2491  263 ASN D N   
8047  C CA  . ASN D 263 ? 0.7486 0.7866 1.0289 0.1709  -0.1124 0.2356  263 ASN D CA  
8048  C C   . ASN D 263 ? 0.7329 0.7562 0.9977 0.1639  -0.1200 0.2155  263 ASN D C   
8049  O O   . ASN D 263 ? 0.7310 0.7255 0.9944 0.1651  -0.1096 0.2035  263 ASN D O   
8050  C CB  . ASN D 263 ? 0.7568 0.7806 1.0287 0.1733  -0.1067 0.2376  263 ASN D CB  
8051  C CG  . ASN D 263 ? 0.7740 0.7954 1.0668 0.1822  -0.0897 0.2534  263 ASN D CG  
8052  O OD1 . ASN D 263 ? 0.7796 0.7954 1.0931 0.1875  -0.0760 0.2569  263 ASN D OD1 
8053  N ND2 . ASN D 263 ? 0.7838 0.8093 1.0723 0.1837  -0.0895 0.2633  263 ASN D ND2 
8054  N N   . VAL D 264 ? 0.6223 0.6647 0.8762 0.1557  -0.1375 0.2117  264 VAL D N   
8055  C CA  . VAL D 264 ? 0.6100 0.6391 0.8500 0.1483  -0.1454 0.1935  264 VAL D CA  
8056  C C   . VAL D 264 ? 0.6058 0.6241 0.8584 0.1497  -0.1378 0.1872  264 VAL D C   
8057  O O   . VAL D 264 ? 0.6054 0.6410 0.8734 0.1515  -0.1372 0.1956  264 VAL D O   
8058  C CB  . VAL D 264 ? 0.6082 0.6604 0.8351 0.1381  -0.1650 0.1915  264 VAL D CB  
8059  C CG1 . VAL D 264 ? 0.6054 0.6456 0.8244 0.1307  -0.1722 0.1744  264 VAL D CG1 
8060  C CG2 . VAL D 264 ? 0.6158 0.6719 0.8259 0.1351  -0.1722 0.1933  264 VAL D CG2 
8061  N N   . THR D 265 ? 0.5617 0.5526 0.8084 0.1484  -0.1323 0.1726  265 THR D N   
8062  C CA  . THR D 265 ? 0.5638 0.5430 0.8201 0.1486  -0.1256 0.1654  265 THR D CA  
8063  C C   . THR D 265 ? 0.5637 0.5398 0.8079 0.1395  -0.1384 0.1512  265 THR D C   
8064  O O   . THR D 265 ? 0.5654 0.5412 0.8164 0.1378  -0.1361 0.1470  265 THR D O   
8065  C CB  . THR D 265 ? 0.5783 0.5280 0.8397 0.1532  -0.1076 0.1598  265 THR D CB  
8066  O OG1 . THR D 265 ? 0.5862 0.5191 0.8296 0.1488  -0.1106 0.1492  265 THR D OG1 
8067  C CG2 . THR D 265 ? 0.5788 0.5292 0.8558 0.1623  -0.0920 0.1736  265 THR D CG2 
8068  N N   . LEU D 266 ? 0.5191 0.4926 0.7418 0.1324  -0.1484 0.1417  266 LEU D N   
8069  C CA  . LEU D 266 ? 0.5197 0.4894 0.7265 0.1224  -0.1568 0.1263  266 LEU D CA  
8070  C C   . LEU D 266 ? 0.5179 0.5043 0.7133 0.1159  -0.1715 0.1262  266 LEU D C   
8071  O O   . LEU D 266 ? 0.5213 0.5098 0.7080 0.1164  -0.1742 0.1292  266 LEU D O   
8072  C CB  . LEU D 266 ? 0.5274 0.4728 0.7188 0.1190  -0.1512 0.1117  266 LEU D CB  
8073  C CG  . LEU D 266 ? 0.5253 0.4678 0.7005 0.1099  -0.1603 0.0988  266 LEU D CG  
8074  C CD1 . LEU D 266 ? 0.5243 0.4697 0.7047 0.1061  -0.1617 0.0948  266 LEU D CD1 
8075  C CD2 . LEU D 266 ? 0.5308 0.4546 0.6928 0.1074  -0.1560 0.0885  266 LEU D CD2 
8076  N N   . LEU D 267 ? 0.4772 0.4749 0.6719 0.1089  -0.1800 0.1222  267 LEU D N   
8077  C CA  . LEU D 267 ? 0.4798 0.4915 0.6621 0.0999  -0.1923 0.1188  267 LEU D CA  
8078  C C   . LEU D 267 ? 0.4760 0.4784 0.6493 0.0910  -0.1955 0.1037  267 LEU D C   
8079  O O   . LEU D 267 ? 0.4741 0.4859 0.6557 0.0872  -0.1986 0.1039  267 LEU D O   
8080  C CB  . LEU D 267 ? 0.4840 0.5266 0.6778 0.0988  -0.2004 0.1331  267 LEU D CB  
8081  C CG  . LEU D 267 ? 0.4908 0.5495 0.6691 0.0867  -0.2126 0.1284  267 LEU D CG  
8082  C CD1 . LEU D 267 ? 0.4963 0.5445 0.6555 0.0854  -0.2123 0.1227  267 LEU D CD1 
8083  C CD2 . LEU D 267 ? 0.4966 0.5907 0.6860 0.0845  -0.2213 0.1448  267 LEU D CD2 
8084  N N   . ASN D 268 ? 0.5286 0.5131 0.6868 0.0881  -0.1942 0.0920  268 ASN D N   
8085  C CA  . ASN D 268 ? 0.5370 0.5120 0.6877 0.0805  -0.1963 0.0794  268 ASN D CA  
8086  C C   . ASN D 268 ? 0.5609 0.5420 0.6986 0.0718  -0.2030 0.0731  268 ASN D C   
8087  O O   . ASN D 268 ? 0.5690 0.5455 0.6956 0.0722  -0.2024 0.0711  268 ASN D O   
8088  C CB  . ASN D 268 ? 0.5299 0.4830 0.6750 0.0828  -0.1895 0.0719  268 ASN D CB  
8089  C CG  . ASN D 268 ? 0.5183 0.4649 0.6729 0.0874  -0.1824 0.0743  268 ASN D CG  
8090  O OD1 . ASN D 268 ? 0.5164 0.4724 0.6828 0.0885  -0.1819 0.0798  268 ASN D OD1 
8091  N ND2 . ASN D 268 ? 0.5155 0.4471 0.6649 0.0890  -0.1764 0.0700  268 ASN D ND2 
8092  N N   . MET D 269 ? 0.5193 0.5106 0.6581 0.0630  -0.2085 0.0695  269 MET D N   
8093  C CA  . MET D 269 ? 0.5542 0.5481 0.6794 0.0519  -0.2127 0.0599  269 MET D CA  
8094  C C   . MET D 269 ? 0.5749 0.5606 0.7013 0.0436  -0.2121 0.0493  269 MET D C   
8095  O O   . MET D 269 ? 0.6104 0.6026 0.7295 0.0319  -0.2156 0.0416  269 MET D O   
8096  C CB  . MET D 269 ? 0.5666 0.5877 0.6892 0.0457  -0.2211 0.0668  269 MET D CB  
8097  C CG  . MET D 269 ? 0.5483 0.5803 0.6729 0.0545  -0.2216 0.0808  269 MET D CG  
8098  S SD  . MET D 269 ? 0.5705 0.6340 0.6846 0.0446  -0.2317 0.0874  269 MET D SD  
8099  C CE  . MET D 269 ? 0.5663 0.6579 0.6950 0.0369  -0.2401 0.0941  269 MET D CE  
8100  N N   . PHE D 270 ? 0.5562 0.5284 0.6915 0.0486  -0.2072 0.0489  270 PHE D N   
8101  C CA  . PHE D 270 ? 0.5734 0.5383 0.7129 0.0420  -0.2059 0.0419  270 PHE D CA  
8102  C C   . PHE D 270 ? 0.6085 0.5557 0.7384 0.0368  -0.2015 0.0299  270 PHE D C   
8103  O O   . PHE D 270 ? 0.6118 0.5505 0.7327 0.0399  -0.1988 0.0273  270 PHE D O   
8104  C CB  . PHE D 270 ? 0.5449 0.5020 0.6956 0.0488  -0.2015 0.0464  270 PHE D CB  
8105  C CG  . PHE D 270 ? 0.5233 0.4658 0.6709 0.0573  -0.1960 0.0475  270 PHE D CG  
8106  C CD1 . PHE D 270 ? 0.5275 0.4537 0.6719 0.0569  -0.1918 0.0419  270 PHE D CD1 
8107  C CD2 . PHE D 270 ? 0.5062 0.4521 0.6556 0.0652  -0.1943 0.0549  270 PHE D CD2 
8108  C CE1 . PHE D 270 ? 0.5104 0.4273 0.6525 0.0632  -0.1878 0.0438  270 PHE D CE1 
8109  C CE2 . PHE D 270 ? 0.4968 0.4302 0.6425 0.0707  -0.1891 0.0547  270 PHE D CE2 
8110  C CZ  . PHE D 270 ? 0.4982 0.4187 0.6398 0.0692  -0.1868 0.0492  270 PHE D CZ  
8111  N N   . GLU D 271 ? 0.6340 0.5751 0.7677 0.0289  -0.1997 0.0229  271 GLU D N   
8112  C CA  . GLU D 271 ? 0.6790 0.6014 0.8078 0.0236  -0.1930 0.0117  271 GLU D CA  
8113  C C   . GLU D 271 ? 0.7200 0.6441 0.8335 0.0167  -0.1931 0.0032  271 GLU D C   
8114  O O   . GLU D 271 ? 0.7306 0.6421 0.8375 0.0205  -0.1877 -0.0004 271 GLU D O   
8115  C CB  . GLU D 271 ? 0.6509 0.5556 0.7842 0.0335  -0.1863 0.0145  271 GLU D CB  
8116  C CG  . GLU D 271 ? 0.6124 0.5167 0.7579 0.0388  -0.1860 0.0227  271 GLU D CG  
8117  C CD  . GLU D 271 ? 0.6039 0.4916 0.7558 0.0423  -0.1789 0.0233  271 GLU D CD  
8118  O OE1 . GLU D 271 ? 0.6305 0.5054 0.7808 0.0401  -0.1731 0.0166  271 GLU D OE1 
8119  O OE2 . GLU D 271 ? 0.5712 0.4597 0.7303 0.0473  -0.1786 0.0312  271 GLU D OE2 
8120  N N   . ASN D 272 ? 0.6788 0.6211 0.7866 0.0057  -0.1994 0.0007  272 ASN D N   
8121  C CA  . ASN D 272 ? 0.7147 0.6623 0.8054 -0.0049 -0.2000 -0.0086 272 ASN D CA  
8122  C C   . ASN D 272 ? 0.7473 0.7009 0.8348 -0.0227 -0.2008 -0.0196 272 ASN D C   
8123  O O   . ASN D 272 ? 0.7491 0.6986 0.8487 -0.0253 -0.1995 -0.0203 272 ASN D O   
8124  C CB  . ASN D 272 ? 0.6838 0.6548 0.7679 -0.0019 -0.2087 0.0019  272 ASN D CB  
8125  C CG  . ASN D 272 ? 0.6716 0.6327 0.7499 0.0093  -0.2049 0.0052  272 ASN D CG  
8126  O OD1 . ASN D 272 ? 0.7069 0.6603 0.7714 0.0047  -0.2005 -0.0037 272 ASN D OD1 
8127  N ND2 . ASN D 272 ? 0.6213 0.5819 0.7100 0.0231  -0.2055 0.0174  272 ASN D ND2 
8128  N N   . GLN D 273 ? 0.7218 0.6854 0.7921 -0.0363 -0.2026 -0.0287 273 GLN D N   
8129  C CA  . GLN D 273 ? 0.7427 0.7163 0.8071 -0.0564 -0.2043 -0.0401 273 GLN D CA  
8130  C C   . GLN D 273 ? 0.7241 0.7359 0.7818 -0.0653 -0.2183 -0.0320 273 GLN D C   
8131  O O   . GLN D 273 ? 0.7453 0.7709 0.7888 -0.0850 -0.2208 -0.0427 273 GLN D O   
8132  C CB  . GLN D 273 ? 0.7849 0.7380 0.8337 -0.0694 -0.1926 -0.0606 273 GLN D CB  
8133  C CG  . GLN D 273 ? 0.7993 0.7163 0.8583 -0.0602 -0.1778 -0.0664 273 GLN D CG  
8134  C CD  . GLN D 273 ? 0.8310 0.7268 0.8818 -0.0760 -0.1640 -0.0875 273 GLN D CD  
8135  O OE1 . GLN D 273 ? 0.8389 0.7362 0.8910 -0.0913 -0.1627 -0.0967 273 GLN D OE1 
8136  N NE2 . GLN D 273 ? 0.8474 0.7229 0.8906 -0.0730 -0.1522 -0.0958 273 GLN D NE2 
8137  N N   . LEU D 274 ? 0.7347 0.7646 0.8032 -0.0514 -0.2266 -0.0126 274 LEU D N   
8138  C CA  . LEU D 274 ? 0.7122 0.7809 0.7801 -0.0567 -0.2397 0.0000  274 LEU D CA  
8139  C C   . LEU D 274 ? 0.7165 0.8046 0.7905 -0.0728 -0.2456 -0.0029 274 LEU D C   
8140  O O   . LEU D 274 ? 0.7184 0.7924 0.8058 -0.0722 -0.2411 -0.0068 274 LEU D O   
8141  C CB  . LEU D 274 ? 0.6639 0.7430 0.7484 -0.0369 -0.2440 0.0217  274 LEU D CB  
8142  C CG  . LEU D 274 ? 0.6514 0.7131 0.7323 -0.0209 -0.2384 0.0262  274 LEU D CG  
8143  C CD1 . LEU D 274 ? 0.6036 0.6641 0.7041 -0.0021 -0.2377 0.0426  274 LEU D CD1 
8144  C CD2 . LEU D 274 ? 0.6589 0.7391 0.7234 -0.0253 -0.2434 0.0303  274 LEU D CD2 
8145  N N   . SER D 275 ? 0.7055 0.8282 0.7698 -0.0880 -0.2560 -0.0003 275 SER D N   
8146  C CA  . SER D 275 ? 0.7116 0.8568 0.7785 -0.1075 -0.2624 -0.0048 275 SER D CA  
8147  C C   . SER D 275 ? 0.6780 0.8715 0.7532 -0.1089 -0.2778 0.0165  275 SER D C   
8148  O O   . SER D 275 ? 0.6519 0.8586 0.7311 -0.0943 -0.2821 0.0344  275 SER D O   
8149  C CB  . SER D 275 ? 0.7545 0.8934 0.7970 -0.1325 -0.2579 -0.0289 275 SER D CB  
8150  O OG  . SER D 275 ? 0.7599 0.9197 0.7806 -0.1410 -0.2636 -0.0282 275 SER D OG  
8151  N N   . GLY D 276 ? 0.7422 0.9630 0.8217 -0.1268 -0.2855 0.0154  276 GLY D N   
8152  C CA  . GLY D 276 ? 0.7089 0.9798 0.7996 -0.1295 -0.3004 0.0373  276 GLY D CA  
8153  C C   . GLY D 276 ? 0.6722 0.9498 0.7955 -0.1101 -0.3016 0.0576  276 GLY D C   
8154  O O   . GLY D 276 ? 0.6748 0.9231 0.8107 -0.1012 -0.2926 0.0519  276 GLY D O   
8155  N N   . GLU D 277 ? 0.7293 1.0467 0.8669 -0.1033 -0.3121 0.0827  277 GLU D N   
8156  C CA  . GLU D 277 ? 0.6929 1.0219 0.8631 -0.0856 -0.3125 0.1039  277 GLU D CA  
8157  C C   . GLU D 277 ? 0.6662 0.9880 0.8457 -0.0606 -0.3083 0.1219  277 GLU D C   
8158  O O   . GLU D 277 ? 0.6647 0.9979 0.8312 -0.0599 -0.3122 0.1285  277 GLU D O   
8159  C CB  . GLU D 277 ? 0.6709 1.0541 0.8573 -0.0971 -0.3263 0.1211  277 GLU D CB  
8160  C CG  . GLU D 277 ? 0.6964 1.0966 0.8666 -0.1278 -0.3332 0.1035  277 GLU D CG  
8161  C CD  . GLU D 277 ? 0.6733 1.1195 0.8661 -0.1373 -0.3435 0.1184  277 GLU D CD  
8162  O OE1 . GLU D 277 ? 0.6444 1.1140 0.8551 -0.1206 -0.3419 0.1423  277 GLU D OE1 
8163  O OE2 . GLU D 277 ? 0.6908 1.1399 0.8807 -0.1583 -0.3454 0.1029  277 GLU D OE2 
8164  N N   . ILE D 278 ? 0.5745 0.8768 0.7758 -0.0411 -0.2995 0.1292  278 ILE D N   
8165  C CA  . ILE D 278 ? 0.5608 0.8531 0.7732 -0.0179 -0.2931 0.1449  278 ILE D CA  
8166  C C   . ILE D 278 ? 0.5632 0.9011 0.7913 -0.0139 -0.3024 0.1724  278 ILE D C   
8167  O O   . ILE D 278 ? 0.5649 0.9290 0.8115 -0.0147 -0.3027 0.1835  278 ILE D O   
8168  C CB  . ILE D 278 ? 0.5428 0.8100 0.7761 -0.0011 -0.2816 0.1470  278 ILE D CB  
8169  C CG1 . ILE D 278 ? 0.5410 0.7654 0.7594 -0.0044 -0.2728 0.1227  278 ILE D CG1 
8170  C CG2 . ILE D 278 ? 0.5326 0.7915 0.7777 0.0207  -0.2739 0.1629  278 ILE D CG2 
8171  C CD1 . ILE D 278 ? 0.5268 0.7309 0.7629 0.0068  -0.2630 0.1229  278 ILE D CD1 
8172  N N   . PRO D 279 ? 0.6304 0.9709 0.8462 -0.0083 -0.3015 0.1794  279 PRO D N   
8173  C CA  . PRO D 279 ? 0.6189 0.9925 0.8414 -0.0040 -0.3005 0.1996  279 PRO D CA  
8174  C C   . PRO D 279 ? 0.6083 0.9809 0.8613 0.0163  -0.2881 0.2173  279 PRO D C   
8175  O O   . PRO D 279 ? 0.5949 0.9356 0.8563 0.0333  -0.2763 0.2170  279 PRO D O   
8176  C CB  . PRO D 279 ? 0.6255 0.9910 0.8287 0.0001  -0.2995 0.2013  279 PRO D CB  
8177  C CG  . PRO D 279 ? 0.6302 0.9528 0.8260 0.0068  -0.2951 0.1864  279 PRO D CG  
8178  C CD  . PRO D 279 ? 0.6470 0.9545 0.8404 -0.0048 -0.2967 0.1667  279 PRO D CD  
8179  N N   . PRO D 280 ? 0.6502 1.0565 0.9198 0.0142  -0.2897 0.2325  280 PRO D N   
8180  C CA  . PRO D 280 ? 0.6442 1.0499 0.9441 0.0327  -0.2768 0.2498  280 PRO D CA  
8181  C C   . PRO D 280 ? 0.6451 1.0361 0.9501 0.0512  -0.2646 0.2623  280 PRO D C   
8182  O O   . PRO D 280 ? 0.6393 1.0177 0.9671 0.0675  -0.2506 0.2718  280 PRO D O   
8183  C CB  . PRO D 280 ? 0.6589 1.1090 0.9721 0.0235  -0.2836 0.2649  280 PRO D CB  
8184  C CG  . PRO D 280 ? 0.6679 1.1355 0.9594 -0.0014 -0.2991 0.2495  280 PRO D CG  
8185  C CD  . PRO D 280 ? 0.6683 1.1145 0.9301 -0.0067 -0.3027 0.2339  280 PRO D CD  
8186  N N   . GLU D 281 ? 0.6893 1.0811 0.9737 0.0482  -0.2688 0.2621  281 GLU D N   
8187  C CA  . GLU D 281 ? 0.6915 1.0685 0.9790 0.0641  -0.2576 0.2729  281 GLU D CA  
8188  C C   . GLU D 281 ? 0.6754 1.0073 0.9638 0.0779  -0.2447 0.2618  281 GLU D C   
8189  O O   . GLU D 281 ? 0.6768 0.9928 0.9736 0.0925  -0.2318 0.2706  281 GLU D O   
8190  C CB  . GLU D 281 ? 0.7050 1.0936 0.9674 0.0553  -0.2663 0.2734  281 GLU D CB  
8191  C CG  . GLU D 281 ? 0.7246 1.1586 0.9796 0.0375  -0.2803 0.2815  281 GLU D CG  
8192  C CD  . GLU D 281 ? 0.7252 1.1689 0.9635 0.0161  -0.2936 0.2623  281 GLU D CD  
8193  O OE1 . GLU D 281 ? 0.7101 1.1358 0.9564 0.0170  -0.2915 0.2504  281 GLU D OE1 
8194  O OE2 . GLU D 281 ? 0.7426 1.2109 0.9593 -0.0026 -0.3053 0.2585  281 GLU D OE2 
8195  N N   . ILE D 282 ? 0.6377 0.9491 0.9188 0.0728  -0.2474 0.2431  282 ILE D N   
8196  C CA  . ILE D 282 ? 0.6243 0.8941 0.9055 0.0842  -0.2356 0.2323  282 ILE D CA  
8197  C C   . ILE D 282 ? 0.6217 0.8814 0.9289 0.1000  -0.2187 0.2427  282 ILE D C   
8198  O O   . ILE D 282 ? 0.6180 0.8477 0.9268 0.1118  -0.2052 0.2401  282 ILE D O   
8199  C CB  . ILE D 282 ? 0.6128 0.8660 0.8842 0.0744  -0.2427 0.2124  282 ILE D CB  
8200  C CG1 . ILE D 282 ? 0.6238 0.8690 0.8679 0.0634  -0.2535 0.1992  282 ILE D CG1 
8201  C CG2 . ILE D 282 ? 0.6023 0.8201 0.8830 0.0859  -0.2293 0.2049  282 ILE D CG2 
8202  C CD1 . ILE D 282 ? 0.6365 0.8543 0.8706 0.0566  -0.2566 0.1785  282 ILE D CD1 
8203  N N   . GLY D 283 ? 0.6316 0.9166 0.9599 0.0997  -0.2185 0.2547  283 GLY D N   
8204  C CA  . GLY D 283 ? 0.6323 0.9103 0.9872 0.1139  -0.2017 0.2660  283 GLY D CA  
8205  C C   . GLY D 283 ? 0.6431 0.9150 1.0054 0.1263  -0.1893 0.2797  283 GLY D C   
8206  O O   . GLY D 283 ? 0.6443 0.8997 1.0257 0.1387  -0.1720 0.2851  283 GLY D O   
8207  N N   . ASN D 284 ? 0.6727 0.9578 1.0208 0.1224  -0.1970 0.2856  284 ASN D N   
8208  C CA  . ASN D 284 ? 0.6832 0.9608 1.0371 0.1334  -0.1856 0.2982  284 ASN D CA  
8209  C C   . ASN D 284 ? 0.6765 0.9133 1.0165 0.1399  -0.1761 0.2842  284 ASN D C   
8210  O O   . ASN D 284 ? 0.6852 0.9108 1.0305 0.1491  -0.1646 0.2928  284 ASN D O   
8211  C CB  . ASN D 284 ? 0.6974 1.0063 1.0416 0.1261  -0.1974 0.3111  284 ASN D CB  
8212  C CG  . ASN D 284 ? 0.7127 1.0559 1.0823 0.1289  -0.1951 0.3363  284 ASN D CG  
8213  O OD1 . ASN D 284 ? 0.7176 1.0530 1.1124 0.1418  -0.1788 0.3488  284 ASN D OD1 
8214  N ND2 . ASN D 284 ? 0.7224 1.1045 1.0855 0.1158  -0.2111 0.3442  284 ASN D ND2 
8215  N N   . MET D 285 ? 0.6262 0.8413 0.9497 0.1348  -0.1804 0.2637  285 MET D N   
8216  C CA  . MET D 285 ? 0.6198 0.7965 0.9315 0.1401  -0.1712 0.2500  285 MET D CA  
8217  C C   . MET D 285 ? 0.6183 0.7712 0.9491 0.1507  -0.1523 0.2489  285 MET D C   
8218  O O   . MET D 285 ? 0.6079 0.7396 0.9359 0.1498  -0.1492 0.2344  285 MET D O   
8219  C CB  . MET D 285 ? 0.6077 0.7721 0.8970 0.1300  -0.1829 0.2303  285 MET D CB  
8220  C CG  . MET D 285 ? 0.6113 0.7935 0.8793 0.1189  -0.1995 0.2286  285 MET D CG  
8221  S SD  . MET D 285 ? 0.6010 0.7547 0.8433 0.1116  -0.2064 0.2061  285 MET D SD  
8222  C CE  . MET D 285 ? 0.6034 0.7748 0.8413 0.0957  -0.2231 0.1964  285 MET D CE  
8223  N N   . THR D 286 ? 0.5905 0.7470 0.9416 0.1603  -0.1389 0.2648  286 THR D N   
8224  C CA  . THR D 286 ? 0.5938 0.7334 0.9675 0.1698  -0.1193 0.2669  286 THR D CA  
8225  C C   . THR D 286 ? 0.5922 0.6911 0.9583 0.1744  -0.1051 0.2524  286 THR D C   
8226  O O   . THR D 286 ? 0.5985 0.6800 0.9820 0.1818  -0.0863 0.2530  286 THR D O   
8227  C CB  . THR D 286 ? 0.6106 0.7668 1.0099 0.1782  -0.1083 0.2895  286 THR D CB  
8228  O OG1 . THR D 286 ? 0.6205 0.7684 1.0136 0.1820  -0.1035 0.2951  286 THR D OG1 
8229  C CG2 . THR D 286 ? 0.6141 0.8134 1.0221 0.1726  -0.1226 0.3051  286 THR D CG2 
8230  N N   . ALA D 287 ? 0.5888 0.6721 0.9303 0.1697  -0.1122 0.2397  287 ALA D N   
8231  C CA  . ALA D 287 ? 0.5874 0.6340 0.9205 0.1719  -0.1004 0.2252  287 ALA D CA  
8232  C C   . ALA D 287 ? 0.5728 0.6061 0.8901 0.1643  -0.1089 0.2065  287 ALA D C   
8233  O O   . ALA D 287 ? 0.5724 0.5769 0.8821 0.1644  -0.1008 0.1939  287 ALA D O   
8234  C CB  . ALA D 287 ? 0.5935 0.6298 0.9132 0.1731  -0.0995 0.2260  287 ALA D CB  
8235  N N   . LEU D 288 ? 0.5869 0.6407 0.9000 0.1569  -0.1248 0.2048  288 LEU D N   
8236  C CA  . LEU D 288 ? 0.5769 0.6191 0.8751 0.1486  -0.1343 0.1880  288 LEU D CA  
8237  C C   . LEU D 288 ? 0.5826 0.6026 0.8899 0.1511  -0.1218 0.1794  288 LEU D C   
8238  O O   . LEU D 288 ? 0.5829 0.6093 0.9103 0.1557  -0.1127 0.1862  288 LEU D O   
8239  C CB  . LEU D 288 ? 0.5708 0.6396 0.8663 0.1396  -0.1519 0.1888  288 LEU D CB  
8240  C CG  . LEU D 288 ? 0.5713 0.6536 0.8475 0.1311  -0.1687 0.1869  288 LEU D CG  
8241  C CD1 . LEU D 288 ? 0.5695 0.6782 0.8460 0.1208  -0.1843 0.1874  288 LEU D CD1 
8242  C CD2 . LEU D 288 ? 0.5751 0.6311 0.8309 0.1273  -0.1714 0.1709  288 LEU D CD2 
8243  N N   . ASP D 289 ? 0.5462 0.5410 0.8391 0.1476  -0.1215 0.1645  289 ASP D N   
8244  C CA  . ASP D 289 ? 0.5628 0.5376 0.8551 0.1453  -0.1117 0.1518  289 ASP D CA  
8245  C C   . ASP D 289 ? 0.5637 0.5409 0.8391 0.1340  -0.1240 0.1386  289 ASP D C   
8246  O O   . ASP D 289 ? 0.5720 0.5486 0.8528 0.1317  -0.1198 0.1344  289 ASP D O   
8247  C CB  . ASP D 289 ? 0.5820 0.5278 0.8618 0.1449  -0.0988 0.1405  289 ASP D CB  
8248  C CG  . ASP D 289 ? 0.6045 0.5327 0.8692 0.1361  -0.0936 0.1223  289 ASP D CG  
8249  O OD1 . ASP D 289 ? 0.6221 0.5432 0.8975 0.1376  -0.0797 0.1205  289 ASP D OD1 
8250  O OD2 . ASP D 289 ? 0.6056 0.5282 0.8483 0.1277  -0.1032 0.1107  289 ASP D OD2 
8251  N N   . THR D 290 ? 0.5187 0.4983 0.7749 0.1272  -0.1379 0.1323  290 THR D N   
8252  C CA  . THR D 290 ? 0.5177 0.4986 0.7596 0.1171  -0.1487 0.1209  290 THR D CA  
8253  C C   . THR D 290 ? 0.5075 0.5078 0.7443 0.1124  -0.1644 0.1246  290 THR D C   
8254  O O   . THR D 290 ? 0.5048 0.5073 0.7347 0.1139  -0.1680 0.1280  290 THR D O   
8255  C CB  . THR D 290 ? 0.5262 0.4848 0.7474 0.1117  -0.1466 0.1058  290 THR D CB  
8256  O OG1 . THR D 290 ? 0.5447 0.4884 0.7679 0.1122  -0.1331 0.1004  290 THR D OG1 
8257  C CG2 . THR D 290 ? 0.5217 0.4824 0.7303 0.1025  -0.1579 0.0969  290 THR D CG2 
8258  N N   . LEU D 291 ? 0.5090 0.5233 0.7485 0.1057  -0.1728 0.1235  291 LEU D N   
8259  C CA  . LEU D 291 ? 0.5094 0.5417 0.7420 0.0979  -0.1869 0.1239  291 LEU D CA  
8260  C C   . LEU D 291 ? 0.5179 0.5430 0.7393 0.0875  -0.1919 0.1101  291 LEU D C   
8261  O O   . LEU D 291 ? 0.5199 0.5468 0.7504 0.0855  -0.1899 0.1092  291 LEU D O   
8262  C CB  . LEU D 291 ? 0.5044 0.5675 0.7562 0.0991  -0.1923 0.1397  291 LEU D CB  
8263  C CG  . LEU D 291 ? 0.5124 0.5976 0.7563 0.0874  -0.2071 0.1388  291 LEU D CG  
8264  C CD1 . LEU D 291 ? 0.5185 0.6034 0.7446 0.0850  -0.2124 0.1371  291 LEU D CD1 
8265  C CD2 . LEU D 291 ? 0.5057 0.6253 0.7710 0.0871  -0.2129 0.1553  291 LEU D CD2 
8266  N N   . SER D 292 ? 0.5006 0.5174 0.7039 0.0812  -0.1972 0.1002  292 SER D N   
8267  C CA  . SER D 292 ? 0.5116 0.5177 0.7056 0.0725  -0.1995 0.0876  292 SER D CA  
8268  C C   . SER D 292 ? 0.5314 0.5455 0.7141 0.0626  -0.2083 0.0819  292 SER D C   
8269  O O   . SER D 292 ? 0.5372 0.5462 0.7071 0.0625  -0.2094 0.0787  292 SER D O   
8270  C CB  . SER D 292 ? 0.5076 0.4891 0.6914 0.0750  -0.1928 0.0793  292 SER D CB  
8271  O OG  . SER D 292 ? 0.5184 0.4906 0.6961 0.0678  -0.1945 0.0699  292 SER D OG  
8272  N N   . LEU D 293 ? 0.5010 0.5274 0.6879 0.0533  -0.2137 0.0797  293 LEU D N   
8273  C CA  . LEU D 293 ? 0.5305 0.5638 0.7059 0.0407  -0.2206 0.0715  293 LEU D CA  
8274  C C   . LEU D 293 ? 0.5543 0.5763 0.7289 0.0315  -0.2192 0.0602  293 LEU D C   
8275  O O   . LEU D 293 ? 0.5820 0.6148 0.7542 0.0188  -0.2242 0.0548  293 LEU D O   
8276  C CB  . LEU D 293 ? 0.5333 0.5988 0.7142 0.0351  -0.2296 0.0810  293 LEU D CB  
8277  C CG  . LEU D 293 ? 0.5106 0.5919 0.6980 0.0452  -0.2307 0.0969  293 LEU D CG  
8278  C CD1 . LEU D 293 ? 0.5035 0.6198 0.7069 0.0425  -0.2382 0.1115  293 LEU D CD1 
8279  C CD2 . LEU D 293 ? 0.5220 0.6014 0.6915 0.0436  -0.2329 0.0942  293 LEU D CD2 
8280  N N   . HIS D 294 ? 0.5467 0.5478 0.7236 0.0367  -0.2121 0.0571  294 HIS D N   
8281  C CA  . HIS D 294 ? 0.5681 0.5591 0.7480 0.0296  -0.2096 0.0498  294 HIS D CA  
8282  C C   . HIS D 294 ? 0.6057 0.5805 0.7733 0.0223  -0.2076 0.0373  294 HIS D C   
8283  O O   . HIS D 294 ? 0.6092 0.5768 0.7655 0.0247  -0.2066 0.0340  294 HIS D O   
8284  C CB  . HIS D 294 ? 0.5456 0.5237 0.7327 0.0374  -0.2029 0.0533  294 HIS D CB  
8285  C CG  . HIS D 294 ? 0.5349 0.4930 0.7134 0.0434  -0.1977 0.0502  294 HIS D CG  
8286  N ND1 . HIS D 294 ? 0.5547 0.4966 0.7288 0.0398  -0.1946 0.0430  294 HIS D ND1 
8287  C CD2 . HIS D 294 ? 0.5082 0.4609 0.6835 0.0523  -0.1945 0.0541  294 HIS D CD2 
8288  C CE1 . HIS D 294 ? 0.5350 0.4650 0.7040 0.0465  -0.1908 0.0439  294 HIS D CE1 
8289  N NE2 . HIS D 294 ? 0.5084 0.4446 0.6769 0.0533  -0.1910 0.0497  294 HIS D NE2 
8290  N N   . THR D 295 ? 0.5860 0.5543 0.7572 0.0131  -0.2055 0.0303  295 THR D N   
8291  C CA  . THR D 295 ? 0.6352 0.5861 0.7982 0.0051  -0.2007 0.0178  295 THR D CA  
8292  C C   . THR D 295 ? 0.6605 0.6201 0.8092 -0.0034 -0.2045 0.0104  295 THR D C   
8293  O O   . THR D 295 ? 0.6740 0.6221 0.8117 -0.0011 -0.2011 0.0053  295 THR D O   
8294  C CB  . THR D 295 ? 0.6268 0.5546 0.7888 0.0144  -0.1929 0.0175  295 THR D CB  
8295  O OG1 . THR D 295 ? 0.5869 0.5123 0.7594 0.0223  -0.1910 0.0265  295 THR D OG1 
8296  C CG2 . THR D 295 ? 0.6834 0.5915 0.8446 0.0072  -0.1850 0.0068  295 THR D CG2 
8297  N N   . ASN D 296 ? 0.6570 0.6394 0.8058 -0.0141 -0.2119 0.0105  296 ASN D N   
8298  C CA  . ASN D 296 ? 0.6752 0.6717 0.8093 -0.0254 -0.2169 0.0042  296 ASN D CA  
8299  C C   . ASN D 296 ? 0.7012 0.7084 0.8351 -0.0444 -0.2193 -0.0049 296 ASN D C   
8300  O O   . ASN D 296 ? 0.7107 0.7091 0.8559 -0.0477 -0.2153 -0.0075 296 ASN D O   
8301  C CB  . ASN D 296 ? 0.6369 0.6593 0.7707 -0.0187 -0.2258 0.0181  296 ASN D CB  
8302  C CG  . ASN D 296 ? 0.6258 0.6374 0.7501 -0.0074 -0.2229 0.0205  296 ASN D CG  
8303  O OD1 . ASN D 296 ? 0.6479 0.6613 0.7565 -0.0135 -0.2236 0.0143  296 ASN D OD1 
8304  N ND2 . ASN D 296 ? 0.5909 0.5913 0.7242 0.0079  -0.2190 0.0288  296 ASN D ND2 
8305  N N   . LYS D 297 ? 0.6656 0.6926 0.7861 -0.0582 -0.2256 -0.0099 297 LYS D N   
8306  C CA  . LYS D 297 ? 0.6855 0.7264 0.8031 -0.0796 -0.2286 -0.0198 297 LYS D CA  
8307  C C   . LYS D 297 ? 0.6597 0.7437 0.7808 -0.0855 -0.2429 -0.0070 297 LYS D C   
8308  O O   . LYS D 297 ? 0.6735 0.7792 0.7832 -0.1050 -0.2490 -0.0139 297 LYS D O   
8309  C CB  . LYS D 297 ? 0.7255 0.7517 0.8225 -0.0959 -0.2217 -0.0403 297 LYS D CB  
8310  C CG  . LYS D 297 ? 0.7514 0.7367 0.8518 -0.0931 -0.2059 -0.0527 297 LYS D CG  
8311  C CD  . LYS D 297 ? 0.7872 0.7546 0.8693 -0.1085 -0.1957 -0.0738 297 LYS D CD  
8312  C CE  . LYS D 297 ? 0.8039 0.7307 0.8946 -0.1023 -0.1786 -0.0822 297 LYS D CE  
8313  N NZ  . LYS D 297 ? 0.8318 0.7367 0.9064 -0.1110 -0.1657 -0.1003 297 LYS D NZ  
8314  N N   . LEU D 298 ? 0.6970 0.7944 0.8350 -0.0691 -0.2476 0.0121  298 LEU D N   
8315  C CA  . LEU D 298 ? 0.6683 0.8070 0.8154 -0.0707 -0.2598 0.0286  298 LEU D CA  
8316  C C   . LEU D 298 ? 0.6708 0.8290 0.8307 -0.0846 -0.2642 0.0281  298 LEU D C   
8317  O O   . LEU D 298 ? 0.6821 0.8200 0.8509 -0.0853 -0.2571 0.0212  298 LEU D O   
8318  C CB  . LEU D 298 ? 0.6261 0.7683 0.7899 -0.0478 -0.2597 0.0485  298 LEU D CB  
8319  C CG  . LEU D 298 ? 0.6088 0.7537 0.7648 -0.0358 -0.2609 0.0578  298 LEU D CG  
8320  C CD1 . LEU D 298 ? 0.6398 0.7612 0.7721 -0.0405 -0.2558 0.0420  298 LEU D CD1 
8321  C CD2 . LEU D 298 ? 0.5741 0.7050 0.7452 -0.0139 -0.2545 0.0698  298 LEU D CD2 
8322  N N   . THR D 299 ? 0.7029 0.9026 0.8643 -0.0964 -0.2764 0.0367  299 THR D N   
8323  C CA  . THR D 299 ? 0.7018 0.9268 0.8760 -0.1115 -0.2823 0.0378  299 THR D CA  
8324  C C   . THR D 299 ? 0.6630 0.9342 0.8558 -0.1061 -0.2943 0.0628  299 THR D C   
8325  O O   . THR D 299 ? 0.6404 0.9234 0.8341 -0.0926 -0.2976 0.0779  299 THR D O   
8326  C CB  . THR D 299 ? 0.7354 0.9673 0.8897 -0.1404 -0.2848 0.0179  299 THR D CB  
8327  O OG1 . THR D 299 ? 0.7373 0.9887 0.8708 -0.1482 -0.2919 0.0181  299 THR D OG1 
8328  C CG2 . THR D 299 ? 0.7738 0.9587 0.9170 -0.1455 -0.2702 -0.0057 299 THR D CG2 
8329  N N   . GLY D 300 ? 0.6801 0.9781 0.8899 -0.1166 -0.3000 0.0680  300 GLY D N   
8330  C CA  . GLY D 300 ? 0.6432 0.9877 0.8757 -0.1120 -0.3105 0.0931  300 GLY D CA  
8331  C C   . GLY D 300 ? 0.6166 0.9527 0.8772 -0.0885 -0.3034 0.1089  300 GLY D C   
8332  O O   . GLY D 300 ? 0.6256 0.9212 0.8859 -0.0770 -0.2913 0.1000  300 GLY D O   
8333  N N   . PRO D 301 ? 0.5981 0.9734 0.8840 -0.0811 -0.3100 0.1332  301 PRO D N   
8334  C CA  . PRO D 301 ? 0.5739 0.9422 0.8877 -0.0594 -0.3013 0.1480  301 PRO D CA  
8335  C C   . PRO D 301 ? 0.5570 0.9037 0.8706 -0.0358 -0.2931 0.1566  301 PRO D C   
8336  O O   . PRO D 301 ? 0.5573 0.9041 0.8543 -0.0346 -0.2965 0.1573  301 PRO D O   
8337  C CB  . PRO D 301 ? 0.5463 0.9683 0.8883 -0.0620 -0.3112 0.1716  301 PRO D CB  
8338  C CG  . PRO D 301 ? 0.5485 0.9972 0.8706 -0.0729 -0.3192 0.1738  301 PRO D CG  
8339  C CD  . PRO D 301 ? 0.5808 1.0110 0.8721 -0.0933 -0.3253 0.1491  301 PRO D CD  
8340  N N   . ILE D 302 ? 0.5164 0.8444 0.8482 -0.0181 -0.2815 0.1626  302 ILE D N   
8341  C CA  . ILE D 302 ? 0.5065 0.8162 0.8420 0.0038  -0.2723 0.1719  302 ILE D CA  
8342  C C   . ILE D 302 ? 0.5086 0.8545 0.8619 0.0126  -0.2748 0.1965  302 ILE D C   
8343  O O   . ILE D 302 ? 0.5121 0.8854 0.8852 0.0118  -0.2738 0.2085  302 ILE D O   
8344  C CB  . ILE D 302 ? 0.4946 0.7753 0.8426 0.0177  -0.2575 0.1698  302 ILE D CB  
8345  C CG1 . ILE D 302 ? 0.5045 0.7482 0.8321 0.0095  -0.2526 0.1463  302 ILE D CG1 
8346  C CG2 . ILE D 302 ? 0.4874 0.7504 0.8399 0.0382  -0.2468 0.1786  302 ILE D CG2 
8347  C CD1 . ILE D 302 ? 0.4980 0.7184 0.8364 0.0192  -0.2397 0.1442  302 ILE D CD1 
8348  N N   . PRO D 303 ? 0.5402 0.8809 0.8811 0.0210  -0.2722 0.2012  303 PRO D N   
8349  C CA  . PRO D 303 ? 0.5351 0.9025 0.8860 0.0290  -0.2683 0.2211  303 PRO D CA  
8350  C C   . PRO D 303 ? 0.5291 0.8906 0.9075 0.0478  -0.2523 0.2348  303 PRO D C   
8351  O O   . PRO D 303 ? 0.5195 0.8479 0.9002 0.0614  -0.2400 0.2307  303 PRO D O   
8352  C CB  . PRO D 303 ? 0.5395 0.8946 0.8701 0.0339  -0.2679 0.2203  303 PRO D CB  
8353  C CG  . PRO D 303 ? 0.5358 0.8503 0.8532 0.0367  -0.2652 0.2031  303 PRO D CG  
8354  C CD  . PRO D 303 ? 0.5502 0.8610 0.8682 0.0229  -0.2728 0.1892  303 PRO D CD  
8355  N N   . SER D 304 ? 0.5511 0.9452 0.9503 0.0474  -0.2520 0.2508  304 SER D N   
8356  C CA  . SER D 304 ? 0.5489 0.9405 0.9765 0.0641  -0.2361 0.2651  304 SER D CA  
8357  C C   . SER D 304 ? 0.5529 0.9282 0.9829 0.0814  -0.2227 0.2748  304 SER D C   
8358  O O   . SER D 304 ? 0.5512 0.9134 1.0018 0.0961  -0.2062 0.2825  304 SER D O   
8359  C CB  . SER D 304 ? 0.5593 0.9921 1.0089 0.0590  -0.2396 0.2819  304 SER D CB  
8360  O OG  . SER D 304 ? 0.5753 1.0382 1.0172 0.0522  -0.2490 0.2931  304 SER D OG  
8361  N N   . THR D 305 ? 0.5624 0.9379 0.9721 0.0791  -0.2286 0.2742  305 THR D N   
8362  C CA  . THR D 305 ? 0.5676 0.9279 0.9788 0.0940  -0.2164 0.2832  305 THR D CA  
8363  C C   . THR D 305 ? 0.5563 0.8716 0.9614 0.1049  -0.2034 0.2700  305 THR D C   
8364  O O   . THR D 305 ? 0.5608 0.8598 0.9707 0.1178  -0.1900 0.2765  305 THR D O   
8365  C CB  . THR D 305 ? 0.5783 0.9529 0.9686 0.0869  -0.2273 0.2860  305 THR D CB  
8366  O OG1 . THR D 305 ? 0.5713 0.9312 0.9333 0.0755  -0.2382 0.2656  305 THR D OG1 
8367  C CG2 . THR D 305 ? 0.5930 1.0139 0.9897 0.0755  -0.2390 0.3005  305 THR D CG2 
8368  N N   . LEU D 306 ? 0.5621 0.8575 0.9573 0.0993  -0.2067 0.2521  306 LEU D N   
8369  C CA  . LEU D 306 ? 0.5530 0.8072 0.9410 0.1080  -0.1953 0.2395  306 LEU D CA  
8370  C C   . LEU D 306 ? 0.5541 0.7942 0.9655 0.1225  -0.1752 0.2467  306 LEU D C   
8371  O O   . LEU D 306 ? 0.5525 0.7609 0.9594 0.1313  -0.1625 0.2399  306 LEU D O   
8372  C CB  . LEU D 306 ? 0.5421 0.7807 0.9179 0.0981  -0.2035 0.2211  306 LEU D CB  
8373  C CG  . LEU D 306 ? 0.5454 0.7855 0.8956 0.0839  -0.2204 0.2090  306 LEU D CG  
8374  C CD1 . LEU D 306 ? 0.5551 0.7644 0.8939 0.0801  -0.2220 0.1906  306 LEU D CD1 
8375  C CD2 . LEU D 306 ? 0.5488 0.7865 0.8827 0.0869  -0.2212 0.2118  306 LEU D CD2 
8376  N N   . GLY D 307 ? 0.5470 0.8102 0.9837 0.1245  -0.1712 0.2599  307 GLY D N   
8377  C CA  . GLY D 307 ? 0.5510 0.8024 1.0120 0.1381  -0.1505 0.2677  307 GLY D CA  
8378  C C   . GLY D 307 ? 0.5633 0.8064 1.0306 0.1499  -0.1369 0.2788  307 GLY D C   
8379  O O   . GLY D 307 ? 0.5684 0.7928 1.0524 0.1611  -0.1169 0.2815  307 GLY D O   
8380  N N   . ASN D 308 ? 0.5852 0.8416 1.0401 0.1471  -0.1462 0.2851  308 ASN D N   
8381  C CA  . ASN D 308 ? 0.5981 0.8475 1.0598 0.1577  -0.1336 0.2968  308 ASN D CA  
8382  C C   . ASN D 308 ? 0.5951 0.8036 1.0414 0.1635  -0.1228 0.2826  308 ASN D C   
8383  O O   . ASN D 308 ? 0.6061 0.8004 1.0632 0.1737  -0.1061 0.2898  308 ASN D O   
8384  C CB  . ASN D 308 ? 0.6071 0.8854 1.0604 0.1521  -0.1475 0.3090  308 ASN D CB  
8385  C CG  . ASN D 308 ? 0.6162 0.9371 1.0898 0.1481  -0.1543 0.3282  308 ASN D CG  
8386  O OD1 . ASN D 308 ? 0.6155 0.9442 1.1118 0.1507  -0.1477 0.3336  308 ASN D OD1 
8387  N ND2 . ASN D 308 ? 0.6259 0.9758 1.0917 0.1411  -0.1674 0.3391  308 ASN D ND2 
8388  N N   . ILE D 309 ? 0.5725 0.7620 0.9951 0.1565  -0.1312 0.2631  309 ILE D N   
8389  C CA  . ILE D 309 ? 0.5701 0.7229 0.9769 0.1604  -0.1225 0.2495  309 ILE D CA  
8390  C C   . ILE D 309 ? 0.5697 0.6964 0.9893 0.1669  -0.1041 0.2424  309 ILE D C   
8391  O O   . ILE D 309 ? 0.5594 0.6758 0.9733 0.1620  -0.1074 0.2296  309 ILE D O   
8392  C CB  . ILE D 309 ? 0.5587 0.7029 0.9361 0.1499  -0.1389 0.2329  309 ILE D CB  
8393  C CG1 . ILE D 309 ? 0.5606 0.7352 0.9268 0.1409  -0.1576 0.2391  309 ILE D CG1 
8394  C CG2 . ILE D 309 ? 0.5588 0.6692 0.9198 0.1535  -0.1310 0.2217  309 ILE D CG2 
8395  C CD1 . ILE D 309 ? 0.5508 0.7221 0.8929 0.1286  -0.1741 0.2233  309 ILE D CD1 
8396  N N   . LYS D 310 ? 0.5500 0.6660 0.9879 0.1775  -0.0838 0.2510  310 LYS D N   
8397  C CA  . LYS D 310 ? 0.5542 0.6460 1.0062 0.1835  -0.0631 0.2449  310 LYS D CA  
8398  C C   . LYS D 310 ? 0.5522 0.6063 0.9855 0.1826  -0.0558 0.2260  310 LYS D C   
8399  O O   . LYS D 310 ? 0.5561 0.5887 0.9967 0.1850  -0.0402 0.2174  310 LYS D O   
8400  C CB  . LYS D 310 ? 0.5725 0.6652 1.0519 0.1942  -0.0419 0.2604  310 LYS D CB  
8401  C CG  . LYS D 310 ? 0.5775 0.7090 1.0788 0.1956  -0.0478 0.2820  310 LYS D CG  
8402  C CD  . LYS D 310 ? 0.5664 0.7190 1.0746 0.1897  -0.0586 0.2814  310 LYS D CD  
8403  C CE  . LYS D 310 ? 0.5762 0.7626 1.1140 0.1931  -0.0564 0.3039  310 LYS D CE  
8404  N NZ  . LYS D 310 ? 0.5665 0.7765 1.1122 0.1865  -0.0675 0.3045  310 LYS D NZ  
8405  N N   . THR D 311 ? 0.5542 0.6003 0.9641 0.1787  -0.0660 0.2196  311 THR D N   
8406  C CA  . THR D 311 ? 0.5537 0.5669 0.9451 0.1764  -0.0614 0.2023  311 THR D CA  
8407  C C   . THR D 311 ? 0.5528 0.5637 0.9251 0.1665  -0.0787 0.1884  311 THR D C   
8408  O O   . THR D 311 ? 0.5705 0.5553 0.9305 0.1638  -0.0752 0.1742  311 THR D O   
8409  C CB  . THR D 311 ? 0.5587 0.5631 0.9369 0.1777  -0.0615 0.2035  311 THR D CB  
8410  O OG1 . THR D 311 ? 0.5518 0.5827 0.9194 0.1733  -0.0816 0.2109  311 THR D OG1 
8411  C CG2 . THR D 311 ? 0.5765 0.5747 0.9739 0.1871  -0.0407 0.2148  311 THR D CG2 
8412  N N   . LEU D 312 ? 0.5461 0.5836 0.9165 0.1604  -0.0968 0.1922  312 LEU D N   
8413  C CA  . LEU D 312 ? 0.5482 0.5840 0.9000 0.1501  -0.1139 0.1795  312 LEU D CA  
8414  C C   . LEU D 312 ? 0.5683 0.5865 0.9165 0.1458  -0.1056 0.1655  312 LEU D C   
8415  O O   . LEU D 312 ? 0.5710 0.5987 0.9378 0.1479  -0.0996 0.1706  312 LEU D O   
8416  C CB  . LEU D 312 ? 0.5338 0.6018 0.8854 0.1430  -0.1320 0.1860  312 LEU D CB  
8417  C CG  . LEU D 312 ? 0.5361 0.6043 0.8697 0.1310  -0.1492 0.1732  312 LEU D CG  
8418  C CD1 . LEU D 312 ? 0.5374 0.5923 0.8446 0.1264  -0.1564 0.1633  312 LEU D CD1 
8419  C CD2 . LEU D 312 ? 0.5277 0.6288 0.8688 0.1241  -0.1633 0.1811  312 LEU D CD2 
8420  N N   . ALA D 313 ? 0.5127 0.5067 0.8349 0.1387  -0.1043 0.1475  313 ALA D N   
8421  C CA  . ALA D 313 ? 0.5364 0.5144 0.8493 0.1325  -0.0959 0.1334  313 ALA D CA  
8422  C C   . ALA D 313 ? 0.5352 0.5153 0.8282 0.1209  -0.1105 0.1224  313 ALA D C   
8423  O O   . ALA D 313 ? 0.5498 0.5276 0.8417 0.1160  -0.1071 0.1164  313 ALA D O   
8424  C CB  . ALA D 313 ? 0.5622 0.5120 0.8624 0.1320  -0.0804 0.1219  313 ALA D CB  
8425  N N   . VAL D 314 ? 0.5278 0.5109 0.8057 0.1166  -0.1251 0.1198  314 VAL D N   
8426  C CA  . VAL D 314 ? 0.5240 0.5078 0.7857 0.1066  -0.1376 0.1104  314 VAL D CA  
8427  C C   . VAL D 314 ? 0.5099 0.5156 0.7758 0.1040  -0.1528 0.1173  314 VAL D C   
8428  O O   . VAL D 314 ? 0.5036 0.5176 0.7709 0.1077  -0.1573 0.1245  314 VAL D O   
8429  C CB  . VAL D 314 ? 0.5274 0.4923 0.7658 0.1021  -0.1390 0.0986  314 VAL D CB  
8430  C CG1 . VAL D 314 ? 0.5233 0.4880 0.7491 0.0930  -0.1495 0.0909  314 VAL D CG1 
8431  C CG2 . VAL D 314 ? 0.5509 0.4971 0.7842 0.1026  -0.1241 0.0919  314 VAL D CG2 
8432  N N   . LEU D 315 ? 0.5007 0.5164 0.7682 0.0967  -0.1601 0.1151  315 LEU D N   
8433  C CA  . LEU D 315 ? 0.4938 0.5301 0.7628 0.0906  -0.1742 0.1186  315 LEU D CA  
8434  C C   . LEU D 315 ? 0.5024 0.5318 0.7584 0.0798  -0.1806 0.1068  315 LEU D C   
8435  O O   . LEU D 315 ? 0.5100 0.5400 0.7726 0.0764  -0.1780 0.1052  315 LEU D O   
8436  C CB  . LEU D 315 ? 0.4896 0.5526 0.7829 0.0929  -0.1755 0.1325  315 LEU D CB  
8437  C CG  . LEU D 315 ? 0.4879 0.5768 0.7827 0.0840  -0.1905 0.1364  315 LEU D CG  
8438  C CD1 . LEU D 315 ? 0.4845 0.5764 0.7657 0.0832  -0.1981 0.1369  315 LEU D CD1 
8439  C CD2 . LEU D 315 ? 0.4804 0.5995 0.8021 0.0870  -0.1916 0.1529  315 LEU D CD2 
8440  N N   . HIS D 316 ? 0.5065 0.5289 0.7456 0.0746  -0.1876 0.0991  316 HIS D N   
8441  C CA  . HIS D 316 ? 0.5184 0.5322 0.7469 0.0650  -0.1921 0.0885  316 HIS D CA  
8442  C C   . HIS D 316 ? 0.5304 0.5596 0.7562 0.0561  -0.2027 0.0872  316 HIS D C   
8443  O O   . HIS D 316 ? 0.5334 0.5616 0.7474 0.0548  -0.2068 0.0844  316 HIS D O   
8444  C CB  . HIS D 316 ? 0.5170 0.5079 0.7290 0.0659  -0.1889 0.0798  316 HIS D CB  
8445  C CG  . HIS D 316 ? 0.5137 0.4912 0.7253 0.0706  -0.1794 0.0792  316 HIS D CG  
8446  N ND1 . HIS D 316 ? 0.5119 0.4726 0.7105 0.0712  -0.1763 0.0735  316 HIS D ND1 
8447  C CD2 . HIS D 316 ? 0.5176 0.4973 0.7395 0.0737  -0.1718 0.0834  316 HIS D CD2 
8448  C CE1 . HIS D 316 ? 0.5177 0.4720 0.7169 0.0731  -0.1681 0.0737  316 HIS D CE1 
8449  N NE2 . HIS D 316 ? 0.5234 0.4876 0.7361 0.0747  -0.1644 0.0789  316 HIS D NE2 
8450  N N   . LEU D 317 ? 0.4813 0.5259 0.7175 0.0487  -0.2067 0.0887  317 LEU D N   
8451  C CA  . LEU D 317 ? 0.4895 0.5492 0.7218 0.0364  -0.2162 0.0851  317 LEU D CA  
8452  C C   . LEU D 317 ? 0.4954 0.5446 0.7244 0.0253  -0.2160 0.0741  317 LEU D C   
8453  O O   . LEU D 317 ? 0.5180 0.5801 0.7462 0.0127  -0.2223 0.0698  317 LEU D O   
8454  C CB  . LEU D 317 ? 0.4905 0.5833 0.7395 0.0348  -0.2224 0.0978  317 LEU D CB  
8455  C CG  . LEU D 317 ? 0.4878 0.5958 0.7453 0.0459  -0.2225 0.1125  317 LEU D CG  
8456  C CD1 . LEU D 317 ? 0.4907 0.6362 0.7660 0.0423  -0.2304 0.1266  317 LEU D CD1 
8457  C CD2 . LEU D 317 ? 0.4918 0.5921 0.7310 0.0467  -0.2251 0.1088  317 LEU D CD2 
8458  N N   . TYR D 318 ? 0.5442 0.5711 0.7713 0.0287  -0.2086 0.0696  318 TYR D N   
8459  C CA  . TYR D 318 ? 0.5709 0.5880 0.7989 0.0197  -0.2068 0.0622  318 TYR D CA  
8460  C C   . TYR D 318 ? 0.6038 0.6079 0.8181 0.0110  -0.2080 0.0502  318 TYR D C   
8461  O O   . TYR D 318 ? 0.6026 0.6026 0.8049 0.0132  -0.2095 0.0472  318 TYR D O   
8462  C CB  . TYR D 318 ? 0.5605 0.5604 0.7908 0.0261  -0.1986 0.0637  318 TYR D CB  
8463  C CG  . TYR D 318 ? 0.5460 0.5267 0.7641 0.0336  -0.1946 0.0613  318 TYR D CG  
8464  C CD1 . TYR D 318 ? 0.5441 0.5069 0.7543 0.0304  -0.1925 0.0543  318 TYR D CD1 
8465  C CD2 . TYR D 318 ? 0.5375 0.5183 0.7538 0.0435  -0.1917 0.0665  318 TYR D CD2 
8466  C CE1 . TYR D 318 ? 0.5299 0.4786 0.7311 0.0369  -0.1892 0.0537  318 TYR D CE1 
8467  C CE2 . TYR D 318 ? 0.5235 0.4888 0.7289 0.0486  -0.1883 0.0642  318 TYR D CE2 
8468  C CZ  . TYR D 318 ? 0.5180 0.4688 0.7161 0.0453  -0.1878 0.0583  318 TYR D CZ  
8469  O OH  . TYR D 318 ? 0.5048 0.4434 0.6941 0.0501  -0.1850 0.0574  318 TYR D OH  
8470  N N   . LEU D 319 ? 0.5537 0.5503 0.7707 0.0009  -0.2059 0.0433  319 LEU D N   
8471  C CA  . LEU D 319 ? 0.5973 0.5785 0.8042 -0.0086 -0.2038 0.0306  319 LEU D CA  
8472  C C   . LEU D 319 ? 0.6100 0.6063 0.8065 -0.0182 -0.2106 0.0248  319 LEU D C   
8473  O O   . LEU D 319 ? 0.6197 0.6074 0.8026 -0.0173 -0.2100 0.0191  319 LEU D O   
8474  C CB  . LEU D 319 ? 0.5969 0.5533 0.7962 0.0000  -0.1970 0.0282  319 LEU D CB  
8475  C CG  . LEU D 319 ? 0.6050 0.5436 0.8124 0.0019  -0.1893 0.0297  319 LEU D CG  
8476  C CD1 . LEU D 319 ? 0.5788 0.5006 0.7812 0.0123  -0.1844 0.0321  319 LEU D CD1 
8477  C CD2 . LEU D 319 ? 0.6670 0.5949 0.8774 -0.0107 -0.1848 0.0200  319 LEU D CD2 
8478  N N   . ASN D 320 ? 0.6585 0.6796 0.8617 -0.0280 -0.2174 0.0270  320 ASN D N   
8479  C CA  . ASN D 320 ? 0.6659 0.7086 0.8600 -0.0401 -0.2256 0.0232  320 ASN D CA  
8480  C C   . ASN D 320 ? 0.6841 0.7416 0.8849 -0.0579 -0.2287 0.0180  320 ASN D C   
8481  O O   . ASN D 320 ? 0.6986 0.7429 0.9090 -0.0608 -0.2226 0.0148  320 ASN D O   
8482  C CB  . ASN D 320 ? 0.6264 0.6948 0.8236 -0.0307 -0.2333 0.0379  320 ASN D CB  
8483  C CG  . ASN D 320 ? 0.6206 0.6792 0.8029 -0.0225 -0.2325 0.0371  320 ASN D CG  
8484  O OD1 . ASN D 320 ? 0.6429 0.7044 0.8096 -0.0322 -0.2352 0.0288  320 ASN D OD1 
8485  N ND2 . ASN D 320 ? 0.5908 0.6376 0.7772 -0.0058 -0.2280 0.0451  320 ASN D ND2 
8486  N N   . GLN D 321 ? 0.6949 0.7809 0.8904 -0.0710 -0.2381 0.0173  321 GLN D N   
8487  C CA  . GLN D 321 ? 0.7068 0.8125 0.9081 -0.0904 -0.2425 0.0126  321 GLN D CA  
8488  C C   . GLN D 321 ? 0.6751 0.8247 0.8890 -0.0910 -0.2548 0.0292  321 GLN D C   
8489  O O   . GLN D 321 ? 0.6802 0.8585 0.8921 -0.1095 -0.2633 0.0269  321 GLN D O   
8490  C CB  . GLN D 321 ? 0.7415 0.8417 0.9232 -0.1118 -0.2414 -0.0069 321 GLN D CB  
8491  C CG  . GLN D 321 ? 0.7701 0.8285 0.9394 -0.1084 -0.2285 -0.0212 321 GLN D CG  
8492  C CD  . GLN D 321 ? 0.8059 0.8519 0.9617 -0.1313 -0.2222 -0.0430 321 GLN D CD  
8493  O OE1 . GLN D 321 ? 0.8261 0.8528 0.9650 -0.1342 -0.2155 -0.0555 321 GLN D OE1 
8494  N NE2 . GLN D 321 ? 0.8134 0.8700 0.9770 -0.1485 -0.2231 -0.0485 321 GLN D NE2 
8495  N N   . LEU D 322 ? 0.6505 0.8068 0.8783 -0.0713 -0.2552 0.0466  322 LEU D N   
8496  C CA  . LEU D 322 ? 0.6189 0.8154 0.8644 -0.0686 -0.2643 0.0653  322 LEU D CA  
8497  C C   . LEU D 322 ? 0.6201 0.8324 0.8848 -0.0777 -0.2653 0.0679  322 LEU D C   
8498  O O   . LEU D 322 ? 0.6327 0.8208 0.9031 -0.0760 -0.2565 0.0617  322 LEU D O   
8499  C CB  . LEU D 322 ? 0.5857 0.7791 0.8425 -0.0448 -0.2604 0.0816  322 LEU D CB  
8500  C CG  . LEU D 322 ? 0.5823 0.7581 0.8228 -0.0337 -0.2580 0.0806  322 LEU D CG  
8501  C CD1 . LEU D 322 ? 0.5583 0.7261 0.8116 -0.0118 -0.2512 0.0942  322 LEU D CD1 
8502  C CD2 . LEU D 322 ? 0.5885 0.7920 0.8184 -0.0418 -0.2685 0.0846  322 LEU D CD2 
8503  N N   . ASN D 323 ? 0.6788 0.9340 0.9545 -0.0877 -0.2763 0.0784  323 ASN D N   
8504  C CA  . ASN D 323 ? 0.6790 0.9549 0.9736 -0.0989 -0.2787 0.0812  323 ASN D CA  
8505  C C   . ASN D 323 ? 0.6416 0.9611 0.9615 -0.0907 -0.2864 0.1059  323 ASN D C   
8506  O O   . ASN D 323 ? 0.6170 0.9430 0.9413 -0.0736 -0.2868 0.1205  323 ASN D O   
8507  C CB  . ASN D 323 ? 0.7075 0.9924 0.9887 -0.1275 -0.2840 0.0641  323 ASN D CB  
8508  C CG  . ASN D 323 ? 0.7012 1.0234 0.9702 -0.1417 -0.2975 0.0669  323 ASN D CG  
8509  O OD1 . ASN D 323 ? 0.6789 1.0159 0.9468 -0.1292 -0.3025 0.0809  323 ASN D OD1 
8510  N ND2 . ASN D 323 ? 0.7204 1.0584 0.9797 -0.1692 -0.3029 0.0533  323 ASN D ND2 
8511  N N   . GLY D 324 ? 0.5706 0.9196 0.9094 -0.1024 -0.2912 0.1115  324 GLY D N   
8512  C CA  . GLY D 324 ? 0.5607 0.9512 0.9290 -0.0936 -0.2966 0.1365  324 GLY D CA  
8513  C C   . GLY D 324 ? 0.5429 0.9154 0.9326 -0.0720 -0.2838 0.1461  324 GLY D C   
8514  O O   . GLY D 324 ? 0.5394 0.8727 0.9220 -0.0679 -0.2727 0.1333  324 GLY D O   
8515  N N   . SER D 325 ? 0.5494 0.9522 0.9662 -0.0583 -0.2847 0.1697  325 SER D N   
8516  C CA  . SER D 325 ? 0.5370 0.9275 0.9764 -0.0390 -0.2714 0.1797  325 SER D CA  
8517  C C   . SER D 325 ? 0.5193 0.8928 0.9584 -0.0161 -0.2633 0.1886  325 SER D C   
8518  O O   . SER D 325 ? 0.5055 0.8943 0.9398 -0.0129 -0.2702 0.1973  325 SER D O   
8519  C CB  . SER D 325 ? 0.5159 0.9508 0.9913 -0.0395 -0.2745 0.1999  325 SER D CB  
8520  O OG  . SER D 325 ? 0.5318 0.9817 1.0088 -0.0616 -0.2810 0.1911  325 SER D OG  
8521  N N   . ILE D 326 ? 0.4813 0.8234 0.9248 -0.0013 -0.2480 0.1863  326 ILE D N   
8522  C CA  . ILE D 326 ? 0.4743 0.7970 0.9184 0.0195  -0.2375 0.1929  326 ILE D CA  
8523  C C   . ILE D 326 ? 0.4723 0.8317 0.9468 0.0312  -0.2381 0.2188  326 ILE D C   
8524  O O   . ILE D 326 ? 0.4715 0.8521 0.9731 0.0339  -0.2333 0.2309  326 ILE D O   
8525  C CB  . ILE D 326 ? 0.4683 0.7554 0.9127 0.0300  -0.2206 0.1855  326 ILE D CB  
8526  C CG1 . ILE D 326 ? 0.4708 0.7230 0.8868 0.0199  -0.2200 0.1632  326 ILE D CG1 
8527  C CG2 . ILE D 326 ? 0.4640 0.7339 0.9107 0.0495  -0.2087 0.1923  326 ILE D CG2 
8528  C CD1 . ILE D 326 ? 0.4669 0.6902 0.8826 0.0266  -0.2054 0.1570  326 ILE D CD1 
8529  N N   . PRO D 327 ? 0.4990 0.8612 0.9634 0.0379  -0.2388 0.2252  327 PRO D N   
8530  C CA  . PRO D 327 ? 0.4851 0.8699 0.9661 0.0489  -0.2311 0.2449  327 PRO D CA  
8531  C C   . PRO D 327 ? 0.4803 0.8484 0.9835 0.0676  -0.2112 0.2528  327 PRO D C   
8532  O O   . PRO D 327 ? 0.4798 0.8127 0.9756 0.0777  -0.2012 0.2444  327 PRO D O   
8533  C CB  . PRO D 327 ? 0.4903 0.8701 0.9504 0.0524  -0.2337 0.2459  327 PRO D CB  
8534  C CG  . PRO D 327 ? 0.4940 0.8612 0.9263 0.0375  -0.2474 0.2271  327 PRO D CG  
8535  C CD  . PRO D 327 ? 0.5059 0.8489 0.9417 0.0351  -0.2454 0.2140  327 PRO D CD  
8536  N N   . PRO D 328 ? 0.4927 0.8852 1.0235 0.0719  -0.2044 0.2684  328 PRO D N   
8537  C CA  . PRO D 328 ? 0.4914 0.8683 1.0449 0.0895  -0.1832 0.2761  328 PRO D CA  
8538  C C   . PRO D 328 ? 0.4966 0.8520 1.0456 0.1049  -0.1700 0.2802  328 PRO D C   
8539  O O   . PRO D 328 ? 0.4959 0.8275 1.0564 0.1182  -0.1512 0.2802  328 PRO D O   
8540  C CB  . PRO D 328 ? 0.4998 0.9133 1.0828 0.0894  -0.1807 0.2945  328 PRO D CB  
8541  C CG  . PRO D 328 ? 0.5011 0.9444 1.0767 0.0691  -0.2011 0.2912  328 PRO D CG  
8542  C CD  . PRO D 328 ? 0.5017 0.9370 1.0446 0.0599  -0.2150 0.2793  328 PRO D CD  
8543  N N   . GLU D 329 ? 0.4903 0.8537 1.0232 0.1029  -0.1784 0.2837  329 GLU D N   
8544  C CA  . GLU D 329 ? 0.4965 0.8405 1.0254 0.1164  -0.1664 0.2882  329 GLU D CA  
8545  C C   . GLU D 329 ? 0.4877 0.7893 0.9965 0.1207  -0.1603 0.2703  329 GLU D C   
8546  O O   . GLU D 329 ? 0.4927 0.7726 1.0014 0.1327  -0.1461 0.2721  329 GLU D O   
8547  C CB  . GLU D 329 ? 0.5066 0.8726 1.0231 0.1113  -0.1785 0.2967  329 GLU D CB  
8548  C CG  . GLU D 329 ? 0.5192 0.9292 1.0556 0.1070  -0.1842 0.3168  329 GLU D CG  
8549  C CD  . GLU D 329 ? 0.5178 0.9566 1.0462 0.0873  -0.2041 0.3114  329 GLU D CD  
8550  O OE1 . GLU D 329 ? 0.5059 0.9300 1.0229 0.0788  -0.2098 0.2937  329 GLU D OE1 
8551  O OE2 . GLU D 329 ? 0.5305 1.0069 1.0649 0.0796  -0.2136 0.3253  329 GLU D OE2 
8552  N N   . LEU D 330 ? 0.5121 0.8013 1.0050 0.1107  -0.1703 0.2536  330 LEU D N   
8553  C CA  . LEU D 330 ? 0.5096 0.7597 0.9840 0.1141  -0.1653 0.2375  330 LEU D CA  
8554  C C   . LEU D 330 ? 0.5167 0.7427 1.0067 0.1272  -0.1435 0.2374  330 LEU D C   
8555  O O   . LEU D 330 ? 0.5249 0.7194 1.0026 0.1334  -0.1343 0.2284  330 LEU D O   
8556  C CB  . LEU D 330 ? 0.5213 0.7643 0.9799 0.1005  -0.1797 0.2217  330 LEU D CB  
8557  C CG  . LEU D 330 ? 0.5221 0.7777 0.9590 0.0864  -0.1995 0.2158  330 LEU D CG  
8558  C CD1 . LEU D 330 ? 0.5423 0.7695 0.9511 0.0752  -0.2035 0.1928  330 LEU D CD1 
8559  C CD2 . LEU D 330 ? 0.5146 0.7685 0.9372 0.0914  -0.1992 0.2199  330 LEU D CD2 
8560  N N   . GLY D 331 ? 0.5011 0.7417 1.0182 0.1307  -0.1344 0.2469  331 GLY D N   
8561  C CA  . GLY D 331 ? 0.5117 0.7317 1.0462 0.1429  -0.1114 0.2474  331 GLY D CA  
8562  C C   . GLY D 331 ? 0.5118 0.7193 1.0526 0.1558  -0.0937 0.2552  331 GLY D C   
8563  O O   . GLY D 331 ? 0.5213 0.7057 1.0730 0.1652  -0.0723 0.2525  331 GLY D O   
8564  N N   . GLU D 332 ? 0.5248 0.7467 1.0594 0.1558  -0.1012 0.2643  332 GLU D N   
8565  C CA  . GLU D 332 ? 0.5381 0.7482 1.0783 0.1671  -0.0856 0.2722  332 GLU D CA  
8566  C C   . GLU D 332 ? 0.5365 0.7162 1.0497 0.1676  -0.0857 0.2589  332 GLU D C   
8567  O O   . GLU D 332 ? 0.5475 0.7174 1.0619 0.1752  -0.0751 0.2646  332 GLU D O   
8568  C CB  . GLU D 332 ? 0.5477 0.7920 1.0994 0.1673  -0.0925 0.2923  332 GLU D CB  
8569  C CG  . GLU D 332 ? 0.5479 0.8289 1.1212 0.1623  -0.0996 0.3049  332 GLU D CG  
8570  C CD  . GLU D 332 ? 0.5574 0.8391 1.1647 0.1729  -0.0777 0.3163  332 GLU D CD  
8571  O OE1 . GLU D 332 ? 0.5661 0.8199 1.1809 0.1841  -0.0556 0.3149  332 GLU D OE1 
8572  O OE2 . GLU D 332 ? 0.5576 0.8677 1.1845 0.1694  -0.0816 0.3264  332 GLU D OE2 
8573  N N   . MET D 333 ? 0.5467 0.7115 1.0369 0.1594  -0.0971 0.2420  333 MET D N   
8574  C CA  . MET D 333 ? 0.5476 0.6816 1.0134 0.1598  -0.0959 0.2286  333 MET D CA  
8575  C C   . MET D 333 ? 0.5672 0.6686 1.0396 0.1673  -0.0736 0.2202  333 MET D C   
8576  O O   . MET D 333 ? 0.5857 0.6704 1.0492 0.1627  -0.0735 0.2066  333 MET D O   
8577  C CB  . MET D 333 ? 0.5487 0.6801 0.9890 0.1478  -0.1163 0.2149  333 MET D CB  
8578  C CG  . MET D 333 ? 0.5349 0.6948 0.9651 0.1388  -0.1367 0.2202  333 MET D CG  
8579  S SD  . MET D 333 ? 0.5411 0.6975 0.9460 0.1233  -0.1583 0.2034  333 MET D SD  
8580  C CE  . MET D 333 ? 0.5606 0.6944 0.9656 0.1209  -0.1479 0.1895  333 MET D CE  
8581  N N   . GLU D 334 ? 0.5678 0.6593 1.0540 0.1775  -0.0534 0.2275  334 GLU D N   
8582  C CA  . GLU D 334 ? 0.5908 0.6537 1.0881 0.1842  -0.0280 0.2206  334 GLU D CA  
8583  C C   . GLU D 334 ? 0.6164 0.6457 1.0888 0.1795  -0.0264 0.2003  334 GLU D C   
8584  O O   . GLU D 334 ? 0.6470 0.6577 1.1100 0.1740  -0.0137 0.1850  334 GLU D O   
8585  C CB  . GLU D 334 ? 0.5953 0.6506 1.1085 0.1943  -0.0067 0.2306  334 GLU D CB  
8586  C CG  . GLU D 334 ? 0.5975 0.6857 1.1241 0.1969  -0.0148 0.2514  334 GLU D CG  
8587  C CD  . GLU D 334 ? 0.6188 0.7002 1.1679 0.2074  0.0091  0.2637  334 GLU D CD  
8588  O OE1 . GLU D 334 ? 0.6291 0.6796 1.1706 0.2105  0.0247  0.2549  334 GLU D OE1 
8589  O OE2 . GLU D 334 ? 0.6265 0.7331 1.2019 0.2119  0.0131  0.2821  334 GLU D OE2 
8590  N N   . SER D 335 ? 0.5432 0.5651 0.9929 0.1760  -0.0382 0.1951  335 SER D N   
8591  C CA  . SER D 335 ? 0.5702 0.5609 0.9861 0.1669  -0.0349 0.1727  335 SER D CA  
8592  C C   . SER D 335 ? 0.5793 0.5710 0.9669 0.1526  -0.0520 0.1574  335 SER D C   
8593  O O   . SER D 335 ? 0.6008 0.5707 0.9609 0.1444  -0.0511 0.1403  335 SER D O   
8594  C CB  . SER D 335 ? 0.5596 0.5416 0.9652 0.1698  -0.0388 0.1746  335 SER D CB  
8595  O OG  . SER D 335 ? 0.5550 0.5337 0.9830 0.1816  -0.0213 0.1876  335 SER D OG  
8596  N N   . MET D 336 ? 0.5564 0.5732 0.9513 0.1490  -0.0665 0.1637  336 MET D N   
8597  C CA  . MET D 336 ? 0.5582 0.5769 0.9286 0.1361  -0.0837 0.1516  336 MET D CA  
8598  C C   . MET D 336 ? 0.5925 0.5891 0.9443 0.1282  -0.0741 0.1343  336 MET D C   
8599  O O   . MET D 336 ? 0.6138 0.6072 0.9772 0.1296  -0.0592 0.1336  336 MET D O   
8600  C CB  . MET D 336 ? 0.5407 0.5895 0.9259 0.1331  -0.0974 0.1614  336 MET D CB  
8601  C CG  . MET D 336 ? 0.5414 0.5916 0.9045 0.1198  -0.1140 0.1499  336 MET D CG  
8602  S SD  . MET D 336 ? 0.5325 0.5700 0.8652 0.1141  -0.1275 0.1397  336 MET D SD  
8603  C CE  . MET D 336 ? 0.5080 0.5660 0.8549 0.1223  -0.1342 0.1569  336 MET D CE  
8604  N N   . ILE D 337 ? 0.5184 0.5013 0.8417 0.1196  -0.0826 0.1211  337 ILE D N   
8605  C CA  . ILE D 337 ? 0.5525 0.5173 0.8552 0.1108  -0.0758 0.1060  337 ILE D CA  
8606  C C   . ILE D 337 ? 0.5456 0.5158 0.8323 0.1008  -0.0920 0.1004  337 ILE D C   
8607  O O   . ILE D 337 ? 0.5673 0.5363 0.8495 0.0945  -0.0889 0.0955  337 ILE D O   
8608  C CB  . ILE D 337 ? 0.5728 0.5150 0.8575 0.1096  -0.0673 0.0960  337 ILE D CB  
8609  C CG1 . ILE D 337 ? 0.5968 0.5264 0.8953 0.1163  -0.0440 0.0967  337 ILE D CG1 
8610  C CG2 . ILE D 337 ? 0.6016 0.5323 0.8597 0.0977  -0.0694 0.0820  337 ILE D CG2 
8611  C CD1 . ILE D 337 ? 0.6119 0.5208 0.8975 0.1159  -0.0352 0.0890  337 ILE D CD1 
8612  N N   . ASP D 338 ? 0.5744 0.5496 0.8526 0.0991  -0.1080 0.1012  338 ASP D N   
8613  C CA  . ASP D 338 ? 0.5646 0.5430 0.8301 0.0903  -0.1220 0.0963  338 ASP D CA  
8614  C C   . ASP D 338 ? 0.5383 0.5370 0.8156 0.0904  -0.1354 0.1045  338 ASP D C   
8615  O O   . ASP D 338 ? 0.5210 0.5237 0.7956 0.0926  -0.1431 0.1072  338 ASP D O   
8616  C CB  . ASP D 338 ? 0.5628 0.5264 0.8054 0.0863  -0.1269 0.0876  338 ASP D CB  
8617  C CG  . ASP D 338 ? 0.5519 0.5170 0.7844 0.0786  -0.1391 0.0838  338 ASP D CG  
8618  O OD1 . ASP D 338 ? 0.5563 0.5291 0.7957 0.0746  -0.1409 0.0854  338 ASP D OD1 
8619  O OD2 . ASP D 338 ? 0.5407 0.4987 0.7598 0.0768  -0.1458 0.0795  338 ASP D OD2 
8620  N N   . LEU D 339 ? 0.5132 0.5257 0.8026 0.0869  -0.1380 0.1081  339 LEU D N   
8621  C CA  . LEU D 339 ? 0.4974 0.5322 0.7984 0.0841  -0.1503 0.1152  339 LEU D CA  
8622  C C   . LEU D 339 ? 0.5019 0.5352 0.7925 0.0730  -0.1597 0.1076  339 LEU D C   
8623  O O   . LEU D 339 ? 0.5158 0.5471 0.8092 0.0690  -0.1556 0.1056  339 LEU D O   
8624  C CB  . LEU D 339 ? 0.4979 0.5528 0.8257 0.0886  -0.1450 0.1271  339 LEU D CB  
8625  C CG  . LEU D 339 ? 0.4864 0.5694 0.8281 0.0836  -0.1579 0.1353  339 LEU D CG  
8626  C CD1 . LEU D 339 ? 0.4716 0.5643 0.8075 0.0837  -0.1692 0.1389  339 LEU D CD1 
8627  C CD2 . LEU D 339 ? 0.4842 0.5882 0.8552 0.0897  -0.1511 0.1491  339 LEU D CD2 
8628  N N   . GLU D 340 ? 0.5228 0.5559 0.8018 0.0681  -0.1708 0.1034  340 GLU D N   
8629  C CA  . GLU D 340 ? 0.5323 0.5599 0.8018 0.0579  -0.1774 0.0954  340 GLU D CA  
8630  C C   . GLU D 340 ? 0.5346 0.5788 0.8064 0.0505  -0.1890 0.0958  340 GLU D C   
8631  O O   . GLU D 340 ? 0.5294 0.5743 0.7920 0.0508  -0.1945 0.0944  340 GLU D O   
8632  C CB  . GLU D 340 ? 0.5317 0.5367 0.7813 0.0575  -0.1765 0.0867  340 GLU D CB  
8633  C CG  . GLU D 340 ? 0.5306 0.5224 0.7742 0.0643  -0.1665 0.0862  340 GLU D CG  
8634  C CD  . GLU D 340 ? 0.5333 0.5075 0.7605 0.0615  -0.1658 0.0794  340 GLU D CD  
8635  O OE1 . GLU D 340 ? 0.5305 0.5001 0.7508 0.0573  -0.1724 0.0754  340 GLU D OE1 
8636  O OE2 . GLU D 340 ? 0.5429 0.5088 0.7645 0.0630  -0.1578 0.0783  340 GLU D OE2 
8637  N N   . ILE D 341 ? 0.4699 0.5281 0.7529 0.0426  -0.1924 0.0972  341 ILE D N   
8638  C CA  . ILE D 341 ? 0.4816 0.5557 0.7645 0.0317  -0.2031 0.0951  341 ILE D CA  
8639  C C   . ILE D 341 ? 0.5079 0.5731 0.7878 0.0198  -0.2037 0.0860  341 ILE D C   
8640  O O   . ILE D 341 ? 0.5241 0.6051 0.8098 0.0084  -0.2100 0.0846  341 ILE D O   
8641  C CB  . ILE D 341 ? 0.4735 0.5802 0.7761 0.0317  -0.2078 0.1076  341 ILE D CB  
8642  C CG1 . ILE D 341 ? 0.4684 0.5815 0.7907 0.0370  -0.1996 0.1156  341 ILE D CG1 
8643  C CG2 . ILE D 341 ? 0.4643 0.5808 0.7679 0.0410  -0.2095 0.1165  341 ILE D CG2 
8644  C CD1 . ILE D 341 ? 0.4667 0.6139 0.8113 0.0335  -0.2050 0.1272  341 ILE D CD1 
8645  N N   . SER D 342 ? 0.5325 0.5733 0.8040 0.0219  -0.1970 0.0804  342 SER D N   
8646  C CA  . SER D 342 ? 0.5600 0.5895 0.8311 0.0127  -0.1952 0.0741  342 SER D CA  
8647  C C   . SER D 342 ? 0.5891 0.6138 0.8510 0.0016  -0.2003 0.0640  342 SER D C   
8648  O O   . SER D 342 ? 0.5865 0.6139 0.8386 0.0013  -0.2051 0.0607  342 SER D O   
8649  C CB  . SER D 342 ? 0.5566 0.5630 0.8197 0.0183  -0.1875 0.0728  342 SER D CB  
8650  O OG  . SER D 342 ? 0.5371 0.5456 0.8040 0.0272  -0.1815 0.0797  342 SER D OG  
8651  N N   . GLU D 343 ? 0.5848 0.6013 0.8501 -0.0082 -0.1979 0.0586  343 GLU D N   
8652  C CA  . GLU D 343 ? 0.6247 0.6287 0.8815 -0.0194 -0.1982 0.0467  343 GLU D CA  
8653  C C   . GLU D 343 ? 0.6287 0.6514 0.8803 -0.0290 -0.2068 0.0418  343 GLU D C   
8654  O O   . GLU D 343 ? 0.6358 0.6520 0.8734 -0.0298 -0.2085 0.0351  343 GLU D O   
8655  C CB  . GLU D 343 ? 0.6304 0.6084 0.8752 -0.0125 -0.1928 0.0427  343 GLU D CB  
8656  C CG  . GLU D 343 ? 0.6292 0.5909 0.8793 -0.0074 -0.1849 0.0475  343 GLU D CG  
8657  C CD  . GLU D 343 ? 0.6051 0.5496 0.8459 0.0027  -0.1812 0.0490  343 GLU D CD  
8658  O OE1 . GLU D 343 ? 0.6267 0.5536 0.8639 0.0005  -0.1772 0.0433  343 GLU D OE1 
8659  O OE2 . GLU D 343 ? 0.5659 0.5147 0.8039 0.0124  -0.1814 0.0557  343 GLU D OE2 
8660  N N   . ASN D 344 ? 0.6255 0.6740 0.8889 -0.0368 -0.2123 0.0460  344 ASN D N   
8661  C CA  . ASN D 344 ? 0.6229 0.6975 0.8837 -0.0477 -0.2220 0.0444  344 ASN D CA  
8662  C C   . ASN D 344 ? 0.6392 0.7292 0.9109 -0.0646 -0.2243 0.0412  344 ASN D C   
8663  O O   . ASN D 344 ? 0.6580 0.7326 0.9369 -0.0681 -0.2172 0.0379  344 ASN D O   
8664  C CB  . ASN D 344 ? 0.5828 0.6826 0.8501 -0.0364 -0.2281 0.0590  344 ASN D CB  
8665  C CG  . ASN D 344 ? 0.5720 0.6650 0.8237 -0.0285 -0.2297 0.0582  344 ASN D CG  
8666  O OD1 . ASN D 344 ? 0.5843 0.6861 0.8238 -0.0380 -0.2357 0.0522  344 ASN D OD1 
8667  N ND2 . ASN D 344 ? 0.5488 0.6270 0.8001 -0.0120 -0.2239 0.0640  344 ASN D ND2 
8668  N N   . LYS D 345 ? 0.6457 0.7678 0.9193 -0.0759 -0.2344 0.0430  345 LYS D N   
8669  C CA  . LYS D 345 ? 0.6554 0.7981 0.9398 -0.0940 -0.2382 0.0405  345 LYS D CA  
8670  C C   . LYS D 345 ? 0.6232 0.8071 0.9273 -0.0911 -0.2468 0.0581  345 LYS D C   
8671  O O   . LYS D 345 ? 0.6211 0.8374 0.9300 -0.1070 -0.2561 0.0591  345 LYS D O   
8672  C CB  . LYS D 345 ? 0.6803 0.8258 0.9483 -0.1161 -0.2421 0.0241  345 LYS D CB  
8673  C CG  . LYS D 345 ? 0.7144 0.8179 0.9678 -0.1201 -0.2306 0.0066  345 LYS D CG  
8674  C CD  . LYS D 345 ? 0.7378 0.8423 0.9728 -0.1418 -0.2323 -0.0113 345 LYS D CD  
8675  C CE  . LYS D 345 ? 0.7682 0.8290 0.9902 -0.1424 -0.2187 -0.0274 345 LYS D CE  
8676  N NZ  . LYS D 345 ? 0.7894 0.8498 0.9902 -0.1616 -0.2188 -0.0453 345 LYS D NZ  
8677  N N   . LEU D 346 ? 0.6212 0.8048 0.9377 -0.0711 -0.2429 0.0724  346 LEU D N   
8678  C CA  . LEU D 346 ? 0.5904 0.8099 0.9294 -0.0649 -0.2478 0.0908  346 LEU D CA  
8679  C C   . LEU D 346 ? 0.5959 0.8291 0.9552 -0.0737 -0.2462 0.0937  346 LEU D C   
8680  O O   . LEU D 346 ? 0.6193 0.8281 0.9769 -0.0784 -0.2384 0.0842  346 LEU D O   
8681  C CB  . LEU D 346 ? 0.5641 0.7742 0.9097 -0.0414 -0.2407 0.1029  346 LEU D CB  
8682  C CG  . LEU D 346 ? 0.5538 0.7510 0.8822 -0.0311 -0.2413 0.1022  346 LEU D CG  
8683  C CD1 . LEU D 346 ? 0.5286 0.7153 0.8650 -0.0100 -0.2323 0.1128  346 LEU D CD1 
8684  C CD2 . LEU D 346 ? 0.5439 0.7734 0.8698 -0.0380 -0.2536 0.1081  346 LEU D CD2 
8685  N N   . THR D 347 ? 0.5892 0.8635 0.9693 -0.0756 -0.2536 0.1085  347 THR D N   
8686  C CA  . THR D 347 ? 0.5902 0.8850 0.9925 -0.0847 -0.2534 0.1135  347 THR D CA  
8687  C C   . THR D 347 ? 0.5574 0.8824 0.9879 -0.0698 -0.2529 0.1359  347 THR D C   
8688  O O   . THR D 347 ? 0.5337 0.8705 0.9670 -0.0566 -0.2553 0.1479  347 THR D O   
8689  C CB  . THR D 347 ? 0.6012 0.9233 1.0017 -0.1109 -0.2646 0.1062  347 THR D CB  
8690  O OG1 . THR D 347 ? 0.5788 0.9394 0.9804 -0.1136 -0.2776 0.1170  347 THR D OG1 
8691  C CG2 . THR D 347 ? 0.6370 0.9263 1.0111 -0.1263 -0.2619 0.0826  347 THR D CG2 
8692  N N   . GLY D 348 ? 0.5757 0.9121 1.0287 -0.0716 -0.2483 0.1421  348 GLY D N   
8693  C CA  . GLY D 348 ? 0.5478 0.9143 1.0314 -0.0589 -0.2461 0.1634  348 GLY D CA  
8694  C C   . GLY D 348 ? 0.5439 0.8839 1.0332 -0.0371 -0.2302 0.1681  348 GLY D C   
8695  O O   . GLY D 348 ? 0.5604 0.8602 1.0288 -0.0319 -0.2221 0.1557  348 GLY D O   
8696  N N   . PRO D 349 ? 0.4919 0.8553 1.0103 -0.0247 -0.2247 0.1865  349 PRO D N   
8697  C CA  . PRO D 349 ? 0.4899 0.8295 1.0150 -0.0066 -0.2072 0.1897  349 PRO D CA  
8698  C C   . PRO D 349 ? 0.4793 0.8015 0.9950 0.0111  -0.2015 0.1927  349 PRO D C   
8699  O O   . PRO D 349 ? 0.4684 0.8045 0.9807 0.0127  -0.2107 0.1983  349 PRO D O   
8700  C CB  . PRO D 349 ? 0.4780 0.8529 1.0411 -0.0021 -0.2029 0.2084  349 PRO D CB  
8701  C CG  . PRO D 349 ? 0.4620 0.8812 1.0391 -0.0079 -0.2185 0.2221  349 PRO D CG  
8702  C CD  . PRO D 349 ? 0.4751 0.8897 1.0233 -0.0276 -0.2334 0.2059  349 PRO D CD  
8703  N N   . VAL D 350 ? 0.5044 0.7965 1.0158 0.0233  -0.1856 0.1889  350 VAL D N   
8704  C CA  . VAL D 350 ? 0.4946 0.7682 0.9990 0.0398  -0.1771 0.1911  350 VAL D CA  
8705  C C   . VAL D 350 ? 0.4737 0.7731 1.0118 0.0539  -0.1693 0.2117  350 VAL D C   
8706  O O   . VAL D 350 ? 0.4765 0.7886 1.0388 0.0562  -0.1602 0.2195  350 VAL D O   
8707  C CB  . VAL D 350 ? 0.5148 0.7484 1.0004 0.0448  -0.1629 0.1783  350 VAL D CB  
8708  C CG1 . VAL D 350 ? 0.5072 0.7234 0.9886 0.0605  -0.1519 0.1805  350 VAL D CG1 
8709  C CG2 . VAL D 350 ? 0.5316 0.7406 0.9867 0.0329  -0.1703 0.1611  350 VAL D CG2 
8710  N N   . PRO D 351 ? 0.5220 0.8297 1.0644 0.0639  -0.1714 0.2218  351 PRO D N   
8711  C CA  . PRO D 351 ? 0.5003 0.8341 1.0791 0.0783  -0.1631 0.2443  351 PRO D CA  
8712  C C   . PRO D 351 ? 0.5122 0.8221 1.1017 0.0928  -0.1390 0.2442  351 PRO D C   
8713  O O   . PRO D 351 ? 0.5322 0.8036 1.0969 0.0951  -0.1290 0.2285  351 PRO D O   
8714  C CB  . PRO D 351 ? 0.4799 0.8201 1.0541 0.0853  -0.1701 0.2527  351 PRO D CB  
8715  C CG  . PRO D 351 ? 0.4887 0.8209 1.0286 0.0696  -0.1874 0.2368  351 PRO D CG  
8716  C CD  . PRO D 351 ? 0.5166 0.8142 1.0334 0.0618  -0.1820 0.2153  351 PRO D CD  
8717  N N   . ASP D 352 ? 0.5786 0.9136 1.2065 0.1020  -0.1290 0.2626  352 ASP D N   
8718  C CA  . ASP D 352 ? 0.5899 0.9050 1.2326 0.1170  -0.1033 0.2647  352 ASP D CA  
8719  C C   . ASP D 352 ? 0.5871 0.8772 1.2211 0.1303  -0.0928 0.2640  352 ASP D C   
8720  O O   . ASP D 352 ? 0.6070 0.8681 1.2396 0.1390  -0.0708 0.2572  352 ASP D O   
8721  C CB  . ASP D 352 ? 0.5725 0.9221 1.2620 0.1260  -0.0939 0.2876  352 ASP D CB  
8722  C CG  . ASP D 352 ? 0.5699 0.9519 1.2738 0.1126  -0.1060 0.2918  352 ASP D CG  
8723  O OD1 . ASP D 352 ? 0.5607 0.9618 1.2507 0.0979  -0.1281 0.2899  352 ASP D OD1 
8724  O OD2 . ASP D 352 ? 0.5812 0.9671 1.3064 0.1151  -0.0917 0.2951  352 ASP D OD2 
8725  N N   . SER D 353 ? 0.5414 0.8410 1.1661 0.1301  -0.1067 0.2694  353 SER D N   
8726  C CA  . SER D 353 ? 0.5394 0.8151 1.1526 0.1409  -0.0961 0.2684  353 SER D CA  
8727  C C   . SER D 353 ? 0.5640 0.7968 1.1488 0.1407  -0.0891 0.2476  353 SER D C   
8728  O O   . SER D 353 ? 0.5688 0.7778 1.1511 0.1513  -0.0741 0.2460  353 SER D O   
8729  C CB  . SER D 353 ? 0.5223 0.8128 1.1183 0.1357  -0.1128 0.2730  353 SER D CB  
8730  O OG  . SER D 353 ? 0.5190 0.8494 1.1259 0.1267  -0.1266 0.2849  353 SER D OG  
8731  N N   . PHE D 354 ? 0.5003 0.7199 1.0572 0.1264  -0.0976 0.2292  354 PHE D N   
8732  C CA  . PHE D 354 ? 0.5264 0.7057 1.0485 0.1229  -0.0909 0.2080  354 PHE D CA  
8733  C C   . PHE D 354 ? 0.5525 0.7081 1.0802 0.1312  -0.0646 0.2034  354 PHE D C   
8734  O O   . PHE D 354 ? 0.5732 0.6973 1.0763 0.1310  -0.0559 0.1892  354 PHE D O   
8735  C CB  . PHE D 354 ? 0.5416 0.7146 1.0389 0.1069  -0.1033 0.1930  354 PHE D CB  
8736  C CG  . PHE D 354 ? 0.5276 0.7049 1.0042 0.0975  -0.1247 0.1880  354 PHE D CG  
8737  C CD1 . PHE D 354 ? 0.5016 0.7067 0.9907 0.0987  -0.1377 0.2013  354 PHE D CD1 
8738  C CD2 . PHE D 354 ? 0.5422 0.6965 0.9872 0.0873  -0.1309 0.1707  354 PHE D CD2 
8739  C CE1 . PHE D 354 ? 0.4951 0.7033 0.9632 0.0888  -0.1557 0.1951  354 PHE D CE1 
8740  C CE2 . PHE D 354 ? 0.5324 0.6885 0.9594 0.0789  -0.1480 0.1653  354 PHE D CE2 
8741  C CZ  . PHE D 354 ? 0.5113 0.6935 0.9487 0.0791  -0.1600 0.1763  354 PHE D CZ  
8742  N N   . GLY D 355 ? 0.5268 0.6977 1.0867 0.1376  -0.0511 0.2150  355 GLY D N   
8743  C CA  . GLY D 355 ? 0.5487 0.6977 1.1167 0.1459  -0.0234 0.2111  355 GLY D CA  
8744  C C   . GLY D 355 ? 0.5469 0.6807 1.1224 0.1591  -0.0090 0.2157  355 GLY D C   
8745  O O   . GLY D 355 ? 0.5709 0.6770 1.1424 0.1630  0.0147  0.2061  355 GLY D O   
8746  N N   . LYS D 356 ? 0.5128 0.6640 1.0986 0.1651  -0.0220 0.2300  356 LYS D N   
8747  C CA  . LYS D 356 ? 0.5047 0.6415 1.0979 0.1776  -0.0093 0.2359  356 LYS D CA  
8748  C C   . LYS D 356 ? 0.5220 0.6255 1.0751 0.1714  -0.0117 0.2161  356 LYS D C   
8749  O O   . LYS D 356 ? 0.5254 0.6084 1.0799 0.1799  0.0034  0.2158  356 LYS D O   
8750  C CB  . LYS D 356 ? 0.4708 0.6387 1.0788 0.1816  -0.0223 0.2563  356 LYS D CB  
8751  C CG  . LYS D 356 ? 0.4774 0.6772 1.1170 0.1847  -0.0177 0.2749  356 LYS D CG  
8752  C CD  . LYS D 356 ? 0.4823 0.7089 1.1232 0.1840  -0.0305 0.2910  356 LYS D CD  
8753  C CE  . LYS D 356 ? 0.4960 0.7482 1.1710 0.1906  -0.0195 0.3124  356 LYS D CE  
8754  N NZ  . LYS D 356 ? 0.5047 0.7792 1.1812 0.1913  -0.0287 0.3291  356 LYS D NZ  
8755  N N   . LEU D 357 ? 0.4983 0.5960 1.0175 0.1571  -0.0292 0.2004  357 LEU D N   
8756  C CA  . LEU D 357 ? 0.5133 0.5827 0.9957 0.1508  -0.0327 0.1829  357 LEU D CA  
8757  C C   . LEU D 357 ? 0.5573 0.5952 1.0248 0.1480  -0.0105 0.1659  357 LEU D C   
8758  O O   . LEU D 357 ? 0.5850 0.6137 1.0300 0.1366  -0.0127 0.1517  357 LEU D O   
8759  C CB  . LEU D 357 ? 0.5072 0.5825 0.9628 0.1374  -0.0573 0.1740  357 LEU D CB  
8760  C CG  . LEU D 357 ? 0.4725 0.5808 0.9397 0.1357  -0.0793 0.1877  357 LEU D CG  
8761  C CD1 . LEU D 357 ? 0.4742 0.5829 0.9151 0.1210  -0.0986 0.1756  357 LEU D CD1 
8762  C CD2 . LEU D 357 ? 0.4482 0.5633 0.9214 0.1441  -0.0841 0.1993  357 LEU D CD2 
8763  N N   . THR D 358 ? 0.5014 0.5229 0.9820 0.1579  0.0121  0.1677  358 THR D N   
8764  C CA  . THR D 358 ? 0.5212 0.5137 0.9903 0.1545  0.0368  0.1515  358 THR D CA  
8765  C C   . THR D 358 ? 0.5397 0.5064 0.9677 0.1430  0.0337  0.1309  358 THR D C   
8766  O O   . THR D 358 ? 0.5851 0.5311 0.9960 0.1353  0.0501  0.1150  358 THR D O   
8767  C CB  . THR D 358 ? 0.5380 0.5193 1.0362 0.1684  0.0645  0.1595  358 THR D CB  
8768  O OG1 . THR D 358 ? 0.5358 0.5169 1.0409 0.1772  0.0595  0.1697  358 THR D OG1 
8769  C CG2 . THR D 358 ? 0.5384 0.5438 1.0783 0.1788  0.0728  0.1783  358 THR D CG2 
8770  N N   . ALA D 359 ? 0.5569 0.5259 0.9686 0.1408  0.0135  0.1310  359 ALA D N   
8771  C CA  . ALA D 359 ? 0.5592 0.5069 0.9349 0.1305  0.0097  0.1136  359 ALA D CA  
8772  C C   . ALA D 359 ? 0.5433 0.5003 0.8955 0.1196  -0.0147 0.1085  359 ALA D C   
8773  O O   . ALA D 359 ? 0.5420 0.4864 0.8672 0.1123  -0.0221 0.0978  359 ALA D O   
8774  C CB  . ALA D 359 ? 0.5618 0.4988 0.9367 0.1369  0.0107  0.1162  359 ALA D CB  
8775  N N   . LEU D 360 ? 0.5186 0.4970 0.8818 0.1181  -0.0263 0.1160  360 LEU D N   
8776  C CA  . LEU D 360 ? 0.5051 0.4918 0.8502 0.1086  -0.0482 0.1125  360 LEU D CA  
8777  C C   . LEU D 360 ? 0.5107 0.4818 0.8277 0.0969  -0.0455 0.0976  360 LEU D C   
8778  O O   . LEU D 360 ? 0.5220 0.4874 0.8389 0.0936  -0.0303 0.0926  360 LEU D O   
8779  C CB  . LEU D 360 ? 0.4961 0.5081 0.8612 0.1085  -0.0580 0.1234  360 LEU D CB  
8780  C CG  . LEU D 360 ? 0.4834 0.5062 0.8366 0.0998  -0.0804 0.1222  360 LEU D CG  
8781  C CD1 . LEU D 360 ? 0.4766 0.5027 0.8244 0.1022  -0.0941 0.1251  360 LEU D CD1 
8782  C CD2 . LEU D 360 ? 0.4781 0.5250 0.8519 0.0979  -0.0869 0.1314  360 LEU D CD2 
8783  N N   . GLU D 361 ? 0.5333 0.4987 0.8271 0.0903  -0.0596 0.0912  361 GLU D N   
8784  C CA  . GLU D 361 ? 0.5671 0.5229 0.8354 0.0790  -0.0604 0.0804  361 GLU D CA  
8785  C C   . GLU D 361 ? 0.5427 0.5081 0.8043 0.0729  -0.0789 0.0823  361 GLU D C   
8786  O O   . GLU D 361 ? 0.5655 0.5328 0.8209 0.0656  -0.0782 0.0805  361 GLU D O   
8787  C CB  . GLU D 361 ? 0.5861 0.5248 0.8330 0.0761  -0.0572 0.0709  361 GLU D CB  
8788  C CG  . GLU D 361 ? 0.6213 0.5458 0.8717 0.0792  -0.0354 0.0657  361 GLU D CG  
8789  C CD  . GLU D 361 ? 0.6519 0.5599 0.8784 0.0724  -0.0313 0.0541  361 GLU D CD  
8790  O OE1 . GLU D 361 ? 0.6604 0.5694 0.8659 0.0635  -0.0432 0.0497  361 GLU D OE1 
8791  O OE2 . GLU D 361 ? 0.6663 0.5606 0.8965 0.0759  -0.0156 0.0502  361 GLU D OE2 
8792  N N   . TRP D 362 ? 0.5973 0.5680 0.8600 0.0752  -0.0941 0.0860  362 TRP D N   
8793  C CA  . TRP D 362 ? 0.5739 0.5518 0.8331 0.0697  -0.1095 0.0873  362 TRP D CA  
8794  C C   . TRP D 362 ? 0.5463 0.5424 0.8266 0.0728  -0.1173 0.0961  362 TRP D C   
8795  O O   . TRP D 362 ? 0.5255 0.5278 0.8146 0.0791  -0.1203 0.1010  362 TRP D O   
8796  C CB  . TRP D 362 ? 0.5543 0.5238 0.7962 0.0677  -0.1201 0.0829  362 TRP D CB  
8797  C CG  . TRP D 362 ? 0.5793 0.5357 0.8004 0.0626  -0.1161 0.0758  362 TRP D CG  
8798  C CD1 . TRP D 362 ? 0.5891 0.5439 0.7986 0.0551  -0.1199 0.0744  362 TRP D CD1 
8799  C CD2 . TRP D 362 ? 0.6005 0.5456 0.8106 0.0637  -0.1078 0.0702  362 TRP D CD2 
8800  N NE1 . TRP D 362 ? 0.6155 0.5618 0.8072 0.0512  -0.1156 0.0691  362 TRP D NE1 
8801  C CE2 . TRP D 362 ? 0.6259 0.5654 0.8168 0.0556  -0.1080 0.0652  362 TRP D CE2 
8802  C CE3 . TRP D 362 ? 0.6029 0.5425 0.8185 0.0705  -0.0996 0.0697  362 TRP D CE3 
8803  C CZ2 . TRP D 362 ? 0.6584 0.5883 0.8341 0.0523  -0.1012 0.0583  362 TRP D CZ2 
8804  C CZ3 . TRP D 362 ? 0.6335 0.5602 0.8345 0.0679  -0.0913 0.0622  362 TRP D CZ3 
8805  C CH2 . TRP D 362 ? 0.6635 0.5859 0.8440 0.0581  -0.0925 0.0558  362 TRP D CH2 
8806  N N   . LEU D 363 ? 0.5279 0.5339 0.8163 0.0676  -0.1206 0.0986  363 LEU D N   
8807  C CA  . LEU D 363 ? 0.5078 0.5332 0.8139 0.0669  -0.1301 0.1057  363 LEU D CA  
8808  C C   . LEU D 363 ? 0.5055 0.5302 0.8037 0.0573  -0.1411 0.1019  363 LEU D C   
8809  O O   . LEU D 363 ? 0.5234 0.5461 0.8212 0.0518  -0.1378 0.1010  363 LEU D O   
8810  C CB  . LEU D 363 ? 0.5184 0.5590 0.8479 0.0696  -0.1216 0.1136  363 LEU D CB  
8811  C CG  . LEU D 363 ? 0.5016 0.5666 0.8505 0.0668  -0.1321 0.1217  363 LEU D CG  
8812  C CD1 . LEU D 363 ? 0.4762 0.5528 0.8300 0.0711  -0.1412 0.1273  363 LEU D CD1 
8813  C CD2 . LEU D 363 ? 0.5114 0.5923 0.8850 0.0695  -0.1227 0.1303  363 LEU D CD2 
8814  N N   . PHE D 364 ? 0.5226 0.5478 0.8145 0.0550  -0.1526 0.0997  364 PHE D N   
8815  C CA  . PHE D 364 ? 0.5261 0.5469 0.8105 0.0460  -0.1611 0.0948  364 PHE D CA  
8816  C C   . PHE D 364 ? 0.5262 0.5663 0.8243 0.0401  -0.1698 0.0976  364 PHE D C   
8817  O O   . PHE D 364 ? 0.5151 0.5644 0.8133 0.0405  -0.1772 0.0984  364 PHE D O   
8818  C CB  . PHE D 364 ? 0.5161 0.5220 0.7825 0.0464  -0.1658 0.0885  364 PHE D CB  
8819  C CG  . PHE D 364 ? 0.5222 0.5109 0.7746 0.0459  -0.1611 0.0850  364 PHE D CG  
8820  C CD1 . PHE D 364 ? 0.5268 0.5090 0.7722 0.0508  -0.1527 0.0849  364 PHE D CD1 
8821  C CD2 . PHE D 364 ? 0.5282 0.5078 0.7748 0.0400  -0.1645 0.0822  364 PHE D CD2 
8822  C CE1 . PHE D 364 ? 0.5362 0.5070 0.7679 0.0485  -0.1496 0.0827  364 PHE D CE1 
8823  C CE2 . PHE D 364 ? 0.5313 0.4990 0.7669 0.0399  -0.1610 0.0820  364 PHE D CE2 
8824  C CZ  . PHE D 364 ? 0.5347 0.4998 0.7621 0.0436  -0.1545 0.0825  364 PHE D CZ  
8825  N N   . LEU D 365 ? 0.5015 0.5491 0.8106 0.0334  -0.1689 0.0993  365 LEU D N   
8826  C CA  . LEU D 365 ? 0.5081 0.5753 0.8303 0.0249  -0.1768 0.1011  365 LEU D CA  
8827  C C   . LEU D 365 ? 0.5331 0.5915 0.8510 0.0129  -0.1797 0.0941  365 LEU D C   
8828  O O   . LEU D 365 ? 0.5459 0.6190 0.8729 0.0029  -0.1858 0.0934  365 LEU D O   
8829  C CB  . LEU D 365 ? 0.5074 0.5959 0.8522 0.0268  -0.1724 0.1109  365 LEU D CB  
8830  C CG  . LEU D 365 ? 0.4885 0.5900 0.8458 0.0385  -0.1679 0.1204  365 LEU D CG  
8831  C CD1 . LEU D 365 ? 0.4914 0.6146 0.8745 0.0396  -0.1626 0.1305  365 LEU D CD1 
8832  C CD2 . LEU D 365 ? 0.4713 0.5860 0.8278 0.0393  -0.1782 0.1232  365 LEU D CD2 
8833  N N   . ARG D 366 ? 0.5557 0.5915 0.8611 0.0132  -0.1752 0.0896  366 ARG D N   
8834  C CA  . ARG D 366 ? 0.5842 0.6093 0.8892 0.0036  -0.1747 0.0854  366 ARG D CA  
8835  C C   . ARG D 366 ? 0.6035 0.6279 0.9050 -0.0061 -0.1820 0.0772  366 ARG D C   
8836  O O   . ARG D 366 ? 0.5919 0.6215 0.8866 -0.0049 -0.1880 0.0743  366 ARG D O   
8837  C CB  . ARG D 366 ? 0.5844 0.5873 0.8770 0.0076  -0.1688 0.0849  366 ARG D CB  
8838  C CG  . ARG D 366 ? 0.5631 0.5547 0.8403 0.0146  -0.1706 0.0816  366 ARG D CG  
8839  C CD  . ARG D 366 ? 0.5630 0.5361 0.8301 0.0164  -0.1664 0.0821  366 ARG D CD  
8840  N NE  . ARG D 366 ? 0.5895 0.5550 0.8633 0.0091  -0.1640 0.0828  366 ARG D NE  
8841  C CZ  . ARG D 366 ? 0.6130 0.5694 0.8884 0.0027  -0.1657 0.0769  366 ARG D CZ  
8842  N NH1 . ARG D 366 ? 0.6149 0.5700 0.8839 0.0019  -0.1706 0.0693  366 ARG D NH1 
8843  N NH2 . ARG D 366 ? 0.6406 0.5884 0.9243 -0.0037 -0.1612 0.0783  366 ARG D NH2 
8844  N N   . ASP D 367 ? 0.5858 0.6033 0.8918 -0.0168 -0.1803 0.0731  367 ASP D N   
8845  C CA  . ASP D 367 ? 0.6175 0.6291 0.9190 -0.0285 -0.1839 0.0627  367 ASP D CA  
8846  C C   . ASP D 367 ? 0.6067 0.6428 0.9103 -0.0356 -0.1933 0.0603  367 ASP D C   
8847  O O   . ASP D 367 ? 0.6038 0.6398 0.8957 -0.0365 -0.1982 0.0547  367 ASP D O   
8848  C CB  . ASP D 367 ? 0.6262 0.6141 0.9125 -0.0243 -0.1817 0.0567  367 ASP D CB  
8849  C CG  . ASP D 367 ? 0.6746 0.6467 0.9590 -0.0364 -0.1789 0.0458  367 ASP D CG  
8850  O OD1 . ASP D 367 ? 0.6856 0.6684 0.9761 -0.0501 -0.1814 0.0401  367 ASP D OD1 
8851  O OD2 . ASP D 367 ? 0.6938 0.6430 0.9717 -0.0327 -0.1733 0.0431  367 ASP D OD2 
8852  N N   . ASN D 368 ? 0.6440 0.7036 0.9635 -0.0409 -0.1957 0.0660  368 ASN D N   
8853  C CA  . ASN D 368 ? 0.6323 0.7212 0.9571 -0.0495 -0.2055 0.0666  368 ASN D CA  
8854  C C   . ASN D 368 ? 0.6453 0.7499 0.9862 -0.0638 -0.2061 0.0666  368 ASN D C   
8855  O O   . ASN D 368 ? 0.6678 0.7559 1.0130 -0.0679 -0.1986 0.0640  368 ASN D O   
8856  C CB  . ASN D 368 ? 0.5936 0.7038 0.9250 -0.0363 -0.2090 0.0791  368 ASN D CB  
8857  C CG  . ASN D 368 ? 0.5797 0.6868 0.8956 -0.0302 -0.2135 0.0770  368 ASN D CG  
8858  O OD1 . ASN D 368 ? 0.5827 0.7047 0.8930 -0.0395 -0.2220 0.0734  368 ASN D OD1 
8859  N ND2 . ASN D 368 ? 0.5639 0.6529 0.8722 -0.0157 -0.2078 0.0793  368 ASN D ND2 
8860  N N   . GLN D 369 ? 0.6797 0.8179 1.0303 -0.0718 -0.2152 0.0708  369 GLN D N   
8861  C CA  . GLN D 369 ? 0.6856 0.8448 1.0533 -0.0863 -0.2172 0.0721  369 GLN D CA  
8862  C C   . GLN D 369 ? 0.6556 0.8491 1.0455 -0.0787 -0.2203 0.0890  369 GLN D C   
8863  O O   . GLN D 369 ? 0.6489 0.8744 1.0535 -0.0908 -0.2272 0.0931  369 GLN D O   
8864  C CB  . GLN D 369 ? 0.6987 0.8702 1.0589 -0.1082 -0.2253 0.0602  369 GLN D CB  
8865  C CG  . GLN D 369 ? 0.7326 0.8689 1.0766 -0.1189 -0.2184 0.0422  369 GLN D CG  
8866  C CD  . GLN D 369 ? 0.7456 0.8925 1.0786 -0.1417 -0.2248 0.0279  369 GLN D CD  
8867  O OE1 . GLN D 369 ? 0.7291 0.9129 1.0646 -0.1500 -0.2365 0.0323  369 GLN D OE1 
8868  N NE2 . GLN D 369 ? 0.7752 0.8906 1.0963 -0.1525 -0.2164 0.0112  369 GLN D NE2 
8869  N N   . LEU D 370 ? 0.6168 0.8041 1.0100 -0.0591 -0.2143 0.0989  370 LEU D N   
8870  C CA  . LEU D 370 ? 0.5908 0.8057 1.0070 -0.0495 -0.2133 0.1152  370 LEU D CA  
8871  C C   . LEU D 370 ? 0.6015 0.8230 1.0366 -0.0548 -0.2071 0.1189  370 LEU D C   
8872  O O   . LEU D 370 ? 0.6274 0.8255 1.0561 -0.0612 -0.2010 0.1104  370 LEU D O   
8873  C CB  . LEU D 370 ? 0.5732 0.7737 0.9860 -0.0286 -0.2053 0.1217  370 LEU D CB  
8874  C CG  . LEU D 370 ? 0.5613 0.7528 0.9555 -0.0223 -0.2101 0.1185  370 LEU D CG  
8875  C CD1 . LEU D 370 ? 0.5512 0.7181 0.9371 -0.0051 -0.1997 0.1198  370 LEU D CD1 
8876  C CD2 . LEU D 370 ? 0.5378 0.7650 0.9433 -0.0222 -0.2201 0.1296  370 LEU D CD2 
8877  N N   . SER D 371 ? 0.5547 0.8092 1.0151 -0.0516 -0.2080 0.1332  371 SER D N   
8878  C CA  . SER D 371 ? 0.5624 0.8309 1.0437 -0.0593 -0.2039 0.1375  371 SER D CA  
8879  C C   . SER D 371 ? 0.5410 0.8316 1.0484 -0.0451 -0.1971 0.1547  371 SER D C   
8880  O O   . SER D 371 ? 0.5199 0.8163 1.0307 -0.0302 -0.1958 0.1636  371 SER D O   
8881  C CB  . SER D 371 ? 0.5651 0.8612 1.0538 -0.0812 -0.2157 0.1343  371 SER D CB  
8882  O OG  . SER D 371 ? 0.5379 0.8723 1.0374 -0.0814 -0.2271 0.1452  371 SER D OG  
8883  N N   . GLY D 372 ? 0.5364 0.8379 1.0634 -0.0498 -0.1911 0.1595  372 GLY D N   
8884  C CA  . GLY D 372 ? 0.5200 0.8441 1.0755 -0.0382 -0.1830 0.1756  372 GLY D CA  
8885  C C   . GLY D 372 ? 0.5325 0.8283 1.0830 -0.0231 -0.1656 0.1754  372 GLY D C   
8886  O O   . GLY D 372 ? 0.5538 0.8146 1.0794 -0.0230 -0.1609 0.1637  372 GLY D O   
8887  N N   . PRO D 373 ? 0.4784 0.7901 1.0532 -0.0109 -0.1550 0.1887  373 PRO D N   
8888  C CA  . PRO D 373 ? 0.4937 0.7797 1.0626 0.0026  -0.1369 0.1875  373 PRO D CA  
8889  C C   . PRO D 373 ? 0.4854 0.7522 1.0378 0.0165  -0.1337 0.1853  373 PRO D C   
8890  O O   . PRO D 373 ? 0.4609 0.7422 1.0175 0.0207  -0.1424 0.1909  373 PRO D O   
8891  C CB  . PRO D 373 ? 0.4849 0.7979 1.0893 0.0096  -0.1259 0.2026  373 PRO D CB  
8892  C CG  . PRO D 373 ? 0.4517 0.8048 1.0800 0.0082  -0.1392 0.2157  373 PRO D CG  
8893  C CD  . PRO D 373 ? 0.4529 0.8086 1.0632 -0.0097 -0.1582 0.2059  373 PRO D CD  
8894  N N   . ILE D 374 ? 0.4902 0.7254 1.0234 0.0226  -0.1209 0.1773  374 ILE D N   
8895  C CA  . ILE D 374 ? 0.4890 0.7037 1.0058 0.0346  -0.1156 0.1738  374 ILE D CA  
8896  C C   . ILE D 374 ? 0.4902 0.7158 1.0313 0.0490  -0.1003 0.1851  374 ILE D C   
8897  O O   . ILE D 374 ? 0.4955 0.7189 1.0466 0.0514  -0.0847 0.1867  374 ILE D O   
8898  C CB  . ILE D 374 ? 0.4932 0.6724 0.9789 0.0332  -0.1087 0.1608  374 ILE D CB  
8899  C CG1 . ILE D 374 ? 0.4921 0.6579 0.9547 0.0230  -0.1232 0.1510  374 ILE D CG1 
8900  C CG2 . ILE D 374 ? 0.4948 0.6553 0.9687 0.0454  -0.0976 0.1580  374 ILE D CG2 
8901  C CD1 . ILE D 374 ? 0.4874 0.6567 0.9438 0.0256  -0.1350 0.1503  374 ILE D CD1 
8902  N N   . PRO D 375 ? 0.4896 0.7268 1.0417 0.0589  -0.1029 0.1936  375 PRO D N   
8903  C CA  . PRO D 375 ? 0.4832 0.7295 1.0623 0.0737  -0.0861 0.2058  375 PRO D CA  
8904  C C   . PRO D 375 ? 0.5123 0.7245 1.0742 0.0811  -0.0660 0.1956  375 PRO D C   
8905  O O   . PRO D 375 ? 0.5238 0.7090 1.0535 0.0788  -0.0688 0.1826  375 PRO D O   
8906  C CB  . PRO D 375 ? 0.4494 0.7135 1.0398 0.0813  -0.0958 0.2171  375 PRO D CB  
8907  C CG  . PRO D 375 ? 0.4397 0.7108 1.0116 0.0679  -0.1190 0.2113  375 PRO D CG  
8908  C CD  . PRO D 375 ? 0.4662 0.7085 1.0075 0.0569  -0.1200 0.1932  375 PRO D CD  
8909  N N   . PRO D 376 ? 0.5101 0.7231 1.0924 0.0894  -0.0448 0.2009  376 PRO D N   
8910  C CA  . PRO D 376 ? 0.5463 0.7269 1.1101 0.0940  -0.0239 0.1893  376 PRO D CA  
8911  C C   . PRO D 376 ? 0.5398 0.7010 1.0899 0.1023  -0.0211 0.1851  376 PRO D C   
8912  O O   . PRO D 376 ? 0.5733 0.7061 1.1016 0.1027  -0.0066 0.1725  376 PRO D O   
8913  C CB  . PRO D 376 ? 0.5562 0.7469 1.1524 0.1025  -0.0010 0.1984  376 PRO D CB  
8914  C CG  . PRO D 376 ? 0.5323 0.7587 1.1578 0.0985  -0.0117 0.2122  376 PRO D CG  
8915  C CD  . PRO D 376 ? 0.4959 0.7401 1.1195 0.0943  -0.0378 0.2175  376 PRO D CD  
8916  N N   . GLY D 377 ? 0.5789 0.7555 1.1403 0.1078  -0.0342 0.1952  377 GLY D N   
8917  C CA  . GLY D 377 ? 0.5711 0.7302 1.1215 0.1160  -0.0312 0.1927  377 GLY D CA  
8918  C C   . GLY D 377 ? 0.5786 0.7150 1.0890 0.1076  -0.0440 0.1772  377 GLY D C   
8919  O O   . GLY D 377 ? 0.5805 0.6975 1.0777 0.1130  -0.0386 0.1720  377 GLY D O   
8920  N N   . ILE D 378 ? 0.5787 0.7171 1.0716 0.0947  -0.0598 0.1703  378 ILE D N   
8921  C CA  . ILE D 378 ? 0.5803 0.6990 1.0388 0.0876  -0.0720 0.1576  378 ILE D CA  
8922  C C   . ILE D 378 ? 0.6157 0.7039 1.0496 0.0877  -0.0574 0.1445  378 ILE D C   
8923  O O   . ILE D 378 ? 0.6129 0.6846 1.0293 0.0903  -0.0581 0.1384  378 ILE D O   
8924  C CB  . ILE D 378 ? 0.5807 0.7051 1.0284 0.0741  -0.0877 0.1532  378 ILE D CB  
8925  C CG1 . ILE D 378 ? 0.5484 0.6989 1.0099 0.0708  -0.1061 0.1617  378 ILE D CG1 
8926  C CG2 . ILE D 378 ? 0.5915 0.6906 1.0046 0.0675  -0.0935 0.1396  378 ILE D CG2 
8927  C CD1 . ILE D 378 ? 0.5508 0.6994 0.9958 0.0568  -0.1215 0.1537  378 ILE D CD1 
8928  N N   . ALA D 379 ? 0.5643 0.6461 0.9955 0.0835  -0.0441 0.1398  379 ALA D N   
8929  C CA  . ALA D 379 ? 0.6084 0.6648 1.0144 0.0805  -0.0301 0.1270  379 ALA D CA  
8930  C C   . ALA D 379 ? 0.6295 0.6767 1.0473 0.0896  -0.0062 0.1267  379 ALA D C   
8931  O O   . ALA D 379 ? 0.6778 0.7070 1.0781 0.0852  0.0098  0.1156  379 ALA D O   
8932  C CB  . ALA D 379 ? 0.6452 0.6995 1.0385 0.0696  -0.0278 0.1220  379 ALA D CB  
8933  N N   . ASN D 380 ? 0.6392 0.6987 1.0863 0.1015  -0.0029 0.1387  380 ASN D N   
8934  C CA  . ASN D 380 ? 0.6525 0.7038 1.1182 0.1119  0.0224  0.1409  380 ASN D CA  
8935  C C   . ASN D 380 ? 0.6729 0.6962 1.1171 0.1131  0.0333  0.1289  380 ASN D C   
8936  O O   . ASN D 380 ? 0.7020 0.7095 1.1510 0.1167  0.0585  0.1236  380 ASN D O   
8937  C CB  . ASN D 380 ? 0.6058 0.6815 1.1119 0.1251  0.0210  0.1608  380 ASN D CB  
8938  C CG  . ASN D 380 ? 0.6144 0.6862 1.1495 0.1369  0.0494  0.1669  380 ASN D CG  
8939  O OD1 . ASN D 380 ? 0.6530 0.7140 1.1865 0.1339  0.0692  0.1589  380 ASN D OD1 
8940  N ND2 . ASN D 380 ? 0.5784 0.6595 1.1412 0.1507  0.0525  0.1820  380 ASN D ND2 
8941  N N   . SER D 381 ? 0.5976 0.6140 1.0191 0.1096  0.0162  0.1241  381 SER D N   
8942  C CA  . SER D 381 ? 0.6162 0.6074 1.0177 0.1097  0.0255  0.1130  381 SER D CA  
8943  C C   . SER D 381 ? 0.6785 0.6497 1.0506 0.0977  0.0387  0.0954  381 SER D C   
8944  O O   . SER D 381 ? 0.6997 0.6746 1.0527 0.0867  0.0283  0.0905  381 SER D O   
8945  C CB  . SER D 381 ? 0.5860 0.5769 0.9700 0.1079  0.0031  0.1123  381 SER D CB  
8946  O OG  . SER D 381 ? 0.6105 0.5774 0.9708 0.1049  0.0106  0.0997  381 SER D OG  
8947  N N   . THR D 382 ? 0.5947 0.5452 0.9637 0.0990  0.0624  0.0863  382 THR D N   
8948  C CA  . THR D 382 ? 0.6584 0.5905 0.9954 0.0851  0.0747  0.0681  382 THR D CA  
8949  C C   . THR D 382 ? 0.6699 0.5941 0.9727 0.0753  0.0581  0.0589  382 THR D C   
8950  O O   . THR D 382 ? 0.7223 0.6406 0.9960 0.0613  0.0593  0.0472  382 THR D O   
8951  C CB  . THR D 382 ? 0.6850 0.5957 1.0277 0.0876  0.1065  0.0591  382 THR D CB  
8952  O OG1 . THR D 382 ? 0.6413 0.5468 1.0058 0.1014  0.1105  0.0672  382 THR D OG1 
8953  C CG2 . THR D 382 ? 0.6977 0.6138 1.0636 0.0911  0.1270  0.0626  382 THR D CG2 
8954  N N   . GLU D 383 ? 0.6656 0.5916 0.9719 0.0820  0.0428  0.0649  383 GLU D N   
8955  C CA  . GLU D 383 ? 0.6681 0.5879 0.9461 0.0744  0.0268  0.0580  383 GLU D CA  
8956  C C   . GLU D 383 ? 0.6394 0.5754 0.9109 0.0708  0.0008  0.0644  383 GLU D C   
8957  O O   . GLU D 383 ? 0.6337 0.5664 0.8848 0.0655  -0.0131 0.0604  383 GLU D O   
8958  C CB  . GLU D 383 ? 0.6336 0.5449 0.9180 0.0832  0.0260  0.0603  383 GLU D CB  
8959  C CG  . GLU D 383 ? 0.6457 0.5403 0.9443 0.0897  0.0529  0.0572  383 GLU D CG  
8960  C CD  . GLU D 383 ? 0.7099 0.5846 0.9845 0.0766  0.0734  0.0384  383 GLU D CD  
8961  O OE1 . GLU D 383 ? 0.7332 0.5975 0.9802 0.0664  0.0692  0.0271  383 GLU D OE1 
8962  O OE2 . GLU D 383 ? 0.7367 0.6073 1.0198 0.0756  0.0943  0.0348  383 GLU D OE2 
8963  N N   . LEU D 384 ? 0.5815 0.5346 0.8713 0.0734  -0.0051 0.0741  384 LEU D N   
8964  C CA  . LEU D 384 ? 0.5509 0.5169 0.8360 0.0693  -0.0275 0.0792  384 LEU D CA  
8965  C C   . LEU D 384 ? 0.5909 0.5516 0.8474 0.0564  -0.0313 0.0712  384 LEU D C   
8966  O O   . LEU D 384 ? 0.6464 0.6039 0.8940 0.0494  -0.0179 0.0656  384 LEU D O   
8967  C CB  . LEU D 384 ? 0.5327 0.5177 0.8431 0.0726  -0.0306 0.0901  384 LEU D CB  
8968  C CG  . LEU D 384 ? 0.5101 0.5080 0.8207 0.0693  -0.0530 0.0957  384 LEU D CG  
8969  C CD1 . LEU D 384 ? 0.4989 0.5029 0.8187 0.0764  -0.0657 0.1015  384 LEU D CD1 
8970  C CD2 . LEU D 384 ? 0.5073 0.5220 0.8361 0.0671  -0.0543 0.1030  384 LEU D CD2 
8971  N N   . THR D 385 ? 0.5824 0.5435 0.8252 0.0531  -0.0490 0.0714  385 THR D N   
8972  C CA  . THR D 385 ? 0.6136 0.5718 0.8313 0.0419  -0.0539 0.0667  385 THR D CA  
8973  C C   . THR D 385 ? 0.5725 0.5400 0.7918 0.0396  -0.0715 0.0739  385 THR D C   
8974  O O   . THR D 385 ? 0.5948 0.5647 0.8015 0.0313  -0.0739 0.0747  385 THR D O   
8975  C CB  . THR D 385 ? 0.6264 0.5734 0.8237 0.0390  -0.0550 0.0591  385 THR D CB  
8976  O OG1 . THR D 385 ? 0.5712 0.5174 0.7760 0.0469  -0.0669 0.0625  385 THR D OG1 
8977  C CG2 . THR D 385 ? 0.6787 0.6139 0.8712 0.0379  -0.0349 0.0497  385 THR D CG2 
8978  N N   . VAL D 386 ? 0.6217 0.5944 0.8558 0.0462  -0.0832 0.0792  386 VAL D N   
8979  C CA  . VAL D 386 ? 0.5857 0.5640 0.8219 0.0435  -0.0982 0.0841  386 VAL D CA  
8980  C C   . VAL D 386 ? 0.5570 0.5476 0.8170 0.0476  -0.1026 0.0903  386 VAL D C   
8981  O O   . VAL D 386 ? 0.5348 0.5294 0.8065 0.0546  -0.1036 0.0922  386 VAL D O   
8982  C CB  . VAL D 386 ? 0.5538 0.5252 0.7783 0.0441  -0.1099 0.0821  386 VAL D CB  
8983  C CG1 . VAL D 386 ? 0.5244 0.4989 0.7523 0.0410  -0.1224 0.0861  386 VAL D CG1 
8984  C CG2 . VAL D 386 ? 0.5839 0.5468 0.7863 0.0394  -0.1061 0.0769  386 VAL D CG2 
8985  N N   . LEU D 387 ? 0.5550 0.5531 0.8224 0.0425  -0.1056 0.0945  387 LEU D N   
8986  C CA  . LEU D 387 ? 0.5361 0.5486 0.8259 0.0435  -0.1102 0.1002  387 LEU D CA  
8987  C C   . LEU D 387 ? 0.5249 0.5381 0.8141 0.0363  -0.1212 0.1014  387 LEU D C   
8988  O O   . LEU D 387 ? 0.5453 0.5592 0.8348 0.0305  -0.1183 0.1037  387 LEU D O   
8989  C CB  . LEU D 387 ? 0.5627 0.5848 0.8680 0.0442  -0.0977 0.1041  387 LEU D CB  
8990  C CG  . LEU D 387 ? 0.5461 0.5873 0.8774 0.0447  -0.1018 0.1115  387 LEU D CG  
8991  C CD1 . LEU D 387 ? 0.5125 0.5628 0.8551 0.0513  -0.1091 0.1147  387 LEU D CD1 
8992  C CD2 . LEU D 387 ? 0.5736 0.6237 0.9208 0.0462  -0.0873 0.1156  387 LEU D CD2 
8993  N N   . GLN D 388 ? 0.5791 0.5912 0.8672 0.0363  -0.1326 0.0997  388 GLN D N   
8994  C CA  . GLN D 388 ? 0.5758 0.5856 0.8642 0.0293  -0.1413 0.0991  388 GLN D CA  
8995  C C   . GLN D 388 ? 0.5744 0.6001 0.8816 0.0255  -0.1465 0.1014  388 GLN D C   
8996  O O   . GLN D 388 ? 0.5579 0.5934 0.8709 0.0282  -0.1521 0.1015  388 GLN D O   
8997  C CB  . GLN D 388 ? 0.5579 0.5558 0.8327 0.0301  -0.1488 0.0943  388 GLN D CB  
8998  C CG  . GLN D 388 ? 0.5557 0.5420 0.8131 0.0341  -0.1449 0.0923  388 GLN D CG  
8999  C CD  . GLN D 388 ? 0.5673 0.5451 0.8154 0.0296  -0.1436 0.0945  388 GLN D CD  
9000  O OE1 . GLN D 388 ? 0.5688 0.5433 0.8216 0.0252  -0.1474 0.0962  388 GLN D OE1 
9001  N NE2 . GLN D 388 ? 0.5810 0.5558 0.8163 0.0302  -0.1377 0.0950  388 GLN D NE2 
9002  N N   . LEU D 389 ? 0.5606 0.5907 0.8774 0.0184  -0.1450 0.1040  389 LEU D N   
9003  C CA  . LEU D 389 ? 0.5647 0.6126 0.9004 0.0128  -0.1494 0.1063  389 LEU D CA  
9004  C C   . LEU D 389 ? 0.5869 0.6302 0.9252 0.0016  -0.1531 0.1038  389 LEU D C   
9005  O O   . LEU D 389 ? 0.5967 0.6551 0.9502 -0.0058 -0.1564 0.1049  389 LEU D O   
9006  C CB  . LEU D 389 ? 0.5720 0.6356 0.9246 0.0154  -0.1410 0.1133  389 LEU D CB  
9007  C CG  . LEU D 389 ? 0.5585 0.6280 0.9149 0.0263  -0.1348 0.1165  389 LEU D CG  
9008  C CD1 . LEU D 389 ? 0.5734 0.6554 0.9474 0.0288  -0.1234 0.1230  389 LEU D CD1 
9009  C CD2 . LEU D 389 ? 0.5331 0.6164 0.8973 0.0290  -0.1441 0.1183  389 LEU D CD2 
9010  N N   . ASP D 390 ? 0.6103 0.6338 0.9356 -0.0001 -0.1521 0.1011  390 ASP D N   
9011  C CA  . ASP D 390 ? 0.6390 0.6544 0.9687 -0.0098 -0.1523 0.0996  390 ASP D CA  
9012  C C   . ASP D 390 ? 0.6510 0.6686 0.9837 -0.0179 -0.1602 0.0919  390 ASP D C   
9013  O O   . ASP D 390 ? 0.6324 0.6561 0.9602 -0.0153 -0.1666 0.0881  390 ASP D O   
9014  C CB  . ASP D 390 ? 0.6416 0.6362 0.9589 -0.0079 -0.1487 0.1009  390 ASP D CB  
9015  C CG  . ASP D 390 ? 0.6221 0.6051 0.9256 -0.0031 -0.1533 0.0955  390 ASP D CG  
9016  O OD1 . ASP D 390 ? 0.5963 0.5815 0.8903 0.0049  -0.1539 0.0956  390 ASP D OD1 
9017  O OD2 . ASP D 390 ? 0.6374 0.6085 0.9404 -0.0078 -0.1552 0.0906  390 ASP D OD2 
9018  N N   . THR D 391 ? 0.6217 0.6342 0.9622 -0.0289 -0.1589 0.0894  391 THR D N   
9019  C CA  . THR D 391 ? 0.6434 0.6548 0.9850 -0.0402 -0.1642 0.0796  391 THR D CA  
9020  C C   . THR D 391 ? 0.6206 0.6591 0.9691 -0.0445 -0.1727 0.0783  391 THR D C   
9021  O O   . THR D 391 ? 0.6083 0.6513 0.9483 -0.0446 -0.1796 0.0731  391 THR D O   
9022  C CB  . THR D 391 ? 0.6517 0.6423 0.9780 -0.0376 -0.1650 0.0725  391 THR D CB  
9023  O OG1 . THR D 391 ? 0.6519 0.6232 0.9734 -0.0305 -0.1578 0.0781  391 THR D OG1 
9024  C CG2 . THR D 391 ? 0.6800 0.6621 1.0072 -0.0517 -0.1654 0.0612  391 THR D CG2 
9025  N N   . ASN D 392 ? 0.6624 0.7209 1.0276 -0.0480 -0.1719 0.0847  392 ASN D N   
9026  C CA  . ASN D 392 ? 0.6401 0.7297 1.0174 -0.0520 -0.1796 0.0875  392 ASN D CA  
9027  C C   . ASN D 392 ? 0.6510 0.7552 1.0472 -0.0638 -0.1778 0.0902  392 ASN D C   
9028  O O   . ASN D 392 ? 0.6766 0.7640 1.0741 -0.0709 -0.1714 0.0871  392 ASN D O   
9029  C CB  . ASN D 392 ? 0.6074 0.7104 0.9878 -0.0367 -0.1791 0.0972  392 ASN D CB  
9030  C CG  . ASN D 392 ? 0.5868 0.6885 0.9536 -0.0299 -0.1852 0.0945  392 ASN D CG  
9031  O OD1 . ASN D 392 ? 0.5792 0.6984 0.9470 -0.0363 -0.1945 0.0928  392 ASN D OD1 
9032  N ND2 . ASN D 392 ? 0.5770 0.6593 0.9303 -0.0179 -0.1802 0.0946  392 ASN D ND2 
9033  N N   . ASN D 393 ? 0.6473 0.7840 1.0600 -0.0660 -0.1830 0.0970  393 ASN D N   
9034  C CA  . ASN D 393 ? 0.6519 0.8072 1.0853 -0.0769 -0.1816 0.1010  393 ASN D CA  
9035  C C   . ASN D 393 ? 0.6302 0.8101 1.0829 -0.0661 -0.1785 0.1152  393 ASN D C   
9036  O O   . ASN D 393 ? 0.6166 0.8283 1.0897 -0.0725 -0.1830 0.1218  393 ASN D O   
9037  C CB  . ASN D 393 ? 0.6515 0.8267 1.0896 -0.0961 -0.1916 0.0941  393 ASN D CB  
9038  C CG  . ASN D 393 ? 0.6740 0.8232 1.0925 -0.1070 -0.1925 0.0783  393 ASN D CG  
9039  O OD1 . ASN D 393 ? 0.6963 0.8284 1.1157 -0.1191 -0.1867 0.0706  393 ASN D OD1 
9040  N ND2 . ASN D 393 ? 0.6672 0.8125 1.0692 -0.1024 -0.1984 0.0736  393 ASN D ND2 
9041  N N   . PHE D 394 ? 0.6294 0.7952 1.0762 -0.0501 -0.1698 0.1201  394 PHE D N   
9042  C CA  . PHE D 394 ? 0.6145 0.7985 1.0793 -0.0396 -0.1629 0.1321  394 PHE D CA  
9043  C C   . PHE D 394 ? 0.6316 0.8206 1.1122 -0.0459 -0.1548 0.1363  394 PHE D C   
9044  O O   . PHE D 394 ? 0.6561 0.8276 1.1302 -0.0551 -0.1521 0.1306  394 PHE D O   
9045  C CB  . PHE D 394 ? 0.6096 0.7749 1.0612 -0.0231 -0.1542 0.1335  394 PHE D CB  
9046  C CG  . PHE D 394 ? 0.5873 0.7508 1.0273 -0.0152 -0.1607 0.1317  394 PHE D CG  
9047  C CD1 . PHE D 394 ? 0.5627 0.7542 1.0168 -0.0140 -0.1688 0.1384  394 PHE D CD1 
9048  C CD2 . PHE D 394 ? 0.5899 0.7257 1.0058 -0.0093 -0.1590 0.1246  394 PHE D CD2 
9049  C CE1 . PHE D 394 ? 0.5434 0.7335 0.9869 -0.0069 -0.1744 0.1379  394 PHE D CE1 
9050  C CE2 . PHE D 394 ? 0.5689 0.7027 0.9744 -0.0025 -0.1644 0.1230  394 PHE D CE2 
9051  C CZ  . PHE D 394 ? 0.5470 0.7071 0.9659 -0.0011 -0.1718 0.1295  394 PHE D CZ  
9052  N N   . THR D 395 ? 0.5784 0.7920 1.0818 -0.0405 -0.1498 0.1473  395 THR D N   
9053  C CA  . THR D 395 ? 0.5909 0.8139 1.1126 -0.0458 -0.1415 0.1528  395 THR D CA  
9054  C C   . THR D 395 ? 0.5891 0.8165 1.1213 -0.0313 -0.1276 0.1619  395 THR D C   
9055  O O   . THR D 395 ? 0.5755 0.8018 1.1045 -0.0180 -0.1249 0.1644  395 THR D O   
9056  C CB  . THR D 395 ? 0.5769 0.8343 1.1232 -0.0592 -0.1503 0.1572  395 THR D CB  
9057  O OG1 . THR D 395 ? 0.5470 0.8353 1.1115 -0.0510 -0.1545 0.1680  395 THR D OG1 
9058  C CG2 . THR D 395 ? 0.5828 0.8355 1.1172 -0.0758 -0.1625 0.1459  395 THR D CG2 
9059  N N   . GLY D 396 ? 0.5511 0.7820 1.0956 -0.0344 -0.1172 0.1662  396 GLY D N   
9060  C CA  . GLY D 396 ? 0.5528 0.7915 1.1112 -0.0229 -0.1022 0.1746  396 GLY D CA  
9061  C C   . GLY D 396 ? 0.5772 0.7867 1.1119 -0.0143 -0.0893 0.1698  396 GLY D C   
9062  O O   . GLY D 396 ? 0.5974 0.7821 1.1076 -0.0187 -0.0906 0.1625  396 GLY D O   
9063  N N   . PHE D 397 ? 0.5835 0.7972 1.1268 -0.0022 -0.0758 0.1746  397 PHE D N   
9064  C CA  . PHE D 397 ? 0.6151 0.8061 1.1386 0.0039  -0.0604 0.1702  397 PHE D CA  
9065  C C   . PHE D 397 ? 0.6091 0.7837 1.1133 0.0136  -0.0610 0.1644  397 PHE D C   
9066  O O   . PHE D 397 ? 0.5777 0.7623 1.0910 0.0195  -0.0690 0.1669  397 PHE D O   
9067  C CB  . PHE D 397 ? 0.6280 0.8308 1.1720 0.0098  -0.0413 0.1769  397 PHE D CB  
9068  C CG  . PHE D 397 ? 0.6336 0.8523 1.1968 0.0006  -0.0381 0.1829  397 PHE D CG  
9069  C CD1 . PHE D 397 ? 0.6038 0.8496 1.1940 -0.0056 -0.0494 0.1901  397 PHE D CD1 
9070  C CD2 . PHE D 397 ? 0.6688 0.8772 1.2229 -0.0029 -0.0235 0.1818  397 PHE D CD2 
9071  C CE1 . PHE D 397 ? 0.6075 0.8681 1.2162 -0.0149 -0.0460 0.1955  397 PHE D CE1 
9072  C CE2 . PHE D 397 ? 0.6704 0.8932 1.2428 -0.0114 -0.0197 0.1879  397 PHE D CE2 
9073  C CZ  . PHE D 397 ? 0.6392 0.8875 1.2395 -0.0172 -0.0308 0.1945  397 PHE D CZ  
9074  N N   . LEU D 398 ? 0.6071 0.7575 1.0841 0.0145  -0.0525 0.1572  398 LEU D N   
9075  C CA  . LEU D 398 ? 0.6074 0.7421 1.0667 0.0231  -0.0491 0.1512  398 LEU D CA  
9076  C C   . LEU D 398 ? 0.6143 0.7549 1.0902 0.0337  -0.0312 0.1545  398 LEU D C   
9077  O O   . LEU D 398 ? 0.6420 0.7865 1.1267 0.0330  -0.0156 0.1566  398 LEU D O   
9078  C CB  . LEU D 398 ? 0.6426 0.7534 1.0683 0.0187  -0.0457 0.1431  398 LEU D CB  
9079  C CG  . LEU D 398 ? 0.6346 0.7347 1.0424 0.0109  -0.0610 0.1403  398 LEU D CG  
9080  C CD1 . LEU D 398 ? 0.6636 0.7439 1.0404 0.0090  -0.0571 0.1347  398 LEU D CD1 
9081  C CD2 . LEU D 398 ? 0.5918 0.6941 1.0027 0.0132  -0.0768 0.1388  398 LEU D CD2 
9082  N N   . PRO D 399 ? 0.6435 0.7843 1.1249 0.0437  -0.0316 0.1553  399 PRO D N   
9083  C CA  . PRO D 399 ? 0.6503 0.7937 1.1496 0.0549  -0.0120 0.1588  399 PRO D CA  
9084  C C   . PRO D 399 ? 0.7026 0.8219 1.1778 0.0543  0.0072  0.1479  399 PRO D C   
9085  O O   . PRO D 399 ? 0.7269 0.8275 1.1694 0.0477  0.0026  0.1382  399 PRO D O   
9086  C CB  . PRO D 399 ? 0.6116 0.7581 1.1185 0.0647  -0.0195 0.1624  399 PRO D CB  
9087  C CG  . PRO D 399 ? 0.5797 0.7355 1.0815 0.0575  -0.0443 0.1636  399 PRO D CG  
9088  C CD  . PRO D 399 ? 0.6066 0.7471 1.0818 0.0455  -0.0493 0.1545  399 PRO D CD  
9089  N N   . ASP D 400 ? 0.7155 0.8366 1.2080 0.0607  0.0297  0.1499  400 ASP D N   
9090  C CA  . ASP D 400 ? 0.7722 0.8721 1.2430 0.0583  0.0512  0.1383  400 ASP D CA  
9091  C C   . ASP D 400 ? 0.7811 0.8599 1.2344 0.0635  0.0572  0.1292  400 ASP D C   
9092  O O   . ASP D 400 ? 0.8325 0.8927 1.2643 0.0595  0.0749  0.1174  400 ASP D O   
9093  C CB  . ASP D 400 ? 0.7863 0.8937 1.2826 0.0629  0.0760  0.1424  400 ASP D CB  
9094  C CG  . ASP D 400 ? 0.7824 0.9102 1.2951 0.0567  0.0723  0.1509  400 ASP D CG  
9095  O OD1 . ASP D 400 ? 0.7372 0.8890 1.2818 0.0610  0.0616  0.1639  400 ASP D OD1 
9096  O OD2 . ASP D 400 ? 0.8242 0.9453 1.3181 0.0467  0.0803  0.1450  400 ASP D OD2 
9097  N N   . THR D 401 ? 0.7069 0.7890 1.1686 0.0711  0.0437  0.1339  401 THR D N   
9098  C CA  . THR D 401 ? 0.7086 0.7713 1.1550 0.0759  0.0476  0.1262  401 THR D CA  
9099  C C   . THR D 401 ? 0.7203 0.7687 1.1291 0.0667  0.0314  0.1163  401 THR D C   
9100  O O   . THR D 401 ? 0.7123 0.7475 1.1090 0.0701  0.0296  0.1110  401 THR D O   
9101  C CB  . THR D 401 ? 0.6512 0.7262 1.1263 0.0892  0.0414  0.1382  401 THR D CB  
9102  O OG1 . THR D 401 ? 0.6089 0.7016 1.0874 0.0862  0.0148  0.1457  401 THR D OG1 
9103  C CG2 . THR D 401 ? 0.6376 0.7286 1.1533 0.0996  0.0585  0.1505  401 THR D CG2 
9104  N N   . ILE D 402 ? 0.7140 0.7651 1.1059 0.0555  0.0207  0.1146  402 ILE D N   
9105  C CA  . ILE D 402 ? 0.7043 0.7480 1.0699 0.0487  0.0011  0.1104  402 ILE D CA  
9106  C C   . ILE D 402 ? 0.7383 0.7613 1.0743 0.0461  0.0072  0.0985  402 ILE D C   
9107  O O   . ILE D 402 ? 0.7098 0.7263 1.0350 0.0479  -0.0054 0.0964  402 ILE D O   
9108  C CB  . ILE D 402 ? 0.7208 0.7701 1.0768 0.0377  -0.0070 0.1124  402 ILE D CB  
9109  C CG1 . ILE D 402 ? 0.7024 0.7445 1.0359 0.0320  -0.0260 0.1101  402 ILE D CG1 
9110  C CG2 . ILE D 402 ? 0.7898 0.8340 1.1324 0.0304  0.0112  0.1073  402 ILE D CG2 
9111  C CD1 . ILE D 402 ? 0.6406 0.6870 0.9845 0.0376  -0.0431 0.1135  402 ILE D CD1 
9112  N N   . CYS D 403 ? 0.6779 0.6909 1.0001 0.0410  0.0270  0.0900  403 CYS D N   
9113  C CA  . CYS D 403 ? 0.7216 0.7167 1.0137 0.0354  0.0335  0.0774  403 CYS D CA  
9114  C C   . CYS D 403 ? 0.7523 0.7356 1.0505 0.0393  0.0600  0.0696  403 CYS D C   
9115  O O   . CYS D 403 ? 0.8179 0.7896 1.0934 0.0298  0.0762  0.0576  403 CYS D O   
9116  C CB  . CYS D 403 ? 0.7803 0.7741 1.0411 0.0206  0.0307  0.0726  403 CYS D CB  
9117  S SG  . CYS D 403 ? 0.8223 0.8007 1.0450 0.0116  0.0298  0.0597  403 CYS D SG  
9118  N N   . ARG D 404 ? 0.7583 0.7451 1.0885 0.0532  0.0653  0.0770  404 ARG D N   
9119  C CA  . ARG D 404 ? 0.7727 0.7486 1.1173 0.0595  0.0932  0.0724  404 ARG D CA  
9120  C C   . ARG D 404 ? 0.8066 0.7589 1.1254 0.0545  0.1051  0.0570  404 ARG D C   
9121  O O   . ARG D 404 ? 0.8526 0.7908 1.1621 0.0488  0.1303  0.0450  404 ARG D O   
9122  C CB  . ARG D 404 ? 0.7066 0.6934 1.0921 0.0764  0.0930  0.0870  404 ARG D CB  
9123  C CG  . ARG D 404 ? 0.7105 0.6876 1.1191 0.0856  0.1232  0.0861  404 ARG D CG  
9124  C CD  . ARG D 404 ? 0.6507 0.6486 1.1058 0.1017  0.1219  0.1060  404 ARG D CD  
9125  N NE  . ARG D 404 ? 0.6027 0.6014 1.0696 0.1125  0.1116  0.1142  404 ARG D NE  
9126  C CZ  . ARG D 404 ? 0.6033 0.5812 1.0690 0.1182  0.1271  0.1086  404 ARG D CZ  
9127  N NH1 . ARG D 404 ? 0.6479 0.6011 1.1008 0.1135  0.1546  0.0931  404 ARG D NH1 
9128  N NH2 . ARG D 404 ? 0.5588 0.5405 1.0362 0.1279  0.1156  0.1185  404 ARG D NH2 
9129  N N   . GLY D 405 ? 0.6785 0.6259 0.9850 0.0554  0.0883  0.0561  405 GLY D N   
9130  C CA  . GLY D 405 ? 0.7071 0.6335 0.9897 0.0497  0.0982  0.0417  405 GLY D CA  
9131  C C   . GLY D 405 ? 0.7724 0.6939 1.0140 0.0312  0.0952  0.0289  405 GLY D C   
9132  O O   . GLY D 405 ? 0.7994 0.7051 1.0189 0.0236  0.1041  0.0156  405 GLY D O   
9133  N N   . GLY D 406 ? 0.6906 0.6268 0.9224 0.0234  0.0827  0.0336  406 GLY D N   
9134  C CA  . GLY D 406 ? 0.7403 0.6764 0.9349 0.0061  0.0784  0.0250  406 GLY D CA  
9135  C C   . GLY D 406 ? 0.7265 0.6609 0.9010 0.0022  0.0587  0.0238  406 GLY D C   
9136  O O   . GLY D 406 ? 0.7630 0.6950 0.9063 -0.0123 0.0595  0.0146  406 GLY D O   
9137  N N   . LYS D 407 ? 0.7558 0.6931 0.9472 0.0142  0.0413  0.0332  407 LYS D N   
9138  C CA  . LYS D 407 ? 0.7350 0.6706 0.9110 0.0124  0.0232  0.0329  407 LYS D CA  
9139  C C   . LYS D 407 ? 0.6804 0.6293 0.8639 0.0165  -0.0016 0.0457  407 LYS D C   
9140  O O   . LYS D 407 ? 0.6471 0.5947 0.8231 0.0175  -0.0166 0.0470  407 LYS D O   
9141  C CB  . LYS D 407 ? 0.6990 0.6215 0.8851 0.0221  0.0279  0.0295  407 LYS D CB  
9142  C CG  . LYS D 407 ? 0.7387 0.6437 0.9175 0.0178  0.0538  0.0155  407 LYS D CG  
9143  C CD  . LYS D 407 ? 0.6998 0.5915 0.8868 0.0266  0.0559  0.0136  407 LYS D CD  
9144  C CE  . LYS D 407 ? 0.7263 0.5974 0.9102 0.0233  0.0845  -0.0004 407 LYS D CE  
9145  N NZ  . LYS D 407 ? 0.6902 0.5476 0.8807 0.0309  0.0862  -0.0016 407 LYS D NZ  
9146  N N   . LEU D 408 ? 0.6875 0.6482 0.8859 0.0183  -0.0050 0.0546  408 LEU D N   
9147  C CA  . LEU D 408 ? 0.6244 0.5954 0.8319 0.0215  -0.0261 0.0654  408 LEU D CA  
9148  C C   . LEU D 408 ? 0.6403 0.6146 0.8245 0.0109  -0.0373 0.0668  408 LEU D C   
9149  O O   . LEU D 408 ? 0.6962 0.6751 0.8667 0.0010  -0.0308 0.0662  408 LEU D O   
9150  C CB  . LEU D 408 ? 0.6043 0.5870 0.8357 0.0251  -0.0252 0.0741  408 LEU D CB  
9151  C CG  . LEU D 408 ? 0.5444 0.5363 0.7896 0.0287  -0.0448 0.0837  408 LEU D CG  
9152  C CD1 . LEU D 408 ? 0.5316 0.5236 0.7930 0.0391  -0.0517 0.0857  408 LEU D CD1 
9153  C CD2 . LEU D 408 ? 0.5428 0.5472 0.8056 0.0272  -0.0436 0.0912  408 LEU D CD2 
9154  N N   . GLU D 409 ? 0.6774 0.6504 0.8577 0.0133  -0.0535 0.0696  409 GLU D N   
9155  C CA  . GLU D 409 ? 0.6750 0.6519 0.8374 0.0054  -0.0648 0.0734  409 GLU D CA  
9156  C C   . GLU D 409 ? 0.6201 0.6040 0.7952 0.0073  -0.0779 0.0846  409 GLU D C   
9157  O O   . GLU D 409 ? 0.6358 0.6268 0.8049 0.0003  -0.0791 0.0911  409 GLU D O   
9158  C CB  . GLU D 409 ? 0.6555 0.6257 0.8061 0.0065  -0.0722 0.0693  409 GLU D CB  
9159  C CG  . GLU D 409 ? 0.7268 0.6918 0.8559 -0.0016 -0.0610 0.0585  409 GLU D CG  
9160  C CD  . GLU D 409 ? 0.7051 0.6640 0.8254 -0.0003 -0.0683 0.0547  409 GLU D CD  
9161  O OE1 . GLU D 409 ? 0.6332 0.5916 0.7636 0.0075  -0.0818 0.0605  409 GLU D OE1 
9162  O OE2 . GLU D 409 ? 0.7658 0.7203 0.8682 -0.0083 -0.0597 0.0451  409 GLU D OE2 
9163  N N   . ASN D 410 ? 0.6651 0.6471 0.8575 0.0159  -0.0869 0.0869  410 ASN D N   
9164  C CA  . ASN D 410 ? 0.6191 0.6042 0.8221 0.0166  -0.0991 0.0949  410 ASN D CA  
9165  C C   . ASN D 410 ? 0.5987 0.5890 0.8252 0.0211  -0.0990 0.0970  410 ASN D C   
9166  O O   . ASN D 410 ? 0.5798 0.5701 0.8168 0.0278  -0.0988 0.0940  410 ASN D O   
9167  C CB  . ASN D 410 ? 0.5747 0.5536 0.7738 0.0201  -0.1110 0.0945  410 ASN D CB  
9168  C CG  . ASN D 410 ? 0.5917 0.5687 0.7697 0.0154  -0.1120 0.0936  410 ASN D CG  
9169  O OD1 . ASN D 410 ? 0.6281 0.6109 0.7945 0.0078  -0.1080 0.0970  410 ASN D OD1 
9170  N ND2 . ASN D 410 ? 0.5674 0.5382 0.7401 0.0192  -0.1175 0.0897  410 ASN D ND2 
9171  N N   . LEU D 411 ? 0.5644 0.5609 0.8000 0.0169  -0.0995 0.1034  411 LEU D N   
9172  C CA  . LEU D 411 ? 0.5527 0.5572 0.8110 0.0187  -0.0994 0.1062  411 LEU D CA  
9173  C C   . LEU D 411 ? 0.5344 0.5392 0.8004 0.0146  -0.1086 0.1117  411 LEU D C   
9174  O O   . LEU D 411 ? 0.5508 0.5546 0.8109 0.0090  -0.1073 0.1171  411 LEU D O   
9175  C CB  . LEU D 411 ? 0.5950 0.6070 0.8594 0.0166  -0.0858 0.1076  411 LEU D CB  
9176  C CG  . LEU D 411 ? 0.5876 0.6114 0.8771 0.0171  -0.0850 0.1124  411 LEU D CG  
9177  C CD1 . LEU D 411 ? 0.5537 0.5836 0.8604 0.0246  -0.0890 0.1115  411 LEU D CD1 
9178  C CD2 . LEU D 411 ? 0.6344 0.6645 0.9278 0.0144  -0.0699 0.1140  411 LEU D CD2 
9179  N N   . THR D 412 ? 0.6154 0.6219 0.8946 0.0165  -0.1170 0.1105  412 THR D N   
9180  C CA  . THR D 412 ? 0.6062 0.6098 0.8925 0.0116  -0.1246 0.1128  412 THR D CA  
9181  C C   . THR D 412 ? 0.6095 0.6251 0.9170 0.0085  -0.1259 0.1138  412 THR D C   
9182  O O   . THR D 412 ? 0.5943 0.6188 0.9106 0.0118  -0.1292 0.1113  412 THR D O   
9183  C CB  . THR D 412 ? 0.5797 0.5736 0.8592 0.0139  -0.1338 0.1083  412 THR D CB  
9184  O OG1 . THR D 412 ? 0.5755 0.5611 0.8369 0.0166  -0.1328 0.1082  412 THR D OG1 
9185  C CG2 . THR D 412 ? 0.5831 0.5702 0.8690 0.0083  -0.1383 0.1096  412 THR D CG2 
9186  N N   . LEU D 413 ? 0.5841 0.6012 0.9003 0.0016  -0.1237 0.1184  413 LEU D N   
9187  C CA  . LEU D 413 ? 0.5936 0.6240 0.9304 -0.0033 -0.1244 0.1197  413 LEU D CA  
9188  C C   . LEU D 413 ? 0.6102 0.6344 0.9542 -0.0123 -0.1280 0.1201  413 LEU D C   
9189  O O   . LEU D 413 ? 0.6288 0.6631 0.9891 -0.0190 -0.1265 0.1223  413 LEU D O   
9190  C CB  . LEU D 413 ? 0.6146 0.6566 0.9603 -0.0034 -0.1139 0.1250  413 LEU D CB  
9191  C CG  . LEU D 413 ? 0.6139 0.6597 0.9543 0.0046  -0.1060 0.1240  413 LEU D CG  
9192  C CD1 . LEU D 413 ? 0.6474 0.7004 0.9931 0.0031  -0.0930 0.1284  413 LEU D CD1 
9193  C CD2 . LEU D 413 ? 0.5880 0.6451 0.9412 0.0104  -0.1101 0.1224  413 LEU D CD2 
9194  N N   . ASP D 414 ? 0.6508 0.6585 0.9846 -0.0129 -0.1316 0.1180  414 ASP D N   
9195  C CA  . ASP D 414 ? 0.6741 0.6712 1.0149 -0.0208 -0.1310 0.1192  414 ASP D CA  
9196  C C   . ASP D 414 ? 0.6953 0.6992 1.0506 -0.0298 -0.1355 0.1127  414 ASP D C   
9197  O O   . ASP D 414 ? 0.6816 0.6951 1.0373 -0.0293 -0.1423 0.1065  414 ASP D O   
9198  C CB  . ASP D 414 ? 0.6618 0.6400 0.9914 -0.0182 -0.1328 0.1183  414 ASP D CB  
9199  C CG  . ASP D 414 ? 0.6498 0.6231 0.9680 -0.0132 -0.1283 0.1276  414 ASP D CG  
9200  O OD1 . ASP D 414 ? 0.6494 0.6333 0.9615 -0.0103 -0.1250 0.1306  414 ASP D OD1 
9201  O OD2 . ASP D 414 ? 0.6441 0.6042 0.9600 -0.0125 -0.1273 0.1324  414 ASP D OD2 
9202  N N   . ASP D 415 ? 0.7063 0.7066 1.0737 -0.0391 -0.1315 0.1149  415 ASP D N   
9203  C CA  . ASP D 415 ? 0.7225 0.7248 1.1017 -0.0511 -0.1347 0.1072  415 ASP D CA  
9204  C C   . ASP D 415 ? 0.7024 0.7306 1.0906 -0.0539 -0.1413 0.1042  415 ASP D C   
9205  O O   . ASP D 415 ? 0.6891 0.7232 1.0748 -0.0571 -0.1492 0.0964  415 ASP D O   
9206  C CB  . ASP D 415 ? 0.7225 0.7058 1.0933 -0.0535 -0.1375 0.0982  415 ASP D CB  
9207  C CG  . ASP D 415 ? 0.7170 0.6764 1.0849 -0.0510 -0.1299 0.1036  415 ASP D CG  
9208  O OD1 . ASP D 415 ? 0.7197 0.6762 1.0973 -0.0542 -0.1226 0.1120  415 ASP D OD1 
9209  O OD2 . ASP D 415 ? 0.7043 0.6490 1.0617 -0.0455 -0.1309 0.1008  415 ASP D OD2 
9210  N N   . ASN D 416 ? 0.7043 0.7495 1.1038 -0.0525 -0.1373 0.1119  416 ASN D N   
9211  C CA  . ASN D 416 ? 0.6799 0.7529 1.0933 -0.0537 -0.1417 0.1132  416 ASN D CA  
9212  C C   . ASN D 416 ? 0.6883 0.7737 1.1208 -0.0619 -0.1361 0.1189  416 ASN D C   
9213  O O   . ASN D 416 ? 0.7089 0.7801 1.1432 -0.0684 -0.1300 0.1200  416 ASN D O   
9214  C CB  . ASN D 416 ? 0.6558 0.7373 1.0642 -0.0394 -0.1405 0.1177  416 ASN D CB  
9215  C CG  . ASN D 416 ? 0.6312 0.7147 1.0301 -0.0344 -0.1494 0.1125  416 ASN D CG  
9216  O OD1 . ASN D 416 ? 0.6280 0.7182 1.0292 -0.0427 -0.1579 0.1068  416 ASN D OD1 
9217  N ND2 . ASN D 416 ? 0.6140 0.6915 1.0013 -0.0220 -0.1467 0.1140  416 ASN D ND2 
9218  N N   . HIS D 417 ? 0.6697 0.7826 1.1189 -0.0617 -0.1376 0.1236  417 HIS D N   
9219  C CA  . HIS D 417 ? 0.6731 0.8021 1.1431 -0.0690 -0.1322 0.1298  417 HIS D CA  
9220  C C   . HIS D 417 ? 0.6667 0.8097 1.1450 -0.0576 -0.1239 0.1393  417 HIS D C   
9221  O O   . HIS D 417 ? 0.6539 0.8227 1.1542 -0.0596 -0.1229 0.1453  417 HIS D O   
9222  C CB  . HIS D 417 ? 0.6582 0.8114 1.1456 -0.0827 -0.1410 0.1271  417 HIS D CB  
9223  C CG  . HIS D 417 ? 0.6688 0.8073 1.1489 -0.0972 -0.1462 0.1158  417 HIS D CG  
9224  N ND1 . HIS D 417 ? 0.6595 0.8091 1.1367 -0.1053 -0.1575 0.1077  417 HIS D ND1 
9225  C CD2 . HIS D 417 ? 0.6879 0.8010 1.1635 -0.1054 -0.1401 0.1111  417 HIS D CD2 
9226  C CE1 . HIS D 417 ? 0.6749 0.8050 1.1449 -0.1186 -0.1573 0.0966  417 HIS D CE1 
9227  N NE2 . HIS D 417 ? 0.6907 0.7977 1.1611 -0.1183 -0.1464 0.0989  417 HIS D NE2 
9228  N N   . PHE D 418 ? 0.6382 0.7649 1.0995 -0.0462 -0.1170 0.1405  418 PHE D N   
9229  C CA  . PHE D 418 ? 0.6378 0.7740 1.1044 -0.0365 -0.1064 0.1471  418 PHE D CA  
9230  C C   . PHE D 418 ? 0.6594 0.7992 1.1365 -0.0419 -0.0956 0.1533  418 PHE D C   
9231  O O   . PHE D 418 ? 0.6762 0.8046 1.1507 -0.0510 -0.0951 0.1532  418 PHE D O   
9232  C CB  . PHE D 418 ? 0.6441 0.7616 1.0868 -0.0256 -0.1018 0.1446  418 PHE D CB  
9233  C CG  . PHE D 418 ? 0.6161 0.7331 1.0514 -0.0181 -0.1098 0.1401  418 PHE D CG  
9234  C CD1 . PHE D 418 ? 0.5914 0.7293 1.0434 -0.0123 -0.1112 0.1436  418 PHE D CD1 
9235  C CD2 . PHE D 418 ? 0.6132 0.7098 1.0264 -0.0165 -0.1155 0.1338  418 PHE D CD2 
9236  C CE1 . PHE D 418 ? 0.5662 0.7040 1.0118 -0.0053 -0.1182 0.1410  418 PHE D CE1 
9237  C CE2 . PHE D 418 ? 0.5865 0.6826 0.9926 -0.0099 -0.1224 0.1299  418 PHE D CE2 
9238  C CZ  . PHE D 418 ? 0.5641 0.6805 0.9859 -0.0045 -0.1238 0.1335  418 PHE D CZ  
9239  N N   . GLU D 419 ? 0.6710 0.8267 1.1617 -0.0361 -0.0858 0.1593  419 GLU D N   
9240  C CA  . GLU D 419 ? 0.6887 0.8509 1.1908 -0.0402 -0.0738 0.1657  419 GLU D CA  
9241  C C   . GLU D 419 ? 0.7077 0.8666 1.2017 -0.0304 -0.0587 0.1676  419 GLU D C   
9242  O O   . GLU D 419 ? 0.7062 0.8584 1.1879 -0.0208 -0.0574 0.1638  419 GLU D O   
9243  C CB  . GLU D 419 ? 0.6685 0.8595 1.2029 -0.0460 -0.0751 0.1714  419 GLU D CB  
9244  C CG  . GLU D 419 ? 0.6527 0.8512 1.1965 -0.0587 -0.0893 0.1682  419 GLU D CG  
9245  C CD  . GLU D 419 ? 0.6293 0.8626 1.2052 -0.0639 -0.0923 0.1746  419 GLU D CD  
9246  O OE1 . GLU D 419 ? 0.6329 0.8768 1.2259 -0.0722 -0.0863 0.1795  419 GLU D OE1 
9247  O OE2 . GLU D 419 ? 0.6056 0.8576 1.1906 -0.0596 -0.1008 0.1761  419 GLU D OE2 
9248  N N   . GLY D 420 ? 0.6291 0.7928 1.1300 -0.0338 -0.0461 0.1729  420 GLY D N   
9249  C CA  . GLY D 420 ? 0.6490 0.8141 1.1473 -0.0266 -0.0291 0.1742  420 GLY D CA  
9250  C C   . GLY D 420 ? 0.6830 0.8265 1.1481 -0.0253 -0.0226 0.1698  420 GLY D C   
9251  O O   . GLY D 420 ? 0.6895 0.8176 1.1348 -0.0292 -0.0315 0.1679  420 GLY D O   
9252  N N   . PRO D 421 ? 0.6094 0.7526 1.0686 -0.0205 -0.0060 0.1684  421 PRO D N   
9253  C CA  . PRO D 421 ? 0.6445 0.7707 1.0706 -0.0220 0.0012  0.1639  421 PRO D CA  
9254  C C   . PRO D 421 ? 0.6502 0.7639 1.0579 -0.0148 -0.0027 0.1556  421 PRO D C   
9255  O O   . PRO D 421 ? 0.6228 0.7400 1.0434 -0.0078 -0.0106 0.1538  421 PRO D O   
9256  C CB  . PRO D 421 ? 0.6666 0.7992 1.0958 -0.0222 0.0228  0.1645  421 PRO D CB  
9257  C CG  . PRO D 421 ? 0.6447 0.7926 1.1064 -0.0138 0.0277  0.1662  421 PRO D CG  
9258  C CD  . PRO D 421 ? 0.6058 0.7651 1.0894 -0.0151 0.0088  0.1714  421 PRO D CD  
9259  N N   . VAL D 422 ? 0.6356 0.7364 1.0129 -0.0176 0.0026  0.1511  422 VAL D N   
9260  C CA  . VAL D 422 ? 0.6479 0.7364 1.0054 -0.0125 0.0013  0.1425  422 VAL D CA  
9261  C C   . VAL D 422 ? 0.6675 0.7564 1.0288 -0.0068 0.0204  0.1362  422 VAL D C   
9262  O O   . VAL D 422 ? 0.6931 0.7829 1.0468 -0.0116 0.0374  0.1347  422 VAL D O   
9263  C CB  . VAL D 422 ? 0.6704 0.7478 0.9941 -0.0196 -0.0019 0.1411  422 VAL D CB  
9264  C CG1 . VAL D 422 ? 0.6743 0.7402 0.9805 -0.0151 -0.0080 0.1330  422 VAL D CG1 
9265  C CG2 . VAL D 422 ? 0.6520 0.7298 0.9771 -0.0255 -0.0151 0.1502  422 VAL D CG2 
9266  N N   . PRO D 423 ? 0.7151 0.8026 1.0881 0.0031  0.0196  0.1327  423 PRO D N   
9267  C CA  . PRO D 423 ? 0.7317 0.8174 1.1124 0.0098  0.0402  0.1276  423 PRO D CA  
9268  C C   . PRO D 423 ? 0.7795 0.8499 1.1271 0.0038  0.0546  0.1165  423 PRO D C   
9269  O O   . PRO D 423 ? 0.7946 0.8560 1.1128 -0.0030 0.0453  0.1127  423 PRO D O   
9270  C CB  . PRO D 423 ? 0.6941 0.7795 1.0898 0.0211  0.0324  0.1276  423 PRO D CB  
9271  C CG  . PRO D 423 ? 0.6455 0.7405 1.0516 0.0199  0.0092  0.1348  423 PRO D CG  
9272  C CD  . PRO D 423 ? 0.6686 0.7568 1.0507 0.0088  0.0009  0.1342  423 PRO D CD  
9273  N N   . LYS D 424 ? 0.7611 0.8295 1.1143 0.0057  0.0787  0.1114  424 LYS D N   
9274  C CA  . LYS D 424 ? 0.8024 0.8572 1.1230 -0.0030 0.0954  0.0990  424 LYS D CA  
9275  C C   . LYS D 424 ? 0.8171 0.8563 1.1168 -0.0017 0.0913  0.0891  424 LYS D C   
9276  O O   . LYS D 424 ? 0.8451 0.8761 1.1099 -0.0127 0.0926  0.0808  424 LYS D O   
9277  C CB  . LYS D 424 ? 0.8142 0.8681 1.1478 -0.0010 0.1247  0.0941  424 LYS D CB  
9278  C CG  . LYS D 424 ? 0.8095 0.8774 1.1541 -0.0063 0.1323  0.1015  424 LYS D CG  
9279  C CD  . LYS D 424 ? 0.8265 0.8902 1.1751 -0.0072 0.1644  0.0937  424 LYS D CD  
9280  C CE  . LYS D 424 ? 0.7970 0.8704 1.1930 0.0076  0.1756  0.1018  424 LYS D CE  
9281  N NZ  . LYS D 424 ? 0.8104 0.8777 1.2134 0.0081  0.2099  0.0941  424 LYS D NZ  
9282  N N   . SER D 425 ? 0.8111 0.8479 1.1314 0.0109  0.0860  0.0907  425 SER D N   
9283  C CA  . SER D 425 ? 0.8231 0.8449 1.1258 0.0127  0.0823  0.0819  425 SER D CA  
9284  C C   . SER D 425 ? 0.8244 0.8450 1.1004 0.0049  0.0598  0.0824  425 SER D C   
9285  O O   . SER D 425 ? 0.8453 0.8543 1.0947 -0.0002 0.0597  0.0732  425 SER D O   
9286  C CB  . SER D 425 ? 0.7804 0.8034 1.1129 0.0280  0.0781  0.0871  425 SER D CB  
9287  O OG  . SER D 425 ? 0.7546 0.7885 1.1223 0.0366  0.0916  0.0947  425 SER D OG  
9288  N N   . LEU D 426 ? 0.7971 0.8294 1.0813 0.0039  0.0417  0.0934  426 LEU D N   
9289  C CA  . LEU D 426 ? 0.7901 0.8213 1.0527 -0.0029 0.0226  0.0958  426 LEU D CA  
9290  C C   . LEU D 426 ? 0.8180 0.8505 1.0523 -0.0167 0.0282  0.0946  426 LEU D C   
9291  O O   . LEU D 426 ? 0.8246 0.8540 1.0338 -0.0232 0.0186  0.0935  426 LEU D O   
9292  C CB  . LEU D 426 ? 0.7428 0.7837 1.0255 0.0002  0.0041  0.1073  426 LEU D CB  
9293  C CG  . LEU D 426 ? 0.7113 0.7488 0.9797 -0.0030 -0.0158 0.1107  426 LEU D CG  
9294  C CD1 . LEU D 426 ? 0.6995 0.7257 0.9522 0.0003  -0.0209 0.1030  426 LEU D CD1 
9295  C CD2 . LEU D 426 ? 0.6499 0.6943 0.9417 0.0005  -0.0305 0.1188  426 LEU D CD2 
9296  N N   . ARG D 427 ? 0.7751 0.8142 1.0135 -0.0214 0.0434  0.0959  427 ARG D N   
9297  C CA  . ARG D 427 ? 0.8012 0.8441 1.0117 -0.0356 0.0496  0.0955  427 ARG D CA  
9298  C C   . ARG D 427 ? 0.8394 0.8732 1.0183 -0.0439 0.0611  0.0816  427 ARG D C   
9299  O O   . ARG D 427 ? 0.8559 0.8935 1.0053 -0.0558 0.0556  0.0820  427 ARG D O   
9300  C CB  . ARG D 427 ? 0.8059 0.8576 1.0288 -0.0386 0.0653  0.0991  427 ARG D CB  
9301  C CG  . ARG D 427 ? 0.8386 0.8946 1.0309 -0.0540 0.0772  0.0965  427 ARG D CG  
9302  C CD  . ARG D 427 ? 0.8430 0.9063 1.0487 -0.0562 0.0958  0.0983  427 ARG D CD  
9303  N NE  . ARG D 427 ? 0.8673 0.9219 1.0698 -0.0567 0.1216  0.0836  427 ARG D NE  
9304  C CZ  . ARG D 427 ? 0.8611 0.9178 1.0878 -0.0516 0.1407  0.0829  427 ARG D CZ  
9305  N NH1 . ARG D 427 ? 0.8351 0.9044 1.0904 -0.0467 0.1361  0.0959  427 ARG D NH1 
9306  N NH2 . ARG D 427 ? 0.8788 0.9246 1.1022 -0.0518 0.1661  0.0687  427 ARG D NH2 
9307  N N   . ASP D 428 ? 0.8294 0.8520 1.0149 -0.0384 0.0773  0.0698  428 ASP D N   
9308  C CA  . ASP D 428 ? 0.8651 0.8767 1.0220 -0.0475 0.0914  0.0540  428 ASP D CA  
9309  C C   . ASP D 428 ? 0.8628 0.8646 1.0114 -0.0437 0.0791  0.0492  428 ASP D C   
9310  O O   . ASP D 428 ? 0.8905 0.8833 1.0137 -0.0528 0.0886  0.0358  428 ASP D O   
9311  C CB  . ASP D 428 ? 0.8759 0.8776 1.0444 -0.0445 0.1203  0.0427  428 ASP D CB  
9312  C CG  . ASP D 428 ? 0.8703 0.8821 1.0549 -0.0449 0.1329  0.0489  428 ASP D CG  
9313  O OD1 . ASP D 428 ? 0.8669 0.8927 1.0457 -0.0514 0.1214  0.0597  428 ASP D OD1 
9314  O OD2 . ASP D 428 ? 0.8674 0.8734 1.0725 -0.0383 0.1552  0.0439  428 ASP D OD2 
9315  N N   . CYS D 429 ? 0.8170 0.8206 0.9856 -0.0319 0.0590  0.0589  429 CYS D N   
9316  C CA  . CYS D 429 ? 0.8083 0.8032 0.9717 -0.0272 0.0468  0.0555  429 CYS D CA  
9317  C C   . CYS D 429 ? 0.8198 0.8191 0.9516 -0.0394 0.0337  0.0560  429 CYS D C   
9318  O O   . CYS D 429 ? 0.7965 0.8062 0.9286 -0.0405 0.0167  0.0685  429 CYS D O   
9319  C CB  . CYS D 429 ? 0.7627 0.7606 0.9553 -0.0128 0.0295  0.0662  429 CYS D CB  
9320  S SG  . CYS D 429 ? 0.7363 0.7244 0.9269 -0.0051 0.0144  0.0636  429 CYS D SG  
9321  N N   . LYS D 430 ? 0.7797 0.7715 0.8860 -0.0485 0.0415  0.0433  430 LYS D N   
9322  C CA  . LYS D 430 ? 0.7921 0.7925 0.8671 -0.0626 0.0312  0.0441  430 LYS D CA  
9323  C C   . LYS D 430 ? 0.7670 0.7650 0.8403 -0.0577 0.0122  0.0469  430 LYS D C   
9324  O O   . LYS D 430 ? 0.7661 0.7736 0.8171 -0.0680 0.0017  0.0501  430 LYS D O   
9325  C CB  . LYS D 430 ? 0.8300 0.8272 0.8744 -0.0794 0.0504  0.0279  430 LYS D CB  
9326  C CG  . LYS D 430 ? 0.8449 0.8485 0.8820 -0.0891 0.0676  0.0259  430 LYS D CG  
9327  C CD  . LYS D 430 ? 0.8690 0.8652 0.8777 -0.1054 0.0906  0.0059  430 LYS D CD  
9328  C CE  . LYS D 430 ? 0.8800 0.8855 0.8752 -0.1183 0.1066  0.0043  430 LYS D CE  
9329  N NZ  . LYS D 430 ? 0.8666 0.8929 0.8650 -0.1186 0.0891  0.0248  430 LYS D NZ  
9330  N N   . SER D 431 ? 0.7995 0.7869 0.8959 -0.0426 0.0077  0.0469  431 SER D N   
9331  C CA  . SER D 431 ? 0.7732 0.7568 0.8682 -0.0377 -0.0079 0.0481  431 SER D CA  
9332  C C   . SER D 431 ? 0.7220 0.7135 0.8306 -0.0305 -0.0293 0.0634  431 SER D C   
9333  O O   . SER D 431 ? 0.6840 0.6717 0.7956 -0.0245 -0.0421 0.0651  431 SER D O   
9334  C CB  . SER D 431 ? 0.7631 0.7311 0.8740 -0.0260 -0.0008 0.0401  431 SER D CB  
9335  O OG  . SER D 431 ? 0.7344 0.7022 0.8757 -0.0131 0.0014  0.0462  431 SER D OG  
9336  N N   . LEU D 432 ? 0.7639 0.7654 0.8808 -0.0316 -0.0322 0.0740  432 LEU D N   
9337  C CA  . LEU D 432 ? 0.6977 0.7036 0.8307 -0.0248 -0.0494 0.0871  432 LEU D CA  
9338  C C   . LEU D 432 ? 0.6670 0.6782 0.7848 -0.0296 -0.0633 0.0940  432 LEU D C   
9339  O O   . LEU D 432 ? 0.7030 0.7234 0.7983 -0.0414 -0.0615 0.0952  432 LEU D O   
9340  C CB  . LEU D 432 ? 0.6983 0.7128 0.8428 -0.0266 -0.0472 0.0967  432 LEU D CB  
9341  C CG  . LEU D 432 ? 0.7156 0.7282 0.8796 -0.0214 -0.0341 0.0927  432 LEU D CG  
9342  C CD1 . LEU D 432 ? 0.6971 0.7186 0.8771 -0.0219 -0.0359 0.1038  432 LEU D CD1 
9343  C CD2 . LEU D 432 ? 0.6733 0.6777 0.8571 -0.0089 -0.0368 0.0884  432 LEU D CD2 
9344  N N   . ILE D 433 ? 0.7037 0.7105 0.8345 -0.0207 -0.0770 0.0990  433 ILE D N   
9345  C CA  . ILE D 433 ? 0.6643 0.6755 0.7873 -0.0225 -0.0901 0.1074  433 ILE D CA  
9346  C C   . ILE D 433 ? 0.6096 0.6216 0.7516 -0.0171 -0.0998 0.1204  433 ILE D C   
9347  O O   . ILE D 433 ? 0.6047 0.6261 0.7436 -0.0220 -0.1037 0.1332  433 ILE D O   
9348  C CB  . ILE D 433 ? 0.6398 0.6425 0.7592 -0.0176 -0.0954 0.0997  433 ILE D CB  
9349  C CG1 . ILE D 433 ? 0.7042 0.7037 0.8055 -0.0240 -0.0836 0.0859  433 ILE D CG1 
9350  C CG2 . ILE D 433 ? 0.5988 0.6075 0.7128 -0.0188 -0.1081 0.1096  433 ILE D CG2 
9351  C CD1 . ILE D 433 ? 0.6880 0.6806 0.7827 -0.0216 -0.0881 0.0791  433 ILE D CD1 
9352  N N   . ARG D 434 ? 0.6753 0.6781 0.8372 -0.0077 -0.1030 0.1176  434 ARG D N   
9353  C CA  . ARG D 434 ? 0.6362 0.6373 0.8171 -0.0041 -0.1096 0.1265  434 ARG D CA  
9354  C C   . ARG D 434 ? 0.6449 0.6464 0.8427 -0.0025 -0.1036 0.1241  434 ARG D C   
9355  O O   . ARG D 434 ? 0.6422 0.6407 0.8468 0.0024  -0.1005 0.1153  434 ARG D O   
9356  C CB  . ARG D 434 ? 0.5847 0.5765 0.7741 0.0031  -0.1197 0.1252  434 ARG D CB  
9357  C CG  . ARG D 434 ? 0.5631 0.5557 0.7492 0.0024  -0.1269 0.1356  434 ARG D CG  
9358  C CD  . ARG D 434 ? 0.5207 0.5024 0.7165 0.0094  -0.1345 0.1330  434 ARG D CD  
9359  N NE  . ARG D 434 ? 0.5051 0.4805 0.7192 0.0108  -0.1363 0.1383  434 ARG D NE  
9360  C CZ  . ARG D 434 ? 0.4973 0.4713 0.7178 0.0105  -0.1380 0.1504  434 ARG D CZ  
9361  N NH1 . ARG D 434 ? 0.4985 0.4809 0.7094 0.0088  -0.1393 0.1609  434 ARG D NH1 
9362  N NH2 . ARG D 434 ? 0.4907 0.4556 0.7286 0.0112  -0.1376 0.1527  434 ARG D NH2 
9363  N N   . VAL D 435 ? 0.5879 0.5944 0.7942 -0.0064 -0.1020 0.1333  435 VAL D N   
9364  C CA  . VAL D 435 ? 0.5962 0.6054 0.8203 -0.0061 -0.0968 0.1329  435 VAL D CA  
9365  C C   . VAL D 435 ? 0.5695 0.5758 0.8103 -0.0064 -0.1031 0.1410  435 VAL D C   
9366  O O   . VAL D 435 ? 0.5732 0.5805 0.8115 -0.0103 -0.1040 0.1518  435 VAL D O   
9367  C CB  . VAL D 435 ? 0.6504 0.6686 0.8680 -0.0125 -0.0847 0.1348  435 VAL D CB  
9368  C CG1 . VAL D 435 ? 0.6565 0.6790 0.8953 -0.0117 -0.0791 0.1351  435 VAL D CG1 
9369  C CG2 . VAL D 435 ? 0.6912 0.7096 0.8908 -0.0139 -0.0760 0.1250  435 VAL D CG2 
9370  N N   . ARG D 436 ? 0.6518 0.6550 0.9100 -0.0031 -0.1070 0.1362  436 ARG D N   
9371  C CA  . ARG D 436 ? 0.6381 0.6365 0.9122 -0.0052 -0.1117 0.1405  436 ARG D CA  
9372  C C   . ARG D 436 ? 0.6504 0.6565 0.9433 -0.0077 -0.1084 0.1388  436 ARG D C   
9373  O O   . ARG D 436 ? 0.6377 0.6476 0.9390 -0.0048 -0.1113 0.1316  436 ARG D O   
9374  C CB  . ARG D 436 ? 0.6060 0.5941 0.8816 -0.0014 -0.1206 0.1352  436 ARG D CB  
9375  C CG  . ARG D 436 ? 0.5909 0.5725 0.8514 0.0015  -0.1241 0.1379  436 ARG D CG  
9376  C CD  . ARG D 436 ? 0.5706 0.5400 0.8387 0.0029  -0.1296 0.1382  436 ARG D CD  
9377  N NE  . ARG D 436 ? 0.5832 0.5482 0.8646 -0.0016 -0.1264 0.1470  436 ARG D NE  
9378  C CZ  . ARG D 436 ? 0.5748 0.5283 0.8621 -0.0009 -0.1269 0.1529  436 ARG D CZ  
9379  N NH1 . ARG D 436 ? 0.5537 0.5000 0.8350 0.0041  -0.1311 0.1508  436 ARG D NH1 
9380  N NH2 . ARG D 436 ? 0.5881 0.5368 0.8891 -0.0049 -0.1219 0.1618  436 ARG D NH2 
9381  N N   . PHE D 437 ? 0.5688 0.5790 0.8691 -0.0134 -0.1027 0.1468  437 PHE D N   
9382  C CA  . PHE D 437 ? 0.5842 0.6031 0.9040 -0.0172 -0.0993 0.1468  437 PHE D CA  
9383  C C   . PHE D 437 ? 0.5855 0.5981 0.9206 -0.0231 -0.1026 0.1498  437 PHE D C   
9384  O O   . PHE D 437 ? 0.6021 0.6226 0.9544 -0.0282 -0.1003 0.1501  437 PHE D O   
9385  C CB  . PHE D 437 ? 0.6188 0.6475 0.9371 -0.0204 -0.0882 0.1528  437 PHE D CB  
9386  C CG  . PHE D 437 ? 0.6324 0.6695 0.9465 -0.0163 -0.0812 0.1468  437 PHE D CG  
9387  C CD1 . PHE D 437 ? 0.6180 0.6508 0.9193 -0.0103 -0.0834 0.1395  437 PHE D CD1 
9388  C CD2 . PHE D 437 ? 0.6625 0.7109 0.9870 -0.0185 -0.0707 0.1488  437 PHE D CD2 
9389  C CE1 . PHE D 437 ? 0.6360 0.6738 0.9353 -0.0064 -0.0744 0.1340  437 PHE D CE1 
9390  C CE2 . PHE D 437 ? 0.6795 0.7337 1.0026 -0.0142 -0.0615 0.1435  437 PHE D CE2 
9391  C CZ  . PHE D 437 ? 0.6676 0.7156 0.9783 -0.0081 -0.0629 0.1360  437 PHE D CZ  
9392  N N   . LYS D 438 ? 0.6144 0.6129 0.9451 -0.0229 -0.1067 0.1519  438 LYS D N   
9393  C CA  . LYS D 438 ? 0.6217 0.6103 0.9663 -0.0289 -0.1059 0.1559  438 LYS D CA  
9394  C C   . LYS D 438 ? 0.6340 0.6253 0.9953 -0.0349 -0.1090 0.1468  438 LYS D C   
9395  O O   . LYS D 438 ? 0.6261 0.6208 0.9860 -0.0330 -0.1157 0.1369  438 LYS D O   
9396  C CB  . LYS D 438 ? 0.6017 0.5738 0.9404 -0.0257 -0.1090 0.1581  438 LYS D CB  
9397  C CG  . LYS D 438 ? 0.6070 0.5661 0.9592 -0.0305 -0.1040 0.1666  438 LYS D CG  
9398  C CD  . LYS D 438 ? 0.5917 0.5325 0.9455 -0.0282 -0.1064 0.1628  438 LYS D CD  
9399  C CE  . LYS D 438 ? 0.5881 0.5149 0.9527 -0.0289 -0.0991 0.1765  438 LYS D CE  
9400  N NZ  . LYS D 438 ? 0.5766 0.5106 0.9312 -0.0230 -0.0982 0.1933  438 LYS D NZ  
9401  N N   . GLY D 439 ? 0.6294 0.6204 1.0064 -0.0433 -0.1042 0.1507  439 GLY D N   
9402  C CA  . GLY D 439 ? 0.6403 0.6343 1.0334 -0.0523 -0.1068 0.1423  439 GLY D CA  
9403  C C   . GLY D 439 ? 0.6477 0.6647 1.0495 -0.0537 -0.1093 0.1386  439 GLY D C   
9404  O O   . GLY D 439 ? 0.6387 0.6635 1.0425 -0.0545 -0.1169 0.1298  439 GLY D O   
9405  N N   . ASN D 440 ? 0.6540 0.6832 1.0622 -0.0540 -0.1022 0.1463  440 ASN D N   
9406  C CA  . ASN D 440 ? 0.6479 0.7001 1.0687 -0.0544 -0.1020 0.1454  440 ASN D CA  
9407  C C   . ASN D 440 ? 0.6552 0.7153 1.0899 -0.0608 -0.0929 0.1537  440 ASN D C   
9408  O O   . ASN D 440 ? 0.6613 0.7089 1.0977 -0.0665 -0.0882 0.1589  440 ASN D O   
9409  C CB  . ASN D 440 ? 0.6438 0.7033 1.0530 -0.0429 -0.1012 0.1450  440 ASN D CB  
9410  C CG  . ASN D 440 ? 0.6173 0.6757 1.0193 -0.0377 -0.1109 0.1368  440 ASN D CG  
9411  O OD1 . ASN D 440 ? 0.5972 0.6707 1.0116 -0.0396 -0.1168 0.1333  440 ASN D OD1 
9412  N ND2 . ASN D 440 ? 0.6083 0.6509 0.9909 -0.0316 -0.1128 0.1348  440 ASN D ND2 
9413  N N   . SER D 441 ? 0.6255 0.7065 1.0720 -0.0595 -0.0893 0.1558  441 SER D N   
9414  C CA  . SER D 441 ? 0.6315 0.7230 1.0923 -0.0649 -0.0797 0.1636  441 SER D CA  
9415  C C   . SER D 441 ? 0.6426 0.7430 1.0974 -0.0567 -0.0697 0.1682  441 SER D C   
9416  O O   . SER D 441 ? 0.6406 0.7581 1.1115 -0.0581 -0.0624 0.1722  441 SER D O   
9417  C CB  . SER D 441 ? 0.6145 0.7255 1.1010 -0.0741 -0.0830 0.1620  441 SER D CB  
9418  O OG  . SER D 441 ? 0.6117 0.7121 1.1024 -0.0852 -0.0890 0.1568  441 SER D OG  
9419  N N   . PHE D 442 ? 0.6592 0.7481 1.0906 -0.0488 -0.0685 0.1670  442 PHE D N   
9420  C CA  . PHE D 442 ? 0.6760 0.7702 1.0977 -0.0429 -0.0574 0.1690  442 PHE D CA  
9421  C C   . PHE D 442 ? 0.6922 0.7884 1.1141 -0.0491 -0.0461 0.1778  442 PHE D C   
9422  O O   . PHE D 442 ? 0.6926 0.7798 1.1133 -0.0555 -0.0475 0.1838  442 PHE D O   
9423  C CB  . PHE D 442 ? 0.6867 0.7676 1.0813 -0.0363 -0.0591 0.1651  442 PHE D CB  
9424  C CG  . PHE D 442 ? 0.6683 0.7492 1.0616 -0.0286 -0.0666 0.1568  442 PHE D CG  
9425  C CD1 . PHE D 442 ? 0.6595 0.7526 1.0622 -0.0222 -0.0607 0.1543  442 PHE D CD1 
9426  C CD2 . PHE D 442 ? 0.6466 0.7153 1.0307 -0.0274 -0.0782 0.1525  442 PHE D CD2 
9427  C CE1 . PHE D 442 ? 0.6294 0.7228 1.0320 -0.0148 -0.0671 0.1487  442 PHE D CE1 
9428  C CE2 . PHE D 442 ? 0.6155 0.6848 0.9977 -0.0207 -0.0849 0.1457  442 PHE D CE2 
9429  C CZ  . PHE D 442 ? 0.6067 0.6888 0.9982 -0.0143 -0.0797 0.1443  442 PHE D CZ  
9430  N N   . SER D 443 ? 0.4830 0.8533 1.1568 0.0459  -0.1836 0.1506  443 SER D N   
9431  C CA  . SER D 443 ? 0.4540 0.8516 1.1925 0.0411  -0.1530 0.1482  443 SER D CA  
9432  C C   . SER D 443 ? 0.4603 0.8411 1.2093 0.0670  -0.1079 0.1535  443 SER D C   
9433  O O   . SER D 443 ? 0.4818 0.8343 1.1985 0.0879  -0.1046 0.1598  443 SER D O   
9434  C CB  . SER D 443 ? 0.4288 0.8938 1.2655 0.0354  -0.1784 0.1600  443 SER D CB  
9435  O OG  . SER D 443 ? 0.4465 0.9378 1.3190 0.0587  -0.2034 0.1797  443 SER D OG  
9436  N N   . GLY D 444 ? 0.4634 0.8570 1.2542 0.0651  -0.0718 0.1509  444 GLY D N   
9437  C CA  . GLY D 444 ? 0.4766 0.8497 1.2724 0.0887  -0.0250 0.1533  444 GLY D CA  
9438  C C   . GLY D 444 ? 0.5116 0.8371 1.2445 0.0785  0.0092  0.1363  444 GLY D C   
9439  O O   . GLY D 444 ? 0.5199 0.8329 1.2146 0.0541  -0.0010 0.1244  444 GLY D O   
9440  N N   . ASP D 445 ? 0.5662 0.8623 1.2866 0.0991  0.0501  0.1357  445 ASP D N   
9441  C CA  . ASP D 445 ? 0.6094 0.8547 1.2621 0.0930  0.0807  0.1205  445 ASP D CA  
9442  C C   . ASP D 445 ? 0.6501 0.8429 1.2171 0.0912  0.0660  0.1098  445 ASP D C   
9443  O O   . ASP D 445 ? 0.6609 0.8348 1.2152 0.1086  0.0617  0.1142  445 ASP D O   
9444  C CB  . ASP D 445 ? 0.6253 0.8543 1.2908 0.1157  0.1303  0.1227  445 ASP D CB  
9445  C CG  . ASP D 445 ? 0.6732 0.8514 1.2684 0.1086  0.1608  0.1082  445 ASP D CG  
9446  O OD1 . ASP D 445 ? 0.7057 0.8446 1.2270 0.0959  0.1450  0.0955  445 ASP D OD1 
9447  O OD2 . ASP D 445 ? 0.6791 0.8570 1.2937 0.1167  0.2016  0.1109  445 ASP D OD2 
9448  N N   . ILE D 446 ? 0.6695 0.8384 1.1817 0.0704  0.0599  0.0971  446 ILE D N   
9449  C CA  . ILE D 446 ? 0.7000 0.8279 1.1425 0.0660  0.0444  0.0888  446 ILE D CA  
9450  C C   . ILE D 446 ? 0.7410 0.8192 1.1404 0.0813  0.0688  0.0827  446 ILE D C   
9451  O O   . ILE D 446 ? 0.7550 0.8046 1.1200 0.0852  0.0573  0.0815  446 ILE D O   
9452  C CB  . ILE D 446 ? 0.7091 0.8270 1.1116 0.0426  0.0340  0.0782  446 ILE D CB  
9453  C CG1 . ILE D 446 ? 0.7341 0.8156 1.0750 0.0385  0.0205  0.0716  446 ILE D CG1 
9454  C CG2 . ILE D 446 ? 0.7319 0.8354 1.1225 0.0380  0.0634  0.0717  446 ILE D CG2 
9455  C CD1 . ILE D 446 ? 0.7119 0.8071 1.0528 0.0347  -0.0104 0.0776  446 ILE D CD1 
9456  N N   . SER D 447 ? 0.7575 0.8208 1.1554 0.0898  0.1034  0.0789  447 SER D N   
9457  C CA  . SER D 447 ? 0.7989 0.8070 1.1465 0.1038  0.1258  0.0703  447 SER D CA  
9458  C C   . SER D 447 ? 0.7916 0.7957 1.1696 0.1299  0.1385  0.0786  447 SER D C   
9459  O O   . SER D 447 ? 0.8259 0.7774 1.1594 0.1420  0.1540  0.0704  447 SER D O   
9460  C CB  . SER D 447 ? 0.8310 0.8143 1.1490 0.1041  0.1592  0.0622  447 SER D CB  
9461  O OG  . SER D 447 ? 0.8103 0.8233 1.1866 0.1175  0.1890  0.0722  447 SER D OG  
9462  N N   . GLU D 448 ? 0.8192 0.8757 1.2723 0.1391  0.1316  0.0945  448 GLU D N   
9463  C CA  . GLU D 448 ? 0.8080 0.8661 1.2974 0.1660  0.1380  0.1062  448 GLU D CA  
9464  C C   . GLU D 448 ? 0.7972 0.8584 1.2833 0.1649  0.1006  0.1145  448 GLU D C   
9465  O O   . GLU D 448 ? 0.8075 0.8425 1.2908 0.1852  0.1044  0.1206  448 GLU D O   
9466  C CB  . GLU D 448 ? 0.7631 0.8814 1.3454 0.1797  0.1514  0.1224  448 GLU D CB  
9467  C CG  . GLU D 448 ? 0.7763 0.8800 1.3719 0.1995  0.2034  0.1210  448 GLU D CG  
9468  C CD  . GLU D 448 ? 0.7221 0.8962 1.4209 0.2065  0.2169  0.1382  448 GLU D CD  
9469  O OE1 . GLU D 448 ? 0.6753 0.9069 1.4390 0.2017  0.1816  0.1522  448 GLU D OE1 
9470  O OE2 . GLU D 448 ? 0.7262 0.8980 1.4414 0.2164  0.2624  0.1384  448 GLU D OE2 
9471  N N   . ALA D 449 ? 0.7202 0.8080 1.2025 0.1426  0.0668  0.1154  449 ALA D N   
9472  C CA  . ALA D 449 ? 0.7088 0.8041 1.1896 0.1426  0.0325  0.1264  449 ALA D CA  
9473  C C   . ALA D 449 ? 0.7437 0.7814 1.1578 0.1404  0.0301  0.1200  449 ALA D C   
9474  O O   . ALA D 449 ? 0.7470 0.7710 1.1599 0.1531  0.0193  0.1318  449 ALA D O   
9475  C CB  . ALA D 449 ? 0.6849 0.8183 1.1722 0.1195  0.0004  0.1270  449 ALA D CB  
9476  N N   . PHE D 450 ? 0.6961 0.6999 1.0573 0.1241  0.0390  0.1032  450 PHE D N   
9477  C CA  . PHE D 450 ? 0.7199 0.6782 1.0259 0.1149  0.0312  0.0973  450 PHE D CA  
9478  C C   . PHE D 450 ? 0.7560 0.6592 1.0239 0.1200  0.0557  0.0833  450 PHE D C   
9479  O O   . PHE D 450 ? 0.7696 0.6661 1.0273 0.1192  0.0754  0.0719  450 PHE D O   
9480  C CB  . PHE D 450 ? 0.7150 0.6821 0.9921 0.0895  0.0137  0.0904  450 PHE D CB  
9481  C CG  . PHE D 450 ? 0.6881 0.6969 0.9868 0.0831  -0.0115 0.1010  450 PHE D CG  
9482  C CD1 . PHE D 450 ? 0.6859 0.6915 0.9779 0.0873  -0.0299 0.1143  450 PHE D CD1 
9483  C CD2 . PHE D 450 ? 0.6695 0.7156 0.9905 0.0728  -0.0169 0.0978  450 PHE D CD2 
9484  C CE1 . PHE D 450 ? 0.6694 0.7066 0.9694 0.0819  -0.0547 0.1228  450 PHE D CE1 
9485  C CE2 . PHE D 450 ? 0.6482 0.7259 0.9820 0.0654  -0.0428 0.1048  450 PHE D CE2 
9486  C CZ  . PHE D 450 ? 0.6504 0.7230 0.9704 0.0705  -0.0625 0.1168  450 PHE D CZ  
9487  N N   . GLY D 451 ? 0.7191 0.5786 0.9618 0.1246  0.0543  0.0843  451 GLY D N   
9488  C CA  . GLY D 451 ? 0.7607 0.5589 0.9601 0.1268  0.0723  0.0690  451 GLY D CA  
9489  C C   . GLY D 451 ? 0.7748 0.5459 0.9262 0.1012  0.0593  0.0556  451 GLY D C   
9490  O O   . GLY D 451 ? 0.7629 0.5588 0.9074 0.0853  0.0514  0.0501  451 GLY D O   
9491  N N   . VAL D 452 ? 0.8201 0.5407 0.9423 0.0969  0.0562  0.0513  452 VAL D N   
9492  C CA  . VAL D 452 ? 0.8334 0.5305 0.9202 0.0716  0.0412  0.0404  452 VAL D CA  
9493  C C   . VAL D 452 ? 0.8231 0.5158 0.9191 0.0626  0.0263  0.0540  452 VAL D C   
9494  O O   . VAL D 452 ? 0.8311 0.5030 0.9375 0.0769  0.0317  0.0650  452 VAL D O   
9495  C CB  . VAL D 452 ? 0.8830 0.5162 0.9212 0.0688  0.0502  0.0196  452 VAL D CB  
9496  C CG1 . VAL D 452 ? 0.8963 0.5324 0.9127 0.0730  0.0636  0.0067  452 VAL D CG1 
9497  C CG2 . VAL D 452 ? 0.9104 0.4939 0.9434 0.0885  0.0668  0.0199  452 VAL D CG2 
9498  N N   . TYR D 453 ? 0.8241 0.5352 0.9169 0.0404  0.0100  0.0548  453 TYR D N   
9499  C CA  . TYR D 453 ? 0.8107 0.5239 0.9135 0.0306  -0.0003 0.0702  453 TYR D CA  
9500  C C   . TYR D 453 ? 0.8144 0.5124 0.9038 0.0045  -0.0110 0.0621  453 TYR D C   
9501  O O   . TYR D 453 ? 0.7875 0.5200 0.8823 -0.0083 -0.0197 0.0614  453 TYR D O   
9502  C CB  . TYR D 453 ? 0.7750 0.5410 0.8994 0.0337  -0.0074 0.0858  453 TYR D CB  
9503  C CG  . TYR D 453 ? 0.7663 0.5594 0.9119 0.0554  -0.0029 0.0918  453 TYR D CG  
9504  C CD1 . TYR D 453 ? 0.7737 0.5567 0.9339 0.0753  0.0003  0.1064  453 TYR D CD1 
9505  C CD2 . TYR D 453 ? 0.7502 0.5797 0.9060 0.0558  -0.0023 0.0845  453 TYR D CD2 
9506  C CE1 . TYR D 453 ? 0.7607 0.5750 0.9506 0.0950  0.0017  0.1137  453 TYR D CE1 
9507  C CE2 . TYR D 453 ? 0.7393 0.5983 0.9248 0.0729  0.0008  0.0911  453 TYR D CE2 
9508  C CZ  . TYR D 453 ? 0.7423 0.5964 0.9476 0.0925  0.0017  0.1058  453 TYR D CZ  
9509  O OH  . TYR D 453 ? 0.7258 0.6156 0.9707 0.1097  0.0022  0.1142  453 TYR D OH  
9510  N N   . PRO D 454 ? 0.8529 0.4995 0.9283 -0.0041 -0.0113 0.0563  454 PRO D N   
9511  C CA  . PRO D 454 ? 0.8552 0.4903 0.9254 -0.0314 -0.0253 0.0479  454 PRO D CA  
9512  C C   . PRO D 454 ? 0.8173 0.4869 0.9156 -0.0461 -0.0313 0.0653  454 PRO D C   
9513  O O   . PRO D 454 ? 0.8004 0.4858 0.9078 -0.0660 -0.0429 0.0611  454 PRO D O   
9514  C CB  . PRO D 454 ? 0.9034 0.4707 0.9549 -0.0368 -0.0240 0.0392  454 PRO D CB  
9515  C CG  . PRO D 454 ? 0.9268 0.4679 0.9673 -0.0081 -0.0057 0.0398  454 PRO D CG  
9516  C CD  . PRO D 454 ? 0.8864 0.4829 0.9543 0.0099  -0.0001 0.0586  454 PRO D CD  
9517  N N   . THR D 455 ? 0.8193 0.4997 0.9306 -0.0356 -0.0230 0.0859  455 THR D N   
9518  C CA  . THR D 455 ? 0.7962 0.5007 0.9262 -0.0470 -0.0227 0.1044  455 THR D CA  
9519  C C   . THR D 455 ? 0.7677 0.5229 0.9011 -0.0375 -0.0218 0.1124  455 THR D C   
9520  O O   . THR D 455 ? 0.7586 0.5297 0.8983 -0.0407 -0.0171 0.1293  455 THR D O   
9521  C CB  . THR D 455 ? 0.8164 0.4884 0.9481 -0.0433 -0.0135 0.1239  455 THR D CB  
9522  O OG1 . THR D 455 ? 0.8264 0.4955 0.9483 -0.0166 -0.0084 0.1321  455 THR D OG1 
9523  C CG2 . THR D 455 ? 0.8480 0.4638 0.9772 -0.0575 -0.0145 0.1155  455 THR D CG2 
9524  N N   . LEU D 456 ? 0.7416 0.5181 0.8684 -0.0262 -0.0246 0.1008  456 LEU D N   
9525  C CA  . LEU D 456 ? 0.7204 0.5393 0.8488 -0.0191 -0.0256 0.1062  456 LEU D CA  
9526  C C   . LEU D 456 ? 0.6989 0.5429 0.8343 -0.0344 -0.0276 0.1052  456 LEU D C   
9527  O O   . LEU D 456 ? 0.6917 0.5348 0.8319 -0.0463 -0.0330 0.0932  456 LEU D O   
9528  C CB  . LEU D 456 ? 0.7176 0.5516 0.8436 -0.0066 -0.0268 0.0942  456 LEU D CB  
9529  C CG  . LEU D 456 ? 0.7040 0.5750 0.8334 0.0021  -0.0301 0.0999  456 LEU D CG  
9530  C CD1 . LEU D 456 ? 0.7149 0.5838 0.8444 0.0149  -0.0320 0.1177  456 LEU D CD1 
9531  C CD2 . LEU D 456 ? 0.7004 0.5866 0.8358 0.0098  -0.0291 0.0878  456 LEU D CD2 
9532  N N   . ASN D 457 ? 0.6720 0.5368 0.8056 -0.0323 -0.0233 0.1183  457 ASN D N   
9533  C CA  . ASN D 457 ? 0.6567 0.5449 0.7983 -0.0423 -0.0198 0.1203  457 ASN D CA  
9534  C C   . ASN D 457 ? 0.6507 0.5662 0.7807 -0.0347 -0.0210 0.1152  457 ASN D C   
9535  O O   . ASN D 457 ? 0.6349 0.5669 0.7720 -0.0398 -0.0226 0.1061  457 ASN D O   
9536  C CB  . ASN D 457 ? 0.6674 0.5495 0.8120 -0.0470 -0.0075 0.1402  457 ASN D CB  
9537  C CG  . ASN D 457 ? 0.6571 0.5647 0.8115 -0.0530 0.0022  0.1447  457 ASN D CG  
9538  O OD1 . ASN D 457 ? 0.6688 0.5877 0.8019 -0.0438 0.0089  0.1491  457 ASN D OD1 
9539  N ND2 . ASN D 457 ? 0.6395 0.5551 0.8267 -0.0680 0.0024  0.1434  457 ASN D ND2 
9540  N N   . PHE D 458 ? 0.6391 0.5573 0.7508 -0.0229 -0.0224 0.1212  458 PHE D N   
9541  C CA  . PHE D 458 ? 0.6429 0.5811 0.7401 -0.0182 -0.0254 0.1163  458 PHE D CA  
9542  C C   . PHE D 458 ? 0.6496 0.5917 0.7423 -0.0074 -0.0369 0.1144  458 PHE D C   
9543  O O   . PHE D 458 ? 0.6624 0.5928 0.7514 0.0009  -0.0402 0.1257  458 PHE D O   
9544  C CB  . PHE D 458 ? 0.6661 0.6038 0.7417 -0.0174 -0.0160 0.1283  458 PHE D CB  
9545  C CG  . PHE D 458 ? 0.6825 0.6318 0.7356 -0.0140 -0.0184 0.1209  458 PHE D CG  
9546  C CD1 . PHE D 458 ? 0.7018 0.6523 0.7342 -0.0069 -0.0325 0.1193  458 PHE D CD1 
9547  C CD2 . PHE D 458 ? 0.6826 0.6399 0.7365 -0.0181 -0.0073 0.1161  458 PHE D CD2 
9548  C CE1 . PHE D 458 ? 0.7248 0.6800 0.7337 -0.0068 -0.0369 0.1105  458 PHE D CE1 
9549  C CE2 . PHE D 458 ? 0.7082 0.6677 0.7370 -0.0149 -0.0079 0.1080  458 PHE D CE2 
9550  C CZ  . PHE D 458 ? 0.7323 0.6884 0.7360 -0.0107 -0.0232 0.1041  458 PHE D CZ  
9551  N N   . ILE D 459 ? 0.6773 0.6364 0.7747 -0.0072 -0.0426 0.1018  459 ILE D N   
9552  C CA  . ILE D 459 ? 0.6787 0.6497 0.7837 0.0011  -0.0537 0.1006  459 ILE D CA  
9553  C C   . ILE D 459 ? 0.6799 0.6687 0.7796 -0.0034 -0.0599 0.0909  459 ILE D C   
9554  O O   . ILE D 459 ? 0.6721 0.6638 0.7737 -0.0104 -0.0533 0.0805  459 ILE D O   
9555  C CB  . ILE D 459 ? 0.6673 0.6357 0.7968 0.0061  -0.0506 0.0951  459 ILE D CB  
9556  C CG1 . ILE D 459 ? 0.6647 0.6520 0.8143 0.0160  -0.0596 0.0972  459 ILE D CG1 
9557  C CG2 . ILE D 459 ? 0.6570 0.6249 0.7901 -0.0016 -0.0429 0.0810  459 ILE D CG2 
9558  C CD1 . ILE D 459 ? 0.6677 0.6445 0.8360 0.0294  -0.0556 0.1036  459 ILE D CD1 
9559  N N   . ASP D 460 ? 0.6673 0.6653 0.7593 0.0003  -0.0746 0.0947  460 ASP D N   
9560  C CA  . ASP D 460 ? 0.6751 0.6841 0.7582 -0.0065 -0.0837 0.0848  460 ASP D CA  
9561  C C   . ASP D 460 ? 0.6628 0.6930 0.7706 -0.0034 -0.1029 0.0861  460 ASP D C   
9562  O O   . ASP D 460 ? 0.6786 0.7100 0.7735 0.0021  -0.1204 0.0955  460 ASP D O   
9563  C CB  . ASP D 460 ? 0.7151 0.7086 0.7529 -0.0083 -0.0847 0.0867  460 ASP D CB  
9564  C CG  . ASP D 460 ? 0.7342 0.7282 0.7557 -0.0167 -0.0905 0.0729  460 ASP D CG  
9565  O OD1 . ASP D 460 ? 0.7086 0.7167 0.7584 -0.0228 -0.0932 0.0631  460 ASP D OD1 
9566  O OD2 . ASP D 460 ? 0.7785 0.7545 0.7562 -0.0170 -0.0903 0.0718  460 ASP D OD2 
9567  N N   . LEU D 461 ? 0.6402 0.6878 0.7846 -0.0066 -0.0995 0.0784  461 LEU D N   
9568  C CA  . LEU D 461 ? 0.6207 0.6959 0.8043 -0.0049 -0.1144 0.0806  461 LEU D CA  
9569  C C   . LEU D 461 ? 0.6179 0.7054 0.8043 -0.0193 -0.1277 0.0701  461 LEU D C   
9570  O O   . LEU D 461 ? 0.5941 0.7092 0.8251 -0.0224 -0.1370 0.0701  461 LEU D O   
9571  C CB  . LEU D 461 ? 0.5986 0.6844 0.8250 0.0016  -0.0974 0.0808  461 LEU D CB  
9572  C CG  . LEU D 461 ? 0.6073 0.6734 0.8302 0.0142  -0.0823 0.0871  461 LEU D CG  
9573  C CD1 . LEU D 461 ? 0.6024 0.6704 0.8541 0.0193  -0.0620 0.0824  461 LEU D CD1 
9574  C CD2 . LEU D 461 ? 0.6114 0.6797 0.8401 0.0278  -0.0960 0.1025  461 LEU D CD2 
9575  N N   . SER D 462 ? 0.6680 0.7344 0.8103 -0.0281 -0.1276 0.0614  462 SER D N   
9576  C CA  . SER D 462 ? 0.6710 0.7378 0.8108 -0.0431 -0.1349 0.0483  462 SER D CA  
9577  C C   . SER D 462 ? 0.6744 0.7582 0.8241 -0.0498 -0.1673 0.0484  462 SER D C   
9578  O O   . SER D 462 ? 0.6877 0.7754 0.8263 -0.0414 -0.1866 0.0586  462 SER D O   
9579  C CB  . SER D 462 ? 0.7114 0.7461 0.7973 -0.0471 -0.1255 0.0397  462 SER D CB  
9580  O OG  . SER D 462 ? 0.7116 0.7345 0.7894 -0.0394 -0.1019 0.0436  462 SER D OG  
9581  N N   . ASN D 463 ? 0.6744 0.7671 0.8459 -0.0659 -0.1749 0.0376  463 ASN D N   
9582  C CA  . ASN D 463 ? 0.6745 0.7852 0.8630 -0.0779 -0.2098 0.0348  463 ASN D CA  
9583  C C   . ASN D 463 ? 0.6419 0.7941 0.8878 -0.0679 -0.2260 0.0507  463 ASN D C   
9584  O O   . ASN D 463 ? 0.6570 0.8158 0.8906 -0.0632 -0.2566 0.0582  463 ASN D O   
9585  C CB  . ASN D 463 ? 0.7304 0.8089 0.8466 -0.0816 -0.2323 0.0278  463 ASN D CB  
9586  C CG  . ASN D 463 ? 0.7688 0.8047 0.8301 -0.0876 -0.2125 0.0129  463 ASN D CG  
9587  O OD1 . ASN D 463 ? 0.7518 0.7848 0.8342 -0.0972 -0.1954 0.0042  463 ASN D OD1 
9588  N ND2 . ASN D 463 ? 0.8242 0.8253 0.8145 -0.0804 -0.2123 0.0115  463 ASN D ND2 
9589  N N   . ASN D 464 ? 0.6420 0.8199 0.9489 -0.0630 -0.2041 0.0567  464 ASN D N   
9590  C CA  . ASN D 464 ? 0.6103 0.8287 0.9818 -0.0504 -0.2115 0.0723  464 ASN D CA  
9591  C C   . ASN D 464 ? 0.5715 0.8230 1.0176 -0.0595 -0.1971 0.0717  464 ASN D C   
9592  O O   . ASN D 464 ? 0.5711 0.8131 1.0154 -0.0779 -0.1881 0.0597  464 ASN D O   
9593  C CB  . ASN D 464 ? 0.6144 0.8206 0.9744 -0.0267 -0.1904 0.0839  464 ASN D CB  
9594  C CG  . ASN D 464 ? 0.6447 0.8343 0.9579 -0.0155 -0.2118 0.0933  464 ASN D CG  
9595  O OD1 . ASN D 464 ? 0.6398 0.8528 0.9767 -0.0079 -0.2398 0.1056  464 ASN D OD1 
9596  N ND2 . ASN D 464 ? 0.6776 0.8272 0.9257 -0.0139 -0.1982 0.0893  464 ASN D ND2 
9597  N N   . ASN D 465 ? 0.6096 0.8983 1.1226 -0.0454 -0.1921 0.0861  465 ASN D N   
9598  C CA  . ASN D 465 ? 0.5729 0.8999 1.1671 -0.0518 -0.1769 0.0896  465 ASN D CA  
9599  C C   . ASN D 465 ? 0.5653 0.8915 1.1829 -0.0314 -0.1335 0.0972  465 ASN D C   
9600  O O   . ASN D 465 ? 0.5357 0.9006 1.2295 -0.0245 -0.1206 0.1079  465 ASN D O   
9601  C CB  . ASN D 465 ? 0.5426 0.9240 1.2116 -0.0550 -0.2128 0.1009  465 ASN D CB  
9602  C CG  . ASN D 465 ? 0.5371 0.9312 1.2230 -0.0862 -0.2414 0.0901  465 ASN D CG  
9603  O OD1 . ASN D 465 ? 0.5152 0.9274 1.2537 -0.1022 -0.2240 0.0876  465 ASN D OD1 
9604  N ND2 . ASN D 465 ? 0.5631 0.9424 1.1995 -0.0958 -0.2844 0.0834  465 ASN D ND2 
9605  N N   . PHE D 466 ? 0.5448 0.8262 1.0981 -0.0215 -0.1105 0.0917  466 PHE D N   
9606  C CA  . PHE D 466 ? 0.5513 0.8213 1.1125 -0.0038 -0.0710 0.0953  466 PHE D CA  
9607  C C   . PHE D 466 ? 0.5472 0.8168 1.1269 -0.0148 -0.0403 0.0899  466 PHE D C   
9608  O O   . PHE D 466 ? 0.5533 0.8068 1.1046 -0.0343 -0.0429 0.0796  466 PHE D O   
9609  C CB  . PHE D 466 ? 0.5880 0.8091 1.0753 0.0060  -0.0606 0.0898  466 PHE D CB  
9610  C CG  . PHE D 466 ? 0.5962 0.8116 1.0652 0.0195  -0.0818 0.0983  466 PHE D CG  
9611  C CD1 . PHE D 466 ? 0.5866 0.8191 1.0972 0.0408  -0.0797 0.1122  466 PHE D CD1 
9612  C CD2 . PHE D 466 ? 0.6157 0.8060 1.0255 0.0125  -0.1007 0.0940  466 PHE D CD2 
9613  C CE1 . PHE D 466 ? 0.5971 0.8196 1.0882 0.0541  -0.0984 0.1224  466 PHE D CE1 
9614  C CE2 . PHE D 466 ? 0.6280 0.8094 1.0177 0.0248  -0.1170 0.1043  466 PHE D CE2 
9615  C CZ  . PHE D 466 ? 0.6189 0.8152 1.0480 0.0453  -0.1170 0.1188  466 PHE D CZ  
9616  N N   . HIS D 467 ? 0.5654 0.8490 1.1900 -0.0006 -0.0087 0.0980  467 HIS D N   
9617  C CA  . HIS D 467 ? 0.5701 0.8472 1.2060 -0.0063 0.0285  0.0960  467 HIS D CA  
9618  C C   . HIS D 467 ? 0.6095 0.8482 1.2053 0.0151  0.0659  0.0947  467 HIS D C   
9619  O O   . HIS D 467 ? 0.6303 0.8482 1.1951 0.0318  0.0617  0.0943  467 HIS D O   
9620  C CB  . HIS D 467 ? 0.5264 0.8581 1.2598 -0.0116 0.0360  0.1078  467 HIS D CB  
9621  C CG  . HIS D 467 ? 0.5105 0.8699 1.3026 0.0148  0.0555  0.1221  467 HIS D CG  
9622  N ND1 . HIS D 467 ? 0.4854 0.8796 1.3213 0.0272  0.0261  0.1326  467 HIS D ND1 
9623  C CD2 . HIS D 467 ? 0.5182 0.8725 1.3302 0.0333  0.1031  0.1283  467 HIS D CD2 
9624  C CE1 . HIS D 467 ? 0.4744 0.8859 1.3606 0.0530  0.0551  0.1451  467 HIS D CE1 
9625  N NE2 . HIS D 467 ? 0.4947 0.8813 1.3660 0.0572  0.1035  0.1419  467 HIS D NE2 
9626  N N   . GLY D 468 ? 0.5930 0.8179 1.1860 0.0138  0.1028  0.0939  468 GLY D N   
9627  C CA  . GLY D 468 ? 0.6413 0.8218 1.1841 0.0321  0.1379  0.0904  468 GLY D CA  
9628  C C   . GLY D 468 ? 0.6892 0.8182 1.1446 0.0235  0.1360  0.0777  468 GLY D C   
9629  O O   . GLY D 468 ? 0.6807 0.8085 1.1189 0.0042  0.1163  0.0728  468 GLY D O   
9630  N N   . GLN D 469 ? 0.7076 0.7918 1.1071 0.0388  0.1561  0.0721  469 GLN D N   
9631  C CA  . GLN D 469 ? 0.7601 0.7959 1.0789 0.0331  0.1536  0.0612  469 GLN D CA  
9632  C C   . GLN D 469 ? 0.7833 0.7936 1.0603 0.0393  0.1321  0.0540  469 GLN D C   
9633  O O   . GLN D 469 ? 0.7716 0.7853 1.0674 0.0536  0.1321  0.0567  469 GLN D O   
9634  C CB  . GLN D 469 ? 0.8057 0.8027 1.0831 0.0424  0.1924  0.0596  469 GLN D CB  
9635  C CG  . GLN D 469 ? 0.7781 0.8002 1.1116 0.0478  0.2290  0.0708  469 GLN D CG  
9636  C CD  . GLN D 469 ? 0.8168 0.8011 1.1026 0.0484  0.2644  0.0714  469 GLN D CD  
9637  O OE1 . GLN D 469 ? 0.8738 0.8062 1.0765 0.0513  0.2636  0.0623  469 GLN D OE1 
9638  N NE2 . GLN D 469 ? 0.7857 0.7956 1.1242 0.0450  0.2947  0.0834  469 GLN D NE2 
9639  N N   . LEU D 470 ? 0.7697 0.7546 0.9940 0.0287  0.1148  0.0462  470 LEU D N   
9640  C CA  . LEU D 470 ? 0.7687 0.7313 0.9583 0.0305  0.0943  0.0403  470 LEU D CA  
9641  C C   . LEU D 470 ? 0.7990 0.7175 0.9481 0.0447  0.1121  0.0337  470 LEU D C   
9642  O O   . LEU D 470 ? 0.8351 0.7209 0.9401 0.0465  0.1293  0.0282  470 LEU D O   
9643  C CB  . LEU D 470 ? 0.7632 0.7144 0.9159 0.0162  0.0742  0.0353  470 LEU D CB  
9644  C CG  . LEU D 470 ? 0.7316 0.7146 0.9104 0.0031  0.0540  0.0388  470 LEU D CG  
9645  C CD1 . LEU D 470 ? 0.7105 0.6795 0.8552 -0.0045 0.0350  0.0348  470 LEU D CD1 
9646  C CD2 . LEU D 470 ? 0.7073 0.7226 0.9316 0.0059  0.0418  0.0452  470 LEU D CD2 
9647  N N   . SER D 471 ? 0.8249 0.7369 0.9830 0.0551  0.1076  0.0342  471 SER D N   
9648  C CA  . SER D 471 ? 0.8582 0.7199 0.9727 0.0674  0.1216  0.0254  471 SER D CA  
9649  C C   . SER D 471 ? 0.8777 0.7021 0.9332 0.0551  0.1012  0.0145  471 SER D C   
9650  O O   . SER D 471 ? 0.8527 0.6945 0.9141 0.0410  0.0752  0.0165  471 SER D O   
9651  C CB  . SER D 471 ? 0.8438 0.7065 0.9878 0.0820  0.1218  0.0304  471 SER D CB  
9652  O OG  . SER D 471 ? 0.8801 0.6854 0.9756 0.0912  0.1314  0.0195  471 SER D OG  
9653  N N   . ALA D 472 ? 0.8862 0.6581 0.8844 0.0606  0.1133  0.0029  472 ALA D N   
9654  C CA  . ALA D 472 ? 0.9075 0.6431 0.8547 0.0484  0.0895  -0.0079 472 ALA D CA  
9655  C C   . ALA D 472 ? 0.8994 0.6208 0.8544 0.0470  0.0741  -0.0099 472 ALA D C   
9656  O O   . ALA D 472 ? 0.9159 0.6083 0.8377 0.0347  0.0532  -0.0185 472 ALA D O   
9657  C CB  . ALA D 472 ? 0.9667 0.6451 0.8413 0.0533  0.1027  -0.0210 472 ALA D CB  
9658  N N   . ASN D 473 ? 0.9655 0.7071 0.9665 0.0585  0.0825  -0.0006 473 ASN D N   
9659  C CA  . ASN D 473 ? 0.9606 0.6863 0.9697 0.0583  0.0701  0.0008  473 ASN D CA  
9660  C C   . ASN D 473 ? 0.9358 0.6811 0.9538 0.0381  0.0404  0.0052  473 ASN D C   
9661  O O   . ASN D 473 ? 0.9441 0.6642 0.9537 0.0310  0.0281  0.0035  473 ASN D O   
9662  C CB  . ASN D 473 ? 0.9348 0.6868 0.9962 0.0759  0.0815  0.0146  473 ASN D CB  
9663  C CG  . ASN D 473 ? 0.9612 0.6832 1.0171 0.0994  0.1131  0.0109  473 ASN D CG  
9664  O OD1 . ASN D 473 ? 1.0049 0.6753 1.0066 0.1024  0.1272  -0.0042 473 ASN D OD1 
9665  N ND2 . ASN D 473 ? 0.9355 0.6887 1.0462 0.1175  0.1245  0.0250  473 ASN D ND2 
9666  N N   . TRP D 474 ? 0.8862 0.6742 0.9229 0.0289  0.0313  0.0114  474 TRP D N   
9667  C CA  . TRP D 474 ? 0.8547 0.6645 0.9045 0.0135  0.0090  0.0175  474 TRP D CA  
9668  C C   . TRP D 474 ? 0.8750 0.6569 0.8938 -0.0015 -0.0070 0.0085  474 TRP D C   
9669  O O   . TRP D 474 ? 0.8474 0.6376 0.8808 -0.0131 -0.0218 0.0141  474 TRP D O   
9670  C CB  . TRP D 474 ? 0.8200 0.6738 0.8905 0.0089  0.0057  0.0238  474 TRP D CB  
9671  C CG  . TRP D 474 ? 0.8014 0.6873 0.9083 0.0191  0.0147  0.0326  474 TRP D CG  
9672  C CD1 . TRP D 474 ? 0.8074 0.7084 0.9267 0.0250  0.0295  0.0323  474 TRP D CD1 
9673  C CD2 . TRP D 474 ? 0.7789 0.6866 0.9163 0.0237  0.0073  0.0442  474 TRP D CD2 
9674  N NE1 . TRP D 474 ? 0.7878 0.7226 0.9502 0.0313  0.0292  0.0422  474 TRP D NE1 
9675  C CE2 . TRP D 474 ? 0.7717 0.7101 0.9420 0.0316  0.0140  0.0494  474 TRP D CE2 
9676  C CE3 . TRP D 474 ? 0.7685 0.6716 0.9079 0.0216  -0.0044 0.0520  474 TRP D CE3 
9677  C CZ2 . TRP D 474 ? 0.7537 0.7190 0.9568 0.0378  0.0044  0.0613  474 TRP D CZ2 
9678  C CZ3 . TRP D 474 ? 0.7557 0.6808 0.9204 0.0294  -0.0103 0.0647  474 TRP D CZ3 
9679  C CH2 . TRP D 474 ? 0.7479 0.7042 0.9430 0.0376  -0.0084 0.0687  474 TRP D CH2 
9680  N N   . GLU D 475 ? 0.9549 0.7037 0.9316 -0.0017 -0.0047 -0.0043 475 GLU D N   
9681  C CA  . GLU D 475 ? 0.9672 0.6912 0.9156 -0.0173 -0.0263 -0.0130 475 GLU D CA  
9682  C C   . GLU D 475 ? 0.9761 0.6687 0.9247 -0.0249 -0.0355 -0.0164 475 GLU D C   
9683  O O   . GLU D 475 ? 0.9659 0.6564 0.9189 -0.0427 -0.0575 -0.0173 475 GLU D O   
9684  C CB  . GLU D 475 ? 1.0157 0.7025 0.9078 -0.0140 -0.0232 -0.0263 475 GLU D CB  
9685  C CG  . GLU D 475 ? 1.0373 0.6970 0.8966 -0.0304 -0.0516 -0.0361 475 GLU D CG  
9686  C CD  . GLU D 475 ? 1.1022 0.7036 0.8890 -0.0254 -0.0487 -0.0526 475 GLU D CD  
9687  O OE1 . GLU D 475 ? 1.1298 0.7004 0.8923 -0.0092 -0.0211 -0.0585 475 GLU D OE1 
9688  O OE2 . GLU D 475 ? 1.1265 0.7121 0.8792 -0.0366 -0.0741 -0.0591 475 GLU D OE2 
9689  N N   . GLN D 476 ? 0.9924 0.6610 0.9412 -0.0116 -0.0184 -0.0168 476 GLN D N   
9690  C CA  . GLN D 476 ? 1.0056 0.6382 0.9543 -0.0180 -0.0243 -0.0188 476 GLN D CA  
9691  C C   . GLN D 476 ? 0.9624 0.6290 0.9574 -0.0281 -0.0340 -0.0019 476 GLN D C   
9692  O O   . GLN D 476 ? 0.9682 0.6095 0.9673 -0.0410 -0.0435 -0.0015 476 GLN D O   
9693  C CB  . GLN D 476 ? 1.0355 0.6327 0.9744 0.0032  -0.0004 -0.0214 476 GLN D CB  
9694  C CG  . GLN D 476 ? 1.0758 0.6361 0.9664 0.0169  0.0175  -0.0370 476 GLN D CG  
9695  C CD  . GLN D 476 ? 1.1185 0.6133 0.9783 0.0300  0.0340  -0.0480 476 GLN D CD  
9696  O OE1 . GLN D 476 ? 1.1134 0.5975 0.9978 0.0339  0.0362  -0.0402 476 GLN D OE1 
9697  N NE2 . GLN D 476 ? 1.1650 0.6102 0.9654 0.0381  0.0473  -0.0658 476 GLN D NE2 
9698  N N   . SER D 477 ? 0.9117 0.6309 0.9383 -0.0233 -0.0307 0.0120  477 SER D N   
9699  C CA  . SER D 477 ? 0.8693 0.6194 0.9301 -0.0317 -0.0373 0.0282  477 SER D CA  
9700  C C   . SER D 477 ? 0.8469 0.6148 0.9158 -0.0514 -0.0540 0.0277  477 SER D C   
9701  O O   . SER D 477 ? 0.8124 0.6207 0.8996 -0.0529 -0.0554 0.0359  477 SER D O   
9702  C CB  . SER D 477 ? 0.8389 0.6313 0.9212 -0.0187 -0.0289 0.0405  477 SER D CB  
9703  O OG  . SER D 477 ? 0.8535 0.6363 0.9400 -0.0003 -0.0165 0.0442  477 SER D OG  
9704  N N   . GLN D 478 ? 0.9092 0.6443 0.9652 -0.0665 -0.0676 0.0178  478 GLN D N   
9705  C CA  . GLN D 478 ? 0.8941 0.6456 0.9598 -0.0844 -0.0876 0.0157  478 GLN D CA  
9706  C C   . GLN D 478 ? 0.8491 0.6419 0.9613 -0.0938 -0.0883 0.0335  478 GLN D C   
9707  O O   . GLN D 478 ? 0.8285 0.6488 0.9599 -0.1036 -0.1008 0.0358  478 GLN D O   
9708  C CB  . GLN D 478 ? 0.9298 0.6355 0.9752 -0.1013 -0.1064 0.0015  478 GLN D CB  
9709  C CG  . GLN D 478 ? 0.9762 0.6458 0.9658 -0.0956 -0.1123 -0.0183 478 GLN D CG  
9710  C CD  . GLN D 478 ? 0.9643 0.6633 0.9480 -0.0977 -0.1268 -0.0191 478 GLN D CD  
9711  O OE1 . GLN D 478 ? 0.9282 0.6645 0.9501 -0.1102 -0.1425 -0.0097 478 GLN D OE1 
9712  N NE2 . GLN D 478 ? 0.9972 0.6790 0.9347 -0.0836 -0.1190 -0.0286 478 GLN D NE2 
9713  N N   . LYS D 479 ? 0.8121 0.6089 0.9415 -0.0891 -0.0740 0.0474  479 LYS D N   
9714  C CA  . LYS D 479 ? 0.7800 0.6099 0.9453 -0.0956 -0.0688 0.0654  479 LYS D CA  
9715  C C   . LYS D 479 ? 0.7588 0.6240 0.9241 -0.0804 -0.0564 0.0738  479 LYS D C   
9716  O O   . LYS D 479 ? 0.7436 0.6300 0.9275 -0.0815 -0.0470 0.0888  479 LYS D O   
9717  C CB  . LYS D 479 ? 0.7909 0.5970 0.9684 -0.1015 -0.0606 0.0775  479 LYS D CB  
9718  C CG  . LYS D 479 ? 0.8144 0.5811 0.9940 -0.1206 -0.0740 0.0683  479 LYS D CG  
9719  C CD  . LYS D 479 ? 0.8194 0.5679 1.0225 -0.1321 -0.0653 0.0842  479 LYS D CD  
9720  C CE  . LYS D 479 ? 0.8436 0.5511 1.0517 -0.1556 -0.0817 0.0730  479 LYS D CE  
9721  N NZ  . LYS D 479 ? 0.8484 0.5367 1.0859 -0.1712 -0.0725 0.0899  479 LYS D NZ  
9722  N N   . LEU D 480 ? 0.7277 0.5965 0.8707 -0.0672 -0.0552 0.0644  480 LEU D N   
9723  C CA  . LEU D 480 ? 0.7120 0.6096 0.8537 -0.0556 -0.0467 0.0698  480 LEU D CA  
9724  C C   . LEU D 480 ? 0.6911 0.6175 0.8461 -0.0606 -0.0488 0.0717  480 LEU D C   
9725  O O   . LEU D 480 ? 0.6900 0.6177 0.8460 -0.0664 -0.0594 0.0640  480 LEU D O   
9726  C CB  . LEU D 480 ? 0.7228 0.6164 0.8452 -0.0431 -0.0444 0.0596  480 LEU D CB  
9727  C CG  . LEU D 480 ? 0.7144 0.6308 0.8370 -0.0322 -0.0381 0.0642  480 LEU D CG  
9728  C CD1 . LEU D 480 ? 0.7232 0.6356 0.8491 -0.0251 -0.0349 0.0761  480 LEU D CD1 
9729  C CD2 . LEU D 480 ? 0.7232 0.6394 0.8370 -0.0241 -0.0350 0.0543  480 LEU D CD2 
9730  N N   . VAL D 481 ? 0.6690 0.6155 0.8304 -0.0565 -0.0387 0.0824  481 VAL D N   
9731  C CA  . VAL D 481 ? 0.6565 0.6277 0.8300 -0.0570 -0.0357 0.0851  481 VAL D CA  
9732  C C   . VAL D 481 ? 0.6616 0.6427 0.8162 -0.0461 -0.0286 0.0827  481 VAL D C   
9733  O O   . VAL D 481 ? 0.6579 0.6527 0.8164 -0.0440 -0.0262 0.0812  481 VAL D O   
9734  C CB  . VAL D 481 ? 0.6524 0.6356 0.8531 -0.0637 -0.0259 0.1000  481 VAL D CB  
9735  C CG1 . VAL D 481 ? 0.6439 0.6217 0.8730 -0.0792 -0.0368 0.1012  481 VAL D CG1 
9736  C CG2 . VAL D 481 ? 0.6704 0.6441 0.8566 -0.0585 -0.0123 0.1115  481 VAL D CG2 
9737  N N   . ALA D 482 ? 0.6447 0.6186 0.7808 -0.0392 -0.0269 0.0824  482 ALA D N   
9738  C CA  . ALA D 482 ? 0.6557 0.6369 0.7748 -0.0323 -0.0249 0.0784  482 ALA D CA  
9739  C C   . ALA D 482 ? 0.6589 0.6358 0.7721 -0.0278 -0.0314 0.0720  482 ALA D C   
9740  O O   . ALA D 482 ? 0.6695 0.6401 0.7816 -0.0238 -0.0336 0.0778  482 ALA D O   
9741  C CB  . ALA D 482 ? 0.6810 0.6626 0.7853 -0.0286 -0.0167 0.0879  482 ALA D CB  
9742  N N   . PHE D 483 ? 0.6576 0.6382 0.7699 -0.0275 -0.0328 0.0622  483 PHE D N   
9743  C CA  . PHE D 483 ? 0.6633 0.6450 0.7786 -0.0234 -0.0347 0.0574  483 PHE D CA  
9744  C C   . PHE D 483 ? 0.6688 0.6618 0.7808 -0.0243 -0.0357 0.0532  483 PHE D C   
9745  O O   . PHE D 483 ? 0.6576 0.6498 0.7663 -0.0272 -0.0320 0.0473  483 PHE D O   
9746  C CB  . PHE D 483 ? 0.6599 0.6302 0.7751 -0.0233 -0.0318 0.0501  483 PHE D CB  
9747  C CG  . PHE D 483 ? 0.6738 0.6438 0.7968 -0.0167 -0.0273 0.0475  483 PHE D CG  
9748  C CD1 . PHE D 483 ? 0.6824 0.6615 0.8196 -0.0106 -0.0300 0.0537  483 PHE D CD1 
9749  C CD2 . PHE D 483 ? 0.6850 0.6454 0.8015 -0.0152 -0.0191 0.0405  483 PHE D CD2 
9750  C CE1 . PHE D 483 ? 0.6936 0.6782 0.8487 -0.0026 -0.0242 0.0534  483 PHE D CE1 
9751  C CE2 . PHE D 483 ? 0.7029 0.6647 0.8317 -0.0076 -0.0092 0.0397  483 PHE D CE2 
9752  C CZ  . PHE D 483 ? 0.7042 0.6809 0.8572 -0.0011 -0.0116 0.0463  483 PHE D CZ  
9753  N N   . ILE D 484 ? 0.6353 0.6361 0.7472 -0.0224 -0.0427 0.0564  484 ILE D N   
9754  C CA  . ILE D 484 ? 0.6412 0.6483 0.7458 -0.0264 -0.0481 0.0514  484 ILE D CA  
9755  C C   . ILE D 484 ? 0.6295 0.6521 0.7562 -0.0259 -0.0576 0.0512  484 ILE D C   
9756  O O   . ILE D 484 ? 0.6350 0.6638 0.7666 -0.0205 -0.0677 0.0588  484 ILE D O   
9757  C CB  . ILE D 484 ? 0.6766 0.6764 0.7535 -0.0260 -0.0513 0.0549  484 ILE D CB  
9758  C CG1 . ILE D 484 ? 0.6792 0.6700 0.7472 -0.0249 -0.0382 0.0586  484 ILE D CG1 
9759  C CG2 . ILE D 484 ? 0.6984 0.6951 0.7589 -0.0316 -0.0571 0.0459  484 ILE D CG2 
9760  C CD1 . ILE D 484 ? 0.7155 0.6964 0.7550 -0.0223 -0.0335 0.0640  484 ILE D CD1 
9761  N N   . LEU D 485 ? 0.6947 0.7244 0.8380 -0.0313 -0.0540 0.0445  485 LEU D N   
9762  C CA  . LEU D 485 ? 0.6807 0.7309 0.8592 -0.0317 -0.0586 0.0456  485 LEU D CA  
9763  C C   . LEU D 485 ? 0.6730 0.7298 0.8605 -0.0443 -0.0630 0.0382  485 LEU D C   
9764  O O   . LEU D 485 ? 0.6589 0.7269 0.8769 -0.0481 -0.0545 0.0374  485 LEU D O   
9765  C CB  . LEU D 485 ? 0.6794 0.7294 0.8777 -0.0247 -0.0419 0.0471  485 LEU D CB  
9766  C CG  . LEU D 485 ? 0.6759 0.7454 0.9127 -0.0155 -0.0420 0.0542  485 LEU D CG  
9767  C CD1 . LEU D 485 ? 0.6995 0.7539 0.9367 -0.0057 -0.0209 0.0539  485 LEU D CD1 
9768  C CD2 . LEU D 485 ? 0.6532 0.7518 0.9317 -0.0225 -0.0476 0.0547  485 LEU D CD2 
9769  N N   . SER D 486 ? 0.7029 0.7487 0.8623 -0.0513 -0.0739 0.0327  486 SER D N   
9770  C CA  . SER D 486 ? 0.7051 0.7465 0.8664 -0.0650 -0.0764 0.0235  486 SER D CA  
9771  C C   . SER D 486 ? 0.6985 0.7621 0.8891 -0.0749 -0.0986 0.0225  486 SER D C   
9772  O O   . SER D 486 ? 0.6990 0.7785 0.8973 -0.0694 -0.1163 0.0291  486 SER D O   
9773  C CB  . SER D 486 ? 0.7411 0.7537 0.8557 -0.0676 -0.0757 0.0158  486 SER D CB  
9774  O OG  . SER D 486 ? 0.7753 0.7821 0.8597 -0.0639 -0.0899 0.0170  486 SER D OG  
9775  N N   . ASN D 487 ? 0.7235 0.7870 0.9319 -0.0901 -0.0990 0.0152  487 ASN D N   
9776  C CA  . ASN D 487 ? 0.7140 0.8002 0.9590 -0.1050 -0.1221 0.0129  487 ASN D CA  
9777  C C   . ASN D 487 ? 0.6818 0.8102 0.9846 -0.0975 -0.1284 0.0256  487 ASN D C   
9778  O O   . ASN D 487 ? 0.6807 0.8297 0.9973 -0.0978 -0.1567 0.0294  487 ASN D O   
9779  C CB  . ASN D 487 ? 0.7510 0.8201 0.9534 -0.1127 -0.1510 0.0039  487 ASN D CB  
9780  C CG  . ASN D 487 ? 0.7453 0.8299 0.9803 -0.1341 -0.1784 -0.0027 487 ASN D CG  
9781  O OD1 . ASN D 487 ? 0.7200 0.8186 1.0037 -0.1470 -0.1692 -0.0032 487 ASN D OD1 
9782  N ND2 . ASN D 487 ? 0.7719 0.8529 0.9798 -0.1389 -0.2127 -0.0072 487 ASN D ND2 
9783  N N   . ASN D 488 ? 0.6456 0.7846 0.9798 -0.0890 -0.1014 0.0328  488 ASN D N   
9784  C CA  . ASN D 488 ? 0.6191 0.7959 1.0145 -0.0801 -0.0983 0.0448  488 ASN D CA  
9785  C C   . ASN D 488 ? 0.5999 0.7930 1.0474 -0.0905 -0.0774 0.0464  488 ASN D C   
9786  O O   . ASN D 488 ? 0.6072 0.7817 1.0426 -0.1066 -0.0708 0.0386  488 ASN D O   
9787  C CB  . ASN D 488 ? 0.6261 0.7942 1.0062 -0.0575 -0.0809 0.0522  488 ASN D CB  
9788  C CG  . ASN D 488 ? 0.6355 0.8044 0.9956 -0.0465 -0.1035 0.0579  488 ASN D CG  
9789  O OD1 . ASN D 488 ? 0.6223 0.8176 1.0209 -0.0358 -0.1133 0.0688  488 ASN D OD1 
9790  N ND2 . ASN D 488 ? 0.6606 0.7995 0.9611 -0.0475 -0.1098 0.0524  488 ASN D ND2 
9791  N N   . SER D 489 ? 0.5683 0.7944 1.0752 -0.0805 -0.0645 0.0580  489 SER D N   
9792  C CA  . SER D 489 ? 0.5539 0.7944 1.1104 -0.0866 -0.0352 0.0628  489 SER D CA  
9793  C C   . SER D 489 ? 0.5757 0.7908 1.1054 -0.0687 0.0049  0.0658  489 SER D C   
9794  O O   . SER D 489 ? 0.5679 0.7994 1.1417 -0.0621 0.0337  0.0746  489 SER D O   
9795  C CB  . SER D 489 ? 0.5163 0.8132 1.1647 -0.0876 -0.0433 0.0748  489 SER D CB  
9796  O OG  . SER D 489 ? 0.5023 0.8218 1.1726 -0.1058 -0.0867 0.0713  489 SER D OG  
9797  N N   . ILE D 490 ? 0.5871 0.7617 1.0450 -0.0607 0.0071  0.0588  490 ILE D N   
9798  C CA  . ILE D 490 ? 0.6186 0.7646 1.0421 -0.0446 0.0373  0.0597  490 ILE D CA  
9799  C C   . ILE D 490 ? 0.6308 0.7604 1.0504 -0.0518 0.0672  0.0604  490 ILE D C   
9800  O O   . ILE D 490 ? 0.6288 0.7449 1.0328 -0.0679 0.0625  0.0558  490 ILE D O   
9801  C CB  . ILE D 490 ? 0.6452 0.7560 1.0003 -0.0386 0.0269  0.0525  490 ILE D CB  
9802  C CG1 . ILE D 490 ? 0.6362 0.7595 0.9933 -0.0313 0.0015  0.0546  490 ILE D CG1 
9803  C CG2 . ILE D 490 ? 0.6873 0.7660 1.0041 -0.0250 0.0522  0.0516  490 ILE D CG2 
9804  C CD1 . ILE D 490 ? 0.6315 0.7764 1.0304 -0.0149 0.0080  0.0640  490 ILE D CD1 
9805  N N   . THR D 491 ? 0.6115 0.7372 1.0407 -0.0386 0.1002  0.0667  491 THR D N   
9806  C CA  . THR D 491 ? 0.6304 0.7358 1.0494 -0.0416 0.1347  0.0703  491 THR D CA  
9807  C C   . THR D 491 ? 0.6867 0.7470 1.0377 -0.0237 0.1561  0.0675  491 THR D C   
9808  O O   . THR D 491 ? 0.7102 0.7561 1.0272 -0.0123 0.1424  0.0616  491 THR D O   
9809  C CB  . THR D 491 ? 0.6008 0.7435 1.0980 -0.0432 0.1598  0.0822  491 THR D CB  
9810  O OG1 . THR D 491 ? 0.6063 0.7601 1.1234 -0.0204 0.1768  0.0875  491 THR D OG1 
9811  C CG2 . THR D 491 ? 0.5494 0.7396 1.1179 -0.0629 0.1306  0.0842  491 THR D CG2 
9812  N N   . GLY D 492 ? 0.6630 0.6976 0.9912 -0.0225 0.1892  0.0720  492 GLY D N   
9813  C CA  . GLY D 492 ? 0.7243 0.7112 0.9808 -0.0063 0.2084  0.0688  492 GLY D CA  
9814  C C   . GLY D 492 ? 0.7537 0.7032 0.9395 -0.0108 0.1886  0.0617  492 GLY D C   
9815  O O   . GLY D 492 ? 0.7264 0.6816 0.9164 -0.0252 0.1695  0.0608  492 GLY D O   
9816  N N   . ALA D 493 ? 0.7684 0.6775 0.8888 0.0025  0.1927  0.0564  493 ALA D N   
9817  C CA  . ALA D 493 ? 0.7938 0.6691 0.8499 0.0006  0.1728  0.0512  493 ALA D CA  
9818  C C   . ALA D 493 ? 0.7942 0.6696 0.8363 0.0037  0.1422  0.0418  493 ALA D C   
9819  O O   . ALA D 493 ? 0.7963 0.6836 0.8606 0.0107  0.1416  0.0388  493 ALA D O   
9820  C CB  . ALA D 493 ? 0.8561 0.6811 0.8416 0.0106  0.1956  0.0528  493 ALA D CB  
9821  N N   . ILE D 494 ? 0.7990 0.6616 0.8085 -0.0014 0.1179  0.0388  494 ILE D N   
9822  C CA  . ILE D 494 ? 0.7885 0.6500 0.7858 -0.0008 0.0903  0.0318  494 ILE D CA  
9823  C C   . ILE D 494 ? 0.8421 0.6631 0.7846 0.0086  0.0933  0.0252  494 ILE D C   
9824  O O   . ILE D 494 ? 0.8859 0.6737 0.7755 0.0109  0.0949  0.0252  494 ILE D O   
9825  C CB  . ILE D 494 ? 0.7627 0.6287 0.7530 -0.0086 0.0661  0.0327  494 ILE D CB  
9826  C CG1 . ILE D 494 ? 0.7164 0.6123 0.7505 -0.0178 0.0643  0.0364  494 ILE D CG1 
9827  C CG2 . ILE D 494 ? 0.7508 0.6201 0.7380 -0.0094 0.0410  0.0277  494 ILE D CG2 
9828  C CD1 . ILE D 494 ? 0.6953 0.5938 0.7239 -0.0223 0.0450  0.0367  494 ILE D CD1 
9829  N N   . PRO D 495 ? 0.8633 0.6808 0.8114 0.0144  0.0924  0.0192  495 PRO D N   
9830  C CA  . PRO D 495 ? 0.9142 0.6850 0.8044 0.0221  0.0942  0.0098  495 PRO D CA  
9831  C C   . PRO D 495 ? 0.9295 0.6806 0.7783 0.0145  0.0636  0.0053  495 PRO D C   
9832  O O   . PRO D 495 ? 0.8871 0.6653 0.7654 0.0052  0.0391  0.0077  495 PRO D O   
9833  C CB  . PRO D 495 ? 0.8936 0.6698 0.8107 0.0271  0.0930  0.0054  495 PRO D CB  
9834  C CG  . PRO D 495 ? 0.8472 0.6729 0.8345 0.0265  0.0996  0.0148  495 PRO D CG  
9835  C CD  . PRO D 495 ? 0.8203 0.6723 0.8243 0.0144  0.0878  0.0209  495 PRO D CD  
9836  N N   . PRO D 496 ? 0.9529 0.6572 0.7333 0.0187  0.0641  -0.0003 496 PRO D N   
9837  C CA  . PRO D 496 ? 0.9747 0.6639 0.7201 0.0112  0.0298  -0.0033 496 PRO D CA  
9838  C C   . PRO D 496 ? 0.9464 0.6417 0.7099 0.0021  0.0011  -0.0107 496 PRO D C   
9839  O O   . PRO D 496 ? 0.9370 0.6444 0.7069 -0.0072 -0.0289 -0.0086 496 PRO D O   
9840  C CB  . PRO D 496 ? 1.0553 0.6856 0.7153 0.0191  0.0374  -0.0095 496 PRO D CB  
9841  C CG  . PRO D 496 ? 1.0712 0.6944 0.7285 0.0306  0.0815  -0.0044 496 PRO D CG  
9842  C CD  . PRO D 496 ? 1.0116 0.6741 0.7417 0.0313  0.0960  -0.0033 496 PRO D CD  
9843  N N   . GLU D 497 ? 1.0451 0.7319 0.8201 0.0049  0.0108  -0.0178 497 GLU D N   
9844  C CA  . GLU D 497 ? 1.0238 0.7094 0.8140 -0.0048 -0.0134 -0.0238 497 GLU D CA  
9845  C C   . GLU D 497 ? 0.9573 0.6954 0.8138 -0.0136 -0.0266 -0.0133 497 GLU D C   
9846  O O   . GLU D 497 ? 0.9375 0.6797 0.8102 -0.0243 -0.0484 -0.0147 497 GLU D O   
9847  C CB  . GLU D 497 ? 1.0349 0.6927 0.8192 0.0033  0.0043  -0.0323 497 GLU D CB  
9848  C CG  . GLU D 497 ? 1.1027 0.6955 0.8103 0.0110  0.0140  -0.0467 497 GLU D CG  
9849  C CD  . GLU D 497 ? 1.1314 0.7132 0.8164 0.0278  0.0525  -0.0435 497 GLU D CD  
9850  O OE1 . GLU D 497 ? 1.0927 0.7186 0.8336 0.0333  0.0731  -0.0312 497 GLU D OE1 
9851  O OE2 . GLU D 497 ? 1.1929 0.7204 0.8031 0.0347  0.0621  -0.0529 497 GLU D OE2 
9852  N N   . ILE D 498 ? 0.8982 0.6734 0.7912 -0.0101 -0.0129 -0.0031 498 ILE D N   
9853  C CA  . ILE D 498 ? 0.8397 0.6575 0.7837 -0.0169 -0.0232 0.0057  498 ILE D CA  
9854  C C   . ILE D 498 ? 0.8315 0.6575 0.7757 -0.0260 -0.0481 0.0084  498 ILE D C   
9855  O O   . ILE D 498 ? 0.7936 0.6404 0.7705 -0.0335 -0.0607 0.0125  498 ILE D O   
9856  C CB  . ILE D 498 ? 0.8147 0.6620 0.7866 -0.0130 -0.0067 0.0133  498 ILE D CB  
9857  C CG1 . ILE D 498 ? 0.8205 0.6698 0.8081 -0.0045 0.0150  0.0131  498 ILE D CG1 
9858  C CG2 . ILE D 498 ? 0.7589 0.6411 0.7693 -0.0192 -0.0173 0.0204  498 ILE D CG2 
9859  C CD1 . ILE D 498 ? 0.7884 0.6559 0.8114 -0.0044 0.0102  0.0161  498 ILE D CD1 
9860  N N   . TRP D 499 ? 0.8590 0.6695 0.7689 -0.0244 -0.0545 0.0081  499 TRP D N   
9861  C CA  . TRP D 499 ? 0.8596 0.6820 0.7762 -0.0307 -0.0800 0.0128  499 TRP D CA  
9862  C C   . TRP D 499 ? 0.8656 0.6742 0.7774 -0.0414 -0.1056 0.0063  499 TRP D C   
9863  O O   . TRP D 499 ? 0.8418 0.6729 0.7825 -0.0492 -0.1274 0.0123  499 TRP D O   
9864  C CB  . TRP D 499 ? 0.9127 0.7189 0.7905 -0.0243 -0.0825 0.0163  499 TRP D CB  
9865  C CG  . TRP D 499 ? 0.9061 0.7145 0.7818 -0.0160 -0.0544 0.0210  499 TRP D CG  
9866  C CD1 . TRP D 499 ? 0.9516 0.7291 0.7837 -0.0087 -0.0351 0.0194  499 TRP D CD1 
9867  C CD2 . TRP D 499 ? 0.8476 0.6884 0.7669 -0.0158 -0.0416 0.0281  499 TRP D CD2 
9868  N NE1 . TRP D 499 ? 0.9192 0.7120 0.7734 -0.0058 -0.0116 0.0261  499 TRP D NE1 
9869  C CE2 . TRP D 499 ? 0.8580 0.6878 0.7632 -0.0107 -0.0175 0.0301  499 TRP D CE2 
9870  C CE3 . TRP D 499 ? 0.7933 0.6678 0.7586 -0.0197 -0.0472 0.0325  499 TRP D CE3 
9871  C CZ2 . TRP D 499 ? 0.8177 0.6690 0.7555 -0.0119 -0.0036 0.0349  499 TRP D CZ2 
9872  C CZ3 . TRP D 499 ? 0.7574 0.6485 0.7452 -0.0186 -0.0322 0.0363  499 TRP D CZ3 
9873  C CH2 . TRP D 499 ? 0.7706 0.6501 0.7456 -0.0159 -0.0129 0.0367  499 TRP D CH2 
9874  N N   . ASN D 500 ? 1.0051 0.7768 0.8851 -0.0424 -0.1026 -0.0056 500 ASN D N   
9875  C CA  . ASN D 500 ? 1.0072 0.7610 0.8848 -0.0558 -0.1271 -0.0133 500 ASN D CA  
9876  C C   . ASN D 500 ? 0.9543 0.7320 0.8866 -0.0636 -0.1242 -0.0084 500 ASN D C   
9877  O O   . ASN D 500 ? 0.9542 0.7168 0.8922 -0.0769 -0.1417 -0.0136 500 ASN D O   
9878  C CB  . ASN D 500 ? 1.0666 0.7603 0.8788 -0.0532 -0.1246 -0.0299 500 ASN D CB  
9879  C CG  . ASN D 500 ? 1.1187 0.7791 0.8710 -0.0561 -0.1499 -0.0371 500 ASN D CG  
9880  O OD1 . ASN D 500 ? 1.1057 0.7921 0.8741 -0.0609 -0.1736 -0.0283 500 ASN D OD1 
9881  N ND2 . ASN D 500 ? 1.1780 0.7783 0.8581 -0.0514 -0.1447 -0.0525 500 ASN D ND2 
9882  N N   . MET D 501 ? 0.8772 0.6883 0.8464 -0.0565 -0.1037 0.0017  501 MET D N   
9883  C CA  . MET D 501 ? 0.8301 0.6648 0.8462 -0.0623 -0.1004 0.0099  501 MET D CA  
9884  C C   . MET D 501 ? 0.7932 0.6653 0.8502 -0.0705 -0.1137 0.0211  501 MET D C   
9885  O O   . MET D 501 ? 0.7594 0.6634 0.8438 -0.0653 -0.1019 0.0313  501 MET D O   
9886  C CB  . MET D 501 ? 0.8073 0.6579 0.8375 -0.0507 -0.0762 0.0156  501 MET D CB  
9887  C CG  . MET D 501 ? 0.8410 0.6648 0.8428 -0.0392 -0.0592 0.0078  501 MET D CG  
9888  S SD  . MET D 501 ? 0.8120 0.6608 0.8444 -0.0279 -0.0385 0.0165  501 MET D SD  
9889  C CE  . MET D 501 ? 0.7589 0.6487 0.8269 -0.0345 -0.0455 0.0289  501 MET D CE  
9890  N N   . THR D 502 ? 0.8363 0.7027 0.8979 -0.0836 -0.1389 0.0187  502 THR D N   
9891  C CA  . THR D 502 ? 0.8069 0.7107 0.9101 -0.0895 -0.1537 0.0299  502 THR D CA  
9892  C C   . THR D 502 ? 0.7581 0.6978 0.9160 -0.0918 -0.1394 0.0441  502 THR D C   
9893  O O   . THR D 502 ? 0.7332 0.7079 0.9258 -0.0890 -0.1389 0.0555  502 THR D O   
9894  C CB  . THR D 502 ? 0.8210 0.7136 0.9264 -0.1060 -0.1875 0.0248  502 THR D CB  
9895  O OG1 . THR D 502 ? 0.8135 0.6920 0.9374 -0.1214 -0.1902 0.0221  502 THR D OG1 
9896  C CG2 . THR D 502 ? 0.8799 0.7283 0.9169 -0.1027 -0.2016 0.0098  502 THR D CG2 
9897  N N   . GLN D 503 ? 0.7779 0.7067 0.9411 -0.0947 -0.1255 0.0450  503 GLN D N   
9898  C CA  . GLN D 503 ? 0.7440 0.6998 0.9496 -0.0969 -0.1105 0.0598  503 GLN D CA  
9899  C C   . GLN D 503 ? 0.7310 0.7049 0.9322 -0.0811 -0.0880 0.0660  503 GLN D C   
9900  O O   . GLN D 503 ? 0.7143 0.7061 0.9395 -0.0803 -0.0731 0.0780  503 GLN D O   
9901  C CB  . GLN D 503 ? 0.7500 0.6818 0.9571 -0.1049 -0.1046 0.0605  503 GLN D CB  
9902  C CG  . GLN D 503 ? 0.7548 0.6750 0.9847 -0.1259 -0.1246 0.0590  503 GLN D CG  
9903  C CD  . GLN D 503 ? 0.7211 0.6808 1.0126 -0.1369 -0.1240 0.0757  503 GLN D CD  
9904  O OE1 . GLN D 503 ? 0.7096 0.6927 1.0298 -0.1448 -0.1437 0.0771  503 GLN D OE1 
9905  N NE2 . GLN D 503 ? 0.7084 0.6761 1.0214 -0.1364 -0.1008 0.0902  503 GLN D NE2 
9906  N N   . LEU D 504 ? 0.7180 0.6841 0.8865 -0.0697 -0.0846 0.0581  504 LEU D N   
9907  C CA  . LEU D 504 ? 0.7091 0.6873 0.8713 -0.0579 -0.0667 0.0614  504 LEU D CA  
9908  C C   . LEU D 504 ? 0.6971 0.7028 0.8844 -0.0545 -0.0611 0.0709  504 LEU D C   
9909  O O   . LEU D 504 ? 0.6996 0.7155 0.8991 -0.0548 -0.0722 0.0723  504 LEU D O   
9910  C CB  . LEU D 504 ? 0.7265 0.6908 0.8557 -0.0496 -0.0647 0.0516  504 LEU D CB  
9911  C CG  . LEU D 504 ? 0.7299 0.6824 0.8430 -0.0440 -0.0540 0.0474  504 LEU D CG  
9912  C CD1 . LEU D 504 ? 0.7415 0.6888 0.8345 -0.0372 -0.0484 0.0411  504 LEU D CD1 
9913  C CD2 . LEU D 504 ? 0.7153 0.6818 0.8402 -0.0413 -0.0443 0.0553  504 LEU D CD2 
9914  N N   . SER D 505 ? 0.6554 0.6706 0.8480 -0.0497 -0.0438 0.0781  505 SER D N   
9915  C CA  . SER D 505 ? 0.6586 0.6930 0.8670 -0.0425 -0.0316 0.0858  505 SER D CA  
9916  C C   . SER D 505 ? 0.6782 0.7048 0.8569 -0.0322 -0.0195 0.0806  505 SER D C   
9917  O O   . SER D 505 ? 0.6936 0.7273 0.8764 -0.0242 -0.0102 0.0831  505 SER D O   
9918  C CB  . SER D 505 ? 0.6543 0.7022 0.8909 -0.0457 -0.0179 0.0994  505 SER D CB  
9919  O OG  . SER D 505 ? 0.6605 0.7278 0.9187 -0.0373 -0.0035 0.1079  505 SER D OG  
9920  N N   . GLN D 506 ? 0.6307 0.6429 0.7830 -0.0322 -0.0195 0.0741  506 GLN D N   
9921  C CA  . GLN D 506 ? 0.6477 0.6522 0.7747 -0.0265 -0.0138 0.0673  506 GLN D CA  
9922  C C   . GLN D 506 ? 0.6375 0.6324 0.7515 -0.0287 -0.0222 0.0587  506 GLN D C   
9923  O O   . GLN D 506 ? 0.6316 0.6230 0.7463 -0.0309 -0.0262 0.0595  506 GLN D O   
9924  C CB  . GLN D 506 ? 0.6740 0.6751 0.7854 -0.0234 -0.0032 0.0712  506 GLN D CB  
9925  C CG  . GLN D 506 ? 0.6977 0.6879 0.7812 -0.0218 -0.0049 0.0621  506 GLN D CG  
9926  C CD  . GLN D 506 ? 0.7446 0.7252 0.8014 -0.0174 0.0048  0.0640  506 GLN D CD  
9927  O OE1 . GLN D 506 ? 0.7544 0.7359 0.8114 -0.0149 0.0153  0.0743  506 GLN D OE1 
9928  N NE2 . GLN D 506 ? 0.7808 0.7485 0.8116 -0.0174 0.0021  0.0540  506 GLN D NE2 
9929  N N   . LEU D 507 ? 0.6376 0.6272 0.7419 -0.0271 -0.0219 0.0520  507 LEU D N   
9930  C CA  . LEU D 507 ? 0.6319 0.6151 0.7294 -0.0287 -0.0244 0.0455  507 LEU D CA  
9931  C C   . LEU D 507 ? 0.6419 0.6224 0.7310 -0.0293 -0.0202 0.0405  507 LEU D C   
9932  O O   . LEU D 507 ? 0.6538 0.6279 0.7365 -0.0276 -0.0154 0.0393  507 LEU D O   
9933  C CB  . LEU D 507 ? 0.6352 0.6091 0.7282 -0.0286 -0.0274 0.0432  507 LEU D CB  
9934  C CG  . LEU D 507 ? 0.6438 0.6084 0.7282 -0.0283 -0.0227 0.0379  507 LEU D CG  
9935  C CD1 . LEU D 507 ? 0.6419 0.6088 0.7345 -0.0277 -0.0225 0.0372  507 LEU D CD1 
9936  C CD2 . LEU D 507 ? 0.6690 0.6170 0.7354 -0.0265 -0.0240 0.0365  507 LEU D CD2 
9937  N N   . ASP D 508 ? 0.6522 0.6369 0.7436 -0.0319 -0.0232 0.0379  508 ASP D N   
9938  C CA  . ASP D 508 ? 0.6646 0.6474 0.7517 -0.0365 -0.0239 0.0321  508 ASP D CA  
9939  C C   . ASP D 508 ? 0.6518 0.6442 0.7577 -0.0402 -0.0265 0.0305  508 ASP D C   
9940  O O   . ASP D 508 ? 0.6517 0.6561 0.7686 -0.0393 -0.0345 0.0332  508 ASP D O   
9941  C CB  . ASP D 508 ? 0.6972 0.6783 0.7685 -0.0367 -0.0288 0.0317  508 ASP D CB  
9942  C CG  . ASP D 508 ? 0.7199 0.6928 0.7807 -0.0440 -0.0337 0.0229  508 ASP D CG  
9943  O OD1 . ASP D 508 ? 0.7039 0.6736 0.7752 -0.0497 -0.0306 0.0184  508 ASP D OD1 
9944  O OD2 . ASP D 508 ? 0.7611 0.7271 0.7998 -0.0449 -0.0407 0.0204  508 ASP D OD2 
9945  N N   . LEU D 509 ? 0.6463 0.6337 0.7579 -0.0433 -0.0183 0.0281  509 LEU D N   
9946  C CA  . LEU D 509 ? 0.6408 0.6394 0.7773 -0.0471 -0.0150 0.0280  509 LEU D CA  
9947  C C   . LEU D 509 ? 0.6430 0.6398 0.7878 -0.0586 -0.0148 0.0233  509 LEU D C   
9948  O O   . LEU D 509 ? 0.6396 0.6419 0.8071 -0.0637 -0.0058 0.0245  509 LEU D O   
9949  C CB  . LEU D 509 ? 0.6499 0.6404 0.7854 -0.0416 -0.0008 0.0305  509 LEU D CB  
9950  C CG  . LEU D 509 ? 0.6576 0.6410 0.7797 -0.0329 -0.0023 0.0324  509 LEU D CG  
9951  C CD1 . LEU D 509 ? 0.6846 0.6527 0.7958 -0.0278 0.0113  0.0323  509 LEU D CD1 
9952  C CD2 . LEU D 509 ? 0.6535 0.6513 0.7921 -0.0296 -0.0108 0.0351  509 LEU D CD2 
9953  N N   . SER D 510 ? 0.6997 0.6860 0.8257 -0.0630 -0.0230 0.0180  510 SER D N   
9954  C CA  . SER D 510 ? 0.7125 0.6864 0.8385 -0.0752 -0.0232 0.0112  510 SER D CA  
9955  C C   . SER D 510 ? 0.7012 0.6963 0.8617 -0.0879 -0.0355 0.0092  510 SER D C   
9956  O O   . SER D 510 ? 0.6878 0.7075 0.8677 -0.0847 -0.0470 0.0131  510 SER D O   
9957  C CB  . SER D 510 ? 0.7456 0.6972 0.8368 -0.0750 -0.0283 0.0042  510 SER D CB  
9958  O OG  . SER D 510 ? 0.7586 0.7192 0.8409 -0.0753 -0.0448 0.0021  510 SER D OG  
9959  N N   . SER D 511 ? 0.7204 0.7059 0.8920 -0.1026 -0.0337 0.0040  511 SER D N   
9960  C CA  . SER D 511 ? 0.7102 0.7162 0.9205 -0.1194 -0.0491 0.0011  511 SER D CA  
9961  C C   . SER D 511 ? 0.6778 0.7219 0.9408 -0.1161 -0.0442 0.0117  511 SER D C   
9962  O O   . SER D 511 ? 0.6630 0.7375 0.9589 -0.1195 -0.0635 0.0136  511 SER D O   
9963  C CB  . SER D 511 ? 0.7285 0.7347 0.9193 -0.1242 -0.0780 -0.0070 511 SER D CB  
9964  O OG  . SER D 511 ? 0.7693 0.7355 0.9080 -0.1255 -0.0779 -0.0177 511 SER D OG  
9965  N N   . ASN D 512 ? 0.6850 0.7255 0.9537 -0.1078 -0.0177 0.0191  512 ASN D N   
9966  C CA  . ASN D 512 ? 0.6666 0.7359 0.9824 -0.1032 -0.0041 0.0288  512 ASN D CA  
9967  C C   . ASN D 512 ? 0.6710 0.7302 1.0030 -0.1110 0.0232  0.0333  512 ASN D C   
9968  O O   . ASN D 512 ? 0.6853 0.7170 0.9969 -0.1220 0.0266  0.0290  512 ASN D O   
9969  C CB  . ASN D 512 ? 0.6723 0.7406 0.9691 -0.0822 0.0047  0.0338  512 ASN D CB  
9970  C CG  . ASN D 512 ? 0.6651 0.7494 0.9612 -0.0748 -0.0187 0.0339  512 ASN D CG  
9971  O OD1 . ASN D 512 ? 0.6488 0.7642 0.9878 -0.0732 -0.0281 0.0393  512 ASN D OD1 
9972  N ND2 . ASN D 512 ? 0.6778 0.7413 0.9276 -0.0693 -0.0272 0.0300  512 ASN D ND2 
9973  N N   . ARG D 513 ? 0.7424 0.8197 1.1091 -0.1043 0.0455  0.0430  513 ARG D N   
9974  C CA  . ARG D 513 ? 0.7516 0.8167 1.1297 -0.1093 0.0776  0.0503  513 ARG D CA  
9975  C C   . ARG D 513 ? 0.7817 0.8226 1.1184 -0.0892 0.1044  0.0556  513 ARG D C   
9976  O O   . ARG D 513 ? 0.7898 0.8325 1.1445 -0.0844 0.1350  0.0646  513 ARG D O   
9977  C CB  . ARG D 513 ? 0.7223 0.8281 1.1810 -0.1211 0.0861  0.0583  513 ARG D CB  
9978  C CG  . ARG D 513 ? 0.7041 0.8233 1.2001 -0.1478 0.0618  0.0526  513 ARG D CG  
9979  C CD  . ARG D 513 ? 0.6788 0.8360 1.2068 -0.1499 0.0237  0.0484  513 ARG D CD  
9980  N NE  . ARG D 513 ? 0.6453 0.8555 1.2578 -0.1501 0.0278  0.0600  513 ARG D NE  
9981  C CZ  . ARG D 513 ? 0.6175 0.8697 1.2858 -0.1612 -0.0058 0.0600  513 ARG D CZ  
9982  N NH1 . ARG D 513 ? 0.6259 0.8684 1.2647 -0.1731 -0.0465 0.0475  513 ARG D NH1 
9983  N NH2 . ARG D 513 ? 0.5835 0.8878 1.3381 -0.1592 0.0016  0.0735  513 ARG D NH2 
9984  N N   . ILE D 514 ? 0.6703 0.6865 0.9497 -0.0775 0.0931  0.0499  514 ILE D N   
9985  C CA  . ILE D 514 ? 0.7073 0.6964 0.9402 -0.0604 0.1105  0.0524  514 ILE D CA  
9986  C C   . ILE D 514 ? 0.7342 0.6873 0.9315 -0.0624 0.1316  0.0576  514 ILE D C   
9987  O O   . ILE D 514 ? 0.7303 0.6682 0.9157 -0.0722 0.1240  0.0563  514 ILE D O   
9988  C CB  . ILE D 514 ? 0.7159 0.6942 0.9083 -0.0509 0.0879  0.0456  514 ILE D CB  
9989  C CG1 . ILE D 514 ? 0.6961 0.7042 0.9187 -0.0468 0.0713  0.0435  514 ILE D CG1 
9990  C CG2 . ILE D 514 ? 0.7597 0.7052 0.8992 -0.0372 0.0993  0.0463  514 ILE D CG2 
9991  C CD1 . ILE D 514 ? 0.6858 0.6914 0.8851 -0.0459 0.0454  0.0380  514 ILE D CD1 
9992  N N   . THR D 515 ? 0.7342 0.6688 0.9099 -0.0514 0.1598  0.0641  515 THR D N   
9993  C CA  . THR D 515 ? 0.7661 0.6628 0.9024 -0.0505 0.1843  0.0723  515 THR D CA  
9994  C C   . THR D 515 ? 0.8165 0.6751 0.8783 -0.0335 0.1835  0.0708  515 THR D C   
9995  O O   . THR D 515 ? 0.8232 0.6857 0.8697 -0.0256 0.1629  0.0625  515 THR D O   
9996  C CB  . THR D 515 ? 0.7645 0.6688 0.9375 -0.0537 0.2225  0.0833  515 THR D CB  
9997  O OG1 . THR D 515 ? 0.7798 0.6925 0.9566 -0.0381 0.2387  0.0833  515 THR D OG1 
9998  C CG2 . THR D 515 ? 0.7135 0.6587 0.9673 -0.0742 0.2175  0.0848  515 THR D CG2 
9999  N N   . GLY D 516 ? 0.8244 0.6436 0.8384 -0.0289 0.2048  0.0796  516 GLY D N   
10000 C CA  . GLY D 516 ? 0.8754 0.6546 0.8127 -0.0147 0.1977  0.0786  516 GLY D CA  
10001 C C   . GLY D 516 ? 0.8721 0.6382 0.7833 -0.0162 0.1700  0.0789  516 GLY D C   
10002 O O   . GLY D 516 ? 0.8369 0.6167 0.7815 -0.0269 0.1619  0.0798  516 GLY D O   
10003 N N   . GLU D 517 ? 0.9557 0.6931 0.8059 -0.0047 0.1549  0.0780  517 GLU D N   
10004 C CA  . GLU D 517 ? 0.9556 0.6820 0.7835 -0.0025 0.1293  0.0813  517 GLU D CA  
10005 C C   . GLU D 517 ? 0.9617 0.6962 0.7754 0.0029  0.0957  0.0724  517 GLU D C   
10006 O O   . GLU D 517 ? 0.9904 0.7174 0.7815 0.0072  0.0933  0.0650  517 GLU D O   
10007 C CB  . GLU D 517 ? 1.0004 0.6802 0.7680 0.0057  0.1417  0.0953  517 GLU D CB  
10008 C CG  . GLU D 517 ? 1.0582 0.7010 0.7629 0.0159  0.1599  0.0976  517 GLU D CG  
10009 C CD  . GLU D 517 ? 1.1022 0.6956 0.7391 0.0252  0.1675  0.1134  517 GLU D CD  
10010 O OE1 . GLU D 517 ? 1.1226 0.7001 0.7175 0.0336  0.1360  0.1151  517 GLU D OE1 
10011 O OE2 . GLU D 517 ? 1.1156 0.6867 0.7434 0.0240  0.2042  0.1258  517 GLU D OE2 
10012 N N   . LEU D 518 ? 0.9066 0.6546 0.7359 0.0022  0.0715  0.0733  518 LEU D N   
10013 C CA  . LEU D 518 ? 0.9031 0.6661 0.7340 0.0046  0.0403  0.0669  518 LEU D CA  
10014 C C   . LEU D 518 ? 0.9555 0.6871 0.7267 0.0138  0.0235  0.0707  518 LEU D C   
10015 O O   . LEU D 518 ? 0.9758 0.6837 0.7156 0.0209  0.0226  0.0824  518 LEU D O   
10016 C CB  . LEU D 518 ? 0.8628 0.6506 0.7321 0.0029  0.0249  0.0688  518 LEU D CB  
10017 C CG  . LEU D 518 ? 0.8166 0.6315 0.7358 -0.0067 0.0344  0.0630  518 LEU D CG  
10018 C CD1 . LEU D 518 ? 0.7931 0.6220 0.7354 -0.0052 0.0222  0.0645  518 LEU D CD1 
10019 C CD2 . LEU D 518 ? 0.7994 0.6369 0.7408 -0.0118 0.0319  0.0533  518 LEU D CD2 
10020 N N   . PRO D 519 ? 0.9438 0.6713 0.6959 0.0136  0.0077  0.0612  519 PRO D N   
10021 C CA  . PRO D 519 ? 0.9958 0.6907 0.6865 0.0200  -0.0145 0.0625  519 PRO D CA  
10022 C C   . PRO D 519 ? 0.9743 0.6891 0.6841 0.0211  -0.0507 0.0684  519 PRO D C   
10023 O O   . PRO D 519 ? 0.9240 0.6773 0.6936 0.0172  -0.0566 0.0694  519 PRO D O   
10024 C CB  . PRO D 519 ? 1.0275 0.7116 0.7001 0.0164  -0.0188 0.0472  519 PRO D CB  
10025 C CG  . PRO D 519 ? 0.9763 0.7031 0.7185 0.0081  -0.0164 0.0410  519 PRO D CG  
10026 C CD  . PRO D 519 ? 0.9275 0.6761 0.7109 0.0071  0.0077  0.0488  519 PRO D CD  
10027 N N   . GLU D 520 ? 1.0708 0.7578 0.7271 0.0274  -0.0751 0.0732  520 GLU D N   
10028 C CA  . GLU D 520 ? 1.0506 0.7609 0.7305 0.0277  -0.1152 0.0781  520 GLU D CA  
10029 C C   . GLU D 520 ? 1.0352 0.7673 0.7443 0.0153  -0.1377 0.0646  520 GLU D C   
10030 O O   . GLU D 520 ? 1.0018 0.7657 0.7532 0.0121  -0.1670 0.0688  520 GLU D O   
10031 C CB  . GLU D 520 ? 1.0952 0.7702 0.7094 0.0375  -0.1410 0.0880  520 GLU D CB  
10032 C CG  . GLU D 520 ? 1.1126 0.7620 0.6961 0.0511  -0.1209 0.1055  520 GLU D CG  
10033 C CD  . GLU D 520 ? 1.0706 0.7527 0.7121 0.0586  -0.1275 0.1205  520 GLU D CD  
10034 O OE1 . GLU D 520 ? 1.0308 0.7560 0.7312 0.0553  -0.1517 0.1193  520 GLU D OE1 
10035 O OE2 . GLU D 520 ? 1.0794 0.7413 0.7074 0.0684  -0.1061 0.1341  520 GLU D OE2 
10036 N N   . SER D 521 ? 0.9969 0.7125 0.6882 0.0088  -0.1227 0.0499  521 SER D N   
10037 C CA  . SER D 521 ? 0.9834 0.7142 0.7032 -0.0035 -0.1390 0.0374  521 SER D CA  
10038 C C   . SER D 521 ? 0.9221 0.7029 0.7228 -0.0093 -0.1306 0.0397  521 SER D C   
10039 O O   . SER D 521 ? 0.9009 0.6979 0.7329 -0.0197 -0.1442 0.0331  521 SER D O   
10040 C CB  . SER D 521 ? 1.0307 0.7237 0.7059 -0.0049 -0.1201 0.0223  521 SER D CB  
10041 O OG  . SER D 521 ? 1.0176 0.7161 0.7141 -0.0165 -0.1359 0.0103  521 SER D OG  
10042 N N   . ILE D 522 ? 0.9172 0.7171 0.7469 -0.0034 -0.1074 0.0483  522 ILE D N   
10043 C CA  . ILE D 522 ? 0.8598 0.6999 0.7536 -0.0071 -0.0976 0.0503  522 ILE D CA  
10044 C C   . ILE D 522 ? 0.8240 0.6951 0.7602 -0.0106 -0.1238 0.0561  522 ILE D C   
10045 O O   . ILE D 522 ? 0.7824 0.6835 0.7670 -0.0157 -0.1197 0.0564  522 ILE D O   
10046 C CB  . ILE D 522 ? 0.8354 0.6809 0.7413 -0.0004 -0.0737 0.0578  522 ILE D CB  
10047 C CG1 . ILE D 522 ? 0.7845 0.6600 0.7393 -0.0053 -0.0602 0.0552  522 ILE D CG1 
10048 C CG2 . ILE D 522 ? 0.8324 0.6795 0.7388 0.0091  -0.0853 0.0709  522 ILE D CG2 
10049 C CD1 . ILE D 522 ? 0.7655 0.6407 0.7287 -0.0022 -0.0389 0.0587  522 ILE D CD1 
10050 N N   . SER D 523 ? 0.8540 0.7179 0.7721 -0.0075 -0.1511 0.0620  523 SER D N   
10051 C CA  . SER D 523 ? 0.8167 0.7146 0.7830 -0.0106 -0.1786 0.0699  523 SER D CA  
10052 C C   . SER D 523 ? 0.7979 0.7084 0.7917 -0.0269 -0.1927 0.0613  523 SER D C   
10053 O O   . SER D 523 ? 0.7550 0.7021 0.8060 -0.0321 -0.2079 0.0689  523 SER D O   
10054 C CB  . SER D 523 ? 0.8420 0.7274 0.7791 -0.0044 -0.2105 0.0781  523 SER D CB  
10055 O OG  . SER D 523 ? 0.8002 0.7275 0.7984 -0.0051 -0.2355 0.0894  523 SER D OG  
10056 N N   . ASN D 524 ? 0.8559 0.7363 0.8138 -0.0344 -0.1854 0.0469  524 ASN D N   
10057 C CA  . ASN D 524 ? 0.8423 0.7236 0.8179 -0.0503 -0.2004 0.0382  524 ASN D CA  
10058 C C   . ASN D 524 ? 0.7863 0.7035 0.8252 -0.0556 -0.1839 0.0430  524 ASN D C   
10059 O O   . ASN D 524 ? 0.7591 0.6892 0.8330 -0.0694 -0.1986 0.0426  524 ASN D O   
10060 C CB  . ASN D 524 ? 0.8931 0.7259 0.8093 -0.0530 -0.1925 0.0218  524 ASN D CB  
10061 C CG  . ASN D 524 ? 0.9456 0.7368 0.7974 -0.0549 -0.2199 0.0137  524 ASN D CG  
10062 O OD1 . ASN D 524 ? 0.9403 0.7423 0.7964 -0.0567 -0.2519 0.0208  524 ASN D OD1 
10063 N ND2 . ASN D 524 ? 0.9974 0.7391 0.7865 -0.0530 -0.2075 -0.0006 524 ASN D ND2 
10064 N N   . ILE D 525 ? 0.7913 0.7211 0.8422 -0.0461 -0.1540 0.0472  525 ILE D N   
10065 C CA  . ILE D 525 ? 0.7423 0.7009 0.8419 -0.0493 -0.1379 0.0523  525 ILE D CA  
10066 C C   . ILE D 525 ? 0.7085 0.7037 0.8547 -0.0440 -0.1400 0.0665  525 ILE D C   
10067 O O   . ILE D 525 ? 0.7022 0.7063 0.8530 -0.0324 -0.1213 0.0719  525 ILE D O   
10068 C CB  . ILE D 525 ? 0.7426 0.6937 0.8283 -0.0429 -0.1091 0.0485  525 ILE D CB  
10069 C CG1 . ILE D 525 ? 0.7714 0.7141 0.8322 -0.0314 -0.0971 0.0497  525 ILE D CG1 
10070 C CG2 . ILE D 525 ? 0.7609 0.6833 0.8173 -0.0470 -0.1054 0.0373  525 ILE D CG2 
10071 C CD1 . ILE D 525 ? 0.7559 0.6989 0.8154 -0.0279 -0.0729 0.0472  525 ILE D CD1 
10072 N N   . ASN D 526 ? 0.7443 0.7610 0.9298 -0.0529 -0.1623 0.0728  526 ASN D N   
10073 C CA  . ASN D 526 ? 0.7133 0.7688 0.9515 -0.0455 -0.1629 0.0884  526 ASN D CA  
10074 C C   . ASN D 526 ? 0.6781 0.7608 0.9634 -0.0459 -0.1375 0.0965  526 ASN D C   
10075 O O   . ASN D 526 ? 0.6611 0.7706 0.9828 -0.0345 -0.1251 0.1087  526 ASN D O   
10076 C CB  . ASN D 526 ? 0.7048 0.7784 0.9736 -0.0536 -0.2000 0.0945  526 ASN D CB  
10077 C CG  . ASN D 526 ? 0.6925 0.7673 0.9838 -0.0758 -0.2167 0.0896  526 ASN D CG  
10078 O OD1 . ASN D 526 ? 0.6893 0.7508 0.9739 -0.0832 -0.1981 0.0832  526 ASN D OD1 
10079 N ND2 . ASN D 526 ? 0.6861 0.7758 1.0057 -0.0872 -0.2538 0.0931  526 ASN D ND2 
10080 N N   . ARG D 527 ? 0.7181 0.7907 0.9994 -0.0568 -0.1275 0.0909  527 ARG D N   
10081 C CA  . ARG D 527 ? 0.6955 0.7862 1.0089 -0.0568 -0.1020 0.0994  527 ARG D CA  
10082 C C   . ARG D 527 ? 0.7091 0.7896 0.9929 -0.0426 -0.0739 0.0973  527 ARG D C   
10083 O O   . ARG D 527 ? 0.7037 0.7935 1.0018 -0.0402 -0.0516 0.1039  527 ARG D O   
10084 C CB  . ARG D 527 ? 0.6897 0.7674 1.0043 -0.0729 -0.1034 0.0959  527 ARG D CB  
10085 C CG  . ARG D 527 ? 0.6733 0.7654 1.0329 -0.0911 -0.1268 0.1006  527 ARG D CG  
10086 C CD  . ARG D 527 ? 0.6655 0.7483 1.0392 -0.1054 -0.1172 0.1031  527 ARG D CD  
10087 N NE  . ARG D 527 ? 0.6436 0.7495 1.0787 -0.1243 -0.1329 0.1124  527 ARG D NE  
10088 C CZ  . ARG D 527 ? 0.6155 0.7576 1.1123 -0.1266 -0.1150 0.1307  527 ARG D CZ  
10089 N NH1 . ARG D 527 ? 0.6132 0.7669 1.1092 -0.1099 -0.0803 0.1405  527 ARG D NH1 
10090 N NH2 . ARG D 527 ? 0.5931 0.7586 1.1533 -0.1468 -0.1319 0.1394  527 ARG D NH2 
10091 N N   . ILE D 528 ? 0.6708 0.7303 0.9124 -0.0343 -0.0745 0.0884  528 ILE D N   
10092 C CA  . ILE D 528 ? 0.6865 0.7329 0.8993 -0.0251 -0.0528 0.0839  528 ILE D CA  
10093 C C   . ILE D 528 ? 0.6888 0.7508 0.9228 -0.0132 -0.0344 0.0929  528 ILE D C   
10094 O O   . ILE D 528 ? 0.6799 0.7594 0.9434 -0.0062 -0.0393 0.1018  528 ILE D O   
10095 C CB  . ILE D 528 ? 0.7112 0.7335 0.8834 -0.0211 -0.0578 0.0747  528 ILE D CB  
10096 C CG1 . ILE D 528 ? 0.7239 0.7317 0.8698 -0.0168 -0.0399 0.0681  528 ILE D CG1 
10097 C CG2 . ILE D 528 ? 0.7190 0.7440 0.8947 -0.0124 -0.0672 0.0804  528 ILE D CG2 
10098 C CD1 . ILE D 528 ? 0.7100 0.7159 0.8510 -0.0228 -0.0337 0.0644  528 ILE D CD1 
10099 N N   . SER D 529 ? 0.6399 0.6938 0.8574 -0.0094 -0.0133 0.0908  529 SER D N   
10100 C CA  . SER D 529 ? 0.6590 0.7161 0.8820 0.0039  0.0084  0.0960  529 SER D CA  
10101 C C   . SER D 529 ? 0.6943 0.7229 0.8712 0.0087  0.0197  0.0846  529 SER D C   
10102 O O   . SER D 529 ? 0.7145 0.7335 0.8842 0.0206  0.0341  0.0845  529 SER D O   
10103 C CB  . SER D 529 ? 0.6578 0.7315 0.9072 0.0042  0.0265  0.1069  529 SER D CB  
10104 O OG  . SER D 529 ? 0.6670 0.7284 0.8922 -0.0045 0.0293  0.1035  529 SER D OG  
10105 N N   . LYS D 530 ? 0.7040 0.7185 0.8525 -0.0005 0.0128  0.0751  530 LYS D N   
10106 C CA  . LYS D 530 ? 0.7211 0.7120 0.8333 -0.0003 0.0164  0.0637  530 LYS D CA  
10107 C C   . LYS D 530 ? 0.7002 0.6845 0.8036 -0.0079 0.0020  0.0569  530 LYS D C   
10108 O O   . LYS D 530 ? 0.6805 0.6695 0.7859 -0.0151 -0.0069 0.0558  530 LYS D O   
10109 C CB  . LYS D 530 ? 0.7427 0.7252 0.8314 -0.0032 0.0226  0.0603  530 LYS D CB  
10110 C CG  . LYS D 530 ? 0.7820 0.7589 0.8613 0.0061  0.0430  0.0646  530 LYS D CG  
10111 C CD  . LYS D 530 ? 0.8263 0.7826 0.8626 0.0039  0.0454  0.0576  530 LYS D CD  
10112 C CE  . LYS D 530 ? 0.8686 0.8147 0.8865 0.0142  0.0693  0.0635  530 LYS D CE  
10113 N NZ  . LYS D 530 ? 0.9026 0.8342 0.8809 0.0113  0.0680  0.0633  530 LYS D NZ  
10114 N N   . LEU D 531 ? 0.6654 0.6350 0.7571 -0.0052 0.0032  0.0529  531 LEU D N   
10115 C CA  . LEU D 531 ? 0.6533 0.6143 0.7356 -0.0109 -0.0044 0.0485  531 LEU D CA  
10116 C C   . LEU D 531 ? 0.6668 0.6092 0.7314 -0.0147 0.0025  0.0402  531 LEU D C   
10117 O O   . LEU D 531 ? 0.6870 0.6127 0.7431 -0.0097 0.0102  0.0399  531 LEU D O   
10118 C CB  . LEU D 531 ? 0.6566 0.6148 0.7413 -0.0055 -0.0106 0.0546  531 LEU D CB  
10119 C CG  . LEU D 531 ? 0.6555 0.6073 0.7286 -0.0104 -0.0198 0.0529  531 LEU D CG  
10120 C CD1 . LEU D 531 ? 0.6700 0.6210 0.7423 -0.0049 -0.0324 0.0602  531 LEU D CD1 
10121 C CD2 . LEU D 531 ? 0.6628 0.5959 0.7175 -0.0132 -0.0106 0.0482  531 LEU D CD2 
10122 N N   . GLN D 532 ? 0.6501 0.5953 0.7127 -0.0236 -0.0011 0.0342  532 GLN D N   
10123 C CA  . GLN D 532 ? 0.6631 0.5953 0.7168 -0.0312 0.0010  0.0260  532 GLN D CA  
10124 C C   . GLN D 532 ? 0.6414 0.5780 0.7061 -0.0387 -0.0006 0.0251  532 GLN D C   
10125 O O   . GLN D 532 ? 0.6252 0.5774 0.7021 -0.0426 -0.0068 0.0244  532 GLN D O   
10126 C CB  . GLN D 532 ? 0.6835 0.6177 0.7280 -0.0348 -0.0038 0.0207  532 GLN D CB  
10127 C CG  . GLN D 532 ? 0.7208 0.6481 0.7505 -0.0258 0.0038  0.0225  532 GLN D CG  
10128 C CD  . GLN D 532 ? 0.7510 0.6805 0.7651 -0.0274 -0.0012 0.0209  532 GLN D CD  
10129 O OE1 . GLN D 532 ? 0.7479 0.6903 0.7677 -0.0227 0.0003  0.0293  532 GLN D OE1 
10130 N NE2 . GLN D 532 ? 0.7819 0.6966 0.7746 -0.0351 -0.0087 0.0108  532 GLN D NE2 
10131 N N   . LEU D 533 ? 0.6642 0.5856 0.7248 -0.0392 0.0074  0.0267  533 LEU D N   
10132 C CA  . LEU D 533 ? 0.6579 0.5798 0.7283 -0.0458 0.0131  0.0272  533 LEU D CA  
10133 C C   . LEU D 533 ? 0.6683 0.5761 0.7433 -0.0570 0.0196  0.0232  533 LEU D C   
10134 O O   . LEU D 533 ? 0.6675 0.5732 0.7538 -0.0629 0.0296  0.0260  533 LEU D O   
10135 C CB  . LEU D 533 ? 0.6702 0.5814 0.7269 -0.0381 0.0194  0.0344  533 LEU D CB  
10136 C CG  . LEU D 533 ? 0.6670 0.5873 0.7185 -0.0304 0.0099  0.0370  533 LEU D CG  
10137 C CD1 . LEU D 533 ? 0.6959 0.5996 0.7249 -0.0247 0.0126  0.0417  533 LEU D CD1 
10138 C CD2 . LEU D 533 ? 0.6473 0.5865 0.7153 -0.0333 0.0050  0.0337  533 LEU D CD2 
10139 N N   . ASN D 534 ? 0.7270 0.6224 0.7927 -0.0605 0.0157  0.0163  534 ASN D N   
10140 C CA  . ASN D 534 ? 0.7447 0.6180 0.8103 -0.0729 0.0201  0.0105  534 ASN D CA  
10141 C C   . ASN D 534 ? 0.7287 0.6208 0.8250 -0.0900 0.0131  0.0062  534 ASN D C   
10142 O O   . ASN D 534 ? 0.7084 0.6295 0.8218 -0.0902 0.0019  0.0063  534 ASN D O   
10143 C CB  . ASN D 534 ? 0.7775 0.6277 0.8185 -0.0716 0.0168  0.0015  534 ASN D CB  
10144 C CG  . ASN D 534 ? 0.7814 0.6475 0.8173 -0.0729 0.0020  -0.0053 534 ASN D CG  
10145 O OD1 . ASN D 534 ? 0.7699 0.6559 0.8063 -0.0623 -0.0007 0.0004  534 ASN D OD1 
10146 N ND2 . ASN D 534 ? 0.8008 0.6554 0.8295 -0.0868 -0.0089 -0.0171 534 ASN D ND2 
10147 N N   . GLY D 535 ? 0.7529 0.6284 0.8602 -0.1046 0.0195  0.0039  535 GLY D N   
10148 C CA  . GLY D 535 ? 0.7375 0.6338 0.8843 -0.1237 0.0113  0.0006  535 GLY D CA  
10149 C C   . GLY D 535 ? 0.7074 0.6362 0.8907 -0.1212 0.0208  0.0113  535 GLY D C   
10150 O O   . GLY D 535 ? 0.6854 0.6484 0.8993 -0.1234 0.0084  0.0113  535 GLY D O   
10151 N N   . ASN D 536 ? 0.7218 0.6364 0.8983 -0.1148 0.0441  0.0211  536 ASN D N   
10152 C CA  . ASN D 536 ? 0.7100 0.6442 0.9072 -0.1083 0.0600  0.0311  536 ASN D CA  
10153 C C   . ASN D 536 ? 0.7249 0.6365 0.9235 -0.1138 0.0870  0.0403  536 ASN D C   
10154 O O   . ASN D 536 ? 0.7365 0.6233 0.9329 -0.1264 0.0903  0.0387  536 ASN D O   
10155 C CB  . ASN D 536 ? 0.7151 0.6493 0.8807 -0.0878 0.0589  0.0337  536 ASN D CB  
10156 C CG  . ASN D 536 ? 0.6948 0.6609 0.8796 -0.0835 0.0430  0.0307  536 ASN D CG  
10157 O OD1 . ASN D 536 ? 0.6837 0.6737 0.9026 -0.0831 0.0491  0.0346  536 ASN D OD1 
10158 N ND2 . ASN D 536 ? 0.6924 0.6580 0.8570 -0.0790 0.0247  0.0251  536 ASN D ND2 
10159 N N   . ARG D 537 ? 0.7877 0.7028 0.9863 -0.1039 0.1085  0.0502  537 ARG D N   
10160 C CA  . ARG D 537 ? 0.8080 0.6980 0.9994 -0.1060 0.1391  0.0619  537 ARG D CA  
10161 C C   . ARG D 537 ? 0.8427 0.7020 0.9736 -0.0856 0.1507  0.0689  537 ARG D C   
10162 O O   . ARG D 537 ? 0.8652 0.7081 0.9824 -0.0808 0.1786  0.0797  537 ARG D O   
10163 C CB  . ARG D 537 ? 0.7913 0.7104 1.0393 -0.1143 0.1602  0.0693  537 ARG D CB  
10164 C CG  . ARG D 537 ? 0.7529 0.7146 1.0674 -0.1319 0.1399  0.0625  537 ARG D CG  
10165 C CD  . ARG D 537 ? 0.7385 0.7142 1.1145 -0.1524 0.1601  0.0711  537 ARG D CD  
10166 N NE  . ARG D 537 ? 0.7326 0.7282 1.1379 -0.1426 0.1928  0.0841  537 ARG D NE  
10167 C CZ  . ARG D 537 ? 0.7391 0.7254 1.1654 -0.1493 0.2305  0.0981  537 ARG D CZ  
10168 N NH1 . ARG D 537 ? 0.7504 0.7081 1.1756 -0.1680 0.2390  0.1017  537 ARG D NH1 
10169 N NH2 . ARG D 537 ? 0.7371 0.7397 1.1846 -0.1363 0.2634  0.1094  537 ARG D NH2 
10170 N N   . LEU D 538 ? 0.7969 0.6473 0.8906 -0.0738 0.1294  0.0634  538 LEU D N   
10171 C CA  . LEU D 538 ? 0.8314 0.6539 0.8692 -0.0566 0.1322  0.0694  538 LEU D CA  
10172 C C   . LEU D 538 ? 0.8586 0.6399 0.8638 -0.0555 0.1468  0.0804  538 LEU D C   
10173 O O   . LEU D 538 ? 0.8516 0.6210 0.8650 -0.0632 0.1427  0.0796  538 LEU D O   
10174 C CB  . LEU D 538 ? 0.8264 0.6558 0.8462 -0.0470 0.1041  0.0623  538 LEU D CB  
10175 C CG  . LEU D 538 ? 0.7988 0.6642 0.8482 -0.0484 0.0881  0.0527  538 LEU D CG  
10176 C CD1 . LEU D 538 ? 0.7833 0.6561 0.8307 -0.0466 0.0651  0.0466  538 LEU D CD1 
10177 C CD2 . LEU D 538 ? 0.8185 0.6849 0.8505 -0.0377 0.0908  0.0527  538 LEU D CD2 
10178 N N   . SER D 539 ? 0.8902 0.6440 0.8520 -0.0444 0.1639  0.0909  539 SER D N   
10179 C CA  . SER D 539 ? 0.9214 0.6316 0.8470 -0.0418 0.1821  0.1053  539 SER D CA  
10180 C C   . SER D 539 ? 0.9621 0.6428 0.8210 -0.0221 0.1701  0.1119  539 SER D C   
10181 O O   . SER D 539 ? 0.9608 0.6576 0.8102 -0.0140 0.1446  0.1035  539 SER D O   
10182 C CB  . SER D 539 ? 0.9325 0.6323 0.8679 -0.0491 0.2204  0.1159  539 SER D CB  
10183 O OG  . SER D 539 ? 0.9530 0.6563 0.8683 -0.0387 0.2334  0.1160  539 SER D OG  
10184 N N   . GLY D 540 ? 1.0082 0.6449 0.8217 -0.0154 0.1860  0.1278  540 GLY D N   
10185 C CA  . GLY D 540 ? 1.0503 0.6567 0.7979 0.0033  0.1702  0.1361  540 GLY D CA  
10186 C C   . GLY D 540 ? 1.0371 0.6488 0.7918 0.0103  0.1400  0.1358  540 GLY D C   
10187 O O   . GLY D 540 ? 1.0027 0.6309 0.8029 0.0015  0.1368  0.1296  540 GLY D O   
10188 N N   . LYS D 541 ? 1.0546 0.6508 0.7627 0.0268  0.1174  0.1426  541 LYS D N   
10189 C CA  . LYS D 541 ? 1.0444 0.6479 0.7638 0.0369  0.0907  0.1460  541 LYS D CA  
10190 C C   . LYS D 541 ? 1.0126 0.6628 0.7697 0.0350  0.0631  0.1307  541 LYS D C   
10191 O O   . LYS D 541 ? 1.0115 0.6795 0.7680 0.0299  0.0576  0.1199  541 LYS D O   
10192 C CB  . LYS D 541 ? 1.0902 0.6589 0.7502 0.0561  0.0755  0.1639  541 LYS D CB  
10193 C CG  . LYS D 541 ? 1.1168 0.6898 0.7376 0.0630  0.0484  0.1601  541 LYS D CG  
10194 C CD  . LYS D 541 ? 1.1591 0.7010 0.7248 0.0820  0.0251  0.1786  541 LYS D CD  
10195 C CE  . LYS D 541 ? 1.2026 0.7276 0.7044 0.0862  0.0047  0.1754  541 LYS D CE  
10196 N NZ  . LYS D 541 ? 1.2469 0.7255 0.6839 0.0850  0.0385  0.1786  541 LYS D NZ  
10197 N N   . ILE D 542 ? 0.9612 0.6278 0.7508 0.0401  0.0490  0.1309  542 ILE D N   
10198 C CA  . ILE D 542 ? 0.9322 0.6414 0.7596 0.0398  0.0260  0.1203  542 ILE D CA  
10199 C C   . ILE D 542 ? 0.9552 0.6684 0.7584 0.0512  -0.0039 0.1267  542 ILE D C   
10200 O O   . ILE D 542 ? 0.9770 0.6729 0.7602 0.0661  -0.0156 0.1421  542 ILE D O   
10201 C CB  . ILE D 542 ? 0.9068 0.6275 0.7733 0.0434  0.0266  0.1196  542 ILE D CB  
10202 C CG1 . ILE D 542 ? 0.8864 0.6016 0.7734 0.0283  0.0501  0.1094  542 ILE D CG1 
10203 C CG2 . ILE D 542 ? 0.8833 0.6456 0.7856 0.0456  0.0061  0.1130  542 ILE D CG2 
10204 C CD1 . ILE D 542 ? 0.8652 0.5913 0.7844 0.0293  0.0502  0.1022  542 ILE D CD1 
10205 N N   . PRO D 543 ? 0.9358 0.6693 0.7401 0.0446  -0.0189 0.1160  543 PRO D N   
10206 C CA  . PRO D 543 ? 0.9608 0.6927 0.7375 0.0517  -0.0508 0.1202  543 PRO D CA  
10207 C C   . PRO D 543 ? 0.9385 0.7001 0.7559 0.0610  -0.0764 0.1284  543 PRO D C   
10208 O O   . PRO D 543 ? 0.8996 0.6934 0.7714 0.0583  -0.0718 0.1241  543 PRO D O   
10209 C CB  . PRO D 543 ? 0.9578 0.7038 0.7364 0.0394  -0.0567 0.1037  543 PRO D CB  
10210 C CG  . PRO D 543 ? 0.9144 0.6884 0.7447 0.0293  -0.0375 0.0938  543 PRO D CG  
10211 C CD  . PRO D 543 ? 0.9095 0.6670 0.7419 0.0304  -0.0101 0.0997  543 PRO D CD  
10212 N N   . SER D 544 ? 0.9717 0.7221 0.7616 0.0729  -0.1035 0.1415  544 SER D N   
10213 C CA  . SER D 544 ? 0.9478 0.7327 0.7854 0.0829  -0.1299 0.1517  544 SER D CA  
10214 C C   . SER D 544 ? 0.9149 0.7417 0.7945 0.0710  -0.1536 0.1414  544 SER D C   
10215 O O   . SER D 544 ? 0.8827 0.7475 0.8180 0.0767  -0.1707 0.1494  544 SER D O   
10216 C CB  . SER D 544 ? 0.9839 0.7475 0.7839 0.0996  -0.1568 0.1709  544 SER D CB  
10217 O OG  . SER D 544 ? 1.0115 0.7631 0.7653 0.0933  -0.1871 0.1660  544 SER D OG  
10218 N N   . GLY D 545 ? 0.9341 0.7539 0.7915 0.0553  -0.1526 0.1249  545 GLY D N   
10219 C CA  . GLY D 545 ? 0.9043 0.7579 0.8013 0.0421  -0.1714 0.1149  545 GLY D CA  
10220 C C   . GLY D 545 ? 0.8518 0.7448 0.8173 0.0382  -0.1535 0.1122  545 GLY D C   
10221 O O   . GLY D 545 ? 0.8208 0.7461 0.8294 0.0291  -0.1679 0.1089  545 GLY D O   
10222 N N   . ILE D 546 ? 0.8375 0.7245 0.8099 0.0439  -0.1220 0.1132  546 ILE D N   
10223 C CA  . ILE D 546 ? 0.7961 0.7131 0.8221 0.0430  -0.1051 0.1114  546 ILE D CA  
10224 C C   . ILE D 546 ? 0.7706 0.7208 0.8483 0.0548  -0.1186 0.1254  546 ILE D C   
10225 O O   . ILE D 546 ? 0.7359 0.7171 0.8620 0.0531  -0.1097 0.1249  546 ILE D O   
10226 C CB  . ILE D 546 ? 0.8022 0.6970 0.8150 0.0458  -0.0728 0.1081  546 ILE D CB  
10227 C CG1 . ILE D 546 ? 0.8207 0.6904 0.7947 0.0341  -0.0598 0.0968  546 ILE D CG1 
10228 C CG2 . ILE D 546 ? 0.7700 0.6866 0.8230 0.0446  -0.0555 0.1035  546 ILE D CG2 
10229 C CD1 . ILE D 546 ? 0.8141 0.6718 0.7893 0.0300  -0.0319 0.0907  546 ILE D CD1 
10230 N N   . ARG D 547 ? 0.8312 0.7763 0.9005 0.0678  -0.1398 0.1398  547 ARG D N   
10231 C CA  . ARG D 547 ? 0.8041 0.7864 0.9317 0.0811  -0.1547 0.1559  547 ARG D CA  
10232 C C   . ARG D 547 ? 0.7647 0.7918 0.9467 0.0678  -0.1733 0.1539  547 ARG D C   
10233 O O   . ARG D 547 ? 0.7289 0.7960 0.9772 0.0755  -0.1707 0.1648  547 ARG D O   
10234 C CB  . ARG D 547 ? 0.8326 0.8026 0.9384 0.0959  -0.1832 0.1724  547 ARG D CB  
10235 C CG  . ARG D 547 ? 0.8490 0.8153 0.9247 0.0837  -0.2236 0.1691  547 ARG D CG  
10236 C CD  . ARG D 547 ? 0.8811 0.8336 0.9294 0.0996  -0.2560 0.1869  547 ARG D CD  
10237 N NE  . ARG D 547 ? 0.8826 0.8515 0.9329 0.0885  -0.3047 0.1865  547 ARG D NE  
10238 C CZ  . ARG D 547 ? 0.9233 0.8548 0.9014 0.0756  -0.3241 0.1741  547 ARG D CZ  
10239 N NH1 . ARG D 547 ? 0.9636 0.8432 0.8662 0.0739  -0.2965 0.1634  547 ARG D NH1 
10240 N NH2 . ARG D 547 ? 0.9247 0.8700 0.9076 0.0639  -0.3715 0.1721  547 ARG D NH2 
10241 N N   . LEU D 548 ? 0.7005 0.7197 0.8573 0.0484  -0.1895 0.1409  548 LEU D N   
10242 C CA  . LEU D 548 ? 0.6685 0.7230 0.8728 0.0328  -0.2111 0.1392  548 LEU D CA  
10243 C C   . LEU D 548 ? 0.6401 0.7089 0.8725 0.0211  -0.1839 0.1298  548 LEU D C   
10244 O O   . LEU D 548 ? 0.6125 0.7085 0.8874 0.0069  -0.1963 0.1296  548 LEU D O   
10245 C CB  . LEU D 548 ? 0.7071 0.7376 0.8643 0.0179  -0.2454 0.1293  548 LEU D CB  
10246 C CG  . LEU D 548 ? 0.7642 0.7768 0.8833 0.0279  -0.2794 0.1387  548 LEU D CG  
10247 C CD1 . LEU D 548 ? 0.8108 0.7967 0.8802 0.0111  -0.3144 0.1260  548 LEU D CD1 
10248 C CD2 . LEU D 548 ? 0.7636 0.8227 0.9530 0.0404  -0.3011 0.1600  548 LEU D CD2 
10249 N N   . LEU D 549 ? 0.7005 0.7502 0.9099 0.0258  -0.1489 0.1231  549 LEU D N   
10250 C CA  . LEU D 549 ? 0.6791 0.7397 0.9089 0.0173  -0.1244 0.1161  549 LEU D CA  
10251 C C   . LEU D 549 ? 0.6524 0.7441 0.9370 0.0297  -0.1049 0.1283  549 LEU D C   
10252 O O   . LEU D 549 ? 0.6605 0.7403 0.9345 0.0392  -0.0757 0.1262  549 LEU D O   
10253 C CB  . LEU D 549 ? 0.7019 0.7284 0.8814 0.0153  -0.1012 0.1028  549 LEU D CB  
10254 C CG  . LEU D 549 ? 0.7376 0.7292 0.8599 0.0102  -0.1114 0.0938  549 LEU D CG  
10255 C CD1 . LEU D 549 ? 0.7512 0.7181 0.8404 0.0087  -0.0861 0.0838  549 LEU D CD1 
10256 C CD2 . LEU D 549 ? 0.7421 0.7330 0.8593 -0.0046 -0.1335 0.0868  549 LEU D CD2 
10257 N N   . THR D 550 ? 0.6466 0.7779 0.9918 0.0288  -0.1213 0.1411  550 THR D N   
10258 C CA  . THR D 550 ? 0.6235 0.7873 1.0274 0.0451  -0.1027 0.1566  550 THR D CA  
10259 C C   . THR D 550 ? 0.6141 0.7854 1.0343 0.0427  -0.0675 0.1543  550 THR D C   
10260 O O   . THR D 550 ? 0.6144 0.7923 1.0545 0.0601  -0.0386 0.1617  550 THR D O   
10261 C CB  . THR D 550 ? 0.5903 0.8005 1.0646 0.0441  -0.1317 0.1730  550 THR D CB  
10262 O OG1 . THR D 550 ? 0.5656 0.7973 1.0730 0.0212  -0.1411 0.1706  550 THR D OG1 
10263 C CG2 . THR D 550 ? 0.6093 0.8072 1.0560 0.0452  -0.1723 0.1746  550 THR D CG2 
10264 N N   . ASN D 551 ? 0.6430 0.8090 1.0508 0.0231  -0.0684 0.1448  551 ASN D N   
10265 C CA  . ASN D 551 ? 0.6431 0.8102 1.0551 0.0206  -0.0369 0.1437  551 ASN D CA  
10266 C C   . ASN D 551 ? 0.6801 0.8092 1.0320 0.0284  -0.0126 0.1313  551 ASN D C   
10267 O O   . ASN D 551 ? 0.6929 0.8160 1.0347 0.0273  0.0112  0.1292  551 ASN D O   
10268 C CB  . ASN D 551 ? 0.6304 0.7994 1.0459 -0.0019 -0.0477 0.1391  551 ASN D CB  
10269 C CG  . ASN D 551 ? 0.5942 0.8048 1.0841 -0.0101 -0.0485 0.1547  551 ASN D CG  
10270 O OD1 . ASN D 551 ? 0.5710 0.8051 1.1015 -0.0191 -0.0789 0.1605  551 ASN D OD1 
10271 N ND2 . ASN D 551 ? 0.5925 0.8116 1.1004 -0.0077 -0.0154 0.1623  551 ASN D ND2 
10272 N N   . LEU D 552 ? 0.6431 0.7454 0.9550 0.0355  -0.0185 0.1242  552 LEU D N   
10273 C CA  . LEU D 552 ? 0.6757 0.7418 0.9344 0.0383  -0.0006 0.1113  552 LEU D CA  
10274 C C   . LEU D 552 ? 0.6943 0.7548 0.9560 0.0544  0.0303  0.1143  552 LEU D C   
10275 O O   . LEU D 552 ? 0.6895 0.7580 0.9770 0.0715  0.0373  0.1246  552 LEU D O   
10276 C CB  . LEU D 552 ? 0.6898 0.7295 0.9130 0.0410  -0.0128 0.1061  552 LEU D CB  
10277 C CG  . LEU D 552 ? 0.7013 0.7161 0.8801 0.0274  -0.0203 0.0924  552 LEU D CG  
10278 C CD1 . LEU D 552 ? 0.7194 0.7079 0.8674 0.0324  -0.0256 0.0914  552 LEU D CD1 
10279 C CD2 . LEU D 552 ? 0.7135 0.7144 0.8698 0.0222  -0.0022 0.0818  552 LEU D CD2 
10280 N N   . GLU D 553 ? 0.6929 0.7368 0.9252 0.0503  0.0485  0.1057  553 GLU D N   
10281 C CA  . GLU D 553 ? 0.7271 0.7520 0.9419 0.0646  0.0787  0.1038  553 GLU D CA  
10282 C C   . GLU D 553 ? 0.7638 0.7445 0.9219 0.0644  0.0826  0.0875  553 GLU D C   
10283 O O   . GLU D 553 ? 0.7897 0.7457 0.9315 0.0789  0.1025  0.0850  553 GLU D O   
10284 C CB  . GLU D 553 ? 0.7457 0.7754 0.9569 0.0611  0.0970  0.1056  553 GLU D CB  
10285 C CG  . GLU D 553 ? 0.7065 0.7782 0.9778 0.0587  0.0985  0.1227  553 GLU D CG  
10286 C CD  . GLU D 553 ? 0.7245 0.7945 0.9833 0.0518  0.1148  0.1252  553 GLU D CD  
10287 O OE1 . GLU D 553 ? 0.7750 0.8108 0.9756 0.0531  0.1264  0.1142  553 GLU D OE1 
10288 O OE2 . GLU D 553 ? 0.6888 0.7896 0.9950 0.0444  0.1148  0.1387  553 GLU D OE2 
10289 N N   . TYR D 554 ? 0.7207 0.6901 0.8515 0.0480  0.0647  0.0767  554 TYR D N   
10290 C CA  . TYR D 554 ? 0.7503 0.6830 0.8347 0.0424  0.0664  0.0612  554 TYR D CA  
10291 C C   . TYR D 554 ? 0.7266 0.6570 0.8069 0.0308  0.0465  0.0575  554 TYR D C   
10292 O O   . TYR D 554 ? 0.7032 0.6507 0.7911 0.0196  0.0321  0.0576  554 TYR D O   
10293 C CB  . TYR D 554 ? 0.7807 0.7047 0.8358 0.0339  0.0703  0.0526  554 TYR D CB  
10294 C CG  . TYR D 554 ? 0.8151 0.7042 0.8258 0.0255  0.0676  0.0361  554 TYR D CG  
10295 C CD1 . TYR D 554 ? 0.7965 0.6865 0.8039 0.0101  0.0487  0.0293  554 TYR D CD1 
10296 C CD2 . TYR D 554 ? 0.8672 0.7217 0.8402 0.0324  0.0842  0.0270  554 TYR D CD2 
10297 C CE1 . TYR D 554 ? 0.8225 0.6864 0.7999 -0.0003 0.0435  0.0153  554 TYR D CE1 
10298 C CE2 . TYR D 554 ? 0.8981 0.7195 0.8312 0.0213  0.0768  0.0104  554 TYR D CE2 
10299 C CZ  . TYR D 554 ? 0.8726 0.7021 0.8128 0.0038  0.0550  0.0053  554 TYR D CZ  
10300 O OH  . TYR D 554 ? 0.8942 0.6963 0.8053 -0.0098 0.0451  -0.0101 554 TYR D OH  
10301 N N   . LEU D 555 ? 0.7670 0.6726 0.8337 0.0344  0.0485  0.0549  555 LEU D N   
10302 C CA  . LEU D 555 ? 0.7519 0.6514 0.8126 0.0258  0.0355  0.0542  555 LEU D CA  
10303 C C   . LEU D 555 ? 0.7718 0.6377 0.8046 0.0172  0.0414  0.0425  555 LEU D C   
10304 O O   . LEU D 555 ? 0.7954 0.6322 0.8141 0.0246  0.0541  0.0398  555 LEU D O   
10305 C CB  . LEU D 555 ? 0.7440 0.6459 0.8182 0.0380  0.0303  0.0672  555 LEU D CB  
10306 C CG  . LEU D 555 ? 0.7406 0.6330 0.8006 0.0312  0.0189  0.0688  555 LEU D CG  
10307 C CD1 . LEU D 555 ? 0.7217 0.6335 0.7844 0.0181  0.0064  0.0647  555 LEU D CD1 
10308 C CD2 . LEU D 555 ? 0.7446 0.6373 0.8110 0.0452  0.0101  0.0834  555 LEU D CD2 
10309 N N   . ASP D 556 ? 0.7726 0.6416 0.8007 0.0015  0.0328  0.0360  556 ASP D N   
10310 C CA  . ASP D 556 ? 0.7843 0.6285 0.7970 -0.0112 0.0356  0.0256  556 ASP D CA  
10311 C C   . ASP D 556 ? 0.7628 0.6111 0.7827 -0.0203 0.0316  0.0289  556 ASP D C   
10312 O O   . ASP D 556 ? 0.7405 0.6121 0.7718 -0.0268 0.0236  0.0287  556 ASP D O   
10313 C CB  . ASP D 556 ? 0.7969 0.6441 0.8011 -0.0219 0.0302  0.0138  556 ASP D CB  
10314 C CG  . ASP D 556 ? 0.8175 0.6347 0.8054 -0.0352 0.0307  0.0012  556 ASP D CG  
10315 O OD1 . ASP D 556 ? 0.8148 0.6117 0.8039 -0.0390 0.0369  0.0025  556 ASP D OD1 
10316 O OD2 . ASP D 556 ? 0.8398 0.6511 0.8116 -0.0427 0.0239  -0.0097 556 ASP D OD2 
10317 N N   . LEU D 557 ? 0.7761 0.5984 0.7872 -0.0193 0.0400  0.0331  557 LEU D N   
10318 C CA  . LEU D 557 ? 0.7677 0.5871 0.7803 -0.0272 0.0428  0.0377  557 LEU D CA  
10319 C C   . LEU D 557 ? 0.7778 0.5705 0.7889 -0.0412 0.0530  0.0329  557 LEU D C   
10320 O O   . LEU D 557 ? 0.7778 0.5617 0.7898 -0.0468 0.0620  0.0394  557 LEU D O   
10321 C CB  . LEU D 557 ? 0.7776 0.5880 0.7775 -0.0134 0.0440  0.0515  557 LEU D CB  
10322 C CG  . LEU D 557 ? 0.7718 0.6072 0.7764 -0.0022 0.0303  0.0573  557 LEU D CG  
10323 C CD1 . LEU D 557 ? 0.7920 0.6138 0.7792 0.0103  0.0265  0.0708  557 LEU D CD1 
10324 C CD2 . LEU D 557 ? 0.7533 0.6129 0.7666 -0.0109 0.0230  0.0523  557 LEU D CD2 
10325 N N   . SER D 558 ? 0.8389 0.6157 0.8459 -0.0480 0.0526  0.0216  558 SER D N   
10326 C CA  . SER D 558 ? 0.8548 0.5994 0.8598 -0.0631 0.0602  0.0157  558 SER D CA  
10327 C C   . SER D 558 ? 0.8382 0.6027 0.8709 -0.0855 0.0550  0.0106  558 SER D C   
10328 O O   . SER D 558 ? 0.8146 0.6168 0.8659 -0.0868 0.0460  0.0111  558 SER D O   
10329 C CB  . SER D 558 ? 0.8845 0.5993 0.8682 -0.0613 0.0602  0.0034  558 SER D CB  
10330 O OG  . SER D 558 ? 0.8862 0.6210 0.8698 -0.0675 0.0462  -0.0084 558 SER D OG  
10331 N N   . SER D 559 ? 0.8741 0.6124 0.9138 -0.1031 0.0616  0.0067  559 SER D N   
10332 C CA  . SER D 559 ? 0.8585 0.6161 0.9362 -0.1262 0.0595  0.0049  559 SER D CA  
10333 C C   . SER D 559 ? 0.8311 0.6206 0.9302 -0.1207 0.0694  0.0188  559 SER D C   
10334 O O   . SER D 559 ? 0.8062 0.6352 0.9343 -0.1248 0.0608  0.0178  559 SER D O   
10335 C CB  . SER D 559 ? 0.8570 0.6366 0.9487 -0.1401 0.0355  -0.0102 559 SER D CB  
10336 O OG  . SER D 559 ? 0.8919 0.6324 0.9652 -0.1536 0.0289  -0.0248 559 SER D OG  
10337 N N   . ASN D 560 ? 0.8391 0.6059 0.9186 -0.1095 0.0883  0.0324  560 ASN D N   
10338 C CA  . ASN D 560 ? 0.8303 0.6131 0.9118 -0.1008 0.1008  0.0451  560 ASN D CA  
10339 C C   . ASN D 560 ? 0.8519 0.5993 0.9220 -0.1033 0.1262  0.0587  560 ASN D C   
10340 O O   . ASN D 560 ? 0.8651 0.5827 0.9392 -0.1164 0.1332  0.0576  560 ASN D O   
10341 C CB  . ASN D 560 ? 0.8315 0.6229 0.8837 -0.0783 0.0913  0.0480  560 ASN D CB  
10342 C CG  . ASN D 560 ? 0.8078 0.6400 0.8793 -0.0766 0.0796  0.0432  560 ASN D CG  
10343 O OD1 . ASN D 560 ? 0.8017 0.6491 0.8889 -0.0784 0.0899  0.0477  560 ASN D OD1 
10344 N ND2 . ASN D 560 ? 0.7981 0.6453 0.8676 -0.0718 0.0611  0.0352  560 ASN D ND2 
10345 N N   . ARG D 561 ? 0.8839 0.6296 0.9355 -0.0913 0.1410  0.0716  561 ARG D N   
10346 C CA  . ARG D 561 ? 0.9104 0.6196 0.9427 -0.0915 0.1682  0.0875  561 ARG D CA  
10347 C C   . ARG D 561 ? 0.9420 0.6219 0.9156 -0.0676 0.1687  0.0995  561 ARG D C   
10348 O O   . ARG D 561 ? 0.9693 0.6235 0.9137 -0.0619 0.1901  0.1144  561 ARG D O   
10349 C CB  . ARG D 561 ? 0.9031 0.6310 0.9647 -0.1007 0.1916  0.0944  561 ARG D CB  
10350 C CG  . ARG D 561 ? 0.8688 0.6335 0.9987 -0.1244 0.1874  0.0850  561 ARG D CG  
10351 C CD  . ARG D 561 ? 0.8637 0.6393 1.0327 -0.1359 0.2191  0.0971  561 ARG D CD  
10352 N NE  . ARG D 561 ? 0.8689 0.6610 1.0259 -0.1186 0.2334  0.1032  561 ARG D NE  
10353 C CZ  . ARG D 561 ? 0.8579 0.6736 1.0567 -0.1232 0.2599  0.1112  561 ARG D CZ  
10354 N NH1 . ARG D 561 ? 0.8350 0.6674 1.0991 -0.1465 0.2740  0.1161  561 ARG D NH1 
10355 N NH2 . ARG D 561 ? 0.8725 0.6939 1.0488 -0.1040 0.2736  0.1146  561 ARG D NH2 
10356 N N   . PHE D 562 ? 0.9113 0.5949 0.8674 -0.0535 0.1451  0.0942  562 PHE D N   
10357 C CA  . PHE D 562 ? 0.9402 0.5996 0.8487 -0.0317 0.1392  0.1063  562 PHE D CA  
10358 C C   . PHE D 562 ? 0.9695 0.5788 0.8535 -0.0290 0.1564  0.1211  562 PHE D C   
10359 O O   . PHE D 562 ? 0.9656 0.5579 0.8680 -0.0390 0.1615  0.1169  562 PHE D O   
10360 C CB  . PHE D 562 ? 0.9283 0.6065 0.8395 -0.0194 0.1126  0.0990  562 PHE D CB  
10361 C CG  . PHE D 562 ? 0.9050 0.6264 0.8338 -0.0203 0.0959  0.0877  562 PHE D CG  
10362 C CD1 . PHE D 562 ? 0.9192 0.6473 0.8252 -0.0123 0.0907  0.0913  562 PHE D CD1 
10363 C CD2 . PHE D 562 ? 0.8754 0.6246 0.8377 -0.0288 0.0855  0.0735  562 PHE D CD2 
10364 C CE1 . PHE D 562 ? 0.9015 0.6633 0.8232 -0.0135 0.0765  0.0811  562 PHE D CE1 
10365 C CE2 . PHE D 562 ? 0.8558 0.6404 0.8326 -0.0288 0.0716  0.0656  562 PHE D CE2 
10366 C CZ  . PHE D 562 ? 0.8674 0.6582 0.8266 -0.0215 0.0676  0.0695  562 PHE D CZ  
10367 N N   . SER D 563 ? 1.0722 0.6522 0.9095 -0.0154 0.1655  0.1384  563 SER D N   
10368 C CA  . SER D 563 ? 1.1019 0.6316 0.9164 -0.0168 0.1906  0.1555  563 SER D CA  
10369 C C   . SER D 563 ? 1.1413 0.6303 0.9015 0.0072  0.1847  0.1749  563 SER D C   
10370 O O   . SER D 563 ? 1.1694 0.6106 0.9069 0.0078  0.2062  0.1914  563 SER D O   
10371 C CB  . SER D 563 ? 1.1133 0.6357 0.9235 -0.0281 0.2216  0.1636  563 SER D CB  
10372 O OG  . SER D 563 ? 1.1446 0.6579 0.9011 -0.0114 0.2219  0.1729  563 SER D OG  
10373 N N   . PHE D 564 ? 1.1599 0.6655 0.9016 0.0264  0.1556  0.1750  564 PHE D N   
10374 C CA  . PHE D 564 ? 1.1982 0.6689 0.8915 0.0501  0.1455  0.1956  564 PHE D CA  
10375 C C   . PHE D 564 ? 1.1836 0.6681 0.9013 0.0650  0.1216  0.1939  564 PHE D C   
10376 O O   . PHE D 564 ? 1.1492 0.6610 0.9135 0.0562  0.1184  0.1769  564 PHE D O   
10377 C CB  . PHE D 564 ? 1.2283 0.6989 0.8700 0.0614  0.1320  0.2022  564 PHE D CB  
10378 C CG  . PHE D 564 ? 1.2651 0.6964 0.8589 0.0572  0.1630  0.2145  564 PHE D CG  
10379 C CD1 . PHE D 564 ? 1.3094 0.6843 0.8509 0.0693  0.1773  0.2391  564 PHE D CD1 
10380 C CD2 . PHE D 564 ? 1.2570 0.7062 0.8587 0.0429  0.1808  0.2032  564 PHE D CD2 
10381 C CE1 . PHE D 564 ? 1.3461 0.6817 0.8401 0.0661  0.2109  0.2524  564 PHE D CE1 
10382 C CE2 . PHE D 564 ? 1.2918 0.7051 0.8516 0.0408  0.2152  0.2157  564 PHE D CE2 
10383 C CZ  . PHE D 564 ? 1.3367 0.6925 0.8410 0.0518  0.2314  0.2404  564 PHE D CZ  
10384 N N   . GLU D 565 ? 1.2304 0.6940 0.9153 0.0891  0.1060  0.2131  565 GLU D N   
10385 C CA  . GLU D 565 ? 1.2206 0.6931 0.9319 0.1076  0.0890  0.2169  565 GLU D CA  
10386 C C   . GLU D 565 ? 1.1871 0.7199 0.9381 0.1091  0.0611  0.2024  565 GLU D C   
10387 O O   . GLU D 565 ? 1.1856 0.7458 0.9271 0.1042  0.0439  0.1967  565 GLU D O   
10388 C CB  . GLU D 565 ? 1.2613 0.6993 0.9310 0.1347  0.0769  0.2447  565 GLU D CB  
10389 C CG  . GLU D 565 ? 1.2993 0.7232 0.9072 0.1389  0.0655  0.2568  565 GLU D CG  
10390 C CD  . GLU D 565 ? 1.3386 0.7020 0.8929 0.1339  0.0987  0.2719  565 GLU D CD  
10391 O OE1 . GLU D 565 ? 1.3255 0.6722 0.9019 0.1156  0.1319  0.2651  565 GLU D OE1 
10392 O OE2 . GLU D 565 ? 1.3851 0.7159 0.8737 0.1477  0.0912  0.2912  565 GLU D OE2 
10393 N N   . ILE D 566 ? 1.0890 0.6380 0.8827 0.1162  0.0594  0.1966  566 ILE D N   
10394 C CA  . ILE D 566 ? 1.0559 0.6607 0.8934 0.1170  0.0396  0.1842  566 ILE D CA  
10395 C C   . ILE D 566 ? 1.0665 0.6957 0.9010 0.1349  0.0063  0.1988  566 ILE D C   
10396 O O   . ILE D 566 ? 1.0907 0.6983 0.9105 0.1570  -0.0021 0.2201  566 ILE D O   
10397 C CB  . ILE D 566 ? 1.0377 0.6446 0.9132 0.1244  0.0513  0.1778  566 ILE D CB  
10398 C CG1 . ILE D 566 ? 1.0300 0.6154 0.9075 0.1023  0.0768  0.1590  566 ILE D CG1 
10399 C CG2 . ILE D 566 ? 1.0078 0.6702 0.9279 0.1299  0.0336  0.1713  566 ILE D CG2 
10400 C CD1 . ILE D 566 ? 1.0092 0.6091 0.9191 0.1019  0.0834  0.1427  566 ILE D CD1 
10401 N N   . PRO D 567 ? 1.0438 0.7164 0.8936 0.1262  -0.0152 0.1889  567 PRO D N   
10402 C CA  . PRO D 567 ? 1.0553 0.7521 0.9060 0.1391  -0.0519 0.2011  567 PRO D CA  
10403 C C   . PRO D 567 ? 1.0435 0.7601 0.9400 0.1625  -0.0621 0.2158  567 PRO D C   
10404 O O   . PRO D 567 ? 1.0087 0.7522 0.9563 0.1632  -0.0502 0.2077  567 PRO D O   
10405 C CB  . PRO D 567 ? 1.0316 0.7718 0.9058 0.1212  -0.0663 0.1830  567 PRO D CB  
10406 C CG  . PRO D 567 ? 1.0231 0.7490 0.8823 0.1006  -0.0386 0.1654  567 PRO D CG  
10407 C CD  . PRO D 567 ? 1.0180 0.7164 0.8837 0.1030  -0.0087 0.1666  567 PRO D CD  
10408 N N   . PRO D 568 ? 1.0732 0.7764 0.9518 0.1838  -0.0833 0.2389  568 PRO D N   
10409 C CA  . PRO D 568 ? 1.0578 0.7840 0.9882 0.2098  -0.0932 0.2561  568 PRO D CA  
10410 C C   . PRO D 568 ? 1.0210 0.8143 1.0149 0.2092  -0.1218 0.2545  568 PRO D C   
10411 O O   . PRO D 568 ? 0.9910 0.8143 1.0450 0.2288  -0.1229 0.2662  568 PRO D O   
10412 C CB  . PRO D 568 ? 1.1026 0.7936 0.9889 0.2317  -0.1123 0.2830  568 PRO D CB  
10413 C CG  . PRO D 568 ? 1.1402 0.7962 0.9482 0.2151  -0.1181 0.2782  568 PRO D CG  
10414 C CD  . PRO D 568 ? 1.1159 0.7923 0.9302 0.1856  -0.1063 0.2501  568 PRO D CD  
10415 N N   . THR D 569 ? 1.0433 0.8591 1.0283 0.1874  -0.1422 0.2408  569 THR D N   
10416 C CA  . THR D 569 ? 0.9987 0.8747 1.0418 0.1819  -0.1718 0.2393  569 THR D CA  
10417 C C   . THR D 569 ? 0.9499 0.8591 1.0432 0.1673  -0.1482 0.2211  569 THR D C   
10418 O O   . THR D 569 ? 0.9117 0.8687 1.0532 0.1580  -0.1675 0.2182  569 THR D O   
10419 C CB  . THR D 569 ? 1.0173 0.8913 1.0172 0.1658  -0.2085 0.2337  569 THR D CB  
10420 O OG1 . THR D 569 ? 1.0251 0.8768 0.9840 0.1425  -0.1876 0.2109  569 THR D OG1 
10421 C CG2 . THR D 569 ? 1.0732 0.9051 1.0073 0.1809  -0.2302 0.2518  569 THR D CG2 
10422 N N   . LEU D 570 ? 0.9615 0.8441 1.0416 0.1634  -0.1085 0.2090  570 LEU D N   
10423 C CA  . LEU D 570 ? 0.9235 0.8312 1.0414 0.1518  -0.0861 0.1929  570 LEU D CA  
10424 C C   . LEU D 570 ? 0.8970 0.8277 1.0737 0.1739  -0.0713 0.2042  570 LEU D C   
10425 O O   . LEU D 570 ? 0.9045 0.8069 1.0750 0.1837  -0.0392 0.2009  570 LEU D O   
10426 C CB  . LEU D 570 ? 0.9389 0.8080 1.0148 0.1368  -0.0554 0.1745  570 LEU D CB  
10427 C CG  . LEU D 570 ? 0.9379 0.8101 0.9901 0.1108  -0.0592 0.1566  570 LEU D CG  
10428 C CD1 . LEU D 570 ? 0.8984 0.8092 0.9931 0.1001  -0.0549 0.1454  570 LEU D CD1 
10429 C CD2 . LEU D 570 ? 0.9573 0.8296 0.9813 0.1060  -0.0907 0.1611  570 LEU D CD2 
10430 N N   . ASN D 571 ? 0.8727 0.8548 1.1093 0.1818  -0.0949 0.2177  571 ASN D N   
10431 C CA  . ASN D 571 ? 0.8445 0.8558 1.1473 0.2053  -0.0791 0.2313  571 ASN D CA  
10432 C C   . ASN D 571 ? 0.7953 0.8708 1.1722 0.1980  -0.0871 0.2335  571 ASN D C   
10433 O O   . ASN D 571 ? 0.7670 0.8790 1.2123 0.2188  -0.0807 0.2504  571 ASN D O   
10434 C CB  . ASN D 571 ? 0.8560 0.8647 1.1730 0.2343  -0.0963 0.2570  571 ASN D CB  
10435 C CG  . ASN D 571 ? 0.8505 0.8928 1.1829 0.2307  -0.1485 0.2706  571 ASN D CG  
10436 O OD1 . ASN D 571 ? 0.8136 0.9072 1.1957 0.2165  -0.1695 0.2693  571 ASN D OD1 
10437 N ND2 . ASN D 571 ? 0.8907 0.9003 1.1771 0.2428  -0.1705 0.2842  571 ASN D ND2 
10438 N N   . ASN D 572 ? 0.7595 0.8493 1.1285 0.1699  -0.0989 0.2187  572 ASN D N   
10439 C CA  . ASN D 572 ? 0.7146 0.8628 1.1527 0.1588  -0.1131 0.2230  572 ASN D CA  
10440 C C   . ASN D 572 ? 0.7050 0.8535 1.1352 0.1370  -0.0901 0.2042  572 ASN D C   
10441 O O   . ASN D 572 ? 0.6892 0.8568 1.1280 0.1143  -0.1100 0.1976  572 ASN D O   
10442 C CB  . ASN D 572 ? 0.7097 0.8784 1.1528 0.1458  -0.1651 0.2284  572 ASN D CB  
10443 C CG  . ASN D 572 ? 0.6584 0.8933 1.1927 0.1389  -0.1847 0.2400  572 ASN D CG  
10444 O OD1 . ASN D 572 ? 0.6261 0.8996 1.2341 0.1568  -0.1668 0.2559  572 ASN D OD1 
10445 N ND2 . ASN D 572 ? 0.6517 0.8982 1.1830 0.1129  -0.2198 0.2321  572 ASN D ND2 
10446 N N   . LEU D 573 ? 0.6769 0.7991 1.0852 0.1435  -0.0491 0.1948  573 LEU D N   
10447 C CA  . LEU D 573 ? 0.6755 0.7940 1.0701 0.1259  -0.0273 0.1787  573 LEU D CA  
10448 C C   . LEU D 573 ? 0.6599 0.8011 1.1025 0.1400  0.0075  0.1861  573 LEU D C   
10449 O O   . LEU D 573 ? 0.6862 0.7944 1.0981 0.1513  0.0415  0.1785  573 LEU D O   
10450 C CB  . LEU D 573 ? 0.7133 0.7779 1.0319 0.1179  -0.0123 0.1594  573 LEU D CB  
10451 C CG  . LEU D 573 ? 0.7354 0.7706 1.0031 0.1094  -0.0361 0.1544  573 LEU D CG  
10452 C CD1 . LEU D 573 ? 0.7651 0.7539 0.9740 0.1018  -0.0163 0.1377  573 LEU D CD1 
10453 C CD2 . LEU D 573 ? 0.7224 0.7768 0.9916 0.0892  -0.0671 0.1511  573 LEU D CD2 
10454 N N   . PRO D 574 ? 0.6559 0.8509 1.1727 0.1385  0.0013  0.2005  574 PRO D N   
10455 C CA  . PRO D 574 ? 0.6393 0.8599 1.2107 0.1563  0.0383  0.2125  574 PRO D CA  
10456 C C   . PRO D 574 ? 0.6600 0.8604 1.1995 0.1491  0.0754  0.1997  574 PRO D C   
10457 O O   . PRO D 574 ? 0.6524 0.8691 1.2289 0.1637  0.1107  0.2094  574 PRO D O   
10458 C CB  . PRO D 574 ? 0.5862 0.8740 1.2506 0.1498  0.0157  0.2318  574 PRO D CB  
10459 C CG  . PRO D 574 ? 0.5826 0.8735 1.2360 0.1365  -0.0370 0.2313  574 PRO D CG  
10460 C CD  . PRO D 574 ? 0.6241 0.8584 1.1818 0.1212  -0.0405 0.2078  574 PRO D CD  
10461 N N   . ARG D 575 ? 0.6979 0.8630 1.1700 0.1288  0.0698  0.1799  575 ARG D N   
10462 C CA  . ARG D 575 ? 0.7252 0.8685 1.1605 0.1225  0.0998  0.1686  575 ARG D CA  
10463 C C   . ARG D 575 ? 0.7755 0.8604 1.1278 0.1216  0.1082  0.1480  575 ARG D C   
10464 O O   . ARG D 575 ? 0.8075 0.8691 1.1192 0.1159  0.1276  0.1370  575 ARG D O   
10465 C CB  . ARG D 575 ? 0.7092 0.8711 1.1517 0.0963  0.0846  0.1661  575 ARG D CB  
10466 C CG  . ARG D 575 ? 0.6609 0.8778 1.1868 0.0916  0.0805  0.1852  575 ARG D CG  
10467 C CD  . ARG D 575 ? 0.6467 0.8714 1.1717 0.0632  0.0583  0.1805  575 ARG D CD  
10468 N NE  . ARG D 575 ? 0.5978 0.8739 1.2067 0.0535  0.0468  0.1979  575 ARG D NE  
10469 C CZ  . ARG D 575 ? 0.5657 0.8733 1.2240 0.0506  0.0117  0.2063  575 ARG D CZ  
10470 N NH1 . ARG D 575 ? 0.5791 0.8695 1.2058 0.0582  -0.0139 0.2003  575 ARG D NH1 
10471 N NH2 . ARG D 575 ? 0.5216 0.8781 1.2627 0.0390  0.0012  0.2222  575 ARG D NH2 
10472 N N   . LEU D 576 ? 0.7393 0.7996 1.0656 0.1260  0.0931  0.1435  576 LEU D N   
10473 C CA  . LEU D 576 ? 0.7794 0.7879 1.0349 0.1193  0.0963  0.1243  576 LEU D CA  
10474 C C   . LEU D 576 ? 0.8164 0.7863 1.0432 0.1376  0.1308  0.1182  576 LEU D C   
10475 O O   . LEU D 576 ? 0.8145 0.7780 1.0600 0.1601  0.1427  0.1277  576 LEU D O   
10476 C CB  . LEU D 576 ? 0.7761 0.7701 1.0154 0.1164  0.0710  0.1240  576 LEU D CB  
10477 C CG  . LEU D 576 ? 0.8058 0.7544 0.9836 0.1036  0.0699  0.1062  576 LEU D CG  
10478 C CD1 . LEU D 576 ? 0.7972 0.7556 0.9604 0.0795  0.0523  0.0967  576 LEU D CD1 
10479 C CD2 . LEU D 576 ? 0.8109 0.7377 0.9765 0.1110  0.0595  0.1116  576 LEU D CD2 
10480 N N   . TYR D 577 ? 0.7761 0.7166 0.9541 0.1287  0.1455  0.1022  577 TYR D N   
10481 C CA  . TYR D 577 ? 0.8216 0.7131 0.9550 0.1423  0.1753  0.0910  577 TYR D CA  
10482 C C   . TYR D 577 ? 0.8569 0.6977 0.9271 0.1275  0.1658  0.0699  577 TYR D C   
10483 O O   . TYR D 577 ? 0.8996 0.6918 0.9234 0.1340  0.1860  0.0564  577 TYR D O   
10484 C CB  . TYR D 577 ? 0.8466 0.7376 0.9670 0.1464  0.2028  0.0897  577 TYR D CB  
10485 C CG  . TYR D 577 ? 0.8695 0.7581 0.9532 0.1229  0.1898  0.0786  577 TYR D CG  
10486 C CD1 . TYR D 577 ? 0.9213 0.7612 0.9344 0.1130  0.1888  0.0576  577 TYR D CD1 
10487 C CD2 . TYR D 577 ? 0.8397 0.7732 0.9609 0.1107  0.1770  0.0897  577 TYR D CD2 
10488 C CE1 . TYR D 577 ? 0.9440 0.7846 0.9274 0.0939  0.1739  0.0500  577 TYR D CE1 
10489 C CE2 . TYR D 577 ? 0.8632 0.7923 0.9517 0.0922  0.1657  0.0818  577 TYR D CE2 
10490 C CZ  . TYR D 577 ? 0.9165 0.8012 0.9374 0.0851  0.1638  0.0630  577 TYR D CZ  
10491 O OH  . TYR D 577 ? 0.9412 0.8244 0.9335 0.0690  0.1499  0.0576  577 TYR D OH  
10492 N N   . TYR D 578 ? 0.8210 0.6701 0.8888 0.1077  0.1367  0.0665  578 TYR D N   
10493 C CA  . TYR D 578 ? 0.8452 0.6549 0.8655 0.0905  0.1274  0.0485  578 TYR D CA  
10494 C C   . TYR D 578 ? 0.8159 0.6332 0.8485 0.0806  0.1051  0.0531  578 TYR D C   
10495 O O   . TYR D 578 ? 0.7830 0.6386 0.8444 0.0748  0.0876  0.0625  578 TYR D O   
10496 C CB  . TYR D 578 ? 0.8646 0.6763 0.8578 0.0717  0.1195  0.0362  578 TYR D CB  
10497 C CG  . TYR D 578 ? 0.8848 0.6632 0.8385 0.0524  0.1072  0.0182  578 TYR D CG  
10498 C CD1 . TYR D 578 ? 0.8543 0.6474 0.8206 0.0352  0.0855  0.0181  578 TYR D CD1 
10499 C CD2 . TYR D 578 ? 0.9328 0.6648 0.8376 0.0507  0.1174  0.0013  578 TYR D CD2 
10500 C CE1 . TYR D 578 ? 0.8654 0.6348 0.8078 0.0165  0.0752  0.0038  578 TYR D CE1 
10501 C CE2 . TYR D 578 ? 0.9465 0.6518 0.8227 0.0299  0.1021  -0.0149 578 TYR D CE2 
10502 C CZ  . TYR D 578 ? 0.9097 0.6375 0.8106 0.0126  0.0814  -0.0125 578 TYR D CZ  
10503 O OH  . TYR D 578 ? 0.9170 0.6242 0.8009 -0.0088 0.0673  -0.0268 578 TYR D OH  
10504 N N   . MET D 579 ? 0.8850 0.6612 0.8921 0.0782  0.1073  0.0463  579 MET D N   
10505 C CA  . MET D 579 ? 0.8663 0.6415 0.8764 0.0686  0.0915  0.0511  579 MET D CA  
10506 C C   . MET D 579 ? 0.8895 0.6185 0.8651 0.0537  0.0952  0.0365  579 MET D C   
10507 O O   . MET D 579 ? 0.9156 0.6011 0.8725 0.0628  0.1106  0.0330  579 MET D O   
10508 C CB  . MET D 579 ? 0.8552 0.6342 0.8872 0.0891  0.0915  0.0700  579 MET D CB  
10509 C CG  . MET D 579 ? 0.8570 0.6133 0.8746 0.0841  0.0835  0.0755  579 MET D CG  
10510 S SD  . MET D 579 ? 0.8432 0.6207 0.8842 0.1031  0.0680  0.1005  579 MET D SD  
10511 C CE  . MET D 579 ? 0.8080 0.6475 0.8844 0.0969  0.0482  0.1033  579 MET D CE  
10512 N N   . ASN D 580 ? 0.8653 0.6032 0.8364 0.0308  0.0818  0.0282  580 ASN D N   
10513 C CA  . ASN D 580 ? 0.8791 0.5825 0.8303 0.0118  0.0818  0.0158  580 ASN D CA  
10514 C C   . ASN D 580 ? 0.8561 0.5668 0.8195 0.0026  0.0756  0.0252  580 ASN D C   
10515 O O   . ASN D 580 ? 0.8309 0.5760 0.8093 -0.0063 0.0641  0.0275  580 ASN D O   
10516 C CB  . ASN D 580 ? 0.8870 0.5975 0.8279 -0.0071 0.0716  -0.0005 580 ASN D CB  
10517 C CG  . ASN D 580 ? 0.9139 0.5811 0.8314 -0.0249 0.0717  -0.0172 580 ASN D CG  
10518 O OD1 . ASN D 580 ? 0.9217 0.5545 0.8349 -0.0277 0.0802  -0.0161 580 ASN D OD1 
10519 N ND2 . ASN D 580 ? 0.9308 0.5984 0.8323 -0.0384 0.0601  -0.0321 580 ASN D ND2 
10520 N N   . LEU D 581 ? 0.8855 0.5584 0.8386 0.0051  0.0860  0.0308  581 LEU D N   
10521 C CA  . LEU D 581 ? 0.8745 0.5458 0.8311 -0.0023 0.0856  0.0415  581 LEU D CA  
10522 C C   . LEU D 581 ? 0.8908 0.5219 0.8391 -0.0214 0.0955  0.0349  581 LEU D C   
10523 O O   . LEU D 581 ? 0.8949 0.5073 0.8396 -0.0234 0.1041  0.0469  581 LEU D O   
10524 C CB  . LEU D 581 ? 0.8787 0.5447 0.8314 0.0203  0.0877  0.0616  581 LEU D CB  
10525 C CG  . LEU D 581 ? 0.8657 0.5691 0.8331 0.0399  0.0759  0.0721  581 LEU D CG  
10526 C CD1 . LEU D 581 ? 0.8716 0.5708 0.8314 0.0531  0.0701  0.0916  581 LEU D CD1 
10527 C CD2 . LEU D 581 ? 0.8407 0.5901 0.8244 0.0299  0.0619  0.0658  581 LEU D CD2 
10528 N N   . SER D 582 ? 0.9670 0.5819 0.9102 -0.0365 0.0939  0.0164  582 SER D N   
10529 C CA  . SER D 582 ? 0.9868 0.5600 0.9253 -0.0576 0.1006  0.0081  582 SER D CA  
10530 C C   . SER D 582 ? 0.9637 0.5620 0.9305 -0.0817 0.0964  0.0102  582 SER D C   
10531 O O   . SER D 582 ? 0.9343 0.5801 0.9201 -0.0818 0.0876  0.0144  582 SER D O   
10532 C CB  . SER D 582 ? 1.0155 0.5615 0.9349 -0.0677 0.0954  -0.0146 582 SER D CB  
10533 O OG  . SER D 582 ? 1.0023 0.5883 0.9303 -0.0780 0.0769  -0.0256 582 SER D OG  
10534 N N   . ARG D 583 ? 1.0142 0.5780 0.9863 -0.1019 0.1053  0.0082  583 ARG D N   
10535 C CA  . ARG D 583 ? 0.9953 0.5818 1.0036 -0.1277 0.1047  0.0096  583 ARG D CA  
10536 C C   . ARG D 583 ? 0.9703 0.5889 0.9905 -0.1175 0.1142  0.0291  583 ARG D C   
10537 O O   . ARG D 583 ? 0.9423 0.6081 0.9871 -0.1213 0.1060  0.0289  583 ARG D O   
10538 C CB  . ARG D 583 ? 0.9837 0.6042 1.0140 -0.1465 0.0816  -0.0082 583 ARG D CB  
10539 C CG  . ARG D 583 ? 1.0197 0.5987 1.0299 -0.1611 0.0713  -0.0293 583 ARG D CG  
10540 C CD  . ARG D 583 ? 1.0188 0.6264 1.0276 -0.1677 0.0449  -0.0460 583 ARG D CD  
10541 N NE  . ARG D 583 ? 1.0558 0.6250 1.0141 -0.1552 0.0421  -0.0607 583 ARG D NE  
10542 C CZ  . ARG D 583 ? 1.0983 0.6083 1.0260 -0.1664 0.0424  -0.0773 583 ARG D CZ  
10543 N NH1 . ARG D 583 ? 1.1094 0.5917 1.0553 -0.1938 0.0421  -0.0819 583 ARG D NH1 
10544 N NH2 . ARG D 583 ? 1.1338 0.6088 1.0111 -0.1499 0.0448  -0.0896 583 ARG D NH2 
10545 N N   . ASN D 584 ? 0.9946 0.5815 0.9919 -0.1031 0.1318  0.0461  584 ASN D N   
10546 C CA  . ASN D 584 ? 0.9869 0.5893 0.9770 -0.0899 0.1412  0.0646  584 ASN D CA  
10547 C C   . ASN D 584 ? 1.0152 0.5680 0.9859 -0.0892 0.1651  0.0821  584 ASN D C   
10548 O O   . ASN D 584 ? 1.0320 0.5471 1.0091 -0.1055 0.1752  0.0789  584 ASN D O   
10549 C CB  . ASN D 584 ? 0.9821 0.6044 0.9505 -0.0629 0.1274  0.0683  584 ASN D CB  
10550 C CG  . ASN D 584 ? 0.9523 0.6277 0.9406 -0.0645 0.1109  0.0592  584 ASN D CG  
10551 O OD1 . ASN D 584 ? 0.9420 0.6402 0.9341 -0.0632 0.1131  0.0656  584 ASN D OD1 
10552 N ND2 . ASN D 584 ? 0.9444 0.6344 0.9404 -0.0659 0.0960  0.0445  584 ASN D ND2 
10553 N N   . ASP D 585 ? 1.1042 0.6528 1.0482 -0.0717 0.1739  0.1009  585 ASP D N   
10554 C CA  . ASP D 585 ? 1.1365 0.6350 1.0540 -0.0686 0.1978  0.1210  585 ASP D CA  
10555 C C   . ASP D 585 ? 1.1617 0.6377 1.0317 -0.0373 0.1927  0.1379  585 ASP D C   
10556 O O   . ASP D 585 ? 1.1889 0.6362 1.0253 -0.0287 0.2080  0.1584  585 ASP D O   
10557 C CB  . ASP D 585 ? 1.1353 0.6419 1.0631 -0.0818 0.2203  0.1319  585 ASP D CB  
10558 C CG  . ASP D 585 ? 1.1221 0.6307 1.1002 -0.1146 0.2335  0.1244  585 ASP D CG  
10559 O OD1 . ASP D 585 ? 1.1433 0.6069 1.1224 -0.1265 0.2439  0.1261  585 ASP D OD1 
10560 O OD2 . ASP D 585 ? 1.0915 0.6464 1.1110 -0.1288 0.2324  0.1172  585 ASP D OD2 
10561 N N   . LEU D 586 ? 1.1004 0.5891 0.9677 -0.0197 0.1714  0.1311  586 LEU D N   
10562 C CA  . LEU D 586 ? 1.1219 0.5957 0.9554 0.0102  0.1623  0.1481  586 LEU D CA  
10563 C C   . LEU D 586 ? 1.1563 0.5679 0.9671 0.0194  0.1786  0.1634  586 LEU D C   
10564 O O   . LEU D 586 ? 1.1603 0.5437 0.9850 0.0096  0.1881  0.1535  586 LEU D O   
10565 C CB  . LEU D 586 ? 1.1031 0.6118 0.9521 0.0259  0.1385  0.1384  586 LEU D CB  
10566 C CG  . LEU D 586 ? 1.0692 0.6358 0.9439 0.0177  0.1213  0.1220  586 LEU D CG  
10567 C CD1 . LEU D 586 ? 1.0499 0.6266 0.9537 -0.0037 0.1246  0.1010  586 LEU D CD1 
10568 C CD2 . LEU D 586 ? 1.0609 0.6567 0.9422 0.0385  0.1001  0.1234  586 LEU D CD2 
10569 N N   . ASP D 587 ? 1.2445 0.6301 1.0155 0.0391  0.1805  0.1875  587 ASP D N   
10570 C CA  . ASP D 587 ? 1.2822 0.6040 1.0250 0.0509  0.1971  0.2076  587 ASP D CA  
10571 C C   . ASP D 587 ? 1.2971 0.6145 1.0221 0.0864  0.1774  0.2232  587 ASP D C   
10572 O O   . ASP D 587 ? 1.2765 0.6425 1.0161 0.0989  0.1515  0.2176  587 ASP D O   
10573 C CB  . ASP D 587 ? 1.3122 0.5983 1.0192 0.0435  0.2205  0.2275  587 ASP D CB  
10574 C CG  . ASP D 587 ? 1.3312 0.6290 0.9931 0.0626  0.2068  0.2438  587 ASP D CG  
10575 O OD1 . ASP D 587 ? 1.3137 0.6551 0.9808 0.0760  0.1766  0.2369  587 ASP D OD1 
10576 O OD2 . ASP D 587 ? 1.3679 0.6277 0.9859 0.0633  0.2267  0.2637  587 ASP D OD2 
10577 N N   . GLN D 588 ? 1.3738 0.6322 1.0716 0.1024  0.1903  0.2444  588 GLN D N   
10578 C CA  . GLN D 588 ? 1.3929 0.6408 1.0749 0.1391  0.1733  0.2653  588 GLN D CA  
10579 C C   . GLN D 588 ? 1.3681 0.6429 1.0929 0.1534  0.1616  0.2518  588 GLN D C   
10580 O O   . GLN D 588 ? 1.3442 0.6329 1.0999 0.1346  0.1692  0.2260  588 GLN D O   
10581 C CB  . GLN D 588 ? 1.4020 0.6795 1.0540 0.1535  0.1470  0.2801  588 GLN D CB  
10582 C CG  . GLN D 588 ? 1.4336 0.6790 1.0334 0.1418  0.1635  0.2934  588 GLN D CG  
10583 C CD  . GLN D 588 ? 1.4685 0.7096 1.0142 0.1650  0.1398  0.3163  588 GLN D CD  
10584 O OE1 . GLN D 588 ? 1.4701 0.7303 1.0206 0.1906  0.1083  0.3259  588 GLN D OE1 
10585 N NE2 . GLN D 588 ? 1.4983 0.7198 0.9963 0.1551  0.1534  0.3233  588 GLN D NE2 
10586 N N   . THR D 589 ? 1.3420 0.6232 1.0684 0.1875  0.1437  0.2703  589 THR D N   
10587 C CA  . THR D 589 ? 1.3270 0.6196 1.0923 0.2074  0.1423  0.2640  589 THR D CA  
10588 C C   . THR D 589 ? 1.2839 0.6518 1.0919 0.2027  0.1223  0.2449  589 THR D C   
10589 O O   . THR D 589 ? 1.2690 0.6826 1.0764 0.1933  0.1008  0.2432  589 THR D O   
10590 C CB  . THR D 589 ? 1.3486 0.6297 1.1114 0.2456  0.1302  0.2922  589 THR D CB  
10591 O OG1 . THR D 589 ? 1.3255 0.6350 1.1359 0.2681  0.1269  0.2877  589 THR D OG1 
10592 C CG2 . THR D 589 ? 1.3564 0.6659 1.0975 0.2577  0.0981  0.3141  589 THR D CG2 
10593 N N   . ILE D 590 ? 1.2210 0.5959 1.0624 0.2099  0.1321  0.2307  590 ILE D N   
10594 C CA  . ILE D 590 ? 1.1554 0.5974 1.0393 0.2102  0.1174  0.2168  590 ILE D CA  
10595 C C   . ILE D 590 ? 1.1494 0.6352 1.0589 0.2392  0.0903  0.2399  590 ILE D C   
10596 O O   . ILE D 590 ? 1.1949 0.6595 1.1117 0.2705  0.0924  0.2609  590 ILE D O   
10597 C CB  . ILE D 590 ? 1.1564 0.5847 1.0600 0.2136  0.1397  0.1978  590 ILE D CB  
10598 C CG1 . ILE D 590 ? 1.1682 0.5535 1.0461 0.1816  0.1594  0.1737  590 ILE D CG1 
10599 C CG2 . ILE D 590 ? 1.0984 0.5927 1.0435 0.2152  0.1292  0.1865  590 ILE D CG2 
10600 C CD1 . ILE D 590 ? 1.2427 0.5494 1.0954 0.1884  0.1839  0.1769  590 ILE D CD1 
10601 N N   . PRO D 591 ? 1.1418 0.6875 1.0683 0.2303  0.0632  0.2374  591 PRO D N   
10602 C CA  . PRO D 591 ? 1.1350 0.7229 1.0881 0.2540  0.0316  0.2595  591 PRO D CA  
10603 C C   . PRO D 591 ? 1.1183 0.7404 1.1337 0.2787  0.0355  0.2639  591 PRO D C   
10604 O O   . PRO D 591 ? 1.0899 0.7206 1.1283 0.2720  0.0575  0.2446  591 PRO D O   
10605 C CB  . PRO D 591 ? 1.1188 0.7551 1.0720 0.2310  0.0054  0.2490  591 PRO D CB  
10606 C CG  . PRO D 591 ? 1.0993 0.7393 1.0549 0.2031  0.0266  0.2203  591 PRO D CG  
10607 C CD  . PRO D 591 ? 1.1217 0.6979 1.0457 0.1980  0.0587  0.2148  591 PRO D CD  
10608 N N   . GLU D 592 ? 1.2523 0.8937 1.2945 0.3087  0.0139  0.2911  592 GLU D N   
10609 C CA  . GLU D 592 ? 1.2226 0.9027 1.3345 0.3362  0.0185  0.3004  592 GLU D CA  
10610 C C   . GLU D 592 ? 1.1771 0.9318 1.3435 0.3225  0.0051  0.2890  592 GLU D C   
10611 O O   . GLU D 592 ? 1.1488 0.9324 1.3702 0.3366  0.0233  0.2878  592 GLU D O   
10612 C CB  . GLU D 592 ? 1.2316 0.9196 1.3657 0.3720  -0.0059 0.3353  592 GLU D CB  
10613 C CG  . GLU D 592 ? 1.2686 0.9026 1.3914 0.3959  0.0209  0.3426  592 GLU D CG  
10614 C CD  . GLU D 592 ? 1.2553 0.9215 1.4446 0.4174  0.0405  0.3402  592 GLU D CD  
10615 O OE1 . GLU D 592 ? 1.2350 0.9690 1.4882 0.4308  0.0155  0.3535  592 GLU D OE1 
10616 O OE2 . GLU D 592 ? 1.2738 0.8963 1.4499 0.4195  0.0811  0.3242  592 GLU D OE2 
10617 N N   . GLY D 593 ? 1.0782 0.8609 1.2290 0.2962  -0.0239 0.2813  593 GLY D N   
10618 C CA  . GLY D 593 ? 1.0365 0.8854 1.2375 0.2814  -0.0381 0.2719  593 GLY D CA  
10619 C C   . GLY D 593 ? 1.0175 0.8693 1.2284 0.2662  -0.0044 0.2473  593 GLY D C   
10620 O O   . GLY D 593 ? 0.9808 0.8851 1.2452 0.2628  -0.0057 0.2445  593 GLY D O   
10621 N N   . LEU D 594 ? 1.0510 0.8462 1.2106 0.2557  0.0247  0.2302  594 LEU D N   
10622 C CA  . LEU D 594 ? 1.0422 0.8345 1.2016 0.2411  0.0529  0.2062  594 LEU D CA  
10623 C C   . LEU D 594 ? 1.0284 0.8339 1.2343 0.2664  0.0787  0.2107  594 LEU D C   
10624 O O   . LEU D 594 ? 1.0126 0.8415 1.2370 0.2582  0.0935  0.1975  594 LEU D O   
10625 C CB  . LEU D 594 ? 1.0749 0.8021 1.1731 0.2251  0.0742  0.1884  594 LEU D CB  
10626 C CG  . LEU D 594 ? 1.0730 0.8025 1.1408 0.1898  0.0679  0.1678  594 LEU D CG  
10627 C CD1 . LEU D 594 ? 1.0684 0.8234 1.1296 0.1799  0.0360  0.1769  594 LEU D CD1 
10628 C CD2 . LEU D 594 ? 1.1011 0.7696 1.1209 0.1751  0.0878  0.1538  594 LEU D CD2 
10629 N N   . THR D 595 ? 1.0902 0.8783 1.3135 0.2991  0.0870  0.2302  595 THR D N   
10630 C CA  . THR D 595 ? 1.0787 0.8767 1.3484 0.3284  0.1163  0.2368  595 THR D CA  
10631 C C   . THR D 595 ? 1.0302 0.9099 1.3798 0.3347  0.1044  0.2495  595 THR D C   
10632 O O   . THR D 595 ? 1.0157 0.9120 1.4118 0.3586  0.1328  0.2560  595 THR D O   
10633 C CB  . THR D 595 ? 1.0977 0.8593 1.3723 0.3649  0.1257  0.2582  595 THR D CB  
10634 O OG1 . THR D 595 ? 1.0749 0.8860 1.3984 0.3816  0.0895  0.2876  595 THR D OG1 
10635 C CG2 . THR D 595 ? 1.1434 0.8266 1.3428 0.3553  0.1310  0.2504  595 THR D CG2 
10636 N N   . LYS D 596 ? 0.9423 0.8709 1.3105 0.3148  0.0650  0.2542  596 LYS D N   
10637 C CA  . LYS D 596 ? 0.8939 0.8995 1.3408 0.3146  0.0512  0.2653  596 LYS D CA  
10638 C C   . LYS D 596 ? 0.8804 0.9055 1.3230 0.2852  0.0606  0.2443  596 LYS D C   
10639 O O   . LYS D 596 ? 0.8403 0.9263 1.3461 0.2796  0.0507  0.2522  596 LYS D O   
10640 C CB  . LYS D 596 ? 0.8773 0.9232 1.3504 0.3110  -0.0015 0.2839  596 LYS D CB  
10641 C CG  . LYS D 596 ? 0.8951 0.9221 1.3705 0.3425  -0.0147 0.3083  596 LYS D CG  
10642 C CD  . LYS D 596 ? 0.9040 0.9437 1.3627 0.3333  -0.0691 0.3203  596 LYS D CD  
10643 C CE  . LYS D 596 ? 0.9405 0.9386 1.3703 0.3619  -0.0783 0.3419  596 LYS D CE  
10644 N NZ  . LYS D 596 ? 0.9702 0.9580 1.3505 0.3505  -0.1263 0.3492  596 LYS D NZ  
10645 N N   . LEU D 597 ? 0.8969 0.8719 1.2695 0.2660  0.0786  0.2193  597 LEU D N   
10646 C CA  . LEU D 597 ? 0.8913 0.8781 1.2529 0.2408  0.0886  0.2003  597 LEU D CA  
10647 C C   . LEU D 597 ? 0.8964 0.8769 1.2725 0.2576  0.1332  0.1967  597 LEU D C   
10648 O O   . LEU D 597 ? 0.9344 0.8614 1.2539 0.2559  0.1604  0.1779  597 LEU D O   
10649 C CB  . LEU D 597 ? 0.9229 0.8630 1.2081 0.2141  0.0845  0.1772  597 LEU D CB  
10650 C CG  . LEU D 597 ? 0.9303 0.8597 1.1840 0.1997  0.0507  0.1786  597 LEU D CG  
10651 C CD1 . LEU D 597 ? 0.9420 0.8530 1.1468 0.1689  0.0470  0.1569  597 LEU D CD1 
10652 C CD2 . LEU D 597 ? 0.9004 0.8830 1.2015 0.2001  0.0149  0.1960  597 LEU D CD2 
10653 N N   . SER D 598 ? 0.8595 0.8955 1.3130 0.2733  0.1405  0.2152  598 SER D N   
10654 C CA  . SER D 598 ? 0.8641 0.8942 1.3397 0.2995  0.1879  0.2186  598 SER D CA  
10655 C C   . SER D 598 ? 0.8931 0.8953 1.3182 0.2845  0.2178  0.1963  598 SER D C   
10656 O O   . SER D 598 ? 0.9281 0.8839 1.3176 0.3017  0.2579  0.1868  598 SER D O   
10657 C CB  . SER D 598 ? 0.8099 0.9151 1.3904 0.3164  0.1888  0.2457  598 SER D CB  
10658 O OG  . SER D 598 ? 0.7765 0.9339 1.3904 0.2878  0.1644  0.2467  598 SER D OG  
10659 N N   . GLN D 599 ? 0.9021 0.9269 1.3183 0.2536  0.1986  0.1876  599 GLN D N   
10660 C CA  . GLN D 599 ? 0.9303 0.9344 1.3035 0.2413  0.2243  0.1709  599 GLN D CA  
10661 C C   . GLN D 599 ? 0.9841 0.9202 1.2635 0.2266  0.2245  0.1439  599 GLN D C   
10662 O O   . GLN D 599 ? 1.0154 0.9293 1.2496 0.2155  0.2403  0.1288  599 GLN D O   
10663 C CB  . GLN D 599 ? 0.8999 0.9539 1.3042 0.2157  0.2050  0.1745  599 GLN D CB  
10664 C CG  . GLN D 599 ? 0.8423 0.9677 1.3469 0.2238  0.2016  0.2006  599 GLN D CG  
10665 C CD  . GLN D 599 ? 0.8355 0.9715 1.3843 0.2558  0.2487  0.2152  599 GLN D CD  
10666 O OE1 . GLN D 599 ? 0.8734 0.9666 1.3720 0.2660  0.2899  0.2040  599 GLN D OE1 
10667 N NE2 . GLN D 599 ? 0.7883 0.9812 1.4313 0.2726  0.2426  0.2407  599 GLN D NE2 
10668 N N   . LEU D 600 ? 0.9382 0.8409 1.1886 0.2255  0.2068  0.1390  600 LEU D N   
10669 C CA  . LEU D 600 ? 0.9809 0.8256 1.1540 0.2069  0.2029  0.1148  600 LEU D CA  
10670 C C   . LEU D 600 ? 1.0303 0.8183 1.1505 0.2175  0.2397  0.0981  600 LEU D C   
10671 O O   . LEU D 600 ? 1.0406 0.8063 1.1685 0.2462  0.2688  0.1040  600 LEU D O   
10672 C CB  . LEU D 600 ? 0.9830 0.8010 1.1423 0.2074  0.1841  0.1170  600 LEU D CB  
10673 C CG  . LEU D 600 ? 0.9884 0.7920 1.1090 0.1772  0.1566  0.1042  600 LEU D CG  
10674 C CD1 . LEU D 600 ? 0.9627 0.8142 1.1007 0.1553  0.1352  0.1035  600 LEU D CD1 
10675 C CD2 . LEU D 600 ? 0.9806 0.7746 1.1050 0.1822  0.1384  0.1165  600 LEU D CD2 
10676 N N   . GLN D 601 ? 1.0220 0.7844 1.0862 0.1952  0.2376  0.0772  601 GLN D N   
10677 C CA  . GLN D 601 ? 1.0781 0.7777 1.0752 0.1996  0.2647  0.0567  601 GLN D CA  
10678 C C   . GLN D 601 ? 1.1122 0.7524 1.0495 0.1813  0.2508  0.0348  601 GLN D C   
10679 O O   . GLN D 601 ? 1.1521 0.7290 1.0448 0.1923  0.2721  0.0217  601 GLN D O   
10680 C CB  . GLN D 601 ? 1.0984 0.8078 1.0700 0.1887  0.2721  0.0495  601 GLN D CB  
10681 C CG  . GLN D 601 ? 1.1619 0.8030 1.0539 0.1945  0.2995  0.0281  601 GLN D CG  
10682 C CD  . GLN D 601 ? 1.1875 0.8342 1.0448 0.1840  0.3042  0.0229  601 GLN D CD  
10683 O OE1 . GLN D 601 ? 1.1566 0.8585 1.0612 0.1847  0.3065  0.0409  601 GLN D OE1 
10684 N NE2 . GLN D 601 ? 1.2448 0.8316 1.0175 0.1734  0.3037  -0.0014 601 GLN D NE2 
10685 N N   . MET D 602 ? 1.0884 0.7461 1.0259 0.1535  0.2170  0.0308  602 MET D N   
10686 C CA  . MET D 602 ? 1.1107 0.7217 1.0051 0.1323  0.2024  0.0128  602 MET D CA  
10687 C C   . MET D 602 ? 1.0727 0.7059 1.0010 0.1244  0.1800  0.0255  602 MET D C   
10688 O O   . MET D 602 ? 1.0341 0.7221 1.0014 0.1189  0.1617  0.0387  602 MET D O   
10689 C CB  . MET D 602 ? 1.1321 0.7397 0.9885 0.1047  0.1855  -0.0057 602 MET D CB  
10690 C CG  . MET D 602 ? 1.1905 0.7447 0.9821 0.1071  0.2034  -0.0262 602 MET D CG  
10691 S SD  . MET D 602 ? 1.2098 0.7850 0.9716 0.0880  0.1874  -0.0351 602 MET D SD  
10692 C CE  . MET D 602 ? 1.2558 0.7683 0.9486 0.0607  0.1669  -0.0656 602 MET D CE  
10693 N N   . LEU D 603 ? 1.0531 0.6383 0.9620 0.1238  0.1827  0.0215  603 LEU D N   
10694 C CA  . LEU D 603 ? 1.0270 0.6212 0.9569 0.1182  0.1664  0.0347  603 LEU D CA  
10695 C C   . LEU D 603 ? 1.0518 0.5910 0.9450 0.0971  0.1643  0.0195  603 LEU D C   
10696 O O   . LEU D 603 ? 1.0856 0.5654 0.9515 0.1059  0.1823  0.0125  603 LEU D O   
10697 C CB  . LEU D 603 ? 1.0157 0.6125 0.9755 0.1491  0.1763  0.0571  603 LEU D CB  
10698 C CG  . LEU D 603 ? 1.0069 0.5920 0.9704 0.1473  0.1639  0.0709  603 LEU D CG  
10699 C CD1 . LEU D 603 ? 0.9742 0.6087 0.9553 0.1287  0.1367  0.0774  603 LEU D CD1 
10700 C CD2 . LEU D 603 ? 1.0036 0.5868 0.9930 0.1815  0.1725  0.0938  603 LEU D CD2 
10701 N N   . ASP D 604 ? 1.0162 0.5738 0.9118 0.0695  0.1439  0.0150  604 ASP D N   
10702 C CA  . ASP D 604 ? 1.0327 0.5476 0.9062 0.0454  0.1408  0.0027  604 ASP D CA  
10703 C C   . ASP D 604 ? 1.0077 0.5345 0.9011 0.0396  0.1335  0.0198  604 ASP D C   
10704 O O   . ASP D 604 ? 0.9755 0.5512 0.8908 0.0323  0.1185  0.0275  604 ASP D O   
10705 C CB  . ASP D 604 ? 1.0372 0.5615 0.8981 0.0170  0.1254  -0.0174 604 ASP D CB  
10706 C CG  . ASP D 604 ? 1.0585 0.5366 0.9009 -0.0096 0.1217  -0.0327 604 ASP D CG  
10707 O OD1 . ASP D 604 ? 1.0728 0.5063 0.9089 -0.0066 0.1345  -0.0279 604 ASP D OD1 
10708 O OD2 . ASP D 604 ? 1.0622 0.5480 0.8986 -0.0340 0.1051  -0.0485 604 ASP D OD2 
10709 N N   . LEU D 605 ? 0.9993 0.4761 0.8803 0.0439  0.1459  0.0259  605 LEU D N   
10710 C CA  . LEU D 605 ? 0.9962 0.4709 0.8848 0.0382  0.1436  0.0426  605 LEU D CA  
10711 C C   . LEU D 605 ? 1.0387 0.4649 0.9134 0.0117  0.1503  0.0331  605 LEU D C   
10712 O O   . LEU D 605 ? 1.0627 0.4638 0.9346 0.0108  0.1584  0.0483  605 LEU D O   
10713 C CB  . LEU D 605 ? 1.0181 0.4795 0.9080 0.0696  0.1516  0.0663  605 LEU D CB  
10714 C CG  . LEU D 605 ? 0.9800 0.4929 0.8946 0.0954  0.1426  0.0795  605 LEU D CG  
10715 C CD1 . LEU D 605 ? 1.0088 0.5082 0.9279 0.1252  0.1457  0.1048  605 LEU D CD1 
10716 C CD2 . LEU D 605 ? 0.9176 0.4904 0.8502 0.0822  0.1217  0.0815  605 LEU D CD2 
10717 N N   . SER D 606 ? 1.1218 0.5335 0.9873 -0.0109 0.1461  0.0091  606 SER D N   
10718 C CA  . SER D 606 ? 1.1469 0.5075 1.0025 -0.0379 0.1509  -0.0024 606 SER D CA  
10719 C C   . SER D 606 ? 1.1210 0.5094 1.0052 -0.0638 0.1449  0.0054  606 SER D C   
10720 O O   . SER D 606 ? 1.0858 0.5319 0.9917 -0.0627 0.1350  0.0142  606 SER D O   
10721 C CB  . SER D 606 ? 1.1731 0.5114 1.0079 -0.0554 0.1424  -0.0316 606 SER D CB  
10722 O OG  . SER D 606 ? 1.1477 0.5442 0.9975 -0.0668 0.1217  -0.0398 606 SER D OG  
10723 N N   . TYR D 607 ? 1.1835 0.5268 1.0684 -0.0873 0.1534  0.0024  607 TYR D N   
10724 C CA  . TYR D 607 ? 1.1633 0.5288 1.0814 -0.1154 0.1527  0.0087  607 TYR D CA  
10725 C C   . TYR D 607 ? 1.1385 0.5364 1.0652 -0.0990 0.1611  0.0352  607 TYR D C   
10726 O O   . TYR D 607 ? 1.1055 0.5597 1.0549 -0.1030 0.1520  0.0384  607 TYR D O   
10727 C CB  . TYR D 607 ? 1.1420 0.5548 1.0872 -0.1408 0.1299  -0.0095 607 TYR D CB  
10728 C CG  . TYR D 607 ? 1.1749 0.5483 1.1085 -0.1648 0.1184  -0.0358 607 TYR D CG  
10729 C CD1 . TYR D 607 ? 1.2023 0.5515 1.0957 -0.1512 0.1114  -0.0538 607 TYR D CD1 
10730 C CD2 . TYR D 607 ? 1.1830 0.5402 1.1440 -0.2015 0.1152  -0.0425 607 TYR D CD2 
10731 C CE1 . TYR D 607 ? 1.2411 0.5453 1.1114 -0.1730 0.0996  -0.0800 607 TYR D CE1 
10732 C CE2 . TYR D 607 ? 1.2188 0.5357 1.1655 -0.2262 0.0997  -0.0685 607 TYR D CE2 
10733 C CZ  . TYR D 607 ? 1.2497 0.5372 1.1457 -0.2114 0.0911  -0.0882 607 TYR D CZ  
10734 O OH  . TYR D 607 ? 1.2923 0.5320 1.1625 -0.2360 0.0743  -0.1161 607 TYR D OH  
10735 N N   . ASN D 608 ? 1.1800 0.5370 1.0831 -0.0785 0.1780  0.0543  608 ASN D N   
10736 C CA  . ASN D 608 ? 1.1701 0.5443 1.0673 -0.0612 0.1848  0.0800  608 ASN D CA  
10737 C C   . ASN D 608 ? 1.2042 0.5149 1.0801 -0.0579 0.2079  0.0995  608 ASN D C   
10738 O O   . ASN D 608 ? 1.2303 0.4878 1.1039 -0.0732 0.2193  0.0921  608 ASN D O   
10739 C CB  . ASN D 608 ? 1.1592 0.5645 1.0444 -0.0280 0.1716  0.0866  608 ASN D CB  
10740 C CG  . ASN D 608 ? 1.1228 0.5960 1.0277 -0.0312 0.1540  0.0809  608 ASN D CG  
10741 O OD1 . ASN D 608 ? 1.1084 0.6047 1.0254 -0.0454 0.1561  0.0852  608 ASN D OD1 
10742 N ND2 . ASN D 608 ? 1.1104 0.6134 1.0192 -0.0173 0.1394  0.0719  608 ASN D ND2 
10743 N N   . GLN D 609 ? 1.3117 0.6237 1.1681 -0.0386 0.2143  0.1247  609 GLN D N   
10744 C CA  . GLN D 609 ? 1.3477 0.5986 1.1763 -0.0309 0.2363  0.1483  609 GLN D CA  
10745 C C   . GLN D 609 ? 1.3676 0.5974 1.1646 0.0088  0.2312  0.1659  609 GLN D C   
10746 O O   . GLN D 609 ? 1.3948 0.5895 1.1609 0.0244  0.2422  0.1922  609 GLN D O   
10747 C CB  . GLN D 609 ? 1.3477 0.6066 1.1712 -0.0407 0.2512  0.1670  609 GLN D CB  
10748 C CG  . GLN D 609 ? 1.3517 0.5924 1.2021 -0.0764 0.2723  0.1639  609 GLN D CG  
10749 C CD  . GLN D 609 ? 1.3442 0.6086 1.1972 -0.0846 0.2887  0.1796  609 GLN D CD  
10750 O OE1 . GLN D 609 ? 1.3701 0.6185 1.1822 -0.0641 0.2981  0.2021  609 GLN D OE1 
10751 N NE2 . GLN D 609 ? 1.3156 0.6189 1.2160 -0.1132 0.2919  0.1676  609 GLN D NE2 
10752 N N   . LEU D 610 ? 1.3260 0.5775 1.1316 0.0262  0.2150  0.1532  610 LEU D N   
10753 C CA  . LEU D 610 ? 1.3390 0.5815 1.1287 0.0650  0.2085  0.1705  610 LEU D CA  
10754 C C   . LEU D 610 ? 1.3799 0.5465 1.1484 0.0769  0.2284  0.1823  610 LEU D C   
10755 O O   . LEU D 610 ? 1.3954 0.5303 1.1696 0.0574  0.2396  0.1638  610 LEU D O   
10756 C CB  . LEU D 610 ? 1.3161 0.6001 1.1281 0.0791  0.1926  0.1541  610 LEU D CB  
10757 C CG  . LEU D 610 ? 1.2766 0.6349 1.1115 0.0687  0.1721  0.1413  610 LEU D CG  
10758 C CD1 . LEU D 610 ? 1.2631 0.6388 1.1169 0.0597  0.1689  0.1143  610 LEU D CD1 
10759 C CD2 . LEU D 610 ? 1.2648 0.6647 1.1019 0.0957  0.1524  0.1588  610 LEU D CD2 
10760 N N   . ASP D 611 ? 1.4792 0.6387 1.2285 0.1065  0.2240  0.2082  611 ASP D N   
10761 C CA  . ASP D 611 ? 1.5303 0.6438 1.2673 0.1207  0.2348  0.2168  611 ASP D CA  
10762 C C   . ASP D 611 ? 1.5383 0.6635 1.2780 0.1633  0.2216  0.2332  611 ASP D C   
10763 O O   . ASP D 611 ? 1.4960 0.6669 1.2523 0.1792  0.2040  0.2353  611 ASP D O   
10764 C CB  . ASP D 611 ? 1.5788 0.6632 1.2902 0.1103  0.2466  0.2354  611 ASP D CB  
10765 C CG  . ASP D 611 ? 1.5810 0.6861 1.2661 0.1300  0.2330  0.2627  611 ASP D CG  
10766 O OD1 . ASP D 611 ? 1.5382 0.6853 1.2287 0.1454  0.2120  0.2655  611 ASP D OD1 
10767 O OD2 . ASP D 611 ? 1.6346 0.7116 1.2909 0.1297  0.2427  0.2812  611 ASP D OD2 
10768 N N   . GLY D 612 ? 1.5626 0.6497 1.2914 0.1818  0.2293  0.2458  612 GLY D N   
10769 C CA  . GLY D 612 ? 1.5753 0.6754 1.3168 0.2220  0.2181  0.2605  612 GLY D CA  
10770 C C   . GLY D 612 ? 1.5774 0.6682 1.3416 0.2315  0.2299  0.2399  612 GLY D C   
10771 O O   . GLY D 612 ? 1.5842 0.6463 1.3448 0.2070  0.2459  0.2138  612 GLY D O   
10772 N N   . GLU D 613 ? 1.5723 0.6889 1.3604 0.2679  0.2210  0.2518  613 GLU D N   
10773 C CA  . GLU D 613 ? 1.5868 0.6939 1.3945 0.2843  0.2362  0.2364  613 GLU D CA  
10774 C C   . GLU D 613 ? 1.5182 0.6824 1.3598 0.2912  0.2286  0.2253  613 GLU D C   
10775 O O   . GLU D 613 ? 1.4669 0.6864 1.3285 0.2980  0.2058  0.2393  613 GLU D O   
10776 C CB  . GLU D 613 ? 1.6438 0.7385 1.4616 0.3220  0.2376  0.2582  613 GLU D CB  
10777 C CG  . GLU D 613 ? 1.7210 0.7531 1.5042 0.3173  0.2481  0.2697  613 GLU D CG  
10778 C CD  . GLU D 613 ? 1.7862 0.7969 1.5788 0.3542  0.2538  0.2874  613 GLU D CD  
10779 O OE1 . GLU D 613 ? 1.7807 0.8312 1.5956 0.3835  0.2322  0.3133  613 GLU D OE1 
10780 O OE2 . GLU D 613 ? 1.8471 0.8008 1.6254 0.3536  0.2782  0.2753  613 GLU D OE2 
10781 N N   . ILE D 614 ? 1.5279 0.6758 1.3725 0.2890  0.2480  0.2000  614 ILE D N   
10782 C CA  . ILE D 614 ? 1.4737 0.6705 1.3486 0.2973  0.2469  0.1891  614 ILE D CA  
10783 C C   . ILE D 614 ? 1.4718 0.7133 1.3913 0.3385  0.2417  0.2113  614 ILE D C   
10784 O O   . ILE D 614 ? 1.5280 0.7432 1.4510 0.3614  0.2580  0.2148  614 ILE D O   
10785 C CB  . ILE D 614 ? 1.4954 0.6549 1.3501 0.2833  0.2702  0.1552  614 ILE D CB  
10786 C CG1 . ILE D 614 ? 1.5059 0.6224 1.3228 0.2399  0.2707  0.1337  614 ILE D CG1 
10787 C CG2 . ILE D 614 ? 1.4446 0.6537 1.3257 0.2908  0.2710  0.1451  614 ILE D CG2 
10788 C CD1 . ILE D 614 ? 1.5542 0.6176 1.3405 0.2244  0.2891  0.1012  614 ILE D CD1 
10789 N N   . SER D 615 ? 1.4911 0.8013 1.4479 0.3470  0.2179  0.2267  615 SER D N   
10790 C CA  . SER D 615 ? 1.4857 0.8489 1.4950 0.3822  0.2061  0.2501  615 SER D CA  
10791 C C   . SER D 615 ? 1.4940 0.8684 1.5337 0.4012  0.2326  0.2383  615 SER D C   
10792 O O   . SER D 615 ? 1.4620 0.8460 1.5018 0.3888  0.2461  0.2171  615 SER D O   
10793 C CB  . SER D 615 ? 1.4208 0.8573 1.4649 0.3813  0.1721  0.2657  615 SER D CB  
10794 O OG  . SER D 615 ? 1.4145 0.9081 1.5176 0.4116  0.1571  0.2870  615 SER D OG  
10795 N N   . SER D 616 ? 1.4678 0.8395 1.5311 0.4323  0.2411  0.2530  616 SER D N   
10796 C CA  . SER D 616 ? 1.4804 0.8713 1.5793 0.4549  0.2673  0.2474  616 SER D CA  
10797 C C   . SER D 616 ? 1.4115 0.8917 1.5763 0.4623  0.2537  0.2567  616 SER D C   
10798 O O   . SER D 616 ? 1.4120 0.9130 1.6047 0.4744  0.2791  0.2492  616 SER D O   
10799 C CB  . SER D 616 ? 1.5507 0.9230 1.6661 0.4881  0.2774  0.2649  616 SER D CB  
10800 O OG  . SER D 616 ? 1.5392 0.9612 1.6971 0.5055  0.2428  0.2964  616 SER D OG  
10801 N N   . GLN D 617 ? 1.4416 0.9728 1.6293 0.4538  0.2152  0.2729  617 GLN D N   
10802 C CA  . GLN D 617 ? 1.3747 0.9916 1.6258 0.4544  0.1975  0.2810  617 GLN D CA  
10803 C C   . GLN D 617 ? 1.3298 0.9530 1.5715 0.4335  0.2159  0.2569  617 GLN D C   
10804 O O   . GLN D 617 ? 1.2798 0.9718 1.5761 0.4333  0.2087  0.2617  617 GLN D O   
10805 C CB  . GLN D 617 ? 1.3395 0.9971 1.6022 0.4459  0.1489  0.3008  617 GLN D CB  
10806 C CG  . GLN D 617 ? 1.2987 1.0486 1.6424 0.4562  0.1210  0.3191  617 GLN D CG  
10807 C CD  . GLN D 617 ? 1.3431 1.1151 1.7385 0.4887  0.1257  0.3366  617 GLN D CD  
10808 O OE1 . GLN D 617 ? 1.3974 1.1387 1.7750 0.5049  0.1143  0.3512  617 GLN D OE1 
10809 N NE2 . GLN D 617 ? 1.3252 1.1492 1.7847 0.4988  0.1446  0.3364  617 GLN D NE2 
10810 N N   . PHE D 618 ? 1.4075 0.9608 1.5824 0.4144  0.2378  0.2312  618 PHE D N   
10811 C CA  . PHE D 618 ? 1.3855 0.9368 1.5439 0.3960  0.2552  0.2067  618 PHE D CA  
10812 C C   . PHE D 618 ? 1.3877 0.9657 1.5802 0.4145  0.2856  0.2026  618 PHE D C   
10813 O O   . PHE D 618 ? 1.3632 0.9620 1.5588 0.4038  0.2961  0.1896  618 PHE D O   
10814 C CB  . PHE D 618 ? 1.4296 0.8953 1.5088 0.3723  0.2712  0.1786  618 PHE D CB  
10815 C CG  . PHE D 618 ? 1.4238 0.8855 1.4715 0.3366  0.2434  0.1723  618 PHE D CG  
10816 C CD1 . PHE D 618 ? 1.3969 0.9056 1.4688 0.3330  0.2085  0.1941  618 PHE D CD1 
10817 C CD2 . PHE D 618 ? 1.4516 0.8690 1.4441 0.3023  0.2489  0.1426  618 PHE D CD2 
10818 C CE1 . PHE D 618 ? 1.3981 0.9071 1.4378 0.2983  0.1855  0.1865  618 PHE D CE1 
10819 C CE2 . PHE D 618 ? 1.4462 0.8712 1.4174 0.2669  0.2240  0.1368  618 PHE D CE2 
10820 C CZ  . PHE D 618 ? 1.4196 0.8892 1.4135 0.2660  0.1952  0.1588  618 PHE D CZ  
10821 N N   . ARG D 619 ? 1.3517 0.9292 1.5695 0.4427  0.3012  0.2151  619 ARG D N   
10822 C CA  . ARG D 619 ? 1.3719 0.9731 1.6232 0.4628  0.3343  0.2148  619 ARG D CA  
10823 C C   . ARG D 619 ? 1.3045 0.9939 1.6250 0.4605  0.3257  0.2261  619 ARG D C   
10824 O O   . ARG D 619 ? 1.3147 1.0192 1.6504 0.4679  0.3575  0.2208  619 ARG D O   
10825 C CB  . ARG D 619 ? 1.4282 1.0289 1.7120 0.4949  0.3433  0.2344  619 ARG D CB  
10826 C CG  . ARG D 619 ? 1.4782 1.0747 1.7758 0.5173  0.3876  0.2310  619 ARG D CG  
10827 C CD  . ARG D 619 ? 1.5076 1.1426 1.8733 0.5500  0.3868  0.2595  619 ARG D CD  
10828 N NE  . ARG D 619 ? 1.5783 1.1865 1.9419 0.5742  0.4342  0.2558  619 ARG D NE  
10829 C CZ  . ARG D 619 ? 1.5895 1.2541 2.0281 0.5994  0.4485  0.2769  619 ARG D CZ  
10830 N NH1 . ARG D 619 ? 1.5340 1.2879 2.0593 0.6021  0.4163  0.3021  619 ARG D NH1 
10831 N NH2 . ARG D 619 ? 1.6638 1.2931 2.0898 0.6214  0.4956  0.2723  619 ARG D NH2 
10832 N N   . SER D 620 ? 1.2522 0.9970 1.6109 0.4485  0.2839  0.2412  620 SER D N   
10833 C CA  . SER D 620 ? 1.1913 1.0227 1.6221 0.4432  0.2708  0.2532  620 SER D CA  
10834 C C   . SER D 620 ? 1.1652 0.9948 1.5721 0.4230  0.2884  0.2329  620 SER D C   
10835 O O   . SER D 620 ? 1.1323 1.0220 1.5934 0.4213  0.2954  0.2396  620 SER D O   
10836 C CB  . SER D 620 ? 1.1454 1.0275 1.6119 0.4326  0.2171  0.2721  620 SER D CB  
10837 O OG  . SER D 620 ? 1.1815 1.0550 1.6547 0.4506  0.1974  0.2898  620 SER D OG  
10838 N N   . LEU D 621 ? 1.1688 0.9301 1.4964 0.4063  0.2950  0.2087  621 LEU D N   
10839 C CA  . LEU D 621 ? 1.1756 0.9393 1.4661 0.3742  0.2965  0.1852  621 LEU D CA  
10840 C C   . LEU D 621 ? 1.1999 0.9375 1.4733 0.3904  0.3468  0.1732  621 LEU D C   
10841 O O   . LEU D 621 ? 1.2530 0.9155 1.4485 0.3862  0.3696  0.1480  621 LEU D O   
10842 C CB  . LEU D 621 ? 1.2116 0.9211 1.4216 0.3406  0.2769  0.1612  621 LEU D CB  
10843 C CG  . LEU D 621 ? 1.1854 0.9300 1.4021 0.3133  0.2291  0.1671  621 LEU D CG  
10844 C CD1 . LEU D 621 ? 1.1533 0.9470 1.4352 0.3332  0.2053  0.1979  621 LEU D CD1 
10845 C CD2 . LEU D 621 ? 1.2200 0.9031 1.3695 0.2927  0.2180  0.1521  621 LEU D CD2 
10846 N N   . GLN D 622 ? 1.0986 0.9002 1.4433 0.4053  0.3621  0.1911  622 GLN D N   
10847 C CA  . GLN D 622 ? 1.1340 0.9192 1.4630 0.4181  0.4089  0.1840  622 GLN D CA  
10848 C C   . GLN D 622 ? 1.1623 0.9042 1.4173 0.4015  0.4290  0.1570  622 GLN D C   
10849 O O   . GLN D 622 ? 1.2162 0.9101 1.4183 0.4100  0.4667  0.1430  622 GLN D O   
10850 C CB  . GLN D 622 ? 1.1024 0.9731 1.5265 0.4276  0.4155  0.2104  622 GLN D CB  
10851 C CG  . GLN D 622 ? 1.1106 1.0198 1.6050 0.4483  0.4024  0.2360  622 GLN D CG  
10852 C CD  . GLN D 622 ? 1.1935 1.0633 1.6730 0.4760  0.4448  0.2365  622 GLN D CD  
10853 O OE1 . GLN D 622 ? 1.2511 1.0415 1.6560 0.4829  0.4596  0.2188  622 GLN D OE1 
10854 N NE2 . GLN D 622 ? 1.2050 1.1282 1.7562 0.4908  0.4647  0.2570  622 GLN D NE2 
10855 N N   . ASN D 623 ? 1.1388 0.8999 1.3756 0.3658  0.3934  0.1474  623 ASN D N   
10856 C CA  . ASN D 623 ? 1.1766 0.9107 1.3439 0.3408  0.3998  0.1235  623 ASN D CA  
10857 C C   . ASN D 623 ? 1.2260 0.8921 1.3035 0.3146  0.3789  0.0947  623 ASN D C   
10858 O O   . ASN D 623 ? 1.2593 0.9029 1.2773 0.2919  0.3763  0.0745  623 ASN D O   
10859 C CB  . ASN D 623 ? 1.1355 0.9431 1.3476 0.3158  0.3747  0.1335  623 ASN D CB  
10860 C CG  . ASN D 623 ? 1.0962 0.9630 1.3858 0.3357  0.4041  0.1574  623 ASN D CG  
10861 O OD1 . ASN D 623 ? 1.1230 0.9673 1.3864 0.3492  0.4482  0.1533  623 ASN D OD1 
10862 N ND2 . ASN D 623 ? 1.0330 0.9746 1.4178 0.3369  0.3799  0.1828  623 ASN D ND2 
10863 N N   . LEU D 624 ? 1.2123 0.8456 1.2806 0.3171  0.3640  0.0937  624 LEU D N   
10864 C CA  . LEU D 624 ? 1.2483 0.8269 1.2468 0.2880  0.3412  0.0696  624 LEU D CA  
10865 C C   . LEU D 624 ? 1.3147 0.8099 1.2271 0.2884  0.3691  0.0411  624 LEU D C   
10866 O O   . LEU D 624 ? 1.3433 0.7847 1.2363 0.3165  0.4027  0.0384  624 LEU D O   
10867 C CB  . LEU D 624 ? 1.2392 0.7996 1.2504 0.2923  0.3238  0.0789  624 LEU D CB  
10868 C CG  . LEU D 624 ? 1.2422 0.7907 1.2223 0.2556  0.2870  0.0672  624 LEU D CG  
10869 C CD1 . LEU D 624 ? 1.2250 0.7758 1.2319 0.2621  0.2692  0.0857  624 LEU D CD1 
10870 C CD2 . LEU D 624 ? 1.2969 0.7666 1.1981 0.2376  0.2948  0.0369  624 LEU D CD2 
10871 N N   . GLU D 625 ? 1.3116 0.7928 1.1698 0.2576  0.3534  0.0195  625 GLU D N   
10872 C CA  . GLU D 625 ? 1.3785 0.7791 1.1457 0.2517  0.3699  -0.0104 625 GLU D CA  
10873 C C   . GLU D 625 ? 1.4067 0.7537 1.1245 0.2217  0.3423  -0.0328 625 GLU D C   
10874 O O   . GLU D 625 ? 1.4616 0.7265 1.1116 0.2227  0.3574  -0.0559 625 GLU D O   
10875 C CB  . GLU D 625 ? 1.3968 0.8132 1.1307 0.2392  0.3713  -0.0191 625 GLU D CB  
10876 C CG  . GLU D 625 ? 1.3726 0.8373 1.1517 0.2657  0.4038  0.0024  625 GLU D CG  
10877 C CD  . GLU D 625 ? 1.4052 0.8647 1.1324 0.2565  0.4131  -0.0072 625 GLU D CD  
10878 O OE1 . GLU D 625 ? 1.4678 0.8556 1.1018 0.2477  0.4162  -0.0342 625 GLU D OE1 
10879 O OE2 . GLU D 625 ? 1.3698 0.8943 1.1476 0.2576  0.4162  0.0127  625 GLU D OE2 
10880 N N   . ARG D 626 ? 1.3819 0.7708 1.1321 0.1947  0.3039  -0.0268 626 ARG D N   
10881 C CA  . ARG D 626 ? 1.4009 0.7496 1.1150 0.1625  0.2778  -0.0457 626 ARG D CA  
10882 C C   . ARG D 626 ? 1.3606 0.7322 1.1230 0.1572  0.2597  -0.0283 626 ARG D C   
10883 O O   . ARG D 626 ? 1.3113 0.7522 1.1280 0.1562  0.2431  -0.0080 626 ARG D O   
10884 C CB  . ARG D 626 ? 1.4042 0.7766 1.0969 0.1292  0.2484  -0.0594 626 ARG D CB  
10885 C CG  . ARG D 626 ? 1.4652 0.7802 1.0792 0.1230  0.2564  -0.0863 626 ARG D CG  
10886 C CD  . ARG D 626 ? 1.4624 0.8201 1.0678 0.1057  0.2359  -0.0886 626 ARG D CD  
10887 N NE  . ARG D 626 ? 1.5214 0.8211 1.0436 0.0910  0.2294  -0.1164 626 ARG D NE  
10888 C CZ  . ARG D 626 ? 1.5446 0.8045 1.0325 0.0612  0.2018  -0.1383 626 ARG D CZ  
10889 N NH1 . ARG D 626 ? 1.5137 0.7848 1.0445 0.0428  0.1825  -0.1348 626 ARG D NH1 
10890 N NH2 . ARG D 626 ? 1.6004 0.8075 1.0088 0.0490  0.1928  -0.1635 626 ARG D NH2 
10891 N N   . LEU D 627 ? 1.3479 0.6561 1.0845 0.1518  0.2626  -0.0371 627 LEU D N   
10892 C CA  . LEU D 627 ? 1.3205 0.6358 1.0917 0.1500  0.2515  -0.0191 627 LEU D CA  
10893 C C   . LEU D 627 ? 1.3442 0.6086 1.0823 0.1161  0.2374  -0.0372 627 LEU D C   
10894 O O   . LEU D 627 ? 1.3936 0.5876 1.0797 0.1082  0.2472  -0.0612 627 LEU D O   
10895 C CB  . LEU D 627 ? 1.3266 0.6124 1.1125 0.1881  0.2780  -0.0018 627 LEU D CB  
10896 C CG  . LEU D 627 ? 1.2978 0.5983 1.1200 0.1924  0.2657  0.0232  627 LEU D CG  
10897 C CD1 . LEU D 627 ? 1.2488 0.6282 1.1087 0.1733  0.2345  0.0352  627 LEU D CD1 
10898 C CD2 . LEU D 627 ? 1.2897 0.5910 1.1447 0.2360  0.2853  0.0483  627 LEU D CD2 
10899 N N   . ASP D 628 ? 1.2772 0.5758 1.0453 0.0953  0.2151  -0.0261 628 ASP D N   
10900 C CA  . ASP D 628 ? 1.2912 0.5508 1.0434 0.0623  0.2037  -0.0378 628 ASP D CA  
10901 C C   . ASP D 628 ? 1.2642 0.5361 1.0482 0.0639  0.2010  -0.0129 628 ASP D C   
10902 O O   . ASP D 628 ? 1.2226 0.5574 1.0398 0.0597  0.1852  0.0023  628 ASP D O   
10903 C CB  . ASP D 628 ? 1.2808 0.5731 1.0317 0.0269  0.1776  -0.0543 628 ASP D CB  
10904 C CG  . ASP D 628 ? 1.3026 0.5492 1.0377 -0.0089 0.1672  -0.0713 628 ASP D CG  
10905 O OD1 . ASP D 628 ? 1.3251 0.5140 1.0506 -0.0082 0.1814  -0.0689 628 ASP D OD1 
10906 O OD2 . ASP D 628 ? 1.2975 0.5662 1.0334 -0.0380 0.1444  -0.0858 628 ASP D OD2 
10907 N N   . LEU D 629 ? 1.2815 0.4878 1.0496 0.0701  0.2172  -0.0087 629 LEU D N   
10908 C CA  . LEU D 629 ? 1.2789 0.4802 1.0642 0.0698  0.2173  0.0148  629 LEU D CA  
10909 C C   . LEU D 629 ? 1.3236 0.4721 1.0939 0.0350  0.2177  0.0040  629 LEU D C   
10910 O O   . LEU D 629 ? 1.3487 0.4687 1.1218 0.0357  0.2264  0.0225  629 LEU D O   
10911 C CB  . LEU D 629 ? 1.3189 0.4889 1.1043 0.1098  0.2367  0.0369  629 LEU D CB  
10912 C CG  . LEU D 629 ? 1.2737 0.5026 1.0930 0.1452  0.2327  0.0632  629 LEU D CG  
10913 C CD1 . LEU D 629 ? 1.2105 0.5081 1.0502 0.1451  0.2211  0.0548  629 LEU D CD1 
10914 C CD2 . LEU D 629 ? 1.3316 0.5189 1.1489 0.1860  0.2556  0.0761  629 LEU D CD2 
10915 N N   . SER D 630 ? 1.3886 0.5237 1.1440 0.0040  0.2077  -0.0242 630 SER D N   
10916 C CA  . SER D 630 ? 1.4152 0.4963 1.1611 -0.0313 0.2072  -0.0370 630 SER D CA  
10917 C C   . SER D 630 ? 1.3806 0.5021 1.1645 -0.0554 0.1984  -0.0204 630 SER D C   
10918 O O   . SER D 630 ? 1.3374 0.5306 1.1486 -0.0503 0.1875  -0.0069 630 SER D O   
10919 C CB  . SER D 630 ? 1.4406 0.5037 1.1625 -0.0593 0.1918  -0.0716 630 SER D CB  
10920 O OG  . SER D 630 ? 1.4028 0.5425 1.1495 -0.0744 0.1674  -0.0754 630 SER D OG  
10921 N N   . HIS D 631 ? 1.4264 0.4967 1.2111 -0.0821 0.2058  -0.0218 631 HIS D N   
10922 C CA  . HIS D 631 ? 1.4005 0.5001 1.2218 -0.1093 0.2033  -0.0080 631 HIS D CA  
10923 C C   . HIS D 631 ? 1.3728 0.5074 1.2048 -0.0830 0.2128  0.0256  631 HIS D C   
10924 O O   . HIS D 631 ? 1.3330 0.5359 1.1893 -0.0844 0.2018  0.0340  631 HIS D O   
10925 C CB  . HIS D 631 ? 1.3707 0.5320 1.2226 -0.1400 0.1779  -0.0247 631 HIS D CB  
10926 C CG  . HIS D 631 ? 1.4030 0.5263 1.2445 -0.1724 0.1636  -0.0560 631 HIS D CG  
10927 N ND1 . HIS D 631 ? 1.4177 0.5252 1.2853 -0.2088 0.1586  -0.0607 631 HIS D ND1 
10928 C CD2 . HIS D 631 ? 1.4283 0.5349 1.2357 -0.1716 0.1492  -0.0831 631 HIS D CD2 
10929 C CE1 . HIS D 631 ? 1.4529 0.5370 1.3048 -0.2300 0.1375  -0.0902 631 HIS D CE1 
10930 N NE2 . HIS D 631 ? 1.4592 0.5338 1.2675 -0.2088 0.1334  -0.1053 631 HIS D NE2 
10931 N N   . ASN D 632 ? 1.4076 0.4992 1.2187 -0.0568 0.2296  0.0437  632 ASN D N   
10932 C CA  . ASN D 632 ? 1.3949 0.5025 1.2045 -0.0308 0.2372  0.0766  632 ASN D CA  
10933 C C   . ASN D 632 ? 1.4457 0.5059 1.2403 -0.0230 0.2518  0.0917  632 ASN D C   
10934 O O   . ASN D 632 ? 1.4943 0.5146 1.2872 -0.0441 0.2565  0.0774  632 ASN D O   
10935 C CB  . ASN D 632 ? 1.3800 0.5206 1.1843 0.0082  0.2295  0.0844  632 ASN D CB  
10936 C CG  . ASN D 632 ? 1.3359 0.5606 1.1642 0.0017  0.2077  0.0768  632 ASN D CG  
10937 O OD1 . ASN D 632 ? 1.3124 0.5783 1.1508 0.0018  0.2016  0.0928  632 ASN D OD1 
10938 N ND2 . ASN D 632 ? 1.3299 0.5746 1.1619 -0.0028 0.1972  0.0526  632 ASN D ND2 
10939 N N   . ASN D 633 ? 1.5442 0.6071 1.3265 0.0068  0.2569  0.1209  633 ASN D N   
10940 C CA  . ASN D 633 ? 1.6097 0.6280 1.3745 0.0180  0.2703  0.1390  633 ASN D CA  
10941 C C   . ASN D 633 ? 1.6336 0.6385 1.3827 0.0623  0.2704  0.1519  633 ASN D C   
10942 O O   . ASN D 633 ? 1.6758 0.6609 1.4099 0.0823  0.2761  0.1766  633 ASN D O   
10943 C CB  . ASN D 633 ? 1.6131 0.6421 1.3737 0.0125  0.2767  0.1651  633 ASN D CB  
10944 C CG  . ASN D 633 ? 1.6886 0.6677 1.4397 0.0009  0.2943  0.1752  633 ASN D CG  
10945 O OD1 . ASN D 633 ? 1.7328 0.6722 1.4880 -0.0149 0.3000  0.1585  633 ASN D OD1 
10946 N ND2 . ASN D 633 ? 1.7095 0.6880 1.4439 0.0089  0.3028  0.2030  633 ASN D ND2 
10947 N N   . LEU D 634 ? 1.5694 0.5872 1.3238 0.0787  0.2644  0.1367  634 LEU D N   
10948 C CA  . LEU D 634 ? 1.5898 0.6037 1.3407 0.1217  0.2658  0.1495  634 LEU D CA  
10949 C C   . LEU D 634 ? 1.6745 0.6270 1.4086 0.1296  0.2818  0.1512  634 LEU D C   
10950 O O   . LEU D 634 ? 1.7152 0.6254 1.4402 0.1037  0.2908  0.1297  634 LEU D O   
10951 C CB  . LEU D 634 ? 1.5556 0.5932 1.3179 0.1350  0.2623  0.1306  634 LEU D CB  
10952 C CG  . LEU D 634 ? 1.4822 0.5790 1.2626 0.1307  0.2469  0.1293  634 LEU D CG  
10953 C CD1 . LEU D 634 ? 1.4699 0.5687 1.2506 0.1079  0.2464  0.0965  634 LEU D CD1 
10954 C CD2 . LEU D 634 ? 1.4607 0.5981 1.2598 0.1714  0.2387  0.1495  634 LEU D CD2 
10955 N N   . SER D 635 ? 1.6616 0.6092 1.3926 0.1655  0.2830  0.1771  635 SER D N   
10956 C CA  . SER D 635 ? 1.7463 0.6354 1.4617 0.1782  0.2985  0.1833  635 SER D CA  
10957 C C   . SER D 635 ? 1.7620 0.6576 1.4879 0.2223  0.3006  0.1908  635 SER D C   
10958 O O   . SER D 635 ? 1.7061 0.6540 1.4545 0.2412  0.2899  0.1921  635 SER D O   
10959 C CB  . SER D 635 ? 1.7858 0.6556 1.4862 0.1778  0.3002  0.2121  635 SER D CB  
10960 O OG  . SER D 635 ? 1.7711 0.6757 1.4749 0.2121  0.2858  0.2415  635 SER D OG  
10961 N N   . GLY D 636 ? 1.8002 0.6433 1.5136 0.2390  0.3155  0.1969  636 GLY D N   
10962 C CA  . GLY D 636 ? 1.8257 0.6710 1.5526 0.2805  0.3218  0.2034  636 GLY D CA  
10963 C C   . GLY D 636 ? 1.8356 0.6641 1.5594 0.2786  0.3367  0.1711  636 GLY D C   
10964 O O   . GLY D 636 ? 1.8365 0.6406 1.5418 0.2439  0.3404  0.1423  636 GLY D O   
10965 N N   . GLN D 637 ? 1.8479 0.6911 1.5902 0.3169  0.3447  0.1766  637 GLN D N   
10966 C CA  . GLN D 637 ? 1.8709 0.6952 1.6051 0.3222  0.3634  0.1490  637 GLN D CA  
10967 C C   . GLN D 637 ? 1.7910 0.6833 1.5521 0.3287  0.3559  0.1423  637 GLN D C   
10968 O O   . GLN D 637 ? 1.7314 0.6884 1.5299 0.3462  0.3390  0.1656  637 GLN D O   
10969 C CB  . GLN D 637 ? 1.9481 0.7395 1.6851 0.3611  0.3843  0.1587  637 GLN D CB  
10970 C CG  . GLN D 637 ? 2.0313 0.7571 1.7457 0.3607  0.3917  0.1711  637 GLN D CG  
10971 C CD  . GLN D 637 ? 2.1269 0.7935 1.8264 0.3857  0.4190  0.1643  637 GLN D CD  
10972 O OE1 . GLN D 637 ? 2.1320 0.8091 1.8383 0.4056  0.4340  0.1517  637 GLN D OE1 
10973 N NE2 . GLN D 637 ? 2.2085 0.8107 1.8863 0.3853  0.4278  0.1733  637 GLN D NE2 
10974 N N   . ILE D 638 ? 1.8481 0.7236 1.5877 0.3134  0.3669  0.1102  638 ILE D N   
10975 C CA  . ILE D 638 ? 1.7850 0.7176 1.5458 0.3212  0.3652  0.1026  638 ILE D CA  
10976 C C   . ILE D 638 ? 1.7920 0.7598 1.5925 0.3681  0.3771  0.1240  638 ILE D C   
10977 O O   . ILE D 638 ? 1.8675 0.7924 1.6556 0.3892  0.4009  0.1208  638 ILE D O   
10978 C CB  . ILE D 638 ? 1.8086 0.7065 1.5289 0.2989  0.3767  0.0644  638 ILE D CB  
10979 C CG1 . ILE D 638 ? 1.8219 0.6770 1.5069 0.2516  0.3638  0.0432  638 ILE D CG1 
10980 C CG2 . ILE D 638 ? 1.7373 0.6961 1.4772 0.3019  0.3724  0.0587  638 ILE D CG2 
10981 C CD1 . ILE D 638 ? 1.8730 0.6784 1.5101 0.2291  0.3715  0.0048  638 ILE D CD1 
10982 N N   . PRO D 639 ? 1.7432 0.7887 1.5942 0.3848  0.3607  0.1464  639 PRO D N   
10983 C CA  . PRO D 639 ? 1.7487 0.8370 1.6503 0.4278  0.3667  0.1711  639 PRO D CA  
10984 C C   . PRO D 639 ? 1.7872 0.8649 1.6874 0.4464  0.3993  0.1553  639 PRO D C   
10985 O O   . PRO D 639 ? 1.7545 0.8505 1.6480 0.4350  0.4064  0.1361  639 PRO D O   
10986 C CB  . PRO D 639 ? 1.6558 0.8325 1.6089 0.4303  0.3386  0.1901  639 PRO D CB  
10987 C CG  . PRO D 639 ? 1.6042 0.7811 1.5294 0.3922  0.3281  0.1687  639 PRO D CG  
10988 C CD  . PRO D 639 ? 1.6568 0.7554 1.5237 0.3638  0.3337  0.1508  639 PRO D CD  
10989 N N   . PRO D 640 ? 1.7863 0.8309 1.6890 0.4757  0.4214  0.1633  640 PRO D N   
10990 C CA  . PRO D 640 ? 1.8358 0.8643 1.7318 0.4953  0.4571  0.1491  640 PRO D CA  
10991 C C   . PRO D 640 ? 1.7783 0.8889 1.7318 0.5141  0.4620  0.1595  640 PRO D C   
10992 O O   . PRO D 640 ? 1.8179 0.9171 1.7624 0.5277  0.4941  0.1477  640 PRO D O   
10993 C CB  . PRO D 640 ? 1.9243 0.9107 1.8241 0.5270  0.4754  0.1640  640 PRO D CB  
10994 C CG  . PRO D 640 ? 1.9441 0.8857 1.8160 0.5088  0.4557  0.1693  640 PRO D CG  
10995 C CD  . PRO D 640 ? 1.8475 0.8494 1.7431 0.4878  0.4187  0.1810  640 PRO D CD  
10996 N N   . SER D 641 ? 1.7989 0.9897 1.8093 0.5142  0.4320  0.1814  641 SER D N   
10997 C CA  . SER D 641 ? 1.7430 1.0138 1.8118 0.5268  0.4356  0.1903  641 SER D CA  
10998 C C   . SER D 641 ? 1.7177 0.9834 1.7507 0.5032  0.4486  0.1620  641 SER D C   
10999 O O   . SER D 641 ? 1.6878 1.0080 1.7601 0.5135  0.4612  0.1665  641 SER D O   
11000 C CB  . SER D 641 ? 1.6613 1.0154 1.7950 0.5275  0.3951  0.2180  641 SER D CB  
11001 O OG  . SER D 641 ? 1.6135 1.0488 1.8146 0.5401  0.3978  0.2296  641 SER D OG  
11002 N N   . PHE D 642 ? 1.7880 0.9899 1.7489 0.4713  0.4455  0.1340  642 PHE D N   
11003 C CA  . PHE D 642 ? 1.7624 0.9597 1.6860 0.4459  0.4494  0.1074  642 PHE D CA  
11004 C C   . PHE D 642 ? 1.8307 0.9906 1.7155 0.4563  0.4884  0.0876  642 PHE D C   
11005 O O   . PHE D 642 ? 1.8173 0.9754 1.6692 0.4390  0.4932  0.0673  642 PHE D O   
11006 C CB  . PHE D 642 ? 1.7626 0.9059 1.6260 0.4065  0.4292  0.0847  642 PHE D CB  
11007 C CG  . PHE D 642 ? 1.6826 0.8705 1.5766 0.3895  0.3925  0.1002  642 PHE D CG  
11008 C CD1 . PHE D 642 ? 1.6258 0.8891 1.5905 0.4100  0.3757  0.1325  642 PHE D CD1 
11009 C CD2 . PHE D 642 ? 1.6698 0.8244 1.5220 0.3519  0.3738  0.0827  642 PHE D CD2 
11010 C CE1 . PHE D 642 ? 1.5624 0.8614 1.5466 0.3946  0.3416  0.1464  642 PHE D CE1 
11011 C CE2 . PHE D 642 ? 1.6039 0.7961 1.4802 0.3371  0.3437  0.0979  642 PHE D CE2 
11012 C CZ  . PHE D 642 ? 1.5524 0.8140 1.4903 0.3592  0.3279  0.1295  642 PHE D CZ  
11013 N N   . LYS D 643 ? 1.7634 0.8907 1.6471 0.4847  0.5165  0.0935  643 LYS D N   
11014 C CA  . LYS D 643 ? 1.8357 0.9275 1.6809 0.4973  0.5562  0.0772  643 LYS D CA  
11015 C C   . LYS D 643 ? 1.7884 0.9541 1.6821 0.5103  0.5703  0.0893  643 LYS D C   
11016 O O   . LYS D 643 ? 1.8355 0.9750 1.6861 0.5118  0.5994  0.0728  643 LYS D O   
11017 C CB  . LYS D 643 ? 1.9279 0.9794 1.7751 0.5304  0.5859  0.0865  643 LYS D CB  
11018 C CG  . LYS D 643 ? 2.0182 0.9718 1.7968 0.5215  0.5901  0.0672  643 LYS D CG  
11019 C CD  . LYS D 643 ? 2.0027 0.9606 1.8157 0.5254  0.5661  0.0885  643 LYS D CD  
11020 C CE  . LYS D 643 ? 2.0504 0.9249 1.7942 0.4944  0.5539  0.0649  643 LYS D CE  
11021 N NZ  . LYS D 643 ? 2.0015 0.8904 1.7683 0.4792  0.5194  0.0808  643 LYS D NZ  
11022 N N   . ASP D 644 ? 1.8002 1.0557 1.7811 0.5188  0.5498  0.1183  644 ASP D N   
11023 C CA  . ASP D 644 ? 1.7544 1.0889 1.7983 0.5311  0.5617  0.1349  644 ASP D CA  
11024 C C   . ASP D 644 ? 1.6838 1.0493 1.7163 0.5028  0.5463  0.1229  644 ASP D C   
11025 O O   . ASP D 644 ? 1.6426 1.0741 1.7268 0.5085  0.5548  0.1364  644 ASP D O   
11026 C CB  . ASP D 644 ? 1.7039 1.1221 1.8520 0.5523  0.5429  0.1722  644 ASP D CB  
11027 C CG  . ASP D 644 ? 1.7729 1.1613 1.9339 0.5810  0.5531  0.1861  644 ASP D CG  
11028 O OD1 . ASP D 644 ? 1.8651 1.1833 1.9734 0.5936  0.5890  0.1717  644 ASP D OD1 
11029 O OD2 . ASP D 644 ? 1.7406 1.1734 1.9615 0.5914  0.5242  0.2113  644 ASP D OD2 
11030 N N   . MET D 645 ? 1.6881 1.0075 1.6567 0.4720  0.5243  0.0987  645 MET D N   
11031 C CA  . MET D 645 ? 1.6242 0.9691 1.5799 0.4453  0.5074  0.0869  645 MET D CA  
11032 C C   . MET D 645 ? 1.6825 0.9818 1.5661 0.4393  0.5369  0.0615  645 MET D C   
11033 O O   . MET D 645 ? 1.7309 0.9569 1.5288 0.4177  0.5333  0.0312  645 MET D O   
11034 C CB  . MET D 645 ? 1.5937 0.9090 1.5150 0.4151  0.4712  0.0733  645 MET D CB  
11035 C CG  . MET D 645 ? 1.5579 0.8997 1.5301 0.4205  0.4434  0.0972  645 MET D CG  
11036 S SD  . MET D 645 ? 1.4723 0.8396 1.4495 0.3878  0.3988  0.0970  645 MET D SD  
11037 C CE  . MET D 645 ? 1.4245 0.8603 1.4866 0.4078  0.3719  0.1372  645 MET D CE  
11038 N N   . LEU D 646 ? 1.5402 0.8839 1.4587 0.4568  0.5645  0.0749  646 LEU D N   
11039 C CA  . LEU D 646 ? 1.6060 0.9065 1.4536 0.4549  0.5957  0.0551  646 LEU D CA  
11040 C C   . LEU D 646 ? 1.5685 0.8679 1.3701 0.4249  0.5773  0.0357  646 LEU D C   
11041 O O   . LEU D 646 ? 1.6355 0.8762 1.3497 0.4150  0.5912  0.0111  646 LEU D O   
11042 C CB  . LEU D 646 ? 1.6192 0.9692 1.5226 0.4821  0.6327  0.0792  646 LEU D CB  
11043 C CG  . LEU D 646 ? 1.6589 1.0189 1.6179 0.5151  0.6536  0.1016  646 LEU D CG  
11044 C CD1 . LEU D 646 ? 1.5746 1.0404 1.6578 0.5270  0.6395  0.1381  646 LEU D CD1 
11045 C CD2 . LEU D 646 ? 1.7626 1.0784 1.6811 0.5369  0.7045  0.0981  646 LEU D CD2 
11046 N N   . ALA D 647 ? 1.5415 0.9028 1.3975 0.4106  0.5452  0.0465  647 ALA D N   
11047 C CA  . ALA D 647 ? 1.5043 0.8681 1.3226 0.3837  0.5274  0.0298  647 ALA D CA  
11048 C C   . ALA D 647 ? 1.5282 0.8234 1.2703 0.3547  0.4990  -0.0007 647 ALA D C   
11049 O O   . ALA D 647 ? 1.5397 0.8149 1.2255 0.3315  0.4872  -0.0217 647 ALA D O   
11050 C CB  . ALA D 647 ? 1.4046 0.8613 1.3138 0.3802  0.5051  0.0538  647 ALA D CB  
11051 N N   . LEU D 648 ? 1.5684 0.8277 1.3084 0.3540  0.4871  -0.0025 648 LEU D N   
11052 C CA  . LEU D 648 ? 1.5806 0.7862 1.2679 0.3224  0.4565  -0.0262 648 LEU D CA  
11053 C C   . LEU D 648 ? 1.6676 0.7943 1.2515 0.3037  0.4615  -0.0614 648 LEU D C   
11054 O O   . LEU D 648 ? 1.7522 0.8333 1.2960 0.3190  0.4889  -0.0684 648 LEU D O   
11055 C CB  . LEU D 648 ? 1.5915 0.7754 1.3012 0.3276  0.4480  -0.0166 648 LEU D CB  
11056 C CG  . LEU D 648 ? 1.5585 0.7301 1.2684 0.2988  0.4115  -0.0207 648 LEU D CG  
11057 C CD1 . LEU D 648 ? 1.5870 0.7337 1.3142 0.3088  0.4106  -0.0078 648 LEU D CD1 
11058 C CD2 . LEU D 648 ? 1.5963 0.7114 1.2302 0.2606  0.3938  -0.0552 648 LEU D CD2 
11059 N N   . THR D 649 ? 1.6205 0.7309 1.1610 0.2700  0.4324  -0.0832 649 THR D N   
11060 C CA  . THR D 649 ? 1.6999 0.7392 1.1432 0.2462  0.4247  -0.1171 649 THR D CA  
11061 C C   . THR D 649 ? 1.7094 0.7080 1.1247 0.2072  0.3861  -0.1383 649 THR D C   
11062 O O   . THR D 649 ? 1.7903 0.7239 1.1348 0.1887  0.3782  -0.1646 649 THR D O   
11063 C CB  . THR D 649 ? 1.7008 0.7566 1.1051 0.2391  0.4242  -0.1259 649 THR D CB  
11064 O OG1 . THR D 649 ? 1.6498 0.7787 1.1036 0.2133  0.3857  -0.1155 649 THR D OG1 
11065 C CG2 . THR D 649 ? 1.6973 0.7916 1.1292 0.2744  0.4657  -0.1040 649 THR D CG2 
11066 N N   . HIS D 650 ? 1.6500 0.6920 1.1237 0.1916  0.3595  -0.1251 650 HIS D N   
11067 C CA  . HIS D 650 ? 1.6551 0.6753 1.1167 0.1503  0.3219  -0.1402 650 HIS D CA  
11068 C C   . HIS D 650 ? 1.6114 0.6548 1.1384 0.1521  0.3154  -0.1170 650 HIS D C   
11069 O O   . HIS D 650 ? 1.5532 0.6771 1.1491 0.1608  0.3076  -0.0891 650 HIS D O   
11070 C CB  . HIS D 650 ? 1.6340 0.7124 1.1019 0.1153  0.2819  -0.1447 650 HIS D CB  
11071 C CG  . HIS D 650 ? 1.6844 0.7315 1.0766 0.1078  0.2800  -0.1686 650 HIS D CG  
11072 N ND1 . HIS D 650 ? 1.7052 0.7513 1.0707 0.1382  0.3129  -0.1651 650 HIS D ND1 
11073 C CD2 . HIS D 650 ? 1.7187 0.7343 1.0552 0.0735  0.2483  -0.1951 650 HIS D CD2 
11074 C CE1 . HIS D 650 ? 1.7551 0.7646 1.0423 0.1239  0.3029  -0.1886 650 HIS D CE1 
11075 N NE2 . HIS D 650 ? 1.7640 0.7555 1.0326 0.0846  0.2609  -0.2074 650 HIS D NE2 
11076 N N   . VAL D 651 ? 1.6316 0.6082 1.1359 0.1414  0.3154  -0.1274 651 VAL D N   
11077 C CA  . VAL D 651 ? 1.5999 0.5864 1.1534 0.1385  0.3081  -0.1068 651 VAL D CA  
11078 C C   . VAL D 651 ? 1.6183 0.5707 1.1533 0.0931  0.2807  -0.1247 651 VAL D C   
11079 O O   . VAL D 651 ? 1.6818 0.5862 1.1645 0.0713  0.2722  -0.1528 651 VAL D O   
11080 C CB  . VAL D 651 ? 1.6366 0.6003 1.2029 0.1710  0.3341  -0.0905 651 VAL D CB  
11081 C CG1 . VAL D 651 ? 1.5838 0.5819 1.2100 0.1798  0.3277  -0.0589 651 VAL D CG1 
11082 C CG2 . VAL D 651 ? 1.6528 0.6316 1.2204 0.2108  0.3648  -0.0831 651 VAL D CG2 
11083 N N   . ASP D 652 ? 1.5900 0.5728 1.1719 0.0784  0.2656  -0.1064 652 ASP D N   
11084 C CA  . ASP D 652 ? 1.6014 0.5556 1.1824 0.0391  0.2466  -0.1155 652 ASP D CA  
11085 C C   . ASP D 652 ? 1.5706 0.5408 1.1977 0.0472  0.2514  -0.0848 652 ASP D C   
11086 O O   . ASP D 652 ? 1.5187 0.5552 1.1891 0.0542  0.2436  -0.0616 652 ASP D O   
11087 C CB  . ASP D 652 ? 1.5799 0.5765 1.1700 -0.0014 0.2127  -0.1283 652 ASP D CB  
11088 C CG  . ASP D 652 ? 1.6076 0.5566 1.1847 -0.0444 0.1952  -0.1480 652 ASP D CG  
11089 O OD1 . ASP D 652 ? 1.6335 0.5534 1.2228 -0.0461 0.2040  -0.1391 652 ASP D OD1 
11090 O OD2 . ASP D 652 ? 1.6140 0.5722 1.1780 -0.0762 0.1682  -0.1691 652 ASP D OD2 
11091 N N   . VAL D 653 ? 1.5894 0.5129 1.2084 0.0459  0.2600  -0.0830 653 VAL D N   
11092 C CA  . VAL D 653 ? 1.5761 0.5059 1.2284 0.0534  0.2651  -0.0537 653 VAL D CA  
11093 C C   . VAL D 653 ? 1.6178 0.5105 1.2675 0.0149  0.2556  -0.0624 653 VAL D C   
11094 O O   . VAL D 653 ? 1.6393 0.5153 1.3024 0.0184  0.2638  -0.0428 653 VAL D O   
11095 C CB  . VAL D 653 ? 1.6123 0.5250 1.2647 0.0981  0.2890  -0.0353 653 VAL D CB  
11096 C CG1 . VAL D 653 ? 1.5797 0.5192 1.2680 0.1131  0.2889  0.0003  653 VAL D CG1 
11097 C CG2 . VAL D 653 ? 1.5929 0.5337 1.2451 0.1325  0.3011  -0.0351 653 VAL D CG2 
11098 N N   . SER D 654 ? 1.6766 0.5585 1.3111 -0.0224 0.2370  -0.0909 654 SER D N   
11099 C CA  . SER D 654 ? 1.7193 0.5711 1.3597 -0.0620 0.2252  -0.1010 654 SER D CA  
11100 C C   . SER D 654 ? 1.6680 0.5568 1.3564 -0.0784 0.2219  -0.0752 654 SER D C   
11101 O O   . SER D 654 ? 1.5939 0.5367 1.3071 -0.0698 0.2201  -0.0575 654 SER D O   
11102 C CB  . SER D 654 ? 1.7349 0.5840 1.3590 -0.0989 0.1987  -0.1342 654 SER D CB  
11103 O OG  . SER D 654 ? 1.6552 0.5661 1.3029 -0.1112 0.1816  -0.1326 654 SER D OG  
11104 N N   . HIS D 655 ? 1.7039 0.5605 1.4034 -0.1019 0.2226  -0.0730 655 HIS D N   
11105 C CA  . HIS D 655 ? 1.6713 0.5566 1.4132 -0.1219 0.2225  -0.0500 655 HIS D CA  
11106 C C   . HIS D 655 ? 1.6315 0.5420 1.3815 -0.0867 0.2395  -0.0149 655 HIS D C   
11107 O O   . HIS D 655 ? 1.5620 0.5262 1.3357 -0.0867 0.2355  0.0003  655 HIS D O   
11108 C CB  . HIS D 655 ? 1.6131 0.5521 1.3895 -0.1581 0.1999  -0.0595 655 HIS D CB  
11109 C CG  . HIS D 655 ? 1.6578 0.5763 1.4340 -0.1966 0.1770  -0.0905 655 HIS D CG  
11110 N ND1 . HIS D 655 ? 1.6968 0.6008 1.5039 -0.2320 0.1705  -0.0909 655 HIS D ND1 
11111 C CD2 . HIS D 655 ? 1.6767 0.5858 1.4240 -0.2046 0.1574  -0.1214 655 HIS D CD2 
11112 C CE1 . HIS D 655 ? 1.7355 0.6246 1.5377 -0.2610 0.1445  -0.1212 655 HIS D CE1 
11113 N NE2 . HIS D 655 ? 1.7261 0.6166 1.4878 -0.2446 0.1358  -0.1406 655 HIS D NE2 
11114 N N   . ASN D 656 ? 1.6828 0.5523 1.4112 -0.0559 0.2572  -0.0023 656 ASN D N   
11115 C CA  . ASN D 656 ? 1.6613 0.5487 1.3936 -0.0201 0.2693  0.0314  656 ASN D CA  
11116 C C   . ASN D 656 ? 1.7381 0.5714 1.4584 -0.0116 0.2855  0.0465  656 ASN D C   
11117 O O   . ASN D 656 ? 1.7976 0.5866 1.5142 -0.0390 0.2873  0.0334  656 ASN D O   
11118 C CB  . ASN D 656 ? 1.6320 0.5409 1.3546 0.0206  0.2712  0.0335  656 ASN D CB  
11119 C CG  . ASN D 656 ? 1.5454 0.5206 1.2896 0.0267  0.2602  0.0460  656 ASN D CG  
11120 O OD1 . ASN D 656 ? 1.5219 0.5215 1.2765 0.0434  0.2611  0.0747  656 ASN D OD1 
11121 N ND2 . ASN D 656 ? 1.5067 0.5083 1.2535 0.0135  0.2487  0.0246  656 ASN D ND2 
11122 N N   . ASN D 657 ? 1.7317 0.5694 1.4475 0.0257  0.2950  0.0755  657 ASN D N   
11123 C CA  . ASN D 657 ? 1.8042 0.5936 1.5074 0.0384  0.3101  0.0950  657 ASN D CA  
11124 C C   . ASN D 657 ? 1.8403 0.6085 1.5281 0.0839  0.3197  0.1022  657 ASN D C   
11125 O O   . ASN D 657 ? 1.8793 0.6289 1.5611 0.1089  0.3285  0.1283  657 ASN D O   
11126 C CB  . ASN D 657 ? 1.7861 0.5987 1.4974 0.0392  0.3117  0.1276  657 ASN D CB  
11127 C CG  . ASN D 657 ? 1.8683 0.6264 1.5651 0.0423  0.3275  0.1465  657 ASN D CG  
11128 O OD1 . ASN D 657 ? 1.9318 0.6381 1.6237 0.0211  0.3356  0.1319  657 ASN D OD1 
11129 N ND2 . ASN D 657 ? 1.8733 0.6408 1.5612 0.0687  0.3304  0.1793  657 ASN D ND2 
11130 N N   . LEU D 658 ? 1.8307 0.6022 1.5124 0.0956  0.3190  0.0799  658 LEU D N   
11131 C CA  . LEU D 658 ? 1.8587 0.6207 1.5341 0.1403  0.3304  0.0871  658 LEU D CA  
11132 C C   . LEU D 658 ? 1.9608 0.6464 1.6107 0.1439  0.3480  0.0772  658 LEU D C   
11133 O O   . LEU D 658 ? 2.0101 0.6492 1.6470 0.1103  0.3493  0.0632  658 LEU D O   
11134 C CB  . LEU D 658 ? 1.8142 0.6109 1.4930 0.1529  0.3274  0.0689  658 LEU D CB  
11135 C CG  . LEU D 658 ? 1.7170 0.5877 1.4213 0.1538  0.3110  0.0766  658 LEU D CG  
11136 C CD1 . LEU D 658 ? 1.6950 0.5884 1.4005 0.1736  0.3149  0.0614  658 LEU D CD1 
11137 C CD2 . LEU D 658 ? 1.6870 0.5955 1.4131 0.1802  0.3046  0.1136  658 LEU D CD2 
11138 N N   . GLN D 659 ? 1.9189 0.5928 1.5654 0.1856  0.3617  0.0854  659 GLN D N   
11139 C CA  . GLN D 659 ? 2.0209 0.6215 1.6417 0.1960  0.3812  0.0765  659 GLN D CA  
11140 C C   . GLN D 659 ? 2.0352 0.6432 1.6570 0.2391  0.3958  0.0754  659 GLN D C   
11141 O O   . GLN D 659 ? 1.9660 0.6386 1.6148 0.2617  0.3897  0.0867  659 GLN D O   
11142 C CB  . GLN D 659 ? 2.0781 0.6417 1.6979 0.2035  0.3884  0.1041  659 GLN D CB  
11143 C CG  . GLN D 659 ? 2.0545 0.6581 1.6968 0.2455  0.3861  0.1421  659 GLN D CG  
11144 C CD  . GLN D 659 ? 2.0983 0.6739 1.7353 0.2443  0.3873  0.1707  659 GLN D CD  
11145 O OE1 . GLN D 659 ? 2.0885 0.6591 1.7210 0.2088  0.3816  0.1713  659 GLN D OE1 
11146 N NE2 . GLN D 659 ? 2.1509 0.7086 1.7893 0.2835  0.3955  0.1957  659 GLN D NE2 
11147 N N   . GLY D 660 ? 2.1307 0.6719 1.7245 0.2497  0.4160  0.0614  660 GLY D N   
11148 C CA  . GLY D 660 ? 2.1604 0.7023 1.7565 0.2935  0.4358  0.0639  660 GLY D CA  
11149 C C   . GLY D 660 ? 2.1679 0.7033 1.7384 0.2890  0.4442  0.0302  660 GLY D C   
11150 O O   . GLY D 660 ? 2.1334 0.6769 1.6885 0.2530  0.4291  0.0059  660 GLY D O   
11151 N N   . PRO D 661 ? 2.1924 0.7126 1.7569 0.3263  0.4689  0.0292  661 PRO D N   
11152 C CA  . PRO D 661 ? 2.2135 0.7219 1.7455 0.3255  0.4814  -0.0014 661 PRO D CA  
11153 C C   . PRO D 661 ? 2.1109 0.7015 1.6702 0.3272  0.4703  0.0004  661 PRO D C   
11154 O O   . PRO D 661 ? 2.0386 0.6990 1.6504 0.3503  0.4640  0.0297  661 PRO D O   
11155 C CB  . PRO D 661 ? 2.2956 0.7716 1.8227 0.3705  0.5148  0.0055  661 PRO D CB  
11156 C CG  . PRO D 661 ? 2.2698 0.7840 1.8508 0.4026  0.5132  0.0468  661 PRO D CG  
11157 C CD  . PRO D 661 ? 2.2429 0.7518 1.8277 0.3709  0.4879  0.0565  661 PRO D CD  
11158 N N   . ILE D 662 ? 2.1584 0.7386 1.6803 0.3025  0.4663  -0.0315 662 ILE D N   
11159 C CA  . ILE D 662 ? 2.0686 0.7187 1.6089 0.2996  0.4558  -0.0333 662 ILE D CA  
11160 C C   . ILE D 662 ? 2.0613 0.7515 1.6279 0.3448  0.4810  -0.0183 662 ILE D C   
11161 O O   . ILE D 662 ? 2.1417 0.7925 1.6961 0.3736  0.5089  -0.0165 662 ILE D O   
11162 C CB  . ILE D 662 ? 2.0837 0.7058 1.5714 0.2607  0.4433  -0.0713 662 ILE D CB  
11163 C CG1 . ILE D 662 ? 2.1987 0.7450 1.6218 0.2656  0.4656  -0.0998 662 ILE D CG1 
11164 C CG2 . ILE D 662 ? 2.0697 0.6748 1.5530 0.2139  0.4140  -0.0807 662 ILE D CG2 
11165 C CD1 . ILE D 662 ? 2.2152 0.7781 1.6292 0.3016  0.4946  -0.0996 662 ILE D CD1 
11166 N N   . PRO D 663 ? 2.0524 0.8211 1.6592 0.3525  0.4731  -0.0062 663 PRO D N   
11167 C CA  . PRO D 663 ? 2.0484 0.8579 1.6830 0.3910  0.4984  0.0058  663 PRO D CA  
11168 C C   . PRO D 663 ? 2.1045 0.8778 1.6814 0.3874  0.5196  -0.0239 663 PRO D C   
11169 O O   . PRO D 663 ? 2.1035 0.8541 1.6326 0.3530  0.5044  -0.0514 663 PRO D O   
11170 C CB  . PRO D 663 ? 1.9312 0.8359 1.6285 0.3931  0.4780  0.0275  663 PRO D CB  
11171 C CG  . PRO D 663 ? 1.8853 0.7964 1.5951 0.3685  0.4461  0.0369  663 PRO D CG  
11172 C CD  . PRO D 663 ? 1.9506 0.7805 1.5973 0.3342  0.4420  0.0089  663 PRO D CD  
11173 N N   . ASP D 664 ? 2.0607 0.8282 1.6410 0.4236  0.5546  -0.0173 664 ASP D N   
11174 C CA  . ASP D 664 ? 2.1252 0.8573 1.6476 0.4261  0.5800  -0.0414 664 ASP D CA  
11175 C C   . ASP D 664 ? 2.0483 0.8577 1.6043 0.4331  0.5830  -0.0321 664 ASP D C   
11176 O O   . ASP D 664 ? 2.0172 0.8870 1.6382 0.4661  0.6007  -0.0042 664 ASP D O   
11177 C CB  . ASP D 664 ? 2.2312 0.9152 1.7390 0.4620  0.6205  -0.0377 664 ASP D CB  
11178 C CG  . ASP D 664 ? 2.3121 0.9527 1.7526 0.4668  0.6501  -0.0614 664 ASP D CG  
11179 O OD1 . ASP D 664 ? 2.3031 0.9332 1.6926 0.4372  0.6352  -0.0859 664 ASP D OD1 
11180 O OD2 . ASP D 664 ? 2.3901 1.0059 1.8274 0.5011  0.6885  -0.0543 664 ASP D OD2 
11181 N N   . ASN D 665 ? 2.1203 0.9286 1.6349 0.4013  0.5648  -0.0548 665 ASN D N   
11182 C CA  . ASN D 665 ? 2.0716 0.9354 1.5985 0.4061  0.5725  -0.0515 665 ASN D CA  
11183 C C   . ASN D 665 ? 2.1160 0.9289 1.5537 0.3752  0.5639  -0.0874 665 ASN D C   
11184 O O   . ASN D 665 ? 2.1764 0.9194 1.5528 0.3489  0.5482  -0.1137 665 ASN D O   
11185 C CB  . ASN D 665 ? 1.9436 0.9002 1.5505 0.4026  0.5472  -0.0272 665 ASN D CB  
11186 C CG  . ASN D 665 ? 1.8933 0.8439 1.4910 0.3652  0.5062  -0.0376 665 ASN D CG  
11187 O OD1 . ASN D 665 ? 1.9327 0.8276 1.4628 0.3335  0.4922  -0.0677 665 ASN D OD1 
11188 N ND2 . ASN D 665 ? 1.8104 0.8194 1.4774 0.3679  0.4852  -0.0119 665 ASN D ND2 
11189 N N   . ALA D 666 ? 2.0902 0.9403 1.5227 0.3774  0.5722  -0.0874 666 ALA D N   
11190 C CA  . ALA D 666 ? 2.1378 0.9426 1.4822 0.3506  0.5626  -0.1193 666 ALA D CA  
11191 C C   . ALA D 666 ? 2.0963 0.8924 1.4217 0.3069  0.5153  -0.1385 666 ALA D C   
11192 O O   . ALA D 666 ? 2.1631 0.8982 1.4105 0.2791  0.4987  -0.1695 666 ALA D O   
11193 C CB  . ALA D 666 ? 2.1066 0.9610 1.4568 0.3616  0.5790  -0.1104 666 ALA D CB  
11194 N N   . ALA D 667 ? 2.0079 0.8644 1.4049 0.2997  0.4921  -0.1199 667 ALA D N   
11195 C CA  . ALA D 667 ? 1.9639 0.8193 1.3519 0.2585  0.4495  -0.1346 667 ALA D CA  
11196 C C   . ALA D 667 ? 2.0128 0.8096 1.3829 0.2379  0.4339  -0.1466 667 ALA D C   
11197 O O   . ALA D 667 ? 2.0402 0.7995 1.3655 0.2001  0.4056  -0.1724 667 ALA D O   
11198 C CB  . ALA D 667 ? 1.8421 0.7798 1.3099 0.2592  0.4330  -0.1094 667 ALA D CB  
11199 N N   . PHE D 668 ? 1.9854 0.7763 1.3935 0.2615  0.4505  -0.1270 668 PHE D N   
11200 C CA  . PHE D 668 ? 2.0407 0.7722 1.4315 0.2439  0.4402  -0.1363 668 PHE D CA  
11201 C C   . PHE D 668 ? 2.1657 0.8108 1.4745 0.2363  0.4509  -0.1672 668 PHE D C   
11202 O O   . PHE D 668 ? 2.2138 0.8065 1.4904 0.2040  0.4299  -0.1878 668 PHE D O   
11203 C CB  . PHE D 668 ? 2.0322 0.7769 1.4795 0.2744  0.4562  -0.1057 668 PHE D CB  
11204 C CG  . PHE D 668 ? 1.9313 0.7375 1.4467 0.2692  0.4336  -0.0796 668 PHE D CG  
11205 C CD1 . PHE D 668 ? 1.9090 0.7031 1.4225 0.2311  0.4036  -0.0866 668 PHE D CD1 
11206 C CD2 . PHE D 668 ? 1.8642 0.7411 1.4469 0.3018  0.4420  -0.0469 668 PHE D CD2 
11207 C CE1 . PHE D 668 ? 1.8254 0.6716 1.3947 0.2271  0.3853  -0.0615 668 PHE D CE1 
11208 C CE2 . PHE D 668 ? 1.7810 0.7104 1.4191 0.2973  0.4190  -0.0230 668 PHE D CE2 
11209 C CZ  . PHE D 668 ? 1.7637 0.6751 1.3909 0.2608  0.3922  -0.0302 668 PHE D CZ  
11210 N N   . ARG D 669 ? 2.1458 0.7749 1.4220 0.2651  0.4837  -0.1699 669 ARG D N   
11211 C CA  . ARG D 669 ? 2.2748 0.8178 1.4650 0.2600  0.4952  -0.1996 669 ARG D CA  
11212 C C   . ARG D 669 ? 2.2955 0.8136 1.4236 0.2171  0.4602  -0.2322 669 ARG D C   
11213 O O   . ARG D 669 ? 2.3758 0.8274 1.4539 0.1898  0.4427  -0.2584 669 ARG D O   
11214 C CB  . ARG D 669 ? 2.3298 0.8670 1.4990 0.3004  0.5398  -0.1927 669 ARG D CB  
11215 C CG  . ARG D 669 ? 2.3615 0.8930 1.5717 0.3415  0.5764  -0.1687 669 ARG D CG  
11216 C CD  . ARG D 669 ? 2.4486 0.9530 1.6218 0.3762  0.6221  -0.1688 669 ARG D CD  
11217 N NE  . ARG D 669 ? 2.3814 0.9597 1.5907 0.3944  0.6371  -0.1499 669 ARG D NE  
11218 C CZ  . ARG D 669 ? 2.3948 0.9712 1.5511 0.3828  0.6360  -0.1650 669 ARG D CZ  
11219 N NH1 . ARG D 669 ? 2.4730 0.9796 1.5360 0.3534  0.6174  -0.1999 669 ARG D NH1 
11220 N NH2 . ARG D 669 ? 2.3321 0.9787 1.5310 0.4007  0.6523  -0.1437 669 ARG D NH2 
11221 N N   . ASN D 670 ? 2.2748 0.8473 1.4081 0.2103  0.4477  -0.2303 670 ASN D N   
11222 C CA  . ASN D 670 ? 2.2903 0.8486 1.3681 0.1722  0.4119  -0.2580 670 ASN D CA  
11223 C C   . ASN D 670 ? 2.2128 0.8028 1.3316 0.1320  0.3670  -0.2602 670 ASN D C   
11224 O O   . ASN D 670 ? 2.2120 0.8035 1.2990 0.0987  0.3323  -0.2800 670 ASN D O   
11225 C CB  . ASN D 670 ? 2.2624 0.8607 1.3214 0.1852  0.4214  -0.2538 670 ASN D CB  
11226 C CG  . ASN D 670 ? 2.3810 0.9210 1.3559 0.2025  0.4490  -0.2688 670 ASN D CG  
11227 O OD1 . ASN D 670 ? 2.3960 0.9463 1.3811 0.2413  0.4925  -0.2508 670 ASN D OD1 
11228 N ND2 . ASN D 670 ? 2.4700 0.9494 1.3633 0.1734  0.4230  -0.3009 670 ASN D ND2 
11229 N N   . ALA D 671 ? 2.1669 0.7830 1.3553 0.1346  0.3666  -0.2389 671 ALA D N   
11230 C CA  . ALA D 671 ? 2.0977 0.7431 1.3277 0.0972  0.3286  -0.2381 671 ALA D CA  
11231 C C   . ALA D 671 ? 2.1754 0.7612 1.3660 0.0563  0.2999  -0.2671 671 ALA D C   
11232 O O   . ALA D 671 ? 2.2683 0.7892 1.4283 0.0614  0.3142  -0.2771 671 ALA D O   
11233 C CB  . ALA D 671 ? 2.0311 0.7102 1.3367 0.1116  0.3378  -0.2068 671 ALA D CB  
11234 N N   . PRO D 672 ? 2.1524 0.7599 1.3467 0.0152  0.2589  -0.2806 672 PRO D N   
11235 C CA  . PRO D 672 ? 2.2223 0.7831 1.3926 -0.0265 0.2274  -0.3068 672 PRO D CA  
11236 C C   . PRO D 672 ? 2.2125 0.7634 1.4370 -0.0399 0.2265  -0.2944 672 PRO D C   
11237 O O   . PRO D 672 ? 2.1351 0.7270 1.4180 -0.0232 0.2413  -0.2648 672 PRO D O   
11238 C CB  . PRO D 672 ? 2.1709 0.7783 1.3479 -0.0622 0.1840  -0.3173 672 PRO D CB  
11239 C CG  . PRO D 672 ? 2.0526 0.7338 1.2828 -0.0452 0.1925  -0.2899 672 PRO D CG  
11240 C CD  . PRO D 672 ? 2.0555 0.7328 1.2773 0.0056  0.2389  -0.2727 672 PRO D CD  
11241 N N   . PRO D 673 ? 2.1939 0.6900 1.4002 -0.0701 0.2091  -0.3155 673 PRO D N   
11242 C CA  . PRO D 673 ? 2.1975 0.6766 1.4519 -0.0813 0.2129  -0.3022 673 PRO D CA  
11243 C C   . PRO D 673 ? 2.0905 0.6365 1.4227 -0.1031 0.1952  -0.2797 673 PRO D C   
11244 O O   . PRO D 673 ? 2.0665 0.6158 1.4420 -0.0947 0.2113  -0.2551 673 PRO D O   
11245 C CB  . PRO D 673 ? 2.3085 0.7205 1.5270 -0.1161 0.1908  -0.3339 673 PRO D CB  
11246 C CG  . PRO D 673 ? 2.3882 0.7614 1.5232 -0.1045 0.1925  -0.3606 673 PRO D CG  
11247 C CD  . PRO D 673 ? 2.3012 0.7413 1.4377 -0.0913 0.1888  -0.3515 673 PRO D CD  
11248 N N   . ASP D 674 ? 2.1500 0.7488 1.4995 -0.1300 0.1632  -0.2862 674 ASP D N   
11249 C CA  . ASP D 674 ? 2.0553 0.7165 1.4789 -0.1520 0.1481  -0.2651 674 ASP D CA  
11250 C C   . ASP D 674 ? 1.9652 0.6747 1.4230 -0.1173 0.1738  -0.2317 674 ASP D C   
11251 O O   . ASP D 674 ? 1.9028 0.6499 1.4179 -0.1273 0.1723  -0.2087 674 ASP D O   
11252 C CB  . ASP D 674 ? 2.0176 0.7254 1.4536 -0.1878 0.1073  -0.2798 674 ASP D CB  
11253 C CG  . ASP D 674 ? 2.0352 0.7429 1.4088 -0.1739 0.1009  -0.2980 674 ASP D CG  
11254 O OD1 . ASP D 674 ? 2.0410 0.7347 1.3791 -0.1326 0.1331  -0.2911 674 ASP D OD1 
11255 O OD2 . ASP D 674 ? 2.0457 0.7695 1.4078 -0.2031 0.0640  -0.3174 674 ASP D OD2 
11256 N N   . ALA D 675 ? 1.9367 0.6479 1.3625 -0.0770 0.1972  -0.2278 675 ALA D N   
11257 C CA  . ALA D 675 ? 1.8550 0.6150 1.3175 -0.0429 0.2187  -0.1965 675 ALA D CA  
11258 C C   . ALA D 675 ? 1.8654 0.6083 1.3549 -0.0194 0.2439  -0.1707 675 ALA D C   
11259 O O   . ALA D 675 ? 1.8019 0.5867 1.3261 0.0085  0.2579  -0.1424 675 ALA D O   
11260 C CB  . ALA D 675 ? 1.8525 0.6219 1.2806 -0.0069 0.2370  -0.1990 675 ALA D CB  
11261 N N   . PHE D 676 ? 1.8437 0.5262 1.3176 -0.0298 0.2481  -0.1792 676 PHE D N   
11262 C CA  . PHE D 676 ? 1.8626 0.5244 1.3594 -0.0112 0.2690  -0.1544 676 PHE D CA  
11263 C C   . PHE D 676 ? 1.8779 0.5245 1.4028 -0.0495 0.2545  -0.1515 676 PHE D C   
11264 O O   . PHE D 676 ? 1.9175 0.5312 1.4510 -0.0398 0.2704  -0.1350 676 PHE D O   
11265 C CB  . PHE D 676 ? 1.9584 0.5557 1.4120 0.0187  0.2954  -0.1621 676 PHE D CB  
11266 C CG  . PHE D 676 ? 1.9509 0.5639 1.3826 0.0591  0.3158  -0.1614 676 PHE D CG  
11267 C CD1 . PHE D 676 ? 1.8960 0.5528 1.3640 0.0996  0.3353  -0.1300 676 PHE D CD1 
11268 C CD2 . PHE D 676 ? 2.0041 0.5891 1.3801 0.0565  0.3151  -0.1910 676 PHE D CD2 
11269 C CE1 . PHE D 676 ? 1.8898 0.5664 1.3480 0.1359  0.3555  -0.1273 676 PHE D CE1 
11270 C CE2 . PHE D 676 ? 2.0018 0.6018 1.3594 0.0938  0.3382  -0.1880 676 PHE D CE2 
11271 C CZ  . PHE D 676 ? 1.9423 0.5903 1.3456 0.1331  0.3593  -0.1558 676 PHE D CZ  
11272 N N   . GLU D 677 ? 1.9238 0.5959 1.4666 -0.0920 0.2252  -0.1651 677 GLU D N   
11273 C CA  . GLU D 677 ? 1.9470 0.6058 1.5211 -0.1324 0.2107  -0.1653 677 GLU D CA  
11274 C C   . GLU D 677 ? 1.8998 0.5863 1.5207 -0.1267 0.2241  -0.1285 677 GLU D C   
11275 O O   . GLU D 677 ? 1.8253 0.5611 1.4642 -0.1025 0.2327  -0.1052 677 GLU D O   
11276 C CB  . GLU D 677 ? 1.9142 0.6110 1.5095 -0.1760 0.1753  -0.1840 677 GLU D CB  
11277 C CG  . GLU D 677 ? 1.9962 0.6486 1.5532 -0.2012 0.1525  -0.2218 677 GLU D CG  
11278 C CD  . GLU D 677 ? 1.9603 0.6600 1.5482 -0.2434 0.1135  -0.2364 677 GLU D CD  
11279 O OE1 . GLU D 677 ? 1.8788 0.6401 1.5255 -0.2573 0.1071  -0.2159 677 GLU D OE1 
11280 O OE2 . GLU D 677 ? 2.0175 0.6938 1.5707 -0.2615 0.0890  -0.2678 677 GLU D OE2 
11281 N N   . GLY D 678 ? 1.9038 0.5558 1.5421 -0.1497 0.2253  -0.1234 678 GLY D N   
11282 C CA  . GLY D 678 ? 1.8664 0.5460 1.5491 -0.1567 0.2332  -0.0913 678 GLY D CA  
11283 C C   . GLY D 678 ? 1.8384 0.5298 1.5192 -0.1129 0.2581  -0.0578 678 GLY D C   
11284 O O   . GLY D 678 ? 1.7732 0.5141 1.4845 -0.1114 0.2599  -0.0324 678 GLY D O   
11285 N N   . ASN D 679 ? 1.9079 0.5566 1.5540 -0.0763 0.2762  -0.0569 679 ASN D N   
11286 C CA  . ASN D 679 ? 1.8983 0.5526 1.5462 -0.0350 0.2968  -0.0238 679 ASN D CA  
11287 C C   . ASN D 679 ? 1.9838 0.5765 1.6249 -0.0355 0.3122  -0.0113 679 ASN D C   
11288 O O   . ASN D 679 ? 2.0483 0.5945 1.6850 -0.0680 0.3077  -0.0291 679 ASN D O   
11289 C CB  . ASN D 679 ? 1.8928 0.5515 1.5178 0.0095  0.3073  -0.0259 679 ASN D CB  
11290 C CG  . ASN D 679 ? 1.7955 0.5262 1.4374 0.0198  0.2970  -0.0218 679 ASN D CG  
11291 O OD1 . ASN D 679 ? 1.7501 0.5186 1.4080 0.0520  0.3028  0.0047  679 ASN D OD1 
11292 N ND2 . ASN D 679 ? 1.7674 0.5169 1.4063 -0.0080 0.2793  -0.0478 679 ASN D ND2 
11293 N N   . LYS D 680 ? 1.9480 0.5405 1.5895 -0.0001 0.3285  0.0206  680 LYS D N   
11294 C CA  . LYS D 680 ? 2.0297 0.5647 1.6642 0.0002  0.3437  0.0362  680 LYS D CA  
11295 C C   . LYS D 680 ? 2.1257 0.5885 1.7265 0.0164  0.3569  0.0190  680 LYS D C   
11296 O O   . LYS D 680 ? 2.2023 0.6067 1.7921 -0.0117 0.3572  0.0014  680 LYS D O   
11297 C CB  . LYS D 680 ? 2.0093 0.5672 1.6516 0.0328  0.3537  0.0770  680 LYS D CB  
11298 C CG  . LYS D 680 ? 2.0973 0.5955 1.7285 0.0385  0.3708  0.0978  680 LYS D CG  
11299 C CD  . LYS D 680 ? 2.1565 0.6082 1.7920 -0.0084 0.3713  0.0836  680 LYS D CD  
11300 C CE  . LYS D 680 ? 2.1176 0.6051 1.7807 -0.0382 0.3681  0.1020  680 LYS D CE  
11301 N NZ  . LYS D 680 ? 2.1296 0.6092 1.8152 -0.0912 0.3570  0.0782  680 LYS D NZ  
11302 N N   . ASP D 681 ? 2.1212 0.5873 1.7074 0.0613  0.3681  0.0236  681 ASP D N   
11303 C CA  . ASP D 681 ? 2.2158 0.6138 1.7683 0.0790  0.3840  0.0062  681 ASP D CA  
11304 C C   . ASP D 681 ? 2.1872 0.6136 1.7301 0.1164  0.3903  -0.0010 681 ASP D C   
11305 O O   . ASP D 681 ? 2.1830 0.6249 1.7350 0.1602  0.4036  0.0231  681 ASP D O   
11306 C CB  . ASP D 681 ? 2.2911 0.6395 1.8386 0.1017  0.4031  0.0322  681 ASP D CB  
11307 C CG  . ASP D 681 ? 2.3971 0.6703 1.9101 0.1201  0.4220  0.0156  681 ASP D CG  
11308 O OD1 . ASP D 681 ? 2.4541 0.6785 1.9427 0.0901  0.4179  -0.0179 681 ASP D OD1 
11309 O OD2 . ASP D 681 ? 2.4275 0.6903 1.9382 0.1648  0.4397  0.0361  681 ASP D OD2 
11310 N N   . LEU D 682 ? 2.2034 0.6311 1.7269 0.0995  0.3816  -0.0343 682 LEU D N   
11311 C CA  . LEU D 682 ? 2.1862 0.6362 1.6972 0.1330  0.3913  -0.0423 682 LEU D CA  
11312 C C   . LEU D 682 ? 2.2983 0.6731 1.7670 0.1518  0.4138  -0.0602 682 LEU D C   
11313 O O   . LEU D 682 ? 2.3855 0.6924 1.8373 0.1418  0.4210  -0.0636 682 LEU D O   
11314 C CB  . LEU D 682 ? 2.1200 0.6144 1.6283 0.1091  0.3717  -0.0653 682 LEU D CB  
11315 C CG  . LEU D 682 ? 2.0066 0.5879 1.5521 0.1259  0.3639  -0.0444 682 LEU D CG  
11316 C CD1 . LEU D 682 ? 1.9580 0.5729 1.5422 0.1257  0.3575  -0.0101 682 LEU D CD1 
11317 C CD2 . LEU D 682 ? 1.9479 0.5665 1.4900 0.0964  0.3428  -0.0672 682 LEU D CD2 
11318 N N   . CYS D 683 ? 2.2795 0.6638 1.7301 0.1797  0.4271  -0.0711 683 CYS D N   
11319 C CA  . CYS D 683 ? 2.3886 0.7037 1.7955 0.2017  0.4526  -0.0878 683 CYS D CA  
11320 C C   . CYS D 683 ? 2.4533 0.7289 1.8700 0.2331  0.4747  -0.0627 683 CYS D C   
11321 O O   . CYS D 683 ? 2.4161 0.7350 1.8687 0.2728  0.4857  -0.0314 683 CYS D O   
11322 C CB  . CYS D 683 ? 2.4710 0.7163 1.8263 0.1610  0.4420  -0.1282 683 CYS D CB  
11323 S SG  . CYS D 683 ? 2.3977 0.6878 1.7492 0.1120  0.4048  -0.1549 683 CYS D SG  
11324 N N   . ASN E 26  ? 0.8948 0.6597 0.8331 0.0461  0.0008  0.0650  26  ASN E N   
11325 C CA  . ASN E 26  ? 0.9597 0.7157 0.8219 0.0638  0.0114  0.0805  26  ASN E CA  
11326 C C   . ASN E 26  ? 0.9678 0.7388 0.8171 0.0644  0.0485  0.1040  26  ASN E C   
11327 O O   . ASN E 26  ? 0.9302 0.7187 0.8352 0.0493  0.0626  0.1165  26  ASN E O   
11328 C CB  . ASN E 26  ? 0.9827 0.7392 0.8067 0.0696  -0.0028 0.0414  26  ASN E CB  
11329 C CG  . ASN E 26  ? 0.9512 0.7200 0.7945 0.0570  0.0098  0.0172  26  ASN E CG  
11330 O OD1 . ASN E 26  ? 0.8996 0.6851 0.7905 0.0447  0.0212  0.0226  26  ASN E OD1 
11331 N ND2 . ASN E 26  ? 0.9589 0.7177 0.7653 0.0596  0.0053  -0.0089 26  ASN E ND2 
11332 N N   . ALA E 27  ? 1.0071 0.7765 0.7861 0.0834  0.0627  0.1051  27  ALA E N   
11333 C CA  . ALA E 27  ? 1.0080 0.7997 0.7742 0.0912  0.1008  0.1258  27  ALA E CA  
11334 C C   . ALA E 27  ? 0.9701 0.7818 0.7842 0.0832  0.1112  0.1075  27  ALA E C   
11335 O O   . ALA E 27  ? 0.9414 0.7852 0.7991 0.0771  0.1340  0.1290  27  ALA E O   
11336 C CB  . ALA E 27  ? 1.0613 0.8473 0.7379 0.1186  0.1118  0.1181  27  ALA E CB  
11337 N N   . GLU E 28  ? 1.0328 0.8294 0.8422 0.0819  0.0938  0.0708  28  GLU E N   
11338 C CA  . GLU E 28  ? 1.0011 0.8127 0.8470 0.0770  0.1007  0.0594  28  GLU E CA  
11339 C C   . GLU E 28  ? 0.9425 0.7829 0.8618 0.0546  0.0944  0.0675  28  GLU E C   
11340 O O   . GLU E 28  ? 0.9168 0.7890 0.8733 0.0532  0.1068  0.0754  28  GLU E O   
11341 C CB  . GLU E 28  ? 1.0026 0.7864 0.8279 0.0746  0.0832  0.0258  28  GLU E CB  
11342 C CG  . GLU E 28  ? 1.0431 0.7932 0.8021 0.0952  0.0867  0.0080  28  GLU E CG  
11343 C CD  . GLU E 28  ? 1.0201 0.7383 0.7738 0.0872  0.0738  -0.0203 28  GLU E CD  
11344 O OE1 . GLU E 28  ? 0.9648 0.6901 0.7532 0.0630  0.0572  -0.0277 28  GLU E OE1 
11345 O OE2 . GLU E 28  ? 1.0554 0.7410 0.7724 0.1048  0.0815  -0.0351 28  GLU E OE2 
11346 N N   . GLY E 29  ? 0.9351 0.7670 0.8783 0.0396  0.0724  0.0617  29  GLY E N   
11347 C CA  . GLY E 29  ? 0.8854 0.7399 0.8967 0.0198  0.0637  0.0603  29  GLY E CA  
11348 C C   . GLY E 29  ? 0.8863 0.7592 0.9370 0.0123  0.0804  0.0927  29  GLY E C   
11349 O O   . GLY E 29  ? 0.8591 0.7649 0.9668 -0.0022 0.0808  0.0908  29  GLY E O   
11350 N N   . ASP E 30  ? 0.8867 0.7436 0.9082 0.0201  0.0942  0.1238  30  ASP E N   
11351 C CA  . ASP E 30  ? 0.8856 0.7638 0.9465 0.0082  0.1164  0.1622  30  ASP E CA  
11352 C C   . ASP E 30  ? 0.8777 0.8075 0.9541 0.0143  0.1445  0.1689  30  ASP E C   
11353 O O   . ASP E 30  ? 0.8548 0.8233 0.9980 -0.0041 0.1559  0.1862  30  ASP E O   
11354 C CB  . ASP E 30  ? 0.9249 0.7785 0.9378 0.0170  0.1290  0.2009  30  ASP E CB  
11355 C CG  . ASP E 30  ? 0.9332 0.7393 0.9530 0.0107  0.0999  0.2060  30  ASP E CG  
11356 O OD1 . ASP E 30  ? 0.9109 0.7066 1.0007 -0.0122 0.0908  0.2153  30  ASP E OD1 
11357 O OD2 . ASP E 30  ? 0.9655 0.7445 0.9246 0.0301  0.0837  0.1986  30  ASP E OD2 
11358 N N   . ALA E 31  ? 0.8656 0.7967 0.8877 0.0405  0.1540  0.1536  31  ALA E N   
11359 C CA  . ALA E 31  ? 0.8570 0.8352 0.8975 0.0546  0.1773  0.1562  31  ALA E CA  
11360 C C   . ALA E 31  ? 0.8211 0.8297 0.9241 0.0416  0.1592  0.1388  31  ALA E C   
11361 O O   . ALA E 31  ? 0.7980 0.8631 0.9615 0.0359  0.1702  0.1509  31  ALA E O   
11362 C CB  . ALA E 31  ? 0.8892 0.8458 0.8571 0.0887  0.1869  0.1387  31  ALA E CB  
11363 N N   . LEU E 32  ? 0.8937 0.8737 0.9832 0.0364  0.1310  0.1104  32  LEU E N   
11364 C CA  . LEU E 32  ? 0.8575 0.8702 0.9924 0.0256  0.1128  0.0943  32  LEU E CA  
11365 C C   . LEU E 32  ? 0.8262 0.8660 1.0329 -0.0043 0.0999  0.0941  32  LEU E C   
11366 O O   . LEU E 32  ? 0.7759 0.8640 1.0324 -0.0132 0.0892  0.0854  32  LEU E O   
11367 C CB  . LEU E 32  ? 0.8568 0.8375 0.9542 0.0256  0.0916  0.0675  32  LEU E CB  
11368 C CG  . LEU E 32  ? 0.8744 0.8244 0.9141 0.0494  0.0994  0.0645  32  LEU E CG  
11369 C CD1 . LEU E 32  ? 0.8610 0.7870 0.8772 0.0393  0.0804  0.0435  32  LEU E CD1 
11370 C CD2 . LEU E 32  ? 0.8585 0.8410 0.9131 0.0714  0.1124  0.0777  32  LEU E CD2 
11371 N N   . SER E 33  ? 0.8268 0.8337 1.0404 -0.0192 0.0974  0.1022  33  SER E N   
11372 C CA  . SER E 33  ? 0.7814 0.8017 1.0701 -0.0487 0.0868  0.1041  33  SER E CA  
11373 C C   . SER E 33  ? 0.7627 0.8329 1.1057 -0.0591 0.1111  0.1357  33  SER E C   
11374 O O   . SER E 33  ? 0.7109 0.8183 1.1316 -0.0847 0.1001  0.1290  33  SER E O   
11375 C CB  . SER E 33  ? 0.7992 0.7607 1.0824 -0.0578 0.0773  0.1110  33  SER E CB  
11376 O OG  . SER E 33  ? 0.7932 0.7239 1.0464 -0.0501 0.0530  0.0767  33  SER E OG  
11377 N N   . ALA E 34  ? 0.7836 0.8618 1.0899 -0.0402 0.1443  0.1665  34  ALA E N   
11378 C CA  . ALA E 34  ? 0.7598 0.9005 1.1207 -0.0481 0.1741  0.1973  34  ALA E CA  
11379 C C   . ALA E 34  ? 0.7131 0.9256 1.1231 -0.0413 0.1679  0.1798  34  ALA E C   
11380 O O   . ALA E 34  ? 0.6926 0.9666 1.1895 -0.0649 0.1696  0.1876  34  ALA E O   
11381 C CB  . ALA E 34  ? 0.7998 0.9408 1.0987 -0.0218 0.2135  0.2275  34  ALA E CB  
11382 N N   . LEU E 35  ? 0.8117 1.0169 1.1698 -0.0099 0.1584  0.1579  35  LEU E N   
11383 C CA  . LEU E 35  ? 0.7661 1.0317 1.1620 0.0012  0.1446  0.1437  35  LEU E CA  
11384 C C   . LEU E 35  ? 0.7180 1.0094 1.1762 -0.0314 0.1093  0.1205  35  LEU E C   
11385 O O   . LEU E 35  ? 0.6715 1.0383 1.2021 -0.0398 0.1007  0.1183  35  LEU E O   
11386 C CB  . LEU E 35  ? 0.7923 1.0228 1.1143 0.0361  0.1365  0.1286  35  LEU E CB  
11387 C CG  . LEU E 35  ? 0.7645 1.0400 1.1000 0.0605  0.1227  0.1225  35  LEU E CG  
11388 C CD1 . LEU E 35  ? 0.8009 1.0193 1.0584 0.0950  0.1257  0.1193  35  LEU E CD1 
11389 C CD2 . LEU E 35  ? 0.7350 1.0367 1.0984 0.0394  0.0847  0.1015  35  LEU E CD2 
11390 N N   . LYS E 36  ? 0.7446 0.9798 1.1774 -0.0475 0.0866  0.0982  36  LYS E N   
11391 C CA  . LYS E 36  ? 0.6990 0.9537 1.1807 -0.0741 0.0518  0.0655  36  LYS E CA  
11392 C C   . LYS E 36  ? 0.6605 0.9554 1.2412 -0.1096 0.0504  0.0718  36  LYS E C   
11393 O O   . LYS E 36  ? 0.6171 0.9617 1.2563 -0.1279 0.0221  0.0441  36  LYS E O   
11394 C CB  . LYS E 36  ? 0.7111 0.8973 1.1522 -0.0811 0.0348  0.0404  36  LYS E CB  
11395 C CG  . LYS E 36  ? 0.6627 0.8604 1.1477 -0.1049 0.0004  -0.0022 36  LYS E CG  
11396 C CD  . LYS E 36  ? 0.6669 0.8015 1.1126 -0.1034 -0.0109 -0.0268 36  LYS E CD  
11397 C CE  . LYS E 36  ? 0.6348 0.7430 1.1437 -0.1300 -0.0309 -0.0516 36  LYS E CE  
11398 N NZ  . LYS E 36  ? 0.5958 0.7183 1.1018 -0.1306 -0.0602 -0.1084 36  LYS E NZ  
11399 N N   . ASN E 37  ? 0.7114 0.9885 1.3121 -0.1218 0.0801  0.1085  37  ASN E N   
11400 C CA  . ASN E 37  ? 0.6801 0.9897 1.3816 -0.1630 0.0823  0.1213  37  ASN E CA  
11401 C C   . ASN E 37  ? 0.6457 1.0582 1.4150 -0.1634 0.0991  0.1383  37  ASN E C   
11402 O O   . ASN E 37  ? 0.6092 1.0691 1.4795 -0.2024 0.0945  0.1410  37  ASN E O   
11403 C CB  . ASN E 37  ? 0.7217 0.9699 1.4171 -0.1792 0.1089  0.1624  37  ASN E CB  
11404 C CG  . ASN E 37  ? 0.7484 0.9012 1.4017 -0.1813 0.0860  0.1448  37  ASN E CG  
11405 O OD1 . ASN E 37  ? 0.7295 0.8501 1.4409 -0.2121 0.0617  0.1271  37  ASN E OD1 
11406 N ND2 . ASN E 37  ? 0.7921 0.9005 1.3493 -0.1470 0.0916  0.1455  37  ASN E ND2 
11407 N N   . SER E 38  ? 0.7051 1.1537 1.4288 -0.1209 0.1174  0.1484  38  SER E N   
11408 C CA  . SER E 38  ? 0.6690 1.2225 1.4593 -0.1113 0.1330  0.1622  38  SER E CA  
11409 C C   . SER E 38  ? 0.6342 1.2500 1.4458 -0.0948 0.0946  0.1301  38  SER E C   
11410 O O   . SER E 38  ? 0.6007 1.3128 1.4759 -0.0827 0.0992  0.1376  38  SER E O   
11411 C CB  . SER E 38  ? 0.7012 1.2603 1.4357 -0.0685 0.1783  0.1923  38  SER E CB  
11412 O OG  . SER E 38  ? 0.6712 1.3148 1.4350 -0.0334 0.1805  0.1894  38  SER E OG  
11413 N N   . LEU E 39  ? 0.6297 1.2002 1.3893 -0.0917 0.0575  0.0963  39  LEU E N   
11414 C CA  . LEU E 39  ? 0.6105 1.2379 1.3748 -0.0757 0.0193  0.0698  39  LEU E CA  
11415 C C   . LEU E 39  ? 0.5824 1.2278 1.3981 -0.1158 -0.0235 0.0284  39  LEU E C   
11416 O O   . LEU E 39  ? 0.5906 1.1647 1.3883 -0.1405 -0.0310 0.0093  39  LEU E O   
11417 C CB  . LEU E 39  ? 0.6523 1.2245 1.3065 -0.0364 0.0122  0.0650  39  LEU E CB  
11418 C CG  . LEU E 39  ? 0.6755 1.2511 1.2839 0.0147  0.0337  0.0914  39  LEU E CG  
11419 C CD1 . LEU E 39  ? 0.6836 1.2555 1.3056 0.0244  0.0806  0.1207  39  LEU E CD1 
11420 C CD2 . LEU E 39  ? 0.7172 1.2129 1.2197 0.0385  0.0282  0.0875  39  LEU E CD2 
11421 N N   . ALA E 40  ? 0.5191 1.2628 1.4023 -0.1198 -0.0536 0.0113  40  ALA E N   
11422 C CA  . ALA E 40  ? 0.5222 1.2921 1.4385 -0.1490 -0.1025 -0.0389 40  ALA E CA  
11423 C C   . ALA E 40  ? 0.5298 1.2837 1.3451 -0.1169 -0.1286 -0.0604 40  ALA E C   
11424 O O   . ALA E 40  ? 0.5405 1.3359 1.3187 -0.0770 -0.1325 -0.0417 40  ALA E O   
11425 C CB  . ALA E 40  ? 0.5290 1.4206 1.5599 -0.1676 -0.1287 -0.0512 40  ALA E CB  
11426 N N   . ASP E 41  ? 0.5619 1.2553 1.3341 -0.1328 -0.1441 -0.0968 41  ASP E N   
11427 C CA  . ASP E 41  ? 0.5939 1.2699 1.2662 -0.1076 -0.1606 -0.1151 41  ASP E CA  
11428 C C   . ASP E 41  ? 0.5767 1.3043 1.2658 -0.1262 -0.2086 -0.1746 41  ASP E C   
11429 O O   . ASP E 41  ? 0.5749 1.2553 1.2521 -0.1453 -0.2177 -0.2164 41  ASP E O   
11430 C CB  . ASP E 41  ? 0.6205 1.1922 1.2207 -0.1046 -0.1347 -0.1114 41  ASP E CB  
11431 C CG  . ASP E 41  ? 0.6557 1.2142 1.1566 -0.0818 -0.1432 -0.1234 41  ASP E CG  
11432 O OD1 . ASP E 41  ? 0.6635 1.2883 1.1439 -0.0714 -0.1724 -0.1392 41  ASP E OD1 
11433 O OD2 . ASP E 41  ? 0.6770 1.1628 1.1204 -0.0753 -0.1204 -0.1149 41  ASP E OD2 
11434 N N   . PRO E 42  ? 0.4590 1.3495 1.2035 -0.0645 -0.2149 -0.0472 42  PRO E N   
11435 C CA  . PRO E 42  ? 0.4945 1.4151 1.2440 -0.0815 -0.2580 -0.0989 42  PRO E CA  
11436 C C   . PRO E 42  ? 0.5199 1.3740 1.1603 -0.0580 -0.2635 -0.1146 42  PRO E C   
11437 O O   . PRO E 42  ? 0.5522 1.3976 1.1873 -0.0799 -0.2874 -0.1618 42  PRO E O   
11438 C CB  . PRO E 42  ? 0.5094 1.5541 1.2982 -0.0605 -0.2912 -0.1035 42  PRO E CB  
11439 C CG  . PRO E 42  ? 0.4892 1.5403 1.2447 -0.0106 -0.2638 -0.0521 42  PRO E CG  
11440 C CD  . PRO E 42  ? 0.4544 1.4269 1.2132 -0.0254 -0.2148 -0.0209 42  PRO E CD  
11441 N N   . ASN E 43  ? 0.5878 1.3937 1.1449 -0.0158 -0.2393 -0.0785 43  ASN E N   
11442 C CA  . ASN E 43  ? 0.6499 1.3989 1.1059 0.0081  -0.2383 -0.0855 43  ASN E CA  
11443 C C   . ASN E 43  ? 0.6760 1.3201 1.1060 -0.0098 -0.2081 -0.0856 43  ASN E C   
11444 O O   . ASN E 43  ? 0.7322 1.3288 1.0878 0.0054  -0.2018 -0.0926 43  ASN E O   
11445 C CB  . ASN E 43  ? 0.6773 1.4292 1.0636 0.0630  -0.2287 -0.0446 43  ASN E CB  
11446 C CG  . ASN E 43  ? 0.6718 1.5202 1.0513 0.0921  -0.2671 -0.0496 43  ASN E CG  
11447 O OD1 . ASN E 43  ? 0.6451 1.5423 1.0415 0.1250  -0.2677 -0.0183 43  ASN E OD1 
11448 N ND2 . ASN E 43  ? 0.6977 1.5777 1.0520 0.0826  -0.3009 -0.0913 43  ASN E ND2 
11449 N N   . LYS E 44  ? 0.6841 1.2960 1.1742 -0.0398 -0.1888 -0.0750 44  LYS E N   
11450 C CA  . LYS E 44  ? 0.6943 1.2140 1.1705 -0.0556 -0.1646 -0.0725 44  LYS E CA  
11451 C C   . LYS E 44  ? 0.7389 1.2022 1.1386 -0.0220 -0.1381 -0.0408 44  LYS E C   
11452 O O   . LYS E 44  ? 0.7717 1.1722 1.1328 -0.0221 -0.1264 -0.0485 44  LYS E O   
11453 C CB  . LYS E 44  ? 0.7038 1.1946 1.1785 -0.0773 -0.1791 -0.1207 44  LYS E CB  
11454 C CG  . LYS E 44  ? 0.6533 1.1790 1.2153 -0.1190 -0.2035 -0.1590 44  LYS E CG  
11455 C CD  . LYS E 44  ? 0.5965 1.1631 1.2424 -0.1400 -0.1985 -0.1306 44  LYS E CD  
11456 C CE  . LYS E 44  ? 0.5447 1.0861 1.2820 -0.1895 -0.2000 -0.1482 44  LYS E CE  
11457 N NZ  . LYS E 44  ? 0.5017 1.0624 1.3056 -0.2074 -0.1793 -0.1036 44  LYS E NZ  
11458 N N   . VAL E 45  ? 0.6577 1.1451 1.0426 0.0068  -0.1280 -0.0071 45  VAL E N   
11459 C CA  . VAL E 45  ? 0.6890 1.1182 1.0126 0.0353  -0.1022 0.0213  45  VAL E CA  
11460 C C   . VAL E 45  ? 0.6691 1.0370 1.0063 0.0164  -0.0798 0.0331  45  VAL E C   
11461 O O   . VAL E 45  ? 0.6998 1.0036 0.9966 0.0212  -0.0653 0.0365  45  VAL E O   
11462 C CB  . VAL E 45  ? 0.6787 1.1468 0.9899 0.0732  -0.0976 0.0496  45  VAL E CB  
11463 C CG1 . VAL E 45  ? 0.6970 1.0988 0.9667 0.0939  -0.0678 0.0756  45  VAL E CG1 
11464 C CG2 . VAL E 45  ? 0.7065 1.2166 0.9792 0.1027  -0.1188 0.0465  45  VAL E CG2 
11465 N N   . LEU E 46  ? 0.6669 1.0578 1.0624 -0.0055 -0.0769 0.0414  46  LEU E N   
11466 C CA  . LEU E 46  ? 0.6472 0.9886 1.0523 -0.0218 -0.0588 0.0575  46  LEU E CA  
11467 C C   . LEU E 46  ? 0.6276 0.9251 1.0572 -0.0521 -0.0660 0.0389  46  LEU E C   
11468 O O   . LEU E 46  ? 0.6053 0.8672 1.0513 -0.0669 -0.0561 0.0549  46  LEU E O   
11469 C CB  . LEU E 46  ? 0.6135 0.9997 1.0669 -0.0317 -0.0483 0.0799  46  LEU E CB  
11470 C CG  . LEU E 46  ? 0.6220 1.0576 1.0628 0.0014  -0.0379 0.0966  46  LEU E CG  
11471 C CD1 . LEU E 46  ? 0.5901 1.0852 1.0908 -0.0119 -0.0248 0.1153  46  LEU E CD1 
11472 C CD2 . LEU E 46  ? 0.6639 1.0443 1.0364 0.0319  -0.0190 0.1093  46  LEU E CD2 
11473 N N   . GLN E 47  ? 0.6086 0.9091 1.0385 -0.0582 -0.0830 0.0056  47  GLN E N   
11474 C CA  . GLN E 47  ? 0.5848 0.8431 1.0429 -0.0829 -0.0888 -0.0185 47  GLN E CA  
11475 C C   . GLN E 47  ? 0.5783 0.7695 1.0139 -0.0785 -0.0731 -0.0042 47  GLN E C   
11476 O O   . GLN E 47  ? 0.5362 0.6921 1.0113 -0.0977 -0.0731 -0.0024 47  GLN E O   
11477 C CB  . GLN E 47  ? 0.6244 0.8951 1.0619 -0.0795 -0.1046 -0.0604 47  GLN E CB  
11478 C CG  . GLN E 47  ? 0.6100 0.8308 1.0630 -0.0945 -0.1050 -0.0910 47  GLN E CG  
11479 C CD  . GLN E 47  ? 0.5559 0.7763 1.0874 -0.1287 -0.1190 -0.1127 47  GLN E CD  
11480 O OE1 . GLN E 47  ? 0.5389 0.8097 1.1118 -0.1444 -0.1329 -0.1160 47  GLN E OE1 
11481 N NE2 . GLN E 47  ? 0.5289 0.6920 1.0898 -0.1407 -0.1149 -0.1273 47  GLN E NE2 
11482 N N   . SER E 48  ? 0.6033 0.7767 0.9808 -0.0530 -0.0609 0.0072  48  SER E N   
11483 C CA  . SER E 48  ? 0.5983 0.7165 0.9585 -0.0495 -0.0497 0.0141  48  SER E CA  
11484 C C   . SER E 48  ? 0.5686 0.6691 0.9437 -0.0560 -0.0447 0.0431  48  SER E C   
11485 O O   . SER E 48  ? 0.5496 0.6101 0.9264 -0.0582 -0.0433 0.0469  48  SER E O   
11486 C CB  . SER E 48  ? 0.6633 0.7692 0.9647 -0.0246 -0.0371 0.0185  48  SER E CB  
11487 O OG  . SER E 48  ? 0.6601 0.7275 0.9473 -0.0199 -0.0265 0.0345  48  SER E OG  
11488 N N   . TRP E 49  ? 0.5663 0.7013 0.9523 -0.0579 -0.0421 0.0638  49  TRP E N   
11489 C CA  . TRP E 49  ? 0.5780 0.7038 0.9564 -0.0572 -0.0325 0.0942  49  TRP E CA  
11490 C C   . TRP E 49  ? 0.5429 0.6482 0.9677 -0.0813 -0.0380 0.1069  49  TRP E C   
11491 O O   . TRP E 49  ? 0.5290 0.6597 0.9957 -0.0992 -0.0361 0.1216  49  TRP E O   
11492 C CB  . TRP E 49  ? 0.6013 0.7770 0.9739 -0.0473 -0.0216 0.1115  49  TRP E CB  
11493 C CG  . TRP E 49  ? 0.6422 0.8250 0.9660 -0.0167 -0.0142 0.1065  49  TRP E CG  
11494 C CD1 . TRP E 49  ? 0.6623 0.8214 0.9554 -0.0028 -0.0172 0.0895  49  TRP E CD1 
11495 C CD2 . TRP E 49  ? 0.6700 0.8816 0.9726 0.0054  0.0008  0.1211  49  TRP E CD2 
11496 N NE1 . TRP E 49  ? 0.6965 0.8613 0.9525 0.0257  -0.0067 0.0958  49  TRP E NE1 
11497 C CE2 . TRP E 49  ? 0.6954 0.8917 0.9578 0.0328  0.0037  0.1121  49  TRP E CE2 
11498 C CE3 . TRP E 49  ? 0.6774 0.9260 0.9919 0.0060  0.0154  0.1417  49  TRP E CE3 
11499 C CZ2 . TRP E 49  ? 0.7147 0.9259 0.9530 0.0627  0.0179  0.1202  49  TRP E CZ2 
11500 C CZ3 . TRP E 49  ? 0.7031 0.9744 0.9912 0.0362  0.0314  0.1464  49  TRP E CZ3 
11501 C CH2 . TRP E 49  ? 0.7164 0.9661 0.9687 0.0652  0.0312  0.1343  49  TRP E CH2 
11502 N N   . ASP E 50  ? 0.5685 0.6277 0.9915 -0.0812 -0.0439 0.1036  50  ASP E N   
11503 C CA  . ASP E 50  ? 0.5443 0.5742 1.0101 -0.0973 -0.0509 0.1192  50  ASP E CA  
11504 C C   . ASP E 50  ? 0.5959 0.6205 1.0339 -0.0917 -0.0463 0.1585  50  ASP E C   
11505 O O   . ASP E 50  ? 0.6277 0.6372 1.0233 -0.0755 -0.0492 0.1591  50  ASP E O   
11506 C CB  . ASP E 50  ? 0.5070 0.4972 0.9902 -0.0948 -0.0607 0.0954  50  ASP E CB  
11507 C CG  . ASP E 50  ? 0.4947 0.4485 1.0213 -0.1032 -0.0695 0.1157  50  ASP E CG  
11508 O OD1 . ASP E 50  ? 0.5096 0.4642 1.0633 -0.1179 -0.0675 0.1451  50  ASP E OD1 
11509 O OD2 . ASP E 50  ? 0.4745 0.3999 1.0125 -0.0941 -0.0771 0.1046  50  ASP E OD2 
11510 N N   . ALA E 51  ? 0.5247 0.5621 0.9884 -0.1067 -0.0393 0.1908  51  ALA E N   
11511 C CA  . ALA E 51  ? 0.5927 0.6354 1.0193 -0.1004 -0.0306 0.2321  51  ALA E CA  
11512 C C   . ALA E 51  ? 0.6137 0.6150 1.0301 -0.0937 -0.0457 0.2505  51  ALA E C   
11513 O O   . ALA E 51  ? 0.6735 0.6799 1.0365 -0.0806 -0.0449 0.2746  51  ALA E O   
11514 C CB  . ALA E 51  ? 0.5961 0.6655 1.0600 -0.1211 -0.0143 0.2666  51  ALA E CB  
11515 N N   . THR E 52  ? 0.5802 0.5445 1.0462 -0.0999 -0.0607 0.2379  52  THR E N   
11516 C CA  . THR E 52  ? 0.5986 0.5272 1.0724 -0.0921 -0.0774 0.2607  52  THR E CA  
11517 C C   . THR E 52  ? 0.6042 0.5268 1.0474 -0.0720 -0.0931 0.2362  52  THR E C   
11518 O O   . THR E 52  ? 0.6160 0.5167 1.0736 -0.0626 -0.1117 0.2493  52  THR E O   
11519 C CB  . THR E 52  ? 0.5648 0.4542 1.1183 -0.1056 -0.0844 0.2584  52  THR E CB  
11520 O OG1 . THR E 52  ? 0.5290 0.4111 1.1086 -0.1040 -0.0889 0.2051  52  THR E OG1 
11521 C CG2 . THR E 52  ? 0.5853 0.4798 1.1818 -0.1320 -0.0692 0.2770  52  THR E CG2 
11522 N N   . LEU E 53  ? 0.5603 0.5019 0.9685 -0.0654 -0.0864 0.2029  53  LEU E N   
11523 C CA  . LEU E 53  ? 0.5699 0.5069 0.9534 -0.0512 -0.0983 0.1819  53  LEU E CA  
11524 C C   . LEU E 53  ? 0.6516 0.6025 0.9710 -0.0399 -0.1039 0.2010  53  LEU E C   
11525 O O   . LEU E 53  ? 0.6926 0.6621 0.9753 -0.0401 -0.0909 0.2248  53  LEU E O   
11526 C CB  . LEU E 53  ? 0.5266 0.4701 0.9006 -0.0496 -0.0862 0.1422  53  LEU E CB  
11527 C CG  . LEU E 53  ? 0.4779 0.4159 0.8981 -0.0585 -0.0794 0.1176  53  LEU E CG  
11528 C CD1 . LEU E 53  ? 0.4548 0.4006 0.8515 -0.0530 -0.0669 0.0872  53  LEU E CD1 
11529 C CD2 . LEU E 53  ? 0.4852 0.3986 0.9627 -0.0594 -0.0917 0.1108  53  LEU E CD2 
11530 N N   . VAL E 54  ? 0.5950 0.5413 0.9028 -0.0301 -0.1232 0.1871  54  VAL E N   
11531 C CA  . VAL E 54  ? 0.6696 0.6300 0.9126 -0.0191 -0.1339 0.1949  54  VAL E CA  
11532 C C   . VAL E 54  ? 0.7031 0.6755 0.8928 -0.0156 -0.1122 0.1760  54  VAL E C   
11533 O O   . VAL E 54  ? 0.7561 0.7461 0.8918 -0.0089 -0.1030 0.1936  54  VAL E O   
11534 C CB  . VAL E 54  ? 0.6800 0.6386 0.9336 -0.0126 -0.1630 0.1748  54  VAL E CB  
11535 C CG1 . VAL E 54  ? 0.7533 0.7294 0.9407 -0.0011 -0.1833 0.1861  54  VAL E CG1 
11536 C CG2 . VAL E 54  ? 0.6355 0.5828 0.9605 -0.0124 -0.1805 0.1855  54  VAL E CG2 
11537 N N   . THR E 55  ? 0.6889 0.6518 0.8924 -0.0176 -0.1017 0.1419  55  THR E N   
11538 C CA  . THR E 55  ? 0.7221 0.6887 0.8844 -0.0104 -0.0811 0.1245  55  THR E CA  
11539 C C   . THR E 55  ? 0.6547 0.6208 0.8481 -0.0146 -0.0621 0.1158  55  THR E C   
11540 O O   . THR E 55  ? 0.5866 0.5442 0.8277 -0.0238 -0.0661 0.1097  55  THR E O   
11541 C CB  . THR E 55  ? 0.7708 0.7208 0.9088 -0.0053 -0.0890 0.0918  55  THR E CB  
11542 O OG1 . THR E 55  ? 0.6977 0.6288 0.8782 -0.0127 -0.0845 0.0699  55  THR E OG1 
11543 C CG2 . THR E 55  ? 0.8189 0.7734 0.9446 -0.0046 -0.1195 0.0925  55  THR E CG2 
11544 N N   . PRO E 56  ? 0.7037 0.6828 0.8701 -0.0054 -0.0421 0.1141  56  PRO E N   
11545 C CA  . PRO E 56  ? 0.6592 0.6460 0.8487 -0.0056 -0.0287 0.1072  56  PRO E CA  
11546 C C   . PRO E 56  ? 0.6430 0.6046 0.8286 -0.0001 -0.0231 0.0834  56  PRO E C   
11547 O O   . PRO E 56  ? 0.6346 0.6045 0.8219 0.0062  -0.0115 0.0805  56  PRO E O   
11548 C CB  . PRO E 56  ? 0.7001 0.7185 0.8651 0.0065  -0.0114 0.1192  56  PRO E CB  
11549 C CG  . PRO E 56  ? 0.7708 0.7811 0.8847 0.0193  -0.0094 0.1160  56  PRO E CG  
11550 C CD  . PRO E 56  ? 0.7794 0.7752 0.8939 0.0083  -0.0311 0.1213  56  PRO E CD  
11551 N N   . CYS E 57  ? 0.7230 0.6573 0.9057 -0.0028 -0.0312 0.0685  57  CYS E N   
11552 C CA  . CYS E 57  ? 0.7083 0.6149 0.8879 0.0002  -0.0203 0.0504  57  CYS E CA  
11553 C C   . CYS E 57  ? 0.6459 0.5520 0.8572 -0.0065 -0.0129 0.0468  57  CYS E C   
11554 O O   . CYS E 57  ? 0.6517 0.5407 0.8522 -0.0007 0.0033  0.0420  57  CYS E O   
11555 C CB  . CYS E 57  ? 0.7190 0.6023 0.9000 -0.0066 -0.0322 0.0330  57  CYS E CB  
11556 S SG  . CYS E 57  ? 0.8361 0.7175 0.9631 0.0045  -0.0403 0.0261  57  CYS E SG  
11557 N N   . THR E 58  ? 0.6751 0.5966 0.9224 -0.0170 -0.0228 0.0491  58  THR E N   
11558 C CA  . THR E 58  ? 0.6336 0.5583 0.9050 -0.0212 -0.0144 0.0394  58  THR E CA  
11559 C C   . THR E 58  ? 0.6641 0.6138 0.9252 -0.0162 -0.0099 0.0437  58  THR E C   
11560 O O   . THR E 58  ? 0.6564 0.6141 0.9289 -0.0185 -0.0056 0.0318  58  THR E O   
11561 C CB  . THR E 58  ? 0.5655 0.4911 0.8875 -0.0324 -0.0267 0.0319  58  THR E CB  
11562 O OG1 . THR E 58  ? 0.5608 0.4975 0.8978 -0.0364 -0.0416 0.0461  58  THR E OG1 
11563 C CG2 . THR E 58  ? 0.5422 0.4546 0.8842 -0.0365 -0.0350 0.0256  58  THR E CG2 
11564 N N   . TRP E 59  ? 0.5947 0.5626 0.8362 -0.0090 -0.0111 0.0578  59  TRP E N   
11565 C CA  . TRP E 59  ? 0.6244 0.6263 0.8644 -0.0042 -0.0097 0.0607  59  TRP E CA  
11566 C C   . TRP E 59  ? 0.6799 0.6808 0.8854 0.0142  0.0028  0.0597  59  TRP E C   
11567 O O   . TRP E 59  ? 0.6942 0.6645 0.8742 0.0247  0.0141  0.0628  59  TRP E O   
11568 C CB  . TRP E 59  ? 0.6468 0.6770 0.8857 -0.0014 -0.0110 0.0782  59  TRP E CB  
11569 C CG  . TRP E 59  ? 0.6128 0.6441 0.8778 -0.0175 -0.0200 0.0902  59  TRP E CG  
11570 C CD1 . TRP E 59  ? 0.5599 0.5685 0.8540 -0.0315 -0.0310 0.0872  59  TRP E CD1 
11571 C CD2 . TRP E 59  ? 0.6370 0.6945 0.9021 -0.0188 -0.0163 0.1120  59  TRP E CD2 
11572 N NE1 . TRP E 59  ? 0.5638 0.5777 0.8724 -0.0404 -0.0365 0.1096  59  TRP E NE1 
11573 C CE2 . TRP E 59  ? 0.6147 0.6594 0.9036 -0.0346 -0.0257 0.1259  59  TRP E CE2 
11574 C CE3 . TRP E 59  ? 0.6699 0.7629 0.9192 -0.0060 -0.0035 0.1231  59  TRP E CE3 
11575 C CZ2 . TRP E 59  ? 0.6465 0.7104 0.9373 -0.0402 -0.0208 0.1543  59  TRP E CZ2 
11576 C CZ3 . TRP E 59  ? 0.6853 0.8032 0.9410 -0.0122 0.0033  0.1465  59  TRP E CZ3 
11577 C CH2 . TRP E 59  ? 0.6799 0.7821 0.9528 -0.0303 -0.0044 0.1639  59  TRP E CH2 
11578 N N   . PHE E 60  ? 0.6355 0.6693 0.8409 0.0184  -0.0007 0.0557  60  PHE E N   
11579 C CA  . PHE E 60  ? 0.6813 0.7195 0.8488 0.0410  0.0084  0.0625  60  PHE E CA  
11580 C C   . PHE E 60  ? 0.6695 0.7265 0.8244 0.0619  0.0108  0.0796  60  PHE E C   
11581 O O   . PHE E 60  ? 0.6395 0.7246 0.8175 0.0566  0.0050  0.0835  60  PHE E O   
11582 C CB  . PHE E 60  ? 0.7104 0.7844 0.8745 0.0416  -0.0005 0.0503  60  PHE E CB  
11583 C CG  . PHE E 60  ? 0.7241 0.7837 0.9004 0.0247  0.0007  0.0279  60  PHE E CG  
11584 C CD1 . PHE E 60  ? 0.7155 0.7321 0.8930 0.0190  0.0161  0.0268  60  PHE E CD1 
11585 C CD2 . PHE E 60  ? 0.7230 0.8150 0.9151 0.0149  -0.0134 0.0040  60  PHE E CD2 
11586 C CE1 . PHE E 60  ? 0.7005 0.7103 0.8965 0.0070  0.0203  0.0052  60  PHE E CE1 
11587 C CE2 . PHE E 60  ? 0.7271 0.8048 0.9316 0.0032  -0.0094 -0.0214 60  PHE E CE2 
11588 C CZ  . PHE E 60  ? 0.7168 0.7551 0.9237 0.0010  0.0091  -0.0193 60  PHE E CZ  
11589 N N   . HIS E 61  ? 0.7248 0.7648 0.8448 0.0875  0.0225  0.0919  61  HIS E N   
11590 C CA  . HIS E 61  ? 0.7131 0.7645 0.8213 0.1155  0.0281  0.1070  61  HIS E CA  
11591 C C   . HIS E 61  ? 0.7028 0.7267 0.8120 0.1149  0.0372  0.1051  61  HIS E C   
11592 O O   . HIS E 61  ? 0.7019 0.7390 0.8057 0.1382  0.0444  0.1124  61  HIS E O   
11593 C CB  . HIS E 61  ? 0.6909 0.8169 0.8227 0.1229  0.0133  0.1101  61  HIS E CB  
11594 C CG  . HIS E 61  ? 0.7053 0.8674 0.8401 0.1151  -0.0035 0.1007  61  HIS E CG  
11595 N ND1 . HIS E 61  ? 0.7467 0.9023 0.8414 0.1347  -0.0025 0.1082  61  HIS E ND1 
11596 C CD2 . HIS E 61  ? 0.6885 0.8913 0.8586 0.0900  -0.0213 0.0825  61  HIS E CD2 
11597 C CE1 . HIS E 61  ? 0.7649 0.9616 0.8635 0.1235  -0.0205 0.0914  61  HIS E CE1 
11598 N NE2 . HIS E 61  ? 0.7261 0.9495 0.8742 0.0954  -0.0328 0.0726  61  HIS E NE2 
11599 N N   . VAL E 62  ? 0.7636 0.7527 0.8781 0.0917  0.0365  0.0936  62  VAL E N   
11600 C CA  . VAL E 62  ? 0.7725 0.7354 0.8783 0.0900  0.0407  0.0873  62  VAL E CA  
11601 C C   . VAL E 62  ? 0.7767 0.6803 0.8749 0.0800  0.0453  0.0757  62  VAL E C   
11602 O O   . VAL E 62  ? 0.7545 0.6512 0.8710 0.0602  0.0403  0.0705  62  VAL E O   
11603 C CB  . VAL E 62  ? 0.7642 0.7564 0.8905 0.0694  0.0289  0.0869  62  VAL E CB  
11604 C CG1 . VAL E 62  ? 0.7938 0.7554 0.9018 0.0645  0.0278  0.0778  62  VAL E CG1 
11605 C CG2 . VAL E 62  ? 0.7595 0.8093 0.8987 0.0778  0.0310  0.0996  62  VAL E CG2 
11606 N N   . THR E 63  ? 0.8477 0.7099 0.9251 0.0930  0.0558  0.0688  63  THR E N   
11607 C CA  . THR E 63  ? 0.8486 0.6558 0.9290 0.0790  0.0593  0.0541  63  THR E CA  
11608 C C   . THR E 63  ? 0.8876 0.6804 0.9566 0.0749  0.0511  0.0327  63  THR E C   
11609 O O   . THR E 63  ? 0.9336 0.7354 0.9780 0.0949  0.0558  0.0298  63  THR E O   
11610 C CB  . THR E 63  ? 0.8600 0.6173 0.9288 0.0951  0.0800  0.0625  63  THR E CB  
11611 O OG1 . THR E 63  ? 0.8991 0.6248 0.9480 0.1175  0.0889  0.0542  63  THR E OG1 
11612 C CG2 . THR E 63  ? 0.8562 0.6405 0.9162 0.1131  0.0863  0.0885  63  THR E CG2 
11613 N N   . CYS E 64  ? 0.8605 0.6379 0.9476 0.0505  0.0383  0.0163  64  CYS E N   
11614 C CA  . CYS E 64  ? 0.9107 0.6801 0.9842 0.0442  0.0232  -0.0074 64  CYS E CA  
11615 C C   . CYS E 64  ? 0.9143 0.6270 0.9969 0.0350  0.0267  -0.0334 64  CYS E C   
11616 O O   . CYS E 64  ? 0.8700 0.5507 0.9776 0.0279  0.0420  -0.0275 64  CYS E O   
11617 C CB  . CYS E 64  ? 0.8914 0.6949 0.9845 0.0242  -0.0018 -0.0065 64  CYS E CB  
11618 S SG  . CYS E 64  ? 0.9085 0.7696 0.9925 0.0297  -0.0086 0.0209  64  CYS E SG  
11619 N N   . ASN E 65  ? 0.9305 0.6316 0.9917 0.0339  0.0132  -0.0629 65  ASN E N   
11620 C CA  . ASN E 65  ? 0.9297 0.5816 1.0093 0.0176  0.0090  -0.0964 65  ASN E CA  
11621 C C   . ASN E 65  ? 0.8876 0.5656 1.0055 -0.0117 -0.0198 -0.1085 65  ASN E C   
11622 O O   . ASN E 65  ? 0.8544 0.5789 0.9855 -0.0160 -0.0320 -0.0872 65  ASN E O   
11623 C CB  . ASN E 65  ? 1.0184 0.6410 1.0541 0.0340  0.0088  -0.1307 65  ASN E CB  
11624 C CG  . ASN E 65  ? 1.0917 0.7622 1.0818 0.0402  -0.0146 -0.1430 65  ASN E CG  
11625 O OD1 . ASN E 65  ? 1.0802 0.7995 1.0772 0.0292  -0.0348 -0.1253 65  ASN E OD1 
11626 N ND2 . ASN E 65  ? 1.1711 0.8253 1.1119 0.0601  -0.0098 -0.1725 65  ASN E ND2 
11627 N N   . SER E 66  ? 0.9320 0.5809 1.0754 -0.0318 -0.0320 -0.1442 66  SER E N   
11628 C CA  . SER E 66  ? 0.8849 0.5657 1.0766 -0.0582 -0.0616 -0.1573 66  SER E CA  
11629 C C   . SER E 66  ? 0.9412 0.6730 1.0980 -0.0515 -0.0985 -0.1629 66  SER E C   
11630 O O   . SER E 66  ? 0.9026 0.6720 1.0990 -0.0661 -0.1263 -0.1635 66  SER E O   
11631 C CB  . SER E 66  ? 0.8697 0.5114 1.1067 -0.0845 -0.0669 -0.1972 66  SER E CB  
11632 O OG  . SER E 66  ? 0.9511 0.5553 1.1434 -0.0757 -0.0721 -0.2349 66  SER E OG  
11633 N N   . ASP E 67  ? 0.8984 0.6344 0.9835 -0.0280 -0.0979 -0.1646 67  ASP E N   
11634 C CA  . ASP E 67  ? 0.9727 0.7576 1.0120 -0.0184 -0.1263 -0.1593 67  ASP E CA  
11635 C C   . ASP E 67  ? 0.9796 0.8015 1.0110 -0.0064 -0.1166 -0.1094 67  ASP E C   
11636 O O   . ASP E 67  ? 1.0528 0.9122 1.0460 0.0024  -0.1341 -0.0937 67  ASP E O   
11637 C CB  . ASP E 67  ? 1.0784 0.8529 1.0407 0.0003  -0.1266 -0.1894 67  ASP E CB  
11638 C CG  . ASP E 67  ? 1.0776 0.8115 1.0478 -0.0134 -0.1402 -0.2477 67  ASP E CG  
11639 O OD1 . ASP E 67  ? 1.0130 0.7480 1.0453 -0.0406 -0.1629 -0.2641 67  ASP E OD1 
11640 O OD2 . ASP E 67  ? 1.1397 0.8419 1.0601 0.0026  -0.1276 -0.2796 67  ASP E OD2 
11641 N N   . ASN E 68  ? 0.9210 0.7328 0.9872 -0.0068 -0.0898 -0.0843 68  ASN E N   
11642 C CA  . ASN E 68  ? 0.9090 0.7514 0.9771 0.0010  -0.0796 -0.0437 68  ASN E CA  
11643 C C   . ASN E 68  ? 1.0073 0.8656 1.0175 0.0228  -0.0640 -0.0304 68  ASN E C   
11644 O O   . ASN E 68  ? 1.0357 0.9295 1.0367 0.0263  -0.0658 -0.0004 68  ASN E O   
11645 C CB  . ASN E 68  ? 0.8909 0.7676 0.9872 -0.0086 -0.1069 -0.0254 68  ASN E CB  
11646 C CG  . ASN E 68  ? 0.7907 0.6624 0.9520 -0.0274 -0.1218 -0.0411 68  ASN E CG  
11647 O OD1 . ASN E 68  ? 0.6904 0.5579 0.8998 -0.0348 -0.1068 -0.0321 68  ASN E OD1 
11648 N ND2 . ASN E 68  ? 0.8173 0.6952 0.9813 -0.0349 -0.1515 -0.0671 68  ASN E ND2 
11649 N N   . SER E 69  ? 0.9899 0.8214 0.9671 0.0376  -0.0461 -0.0521 69  SER E N   
11650 C CA  . SER E 69  ? 1.0592 0.9086 0.9909 0.0621  -0.0243 -0.0425 69  SER E CA  
11651 C C   . SER E 69  ? 0.9917 0.8281 0.9460 0.0746  0.0038  -0.0295 69  SER E C   
11652 O O   . SER E 69  ? 0.9467 0.7377 0.9209 0.0735  0.0117  -0.0437 69  SER E O   
11653 C CB  . SER E 69  ? 1.1416 0.9742 1.0162 0.0769  -0.0242 -0.0803 69  SER E CB  
11654 O OG  . SER E 69  ? 1.2156 1.0886 1.0391 0.0972  -0.0104 -0.0672 69  SER E OG  
11655 N N   . VAL E 70  ? 1.0401 0.9183 0.9933 0.0864  0.0183  -0.0007 70  VAL E N   
11656 C CA  . VAL E 70  ? 0.9698 0.8499 0.9470 0.0996  0.0380  0.0144  70  VAL E CA  
11657 C C   . VAL E 70  ? 0.9927 0.8364 0.9476 0.1270  0.0576  -0.0057 70  VAL E C   
11658 O O   . VAL E 70  ? 1.0584 0.9055 0.9751 0.1449  0.0662  -0.0232 70  VAL E O   
11659 C CB  . VAL E 70  ? 0.9441 0.8860 0.9327 0.1040  0.0459  0.0447  70  VAL E CB  
11660 C CG1 . VAL E 70  ? 0.8848 0.8402 0.8938 0.1238  0.0625  0.0559  70  VAL E CG1 
11661 C CG2 . VAL E 70  ? 0.8948 0.8583 0.9164 0.0767  0.0279  0.0640  70  VAL E CG2 
11662 N N   . THR E 71  ? 1.0330 0.8393 1.0098 0.1325  0.0666  -0.0025 71  THR E N   
11663 C CA  . THR E 71  ? 1.0474 0.8095 1.0118 0.1617  0.0865  -0.0147 71  THR E CA  
11664 C C   . THR E 71  ? 0.9966 0.7726 0.9783 0.1865  0.1011  0.0143  71  THR E C   
11665 O O   . THR E 71  ? 1.0131 0.7630 0.9865 0.2196  0.1186  0.0105  71  THR E O   
11666 C CB  . THR E 71  ? 1.0543 0.7391 1.0257 0.1480  0.0849  -0.0391 71  THR E CB  
11667 O OG1 . THR E 71  ? 0.9896 0.6650 0.9946 0.1260  0.0812  -0.0192 71  THR E OG1 
11668 C CG2 . THR E 71  ? 1.1106 0.7858 1.0646 0.1273  0.0657  -0.0754 71  THR E CG2 
11669 N N   . ARG E 72  ? 0.9835 0.7998 0.9891 0.1743  0.0928  0.0409  72  ARG E N   
11670 C CA  . ARG E 72  ? 0.9454 0.7868 0.9637 0.1979  0.0997  0.0670  72  ARG E CA  
11671 C C   . ARG E 72  ? 0.9060 0.8254 0.9466 0.1853  0.0871  0.0837  72  ARG E C   
11672 O O   . ARG E 72  ? 0.8936 0.8257 0.9452 0.1535  0.0733  0.0811  72  ARG E O   
11673 C CB  . ARG E 72  ? 0.9268 0.7195 0.9486 0.1957  0.1032  0.0799  72  ARG E CB  
11674 C CG  . ARG E 72  ? 0.9601 0.6695 0.9706 0.2117  0.1204  0.0718  72  ARG E CG  
11675 C CD  . ARG E 72  ? 0.9487 0.6204 0.9606 0.2172  0.1301  0.0998  72  ARG E CD  
11676 N NE  . ARG E 72  ? 0.9380 0.6533 0.9450 0.2513  0.1300  0.1307  72  ARG E NE  
11677 C CZ  . ARG E 72  ? 0.9582 0.6404 0.9573 0.2913  0.1436  0.1511  72  ARG E CZ  
11678 N NH1 . ARG E 72  ? 0.9927 0.5875 0.9893 0.3009  0.1619  0.1437  72  ARG E NH1 
11679 N NH2 . ARG E 72  ? 0.9448 0.6829 0.9428 0.3232  0.1367  0.1786  72  ARG E NH2 
11680 N N   . VAL E 73  ? 0.8826 0.8540 0.9366 0.2108  0.0911  0.0995  73  VAL E N   
11681 C CA  . VAL E 73  ? 0.8406 0.8866 0.9259 0.1990  0.0777  0.1134  73  VAL E CA  
11682 C C   . VAL E 73  ? 0.8208 0.8887 0.9127 0.2287  0.0755  0.1305  73  VAL E C   
11683 O O   . VAL E 73  ? 0.8192 0.9157 0.9194 0.2638  0.0844  0.1378  73  VAL E O   
11684 C CB  . VAL E 73  ? 0.8386 0.9487 0.9436 0.1970  0.0827  0.1151  73  VAL E CB  
11685 C CG1 . VAL E 73  ? 0.7912 0.9733 0.9406 0.1785  0.0681  0.1269  73  VAL E CG1 
11686 C CG2 . VAL E 73  ? 0.8792 0.9654 0.9640 0.1741  0.0846  0.1036  73  VAL E CG2 
11687 N N   . ASP E 74  ? 0.8261 0.8836 0.9125 0.2182  0.0640  0.1372  74  ASP E N   
11688 C CA  . ASP E 74  ? 0.8257 0.8982 0.9037 0.2483  0.0595  0.1568  74  ASP E CA  
11689 C C   . ASP E 74  ? 0.7974 0.9563 0.9038 0.2383  0.0363  0.1578  74  ASP E C   
11690 O O   . ASP E 74  ? 0.8051 0.9688 0.9051 0.2165  0.0231  0.1526  74  ASP E O   
11691 C CB  . ASP E 74  ? 0.8547 0.8589 0.8988 0.2455  0.0660  0.1651  74  ASP E CB  
11692 C CG  . ASP E 74  ? 0.8800 0.7966 0.9070 0.2526  0.0881  0.1617  74  ASP E CG  
11693 O OD1 . ASP E 74  ? 0.8836 0.7645 0.9132 0.2218  0.0912  0.1413  74  ASP E OD1 
11694 O OD2 . ASP E 74  ? 0.8982 0.7817 0.9130 0.2894  0.1004  0.1783  74  ASP E OD2 
11695 N N   . LEU E 75  ? 0.7719 1.0022 0.9141 0.2540  0.0321  0.1611  75  LEU E N   
11696 C CA  . LEU E 75  ? 0.7384 1.0578 0.9223 0.2403  0.0086  0.1574  75  LEU E CA  
11697 C C   . LEU E 75  ? 0.7229 1.1080 0.9218 0.2815  -0.0045 0.1729  75  LEU E C   
11698 O O   . LEU E 75  ? 0.6852 1.1603 0.9370 0.2774  -0.0203 0.1690  75  LEU E O   
11699 C CB  . LEU E 75  ? 0.7092 1.0718 0.9407 0.2125  0.0133  0.1482  75  LEU E CB  
11700 C CG  . LEU E 75  ? 0.7170 1.0378 0.9460 0.1684  0.0153  0.1357  75  LEU E CG  
11701 C CD1 . LEU E 75  ? 0.6977 1.0577 0.9666 0.1484  0.0252  0.1378  75  LEU E CD1 
11702 C CD2 . LEU E 75  ? 0.7139 1.0400 0.9499 0.1409  -0.0072 0.1229  75  LEU E CD2 
11703 N N   . GLY E 76  ? 0.8033 1.1462 0.9619 0.3215  0.0013  0.1926  76  GLY E N   
11704 C CA  . GLY E 76  ? 0.7924 1.1966 0.9622 0.3667  -0.0148 0.2126  76  GLY E CA  
11705 C C   . GLY E 76  ? 0.7932 1.2550 0.9548 0.3578  -0.0496 0.2105  76  GLY E C   
11706 O O   . GLY E 76  ? 0.8258 1.2467 0.9451 0.3334  -0.0532 0.2033  76  GLY E O   
11707 N N   . ASN E 77  ? 0.7490 1.3130 0.9535 0.3792  -0.0759 0.2139  77  ASN E N   
11708 C CA  . ASN E 77  ? 0.7506 1.3853 0.9481 0.3764  -0.1160 0.2073  77  ASN E CA  
11709 C C   . ASN E 77  ? 0.7513 1.3910 0.9577 0.3169  -0.1275 0.1707  77  ASN E C   
11710 O O   . ASN E 77  ? 0.7915 1.4136 0.9470 0.3059  -0.1408 0.1613  77  ASN E O   
11711 C CB  . ASN E 77  ? 0.8031 1.3957 0.9200 0.4137  -0.1214 0.2364  77  ASN E CB  
11712 C CG  . ASN E 77  ? 0.8118 1.3772 0.9190 0.4728  -0.1068 0.2755  77  ASN E CG  
11713 O OD1 . ASN E 77  ? 0.8363 1.4605 0.9708 0.4949  -0.1238 0.2797  77  ASN E OD1 
11714 N ND2 . ASN E 77  ? 0.8445 1.2984 0.9124 0.4820  -0.0706 0.2931  77  ASN E ND2 
11715 N N   . ALA E 78  ? 0.7550 1.4168 1.0260 0.2800  -0.1195 0.1511  78  ALA E N   
11716 C CA  . ALA E 78  ? 0.7524 1.4105 1.0435 0.2246  -0.1279 0.1187  78  ALA E CA  
11717 C C   . ALA E 78  ? 0.7005 1.4615 1.0770 0.1983  -0.1545 0.0965  78  ALA E C   
11718 O O   . ALA E 78  ? 0.6910 1.4494 1.1003 0.1505  -0.1606 0.0694  78  ALA E O   
11719 C CB  . ALA E 78  ? 0.7565 1.3336 1.0459 0.1972  -0.0940 0.1181  78  ALA E CB  
11720 N N   . ASN E 79  ? 0.7223 1.5743 1.1427 0.2287  -0.1707 0.1074  79  ASN E N   
11721 C CA  . ASN E 79  ? 0.6714 1.6365 1.1841 0.2047  -0.1999 0.0857  79  ASN E CA  
11722 C C   . ASN E 79  ? 0.6362 1.6016 1.2228 0.1553  -0.1769 0.0770  79  ASN E C   
11723 O O   . ASN E 79  ? 0.6097 1.6250 1.2636 0.1107  -0.1969 0.0498  79  ASN E O   
11724 C CB  . ASN E 79  ? 0.6871 1.6906 1.1863 0.1862  -0.2451 0.0512  79  ASN E CB  
11725 C CG  . ASN E 79  ? 0.7388 1.7221 1.1403 0.2322  -0.2613 0.0650  79  ASN E CG  
11726 O OD1 . ASN E 79  ? 0.7548 1.7053 1.1136 0.2804  -0.2425 0.1036  79  ASN E OD1 
11727 N ND2 . ASN E 79  ? 0.7693 1.7694 1.1330 0.2182  -0.2942 0.0337  79  ASN E ND2 
11728 N N   . LEU E 80  ? 0.7192 1.4670 1.1553 0.1026  -0.2413 0.3278  80  LEU E N   
11729 C CA  . LEU E 80  ? 0.7337 1.4629 1.1990 0.0832  -0.2038 0.3141  80  LEU E CA  
11730 C C   . LEU E 80  ? 0.7133 1.5078 1.2849 0.0874  -0.1917 0.3226  80  LEU E C   
11731 O O   . LEU E 80  ? 0.6917 1.5160 1.3049 0.1193  -0.1892 0.3421  80  LEU E O   
11732 C CB  . LEU E 80  ? 0.7545 1.4076 1.1636 0.0966  -0.1622 0.3175  80  LEU E CB  
11733 C CG  . LEU E 80  ? 0.7795 1.3625 1.1042 0.0812  -0.1567 0.3009  80  LEU E CG  
11734 C CD1 . LEU E 80  ? 0.8096 1.3863 1.1444 0.0466  -0.1534 0.2802  80  LEU E CD1 
11735 C CD2 . LEU E 80  ? 0.7711 1.3469 1.0393 0.0836  -0.1878 0.2998  80  LEU E CD2 
11736 N N   . SER E 81  ? 0.6447 1.4614 1.2670 0.0551  -0.1823 0.3081  81  SER E N   
11737 C CA  . SER E 81  ? 0.6265 1.5051 1.3559 0.0531  -0.1600 0.3153  81  SER E CA  
11738 C C   . SER E 81  ? 0.6688 1.5060 1.3930 0.0327  -0.1079 0.3128  81  SER E C   
11739 O O   . SER E 81  ? 0.7060 1.4862 1.3716 0.0081  -0.1060 0.3004  81  SER E O   
11740 C CB  . SER E 81  ? 0.6046 1.5683 1.4248 0.0299  -0.2025 0.3044  81  SER E CB  
11741 O OG  . SER E 81  ? 0.6258 1.5686 1.4229 -0.0104 -0.2225 0.2792  81  SER E OG  
11742 N N   . GLY E 82  ? 0.6583 1.5234 1.4408 0.0458  -0.0647 0.3257  82  GLY E N   
11743 C CA  . GLY E 82  ? 0.7039 1.5300 1.4693 0.0333  -0.0094 0.3299  82  GLY E CA  
11744 C C   . GLY E 82  ? 0.7129 1.5410 1.4826 0.0707  0.0371  0.3416  82  GLY E C   
11745 O O   . GLY E 82  ? 0.6718 1.5528 1.5010 0.0999  0.0299  0.3469  82  GLY E O   
11746 N N   . GLN E 83  ? 0.6933 1.4617 1.3970 0.0712  0.0825  0.3441  83  GLN E N   
11747 C CA  . GLN E 83  ? 0.7150 1.4799 1.4109 0.1043  0.1324  0.3488  83  GLN E CA  
11748 C C   . GLN E 83  ? 0.7782 1.4513 1.3516 0.1228  0.1407  0.3411  83  GLN E C   
11749 O O   . GLN E 83  ? 0.8167 1.4304 1.3172 0.1021  0.1277  0.3375  83  GLN E O   
11750 C CB  . GLN E 83  ? 0.7244 1.5214 1.4684 0.0862  0.1884  0.3600  83  GLN E CB  
11751 C CG  . GLN E 83  ? 0.6705 1.5457 1.5332 0.0505  0.1768  0.3658  83  GLN E CG  
11752 C CD  . GLN E 83  ? 0.6387 1.6067 1.6205 0.0645  0.2121  0.3729  83  GLN E CD  
11753 O OE1 . GLN E 83  ? 0.6525 1.6207 1.6205 0.0990  0.2567  0.3739  83  GLN E OE1 
11754 N NE2 . GLN E 83  ? 0.6020 1.6519 1.7064 0.0378  0.1926  0.3745  83  GLN E NE2 
11755 N N   . LEU E 84  ? 0.7224 1.3847 1.2798 0.1628  0.1605  0.3359  84  LEU E N   
11756 C CA  . LEU E 84  ? 0.7861 1.3663 1.2365 0.1805  0.1707  0.3241  84  LEU E CA  
11757 C C   . LEU E 84  ? 0.8476 1.3969 1.2418 0.1673  0.2147  0.3270  84  LEU E C   
11758 O O   . LEU E 84  ? 0.8347 1.4279 1.2785 0.1496  0.2483  0.3406  84  LEU E O   
11759 C CB  . LEU E 84  ? 0.7836 1.3590 1.2391 0.2258  0.1833  0.3134  84  LEU E CB  
11760 C CG  . LEU E 84  ? 0.7417 1.3002 1.2012 0.2472  0.1411  0.3111  84  LEU E CG  
11761 C CD1 . LEU E 84  ? 0.6691 1.2944 1.2129 0.2394  0.1045  0.3271  84  LEU E CD1 
11762 C CD2 . LEU E 84  ? 0.7531 1.2965 1.2207 0.2915  0.1633  0.2985  84  LEU E CD2 
11763 N N   . VAL E 85  ? 0.8111 1.2845 1.1017 0.1754  0.2135  0.3162  85  VAL E N   
11764 C CA  . VAL E 85  ? 0.8611 1.2939 1.0776 0.1657  0.2462  0.3216  85  VAL E CA  
11765 C C   . VAL E 85  ? 0.9130 1.3068 1.0559 0.2022  0.2711  0.3028  85  VAL E C   
11766 O O   . VAL E 85  ? 0.9260 1.2921 1.0503 0.2260  0.2470  0.2824  85  VAL E O   
11767 C CB  . VAL E 85  ? 0.8723 1.2484 1.0295 0.1385  0.2127  0.3245  85  VAL E CB  
11768 C CG1 . VAL E 85  ? 0.9128 1.2358 0.9799 0.1368  0.2389  0.3316  85  VAL E CG1 
11769 C CG2 . VAL E 85  ? 0.8320 1.2446 1.0601 0.1012  0.1952  0.3384  85  VAL E CG2 
11770 N N   . MET E 86  ? 1.0387 1.4296 1.1388 0.2058  0.3200  0.3094  86  MET E N   
11771 C CA  . MET E 86  ? 1.0945 1.4467 1.1103 0.2402  0.3432  0.2867  86  MET E CA  
11772 C C   . MET E 86  ? 1.1355 1.4086 1.0537 0.2440  0.3034  0.2696  86  MET E C   
11773 O O   . MET E 86  ? 1.1793 1.4179 1.0415 0.2740  0.3041  0.2407  86  MET E O   
11774 C CB  . MET E 86  ? 1.1198 1.4850 1.0945 0.2404  0.4046  0.3014  86  MET E CB  
11775 C CG  . MET E 86  ? 1.1411 1.4601 1.0349 0.2134  0.4054  0.3270  86  MET E CG  
11776 S SD  . MET E 86  ? 1.2008 1.4278 0.9391 0.2346  0.3810  0.3059  86  MET E SD  
11777 C CE  . MET E 86  ? 1.2210 1.4197 0.8783 0.2118  0.4124  0.3491  86  MET E CE  
11778 N N   . GLN E 87  ? 1.0829 1.3283 0.9860 0.2150  0.2682  0.2834  87  GLN E N   
11779 C CA  . GLN E 87  ? 1.1017 1.2790 0.9230 0.2176  0.2309  0.2684  87  GLN E CA  
11780 C C   . GLN E 87  ? 1.1087 1.2687 0.9443 0.2355  0.1957  0.2402  87  GLN E C   
11781 O O   . GLN E 87  ? 1.1259 1.2337 0.9003 0.2427  0.1692  0.2212  87  GLN E O   
11782 C CB  . GLN E 87  ? 1.0589 1.2171 0.8794 0.1838  0.2030  0.2883  87  GLN E CB  
11783 C CG  . GLN E 87  ? 1.0760 1.2010 0.8263 0.1730  0.2221  0.3105  87  GLN E CG  
11784 C CD  . GLN E 87  ? 1.0688 1.2365 0.8692 0.1501  0.2637  0.3436  87  GLN E CD  
11785 O OE1 . GLN E 87  ? 1.0675 1.2918 0.9273 0.1564  0.2976  0.3450  87  GLN E OE1 
11786 N NE2 . GLN E 87  ? 1.0616 1.2016 0.8453 0.1236  0.2619  0.3706  87  GLN E NE2 
11787 N N   . LEU E 88  ? 1.0588 1.2615 0.9774 0.2428  0.1945  0.2393  88  LEU E N   
11788 C CA  . LEU E 88  ? 1.0646 1.2492 1.0033 0.2592  0.1652  0.2200  88  LEU E CA  
11789 C C   . LEU E 88  ? 1.1185 1.2626 1.0080 0.2912  0.1745  0.1873  88  LEU E C   
11790 O O   . LEU E 88  ? 1.1016 1.2186 1.0044 0.3026  0.1498  0.1701  88  LEU E O   
11791 C CB  . LEU E 88  ? 0.9908 1.2312 1.0269 0.2647  0.1650  0.2318  88  LEU E CB  
11792 C CG  . LEU E 88  ? 0.9202 1.1993 1.0086 0.2347  0.1416  0.2560  88  LEU E CG  
11793 C CD1 . LEU E 88  ? 0.8410 1.1760 1.0205 0.2461  0.1351  0.2666  88  LEU E CD1 
11794 C CD2 . LEU E 88  ? 0.8757 1.1100 0.9231 0.2197  0.1021  0.2510  88  LEU E CD2 
11795 N N   . GLY E 89  ? 1.1265 1.2658 0.9607 0.3054  0.2104  0.1778  89  GLY E N   
11796 C CA  . GLY E 89  ? 1.1804 1.2774 0.9525 0.3349  0.2158  0.1399  89  GLY E CA  
11797 C C   . GLY E 89  ? 1.2223 1.2611 0.9027 0.3299  0.1862  0.1242  89  GLY E C   
11798 O O   . GLY E 89  ? 1.2702 1.2732 0.8903 0.3530  0.1858  0.0887  89  GLY E O   
11799 N N   . GLN E 90  ? 1.2437 1.2731 0.9156 0.3016  0.1588  0.1467  90  GLN E N   
11800 C CA  . GLN E 90  ? 1.2489 1.2285 0.8464 0.2969  0.1263  0.1351  90  GLN E CA  
11801 C C   . GLN E 90  ? 1.2386 1.1912 0.8660 0.2929  0.0819  0.1152  90  GLN E C   
11802 O O   . GLN E 90  ? 1.2113 1.1323 0.8007 0.2845  0.0499  0.1086  90  GLN E O   
11803 C CB  . GLN E 90  ? 1.1894 1.1703 0.7648 0.2709  0.1232  0.1699  90  GLN E CB  
11804 C CG  . GLN E 90  ? 1.2239 1.1958 0.7163 0.2773  0.1536  0.1836  90  GLN E CG  
11805 C CD  . GLN E 90  ? 1.2242 1.2462 0.7538 0.2728  0.2063  0.2098  90  GLN E CD  
11806 O OE1 . GLN E 90  ? 1.1791 1.2251 0.7539 0.2459  0.2144  0.2435  90  GLN E OE1 
11807 N NE2 . GLN E 90  ? 1.2714 1.3110 0.7885 0.2990  0.2429  0.1911  90  GLN E NE2 
11808 N N   . LEU E 91  ? 1.2509 1.2164 0.9493 0.2987  0.0802  0.1084  91  LEU E N   
11809 C CA  . LEU E 91  ? 1.2031 1.1432 0.9336 0.2934  0.0448  0.0941  91  LEU E CA  
11810 C C   . LEU E 91  ? 1.2570 1.1671 0.9911 0.3188  0.0449  0.0562  91  LEU E C   
11811 O O   . LEU E 91  ? 1.2029 1.1221 1.0012 0.3284  0.0530  0.0578  91  LEU E O   
11812 C CB  . LEU E 91  ? 1.0803 1.0531 0.8878 0.2763  0.0386  0.1230  91  LEU E CB  
11813 C CG  . LEU E 91  ? 1.0195 1.0276 0.8316 0.2534  0.0442  0.1553  91  LEU E CG  
11814 C CD1 . LEU E 91  ? 0.9302 0.9812 0.8151 0.2425  0.0420  0.1800  91  LEU E CD1 
11815 C CD2 . LEU E 91  ? 0.9731 0.9568 0.7461 0.2344  0.0182  0.1554  91  LEU E CD2 
11816 N N   . PRO E 92  ? 1.2299 1.1023 0.8975 0.3312  0.0331  0.0208  92  PRO E N   
11817 C CA  . PRO E 92  ? 1.2483 1.0906 0.9158 0.3570  0.0351  -0.0232 92  PRO E CA  
11818 C C   . PRO E 92  ? 1.1927 1.0118 0.9362 0.3523  0.0126  -0.0337 92  PRO E C   
11819 O O   . PRO E 92  ? 1.1891 0.9905 0.9672 0.3726  0.0227  -0.0573 92  PRO E O   
11820 C CB  . PRO E 92  ? 1.3103 1.1192 0.8840 0.3657  0.0160  -0.0580 92  PRO E CB  
11821 C CG  . PRO E 92  ? 1.2991 1.1108 0.8524 0.3411  -0.0104 -0.0326 92  PRO E CG  
11822 C CD  . PRO E 92  ? 1.2595 1.1132 0.8511 0.3235  0.0127  0.0174  92  PRO E CD  
11823 N N   . ASN E 93  ? 1.2241 1.0414 0.9969 0.3266  -0.0149 -0.0162 93  ASN E N   
11824 C CA  . ASN E 93  ? 1.1643 0.9599 1.0077 0.3182  -0.0326 -0.0197 93  ASN E CA  
11825 C C   . ASN E 93  ? 1.0757 0.9019 0.9858 0.3086  -0.0209 0.0254  93  ASN E C   
11826 O O   . ASN E 93  ? 1.0271 0.8383 0.9923 0.2987  -0.0326 0.0345  93  ASN E O   
11827 C CB  . ASN E 93  ? 1.1545 0.9324 0.9930 0.2971  -0.0674 -0.0310 93  ASN E CB  
11828 C CG  . ASN E 93  ? 1.2276 0.9684 1.0216 0.3089  -0.0896 -0.0833 93  ASN E CG  
11829 O OD1 . ASN E 93  ? 1.2641 1.0046 1.0031 0.3048  -0.1101 -0.0930 93  ASN E OD1 
11830 N ND2 . ASN E 93  ? 1.2442 0.9519 1.0628 0.3251  -0.0885 -0.1188 93  ASN E ND2 
11831 N N   . LEU E 94  ? 1.1659 1.0355 1.0726 0.3110  0.0013  0.0545  94  LEU E N   
11832 C CA  . LEU E 94  ? 1.0799 0.9849 1.0455 0.3041  0.0071  0.0956  94  LEU E CA  
11833 C C   . LEU E 94  ? 1.0692 0.9585 1.0952 0.3256  0.0149  0.0949  94  LEU E C   
11834 O O   . LEU E 94  ? 1.1056 0.9979 1.1384 0.3520  0.0366  0.0800  94  LEU E O   
11835 C CB  . LEU E 94  ? 1.0695 1.0266 1.0261 0.3028  0.0275  0.1198  94  LEU E CB  
11836 C CG  . LEU E 94  ? 0.9825 0.9860 0.9961 0.2953  0.0280  0.1596  94  LEU E CG  
11837 C CD1 . LEU E 94  ? 0.9106 0.9122 0.9330 0.2704  0.0024  0.1784  94  LEU E CD1 
11838 C CD2 . LEU E 94  ? 0.9820 1.0368 0.9917 0.2895  0.0458  0.1768  94  LEU E CD2 
11839 N N   . GLN E 95  ? 1.0651 0.9371 1.1368 0.3154  -0.0004 0.1125  95  GLN E N   
11840 C CA  . GLN E 95  ? 1.0574 0.9046 1.1911 0.3348  0.0038  0.1183  95  GLN E CA  
11841 C C   . GLN E 95  ? 0.9916 0.8805 1.1720 0.3408  0.0086  0.1661  95  GLN E C   
11842 O O   . GLN E 95  ? 0.9924 0.8742 1.2221 0.3676  0.0180  0.1709  95  GLN E O   
11843 C CB  . GLN E 95  ? 1.0576 0.8547 1.2184 0.3202  -0.0141 0.1135  95  GLN E CB  
11844 C CG  . GLN E 95  ? 1.1221 0.8778 1.2512 0.3161  -0.0257 0.0614  95  GLN E CG  
11845 C CD  . GLN E 95  ? 1.1192 0.8314 1.2918 0.2980  -0.0423 0.0567  95  GLN E CD  
11846 O OE1 . GLN E 95  ? 1.0714 0.7834 1.2900 0.2869  -0.0414 0.0975  95  GLN E OE1 
11847 N NE2 . GLN E 95  ? 1.1661 0.8429 1.3247 0.2943  -0.0579 0.0077  95  GLN E NE2 
11848 N N   . TYR E 96  ? 0.9879 0.9200 1.1560 0.3184  -0.0004 0.1992  96  TYR E N   
11849 C CA  . TYR E 96  ? 0.9277 0.9045 1.1340 0.3225  -0.0035 0.2432  96  TYR E CA  
11850 C C   . TYR E 96  ? 0.9016 0.9394 1.0839 0.3093  -0.0017 0.2522  96  TYR E C   
11851 O O   . TYR E 96  ? 0.8889 0.9329 1.0289 0.2831  -0.0103 0.2488  96  TYR E O   
11852 C CB  . TYR E 96  ? 0.8917 0.8565 1.1104 0.3061  -0.0205 0.2777  96  TYR E CB  
11853 C CG  . TYR E 96  ? 0.9231 0.8259 1.1791 0.3160  -0.0208 0.2775  96  TYR E CG  
11854 C CD1 . TYR E 96  ? 0.9506 0.8026 1.1950 0.3032  -0.0225 0.2447  96  TYR E CD1 
11855 C CD2 . TYR E 96  ? 0.9345 0.8287 1.2439 0.3382  -0.0216 0.3105  96  TYR E CD2 
11856 C CE1 . TYR E 96  ? 0.9780 0.7709 1.2670 0.3087  -0.0229 0.2427  96  TYR E CE1 
11857 C CE2 . TYR E 96  ? 0.9689 0.7990 1.3189 0.3461  -0.0210 0.3127  96  TYR E CE2 
11858 C CZ  . TYR E 96  ? 0.9865 0.7653 1.3281 0.3295  -0.0206 0.2777  96  TYR E CZ  
11859 O OH  . TYR E 96  ? 1.0218 0.7345 1.4141 0.3340  -0.0203 0.2785  96  TYR E OH  
11860 N N   . LEU E 97  ? 0.8829 0.9658 1.1009 0.3271  0.0094  0.2628  97  LEU E N   
11861 C CA  . LEU E 97  ? 0.8610 1.0058 1.0750 0.3134  0.0119  0.2729  97  LEU E CA  
11862 C C   . LEU E 97  ? 0.8042 0.9995 1.0712 0.3190  -0.0042 0.3102  97  LEU E C   
11863 O O   . LEU E 97  ? 0.8039 1.0227 1.1280 0.3466  0.0035  0.3183  97  LEU E O   
11864 C CB  . LEU E 97  ? 0.9132 1.0758 1.1268 0.3272  0.0420  0.2504  97  LEU E CB  
11865 C CG  . LEU E 97  ? 0.9125 1.1272 1.1169 0.3066  0.0506  0.2567  97  LEU E CG  
11866 C CD1 . LEU E 97  ? 0.9124 1.1052 1.0552 0.2749  0.0364  0.2518  97  LEU E CD1 
11867 C CD2 . LEU E 97  ? 0.9761 1.2047 1.1786 0.3219  0.0880  0.2383  97  LEU E CD2 
11868 N N   . GLU E 98  ? 0.8506 1.0643 1.0987 0.2954  -0.0278 0.3310  98  GLU E N   
11869 C CA  . GLU E 98  ? 0.8381 1.0939 1.1195 0.2984  -0.0504 0.3648  98  GLU E CA  
11870 C C   . GLU E 98  ? 0.8086 1.1317 1.0946 0.2795  -0.0620 0.3695  98  GLU E C   
11871 O O   . GLU E 98  ? 0.8003 1.1279 1.0441 0.2515  -0.0775 0.3682  98  GLU E O   
11872 C CB  . GLU E 98  ? 0.8545 1.0715 1.0996 0.2805  -0.0663 0.3748  98  GLU E CB  
11873 C CG  . GLU E 98  ? 0.8813 1.0288 1.1253 0.2920  -0.0554 0.3691  98  GLU E CG  
11874 C CD  . GLU E 98  ? 0.9083 1.0352 1.2030 0.3200  -0.0520 0.3774  98  GLU E CD  
11875 O OE1 . GLU E 98  ? 0.9038 1.0738 1.2370 0.3345  -0.0560 0.3859  98  GLU E OE1 
11876 O OE2 . GLU E 98  ? 0.9364 1.0033 1.2385 0.3276  -0.0464 0.3743  98  GLU E OE2 
11877 N N   . LEU E 99  ? 0.7626 1.1368 1.1044 0.2922  -0.0527 0.3692  99  LEU E N   
11878 C CA  . LEU E 99  ? 0.7367 1.1791 1.1029 0.2727  -0.0648 0.3722  99  LEU E CA  
11879 C C   . LEU E 99  ? 0.7334 1.2297 1.1605 0.2849  -0.0863 0.3901  99  LEU E C   
11880 O O   . LEU E 99  ? 0.7113 1.2760 1.1890 0.2773  -0.0932 0.3915  99  LEU E O   
11881 C CB  . LEU E 99  ? 0.7545 1.2115 1.1333 0.2645  -0.0322 0.3501  99  LEU E CB  
11882 C CG  . LEU E 99  ? 0.7874 1.2015 1.0966 0.2369  -0.0207 0.3292  99  LEU E CG  
11883 C CD1 . LEU E 99  ? 0.8338 1.1854 1.1033 0.2533  0.0053  0.3105  99  LEU E CD1 
11884 C CD2 . LEU E 99  ? 0.8088 1.2634 1.1390 0.2146  -0.0070 0.3236  99  LEU E CD2 
11885 N N   . TYR E 100 ? 0.7808 1.2418 1.2024 0.2992  -0.0974 0.3996  100 TYR E N   
11886 C CA  . TYR E 100 ? 0.7924 1.2900 1.2631 0.3134  -0.1186 0.4130  100 TYR E CA  
11887 C C   . TYR E 100 ? 0.7909 1.3309 1.2425 0.2897  -0.1552 0.4189  100 TYR E C   
11888 O O   . TYR E 100 ? 0.7890 1.3162 1.1799 0.2632  -0.1640 0.4132  100 TYR E O   
11889 C CB  . TYR E 100 ? 0.8314 1.2720 1.2946 0.3348  -0.1219 0.4255  100 TYR E CB  
11890 C CG  . TYR E 100 ? 0.8550 1.2400 1.2431 0.3170  -0.1325 0.4347  100 TYR E CG  
11891 C CD1 . TYR E 100 ? 0.8822 1.2806 1.2372 0.3053  -0.1621 0.4516  100 TYR E CD1 
11892 C CD2 . TYR E 100 ? 0.8555 1.1774 1.2088 0.3135  -0.1116 0.4257  100 TYR E CD2 
11893 C CE1 . TYR E 100 ? 0.9086 1.2623 1.1986 0.2903  -0.1650 0.4614  100 TYR E CE1 
11894 C CE2 . TYR E 100 ? 0.8768 1.1551 1.1736 0.2963  -0.1174 0.4347  100 TYR E CE2 
11895 C CZ  . TYR E 100 ? 0.9033 1.1992 1.1690 0.2847  -0.1412 0.4537  100 TYR E CZ  
11896 O OH  . TYR E 100 ? 0.9297 1.1883 1.1417 0.2690  -0.1410 0.4647  100 TYR E OH  
11897 N N   . SER E 101 ? 0.7516 1.3434 1.2583 0.3016  -0.1774 0.4268  101 SER E N   
11898 C CA  . SER E 101 ? 0.7726 1.4060 1.2657 0.2861  -0.2182 0.4301  101 SER E CA  
11899 C C   . SER E 101 ? 0.7310 1.4025 1.2138 0.2526  -0.2237 0.4119  101 SER E C   
11900 O O   . SER E 101 ? 0.7356 1.3921 1.1511 0.2304  -0.2402 0.4059  101 SER E O   
11901 C CB  . SER E 101 ? 0.8213 1.4062 1.2382 0.2855  -0.2376 0.4458  101 SER E CB  
11902 O OG  . SER E 101 ? 0.8704 1.4279 1.3089 0.3160  -0.2394 0.4663  101 SER E OG  
11903 N N   . ASN E 102 ? 0.7820 1.5041 1.3374 0.2494  -0.2073 0.4026  102 ASN E N   
11904 C CA  . ASN E 102 ? 0.7525 1.5179 1.3213 0.2170  -0.2123 0.3873  102 ASN E CA  
11905 C C   . ASN E 102 ? 0.7356 1.5816 1.4135 0.2170  -0.2122 0.3827  102 ASN E C   
11906 O O   . ASN E 102 ? 0.7591 1.6272 1.4952 0.2442  -0.2107 0.3897  102 ASN E O   
11907 C CB  . ASN E 102 ? 0.7310 1.4605 1.2662 0.2051  -0.1781 0.3822  102 ASN E CB  
11908 C CG  . ASN E 102 ? 0.7514 1.4147 1.1847 0.1932  -0.1852 0.3784  102 ASN E CG  
11909 O OD1 . ASN E 102 ? 0.7594 1.4299 1.1536 0.1694  -0.2117 0.3676  102 ASN E OD1 
11910 N ND2 . ASN E 102 ? 0.7635 1.3629 1.1574 0.2095  -0.1604 0.3833  102 ASN E ND2 
11911 N N   . ASN E 103 ? 0.6719 1.5620 1.3839 0.1848  -0.2132 0.3697  103 ASN E N   
11912 C CA  . ASN E 103 ? 0.6651 1.6335 1.4888 0.1756  -0.2079 0.3627  103 ASN E CA  
11913 C C   . ASN E 103 ? 0.6268 1.6057 1.4938 0.1659  -0.1533 0.3649  103 ASN E C   
11914 O O   . ASN E 103 ? 0.6173 1.6476 1.5545 0.1363  -0.1438 0.3571  103 ASN E O   
11915 C CB  . ASN E 103 ? 0.6770 1.6924 1.5218 0.1419  -0.2526 0.3436  103 ASN E CB  
11916 C CG  . ASN E 103 ? 0.6862 1.7838 1.6533 0.1356  -0.2567 0.3341  103 ASN E CG  
11917 O OD1 . ASN E 103 ? 0.7050 1.8278 1.7271 0.1661  -0.2498 0.3416  103 ASN E OD1 
11918 N ND2 . ASN E 103 ? 0.6781 1.8160 1.6933 0.0949  -0.2674 0.3151  103 ASN E ND2 
11919 N N   . ILE E 104 ? 0.6879 1.6070 1.5050 0.1884  -0.1141 0.3715  104 ILE E N   
11920 C CA  . ILE E 104 ? 0.7185 1.6067 1.5254 0.1770  -0.0563 0.3613  104 ILE E CA  
11921 C C   . ILE E 104 ? 0.7021 1.6563 1.6156 0.1959  -0.0203 0.3659  104 ILE E C   
11922 O O   . ILE E 104 ? 0.6894 1.6735 1.6539 0.2352  -0.0257 0.3757  104 ILE E O   
11923 C CB  . ILE E 104 ? 0.7635 1.5565 1.4661 0.1934  -0.0314 0.3577  104 ILE E CB  
11924 C CG1 . ILE E 104 ? 0.7611 1.5042 1.3791 0.1870  -0.0719 0.3581  104 ILE E CG1 
11925 C CG2 . ILE E 104 ? 0.8198 1.5712 1.4798 0.1719  0.0134  0.3463  104 ILE E CG2 
11926 C CD1 . ILE E 104 ? 0.7922 1.4490 1.3236 0.2034  -0.0539 0.3545  104 ILE E CD1 
11927 N N   . THR E 105 ? 0.6260 1.6029 1.5771 0.1689  0.0188  0.3604  105 THR E N   
11928 C CA  . THR E 105 ? 0.6168 1.6685 1.6792 0.1798  0.0594  0.3640  105 THR E CA  
11929 C C   . THR E 105 ? 0.6614 1.6694 1.6772 0.1828  0.1306  0.3606  105 THR E C   
11930 O O   . THR E 105 ? 0.7071 1.6285 1.6077 0.1768  0.1413  0.3555  105 THR E O   
11931 C CB  . THR E 105 ? 0.5959 1.7333 1.7670 0.1416  0.0425  0.3638  105 THR E CB  
11932 O OG1 . THR E 105 ? 0.6156 1.8102 1.8818 0.1495  0.0835  0.3599  105 THR E OG1 
11933 C CG2 . THR E 105 ? 0.6235 1.7191 1.7474 0.0908  0.0532  0.3581  105 THR E CG2 
11934 N N   . GLY E 106 ? 0.6386 1.7108 1.7444 0.1934  0.1797  0.3630  106 GLY E N   
11935 C CA  . GLY E 106 ? 0.6843 1.7238 1.7429 0.2010  0.2512  0.3601  106 GLY E CA  
11936 C C   . GLY E 106 ? 0.7006 1.7116 1.7280 0.2549  0.2749  0.3487  106 GLY E C   
11937 O O   . GLY E 106 ? 0.6705 1.7073 1.7517 0.2903  0.2478  0.3472  106 GLY E O   
11938 N N   . THR E 107 ? 0.7171 1.6732 1.6572 0.2617  0.3272  0.3403  107 THR E N   
11939 C CA  . THR E 107 ? 0.7487 1.6705 1.6482 0.3101  0.3598  0.3214  107 THR E CA  
11940 C C   . THR E 107 ? 0.8049 1.6192 1.5696 0.3185  0.3362  0.3083  107 THR E C   
11941 O O   . THR E 107 ? 0.8281 1.5907 1.5186 0.2868  0.3034  0.3145  107 THR E O   
11942 C CB  . THR E 107 ? 0.7884 1.7369 1.6896 0.3163  0.4406  0.3165  107 THR E CB  
11943 O OG1 . THR E 107 ? 0.8195 1.7608 1.7194 0.3695  0.4724  0.2920  107 THR E OG1 
11944 C CG2 . THR E 107 ? 0.8462 1.7247 1.6188 0.2879  0.4644  0.3206  107 THR E CG2 
11945 N N   . ILE E 108 ? 0.8130 1.5971 1.5582 0.3636  0.3522  0.2873  108 ILE E N   
11946 C CA  . ILE E 108 ? 0.8660 1.5518 1.5022 0.3780  0.3304  0.2693  108 ILE E CA  
11947 C C   . ILE E 108 ? 0.9453 1.5862 1.4815 0.3817  0.3805  0.2497  108 ILE E C   
11948 O O   . ILE E 108 ? 0.9562 1.6308 1.5165 0.4060  0.4347  0.2366  108 ILE E O   
11949 C CB  . ILE E 108 ? 0.8411 1.5194 1.5288 0.4262  0.3158  0.2564  108 ILE E CB  
11950 C CG1 . ILE E 108 ? 0.7747 1.4688 1.5204 0.4241  0.2540  0.2797  108 ILE E CG1 
11951 C CG2 . ILE E 108 ? 0.9056 1.4865 1.4963 0.4500  0.3155  0.2266  108 ILE E CG2 
11952 C CD1 . ILE E 108 ? 0.7120 1.4968 1.5491 0.3981  0.2361  0.3051  108 ILE E CD1 
11953 N N   . PRO E 109 ? 0.9320 1.5033 1.3572 0.3580  0.3642  0.2484  109 PRO E N   
11954 C CA  . PRO E 109 ? 1.0072 1.5360 1.3273 0.3609  0.4047  0.2337  109 PRO E CA  
11955 C C   . PRO E 109 ? 1.0517 1.5460 1.3317 0.4066  0.4288  0.1952  109 PRO E C   
11956 O O   . PRO E 109 ? 1.0672 1.5050 1.3214 0.4252  0.3946  0.1732  109 PRO E O   
11957 C CB  . PRO E 109 ? 1.0430 1.5020 1.2716 0.3329  0.3616  0.2384  109 PRO E CB  
11958 C CG  . PRO E 109 ? 0.9827 1.4487 1.2743 0.3191  0.2998  0.2517  109 PRO E CG  
11959 C CD  . PRO E 109 ? 0.9325 1.4439 1.3150 0.3487  0.3051  0.2479  109 PRO E CD  
11960 N N   . GLU E 110 ? 1.0647 1.5890 1.3307 0.4232  0.4922  0.1848  110 GLU E N   
11961 C CA  . GLU E 110 ? 1.1227 1.6006 1.3226 0.4653  0.5130  0.1396  110 GLU E CA  
11962 C C   . GLU E 110 ? 1.1925 1.5813 1.2578 0.4573  0.4830  0.1227  110 GLU E C   
11963 O O   . GLU E 110 ? 1.2359 1.5740 1.2525 0.4878  0.4782  0.0810  110 GLU E O   
11964 C CB  . GLU E 110 ? 1.1855 1.7112 1.3805 0.4867  0.5896  0.1280  110 GLU E CB  
11965 C CG  . GLU E 110 ? 1.2379 1.7592 1.3374 0.4629  0.6257  0.1459  110 GLU E CG  
11966 C CD  . GLU E 110 ? 1.3267 1.8907 1.4160 0.4856  0.7006  0.1311  110 GLU E CD  
11967 O OE1 . GLU E 110 ? 1.3243 1.9410 1.5226 0.5028  0.7168  0.1165  110 GLU E OE1 
11968 O OE2 . GLU E 110 ? 1.4092 1.9422 1.3800 0.4748  0.7258  0.1310  110 GLU E OE2 
11969 N N   . GLN E 111 ? 1.1797 1.5478 1.1977 0.4171  0.4553  0.1519  111 GLN E N   
11970 C CA  . GLN E 111 ? 1.2350 1.5238 1.1425 0.4084  0.4171  0.1385  111 GLN E CA  
11971 C C   . GLN E 111 ? 1.2217 1.4671 1.1544 0.4105  0.3584  0.1245  111 GLN E C   
11972 O O   . GLN E 111 ? 1.2680 1.4499 1.1217 0.4098  0.3284  0.1040  111 GLN E O   
11973 C CB  . GLN E 111 ? 1.2371 1.5204 1.0997 0.3677  0.4085  0.1757  111 GLN E CB  
11974 C CG  . GLN E 111 ? 1.2705 1.5636 1.0590 0.3656  0.4623  0.1884  111 GLN E CG  
11975 C CD  . GLN E 111 ? 1.3287 1.6048 1.0411 0.4064  0.4991  0.1482  111 GLN E CD  
11976 O OE1 . GLN E 111 ? 1.3336 1.6592 1.0667 0.4229  0.5593  0.1469  111 GLN E OE1 
11977 N NE2 . GLN E 111 ? 1.3760 1.5842 1.0005 0.4224  0.4638  0.1126  111 GLN E NE2 
11978 N N   . LEU E 112 ? 1.1369 1.4162 1.1772 0.4125  0.3407  0.1373  112 LEU E N   
11979 C CA  . LEU E 112 ? 1.1029 1.3390 1.1658 0.4185  0.2928  0.1265  112 LEU E CA  
11980 C C   . LEU E 112 ? 1.1642 1.3504 1.2017 0.4556  0.2980  0.0804  112 LEU E C   
11981 O O   . LEU E 112 ? 1.1518 1.2875 1.1934 0.4580  0.2603  0.0678  112 LEU E O   
11982 C CB  . LEU E 112 ? 1.0409 1.3254 1.2179 0.4172  0.2744  0.1541  112 LEU E CB  
11983 C CG  . LEU E 112 ? 0.9740 1.2511 1.1583 0.3837  0.2254  0.1820  112 LEU E CG  
11984 C CD1 . LEU E 112 ? 0.9656 1.2373 1.0846 0.3492  0.2248  0.1937  112 LEU E CD1 
11985 C CD2 . LEU E 112 ? 0.9246 1.2647 1.2105 0.3798  0.2098  0.2130  112 LEU E CD2 
11986 N N   . GLY E 113 ? 1.2129 1.4127 1.2289 0.4841  0.3457  0.0536  113 GLY E N   
11987 C CA  . GLY E 113 ? 1.2613 1.4099 1.2418 0.5196  0.3517  0.0008  113 GLY E CA  
11988 C C   . GLY E 113 ? 1.3290 1.4082 1.1960 0.5115  0.3253  -0.0283 113 GLY E C   
11989 O O   . GLY E 113 ? 1.3694 1.3992 1.2075 0.5374  0.3202  -0.0777 113 GLY E O   
11990 N N   . ASN E 114 ? 1.3623 1.4368 1.1699 0.4774  0.3062  -0.0014 114 ASN E N   
11991 C CA  . ASN E 114 ? 1.4203 1.4352 1.1260 0.4697  0.2756  -0.0254 114 ASN E CA  
11992 C C   . ASN E 114 ? 1.3997 1.3725 1.1343 0.4510  0.2188  -0.0249 114 ASN E C   
11993 O O   . ASN E 114 ? 1.4410 1.3662 1.1085 0.4457  0.1880  -0.0492 114 ASN E O   
11994 C CB  . ASN E 114 ? 1.4439 1.4715 1.0683 0.4463  0.2854  0.0042  114 ASN E CB  
11995 C CG  . ASN E 114 ? 1.4762 1.5315 1.0396 0.4652  0.3437  -0.0009 114 ASN E CG  
11996 O OD1 . ASN E 114 ? 1.5007 1.5509 0.9744 0.4537  0.3541  0.0162  114 ASN E OD1 
11997 N ND2 . ASN E 114 ? 1.4729 1.5579 1.0857 0.4953  0.3840  -0.0224 114 ASN E ND2 
11998 N N   . LEU E 115 ? 1.5204 1.2172 0.9720 0.3758  0.1425  0.0526  115 LEU E N   
11999 C CA  . LEU E 115 ? 1.4707 1.1744 0.9900 0.3532  0.1067  0.0293  115 LEU E CA  
12000 C C   . LEU E 115 ? 1.4735 1.1362 0.9873 0.3735  0.0998  -0.0058 115 LEU E C   
12001 O O   . LEU E 115 ? 1.4337 1.1129 0.9923 0.3760  0.1214  0.0016  115 LEU E O   
12002 C CB  . LEU E 115 ? 1.3924 1.1631 1.0000 0.3240  0.1208  0.0585  115 LEU E CB  
12003 C CG  . LEU E 115 ? 1.3736 1.1861 0.9968 0.3005  0.1267  0.0894  115 LEU E CG  
12004 C CD1 . LEU E 115 ? 1.2914 1.1663 0.9970 0.2738  0.1325  0.1108  115 LEU E CD1 
12005 C CD2 . LEU E 115 ? 1.3873 1.1674 0.9831 0.2890  0.0894  0.0715  115 LEU E CD2 
12006 N N   . THR E 116 ? 1.5616 1.1651 1.0173 0.3903  0.0660  -0.0461 116 THR E N   
12007 C CA  . THR E 116 ? 1.5781 1.1327 1.0160 0.4128  0.0585  -0.0852 116 THR E CA  
12008 C C   . THR E 116 ? 1.5145 1.0782 1.0455 0.3887  0.0511  -0.1016 116 THR E C   
12009 O O   . THR E 116 ? 1.5124 1.0531 1.0545 0.4018  0.0684  -0.1118 116 THR E O   
12010 C CB  . THR E 116 ? 1.6418 1.1332 1.0017 0.4339  0.0128  -0.1302 116 THR E CB  
12011 O OG1 . THR E 116 ? 1.7155 1.1804 0.9650 0.4627  0.0297  -0.1119 116 THR E OG1 
12012 C CG2 . THR E 116 ? 1.6552 1.0956 1.0102 0.4517  -0.0034 -0.1801 116 THR E CG2 
12013 N N   . GLU E 117 ? 1.4966 1.0890 1.0930 0.3539  0.0304  -0.1029 117 GLU E N   
12014 C CA  . GLU E 117 ? 1.4500 1.0440 1.1291 0.3274  0.0288  -0.1188 117 GLU E CA  
12015 C C   . GLU E 117 ? 1.4056 1.0432 1.1325 0.3096  0.0646  -0.0736 117 GLU E C   
12016 O O   . GLU E 117 ? 1.3789 1.0149 1.1644 0.2850  0.0692  -0.0784 117 GLU E O   
12017 C CB  . GLU E 117 ? 1.4255 1.0243 1.1531 0.3006  -0.0104 -0.1518 117 GLU E CB  
12018 C CG  . GLU E 117 ? 1.4166 0.9801 1.1996 0.2894  -0.0281 -0.2032 117 GLU E CG  
12019 C CD  . GLU E 117 ? 1.4631 0.9707 1.1909 0.3217  -0.0557 -0.2477 117 GLU E CD  
12020 O OE1 . GLU E 117 ? 1.5067 0.9995 1.1419 0.3543  -0.0606 -0.2375 117 GLU E OE1 
12021 O OE2 . GLU E 117 ? 1.4611 0.9362 1.2362 0.3138  -0.0709 -0.2942 117 GLU E OE2 
12022 N N   . LEU E 118 ? 1.3745 1.0483 1.0770 0.3222  0.0902  -0.0316 118 LEU E N   
12023 C CA  . LEU E 118 ? 1.3290 1.0490 1.0751 0.3088  0.1141  0.0091  118 LEU E CA  
12024 C C   . LEU E 118 ? 1.3239 1.0163 1.0900 0.3195  0.1332  0.0115  118 LEU E C   
12025 O O   . LEU E 118 ? 1.3520 1.0100 1.0890 0.3503  0.1447  0.0010  118 LEU E O   
12026 C CB  . LEU E 118 ? 1.3261 1.0937 1.0533 0.3223  0.1351  0.0466  118 LEU E CB  
12027 C CG  . LEU E 118 ? 1.2759 1.1036 1.0511 0.3078  0.1484  0.0857  118 LEU E CG  
12028 C CD1 . LEU E 118 ? 1.2482 1.0921 1.0570 0.2697  0.1284  0.0842  118 LEU E CD1 
12029 C CD2 . LEU E 118 ? 1.2750 1.1531 1.0453 0.3169  0.1673  0.1141  118 LEU E CD2 
12030 N N   . VAL E 119 ? 1.2988 0.9984 1.1075 0.2954  0.1381  0.0254  119 VAL E N   
12031 C CA  . VAL E 119 ? 1.3057 0.9667 1.1277 0.3027  0.1566  0.0325  119 VAL E CA  
12032 C C   . VAL E 119 ? 1.2830 0.9820 1.1132 0.3109  0.1720  0.0801  119 VAL E C   
12033 O O   . VAL E 119 ? 1.2914 0.9740 1.1146 0.3411  0.1873  0.0961  119 VAL E O   
12034 C CB  . VAL E 119 ? 1.3137 0.9332 1.1701 0.2696  0.1536  0.0073  119 VAL E CB  
12035 C CG1 . VAL E 119 ? 1.3246 0.9067 1.1893 0.2688  0.1790  0.0313  119 VAL E CG1 
12036 C CG2 . VAL E 119 ? 1.3415 0.9127 1.1999 0.2716  0.1374  -0.0457 119 VAL E CG2 
12037 N N   . SER E 120 ? 1.2693 1.0186 1.1152 0.2870  0.1643  0.1004  120 SER E N   
12038 C CA  . SER E 120 ? 1.2485 1.0392 1.1029 0.2935  0.1687  0.1408  120 SER E CA  
12039 C C   . SER E 120 ? 1.2149 1.0798 1.0804 0.2906  0.1603  0.1549  120 SER E C   
12040 O O   . SER E 120 ? 1.2081 1.0895 1.0757 0.2654  0.1483  0.1416  120 SER E O   
12041 C CB  . SER E 120 ? 1.2575 1.0323 1.1159 0.2654  0.1683  0.1513  120 SER E CB  
12042 O OG  . SER E 120 ? 1.2402 1.0527 1.0966 0.2746  0.1641  0.1877  120 SER E OG  
12043 N N   . LEU E 121 ? 1.1684 1.0769 1.0475 0.3165  0.1671  0.1808  121 LEU E N   
12044 C CA  . LEU E 121 ? 1.1348 1.1168 1.0382 0.3125  0.1651  0.1950  121 LEU E CA  
12045 C C   . LEU E 121 ? 1.1094 1.1427 1.0464 0.3198  0.1561  0.2243  121 LEU E C   
12046 O O   . LEU E 121 ? 1.1167 1.1659 1.0718 0.3545  0.1638  0.2381  121 LEU E O   
12047 C CB  . LEU E 121 ? 1.1515 1.1425 1.0477 0.3394  0.1863  0.1898  121 LEU E CB  
12048 C CG  . LEU E 121 ? 1.1386 1.1888 1.0527 0.3292  0.1946  0.1995  121 LEU E CG  
12049 C CD1 . LEU E 121 ? 1.1073 1.2332 1.0818 0.3433  0.2030  0.2249  121 LEU E CD1 
12050 C CD2 . LEU E 121 ? 1.1244 1.1811 1.0368 0.2882  0.1734  0.1951  121 LEU E CD2 
12051 N N   . ASP E 122 ? 1.1424 1.2004 1.0874 0.2900  0.1368  0.2308  122 ASP E N   
12052 C CA  . ASP E 122 ? 1.1242 1.2220 1.0888 0.2958  0.1185  0.2541  122 ASP E CA  
12053 C C   . ASP E 122 ? 1.0930 1.2708 1.1033 0.2771  0.1061  0.2586  122 ASP E C   
12054 O O   . ASP E 122 ? 1.0842 1.2689 1.0897 0.2427  0.0928  0.2515  122 ASP E O   
12055 C CB  . ASP E 122 ? 1.1417 1.1919 1.0666 0.2779  0.1074  0.2565  122 ASP E CB  
12056 C CG  . ASP E 122 ? 1.1835 1.1530 1.0708 0.2963  0.1228  0.2576  122 ASP E CG  
12057 O OD1 . ASP E 122 ? 1.1955 1.1426 1.0868 0.3208  0.1388  0.2504  122 ASP E OD1 
12058 O OD2 . ASP E 122 ? 1.2110 1.1336 1.0613 0.2851  0.1222  0.2648  122 ASP E OD2 
12059 N N   . LEU E 123 ? 1.0528 1.2911 1.1142 0.2993  0.1127  0.2686  123 LEU E N   
12060 C CA  . LEU E 123 ? 1.0315 1.3523 1.1546 0.2827  0.1028  0.2736  123 LEU E CA  
12061 C C   . LEU E 123 ? 1.0116 1.3896 1.1818 0.3040  0.0752  0.2880  123 LEU E C   
12062 O O   . LEU E 123 ? 0.9860 1.4440 1.2289 0.2969  0.0667  0.2895  123 LEU E O   
12063 C CB  . LEU E 123 ? 1.0259 1.3799 1.1844 0.2860  0.1364  0.2711  123 LEU E CB  
12064 C CG  . LEU E 123 ? 1.0466 1.3643 1.1671 0.2606  0.1562  0.2591  123 LEU E CG  
12065 C CD1 . LEU E 123 ? 1.0763 1.3101 1.1243 0.2558  0.1496  0.2437  123 LEU E CD1 
12066 C CD2 . LEU E 123 ? 1.0458 1.3735 1.1746 0.2796  0.1974  0.2606  123 LEU E CD2 
12067 N N   . TYR E 124 ? 1.0845 1.4194 1.2146 0.3297  0.0591  0.2979  124 TYR E N   
12068 C CA  . TYR E 124 ? 1.0777 1.4545 1.2398 0.3614  0.0272  0.3127  124 TYR E CA  
12069 C C   . TYR E 124 ? 1.0697 1.4957 1.2492 0.3362  -0.0137 0.3113  124 TYR E C   
12070 O O   . TYR E 124 ? 1.0763 1.4821 1.2225 0.2959  -0.0165 0.3011  124 TYR E O   
12071 C CB  . TYR E 124 ? 1.1118 1.4073 1.2054 0.3948  0.0225  0.3268  124 TYR E CB  
12072 C CG  . TYR E 124 ? 1.1457 1.3602 1.1495 0.3715  0.0154  0.3293  124 TYR E CG  
12073 C CD1 . TYR E 124 ? 1.1582 1.3870 1.1383 0.3542  -0.0185 0.3330  124 TYR E CD1 
12074 C CD2 . TYR E 124 ? 1.1692 1.2917 1.1140 0.3675  0.0449  0.3256  124 TYR E CD2 
12075 C CE1 . TYR E 124 ? 1.1937 1.3471 1.0892 0.3343  -0.0167 0.3352  124 TYR E CE1 
12076 C CE2 . TYR E 124 ? 1.2009 1.2524 1.0748 0.3444  0.0470  0.3269  124 TYR E CE2 
12077 C CZ  . TYR E 124 ? 1.2132 1.2799 1.0598 0.3282  0.0191  0.3330  124 TYR E CZ  
12078 O OH  . TYR E 124 ? 1.2498 1.2468 1.0228 0.3053  0.0278  0.3341  124 TYR E OH  
12079 N N   . LEU E 125 ? 0.9978 1.4903 1.2343 0.3629  -0.0484 0.3182  125 LEU E N   
12080 C CA  . LEU E 125 ? 0.9973 1.5431 1.2570 0.3453  -0.0960 0.3125  125 LEU E CA  
12081 C C   . LEU E 125 ? 0.9662 1.5604 1.2778 0.2939  -0.0852 0.2941  125 LEU E C   
12082 O O   . LEU E 125 ? 0.9803 1.5498 1.2484 0.2581  -0.0978 0.2845  125 LEU E O   
12083 C CB  . LEU E 125 ? 1.0528 1.5240 1.2033 0.3441  -0.1249 0.3201  125 LEU E CB  
12084 C CG  . LEU E 125 ? 1.1068 1.5354 1.2033 0.3965  -0.1525 0.3423  125 LEU E CG  
12085 C CD1 . LEU E 125 ? 1.1581 1.4642 1.1349 0.4005  -0.1279 0.3572  125 LEU E CD1 
12086 C CD2 . LEU E 125 ? 1.1394 1.6096 1.2340 0.4084  -0.2174 0.3420  125 LEU E CD2 
12087 N N   . ASN E 126 ? 0.9523 1.6126 1.3578 0.2919  -0.0580 0.2897  126 ASN E N   
12088 C CA  . ASN E 126 ? 0.9303 1.6325 1.3908 0.2457  -0.0405 0.2766  126 ASN E CA  
12089 C C   . ASN E 126 ? 0.8834 1.6938 1.4786 0.2518  -0.0382 0.2724  126 ASN E C   
12090 O O   . ASN E 126 ? 0.8680 1.7271 1.5167 0.2924  -0.0598 0.2760  126 ASN E O   
12091 C CB  . ASN E 126 ? 0.9468 1.5879 1.3591 0.2284  0.0121  0.2768  126 ASN E CB  
12092 C CG  . ASN E 126 ? 0.9823 1.5395 1.2960 0.2045  0.0066  0.2712  126 ASN E CG  
12093 O OD1 . ASN E 126 ? 0.9846 1.5453 1.2945 0.1691  -0.0123 0.2606  126 ASN E OD1 
12094 N ND2 . ASN E 126 ? 1.0072 1.4894 1.2478 0.2236  0.0242  0.2753  126 ASN E ND2 
12095 N N   . ASN E 127 ? 0.8668 1.7135 1.5217 0.2115  -0.0101 0.2642  127 ASN E N   
12096 C CA  . ASN E 127 ? 0.8191 1.7678 1.6130 0.2071  0.0064  0.2585  127 ASN E CA  
12097 C C   . ASN E 127 ? 0.8149 1.7512 1.6201 0.1975  0.0805  0.2658  127 ASN E C   
12098 O O   . ASN E 127 ? 0.7847 1.7795 1.6826 0.1689  0.1108  0.2616  127 ASN E O   
12099 C CB  . ASN E 127 ? 0.7985 1.8084 1.6687 0.1636  -0.0278 0.2409  127 ASN E CB  
12100 C CG  . ASN E 127 ? 0.7550 1.8877 1.7880 0.1696  -0.0373 0.2291  127 ASN E CG  
12101 O OD1 . ASN E 127 ? 0.7267 1.9148 1.8572 0.1284  -0.0173 0.2182  127 ASN E OD1 
12102 N ND2 . ASN E 127 ? 0.7510 1.9255 1.8199 0.2213  -0.0673 0.2305  127 ASN E ND2 
12103 N N   . LEU E 128 ? 0.9216 1.7769 1.6288 0.2208  0.1112  0.2759  128 LEU E N   
12104 C CA  . LEU E 128 ? 0.9290 1.7581 1.6205 0.2193  0.1784  0.2822  128 LEU E CA  
12105 C C   . LEU E 128 ? 0.8923 1.8009 1.6899 0.2482  0.2148  0.2831  128 LEU E C   
12106 O O   . LEU E 128 ? 0.8695 1.8340 1.7308 0.2839  0.1856  0.2800  128 LEU E O   
12107 C CB  . LEU E 128 ? 0.9758 1.6993 1.5371 0.2407  0.1911  0.2862  128 LEU E CB  
12108 C CG  . LEU E 128 ? 1.0112 1.6588 1.4777 0.2140  0.1603  0.2819  128 LEU E CG  
12109 C CD1 . LEU E 128 ? 1.0484 1.6104 1.4156 0.2419  0.1575  0.2812  128 LEU E CD1 
12110 C CD2 . LEU E 128 ? 1.0237 1.6408 1.4649 0.1734  0.1858  0.2810  128 LEU E CD2 
12111 N N   . SER E 129 ? 0.8838 1.7945 1.6982 0.2343  0.2809  0.2874  129 SER E N   
12112 C CA  . SER E 129 ? 0.8515 1.8409 1.7747 0.2557  0.3294  0.2864  129 SER E CA  
12113 C C   . SER E 129 ? 0.8852 1.8101 1.7300 0.2694  0.4034  0.2943  129 SER E C   
12114 O O   . SER E 129 ? 0.9302 1.7521 1.6393 0.2658  0.4075  0.2990  129 SER E O   
12115 C CB  . SER E 129 ? 0.8097 1.8990 1.8783 0.2147  0.3407  0.2802  129 SER E CB  
12116 O OG  . SER E 129 ? 0.8276 1.8730 1.8591 0.1687  0.3903  0.2892  129 SER E OG  
12117 N N   . GLY E 130 ? 0.8894 1.8770 1.8223 0.2873  0.4616  0.2931  130 GLY E N   
12118 C CA  . GLY E 130 ? 0.9271 1.8583 1.7867 0.3044  0.5373  0.2987  130 GLY E CA  
12119 C C   . GLY E 130 ? 0.9521 1.8370 1.7445 0.3636  0.5345  0.2924  130 GLY E C   
12120 O O   . GLY E 130 ? 0.9325 1.8478 1.7660 0.3957  0.4840  0.2860  130 GLY E O   
12121 N N   . PRO E 131 ? 1.0041 1.8065 1.6845 0.3806  0.5876  0.2936  131 PRO E N   
12122 C CA  . PRO E 131 ? 1.0405 1.7895 1.6531 0.4358  0.5874  0.2833  131 PRO E CA  
12123 C C   . PRO E 131 ? 1.0379 1.6874 1.5256 0.4383  0.5288  0.2801  131 PRO E C   
12124 O O   . PRO E 131 ? 1.0345 1.6608 1.4899 0.3996  0.4872  0.2854  131 PRO E O   
12125 C CB  . PRO E 131 ? 1.1298 1.8293 1.6709 0.4468  0.6679  0.2810  131 PRO E CB  
12126 C CG  . PRO E 131 ? 1.1431 1.8183 1.6446 0.3944  0.6953  0.2962  131 PRO E CG  
12127 C CD  . PRO E 131 ? 1.0580 1.7983 1.6525 0.3510  0.6441  0.3040  131 PRO E CD  
12128 N N   . ILE E 132 ? 1.1384 1.7302 1.5638 0.4835  0.5273  0.2689  132 ILE E N   
12129 C CA  . ILE E 132 ? 1.1777 1.6641 1.4803 0.4860  0.4877  0.2613  132 ILE E CA  
12130 C C   . ILE E 132 ? 1.2377 1.6398 1.4227 0.4947  0.5333  0.2512  132 ILE E C   
12131 O O   . ILE E 132 ? 1.2659 1.6486 1.4308 0.5366  0.5719  0.2393  132 ILE E O   
12132 C CB  . ILE E 132 ? 1.1774 1.6437 1.4855 0.5278  0.4529  0.2541  132 ILE E CB  
12133 C CG1 . ILE E 132 ? 1.1365 1.6613 1.5245 0.5200  0.3953  0.2657  132 ILE E CG1 
12134 C CG2 . ILE E 132 ? 1.2291 1.5796 1.4129 0.5325  0.4321  0.2406  132 ILE E CG2 
12135 C CD1 . ILE E 132 ? 1.0844 1.7316 1.6137 0.5204  0.4015  0.2728  132 ILE E CD1 
12136 N N   . PRO E 133 ? 1.2541 1.6052 1.3594 0.4594  0.5311  0.2549  133 PRO E N   
12137 C CA  . PRO E 133 ? 1.3184 1.5867 1.3013 0.4702  0.5713  0.2467  133 PRO E CA  
12138 C C   . PRO E 133 ? 1.3645 1.5597 1.2693 0.5158  0.5695  0.2218  133 PRO E C   
12139 O O   . PRO E 133 ? 1.3615 1.5301 1.2645 0.5248  0.5211  0.2102  133 PRO E O   
12140 C CB  . PRO E 133 ? 1.3422 1.5547 1.2503 0.4309  0.5354  0.2505  133 PRO E CB  
12141 C CG  . PRO E 133 ? 1.2841 1.5716 1.2958 0.3916  0.5005  0.2657  133 PRO E CG  
12142 C CD  . PRO E 133 ? 1.2293 1.6094 1.3667 0.4091  0.5007  0.2688  133 PRO E CD  
12143 N N   . SER E 134 ? 1.4546 1.6181 1.3001 0.5459  0.6277  0.2130  134 SER E N   
12144 C CA  . SER E 134 ? 1.5058 1.5918 1.2696 0.5893  0.6253  0.1841  134 SER E CA  
12145 C C   . SER E 134 ? 1.5627 1.5466 1.2045 0.5797  0.5771  0.1648  134 SER E C   
12146 O O   . SER E 134 ? 1.5983 1.5178 1.1878 0.6077  0.5572  0.1364  134 SER E O   
12147 C CB  . SER E 134 ? 1.5552 1.6227 1.2772 0.6149  0.6880  0.1748  134 SER E CB  
12148 O OG  . SER E 134 ? 1.6255 1.6414 1.2459 0.5941  0.7117  0.1817  134 SER E OG  
12149 N N   . THR E 135 ? 1.5432 1.5111 1.1457 0.5416  0.5566  0.1768  135 THR E N   
12150 C CA  . THR E 135 ? 1.5955 1.4753 1.0960 0.5336  0.5064  0.1560  135 THR E CA  
12151 C C   . THR E 135 ? 1.5676 1.4444 1.1152 0.5208  0.4436  0.1426  135 THR E C   
12152 O O   . THR E 135 ? 1.6087 1.4157 1.0890 0.5184  0.4021  0.1170  135 THR E O   
12153 C CB  . THR E 135 ? 1.6109 1.4762 1.0654 0.4994  0.5007  0.1741  135 THR E CB  
12154 O OG1 . THR E 135 ? 1.5406 1.4943 1.1083 0.4632  0.5047  0.2041  135 THR E OG1 
12155 C CG2 . THR E 135 ? 1.6727 1.4904 1.0210 0.5177  0.5581  0.1804  135 THR E CG2 
12156 N N   . LEU E 136 ? 1.4984 1.4458 1.1575 0.5134  0.4355  0.1581  136 LEU E N   
12157 C CA  . LEU E 136 ? 1.4575 1.3912 1.1486 0.5023  0.3844  0.1488  136 LEU E CA  
12158 C C   . LEU E 136 ? 1.4996 1.3606 1.1457 0.5347  0.3760  0.1170  136 LEU E C   
12159 O O   . LEU E 136 ? 1.4858 1.3119 1.1380 0.5226  0.3372  0.1035  136 LEU E O   
12160 C CB  . LEU E 136 ? 1.3885 1.4034 1.1912 0.4935  0.3765  0.1738  136 LEU E CB  
12161 C CG  . LEU E 136 ? 1.3436 1.4268 1.2052 0.4522  0.3634  0.1988  136 LEU E CG  
12162 C CD1 . LEU E 136 ? 1.3205 1.4785 1.2380 0.4510  0.4065  0.2189  136 LEU E CD1 
12163 C CD2 . LEU E 136 ? 1.3054 1.4220 1.2330 0.4408  0.3257  0.2092  136 LEU E CD2 
12164 N N   . GLY E 137 ? 1.5188 1.3538 1.1219 0.5743  0.4148  0.1033  137 GLY E N   
12165 C CA  . GLY E 137 ? 1.5877 1.3441 1.1396 0.6050  0.4066  0.0674  137 GLY E CA  
12166 C C   . GLY E 137 ? 1.6365 1.3095 1.0928 0.5966  0.3723  0.0325  137 GLY E C   
12167 O O   . GLY E 137 ? 1.6887 1.2943 1.1126 0.6149  0.3555  -0.0030 137 GLY E O   
12168 N N   . ARG E 138 ? 1.7074 1.3814 1.1221 0.5707  0.3584  0.0396  138 ARG E N   
12169 C CA  . ARG E 138 ? 1.7596 1.3598 1.0917 0.5650  0.3156  0.0050  138 ARG E CA  
12170 C C   . ARG E 138 ? 1.7244 1.3160 1.1116 0.5344  0.2629  -0.0107 138 ARG E C   
12171 O O   . ARG E 138 ? 1.7557 1.2879 1.0978 0.5328  0.2231  -0.0494 138 ARG E O   
12172 C CB  . ARG E 138 ? 1.7943 1.3924 1.0618 0.5513  0.3161  0.0204  138 ARG E CB  
12173 C CG  . ARG E 138 ? 1.8308 1.4277 1.0323 0.5768  0.3761  0.0378  138 ARG E CG  
12174 C CD  . ARG E 138 ? 1.9086 1.4357 0.9777 0.5834  0.3646  0.0290  138 ARG E CD  
12175 N NE  . ARG E 138 ? 1.9131 1.4615 0.9504 0.5790  0.4194  0.0683  138 ARG E NE  
12176 C CZ  . ARG E 138 ? 1.9258 1.4596 0.9206 0.5567  0.4077  0.0892  138 ARG E CZ  
12177 N NH1 . ARG E 138 ? 1.9352 1.4401 0.9184 0.5395  0.3404  0.0735  138 ARG E NH1 
12178 N NH2 . ARG E 138 ? 1.9276 1.4746 0.8960 0.5517  0.4673  0.1260  138 ARG E NH2 
12179 N N   . LEU E 139 ? 1.6577 1.3065 1.1407 0.5109  0.2622  0.0164  139 LEU E N   
12180 C CA  . LEU E 139 ? 1.6223 1.2633 1.1570 0.4795  0.2232  0.0057  139 LEU E CA  
12181 C C   . LEU E 139 ? 1.6246 1.2130 1.1717 0.4966  0.2211  -0.0207 139 LEU E C   
12182 O O   . LEU E 139 ? 1.5936 1.1980 1.1948 0.5011  0.2359  -0.0011 139 LEU E O   
12183 C CB  . LEU E 139 ? 1.5645 1.2776 1.1776 0.4503  0.2254  0.0455  139 LEU E CB  
12184 C CG  . LEU E 139 ? 1.5579 1.3357 1.1788 0.4424  0.2465  0.0800  139 LEU E CG  
12185 C CD1 . LEU E 139 ? 1.5009 1.3474 1.2027 0.4160  0.2423  0.1124  139 LEU E CD1 
12186 C CD2 . LEU E 139 ? 1.5980 1.3543 1.1603 0.4278  0.2296  0.0710  139 LEU E CD2 
12187 N N   . LYS E 140 ? 1.6882 1.2068 1.1804 0.5084  0.1999  -0.0674 140 LYS E N   
12188 C CA  . LYS E 140 ? 1.7019 1.1594 1.2028 0.5236  0.1979  -0.0993 140 LYS E CA  
12189 C C   . LYS E 140 ? 1.6657 1.1144 1.2414 0.4885  0.1796  -0.1017 140 LYS E C   
12190 O O   . LYS E 140 ? 1.6734 1.0782 1.2733 0.4971  0.1894  -0.1114 140 LYS E O   
12191 C CB  . LYS E 140 ? 1.7617 1.1474 1.1856 0.5431  0.1738  -0.1548 140 LYS E CB  
12192 C CG  . LYS E 140 ? 1.8159 1.1919 1.1437 0.5817  0.1978  -0.1549 140 LYS E CG  
12193 C CD  . LYS E 140 ? 1.8076 1.2133 1.1516 0.6115  0.2530  -0.1234 140 LYS E CD  
12194 C CE  . LYS E 140 ? 1.8623 1.2615 1.1143 0.6472  0.2886  -0.1221 140 LYS E CE  
12195 N NZ  . LYS E 140 ? 1.9474 1.2579 1.1016 0.6810  0.2781  -0.1763 140 LYS E NZ  
12196 N N   . LYS E 141 ? 1.5765 1.0598 1.1866 0.4498  0.1575  -0.0934 141 LYS E N   
12197 C CA  . LYS E 141 ? 1.5485 1.0250 1.2265 0.4143  0.1491  -0.0935 141 LYS E CA  
12198 C C   . LYS E 141 ? 1.5132 1.0364 1.2323 0.4053  0.1727  -0.0405 141 LYS E C   
12199 O O   . LYS E 141 ? 1.4999 1.0143 1.2626 0.3768  0.1724  -0.0335 141 LYS E O   
12200 C CB  . LYS E 141 ? 1.5341 1.0222 1.2330 0.3789  0.1138  -0.1177 141 LYS E CB  
12201 C CG  . LYS E 141 ? 1.5658 1.0036 1.2372 0.3858  0.0780  -0.1778 141 LYS E CG  
12202 C CD  . LYS E 141 ? 1.5686 0.9590 1.3017 0.3633  0.0684  -0.2177 141 LYS E CD  
12203 C CE  . LYS E 141 ? 1.5302 0.9529 1.3419 0.3168  0.0655  -0.2107 141 LYS E CE  
12204 N NZ  . LYS E 141 ? 1.5238 0.9263 1.3882 0.2929  0.0295  -0.2704 141 LYS E NZ  
12205 N N   . LEU E 142 ? 1.4633 1.0349 1.1696 0.4290  0.1932  -0.0052 142 LEU E N   
12206 C CA  . LEU E 142 ? 1.4185 1.0433 1.1646 0.4224  0.2052  0.0416  142 LEU E CA  
12207 C C   . LEU E 142 ? 1.4372 1.0205 1.2028 0.4369  0.2189  0.0540  142 LEU E C   
12208 O O   . LEU E 142 ? 1.4853 1.0298 1.2354 0.4727  0.2339  0.0445  142 LEU E O   
12209 C CB  . LEU E 142 ? 1.4014 1.0920 1.1435 0.4449  0.2229  0.0696  142 LEU E CB  
12210 C CG  . LEU E 142 ? 1.3540 1.1132 1.1438 0.4379  0.2263  0.1131  142 LEU E CG  
12211 C CD1 . LEU E 142 ? 1.3159 1.1199 1.1185 0.3976  0.2080  0.1216  142 LEU E CD1 
12212 C CD2 . LEU E 142 ? 1.3495 1.1616 1.1555 0.4724  0.2510  0.1334  142 LEU E CD2 
12213 N N   . ARG E 143 ? 1.4509 1.0351 1.2435 0.4107  0.2151  0.0756  143 ARG E N   
12214 C CA  . ARG E 143 ? 1.4729 1.0097 1.2726 0.4229  0.2279  0.0963  143 ARG E CA  
12215 C C   . ARG E 143 ? 1.4556 1.0450 1.2676 0.4385  0.2289  0.1444  143 ARG E C   
12216 O O   . ARG E 143 ? 1.4709 1.0390 1.2822 0.4755  0.2382  0.1636  143 ARG E O   
12217 C CB  . ARG E 143 ? 1.4944 0.9753 1.3048 0.3829  0.2278  0.0850  143 ARG E CB  
12218 C CG  . ARG E 143 ? 1.5286 0.9240 1.3401 0.3806  0.2341  0.0434  143 ARG E CG  
12219 C CD  . ARG E 143 ? 1.5538 0.8918 1.3869 0.3421  0.2464  0.0414  143 ARG E CD  
12220 N NE  . ARG E 143 ? 1.5293 0.9022 1.3910 0.2975  0.2338  0.0204  143 ARG E NE  
12221 C CZ  . ARG E 143 ? 1.5392 0.8922 1.4242 0.2585  0.2481  0.0252  143 ARG E CZ  
12222 N NH1 . ARG E 143 ? 1.5814 0.8713 1.4538 0.2563  0.2770  0.0535  143 ARG E NH1 
12223 N NH2 . ARG E 143 ? 1.5103 0.9035 1.4285 0.2228  0.2356  0.0017  143 ARG E NH2 
12224 N N   . PHE E 144 ? 1.3751 1.0313 1.2001 0.4131  0.2155  0.1615  144 PHE E N   
12225 C CA  . PHE E 144 ? 1.3588 1.0670 1.1977 0.4227  0.2075  0.2017  144 PHE E CA  
12226 C C   . PHE E 144 ? 1.3162 1.1192 1.1823 0.4250  0.2010  0.2081  144 PHE E C   
12227 O O   . PHE E 144 ? 1.3020 1.1321 1.1683 0.3950  0.1953  0.1930  144 PHE E O   
12228 C CB  . PHE E 144 ? 1.3714 1.0664 1.1995 0.3865  0.1985  0.2158  144 PHE E CB  
12229 C CG  . PHE E 144 ? 1.4172 1.0206 1.2257 0.3656  0.2131  0.2006  144 PHE E CG  
12230 C CD1 . PHE E 144 ? 1.4102 0.9958 1.2296 0.3307  0.2147  0.1627  144 PHE E CD1 
12231 C CD2 . PHE E 144 ? 1.4693 1.0024 1.2522 0.3813  0.2253  0.2238  144 PHE E CD2 
12232 C CE1 . PHE E 144 ? 1.4476 0.9560 1.2671 0.3081  0.2308  0.1449  144 PHE E CE1 
12233 C CE2 . PHE E 144 ? 1.5152 0.9604 1.2861 0.3577  0.2461  0.2108  144 PHE E CE2 
12234 C CZ  . PHE E 144 ? 1.5012 0.9382 1.2976 0.3190  0.2503  0.1695  144 PHE E CZ  
12235 N N   . LEU E 145 ? 1.3118 1.1639 1.2061 0.4604  0.2023  0.2302  145 LEU E N   
12236 C CA  . LEU E 145 ? 1.2743 1.2212 1.2101 0.4607  0.2013  0.2382  145 LEU E CA  
12237 C C   . LEU E 145 ? 1.2560 1.2596 1.2318 0.4777  0.1820  0.2685  145 LEU E C   
12238 O O   . LEU E 145 ? 1.2622 1.2655 1.2570 0.5215  0.1843  0.2800  145 LEU E O   
12239 C CB  . LEU E 145 ? 1.2752 1.2361 1.2193 0.4909  0.2291  0.2239  145 LEU E CB  
12240 C CG  . LEU E 145 ? 1.2471 1.2964 1.2317 0.4840  0.2404  0.2294  145 LEU E CG  
12241 C CD1 . LEU E 145 ? 1.2683 1.2949 1.2144 0.4860  0.2680  0.2065  145 LEU E CD1 
12242 C CD2 . LEU E 145 ? 1.2229 1.3423 1.2757 0.5200  0.2472  0.2475  145 LEU E CD2 
12243 N N   . ARG E 146 ? 1.2101 1.2611 1.1991 0.4460  0.1595  0.2787  146 ARG E N   
12244 C CA  . ARG E 146 ? 1.1951 1.3032 1.2191 0.4592  0.1314  0.3025  146 ARG E CA  
12245 C C   . ARG E 146 ? 1.1562 1.3658 1.2451 0.4412  0.1263  0.3008  146 ARG E C   
12246 O O   . ARG E 146 ? 1.1488 1.3723 1.2304 0.3986  0.1200  0.2935  146 ARG E O   
12247 C CB  . ARG E 146 ? 1.2163 1.2814 1.1905 0.4379  0.1071  0.3145  146 ARG E CB  
12248 C CG  . ARG E 146 ? 1.2649 1.2278 1.1789 0.4554  0.1148  0.3232  146 ARG E CG  
12249 C CD  . ARG E 146 ? 1.2888 1.1913 1.1493 0.4115  0.1196  0.3164  146 ARG E CD  
12250 N NE  . ARG E 146 ? 1.3398 1.1379 1.1540 0.4169  0.1417  0.3154  146 ARG E NE  
12251 C CZ  . ARG E 146 ? 1.3594 1.1031 1.1552 0.3820  0.1620  0.2927  146 ARG E CZ  
12252 N NH1 . ARG E 146 ? 1.3316 1.1123 1.1457 0.3437  0.1606  0.2693  146 ARG E NH1 
12253 N NH2 . ARG E 146 ? 1.4118 1.0608 1.1757 0.3859  0.1834  0.2920  146 ARG E NH2 
12254 N N   . LEU E 147 ? 1.1332 1.3918 1.6743 0.5893  0.4684  0.4174  147 LEU E N   
12255 C CA  . LEU E 147 ? 1.0819 1.4509 1.6822 0.5670  0.4477  0.4151  147 LEU E CA  
12256 C C   . LEU E 147 ? 1.0776 1.5576 1.7193 0.6090  0.4374  0.4291  147 LEU E C   
12257 O O   . LEU E 147 ? 1.0468 1.6273 1.7516 0.6026  0.4302  0.4253  147 LEU E O   
12258 C CB  . LEU E 147 ? 1.0965 1.4629 1.6961 0.5586  0.4706  0.4125  147 LEU E CB  
12259 C CG  . LEU E 147 ? 1.1237 1.3850 1.6710 0.5326  0.4818  0.3969  147 LEU E CG  
12260 C CD1 . LEU E 147 ? 1.1276 1.4197 1.6819 0.5115  0.4928  0.3969  147 LEU E CD1 
12261 C CD2 . LEU E 147 ? 1.0975 1.2924 1.6327 0.4887  0.4528  0.3766  147 LEU E CD2 
12262 N N   . ASN E 148 ? 1.1156 1.5782 1.7241 0.6535  0.4371  0.4437  148 ASN E N   
12263 C CA  . ASN E 148 ? 1.1371 1.6896 1.7620 0.6989  0.4196  0.4527  148 ASN E CA  
12264 C C   . ASN E 148 ? 1.0739 1.7424 1.7668 0.6787  0.3770  0.4372  148 ASN E C   
12265 O O   . ASN E 148 ? 1.0212 1.6846 1.7343 0.6264  0.3601  0.4216  148 ASN E O   
12266 C CB  . ASN E 148 ? 1.2187 1.6994 1.7637 0.7455  0.4274  0.4730  148 ASN E CB  
12267 C CG  . ASN E 148 ? 1.2160 1.6299 1.7263 0.7323  0.4278  0.4766  148 ASN E CG  
12268 O OD1 . ASN E 148 ? 1.1650 1.6384 1.7079 0.7087  0.3970  0.4645  148 ASN E OD1 
12269 N ND2 . ASN E 148 ? 1.2768 1.5632 1.7223 0.7396  0.4627  0.4871  148 ASN E ND2 
12270 N N   . ASN E 149 ? 1.0921 1.8548 1.8122 0.7096  0.3518  0.4308  149 ASN E N   
12271 C CA  . ASN E 149 ? 1.0437 1.9268 1.8359 0.6942  0.3069  0.4055  149 ASN E CA  
12272 C C   . ASN E 149 ? 0.9621 1.8922 1.8405 0.6288  0.3061  0.3851  149 ASN E C   
12273 O O   . ASN E 149 ? 0.9076 1.8562 1.8180 0.5896  0.2850  0.3723  149 ASN E O   
12274 C CB  . ASN E 149 ? 1.0523 1.9272 1.8032 0.7083  0.2808  0.4083  149 ASN E CB  
12275 C CG  . ASN E 149 ? 1.1190 2.0471 1.8397 0.7693  0.2506  0.4088  149 ASN E CG  
12276 O OD1 . ASN E 149 ? 1.0973 2.1341 1.8746 0.7686  0.2066  0.3791  149 ASN E OD1 
12277 N ND2 . ASN E 149 ? 1.2087 2.0563 1.8405 0.8225  0.2733  0.4399  149 ASN E ND2 
12278 N N   . ASN E 150 ? 0.9623 1.9076 1.8766 0.6179  0.3327  0.3836  150 ASN E N   
12279 C CA  . ASN E 150 ? 0.9066 1.8862 1.8941 0.5603  0.3429  0.3718  150 ASN E CA  
12280 C C   . ASN E 150 ? 0.9183 1.9816 1.9761 0.5627  0.3538  0.3555  150 ASN E C   
12281 O O   . ASN E 150 ? 0.9636 2.0604 2.0182 0.6091  0.3487  0.3503  150 ASN E O   
12282 C CB  . ASN E 150 ? 0.9137 1.7780 1.8439 0.5325  0.3780  0.3892  150 ASN E CB  
12283 C CG  . ASN E 150 ? 0.8810 1.6821 1.7865 0.4809  0.3532  0.3794  150 ASN E CG  
12284 O OD1 . ASN E 150 ? 0.8366 1.6692 1.7978 0.4292  0.3392  0.3653  150 ASN E OD1 
12285 N ND2 . ASN E 150 ? 0.9066 1.6169 1.7352 0.4949  0.3502  0.3854  150 ASN E ND2 
12286 N N   . SER E 151 ? 0.8836 1.9775 2.0086 0.5119  0.3711  0.3470  151 SER E N   
12287 C CA  . SER E 151 ? 0.8983 2.0625 2.0971 0.5050  0.3943  0.3308  151 SER E CA  
12288 C C   . SER E 151 ? 0.9311 2.0297 2.0931 0.4980  0.4550  0.3568  151 SER E C   
12289 O O   . SER E 151 ? 0.9367 2.0717 2.1572 0.4684  0.4872  0.3504  151 SER E O   
12290 C CB  . SER E 151 ? 0.8523 2.1015 2.1597 0.4526  0.3753  0.2978  151 SER E CB  
12291 O OG  . SER E 151 ? 0.8723 2.2015 2.2645 0.4510  0.3941  0.2719  151 SER E OG  
12292 N N   . LEU E 152 ? 0.9617 1.9593 2.0245 0.5254  0.4736  0.3832  152 LEU E N   
12293 C CA  . LEU E 152 ? 1.0026 1.9296 2.0150 0.5248  0.5286  0.4029  152 LEU E CA  
12294 C C   . LEU E 152 ? 1.0559 2.0188 2.0831 0.5552  0.5585  0.3953  152 LEU E C   
12295 O O   . LEU E 152 ? 1.0770 2.0716 2.1084 0.5973  0.5369  0.3845  152 LEU E O   
12296 C CB  . LEU E 152 ? 1.0358 1.8301 1.9285 0.5389  0.5253  0.4149  152 LEU E CB  
12297 C CG  . LEU E 152 ? 1.0230 1.7212 1.8570 0.4890  0.5045  0.4136  152 LEU E CG  
12298 C CD1 . LEU E 152 ? 0.9581 1.7152 1.8618 0.4449  0.4662  0.4020  152 LEU E CD1 
12299 C CD2 . LEU E 152 ? 1.0441 1.6423 1.7955 0.5115  0.4912  0.4148  152 LEU E CD2 
12300 N N   . SER E 153 ? 1.0859 2.0406 2.1183 0.5349  0.6100  0.4012  153 SER E N   
12301 C CA  . SER E 153 ? 1.1374 2.1316 2.1960 0.5563  0.6441  0.3896  153 SER E CA  
12302 C C   . SER E 153 ? 1.1993 2.1138 2.1819 0.5561  0.7052  0.4071  153 SER E C   
12303 O O   . SER E 153 ? 1.2027 2.0730 2.1560 0.5206  0.7321  0.4239  153 SER E O   
12304 C CB  . SER E 153 ? 1.1187 2.2257 2.3002 0.5252  0.6460  0.3632  153 SER E CB  
12305 O OG  . SER E 153 ? 1.1115 2.2060 2.3122 0.4698  0.6774  0.3742  153 SER E OG  
12306 N N   . GLY E 154 ? 1.2558 2.1500 2.2028 0.5973  0.7261  0.4018  154 GLY E N   
12307 C CA  . GLY E 154 ? 1.3268 2.1465 2.1940 0.6042  0.7816  0.4107  154 GLY E CA  
12308 C C   . GLY E 154 ? 1.3739 2.1414 2.1820 0.6564  0.7804  0.4047  154 GLY E C   
12309 O O   . GLY E 154 ? 1.3720 2.1883 2.2249 0.6874  0.7550  0.3921  154 GLY E O   
12310 N N   . GLU E 155 ? 1.4240 2.0899 2.1312 0.6660  0.8082  0.4113  155 GLU E N   
12311 C CA  . GLU E 155 ? 1.4745 2.0710 2.1195 0.7093  0.8091  0.4030  155 GLU E CA  
12312 C C   . GLU E 155 ? 1.4759 1.9627 2.0340 0.7108  0.7968  0.4075  155 GLU E C   
12313 O O   . GLU E 155 ? 1.4652 1.9164 1.9870 0.6771  0.7970  0.4134  155 GLU E O   
12314 C CB  . GLU E 155 ? 1.5548 2.1406 2.1720 0.7227  0.8618  0.3907  155 GLU E CB  
12315 C CG  . GLU E 155 ? 1.6084 2.1432 2.1885 0.7672  0.8623  0.3764  155 GLU E CG  
12316 C CD  . GLU E 155 ? 1.6757 2.2409 2.2692 0.7811  0.9077  0.3591  155 GLU E CD  
12317 O OE1 . GLU E 155 ? 1.7171 2.2745 2.2766 0.7599  0.9529  0.3584  155 GLU E OE1 
12318 O OE2 . GLU E 155 ? 1.6948 2.2890 2.3297 0.8139  0.9000  0.3465  155 GLU E OE2 
12319 N N   . ILE E 156 ? 1.4986 1.9231 2.0213 0.7425  0.7785  0.4003  156 ILE E N   
12320 C CA  . ILE E 156 ? 1.5023 1.8208 1.9576 0.7421  0.7644  0.3956  156 ILE E CA  
12321 C C   . ILE E 156 ? 1.5651 1.8099 1.9413 0.7417  0.7993  0.3799  156 ILE E C   
12322 O O   . ILE E 156 ? 1.6303 1.8641 1.9816 0.7645  0.8308  0.3668  156 ILE E O   
12323 C CB  . ILE E 156 ? 1.5259 1.7878 1.9645 0.7704  0.7428  0.3905  156 ILE E CB  
12324 C CG1 . ILE E 156 ? 1.4757 1.7794 1.9579 0.7708  0.7025  0.4069  156 ILE E CG1 
12325 C CG2 . ILE E 156 ? 1.5550 1.6972 1.9264 0.7684  0.7411  0.3728  156 ILE E CG2 
12326 C CD1 . ILE E 156 ? 1.4851 1.8732 2.0203 0.7968  0.6965  0.4123  156 ILE E CD1 
12327 N N   . PRO E 157 ? 1.5639 1.7462 1.8821 0.6998  0.7726  0.3736  157 PRO E N   
12328 C CA  . PRO E 157 ? 1.6423 1.7391 1.8630 0.6974  0.7860  0.3516  157 PRO E CA  
12329 C C   . PRO E 157 ? 1.6883 1.7072 1.8759 0.7365  0.7921  0.3229  157 PRO E C   
12330 O O   . PRO E 157 ? 1.6565 1.6421 1.8711 0.7452  0.7692  0.3183  157 PRO E O   
12331 C CB  . PRO E 157 ? 1.6222 1.6687 1.8019 0.6501  0.7412  0.3495  157 PRO E CB  
12332 C CG  . PRO E 157 ? 1.5309 1.6442 1.7917 0.6228  0.7116  0.3712  157 PRO E CG  
12333 C CD  . PRO E 157 ? 1.4974 1.7049 1.8432 0.6526  0.7326  0.3867  157 PRO E CD  
12334 N N   . ARG E 158 ? 1.9324 1.5286 1.4677 0.4129  0.8289  0.0612  158 ARG E N   
12335 C CA  . ARG E 158 ? 1.9624 1.5222 1.4307 0.4455  0.8036  0.0251  158 ARG E CA  
12336 C C   . ARG E 158 ? 1.9690 1.4607 1.3321 0.4415  0.7546  0.0275  158 ARG E C   
12337 O O   . ARG E 158 ? 1.9695 1.4281 1.3058 0.4598  0.7186  -0.0047 158 ARG E O   
12338 C CB  . ARG E 158 ? 2.0580 1.6318 1.4735 0.4730  0.8623  0.0041  158 ARG E CB  
12339 C CG  . ARG E 158 ? 2.1504 1.6799 1.4201 0.4779  0.8834  0.0185  158 ARG E CG  
12340 C CD  . ARG E 158 ? 2.2000 1.6879 1.3755 0.5128  0.8541  -0.0244 158 ARG E CD  
12341 N NE  . ARG E 158 ? 2.2784 1.7224 1.3152 0.5196  0.8509  -0.0141 158 ARG E NE  
12342 C CZ  . ARG E 158 ? 2.3083 1.7144 1.2682 0.5389  0.8025  -0.0493 158 ARG E CZ  
12343 N NH1 . ARG E 158 ? 2.2745 1.6685 1.2716 0.5536  0.7671  -0.0954 158 ARG E NH1 
12344 N NH2 . ARG E 158 ? 2.3792 1.7585 1.2291 0.5440  0.7878  -0.0399 158 ARG E NH2 
12345 N N   . SER E 159 ? 1.9861 1.4554 1.2950 0.4185  0.7528  0.0617  159 SER E N   
12346 C CA  . SER E 159 ? 2.0028 1.4142 1.2120 0.4184  0.7058  0.0572  159 SER E CA  
12347 C C   . SER E 159 ? 1.9713 1.3683 1.2298 0.4071  0.6413  0.0436  159 SER E C   
12348 O O   . SER E 159 ? 1.9767 1.3324 1.1759 0.4148  0.6038  0.0172  159 SER E O   
12349 C CB  . SER E 159 ? 2.0225 1.4128 1.1724 0.3987  0.7141  0.0985  159 SER E CB  
12350 O OG  . SER E 159 ? 1.9915 1.4121 1.2421 0.3658  0.7130  0.1303  159 SER E OG  
12351 N N   . LEU E 160 ? 1.9583 1.3909 1.3263 0.3908  0.6296  0.0581  160 LEU E N   
12352 C CA  . LEU E 160 ? 1.9308 1.3502 1.3405 0.3826  0.5742  0.0511  160 LEU E CA  
12353 C C   . LEU E 160 ? 1.9250 1.3164 1.3305 0.4068  0.5607  0.0152  160 LEU E C   
12354 O O   . LEU E 160 ? 1.9052 1.2682 1.3217 0.4003  0.5197  0.0090  160 LEU E O   
12355 C CB  . LEU E 160 ? 1.9016 1.3714 1.4254 0.3703  0.5665  0.0706  160 LEU E CB  
12356 C CG  . LEU E 160 ? 1.9006 1.3983 1.4542 0.3420  0.5745  0.1031  160 LEU E CG  
12357 C CD1 . LEU E 160 ? 1.8720 1.4306 1.5535 0.3369  0.5666  0.1085  160 LEU E CD1 
12358 C CD2 . LEU E 160 ? 1.9022 1.3610 1.3935 0.3217  0.5322  0.1146  160 LEU E CD2 
12359 N N   . THR E 161 ? 1.9200 1.3170 1.3131 0.4343  0.5965  -0.0085 161 THR E N   
12360 C CA  . THR E 161 ? 1.9170 1.2810 1.3082 0.4591  0.5851  -0.0458 161 THR E CA  
12361 C C   . THR E 161 ? 1.9405 1.2538 1.2406 0.4645  0.5696  -0.0782 161 THR E C   
12362 O O   . THR E 161 ? 1.9502 1.2256 1.2549 0.4776  0.5533  -0.1114 161 THR E O   
12363 C CB  . THR E 161 ? 1.9236 1.3215 1.3523 0.4901  0.6264  -0.0652 161 THR E CB  
12364 O OG1 . THR E 161 ? 1.9621 1.3867 1.3393 0.4947  0.6733  -0.0632 161 THR E OG1 
12365 C CG2 . THR E 161 ? 1.8963 1.3440 1.4334 0.4923  0.6301  -0.0488 161 THR E CG2 
12366 N N   . ALA E 162 ? 1.9424 1.2518 1.1627 0.4572  0.5728  -0.0721 162 ALA E N   
12367 C CA  . ALA E 162 ? 2.0001 1.2707 1.1330 0.4695  0.5544  -0.1113 162 ALA E CA  
12368 C C   . ALA E 162 ? 1.9614 1.2027 1.0750 0.4440  0.5052  -0.1129 162 ALA E C   
12369 O O   . ALA E 162 ? 2.0037 1.2171 1.0574 0.4533  0.4828  -0.1537 162 ALA E O   
12370 C CB  . ALA E 162 ? 2.0831 1.3655 1.1217 0.4905  0.5885  -0.1105 162 ALA E CB  
12371 N N   . VAL E 163 ? 1.9959 1.2486 1.1635 0.4143  0.4866  -0.0759 163 VAL E N   
12372 C CA  . VAL E 163 ? 1.9765 1.2107 1.1280 0.3894  0.4422  -0.0770 163 VAL E CA  
12373 C C   . VAL E 163 ? 1.9499 1.1459 1.1142 0.3861  0.4148  -0.1210 163 VAL E C   
12374 O O   . VAL E 163 ? 1.9426 1.1205 1.0703 0.3768  0.3836  -0.1499 163 VAL E O   
12375 C CB  . VAL E 163 ? 1.9566 1.2176 1.1728 0.3618  0.4295  -0.0318 163 VAL E CB  
12376 C CG1 . VAL E 163 ? 1.9349 1.2109 1.2375 0.3660  0.4405  -0.0196 163 VAL E CG1 
12377 C CG2 . VAL E 163 ? 1.9285 1.1746 1.1402 0.3365  0.3829  -0.0381 163 VAL E CG2 
12378 N N   . LEU E 164 ? 2.0015 1.1836 1.2243 0.3927  0.4259  -0.1267 164 LEU E N   
12379 C CA  . LEU E 164 ? 1.9980 1.1334 1.2458 0.3900  0.4126  -0.1636 164 LEU E CA  
12380 C C   . LEU E 164 ? 1.9525 1.0711 1.2289 0.3558  0.3823  -0.1544 164 LEU E C   
12381 O O   . LEU E 164 ? 1.9509 1.0257 1.2540 0.3465  0.3765  -0.1798 164 LEU E O   
12382 C CB  . LEU E 164 ? 2.0374 1.1495 1.2358 0.4078  0.4094  -0.2264 164 LEU E CB  
12383 C CG  . LEU E 164 ? 2.0367 1.1434 1.1852 0.3976  0.3767  -0.2654 164 LEU E CG  
12384 C CD1 . LEU E 164 ? 2.0175 1.0849 1.2117 0.3745  0.3552  -0.3072 164 LEU E CD1 
12385 C CD2 . LEU E 164 ? 2.1017 1.2181 1.1706 0.4345  0.3825  -0.3065 164 LEU E CD2 
12386 N N   . THR E 165 ? 1.8786 1.0295 1.1542 0.3361  0.3658  -0.1196 165 THR E N   
12387 C CA  . THR E 165 ? 1.8411 0.9864 1.1454 0.3055  0.3388  -0.1092 165 THR E CA  
12388 C C   . THR E 165 ? 1.8302 0.9980 1.1865 0.3013  0.3398  -0.0588 165 THR E C   
12389 O O   . THR E 165 ? 1.7999 0.9619 1.1802 0.2809  0.3216  -0.0473 165 THR E O   
12390 C CB  . THR E 165 ? 1.8278 0.9944 1.0920 0.2886  0.3091  -0.1190 165 THR E CB  
12391 O OG1 . THR E 165 ? 1.8619 1.0206 1.0628 0.3074  0.3087  -0.1600 165 THR E OG1 
12392 C CG2 . THR E 165 ? 1.7827 0.9359 1.0708 0.2586  0.2826  -0.1378 165 THR E CG2 
12393 N N   . LEU E 166 ? 1.7917 0.9893 1.1680 0.3223  0.3607  -0.0331 166 LEU E N   
12394 C CA  . LEU E 166 ? 1.7768 1.0051 1.2087 0.3255  0.3574  0.0057  166 LEU E CA  
12395 C C   . LEU E 166 ? 1.7593 0.9467 1.2186 0.3345  0.3562  0.0104  166 LEU E C   
12396 O O   . LEU E 166 ? 1.7770 0.9322 1.2425 0.3587  0.3761  -0.0014 166 LEU E O   
12397 C CB  . LEU E 166 ? 1.8009 1.0724 1.2601 0.3478  0.3838  0.0202  166 LEU E CB  
12398 C CG  . LEU E 166 ? 1.8089 1.1355 1.2836 0.3346  0.3824  0.0444  166 LEU E CG  
12399 C CD1 . LEU E 166 ? 1.7747 1.1380 1.3131 0.3292  0.3585  0.0697  166 LEU E CD1 
12400 C CD2 . LEU E 166 ? 1.8195 1.1342 1.2329 0.3129  0.3668  0.0366  166 LEU E CD2 
12401 N N   . GLN E 167 ? 1.8005 0.9857 1.2723 0.3177  0.3342  0.0285  167 GLN E N   
12402 C CA  . GLN E 167 ? 1.7928 0.9365 1.2809 0.3296  0.3355  0.0449  167 GLN E CA  
12403 C C   . GLN E 167 ? 1.7732 0.9605 1.2989 0.3525  0.3236  0.0797  167 GLN E C   
12404 O O   . GLN E 167 ? 1.7837 0.9445 1.3221 0.3845  0.3301  0.0929  167 GLN E O   
12405 C CB  . GLN E 167 ? 1.7767 0.8832 1.2480 0.2981  0.3249  0.0396  167 GLN E CB  
12406 C CG  . GLN E 167 ? 1.7883 0.8547 1.2359 0.2758  0.3325  -0.0056 167 GLN E CG  
12407 C CD  . GLN E 167 ? 1.8130 0.7986 1.2656 0.2711  0.3522  -0.0157 167 GLN E CD  
12408 O OE1 . GLN E 167 ? 1.8473 0.7924 1.3091 0.2975  0.3679  0.0075  167 GLN E OE1 
12409 N NE2 . GLN E 167 ? 1.8086 0.7686 1.2589 0.2383  0.3519  -0.0524 167 GLN E NE2 
12410 N N   . VAL E 168 ? 1.6760 0.9296 1.2218 0.3405  0.3038  0.0911  168 VAL E N   
12411 C CA  . VAL E 168 ? 1.6492 0.9566 1.2410 0.3616  0.2863  0.1146  168 VAL E CA  
12412 C C   . VAL E 168 ? 1.6562 1.0310 1.2908 0.3638  0.2919  0.1112  168 VAL E C   
12413 O O   . VAL E 168 ? 1.6571 1.0529 1.2812 0.3359  0.2900  0.1063  168 VAL E O   
12414 C CB  . VAL E 168 ? 1.6066 0.9340 1.1963 0.3437  0.2559  0.1286  168 VAL E CB  
12415 C CG1 . VAL E 168 ? 1.5854 0.9683 1.2218 0.3747  0.2341  0.1466  168 VAL E CG1 
12416 C CG2 . VAL E 168 ? 1.6150 0.8723 1.1605 0.3319  0.2609  0.1308  168 VAL E CG2 
12417 N N   . LEU E 169 ? 1.5955 1.0020 1.2797 0.3979  0.3004  0.1130  169 LEU E N   
12418 C CA  . LEU E 169 ? 1.6063 1.0824 1.3502 0.3999  0.3122  0.1085  169 LEU E CA  
12419 C C   . LEU E 169 ? 1.5792 1.1136 1.3975 0.4325  0.2917  0.1118  169 LEU E C   
12420 O O   . LEU E 169 ? 1.5773 1.0898 1.3949 0.4706  0.2842  0.1128  169 LEU E O   
12421 C CB  . LEU E 169 ? 1.6505 1.1160 1.3888 0.4106  0.3532  0.0920  169 LEU E CB  
12422 C CG  . LEU E 169 ? 1.6698 1.1988 1.4655 0.4107  0.3832  0.0857  169 LEU E CG  
12423 C CD1 . LEU E 169 ? 1.6442 1.2388 1.5363 0.4422  0.3785  0.0787  169 LEU E CD1 
12424 C CD2 . LEU E 169 ? 1.6777 1.2313 1.4710 0.3730  0.3824  0.0977  169 LEU E CD2 
12425 N N   . ASP E 170 ? 1.5452 1.1512 1.4280 0.4201  0.2806  0.1111  170 ASP E N   
12426 C CA  . ASP E 170 ? 1.5184 1.1963 1.4907 0.4530  0.2615  0.1018  170 ASP E CA  
12427 C C   . ASP E 170 ? 1.5187 1.2685 1.5754 0.4304  0.2769  0.0914  170 ASP E C   
12428 O O   . ASP E 170 ? 1.5098 1.2745 1.5719 0.3966  0.2647  0.0993  170 ASP E O   
12429 C CB  . ASP E 170 ? 1.4783 1.1679 1.4461 0.4680  0.2141  0.1111  170 ASP E CB  
12430 C CG  . ASP E 170 ? 1.4530 1.2119 1.5015 0.5169  0.1877  0.0952  170 ASP E CG  
12431 O OD1 . ASP E 170 ? 1.4655 1.2482 1.5641 0.5451  0.2057  0.0768  170 ASP E OD1 
12432 O OD2 . ASP E 170 ? 1.4179 1.2121 1.4809 0.5306  0.1470  0.0964  170 ASP E OD2 
12433 N N   . LEU E 171 ? 1.1316 1.5350 1.6482 0.2509  0.1451  0.2225  171 LEU E N   
12434 C CA  . LEU E 171 ? 1.1057 1.5602 1.7160 0.2252  0.1558  0.2067  171 LEU E CA  
12435 C C   . LEU E 171 ? 1.0476 1.5813 1.7541 0.2544  0.1354  0.1732  171 LEU E C   
12436 O O   . LEU E 171 ? 1.0293 1.6090 1.8238 0.2442  0.1603  0.1562  171 LEU E O   
12437 C CB  . LEU E 171 ? 1.1520 1.5846 1.7572 0.1983  0.2083  0.2212  171 LEU E CB  
12438 C CG  . LEU E 171 ? 1.1866 1.5999 1.7520 0.2172  0.2390  0.2268  171 LEU E CG  
12439 C CD1 . LEU E 171 ? 1.1462 1.6248 1.7975 0.2419  0.2458  0.2016  171 LEU E CD1 
12440 C CD2 . LEU E 171 ? 1.2396 1.6130 1.7580 0.1901  0.2841  0.2455  171 LEU E CD2 
12441 N N   . SER E 172 ? 1.0748 1.6266 1.7651 0.2946  0.0907  0.1614  172 SER E N   
12442 C CA  . SER E 172 ? 1.0289 1.6580 1.8020 0.3338  0.0602  0.1240  172 SER E CA  
12443 C C   . SER E 172 ? 0.9694 1.6678 1.8574 0.3147  0.0385  0.0856  172 SER E C   
12444 O O   . SER E 172 ? 0.9610 1.6403 1.8500 0.2769  0.0399  0.0923  172 SER E O   
12445 C CB  . SER E 172 ? 1.0305 1.6497 1.7308 0.3910  0.0186  0.1275  172 SER E CB  
12446 O OG  . SER E 172 ? 1.0779 1.6325 1.6924 0.4096  0.0421  0.1602  172 SER E OG  
12447 N N   . ASN E 173 ? 1.0143 1.7951 2.0094 0.3429  0.0167  0.0403  173 ASN E N   
12448 C CA  . ASN E 173 ? 0.9336 1.7934 2.0563 0.3367  -0.0154 -0.0108 173 ASN E CA  
12449 C C   . ASN E 173 ? 0.9046 1.7638 2.1178 0.2704  0.0296  -0.0100 173 ASN E C   
12450 O O   . ASN E 173 ? 0.8534 1.7297 2.1232 0.2471  0.0109  -0.0289 173 ASN E O   
12451 C CB  . ASN E 173 ? 0.9147 1.7773 1.9851 0.3614  -0.0723 -0.0210 173 ASN E CB  
12452 C CG  . ASN E 173 ? 0.9378 1.8045 1.9220 0.4339  -0.1154 -0.0217 173 ASN E CG  
12453 O OD1 . ASN E 173 ? 0.8751 1.8166 1.9249 0.4829  -0.1571 -0.0682 173 ASN E OD1 
12454 N ND2 . ASN E 173 ? 0.9949 1.7794 1.8337 0.4433  -0.1049 0.0290  173 ASN E ND2 
12455 N N   . ASN E 174 ? 0.9050 1.7399 2.1275 0.2416  0.0917  0.0137  174 ASN E N   
12456 C CA  . ASN E 174 ? 0.8841 1.7222 2.2017 0.1849  0.1437  0.0158  174 ASN E CA  
12457 C C   . ASN E 174 ? 0.8874 1.7509 2.2674 0.1777  0.2007  0.0121  174 ASN E C   
12458 O O   . ASN E 174 ? 0.9435 1.7764 2.2352 0.1993  0.2175  0.0347  174 ASN E O   
12459 C CB  . ASN E 174 ? 0.9504 1.6972 2.1694 0.1428  0.1742  0.0697  174 ASN E CB  
12460 C CG  . ASN E 174 ? 1.0347 1.7056 2.0878 0.1587  0.1791  0.1138  174 ASN E CG  
12461 O OD1 . ASN E 174 ? 1.0391 1.7111 2.0311 0.2008  0.1426  0.1089  174 ASN E OD1 
12462 N ND2 . ASN E 174 ? 1.1012 1.7033 2.0814 0.1273  0.2249  0.1561  174 ASN E ND2 
12463 N N   . PRO E 175 ? 0.8024 1.7217 2.3403 0.1468  0.2344  -0.0186 175 PRO E N   
12464 C CA  . PRO E 175 ? 0.7875 1.7499 2.4095 0.1440  0.2879  -0.0344 175 PRO E CA  
12465 C C   . PRO E 175 ? 0.8673 1.7599 2.4017 0.1130  0.3676  0.0218  175 PRO E C   
12466 O O   . PRO E 175 ? 0.8614 1.7448 2.4589 0.0671  0.4324  0.0365  175 PRO E O   
12467 C CB  . PRO E 175 ? 0.7337 1.7657 2.5451 0.1139  0.2977  -0.0860 175 PRO E CB  
12468 C CG  . PRO E 175 ? 0.7207 1.7140 2.5326 0.0803  0.2870  -0.0682 175 PRO E CG  
12469 C CD  . PRO E 175 ? 0.7252 1.6851 2.3958 0.1197  0.2177  -0.0536 175 PRO E CD  
12470 N N   . LEU E 176 ? 0.9526 1.7945 2.3419 0.1403  0.3650  0.0524  176 LEU E N   
12471 C CA  . LEU E 176 ? 1.0221 1.8050 2.3189 0.1221  0.4322  0.0966  176 LEU E CA  
12472 C C   . LEU E 176 ? 1.0024 1.8401 2.3641 0.1395  0.4704  0.0698  176 LEU E C   
12473 O O   . LEU E 176 ? 0.9384 1.8562 2.4148 0.1667  0.4405  0.0180  176 LEU E O   
12474 C CB  . LEU E 176 ? 1.1007 1.7996 2.2175 0.1397  0.4070  0.1362  176 LEU E CB  
12475 C CG  . LEU E 176 ? 1.1716 1.7861 2.1730 0.1094  0.4492  0.1878  176 LEU E CG  
12476 C CD1 . LEU E 176 ? 1.1631 1.7583 2.2017 0.0706  0.4529  0.2029  176 LEU E CD1 
12477 C CD2 . LEU E 176 ? 1.2249 1.7744 2.0805 0.1322  0.4113  0.2087  176 LEU E CD2 
12478 N N   . THR E 177 ? 1.0480 1.8460 2.3370 0.1274  0.5355  0.1010  177 THR E N   
12479 C CA  . THR E 177 ? 1.0317 1.8804 2.3806 0.1400  0.5822  0.0761  177 THR E CA  
12480 C C   . THR E 177 ? 1.1073 1.8965 2.3059 0.1584  0.6051  0.1054  177 THR E C   
12481 O O   . THR E 177 ? 1.1698 1.8791 2.2322 0.1480  0.6082  0.1488  177 THR E O   
12482 C CB  . THR E 177 ? 0.9994 1.8843 2.4660 0.0962  0.6661  0.0728  177 THR E CB  
12483 O OG1 . THR E 177 ? 1.0643 1.8679 2.4135 0.0655  0.7262  0.1324  177 THR E OG1 
12484 C CG2 . THR E 177 ? 0.9679 1.8978 2.5800 0.0703  0.6415  0.0407  177 THR E CG2 
12485 N N   . GLY E 178 ? 1.0935 1.9253 2.3249 0.1885  0.6177  0.0751  178 GLY E N   
12486 C CA  . GLY E 178 ? 1.1533 1.9408 2.2654 0.2090  0.6404  0.0902  178 GLY E CA  
12487 C C   . GLY E 178 ? 1.1682 1.9398 2.2303 0.2581  0.5748  0.0759  178 GLY E C   
12488 O O   . GLY E 178 ? 1.1380 1.9304 2.2433 0.2805  0.5124  0.0590  178 GLY E O   
12489 N N   . ASP E 179 ? 1.1955 1.9279 2.1643 0.2773  0.5926  0.0824  179 ASP E N   
12490 C CA  . ASP E 179 ? 1.2173 1.9167 2.1300 0.3210  0.5427  0.0751  179 ASP E CA  
12491 C C   . ASP E 179 ? 1.2668 1.8775 2.0470 0.3150  0.5133  0.1116  179 ASP E C   
12492 O O   . ASP E 179 ? 1.3014 1.8711 2.0071 0.2851  0.5406  0.1386  179 ASP E O   
12493 C CB  . ASP E 179 ? 1.2357 1.9455 2.1410 0.3467  0.5763  0.0520  179 ASP E CB  
12494 C CG  . ASP E 179 ? 1.1852 1.9783 2.2249 0.3752  0.5737  0.0054  179 ASP E CG  
12495 O OD1 . ASP E 179 ? 1.1325 1.9922 2.2875 0.3605  0.5766  -0.0128 179 ASP E OD1 
12496 O OD2 . ASP E 179 ? 1.1971 1.9908 2.2357 0.4137  0.5673  -0.0175 179 ASP E OD2 
12497 N N   . ILE E 180 ? 1.2659 1.8461 2.0186 0.3461  0.4585  0.1119  180 ILE E N   
12498 C CA  . ILE E 180 ? 1.3034 1.8052 1.9508 0.3413  0.4290  0.1408  180 ILE E CA  
12499 C C   . ILE E 180 ? 1.3549 1.8021 1.9155 0.3476  0.4515  0.1422  180 ILE E C   
12500 O O   . ILE E 180 ? 1.3595 1.8063 1.9314 0.3796  0.4537  0.1217  180 ILE E O   
12501 C CB  . ILE E 180 ? 1.2878 1.7739 1.9368 0.3737  0.3719  0.1430  180 ILE E CB  
12502 C CG1 . ILE E 180 ? 1.2730 1.7861 1.9743 0.4214  0.3619  0.1177  180 ILE E CG1 
12503 C CG2 . ILE E 180 ? 1.2470 1.7723 1.9484 0.3631  0.3407  0.1440  180 ILE E CG2 
12504 C CD1 . ILE E 180 ? 1.2582 1.7598 1.9597 0.4620  0.3077  0.1231  180 ILE E CD1 
12505 N N   . PRO E 181 ? 1.3651 1.7671 1.8423 0.3216  0.4653  0.1612  181 PRO E N   
12506 C CA  . PRO E 181 ? 1.4144 1.7693 1.8120 0.3325  0.4785  0.1528  181 PRO E CA  
12507 C C   . PRO E 181 ? 1.4266 1.7264 1.7964 0.3534  0.4397  0.1505  181 PRO E C   
12508 O O   . PRO E 181 ? 1.4112 1.6915 1.7844 0.3510  0.4045  0.1677  181 PRO E O   
12509 C CB  . PRO E 181 ? 1.4527 1.7764 1.7704 0.3030  0.4933  0.1739  181 PRO E CB  
12510 C CG  . PRO E 181 ? 1.4193 1.7831 1.7903 0.2749  0.5090  0.1928  181 PRO E CG  
12511 C CD  . PRO E 181 ? 1.3674 1.7653 1.8269 0.2841  0.4725  0.1858  181 PRO E CD  
12512 N N   . VAL E 182 ? 1.4125 1.6876 1.7595 0.3752  0.4500  0.1271  182 VAL E N   
12513 C CA  . VAL E 182 ? 1.4293 1.6416 1.7522 0.3907  0.4247  0.1224  182 VAL E CA  
12514 C C   . VAL E 182 ? 1.4788 1.6575 1.7382 0.3880  0.4374  0.0996  182 VAL E C   
12515 O O   . VAL E 182 ? 1.4948 1.6301 1.7512 0.4041  0.4288  0.0784  182 VAL E O   
12516 C CB  . VAL E 182 ? 1.4078 1.6219 1.7902 0.4286  0.4183  0.1091  182 VAL E CB  
12517 C CG1 . VAL E 182 ? 1.4218 1.5613 1.7889 0.4436  0.3991  0.1117  182 VAL E CG1 
12518 C CG2 . VAL E 182 ? 1.3635 1.6240 1.8065 0.4389  0.4017  0.1236  182 VAL E CG2 
12519 N N   . ASN E 183 ? 1.4792 1.6762 1.6883 0.3701  0.4579  0.1023  183 ASN E N   
12520 C CA  . ASN E 183 ? 1.5303 1.7131 1.6758 0.3801  0.4732  0.0727  183 ASN E CA  
12521 C C   . ASN E 183 ? 1.5643 1.6884 1.6697 0.3815  0.4430  0.0542  183 ASN E C   
12522 O O   . ASN E 183 ? 1.5755 1.6801 1.6963 0.4033  0.4402  0.0163  183 ASN E O   
12523 C CB  . ASN E 183 ? 1.5568 1.7621 1.6407 0.3643  0.5016  0.0897  183 ASN E CB  
12524 C CG  . ASN E 183 ? 1.6106 1.8172 1.6225 0.3858  0.5253  0.0580  183 ASN E CG  
12525 O OD1 . ASN E 183 ? 1.6246 1.8225 1.6442 0.4113  0.5187  0.0158  183 ASN E OD1 
12526 N ND2 . ASN E 183 ? 1.6425 1.8572 1.5816 0.3781  0.5536  0.0780  183 ASN E ND2 
12527 N N   . GLY E 184 ? 1.5286 1.6258 1.5948 0.3588  0.4204  0.0750  184 GLY E N   
12528 C CA  . GLY E 184 ? 1.5582 1.6069 1.5991 0.3598  0.3931  0.0493  184 GLY E CA  
12529 C C   . GLY E 184 ? 1.5338 1.5449 1.6040 0.3419  0.3652  0.0672  184 GLY E C   
12530 O O   . GLY E 184 ? 1.5372 1.5083 1.6264 0.3455  0.3515  0.0409  184 GLY E O   
12531 N N   . SER E 185 ? 1.5455 1.5708 1.6257 0.3227  0.3592  0.1087  185 SER E N   
12532 C CA  . SER E 185 ? 1.5235 1.5191 1.6206 0.3065  0.3349  0.1277  185 SER E CA  
12533 C C   . SER E 185 ? 1.4733 1.4860 1.6175 0.3094  0.3335  0.1593  185 SER E C   
12534 O O   . SER E 185 ? 1.4523 1.4372 1.6090 0.3049  0.3183  0.1740  185 SER E O   
12535 C CB  . SER E 185 ? 1.5475 1.5401 1.5991 0.2825  0.3167  0.1405  185 SER E CB  
12536 O OG  . SER E 185 ? 1.5122 1.5065 1.5874 0.2660  0.3008  0.1706  185 SER E OG  
12537 N N   . PHE E 186 ? 1.4804 1.5402 1.6513 0.3195  0.3490  0.1670  186 PHE E N   
12538 C CA  . PHE E 186 ? 1.4355 1.5205 1.6555 0.3311  0.3417  0.1874  186 PHE E CA  
12539 C C   . PHE E 186 ? 1.4241 1.4864 1.6766 0.3639  0.3451  0.1795  186 PHE E C   
12540 O O   . PHE E 186 ? 1.3934 1.4761 1.6820 0.3848  0.3364  0.1932  186 PHE E O   
12541 C CB  . PHE E 186 ? 1.4150 1.5663 1.6677 0.3281  0.3566  0.1909  186 PHE E CB  
12542 C CG  . PHE E 186 ? 1.4147 1.5859 1.6535 0.2966  0.3530  0.2083  186 PHE E CG  
12543 C CD1 . PHE E 186 ? 1.4529 1.5884 1.6310 0.2758  0.3473  0.2117  186 PHE E CD1 
12544 C CD2 . PHE E 186 ? 1.3759 1.6019 1.6713 0.2900  0.3543  0.2171  186 PHE E CD2 
12545 C CE1 . PHE E 186 ? 1.4532 1.6000 1.6207 0.2497  0.3440  0.2299  186 PHE E CE1 
12546 C CE2 . PHE E 186 ? 1.3727 1.6121 1.6676 0.2601  0.3537  0.2321  186 PHE E CE2 
12547 C CZ  . PHE E 186 ? 1.4118 1.6079 1.6392 0.2403  0.3494  0.2416  186 PHE E CZ  
12548 N N   . SER E 187 ? 1.4906 1.5111 1.7344 0.3721  0.3555  0.1548  187 SER E N   
12549 C CA  . SER E 187 ? 1.4844 1.4735 1.7650 0.4033  0.3621  0.1470  187 SER E CA  
12550 C C   . SER E 187 ? 1.4673 1.4104 1.7527 0.4128  0.3491  0.1796  187 SER E C   
12551 O O   . SER E 187 ? 1.4568 1.3862 1.7692 0.4459  0.3496  0.1913  187 SER E O   
12552 C CB  . SER E 187 ? 1.5140 1.4652 1.7935 0.4060  0.3744  0.1077  187 SER E CB  
12553 O OG  . SER E 187 ? 1.5305 1.4458 1.7809 0.3809  0.3648  0.1010  187 SER E OG  
12554 N N   . LEU E 188 ? 1.4672 1.3850 1.7228 0.3878  0.3385  0.1950  188 LEU E N   
12555 C CA  . LEU E 188 ? 1.4531 1.3275 1.7017 0.3961  0.3324  0.2282  188 LEU E CA  
12556 C C   . LEU E 188 ? 1.4241 1.3431 1.6628 0.4047  0.3104  0.2569  188 LEU E C   
12557 O O   . LEU E 188 ? 1.4134 1.3031 1.6363 0.4231  0.3040  0.2864  188 LEU E O   
12558 C CB  . LEU E 188 ? 1.4622 1.2920 1.6919 0.3655  0.3342  0.2253  188 LEU E CB  
12559 C CG  . LEU E 188 ? 1.4846 1.2743 1.7329 0.3530  0.3490  0.1860  188 LEU E CG  
12560 C CD1 . LEU E 188 ? 1.5019 1.3343 1.7310 0.3357  0.3397  0.1504  188 LEU E CD1 
12561 C CD2 . LEU E 188 ? 1.4825 1.2167 1.7357 0.3333  0.3562  0.1903  188 LEU E CD2 
12562 N N   . PHE E 189 ? 1.3865 1.3746 1.6360 0.3943  0.3008  0.2474  189 PHE E N   
12563 C CA  . PHE E 189 ? 1.3538 1.3912 1.6094 0.3984  0.2767  0.2636  189 PHE E CA  
12564 C C   . PHE E 189 ? 1.3348 1.3997 1.6229 0.4439  0.2665  0.2676  189 PHE E C   
12565 O O   . PHE E 189 ? 1.3434 1.4145 1.6622 0.4644  0.2800  0.2518  189 PHE E O   
12566 C CB  . PHE E 189 ? 1.3491 1.4450 1.6179 0.3667  0.2751  0.2508  189 PHE E CB  
12567 C CG  . PHE E 189 ? 1.3695 1.4413 1.6002 0.3287  0.2738  0.2509  189 PHE E CG  
12568 C CD1 . PHE E 189 ? 1.3787 1.3922 1.5780 0.3224  0.2713  0.2572  189 PHE E CD1 
12569 C CD2 . PHE E 189 ? 1.3814 1.4865 1.6112 0.3009  0.2772  0.2447  189 PHE E CD2 
12570 C CE1 . PHE E 189 ? 1.3962 1.3926 1.5687 0.2908  0.2657  0.2505  189 PHE E CE1 
12571 C CE2 . PHE E 189 ? 1.4078 1.4876 1.5993 0.2725  0.2711  0.2444  189 PHE E CE2 
12572 C CZ  . PHE E 189 ? 1.4139 1.4431 1.5791 0.2683  0.2620  0.2440  189 PHE E CZ  
12573 N N   . THR E 190 ? 1.3592 1.4435 1.6404 0.4637  0.2390  0.2848  190 THR E N   
12574 C CA  . THR E 190 ? 1.3455 1.4540 1.6477 0.5166  0.2187  0.2882  190 THR E CA  
12575 C C   . THR E 190 ? 1.3058 1.5065 1.6575 0.5170  0.1906  0.2685  190 THR E C   
12576 O O   . THR E 190 ? 1.2909 1.5213 1.6508 0.4756  0.1889  0.2617  190 THR E O   
12577 C CB  . THR E 190 ? 1.3583 1.4041 1.6016 0.5521  0.2093  0.3240  190 THR E CB  
12578 O OG1 . THR E 190 ? 1.3337 1.4133 1.5539 0.5540  0.1795  0.3319  190 THR E OG1 
12579 C CG2 . THR E 190 ? 1.3883 1.3452 1.5920 0.5280  0.2421  0.3417  190 THR E CG2 
12580 N N   . PRO E 191 ? 1.2619 1.5100 1.6562 0.5635  0.1673  0.2551  191 PRO E N   
12581 C CA  . PRO E 191 ? 1.2191 1.5639 1.6872 0.5612  0.1427  0.2241  191 PRO E CA  
12582 C C   . PRO E 191 ? 1.1923 1.5620 1.6452 0.5508  0.1114  0.2271  191 PRO E C   
12583 O O   . PRO E 191 ? 1.1549 1.6023 1.6819 0.5369  0.0959  0.1971  191 PRO E O   
12584 C CB  . PRO E 191 ? 1.2107 1.5913 1.7203 0.6254  0.1165  0.2070  191 PRO E CB  
12585 C CG  . PRO E 191 ? 1.2491 1.5638 1.7334 0.6429  0.1444  0.2204  191 PRO E CG  
12586 C CD  . PRO E 191 ? 1.2814 1.5023 1.6788 0.6173  0.1666  0.2583  191 PRO E CD  
12587 N N   . ILE E 192 ? 1.2593 1.5686 1.6282 0.5567  0.1044  0.2587  192 ILE E N   
12588 C CA  . ILE E 192 ? 1.2318 1.5696 1.5879 0.5467  0.0753  0.2562  192 ILE E CA  
12589 C C   . ILE E 192 ? 1.2189 1.5744 1.6074 0.4803  0.0919  0.2450  192 ILE E C   
12590 O O   . ILE E 192 ? 1.1834 1.5939 1.6134 0.4659  0.0678  0.2250  192 ILE E O   
12591 C CB  . ILE E 192 ? 1.2555 1.5230 1.5110 0.5682  0.0723  0.2935  192 ILE E CB  
12592 C CG1 . ILE E 192 ? 1.2262 1.5287 1.4662 0.5621  0.0411  0.2861  192 ILE E CG1 
12593 C CG2 . ILE E 192 ? 1.2911 1.4729 1.5004 0.5310  0.1166  0.3195  192 ILE E CG2 
12594 C CD1 . ILE E 192 ? 1.1796 1.5805 1.4882 0.5898  -0.0069 0.2453  192 ILE E CD1 
12595 N N   . SER E 193 ? 1.1834 1.4929 1.5554 0.4428  0.1312  0.2550  193 SER E N   
12596 C CA  . SER E 193 ? 1.1793 1.4977 1.5692 0.3872  0.1468  0.2485  193 SER E CA  
12597 C C   . SER E 193 ? 1.1531 1.5470 1.6355 0.3720  0.1502  0.2215  193 SER E C   
12598 O O   . SER E 193 ? 1.1476 1.5559 1.6536 0.3312  0.1568  0.2180  193 SER E O   
12599 C CB  . SER E 193 ? 1.2265 1.4831 1.5733 0.3618  0.1839  0.2598  193 SER E CB  
12600 O OG  . SER E 193 ? 1.2462 1.4335 1.5278 0.3722  0.1863  0.2797  193 SER E OG  
12601 N N   . PHE E 194 ? 1.1182 1.5591 1.6596 0.4044  0.1478  0.2017  194 PHE E N   
12602 C CA  . PHE E 194 ? 1.0915 1.6049 1.7357 0.3884  0.1622  0.1725  194 PHE E CA  
12603 C C   . PHE E 194 ? 1.0433 1.6366 1.7731 0.4274  0.1226  0.1374  194 PHE E C   
12604 O O   . PHE E 194 ? 1.0198 1.6768 1.8483 0.4280  0.1355  0.1063  194 PHE E O   
12605 C CB  . PHE E 194 ? 1.1177 1.6244 1.7735 0.3854  0.2067  0.1695  194 PHE E CB  
12606 C CG  . PHE E 194 ? 1.1705 1.6006 1.7377 0.3624  0.2383  0.1950  194 PHE E CG  
12607 C CD1 . PHE E 194 ? 1.2013 1.5657 1.6950 0.3860  0.2316  0.2120  194 PHE E CD1 
12608 C CD2 . PHE E 194 ? 1.1907 1.6137 1.7507 0.3198  0.2752  0.2001  194 PHE E CD2 
12609 C CE1 . PHE E 194 ? 1.2461 1.5475 1.6749 0.3660  0.2568  0.2243  194 PHE E CE1 
12610 C CE2 . PHE E 194 ? 1.2416 1.6007 1.7196 0.3059  0.2967  0.2154  194 PHE E CE2 
12611 C CZ  . PHE E 194 ? 1.2668 1.5693 1.6862 0.3283  0.2853  0.2228  194 PHE E CZ  
12612 N N   . ALA E 195 ? 1.1065 1.7014 1.8021 0.4629  0.0750  0.1379  195 ALA E N   
12613 C CA  . ALA E 195 ? 1.0663 1.7394 1.8338 0.5109  0.0279  0.0987  195 ALA E CA  
12614 C C   . ALA E 195 ? 1.0171 1.7737 1.9118 0.4783  0.0221  0.0561  195 ALA E C   
12615 O O   . ALA E 195 ? 1.0109 1.7535 1.9124 0.4249  0.0416  0.0656  195 ALA E O   
12616 C CB  . ALA E 195 ? 1.0644 1.7166 1.7483 0.5584  -0.0200 0.1112  195 ALA E CB  
12617 N N   . ASN E 196 ? 1.0251 1.8682 2.0301 0.5116  -0.0042 0.0062  196 ASN E N   
12618 C CA  . ASN E 196 ? 0.9564 1.8884 2.1105 0.4857  -0.0115 -0.0451 196 ASN E CA  
12619 C C   . ASN E 196 ? 0.9454 1.8722 2.1641 0.4155  0.0577  -0.0365 196 ASN E C   
12620 O O   . ASN E 196 ? 0.8832 1.8542 2.2073 0.3765  0.0661  -0.0620 196 ASN E O   
12621 C CB  . ASN E 196 ? 0.9144 1.8626 2.0633 0.4840  -0.0572 -0.0582 196 ASN E CB  
12622 C CG  . ASN E 196 ? 0.8150 1.8727 2.1304 0.4882  -0.0912 -0.1303 196 ASN E CG  
12623 O OD1 . ASN E 196 ? 0.7703 1.8486 2.1761 0.4331  -0.0697 -0.1450 196 ASN E OD1 
12624 N ND2 . ASN E 196 ? 0.8450 1.9309 2.1551 0.5354  -0.1361 -0.1606 196 ASN E ND2 
12625 N N   . THR E 197 ? 0.9900 1.8608 2.1461 0.4005  0.1093  -0.0011 197 THR E N   
12626 C CA  . THR E 197 ? 0.9935 1.8530 2.1859 0.3425  0.1788  0.0124  197 THR E CA  
12627 C C   . THR E 197 ? 1.0168 1.8785 2.2142 0.3556  0.2200  0.0111  197 THR E C   
12628 O O   . THR E 197 ? 1.0634 1.8763 2.1655 0.3890  0.2116  0.0314  197 THR E O   
12629 C CB  . THR E 197 ? 1.0468 1.8160 2.1209 0.3009  0.2042  0.0653  197 THR E CB  
12630 O OG1 . THR E 197 ? 1.1081 1.8069 2.0593 0.3184  0.2164  0.0985  197 THR E OG1 
12631 C CG2 . THR E 197 ? 1.0337 1.7876 2.0732 0.2984  0.1564  0.0700  197 THR E CG2 
12632 N N   . LYS E 198 ? 0.9589 1.8758 2.2725 0.3281  0.2683  -0.0139 198 LYS E N   
12633 C CA  . LYS E 198 ? 0.9798 1.8984 2.3009 0.3251  0.3268  -0.0131 198 LYS E CA  
12634 C C   . LYS E 198 ? 0.9852 1.9249 2.3056 0.3885  0.2910  -0.0375 198 LYS E C   
12635 O O   . LYS E 198 ? 0.9472 1.9391 2.3269 0.4314  0.2315  -0.0731 198 LYS E O   
12636 C CB  . LYS E 198 ? 1.0510 1.8801 2.2381 0.2946  0.3728  0.0400  198 LYS E CB  
12637 C CG  . LYS E 198 ? 1.0662 1.8495 2.2098 0.2471  0.3859  0.0739  198 LYS E CG  
12638 C CD  . LYS E 198 ? 1.1350 1.8433 2.1588 0.2245  0.4365  0.1166  198 LYS E CD  
12639 C CE  . LYS E 198 ? 1.1850 1.8401 2.0940 0.2594  0.4204  0.1285  198 LYS E CE  
12640 N NZ  . LYS E 198 ? 1.1803 1.8196 2.0557 0.2965  0.3537  0.1255  198 LYS E NZ  
12641 N N   . LEU E 199 ? 0.9418 1.8394 2.1923 0.3996  0.3229  -0.0202 199 LEU E N   
12642 C CA  . LEU E 199 ? 0.9679 1.8748 2.2186 0.4583  0.2976  -0.0401 199 LEU E CA  
12643 C C   . LEU E 199 ? 1.0001 1.8327 2.1433 0.4594  0.3337  -0.0103 199 LEU E C   
12644 O O   . LEU E 199 ? 1.0286 1.8414 2.1459 0.5066  0.3141  -0.0158 199 LEU E O   
12645 C CB  . LEU E 199 ? 0.9690 1.9796 2.3803 0.4737  0.3086  -0.0997 199 LEU E CB  
12646 C CG  . LEU E 199 ? 0.9927 2.0354 2.4374 0.5475  0.2537  -0.1338 199 LEU E CG  
12647 C CD1 . LEU E 199 ? 0.9872 2.0418 2.4240 0.5872  0.1742  -0.1414 199 LEU E CD1 
12648 C CD2 . LEU E 199 ? 1.0079 2.1419 2.5907 0.5529  0.2730  -0.1917 199 LEU E CD2 
12649 N N   . PRO F 1   ? 0.6583 0.8212 1.3132 0.0070  0.0552  0.1124  1   PRO F N   
12650 C CA  . PRO F 1   ? 0.6681 0.7742 1.3514 -0.0050 0.0470  0.1047  1   PRO F CA  
12651 C C   . PRO F 1   ? 0.6652 0.7229 1.3393 0.0068  0.0445  0.1246  1   PRO F C   
12652 O O   . PRO F 1   ? 0.6566 0.7214 1.3131 0.0232  0.0514  0.1259  1   PRO F O   
12653 C CB  . PRO F 1   ? 0.6761 0.7945 1.3869 -0.0142 0.0511  0.0698  1   PRO F CB  
12654 C CG  . PRO F 1   ? 0.6726 0.8604 1.3613 -0.0147 0.0576  0.0583  1   PRO F CG  
12655 C CD  . PRO F 1   ? 0.6618 0.8823 1.3250 -0.0045 0.0567  0.0876  1   PRO F CD  
12656 N N   . VAL F 2   ? 0.6758 0.6872 1.3597 -0.0050 0.0339  0.1413  2   VAL F N   
12657 C CA  . VAL F 2   ? 0.6789 0.6494 1.3500 -0.0023 0.0284  0.1645  2   VAL F CA  
12658 C C   . VAL F 2   ? 0.6746 0.6357 1.3809 0.0051  0.0258  0.1535  2   VAL F C   
12659 O O   . VAL F 2   ? 0.6809 0.6348 1.4371 -0.0011 0.0226  0.1387  2   VAL F O   
12660 C CB  . VAL F 2   ? 0.6971 0.6272 1.3702 -0.0235 0.0145  0.1879  2   VAL F CB  
12661 C CG1 . VAL F 2   ? 0.7054 0.5989 1.3808 -0.0290 0.0023  0.2111  2   VAL F CG1 
12662 C CG2 . VAL F 2   ? 0.7053 0.6362 1.3322 -0.0302 0.0232  0.2019  2   VAL F CG2 
12663 N N   . ARG F 3   ? 0.6675 0.6265 1.3497 0.0182  0.0310  0.1602  3   ARG F N   
12664 C CA  . ARG F 3   ? 0.6631 0.6157 1.3769 0.0263  0.0309  0.1514  3   ARG F CA  
12665 C C   . ARG F 3   ? 0.6680 0.5910 1.3663 0.0231  0.0221  0.1803  3   ARG F C   
12666 O O   . ARG F 3   ? 0.6779 0.5846 1.3293 0.0138  0.0206  0.2026  3   ARG F O   
12667 C CB  . ARG F 3   ? 0.6520 0.6393 1.3504 0.0424  0.0471  0.1266  3   ARG F CB  
12668 C CG  . ARG F 3   ? 0.6501 0.6801 1.3361 0.0415  0.0553  0.1072  3   ARG F CG  
12669 C CD  . ARG F 3   ? 0.6435 0.7112 1.3073 0.0541  0.0682  0.0904  3   ARG F CD  
12670 N NE  . ARG F 3   ? 0.6434 0.7624 1.2891 0.0513  0.0724  0.0832  3   ARG F NE  
12671 C CZ  . ARG F 3   ? 0.6394 0.7789 1.2550 0.0589  0.0744  0.1061  3   ARG F CZ  
12672 N NH1 . ARG F 3   ? 0.6394 0.7457 1.2310 0.0678  0.0771  0.1332  3   ARG F NH1 
12673 N NH2 . ARG F 3   ? 0.6397 0.8356 1.2502 0.0549  0.0760  0.1025  3   ARG F NH2 
12674 N N   . SER F 4   ? 0.6655 0.5822 1.4030 0.0278  0.0186  0.1794  4   SER F N   
12675 C CA  . SER F 4   ? 0.6708 0.5692 1.3969 0.0223  0.0093  0.2061  4   SER F CA  
12676 C C   . SER F 4   ? 0.6625 0.5725 1.3475 0.0369  0.0254  0.1950  4   SER F C   
12677 O O   . SER F 4   ? 0.6512 0.5844 1.3433 0.0529  0.0399  0.1664  4   SER F O   
12678 C CB  . SER F 4   ? 0.6738 0.5640 1.4761 0.0198  -0.0041 0.2180  4   SER F CB  
12679 O OG  . SER F 4   ? 0.6654 0.5697 1.5166 0.0361  0.0114  0.1856  4   SER F OG  
12680 N N   . SER F 5   ? 0.6737 0.5659 1.3110 0.0273  0.0240  0.2176  5   SER F N   
12681 C CA  . SER F 5   ? 0.6715 0.5680 1.2650 0.0393  0.0413  0.2096  5   SER F CA  
12682 C C   . SER F 5   ? 0.6601 0.5692 1.3004 0.0494  0.0406  0.1973  5   SER F C   
12683 O O   . SER F 5   ? 0.6596 0.5669 1.3623 0.0431  0.0252  0.2074  5   SER F O   
12684 C CB  . SER F 5   ? 0.6954 0.5628 1.2246 0.0202  0.0437  0.2351  5   SER F CB  
12685 O OG  . SER F 5   ? 0.7099 0.5621 1.2596 -0.0066 0.0196  0.2630  5   SER F OG  
12686 N N   . GLN F 6   ? 0.6533 0.5762 1.2669 0.0659  0.0593  0.1771  6   GLN F N   
12687 C CA  . GLN F 6   ? 0.6448 0.5802 1.2961 0.0757  0.0645  0.1600  6   GLN F CA  
12688 C C   . GLN F 6   ? 0.6520 0.5781 1.2560 0.0746  0.0723  0.1691  6   GLN F C   
12689 O O   . GLN F 6   ? 0.6594 0.5805 1.1971 0.0802  0.0882  0.1681  6   GLN F O   
12690 C CB  . GLN F 6   ? 0.6360 0.5979 1.2964 0.0907  0.0807  0.1240  6   GLN F CB  
12691 C CG  . GLN F 6   ? 0.6348 0.6040 1.3577 0.0874  0.0773  0.1069  6   GLN F CG  
12692 C CD  . GLN F 6   ? 0.6362 0.6069 1.4237 0.0908  0.0864  0.0858  6   GLN F CD  
12693 O OE1 . GLN F 6   ? 0.6348 0.6120 1.4125 0.0978  0.0981  0.0742  6   GLN F OE1 
12694 N NE2 . GLN F 6   ? 0.6428 0.6044 1.4987 0.0858  0.0846  0.0809  6   GLN F NE2 
12695 N N   . SER F 7   ? 0.6526 0.5772 1.2944 0.0677  0.0632  0.1794  7   SER F N   
12696 C CA  . SER F 7   ? 0.6618 0.5796 1.2611 0.0630  0.0707  0.1861  7   SER F CA  
12697 C C   . SER F 7   ? 0.6543 0.5862 1.2382 0.0831  0.0934  0.1547  7   SER F C   
12698 O O   . SER F 7   ? 0.6428 0.5931 1.2812 0.0941  0.0982  0.1309  7   SER F O   
12699 C CB  . SER F 7   ? 0.6643 0.5866 1.3164 0.0483  0.0523  0.2089  7   SER F CB  
12700 O OG  . SER F 7   ? 0.6811 0.5934 1.2778 0.0325  0.0553  0.2232  7   SER F OG  
12701 N N   . SER F 8   ? 0.6665 0.5869 1.1751 0.0857  0.1103  0.1550  8   SER F N   
12702 C CA  . SER F 8   ? 0.6642 0.5977 1.1502 0.1026  0.1310  0.1306  8   SER F CA  
12703 C C   . SER F 8   ? 0.6658 0.6004 1.1682 0.0981  0.1334  0.1264  8   SER F C   
12704 O O   . SER F 8   ? 0.6749 0.5972 1.1782 0.0801  0.1226  0.1487  8   SER F O   
12705 C CB  . SER F 8   ? 0.6807 0.5999 1.0856 0.1098  0.1509  0.1372  8   SER F CB  
12706 O OG  . SER F 8   ? 0.6749 0.6199 1.0709 0.1290  0.1644  0.1173  8   SER F OG  
12707 N N   . GLN F 9   ? 0.6598 0.6125 1.1759 0.1109  0.1474  0.0981  9   GLN F N   
12708 C CA  . GLN F 9   ? 0.6621 0.6177 1.1938 0.1078  0.1538  0.0909  9   GLN F CA  
12709 C C   . GLN F 9   ? 0.6816 0.6166 1.1329 0.1024  0.1665  0.1020  9   GLN F C   
12710 O O   . GLN F 9   ? 0.6945 0.6145 1.0790 0.1079  0.1787  0.1076  9   GLN F O   
12711 C CB  . GLN F 9   ? 0.6571 0.6338 1.2184 0.1192  0.1698  0.0542  9   GLN F CB  
12712 C CG  . GLN F 9   ? 0.6501 0.6370 1.3025 0.1168  0.1685  0.0438  9   GLN F CG  
12713 C CD  . GLN F 9   ? 0.6528 0.6542 1.3379 0.1227  0.1881  0.0030  9   GLN F CD  
12714 O OE1 . GLN F 9   ? 0.6620 0.6710 1.2937 0.1253  0.2037  -0.0189 9   GLN F OE1 
12715 N NE2 . GLN F 9   ? 0.6508 0.6544 1.4230 0.1221  0.1896  -0.0063 9   GLN F NE2 
12716 N N   . ALA F 10  ? 0.6871 0.6211 1.1486 0.0908  0.1659  0.1068  10  ALA F N   
12717 C CA  . ALA F 10  ? 0.7112 0.6229 1.0961 0.0816  0.1814  0.1136  10  ALA F CA  
12718 C C   . ALA F 10  ? 0.7168 0.6307 1.0612 0.0995  0.2067  0.0882  10  ALA F C   
12719 O O   . ALA F 10  ? 0.7032 0.6415 1.0878 0.1116  0.2107  0.0626  10  ALA F O   
12720 C CB  . ALA F 10  ? 0.7166 0.6341 1.1266 0.0604  0.1720  0.1263  10  ALA F CB  
12721 N N   . GLY F 11  ? 0.7432 0.6288 1.0052 0.0985  0.2263  0.0963  11  GLY F N   
12722 C CA  . GLY F 11  ? 0.7542 0.6408 0.9735 0.1145  0.2499  0.0796  11  GLY F CA  
12723 C C   . GLY F 11  ? 0.7551 0.6517 0.9893 0.1082  0.2562  0.0611  11  GLY F C   
12724 O O   . GLY F 11  ? 0.7612 0.6504 1.0028 0.0889  0.2510  0.0697  11  GLY F O   
12725 N N   . GLY F 12  ? 0.7520 0.6689 0.9899 0.1215  0.2674  0.0363  12  GLY F N   
12726 C CA  . GLY F 12  ? 0.7552 0.6818 1.0075 0.1158  0.2774  0.0144  12  GLY F CA  
12727 C C   . GLY F 12  ? 0.7833 0.6934 0.9586 0.1197  0.3022  0.0099  12  GLY F C   
12728 O O   . GLY F 12  ? 0.7986 0.6973 0.9193 0.1324  0.3128  0.0216  12  GLY F O   
12729 N N   . ARG F 13  ? 0.7925 0.7018 0.9663 0.1095  0.3129  -0.0044 13  ARG F N   
12730 C CA  . ARG F 13  ? 0.8227 0.7140 0.9234 0.1115  0.3377  -0.0094 13  ARG F CA  
12731 C C   . ARG F 13  ? 0.8239 0.7422 0.9316 0.1184  0.3470  -0.0384 13  ARG F C   
12732 O O   . ARG F 13  ? 0.8410 0.7606 0.8990 0.1297  0.3572  -0.0348 13  ARG F O   
12733 C CB  . ARG F 13  ? 0.8390 0.7118 0.9215 0.0916  0.3463  -0.0082 13  ARG F CB  
12734 C CG  . ARG F 13  ? 0.8800 0.7144 0.8685 0.0902  0.3738  -0.0009 13  ARG F CG  
12735 C CD  . ARG F 13  ? 0.8996 0.7149 0.8665 0.0640  0.3809  0.0018  13  ARG F CD  
12736 N NE  . ARG F 13  ? 0.9439 0.7070 0.8202 0.0557  0.4047  0.0198  13  ARG F NE  
12737 C CZ  . ARG F 13  ? 0.9814 0.7158 0.7946 0.0453  0.4314  0.0140  13  ARG F CZ  
12738 N NH1 . ARG F 13  ? 0.9778 0.7336 0.8063 0.0418  0.4358  -0.0091 13  ARG F NH1 
12739 N NH2 . ARG F 13  ? 1.0282 0.7075 0.7601 0.0367  0.4579  0.0305  13  ARG F NH2 
# 
