data_7QQB
# 
_entry.id   7QQB 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.372 
_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   7QQB         pdb_00007qqb 10.2210/pdb7qqb/pdb 
WWPDB D_1292120101 ?            ?                   
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        7QQB 
_pdbx_database_status.recvd_initial_deposition_date   2022-01-07 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Serris, A.'         1 ?                   
'Rey, F.A.'          2 ?                   
'Guardado-Calvo, P.' 3 0000-0001-7292-5270 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Sci Transl Med' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1946-6242 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            15 
_citation.language                  ? 
_citation.page_first                eadg1855 
_citation.page_last                 eadg1855 
_citation.title                     'Structural and mechanistic basis of neutralization by a pan-hantavirus protective antibody.' 
_citation.year                      2023 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1126/scitranslmed.adg1855 
_citation.pdbx_database_id_PubMed   37315110 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Mittler, E.'        1  0000-0002-5935-6314 
primary 'Serris, A.'         2  0000-0002-7444-4662 
primary 'Esterman, E.S.'     3  0000-0001-7365-0547 
primary 'Florez, C.'         4  0000-0002-0407-861X 
primary 'Polanco, L.C.'      5  ?                   
primary 
;O'Brien, C.M.
;
6  0000-0001-7160-0220 
primary 'Slough, M.M.'       7  0000-0003-3514-578X 
primary 'Tynell, J.'         8  0000-0001-6930-5230 
primary 'Groning, R.'        9  0000-0001-5384-8038 
primary 'Sun, Y.'            10 0000-0002-5747-3306 
primary 'Abelson, D.M.'      11 ?                   
primary 'Wec, A.Z.'          12 0000-0002-2134-2152 
primary 'Haslwanter, D.'     13 0000-0003-2727-0468 
primary 'Keller, M.'         14 0000-0003-3229-8377 
primary 'Ye, C.'             15 ?                   
primary 'Bakken, R.R.'       16 ?                   
primary 'Jangra, R.K.'       17 0000-0002-3119-0869 
primary 'Dye, J.M.'          18 ?                   
primary 'Ahlm, C.'           19 0000-0003-2018-8592 
primary 'Rappazzo, C.G.'     20 0000-0002-8415-444X 
primary 'Ulrich, R.G.'       21 0000-0002-5620-1528 
primary 'Zeitlin, L.'        22 0000-0002-6857-1024 
primary 'Geoghegan, J.C.'    23 ?                   
primary 'Bradfute, S.B.'     24 0000-0002-1985-751X 
primary 'Sidoli, S.'         25 0000-0001-9073-6641 
primary 'Forsell, M.N.E.'    26 0000-0001-6904-742X 
primary 'Strandin, T.'       27 0000-0002-2454-7479 
primary 'Rey, F.A.'          28 0000-0002-9953-7988 
primary 'Herbert, A.S.'      29 0009-0001-5256-7733 
primary 'Walker, L.M.'       30 0000-0001-7704-3197 
primary 'Chandran, K.'       31 0000-0003-0232-7077 
primary 'Guardado-Calvo, P.' 32 0000-0001-7292-5270 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     7QQB 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     83.876 
_cell.length_a_esd                 ? 
_cell.length_b                     109.304 
_cell.length_b_esd                 ? 
_cell.length_c                     149.540 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
# 
_symmetry.entry_id                         7QQB 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 2 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
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 'Envelope polyprotein' 95672.578 2  ? ? ? ? 
2 polymer     man 'Single Chain Variable Fragment (scFv) of ADI-42898' 31558.834 2  ? ? ? ? 
3 branched    man 
;alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose
;
1072.964  1  ? ? ? ? 
4 branched    man '2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose' 424.401   2  ? ? ? ? 
5 non-polymer syn GLYCEROL 92.094    1  ? ? ? ? 
6 water       nat water 18.015    26 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'M polyprotein' 
# 
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 
;RSSRGDTRNLNELKMECPHTIGLGQGLVIGSIELPPVPLIQVESLKLESSCNFDLHTSTSSQQAFTKWTWEVKSDLAENT
QASSTSFQTKSSEVNLRGLCLVPPLVIETAARTRKTIACFDLSCNQTTCQPTVFLMGPIQTCITTKSCLLGLGDQRIQVN
YEKTYCVSGQLIEGICFNPVHTMALSQPSHTYDIVTVMVRCFLIVKKVTTGDSMKIEKSFETLVQKTGCTDNGFQGYYVC
LIGSSSEPLYIPTLDDYRSAEVLSRMAFAPHGEDHDIEKNAISAMRIVGKVTGKAPSTESSDTVQGIAFSGNPLYTSTGV
LTAKDDPVYVWAPGIMMEGNHSVCDKKTLPLTWTGFIPLPGEIEGGSGLVPRGSGGGSGGGSWSHPQFEKGGGTGGGTLV
PRGSGTGGETQNLNSGWTDTAHGSGVIPMRTDLELDFSLPSSASYTYRRQLQNPANEQEKIPFHLQISKQVIHAEIQHLG
HWMDGTFNLKTAFHCYGSCEKYAYPWQTAGCFVEKDYEYESGWGCNPADCPGVGTGCTACGVYLDKLKSVGKAFKIVSLR
YTRKACIQLGTEQTCKNVDSNDCLVTTSVKVCLIGTVSKFQPSDTLLFLGPLEQGGLIFKQWCTTTCQFGDPGDIMSTPV
GMKCPELSGSFRKKCAFATTPVCQFDGNTISGYKRMIATKDSFQSFNVTEPHISASSLEWIDPDSSLRDHINVIVGRDLS
FQDLSETPCQVDLTTTSIDGAWGSGVGFNLICSVSLTECSTFLTSIKACDSAMCYGSTTANLVRGQNTVHIVGKGGHSGS
KFMCCHDTKCSSTGLVAAAPHLDRVTGYNQADSDKIFDDGAPEGLVPRGSGPFEDDDDKAGWSHPQFEKGGGSGGGSGGG
SWSHPQFEK
;
;RSSRGDTRNLNELKMECPHTIGLGQGLVIGSIELPPVPLIQVESLKLESSCNFDLHTSTSSQQAFTKWTWEVKSDLAENT
QASSTSFQTKSSEVNLRGLCLVPPLVIETAARTRKTIACFDLSCNQTTCQPTVFLMGPIQTCITTKSCLLGLGDQRIQVN
YEKTYCVSGQLIEGICFNPVHTMALSQPSHTYDIVTVMVRCFLIVKKVTTGDSMKIEKSFETLVQKTGCTDNGFQGYYVC
LIGSSSEPLYIPTLDDYRSAEVLSRMAFAPHGEDHDIEKNAISAMRIVGKVTGKAPSTESSDTVQGIAFSGNPLYTSTGV
LTAKDDPVYVWAPGIMMEGNHSVCDKKTLPLTWTGFIPLPGEIEGGSGLVPRGSGGGSGGGSWSHPQFEKGGGTGGGTLV
PRGSGTGGETQNLNSGWTDTAHGSGVIPMRTDLELDFSLPSSASYTYRRQLQNPANEQEKIPFHLQISKQVIHAEIQHLG
HWMDGTFNLKTAFHCYGSCEKYAYPWQTAGCFVEKDYEYESGWGCNPADCPGVGTGCTACGVYLDKLKSVGKAFKIVSLR
YTRKACIQLGTEQTCKNVDSNDCLVTTSVKVCLIGTVSKFQPSDTLLFLGPLEQGGLIFKQWCTTTCQFGDPGDIMSTPV
GMKCPELSGSFRKKCAFATTPVCQFDGNTISGYKRMIATKDSFQSFNVTEPHISASSLEWIDPDSSLRDHINVIVGRDLS
FQDLSETPCQVDLTTTSIDGAWGSGVGFNLICSVSLTECSTFLTSIKACDSAMCYGSTTANLVRGQNTVHIVGKGGHSGS
KFMCCHDTKCSSTGLVAAAPHLDRVTGYNQADSDKIFDDGAPEGLVPRGSGPFEDDDDKAGWSHPQFEKGGGSGGGSGGG
SWSHPQFEK
;
A,B ? 
2 'polypeptide(L)' no no 
;RSQVQLVESGGGVVQPGRSLRLSCAASGFTFSSYAMHWVRQAPGKGLEWVAVTWFDVSKKDYADSVKGRFTISRDNSKNT
LYLQMNSLRAEDTAVYYCARNLIRYSGSYFPVHGMDVWGQGTTVTVSSGTGGSGGGGSGGGGSGGGASDIVMTQSPLSLP
VTPGEPASISCRSSQSLLHTYGYNCLDWYLQRPGQSPQLLISLGSYRASGVPDRFSGSGSGTDFTLKISRVEAEDVGVYY
CMQALHPFTFGGGTKVEIKGPFEDDDDKAGWSHPQFEKGGGSGGGSGGGSWSHPQFEK
;
;RSQVQLVESGGGVVQPGRSLRLSCAASGFTFSSYAMHWVRQAPGKGLEWVAVTWFDVSKKDYADSVKGRFTISRDNSKNT
LYLQMNSLRAEDTAVYYCARNLIRYSGSYFPVHGMDVWGQGTTVTVSSGTGGSGGGGSGGGGSGGGASDIVMTQSPLSLP
VTPGEPASISCRSSQSLLHTYGYNCLDWYLQRPGQSPQLLISLGSYRASGVPDRFSGSGSGTDFTLKISRVEAEDVGVYY
CMQALHPFTFGGGTKVEIKGPFEDDDDKAGWSHPQFEKGGGSGGGSGGGSWSHPQFEK
;
H,L ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ARG n 
1 2   SER n 
1 3   SER n 
1 4   ARG n 
1 5   GLY n 
1 6   ASP n 
1 7   THR n 
1 8   ARG n 
1 9   ASN n 
1 10  LEU n 
1 11  ASN n 
1 12  GLU n 
1 13  LEU n 
1 14  LYS n 
1 15  MET n 
1 16  GLU n 
1 17  CYS n 
1 18  PRO n 
1 19  HIS n 
1 20  THR n 
1 21  ILE n 
1 22  GLY n 
1 23  LEU n 
1 24  GLY n 
1 25  GLN n 
1 26  GLY n 
1 27  LEU n 
1 28  VAL n 
1 29  ILE n 
1 30  GLY n 
1 31  SER n 
1 32  ILE n 
1 33  GLU n 
1 34  LEU n 
1 35  PRO n 
1 36  PRO n 
1 37  VAL n 
1 38  PRO n 
1 39  LEU n 
1 40  ILE n 
1 41  GLN n 
1 42  VAL n 
1 43  GLU n 
1 44  SER n 
1 45  LEU n 
1 46  LYS n 
1 47  LEU n 
1 48  GLU n 
1 49  SER n 
1 50  SER n 
1 51  CYS n 
1 52  ASN n 
1 53  PHE n 
1 54  ASP n 
1 55  LEU n 
1 56  HIS n 
1 57  THR n 
1 58  SER n 
1 59  THR n 
1 60  SER n 
1 61  SER n 
1 62  GLN n 
1 63  GLN n 
1 64  ALA n 
1 65  PHE n 
1 66  THR n 
1 67  LYS n 
1 68  TRP n 
1 69  THR n 
1 70  TRP n 
1 71  GLU n 
1 72  VAL n 
1 73  LYS n 
1 74  SER n 
1 75  ASP n 
1 76  LEU n 
1 77  ALA n 
1 78  GLU n 
1 79  ASN n 
1 80  THR n 
1 81  GLN n 
1 82  ALA n 
1 83  SER n 
1 84  SER n 
1 85  THR n 
1 86  SER n 
1 87  PHE n 
1 88  GLN n 
1 89  THR n 
1 90  LYS n 
1 91  SER n 
1 92  SER n 
1 93  GLU n 
1 94  VAL n 
1 95  ASN n 
1 96  LEU n 
1 97  ARG n 
1 98  GLY n 
1 99  LEU n 
1 100 CYS n 
1 101 LEU n 
1 102 VAL n 
1 103 PRO n 
1 104 PRO n 
1 105 LEU n 
1 106 VAL n 
1 107 ILE n 
1 108 GLU n 
1 109 THR n 
1 110 ALA n 
1 111 ALA n 
1 112 ARG n 
1 113 THR n 
1 114 ARG n 
1 115 LYS n 
1 116 THR n 
1 117 ILE n 
1 118 ALA n 
1 119 CYS n 
1 120 PHE n 
1 121 ASP n 
1 122 LEU n 
1 123 SER n 
1 124 CYS n 
1 125 ASN n 
1 126 GLN n 
1 127 THR n 
1 128 THR n 
1 129 CYS n 
1 130 GLN n 
1 131 PRO n 
1 132 THR n 
1 133 VAL n 
1 134 PHE n 
1 135 LEU n 
1 136 MET n 
1 137 GLY n 
1 138 PRO n 
1 139 ILE n 
1 140 GLN n 
1 141 THR n 
1 142 CYS n 
1 143 ILE n 
1 144 THR n 
1 145 THR n 
1 146 LYS n 
1 147 SER n 
1 148 CYS n 
1 149 LEU n 
1 150 LEU n 
1 151 GLY n 
1 152 LEU n 
1 153 GLY n 
1 154 ASP n 
1 155 GLN n 
1 156 ARG n 
1 157 ILE n 
1 158 GLN n 
1 159 VAL n 
1 160 ASN n 
1 161 TYR n 
1 162 GLU n 
1 163 LYS n 
1 164 THR n 
1 165 TYR n 
1 166 CYS n 
1 167 VAL n 
1 168 SER n 
1 169 GLY n 
1 170 GLN n 
1 171 LEU n 
1 172 ILE n 
1 173 GLU n 
1 174 GLY n 
1 175 ILE n 
1 176 CYS n 
1 177 PHE n 
1 178 ASN n 
1 179 PRO n 
1 180 VAL n 
1 181 HIS n 
1 182 THR n 
1 183 MET n 
1 184 ALA n 
1 185 LEU n 
1 186 SER n 
1 187 GLN n 
1 188 PRO n 
1 189 SER n 
1 190 HIS n 
1 191 THR n 
1 192 TYR n 
1 193 ASP n 
1 194 ILE n 
1 195 VAL n 
1 196 THR n 
1 197 VAL n 
1 198 MET n 
1 199 VAL n 
1 200 ARG n 
1 201 CYS n 
1 202 PHE n 
1 203 LEU n 
1 204 ILE n 
1 205 VAL n 
1 206 LYS n 
1 207 LYS n 
1 208 VAL n 
1 209 THR n 
1 210 THR n 
1 211 GLY n 
1 212 ASP n 
1 213 SER n 
1 214 MET n 
1 215 LYS n 
1 216 ILE n 
1 217 GLU n 
1 218 LYS n 
1 219 SER n 
1 220 PHE n 
1 221 GLU n 
1 222 THR n 
1 223 LEU n 
1 224 VAL n 
1 225 GLN n 
1 226 LYS n 
1 227 THR n 
1 228 GLY n 
1 229 CYS n 
1 230 THR n 
1 231 ASP n 
1 232 ASN n 
1 233 GLY n 
1 234 PHE n 
1 235 GLN n 
1 236 GLY n 
1 237 TYR n 
1 238 TYR n 
1 239 VAL n 
1 240 CYS n 
1 241 LEU n 
1 242 ILE n 
1 243 GLY n 
1 244 SER n 
1 245 SER n 
1 246 SER n 
1 247 GLU n 
1 248 PRO n 
1 249 LEU n 
1 250 TYR n 
1 251 ILE n 
1 252 PRO n 
1 253 THR n 
1 254 LEU n 
1 255 ASP n 
1 256 ASP n 
1 257 TYR n 
1 258 ARG n 
1 259 SER n 
1 260 ALA n 
1 261 GLU n 
1 262 VAL n 
1 263 LEU n 
1 264 SER n 
1 265 ARG n 
1 266 MET n 
1 267 ALA n 
1 268 PHE n 
1 269 ALA n 
1 270 PRO n 
1 271 HIS n 
1 272 GLY n 
1 273 GLU n 
1 274 ASP n 
1 275 HIS n 
1 276 ASP n 
1 277 ILE n 
1 278 GLU n 
1 279 LYS n 
1 280 ASN n 
1 281 ALA n 
1 282 ILE n 
1 283 SER n 
1 284 ALA n 
1 285 MET n 
1 286 ARG n 
1 287 ILE n 
1 288 VAL n 
1 289 GLY n 
1 290 LYS n 
1 291 VAL n 
1 292 THR n 
1 293 GLY n 
1 294 LYS n 
1 295 ALA n 
1 296 PRO n 
1 297 SER n 
1 298 THR n 
1 299 GLU n 
1 300 SER n 
1 301 SER n 
1 302 ASP n 
1 303 THR n 
1 304 VAL n 
1 305 GLN n 
1 306 GLY n 
1 307 ILE n 
1 308 ALA n 
1 309 PHE n 
1 310 SER n 
1 311 GLY n 
1 312 ASN n 
1 313 PRO n 
1 314 LEU n 
1 315 TYR n 
1 316 THR n 
1 317 SER n 
1 318 THR n 
1 319 GLY n 
1 320 VAL n 
1 321 LEU n 
1 322 THR n 
1 323 ALA n 
1 324 LYS n 
1 325 ASP n 
1 326 ASP n 
1 327 PRO n 
1 328 VAL n 
1 329 TYR n 
1 330 VAL n 
1 331 TRP n 
1 332 ALA n 
1 333 PRO n 
1 334 GLY n 
1 335 ILE n 
1 336 MET n 
1 337 MET n 
1 338 GLU n 
1 339 GLY n 
1 340 ASN n 
1 341 HIS n 
1 342 SER n 
1 343 VAL n 
1 344 CYS n 
1 345 ASP n 
1 346 LYS n 
1 347 LYS n 
1 348 THR n 
1 349 LEU n 
1 350 PRO n 
1 351 LEU n 
1 352 THR n 
1 353 TRP n 
1 354 THR n 
1 355 GLY n 
1 356 PHE n 
1 357 ILE n 
1 358 PRO n 
1 359 LEU n 
1 360 PRO n 
1 361 GLY n 
1 362 GLU n 
1 363 ILE n 
1 364 GLU n 
1 365 GLY n 
1 366 GLY n 
1 367 SER n 
1 368 GLY n 
1 369 LEU n 
1 370 VAL n 
1 371 PRO n 
1 372 ARG n 
1 373 GLY n 
1 374 SER n 
1 375 GLY n 
1 376 GLY n 
1 377 GLY n 
1 378 SER n 
1 379 GLY n 
1 380 GLY n 
1 381 GLY n 
1 382 SER n 
1 383 TRP n 
1 384 SER n 
1 385 HIS n 
1 386 PRO n 
1 387 GLN n 
1 388 PHE n 
1 389 GLU n 
1 390 LYS n 
1 391 GLY n 
1 392 GLY n 
1 393 GLY n 
1 394 THR n 
1 395 GLY n 
1 396 GLY n 
1 397 GLY n 
1 398 THR n 
1 399 LEU n 
1 400 VAL n 
1 401 PRO n 
1 402 ARG n 
1 403 GLY n 
1 404 SER n 
1 405 GLY n 
1 406 THR n 
1 407 GLY n 
1 408 GLY n 
1 409 GLU n 
1 410 THR n 
1 411 GLN n 
1 412 ASN n 
1 413 LEU n 
1 414 ASN n 
1 415 SER n 
1 416 GLY n 
1 417 TRP n 
1 418 THR n 
1 419 ASP n 
1 420 THR n 
1 421 ALA n 
1 422 HIS n 
1 423 GLY n 
1 424 SER n 
1 425 GLY n 
1 426 VAL n 
1 427 ILE n 
1 428 PRO n 
1 429 MET n 
1 430 ARG n 
1 431 THR n 
1 432 ASP n 
1 433 LEU n 
1 434 GLU n 
1 435 LEU n 
1 436 ASP n 
1 437 PHE n 
1 438 SER n 
1 439 LEU n 
1 440 PRO n 
1 441 SER n 
1 442 SER n 
1 443 ALA n 
1 444 SER n 
1 445 TYR n 
1 446 THR n 
1 447 TYR n 
1 448 ARG n 
1 449 ARG n 
1 450 GLN n 
1 451 LEU n 
1 452 GLN n 
1 453 ASN n 
1 454 PRO n 
1 455 ALA n 
1 456 ASN n 
1 457 GLU n 
1 458 GLN n 
1 459 GLU n 
1 460 LYS n 
1 461 ILE n 
1 462 PRO n 
1 463 PHE n 
1 464 HIS n 
1 465 LEU n 
1 466 GLN n 
1 467 ILE n 
1 468 SER n 
1 469 LYS n 
1 470 GLN n 
1 471 VAL n 
1 472 ILE n 
1 473 HIS n 
1 474 ALA n 
1 475 GLU n 
1 476 ILE n 
1 477 GLN n 
1 478 HIS n 
1 479 LEU n 
1 480 GLY n 
1 481 HIS n 
1 482 TRP n 
1 483 MET n 
1 484 ASP n 
1 485 GLY n 
1 486 THR n 
1 487 PHE n 
1 488 ASN n 
1 489 LEU n 
1 490 LYS n 
1 491 THR n 
1 492 ALA n 
1 493 PHE n 
1 494 HIS n 
1 495 CYS n 
1 496 TYR n 
1 497 GLY n 
1 498 SER n 
1 499 CYS n 
1 500 GLU n 
1 501 LYS n 
1 502 TYR n 
1 503 ALA n 
1 504 TYR n 
1 505 PRO n 
1 506 TRP n 
1 507 GLN n 
1 508 THR n 
1 509 ALA n 
1 510 GLY n 
1 511 CYS n 
1 512 PHE n 
1 513 VAL n 
1 514 GLU n 
1 515 LYS n 
1 516 ASP n 
1 517 TYR n 
1 518 GLU n 
1 519 TYR n 
1 520 GLU n 
1 521 SER n 
1 522 GLY n 
1 523 TRP n 
1 524 GLY n 
1 525 CYS n 
1 526 ASN n 
1 527 PRO n 
1 528 ALA n 
1 529 ASP n 
1 530 CYS n 
1 531 PRO n 
1 532 GLY n 
1 533 VAL n 
1 534 GLY n 
1 535 THR n 
1 536 GLY n 
1 537 CYS n 
1 538 THR n 
1 539 ALA n 
1 540 CYS n 
1 541 GLY n 
1 542 VAL n 
1 543 TYR n 
1 544 LEU n 
1 545 ASP n 
1 546 LYS n 
1 547 LEU n 
1 548 LYS n 
1 549 SER n 
1 550 VAL n 
1 551 GLY n 
1 552 LYS n 
1 553 ALA n 
1 554 PHE n 
1 555 LYS n 
1 556 ILE n 
1 557 VAL n 
1 558 SER n 
1 559 LEU n 
1 560 ARG n 
1 561 TYR n 
1 562 THR n 
1 563 ARG n 
1 564 LYS n 
1 565 ALA n 
1 566 CYS n 
1 567 ILE n 
1 568 GLN n 
1 569 LEU n 
1 570 GLY n 
1 571 THR n 
1 572 GLU n 
1 573 GLN n 
1 574 THR n 
1 575 CYS n 
1 576 LYS n 
1 577 ASN n 
1 578 VAL n 
1 579 ASP n 
1 580 SER n 
1 581 ASN n 
1 582 ASP n 
1 583 CYS n 
1 584 LEU n 
1 585 VAL n 
1 586 THR n 
1 587 THR n 
1 588 SER n 
1 589 VAL n 
1 590 LYS n 
1 591 VAL n 
1 592 CYS n 
1 593 LEU n 
1 594 ILE n 
1 595 GLY n 
1 596 THR n 
1 597 VAL n 
1 598 SER n 
1 599 LYS n 
1 600 PHE n 
1 601 GLN n 
1 602 PRO n 
1 603 SER n 
1 604 ASP n 
1 605 THR n 
1 606 LEU n 
1 607 LEU n 
1 608 PHE n 
1 609 LEU n 
1 610 GLY n 
1 611 PRO n 
1 612 LEU n 
1 613 GLU n 
1 614 GLN n 
1 615 GLY n 
1 616 GLY n 
1 617 LEU n 
1 618 ILE n 
1 619 PHE n 
1 620 LYS n 
1 621 GLN n 
1 622 TRP n 
1 623 CYS n 
1 624 THR n 
1 625 THR n 
1 626 THR n 
1 627 CYS n 
1 628 GLN n 
1 629 PHE n 
1 630 GLY n 
1 631 ASP n 
1 632 PRO n 
1 633 GLY n 
1 634 ASP n 
1 635 ILE n 
1 636 MET n 
1 637 SER n 
1 638 THR n 
1 639 PRO n 
1 640 VAL n 
1 641 GLY n 
1 642 MET n 
1 643 LYS n 
1 644 CYS n 
1 645 PRO n 
1 646 GLU n 
1 647 LEU n 
1 648 SER n 
1 649 GLY n 
1 650 SER n 
1 651 PHE n 
1 652 ARG n 
1 653 LYS n 
1 654 LYS n 
1 655 CYS n 
1 656 ALA n 
1 657 PHE n 
1 658 ALA n 
1 659 THR n 
1 660 THR n 
1 661 PRO n 
1 662 VAL n 
1 663 CYS n 
1 664 GLN n 
1 665 PHE n 
1 666 ASP n 
1 667 GLY n 
1 668 ASN n 
1 669 THR n 
1 670 ILE n 
1 671 SER n 
1 672 GLY n 
1 673 TYR n 
1 674 LYS n 
1 675 ARG n 
1 676 MET n 
1 677 ILE n 
1 678 ALA n 
1 679 THR n 
1 680 LYS n 
1 681 ASP n 
1 682 SER n 
1 683 PHE n 
1 684 GLN n 
1 685 SER n 
1 686 PHE n 
1 687 ASN n 
1 688 VAL n 
1 689 THR n 
1 690 GLU n 
1 691 PRO n 
1 692 HIS n 
1 693 ILE n 
1 694 SER n 
1 695 ALA n 
1 696 SER n 
1 697 SER n 
1 698 LEU n 
1 699 GLU n 
1 700 TRP n 
1 701 ILE n 
1 702 ASP n 
1 703 PRO n 
1 704 ASP n 
1 705 SER n 
1 706 SER n 
1 707 LEU n 
1 708 ARG n 
1 709 ASP n 
1 710 HIS n 
1 711 ILE n 
1 712 ASN n 
1 713 VAL n 
1 714 ILE n 
1 715 VAL n 
1 716 GLY n 
1 717 ARG n 
1 718 ASP n 
1 719 LEU n 
1 720 SER n 
1 721 PHE n 
1 722 GLN n 
1 723 ASP n 
1 724 LEU n 
1 725 SER n 
1 726 GLU n 
1 727 THR n 
1 728 PRO n 
1 729 CYS n 
1 730 GLN n 
1 731 VAL n 
1 732 ASP n 
1 733 LEU n 
1 734 THR n 
1 735 THR n 
1 736 THR n 
1 737 SER n 
1 738 ILE n 
1 739 ASP n 
1 740 GLY n 
1 741 ALA n 
1 742 TRP n 
1 743 GLY n 
1 744 SER n 
1 745 GLY n 
1 746 VAL n 
1 747 GLY n 
1 748 PHE n 
1 749 ASN n 
1 750 LEU n 
1 751 ILE n 
1 752 CYS n 
1 753 SER n 
1 754 VAL n 
1 755 SER n 
1 756 LEU n 
1 757 THR n 
1 758 GLU n 
1 759 CYS n 
1 760 SER n 
1 761 THR n 
1 762 PHE n 
1 763 LEU n 
1 764 THR n 
1 765 SER n 
1 766 ILE n 
1 767 LYS n 
1 768 ALA n 
1 769 CYS n 
1 770 ASP n 
1 771 SER n 
1 772 ALA n 
1 773 MET n 
1 774 CYS n 
1 775 TYR n 
1 776 GLY n 
1 777 SER n 
1 778 THR n 
1 779 THR n 
1 780 ALA n 
1 781 ASN n 
1 782 LEU n 
1 783 VAL n 
1 784 ARG n 
1 785 GLY n 
1 786 GLN n 
1 787 ASN n 
1 788 THR n 
1 789 VAL n 
1 790 HIS n 
1 791 ILE n 
1 792 VAL n 
1 793 GLY n 
1 794 LYS n 
1 795 GLY n 
1 796 GLY n 
1 797 HIS n 
1 798 SER n 
1 799 GLY n 
1 800 SER n 
1 801 LYS n 
1 802 PHE n 
1 803 MET n 
1 804 CYS n 
1 805 CYS n 
1 806 HIS n 
1 807 ASP n 
1 808 THR n 
1 809 LYS n 
1 810 CYS n 
1 811 SER n 
1 812 SER n 
1 813 THR n 
1 814 GLY n 
1 815 LEU n 
1 816 VAL n 
1 817 ALA n 
1 818 ALA n 
1 819 ALA n 
1 820 PRO n 
1 821 HIS n 
1 822 LEU n 
1 823 ASP n 
1 824 ARG n 
1 825 VAL n 
1 826 THR n 
1 827 GLY n 
1 828 TYR n 
1 829 ASN n 
1 830 GLN n 
1 831 ALA n 
1 832 ASP n 
1 833 SER n 
1 834 ASP n 
1 835 LYS n 
1 836 ILE n 
1 837 PHE n 
1 838 ASP n 
1 839 ASP n 
1 840 GLY n 
1 841 ALA n 
1 842 PRO n 
1 843 GLU n 
1 844 GLY n 
1 845 LEU n 
1 846 VAL n 
1 847 PRO n 
1 848 ARG n 
1 849 GLY n 
1 850 SER n 
1 851 GLY n 
1 852 PRO n 
1 853 PHE n 
1 854 GLU n 
1 855 ASP n 
1 856 ASP n 
1 857 ASP n 
1 858 ASP n 
1 859 LYS n 
1 860 ALA n 
1 861 GLY n 
1 862 TRP n 
1 863 SER n 
1 864 HIS n 
1 865 PRO n 
1 866 GLN n 
1 867 PHE n 
1 868 GLU n 
1 869 LYS n 
1 870 GLY n 
1 871 GLY n 
1 872 GLY n 
1 873 SER n 
1 874 GLY n 
1 875 GLY n 
1 876 GLY n 
1 877 SER n 
1 878 GLY n 
1 879 GLY n 
1 880 GLY n 
1 881 SER n 
1 882 TRP n 
1 883 SER n 
1 884 HIS n 
1 885 PRO n 
1 886 GLN n 
1 887 PHE n 
1 888 GLU n 
1 889 LYS n 
2 1   ARG n 
2 2   SER n 
2 3   GLN n 
2 4   VAL n 
2 5   GLN n 
2 6   LEU n 
2 7   VAL n 
2 8   GLU n 
2 9   SER n 
2 10  GLY n 
2 11  GLY n 
2 12  GLY n 
2 13  VAL n 
2 14  VAL n 
2 15  GLN n 
2 16  PRO n 
2 17  GLY n 
2 18  ARG n 
2 19  SER n 
2 20  LEU n 
2 21  ARG n 
2 22  LEU n 
2 23  SER n 
2 24  CYS n 
2 25  ALA n 
2 26  ALA n 
2 27  SER n 
2 28  GLY n 
2 29  PHE n 
2 30  THR n 
2 31  PHE n 
2 32  SER n 
2 33  SER n 
2 34  TYR n 
2 35  ALA n 
2 36  MET n 
2 37  HIS n 
2 38  TRP n 
2 39  VAL n 
2 40  ARG n 
2 41  GLN n 
2 42  ALA n 
2 43  PRO n 
2 44  GLY n 
2 45  LYS n 
2 46  GLY n 
2 47  LEU n 
2 48  GLU n 
2 49  TRP n 
2 50  VAL n 
2 51  ALA n 
2 52  VAL n 
2 53  THR n 
2 54  TRP n 
2 55  PHE n 
2 56  ASP n 
2 57  VAL n 
2 58  SER n 
2 59  LYS n 
2 60  LYS n 
2 61  ASP n 
2 62  TYR n 
2 63  ALA n 
2 64  ASP n 
2 65  SER n 
2 66  VAL n 
2 67  LYS n 
2 68  GLY n 
2 69  ARG n 
2 70  PHE n 
2 71  THR n 
2 72  ILE n 
2 73  SER n 
2 74  ARG n 
2 75  ASP n 
2 76  ASN n 
2 77  SER n 
2 78  LYS n 
2 79  ASN n 
2 80  THR n 
2 81  LEU n 
2 82  TYR n 
2 83  LEU n 
2 84  GLN n 
2 85  MET n 
2 86  ASN n 
2 87  SER n 
2 88  LEU n 
2 89  ARG n 
2 90  ALA n 
2 91  GLU n 
2 92  ASP n 
2 93  THR n 
2 94  ALA n 
2 95  VAL n 
2 96  TYR n 
2 97  TYR n 
2 98  CYS n 
2 99  ALA n 
2 100 ARG n 
2 101 ASN n 
2 102 LEU n 
2 103 ILE n 
2 104 ARG n 
2 105 TYR n 
2 106 SER n 
2 107 GLY n 
2 108 SER n 
2 109 TYR n 
2 110 PHE n 
2 111 PRO n 
2 112 VAL n 
2 113 HIS n 
2 114 GLY n 
2 115 MET n 
2 116 ASP n 
2 117 VAL n 
2 118 TRP n 
2 119 GLY n 
2 120 GLN n 
2 121 GLY n 
2 122 THR n 
2 123 THR n 
2 124 VAL n 
2 125 THR n 
2 126 VAL n 
2 127 SER n 
2 128 SER n 
2 129 GLY n 
2 130 THR n 
2 131 GLY n 
2 132 GLY n 
2 133 SER n 
2 134 GLY n 
2 135 GLY n 
2 136 GLY n 
2 137 GLY n 
2 138 SER n 
2 139 GLY n 
2 140 GLY n 
2 141 GLY n 
2 142 GLY n 
2 143 SER n 
2 144 GLY n 
2 145 GLY n 
2 146 GLY n 
2 147 ALA n 
2 148 SER n 
2 149 ASP n 
2 150 ILE n 
2 151 VAL n 
2 152 MET n 
2 153 THR n 
2 154 GLN n 
2 155 SER n 
2 156 PRO n 
2 157 LEU n 
2 158 SER n 
2 159 LEU n 
2 160 PRO n 
2 161 VAL n 
2 162 THR n 
2 163 PRO n 
2 164 GLY n 
2 165 GLU n 
2 166 PRO n 
2 167 ALA n 
2 168 SER n 
2 169 ILE n 
2 170 SER n 
2 171 CYS n 
2 172 ARG n 
2 173 SER n 
2 174 SER n 
2 175 GLN n 
2 176 SER n 
2 177 LEU n 
2 178 LEU n 
2 179 HIS n 
2 180 THR n 
2 181 TYR n 
2 182 GLY n 
2 183 TYR n 
2 184 ASN n 
2 185 CYS n 
2 186 LEU n 
2 187 ASP n 
2 188 TRP n 
2 189 TYR n 
2 190 LEU n 
2 191 GLN n 
2 192 ARG n 
2 193 PRO n 
2 194 GLY n 
2 195 GLN n 
2 196 SER n 
2 197 PRO n 
2 198 GLN n 
2 199 LEU n 
2 200 LEU n 
2 201 ILE n 
2 202 SER n 
2 203 LEU n 
2 204 GLY n 
2 205 SER n 
2 206 TYR n 
2 207 ARG n 
2 208 ALA n 
2 209 SER n 
2 210 GLY n 
2 211 VAL n 
2 212 PRO n 
2 213 ASP n 
2 214 ARG n 
2 215 PHE n 
2 216 SER n 
2 217 GLY n 
2 218 SER n 
2 219 GLY n 
2 220 SER n 
2 221 GLY n 
2 222 THR n 
2 223 ASP n 
2 224 PHE n 
2 225 THR n 
2 226 LEU n 
2 227 LYS n 
2 228 ILE n 
2 229 SER n 
2 230 ARG n 
2 231 VAL n 
2 232 GLU n 
2 233 ALA n 
2 234 GLU n 
2 235 ASP n 
2 236 VAL n 
2 237 GLY n 
2 238 VAL n 
2 239 TYR n 
2 240 TYR n 
2 241 CYS n 
2 242 MET n 
2 243 GLN n 
2 244 ALA n 
2 245 LEU n 
2 246 HIS n 
2 247 PRO n 
2 248 PHE n 
2 249 THR n 
2 250 PHE n 
2 251 GLY n 
2 252 GLY n 
2 253 GLY n 
2 254 THR n 
2 255 LYS n 
2 256 VAL n 
2 257 GLU n 
2 258 ILE n 
2 259 LYS n 
2 260 GLY n 
2 261 PRO n 
2 262 PHE n 
2 263 GLU n 
2 264 ASP n 
2 265 ASP n 
2 266 ASP n 
2 267 ASP n 
2 268 LYS n 
2 269 ALA n 
2 270 GLY n 
2 271 TRP n 
2 272 SER n 
2 273 HIS n 
2 274 PRO n 
2 275 GLN n 
2 276 PHE n 
2 277 GLU n 
2 278 LYS n 
2 279 GLY n 
2 280 GLY n 
2 281 GLY n 
2 282 SER n 
2 283 GLY n 
2 284 GLY n 
2 285 GLY n 
2 286 SER n 
2 287 GLY n 
2 288 GLY n 
2 289 GLY n 
2 290 SER n 
2 291 TRP n 
2 292 SER n 
2 293 HIS n 
2 294 PRO n 
2 295 GLN n 
2 296 PHE n 
2 297 GLU n 
2 298 LYS 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   408 ? ? ? ? ? ? ? ? ? 'Puumala orthohantavirus' 1980486 ? ? ? ? ? ? ? ? 
'Drosophila melanogaster' 7227 ? ? ? ? ? ? ? ? 'S2 cells' ? ? ? ? ? ? ? ? ? ? ? ? 
1 2 sample 'Biological sequence' 409 889 ? ? ? ? ? ? ? ? ? 'Puumala orthohantavirus' 1980486 ? ? ? ? ? ? ? ? 
'Drosophila melanogaster' 7227 ? ? ? ? ? ? ? ? 'S2 cells' ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1   298 ? ? ? ? ? ? ? ? ? 'Homo sapiens'            9606    ? ? ? ? ? ? ? ? 
'Drosophila melanogaster' 7227 ? ? ? ? ? ? ? ? 'S2 cells' ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 A0A0B4U5I0_9VIRU A0A0B4U5I0 ? 1 
;SRGDTRNLNELKMECPHTIGLGQGLVIGSIELPPVPLIQVESLKLESSCNFDLHTSTSSQQAFTKWTWEVKSDLAENTQA
SSTSFQTKSSEVNLRGLCLVPPLVIETAARTRKTIACFDLSCNQTTCQPTVFLMGPIQTCITTKSCLLGLGDQRIQVNYE
KTYCVSGQLIEGICFNPVHTMALSQPSHTYDIVTVMVRCFLIVKKVTTGDSMKIEKSFETLVQKTGCTDNGFQGYYVCLI
GSSSEPLYIPTLDDYRSAEVLSRMAFAPHGEDHDIEKNAISAMRIVGKVTGKAPSTESSDTVQGIAFSGNPLYTSTGVLT
AKDDPVYVWAPGIMMEGNHSVCEKKTLPLTWTGFIPLPGEIE
;
20  
2 UNP A0A6M3W7M6_9VIRU A0A6M3W7M6 ? 1 
;ETQNLNSGWTDTAHGSGVIPMRTDLELDFSLPSSASYTYRRQLQNPANEQEKIPFHLQISKQVIHAEIQHLGHWMDGTFN
LKTAFHCYGSCEKYAYPWQTAGCFVEKDYEYESGWGCNPADCPGVGTGCTACGVYLDKLKSVGKAFKIVSLRYTRKACIQ
LGTEQTCKNVDSNDCLVTTSVKVCLIGTVSKFQPSDTLLFLGPLEQGGLIFKQWCTTTCQFGDPGDIMSTPVGMKCPELS
GSFRKKCAFATTPVCQFDGNTISGYKRMIATKDSFQSFNVTEPHISASSLEWIDPDSSLRDHINVIVGRDLSFQDLSETP
CQVDLTTTSIDGAWGSGVGFNLICSVSLTECSTFLTSIKACDSAMCYGSTTANLVRGQNTVHIVGKGGHSGSKFMCCHDT
KCSSTGLVAAAPHLDRVTGYNQADSDKIFDDGAPE
;
659 
3 PDB 7QQB             7QQB       ? 2 ? 1   
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7QQB A 3   ? 364 ? A0A0B4U5I0 20   ? 381  ? 20   381  
2 2 7QQB A 409 ? 843 ? A0A6M3W7M6 659  ? 1093 ? 426  860  
3 1 7QQB B 3   ? 364 ? A0A0B4U5I0 20   ? 381  ? 253  614  
4 2 7QQB B 409 ? 843 ? A0A6M3W7M6 659  ? 1093 ? 659  1093 
5 3 7QQB H 1   ? 298 ? 7QQB       -1   ? 283  ? -1   283  
6 3 7QQB L 1   ? 298 ? 7QQB       -147 ? 145  ? -147 145  
# 
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 7QQB ARG A 1   ? UNP A0A0B4U5I0 ?   ?   'expression tag' 18   1   
1 7QQB SER A 2   ? UNP A0A0B4U5I0 ?   ?   'expression tag' 19   2   
1 7QQB ASP A 345 ? UNP A0A0B4U5I0 GLU 362 conflict         362  3   
1 7QQB GLY A 365 ? UNP A0A0B4U5I0 ?   ?   linker           382  4   
1 7QQB GLY A 366 ? UNP A0A0B4U5I0 ?   ?   linker           383  5   
1 7QQB SER A 367 ? UNP A0A0B4U5I0 ?   ?   linker           384  6   
1 7QQB GLY A 368 ? UNP A0A0B4U5I0 ?   ?   linker           385  7   
1 7QQB LEU A 369 ? UNP A0A0B4U5I0 ?   ?   linker           386  8   
1 7QQB VAL A 370 ? UNP A0A0B4U5I0 ?   ?   linker           387  9   
1 7QQB PRO A 371 ? UNP A0A0B4U5I0 ?   ?   linker           388  10  
1 7QQB ARG A 372 ? UNP A0A0B4U5I0 ?   ?   linker           389  11  
1 7QQB GLY A 373 ? UNP A0A0B4U5I0 ?   ?   linker           390  12  
1 7QQB SER A 374 ? UNP A0A0B4U5I0 ?   ?   linker           391  13  
1 7QQB GLY A 375 ? UNP A0A0B4U5I0 ?   ?   linker           392  14  
1 7QQB GLY A 376 ? UNP A0A0B4U5I0 ?   ?   linker           393  15  
1 7QQB GLY A 377 ? UNP A0A0B4U5I0 ?   ?   linker           394  16  
1 7QQB SER A 378 ? UNP A0A0B4U5I0 ?   ?   linker           395  17  
1 7QQB GLY A 379 ? UNP A0A0B4U5I0 ?   ?   linker           396  18  
1 7QQB GLY A 380 ? UNP A0A0B4U5I0 ?   ?   linker           397  19  
1 7QQB GLY A 381 ? UNP A0A0B4U5I0 ?   ?   linker           398  20  
1 7QQB SER A 382 ? UNP A0A0B4U5I0 ?   ?   linker           399  21  
1 7QQB TRP A 383 ? UNP A0A0B4U5I0 ?   ?   linker           400  22  
1 7QQB SER A 384 ? UNP A0A0B4U5I0 ?   ?   linker           401  23  
1 7QQB HIS A 385 ? UNP A0A0B4U5I0 ?   ?   linker           402  24  
1 7QQB PRO A 386 ? UNP A0A0B4U5I0 ?   ?   linker           403  25  
1 7QQB GLN A 387 ? UNP A0A0B4U5I0 ?   ?   linker           404  26  
1 7QQB PHE A 388 ? UNP A0A0B4U5I0 ?   ?   linker           405  27  
1 7QQB GLU A 389 ? UNP A0A0B4U5I0 ?   ?   linker           406  28  
1 7QQB LYS A 390 ? UNP A0A0B4U5I0 ?   ?   linker           407  29  
1 7QQB GLY A 391 ? UNP A0A0B4U5I0 ?   ?   linker           408  30  
1 7QQB GLY A 392 ? UNP A0A0B4U5I0 ?   ?   linker           409  31  
1 7QQB GLY A 393 ? UNP A0A0B4U5I0 ?   ?   linker           410  32  
1 7QQB THR A 394 ? UNP A0A0B4U5I0 ?   ?   linker           411  33  
1 7QQB GLY A 395 ? UNP A0A0B4U5I0 ?   ?   linker           412  34  
1 7QQB GLY A 396 ? UNP A0A0B4U5I0 ?   ?   linker           413  35  
1 7QQB GLY A 397 ? UNP A0A0B4U5I0 ?   ?   linker           414  36  
1 7QQB THR A 398 ? UNP A0A0B4U5I0 ?   ?   linker           415  37  
1 7QQB LEU A 399 ? UNP A0A0B4U5I0 ?   ?   linker           416  38  
1 7QQB VAL A 400 ? UNP A0A0B4U5I0 ?   ?   linker           417  39  
1 7QQB PRO A 401 ? UNP A0A0B4U5I0 ?   ?   linker           418  40  
1 7QQB ARG A 402 ? UNP A0A0B4U5I0 ?   ?   linker           419  41  
1 7QQB GLY A 403 ? UNP A0A0B4U5I0 ?   ?   linker           420  42  
1 7QQB SER A 404 ? UNP A0A0B4U5I0 ?   ?   linker           421  43  
1 7QQB GLY A 405 ? UNP A0A0B4U5I0 ?   ?   linker           422  44  
1 7QQB THR A 406 ? UNP A0A0B4U5I0 ?   ?   linker           423  45  
1 7QQB GLY A 407 ? UNP A0A0B4U5I0 ?   ?   linker           424  46  
1 7QQB GLY A 408 ? UNP A0A0B4U5I0 ?   ?   linker           425  47  
2 7QQB GLY A 844 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 861  48  
2 7QQB LEU A 845 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 862  49  
2 7QQB VAL A 846 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 863  50  
2 7QQB PRO A 847 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 864  51  
2 7QQB ARG A 848 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 865  52  
2 7QQB GLY A 849 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 866  53  
2 7QQB SER A 850 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 867  54  
2 7QQB GLY A 851 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 868  55  
2 7QQB PRO A 852 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 869  56  
2 7QQB PHE A 853 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 870  57  
2 7QQB GLU A 854 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 871  58  
2 7QQB ASP A 855 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 872  59  
2 7QQB ASP A 856 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 873  60  
2 7QQB ASP A 857 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 874  61  
2 7QQB ASP A 858 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 875  62  
2 7QQB LYS A 859 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 876  63  
2 7QQB ALA A 860 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 877  64  
2 7QQB GLY A 861 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 878  65  
2 7QQB TRP A 862 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 879  66  
2 7QQB SER A 863 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 880  67  
2 7QQB HIS A 864 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 881  68  
2 7QQB PRO A 865 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 882  69  
2 7QQB GLN A 866 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 883  70  
2 7QQB PHE A 867 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 884  71  
2 7QQB GLU A 868 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 885  72  
2 7QQB LYS A 869 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 886  73  
2 7QQB GLY A 870 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 887  74  
2 7QQB GLY A 871 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 888  75  
2 7QQB GLY A 872 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 889  76  
2 7QQB SER A 873 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 890  77  
2 7QQB GLY A 874 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 891  78  
2 7QQB GLY A 875 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 892  79  
2 7QQB GLY A 876 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 893  80  
2 7QQB SER A 877 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 894  81  
2 7QQB GLY A 878 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 895  82  
2 7QQB GLY A 879 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 896  83  
2 7QQB GLY A 880 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 897  84  
2 7QQB SER A 881 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 898  85  
2 7QQB TRP A 882 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 899  86  
2 7QQB SER A 883 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 900  87  
2 7QQB HIS A 884 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 901  88  
2 7QQB PRO A 885 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 902  89  
2 7QQB GLN A 886 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 903  90  
2 7QQB PHE A 887 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 904  91  
2 7QQB GLU A 888 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 905  92  
2 7QQB LYS A 889 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 906  93  
3 7QQB ARG B 1   ? UNP A0A0B4U5I0 ?   ?   'expression tag' 251  94  
3 7QQB SER B 2   ? UNP A0A0B4U5I0 ?   ?   'expression tag' 252  95  
3 7QQB ASP B 345 ? UNP A0A0B4U5I0 GLU 362 conflict         595  96  
3 7QQB GLY B 365 ? UNP A0A0B4U5I0 ?   ?   linker           615  97  
3 7QQB GLY B 366 ? UNP A0A0B4U5I0 ?   ?   linker           616  98  
3 7QQB SER B 367 ? UNP A0A0B4U5I0 ?   ?   linker           617  99  
3 7QQB GLY B 368 ? UNP A0A0B4U5I0 ?   ?   linker           618  100 
3 7QQB LEU B 369 ? UNP A0A0B4U5I0 ?   ?   linker           619  101 
3 7QQB VAL B 370 ? UNP A0A0B4U5I0 ?   ?   linker           620  102 
3 7QQB PRO B 371 ? UNP A0A0B4U5I0 ?   ?   linker           621  103 
3 7QQB ARG B 372 ? UNP A0A0B4U5I0 ?   ?   linker           622  104 
3 7QQB GLY B 373 ? UNP A0A0B4U5I0 ?   ?   linker           623  105 
3 7QQB SER B 374 ? UNP A0A0B4U5I0 ?   ?   linker           624  106 
3 7QQB GLY B 375 ? UNP A0A0B4U5I0 ?   ?   linker           625  107 
3 7QQB GLY B 376 ? UNP A0A0B4U5I0 ?   ?   linker           626  108 
3 7QQB GLY B 377 ? UNP A0A0B4U5I0 ?   ?   linker           627  109 
3 7QQB SER B 378 ? UNP A0A0B4U5I0 ?   ?   linker           628  110 
3 7QQB GLY B 379 ? UNP A0A0B4U5I0 ?   ?   linker           629  111 
3 7QQB GLY B 380 ? UNP A0A0B4U5I0 ?   ?   linker           630  112 
3 7QQB GLY B 381 ? UNP A0A0B4U5I0 ?   ?   linker           631  113 
3 7QQB SER B 382 ? UNP A0A0B4U5I0 ?   ?   linker           632  114 
3 7QQB TRP B 383 ? UNP A0A0B4U5I0 ?   ?   linker           633  115 
3 7QQB SER B 384 ? UNP A0A0B4U5I0 ?   ?   linker           634  116 
3 7QQB HIS B 385 ? UNP A0A0B4U5I0 ?   ?   linker           635  117 
3 7QQB PRO B 386 ? UNP A0A0B4U5I0 ?   ?   linker           636  118 
3 7QQB GLN B 387 ? UNP A0A0B4U5I0 ?   ?   linker           637  119 
3 7QQB PHE B 388 ? UNP A0A0B4U5I0 ?   ?   linker           638  120 
3 7QQB GLU B 389 ? UNP A0A0B4U5I0 ?   ?   linker           639  121 
3 7QQB LYS B 390 ? UNP A0A0B4U5I0 ?   ?   linker           640  122 
3 7QQB GLY B 391 ? UNP A0A0B4U5I0 ?   ?   linker           641  123 
3 7QQB GLY B 392 ? UNP A0A0B4U5I0 ?   ?   linker           642  124 
3 7QQB GLY B 393 ? UNP A0A0B4U5I0 ?   ?   linker           643  125 
3 7QQB THR B 394 ? UNP A0A0B4U5I0 ?   ?   linker           644  126 
3 7QQB GLY B 395 ? UNP A0A0B4U5I0 ?   ?   linker           645  127 
3 7QQB GLY B 396 ? UNP A0A0B4U5I0 ?   ?   linker           646  128 
3 7QQB GLY B 397 ? UNP A0A0B4U5I0 ?   ?   linker           647  129 
3 7QQB THR B 398 ? UNP A0A0B4U5I0 ?   ?   linker           648  130 
3 7QQB LEU B 399 ? UNP A0A0B4U5I0 ?   ?   linker           649  131 
3 7QQB VAL B 400 ? UNP A0A0B4U5I0 ?   ?   linker           650  132 
3 7QQB PRO B 401 ? UNP A0A0B4U5I0 ?   ?   linker           651  133 
3 7QQB ARG B 402 ? UNP A0A0B4U5I0 ?   ?   linker           652  134 
3 7QQB GLY B 403 ? UNP A0A0B4U5I0 ?   ?   linker           653  135 
3 7QQB SER B 404 ? UNP A0A0B4U5I0 ?   ?   linker           654  136 
3 7QQB GLY B 405 ? UNP A0A0B4U5I0 ?   ?   linker           655  137 
3 7QQB THR B 406 ? UNP A0A0B4U5I0 ?   ?   linker           656  138 
3 7QQB GLY B 407 ? UNP A0A0B4U5I0 ?   ?   linker           657  139 
3 7QQB GLY B 408 ? UNP A0A0B4U5I0 ?   ?   linker           658  140 
4 7QQB GLY B 844 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 1094 141 
4 7QQB LEU B 845 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 1095 142 
4 7QQB VAL B 846 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 1096 143 
4 7QQB PRO B 847 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 1097 144 
4 7QQB ARG B 848 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 1098 145 
4 7QQB GLY B 849 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 1099 146 
4 7QQB SER B 850 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 1100 147 
4 7QQB GLY B 851 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 1101 148 
4 7QQB PRO B 852 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 1102 149 
4 7QQB PHE B 853 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 1103 150 
4 7QQB GLU B 854 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 1104 151 
4 7QQB ASP B 855 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 1105 152 
4 7QQB ASP B 856 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 1106 153 
4 7QQB ASP B 857 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 1107 154 
4 7QQB ASP B 858 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 1108 155 
4 7QQB LYS B 859 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 1109 156 
4 7QQB ALA B 860 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 1110 157 
4 7QQB GLY B 861 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 1111 158 
4 7QQB TRP B 862 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 1112 159 
4 7QQB SER B 863 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 1113 160 
4 7QQB HIS B 864 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 1114 161 
4 7QQB PRO B 865 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 1115 162 
4 7QQB GLN B 866 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 1116 163 
4 7QQB PHE B 867 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 1117 164 
4 7QQB GLU B 868 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 1118 165 
4 7QQB LYS B 869 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 1119 166 
4 7QQB GLY B 870 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 1120 167 
4 7QQB GLY B 871 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 1121 168 
4 7QQB GLY B 872 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 1122 169 
4 7QQB SER B 873 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 1123 170 
4 7QQB GLY B 874 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 1124 171 
4 7QQB GLY B 875 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 1125 172 
4 7QQB GLY B 876 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 1126 173 
4 7QQB SER B 877 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 1127 174 
4 7QQB GLY B 878 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 1128 175 
4 7QQB GLY B 879 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 1129 176 
4 7QQB GLY B 880 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 1130 177 
4 7QQB SER B 881 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 1131 178 
4 7QQB TRP B 882 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 1132 179 
4 7QQB SER B 883 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 1133 180 
4 7QQB HIS B 884 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 1134 181 
4 7QQB PRO B 885 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 1135 182 
4 7QQB GLN B 886 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 1136 183 
4 7QQB PHE B 887 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 1137 184 
4 7QQB GLU B 888 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 1138 185 
4 7QQB LYS B 889 ? UNP A0A6M3W7M6 ?   ?   'expression tag' 1139 186 
# 
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 
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  
GOL non-polymer                   . GLYCEROL                                 'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       
92.094  
HIS 'L-peptide linking'           y HISTIDINE                                ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer                   . WATER                                    ? 'H2 O'           18.015  
ILE 'L-peptide linking'           y ISOLEUCINE                               ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking'           y LEUCINE                                  ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking'           y LYSINE                                   ? 'C6 H15 N2 O2 1' 147.195 
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 
# 
_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                   7QQB 
_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            ? 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         ? 
_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_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            298 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '25%(w/v) PEG 1000, 0.1M Hepes 7.5' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2020-01-27 
_diffrn_detector.pdbx_frequency               ? 
# 
_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   0.98 
_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                        'SOLEIL BEAMLINE PROXIMA 1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.98 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'PROXIMA 1' 
_diffrn_source.pdbx_synchrotron_site       SOLEIL 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       7QQB 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.600 
_reflns.d_resolution_low                               39.890 
_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                                     43057 
_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                           100.000 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                11.500 
_reflns.pdbx_Rmerge_I_obs                              0.120 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          14.200 
_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                                0.126 
_reflns.pdbx_Rpim_I_all                                0.037 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       495751 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_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                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_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 
_reflns_shell.percent_possible_all 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_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_Rsym_value 
_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 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_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 
2.600 2.700  ? ? 53168 ? ? ? 4457 100.000 ? ? ? ? 2.912 ? ? ? ? ? ? ? ? 11.900 ? ? ? 0.900  3.043 0.879 ? 1 1 0.503 ? ? ? ? ? ? ? 
? ? ? 
9.730 39.890 ? ? 8957  ? ? ? 925  98.700  ? ? ? ? 0.029 ? ? ? ? ? ? ? ? 9.700  ? ? ? 57.400 0.030 0.010 ? 2 1 0.999 ? ? ? ? ? ? ? 
? ? ? 
# 
_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                                209.450 
_refine.B_iso_mean                               85.6355 
_refine.B_iso_min                                44.100 
_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                                 7QQB 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.6 
_refine.ls_d_res_low                             39 
_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                     43057 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    100 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       0.249 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.212 
_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                    ? 
_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                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      6Y5F 
_refine.pdbx_stereochemistry_target_values       ? 
_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             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_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                 ? 
_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                            ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        7674 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         134 
_refine_hist.number_atoms_solvent             26 
_refine_hist.number_atoms_total               7834 
_refine_hist.d_res_high                       2.6 
_refine_hist.d_res_low                        39 
# 
_struct.entry_id                     7QQB 
_struct.title                        
;Crystal structure of the envelope glycoprotein complex of Puumala virus in complex with the scFv fragment of the broadly neutralizing human antibody ADI-42898
;
_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        7QQB 
_struct_keywords.text            'hantavirus, neutralizing antibodies, fusion proteins, bunyavirus, VIRAL PROTEIN' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 4 ? 
G N N 4 ? 
H N N 5 ? 
I N N 6 ? 
J N N 6 ? 
K N N 6 ? 
L N N 6 ? 
# 
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 ILE A 40  ? VAL A 42  ? ILE A 57  VAL A 59  5 ? 3  
HELX_P HELX_P2  AA2 THR A 57  ? SER A 60  ? THR A 74  SER A 77  5 ? 4  
HELX_P HELX_P3  AA3 THR A 109 ? ARG A 114 ? THR A 126 ARG A 131 1 ? 6  
HELX_P HELX_P4  AA4 GLN A 140 ? THR A 145 ? GLN A 157 THR A 162 1 ? 6  
HELX_P HELX_P5  AA5 LYS A 215 ? VAL A 224 ? LYS A 232 VAL A 241 1 ? 10 
HELX_P HELX_P6  AA6 ASP A 256 ? ALA A 269 ? ASP A 273 ALA A 286 1 ? 14 
HELX_P HELX_P7  AA7 TYR B 504 ? ALA B 509 ? TYR B 754 ALA B 759 5 ? 6  
HELX_P HELX_P8  AA8 PRO B 611 ? GLY B 615 ? PRO B 861 GLY B 865 5 ? 5  
HELX_P HELX_P9  AA9 SER B 671 ? ALA B 678 ? SER B 921 ALA B 928 1 ? 8  
HELX_P HELX_P10 AB1 THR B 679 ? PHE B 683 ? THR B 929 PHE B 933 5 ? 5  
HELX_P HELX_P11 AB2 SER B 720 ? SER B 725 ? SER B 970 SER B 975 1 ? 6  
HELX_P HELX_P12 AB3 ARG C 89  ? THR C 93  ? ARG H 83  THR H 87  5 ? 5  
HELX_P HELX_P13 AB4 GLU D 232 ? VAL D 236 ? GLU L 79  VAL L 83  5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ?    ? A CYS 17  SG  ? ? ? 1_555 A CYS 142 SG ? ? A CYS 34   A CYS 159  1_555 ? ? ? ? ? ? ? 2.029 ? ? 
disulf2  disulf ?    ? A CYS 51  SG  ? ? ? 1_555 A CYS 148 SG ? ? A CYS 68   A CYS 165  1_555 ? ? ? ? ? ? ? 2.026 ? ? 
disulf3  disulf ?    ? A CYS 100 SG  ? ? ? 1_555 A CYS 119 SG ? ? A CYS 117  A CYS 136  1_555 ? ? ? ? ? ? ? 2.033 ? ? 
disulf4  disulf ?    ? A CYS 124 SG  ? ? ? 1_555 A CYS 129 SG ? ? A CYS 141  A CYS 146  1_555 ? ? ? ? ? ? ? 2.029 ? ? 
disulf5  disulf ?    ? A CYS 166 SG  ? ? ? 1_555 A CYS 176 SG ? ? A CYS 183  A CYS 193  1_555 ? ? ? ? ? ? ? 2.032 ? ? 
disulf6  disulf ?    ? A CYS 201 SG  ? ? ? 1_555 A CYS 240 SG ? ? A CYS 218  A CYS 257  1_555 ? ? ? ? ? ? ? 2.029 ? ? 
disulf7  disulf ?    ? A CYS 229 SG  ? ? ? 1_555 A CYS 344 SG ? ? A CYS 246  A CYS 361  1_555 ? ? ? ? ? ? ? 2.034 ? ? 
disulf8  disulf ?    ? B CYS 495 SG  ? ? ? 1_555 B CYS 530 SG ? ? B CYS 745  B CYS 780  1_555 ? ? ? ? ? ? ? 2.037 ? ? 
disulf9  disulf ?    ? B CYS 499 SG  ? ? ? 1_555 B CYS 537 SG ? ? B CYS 749  B CYS 787  1_555 ? ? ? ? ? ? ? 2.031 ? ? 
disulf10 disulf ?    ? B CYS 511 SG  ? ? ? 1_555 B CYS 644 SG ? ? B CYS 761  B CYS 894  1_555 ? ? ? ? ? ? ? 2.017 ? ? 
disulf11 disulf ?    ? B CYS 525 SG  ? ? ? 1_555 B CYS 655 SG ? ? B CYS 775  B CYS 905  1_555 ? ? ? ? ? ? ? 2.030 ? ? 
disulf12 disulf ?    ? B CYS 540 SG  ? ? ? 1_555 B CYS 663 SG ? ? B CYS 790  B CYS 913  1_555 ? ? ? ? ? ? ? 2.026 ? ? 
disulf13 disulf ?    ? B CYS 566 SG  ? ? ? 1_555 B CYS 575 SG ? ? B CYS 816  B CYS 825  1_555 ? ? ? ? ? ? ? 2.034 ? ? 
disulf14 disulf ?    ? B CYS 583 SG  ? ? ? 1_555 B CYS 592 SG ? ? B CYS 833  B CYS 842  1_555 ? ? ? ? ? ? ? 2.033 ? ? 
disulf15 disulf ?    ? B CYS 623 SG  ? ? ? 1_555 B CYS 627 SG ? ? B CYS 873  B CYS 877  1_555 ? ? ? ? ? ? ? 2.032 ? ? 
disulf16 disulf ?    ? B CYS 729 SG  ? ? ? 1_555 B CYS 759 SG ? ? B CYS 979  B CYS 1009 1_555 ? ? ? ? ? ? ? 2.030 ? ? 
disulf17 disulf ?    ? B CYS 752 SG  ? ? ? 1_555 B CYS 804 SG ? ? B CYS 1002 B CYS 1054 1_555 ? ? ? ? ? ? ? 2.024 ? ? 
disulf18 disulf ?    ? B CYS 769 SG  ? ? ? 1_555 B CYS 774 SG ? ? B CYS 1019 B CYS 1024 1_555 ? ? ? ? ? ? ? 2.025 ? ? 
disulf19 disulf ?    ? B CYS 805 SG  ? ? ? 1_555 B CYS 810 SG ? ? B CYS 1055 B CYS 1060 1_555 ? ? ? ? ? ? ? 2.031 ? ? 
disulf20 disulf ?    ? C CYS 24  SG  ? ? ? 1_555 C CYS 98  SG ? ? H CYS 22   H CYS 92   1_555 ? ? ? ? ? ? ? 2.029 ? ? 
disulf21 disulf ?    ? D CYS 171 SG  ? ? ? 1_555 D CYS 241 SG ? ? L CYS 23   L CYS 88   1_555 ? ? ? ? ? ? ? 2.033 ? ? 
covale1  covale one  ? A ASN 125 ND2 ? ? ? 1_555 F NAG .   C1 ? ? A ASN 142  D NAG 1    1_555 ? ? ? ? ? ? ? 1.447 ? 
N-Glycosylation 
covale2  covale one  ? A ASN 340 ND2 ? ? ? 1_555 E NAG .   C1 ? ? A ASN 357  C NAG 1    1_555 ? ? ? ? ? ? ? 1.442 ? 
N-Glycosylation 
covale3  covale one  ? B ASN 687 ND2 ? ? ? 1_555 G NAG .   C1 ? ? B ASN 937  E NAG 1    1_555 ? ? ? ? ? ? ? 1.446 ? 
N-Glycosylation 
covale4  covale both ? E NAG .   O4  ? ? ? 1_555 E NAG .   C1 ? ? C NAG 1    C NAG 2    1_555 ? ? ? ? ? ? ? 1.442 ? ? 
covale5  covale both ? E NAG .   O4  ? ? ? 1_555 E BMA .   C1 ? ? C NAG 2    C BMA 3    1_555 ? ? ? ? ? ? ? 1.445 ? ? 
covale6  covale both ? E BMA .   O3  ? ? ? 1_555 E MAN .   C1 ? ? C BMA 3    C MAN 4    1_555 ? ? ? ? ? ? ? 1.443 ? ? 
covale7  covale both ? E BMA .   O6  ? ? ? 1_555 E MAN .   C1 ? ? C BMA 3    C MAN 6    1_555 ? ? ? ? ? ? ? 1.444 ? ? 
covale8  covale both ? E MAN .   O2  ? ? ? 1_555 E MAN .   C1 ? ? C MAN 4    C MAN 5    1_555 ? ? ? ? ? ? ? 1.448 ? ? 
covale9  covale both ? F NAG .   O4  ? ? ? 1_555 F NAG .   C1 ? ? D NAG 1    D NAG 2    1_555 ? ? ? ? ? ? ? 1.441 ? ? 
covale10 covale both ? G NAG .   O4  ? ? ? 1_555 G NAG .   C1 ? ? E NAG 1    E NAG 2    1_555 ? ? ? ? ? ? ? 1.448 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 ILE 251 A . ? ILE 268 A PRO 252 A ? PRO 269 A 1 0.34 
2 ALA 295 A . ? ALA 312 A PRO 296 A ? PRO 313 A 1 0.95 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4  ? 
AA2 ? 5  ? 
AA3 ? 5  ? 
AA4 ? 6  ? 
AA5 ? 17 ? 
AA6 ? 6  ? 
AA7 ? 4  ? 
AA8 ? 2  ? 
AA9 ? 4  ? 
AB1 ? 6  ? 
AB2 ? 4  ? 
AB3 ? 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  ? parallel      
AA1 2  3  ? anti-parallel 
AA1 3  4  ? anti-parallel 
AA2 1  4  ? anti-parallel 
AA2 1  5  ? anti-parallel 
AA2 2  4  ? anti-parallel 
AA2 3  4  ? anti-parallel 
AA3 1  2  ? anti-parallel 
AA3 2  3  ? parallel      
AA3 3  4  ? anti-parallel 
AA3 4  5  ? anti-parallel 
AA4 1  2  ? anti-parallel 
AA4 2  3  ? anti-parallel 
AA4 3  4  ? anti-parallel 
AA4 4  5  ? anti-parallel 
AA4 5  6  ? anti-parallel 
AA5 1  2  ? anti-parallel 
AA5 1  6  ? parallel      
AA5 2  3  ? anti-parallel 
AA5 4  5  ? parallel      
AA5 5  6  ? anti-parallel 
AA5 5  17 ? parallel      
AA5 6  8  ? anti-parallel 
AA5 6  12 ? anti-parallel 
AA5 6  16 ? anti-parallel 
AA5 7  8  ? anti-parallel 
AA5 8  9  ? anti-parallel 
AA5 8  10 ? anti-parallel 
AA5 10 11 ? anti-parallel 
AA5 11 14 ? anti-parallel 
AA5 12 13 ? anti-parallel 
AA5 15 16 ? anti-parallel 
AA6 1  4  ? anti-parallel 
AA6 2  3  ? anti-parallel 
AA6 3  4  ? anti-parallel 
AA6 3  5  ? anti-parallel 
AA6 5  6  ? anti-parallel 
AA7 1  2  ? anti-parallel 
AA7 2  3  ? anti-parallel 
AA7 3  4  ? anti-parallel 
AA8 1  2  ? anti-parallel 
AA9 1  2  ? anti-parallel 
AA9 2  3  ? anti-parallel 
AA9 3  4  ? anti-parallel 
AB1 1  2  ? parallel      
AB1 2  3  ? anti-parallel 
AB1 3  4  ? anti-parallel 
AB1 4  5  ? anti-parallel 
AB1 5  6  ? anti-parallel 
AB2 1  2  ? anti-parallel 
AB2 2  3  ? anti-parallel 
AB2 3  4  ? anti-parallel 
AB3 1  2  ? parallel      
AB3 2  3  ? anti-parallel 
AB3 3  4  ? anti-parallel 
AB3 4  5  ? anti-parallel 
AB3 5  6  ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  LEU A 10  ? CYS A 17  ? LEU A 27   CYS A 34   
AA1 2  GLN A 155 ? LYS A 163 ? GLN A 172  LYS A 180  
AA1 3  SER A 147 ? LEU A 152 ? SER A 164  LEU A 169  
AA1 4  LEU A 47  ? GLU A 48  ? LEU A 64   GLU A 65   
AA2 1  LEU A 27  ? GLU A 33  ? LEU A 44   GLU A 50   
AA2 2  VAL A 37  ? PRO A 38  ? VAL A 54   PRO A 55   
AA2 3  ILE A 117 ? CYS A 124 ? ILE A 134  CYS A 141  
AA2 4  THR A 128 ? PRO A 138 ? THR A 145  PRO A 155  
AA2 5  SER A 245 ? SER A 246 ? SER A 262  SER A 263  
AA3 1  PHE A 87  ? ARG A 97  ? PHE A 104  ARG A 114  
AA3 2  GLN A 62  ? VAL A 72  ? GLN A 79   VAL A 89   
AA3 3  TYR A 329 ? TRP A 331 ? TYR A 346  TRP A 348  
AA3 4  THR A 318 ? LEU A 321 ? THR A 335  LEU A 338  
AA3 5  THR A 348 ? PRO A 350 ? THR A 365  PRO A 367  
AA4 1  GLN A 170 ? ILE A 172 ? GLN A 187  ILE A 189  
AA4 2  ILE A 175 ? PRO A 179 ? ILE A 192  PRO A 196  
AA4 3  THR A 352 ? ILE A 363 ? THR A 369  ILE A 380  
AA4 4  ILE A 194 ? VAL A 205 ? ILE A 211  VAL A 222  
AA4 5  GLY A 236 ? ILE A 242 ? GLY A 253  ILE A 259  
AA4 6  LEU A 249 ? ILE A 251 ? LEU A 266  ILE A 268  
AA5 1  SER A 283 ? GLY A 293 ? SER A 300  GLY A 310  
AA5 2  VAL A 304 ? SER A 310 ? VAL A 321  SER A 327  
AA5 3  ILE A 335 ? MET A 337 ? ILE A 352  MET A 354  
AA5 4  VAL B 426 ? PRO B 428 ? VAL B 676  PRO B 678  
AA5 5  SER B 444 ? GLN B 452 ? SER B 694  GLN B 702  
AA5 6  LYS B 460 ? HIS B 494 ? LYS B 710  HIS B 744  
AA5 7  CYS B 511 ? TYR B 517 ? CYS B 761  TYR B 767  
AA5 8  THR B 538 ? LEU B 569 ? THR B 788  LEU B 819  
AA5 9  GLU B 572 ? VAL B 578 ? GLU B 822  VAL B 828  
AA5 10 THR B 605 ? PHE B 608 ? THR B 855  PHE B 858  
AA5 11 GLY B 616 ? PHE B 619 ? GLY B 866  PHE B 869  
AA5 12 MET B 636 ? SER B 637 ? MET B 886  SER B 887  
AA5 13 MET B 642 ? LYS B 643 ? MET B 892  LYS B 893  
AA5 14 GLN B 684 ? PHE B 686 ? GLN B 934  PHE B 936  
AA5 15 THR B 689 ? ILE B 693 ? THR B 939  ILE B 943  
AA5 16 SER B 697 ? ILE B 701 ? SER B 947  ILE B 951  
AA5 17 LYS B 835 ? ASP B 838 ? LYS B 1085 ASP B 1088 
AA6 1  THR B 420 ? ALA B 421 ? THR B 670  ALA B 671  
AA6 2  GLN B 730 ? GLY B 740 ? GLN B 980  GLY B 990  
AA6 3  PHE B 748 ? CYS B 769 ? PHE B 998  CYS B 1019 
AA6 4  MET B 773 ? GLY B 793 ? MET B 1023 GLY B 1043 
AA6 5  MET B 803 ? HIS B 806 ? MET B 1053 HIS B 1056 
AA6 6  LYS B 809 ? CYS B 810 ? LYS B 1059 CYS B 1060 
AA7 1  LEU B 433 ? PRO B 440 ? LEU B 683  PRO B 690  
AA7 2  ARG B 708 ? VAL B 715 ? ARG B 958  VAL B 965  
AA7 3  VAL B 589 ? VAL B 597 ? VAL B 839  VAL B 847  
AA7 4  LEU B 584 ? VAL B 585 ? LEU B 834  VAL B 835  
AA8 1  SER B 650 ? ALA B 656 ? SER B 900  ALA B 906  
AA8 2  THR B 660 ? ASP B 666 ? THR B 910  ASP B 916  
AA9 1  GLN C 5   ? SER C 9   ? GLN H 3    SER H 7    
AA9 2  SER C 19  ? SER C 27  ? SER H 17   SER H 25   
AA9 3  THR C 80  ? ASN C 86  A THR H 77   ASN H 82   
AA9 4  PHE C 70  ? THR C 71  ? PHE H 67   THR H 68   
AB1 1  VAL C 13  ? VAL C 14  ? VAL H 11   VAL H 12   
AB1 2  THR C 122 ? VAL C 126 ? THR H 107  VAL H 111  
AB1 3  ALA C 94  ? LEU C 102 ? ALA H 88   LEU H 96   
AB1 4  TYR C 34  ? GLN C 41  ? TYR H 32   GLN H 39   
AB1 5  GLU C 48  ? TRP C 54  ? GLU H 46   TRP H 52   
AB1 6  LYS C 59  ? TYR C 62  ? LYS H 56   TYR H 59   
AB2 1  MET D 152 ? GLN D 154 ? MET L 4    GLN L 6    
AB2 2  ALA D 167 ? SER D 173 ? ALA L 19   SER L 25   
AB2 3  ASP D 223 ? ILE D 228 ? ASP L 70   ILE L 75   
AB2 4  PHE D 215 ? SER D 220 ? PHE L 62   SER L 67   
AB3 1  SER D 158 ? PRO D 160 ? SER L 10   PRO L 12   
AB3 2  THR D 254 ? GLU D 257 ? THR L 101  GLU L 104  
AB3 3  GLY D 237 ? GLN D 243 ? GLY L 84   GLN L 90   
AB3 4  LEU D 186 ? GLN D 191 ? LEU L 33   GLN L 38   
AB3 5  PRO D 197 ? SER D 202 ? PRO L 44   SER L 49   
AB3 6  TYR D 206 ? ARG D 207 ? TYR L 53   ARG L 54   
# 
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 MET A 15  ? N MET A 32   O ASN A 160 ? O ASN A 177  
AA1 2  3  O GLN A 155 ? O GLN A 172  N LEU A 152 ? N LEU A 169  
AA1 3  4  O GLY A 151 ? O GLY A 168  N GLU A 48  ? N GLU A 65   
AA2 1  4  N GLY A 30  ? N GLY A 47   O LEU A 135 ? O LEU A 152  
AA2 1  5  N LEU A 27  ? N LEU A 44   O SER A 246 ? O SER A 263  
AA2 2  4  N VAL A 37  ? N VAL A 54   O CYS A 129 ? O CYS A 146  
AA2 3  4  N ILE A 117 ? N ILE A 134  O MET A 136 ? O MET A 153  
AA3 1  2  O VAL A 94  ? O VAL A 111  N PHE A 65  ? N PHE A 82   
AA3 2  3  N THR A 66  ? N THR A 83   O TYR A 329 ? O TYR A 346  
AA3 3  4  O VAL A 330 ? O VAL A 347  N GLY A 319 ? N GLY A 336  
AA3 4  5  N VAL A 320 ? N VAL A 337  O LEU A 349 ? O LEU A 366  
AA4 1  2  N ILE A 172 ? N ILE A 189  O ILE A 175 ? O ILE A 192  
AA4 2  3  N ASN A 178 ? N ASN A 195  O GLU A 362 ? O GLU A 379  
AA4 3  4  O LEU A 359 ? O LEU A 376  N VAL A 195 ? N VAL A 212  
AA4 4  5  N ILE A 204 ? N ILE A 221  O TYR A 237 ? O TYR A 254  
AA4 5  6  N TYR A 238 ? N TYR A 255  O ILE A 251 ? O ILE A 268  
AA5 1  2  N GLY A 293 ? N GLY A 310  O VAL A 304 ? O VAL A 321  
AA5 1  6  N SER A 283 ? N SER A 300  O THR B 491 ? O THR B 741  
AA5 2  3  N ILE A 307 ? N ILE A 324  O MET A 336 ? O MET A 353  
AA5 4  5  N ILE B 427 ? N ILE B 677  O GLN B 450 ? O GLN B 700  
AA5 5  6  N TYR B 447 ? N TYR B 697  O LEU B 465 ? O LEU B 715  
AA5 5  17 N SER B 444 ? N SER B 694  O ILE B 836 ? O ILE B 1086 
AA5 6  8  N GLU B 475 ? N GLU B 725  O VAL B 557 ? O VAL B 807  
AA5 6  12 N HIS B 481 ? N HIS B 731  O SER B 637 ? O SER B 887  
AA5 6  16 N ILE B 472 ? N ILE B 722  O TRP B 700 ? O TRP B 950  
AA5 7  8  N LYS B 515 ? N LYS B 765  O CYS B 540 ? O CYS B 790  
AA5 8  9  N ILE B 567 ? N ILE B 817  O THR B 574 ? O THR B 824  
AA5 8  10 N PHE B 554 ? N PHE B 804  O LEU B 606 ? O LEU B 856  
AA5 10 11 N LEU B 607 ? N LEU B 857  O LEU B 617 ? O LEU B 867  
AA5 11 14 N ILE B 618 ? N ILE B 868  O GLN B 684 ? O GLN B 934  
AA5 12 13 N MET B 636 ? N MET B 886  O LYS B 643 ? O LYS B 893  
AA5 15 16 N HIS B 692 ? N HIS B 942  O GLU B 699 ? O GLU B 949  
AA6 1  4  N THR B 420 ? N THR B 670  O CYS B 774 ? O CYS B 1024 
AA6 2  3  N GLN B 730 ? N GLN B 980  O THR B 757 ? O THR B 1007 
AA6 3  4  N VAL B 754 ? N VAL B 1004 O ASN B 787 ? O ASN B 1037 
AA6 3  5  N LYS B 767 ? N LYS B 1017 O CYS B 805 ? O CYS B 1055 
AA6 5  6  N HIS B 806 ? N HIS B 1056 O LYS B 809 ? O LYS B 1059 
AA7 1  2  N LEU B 433 ? N LEU B 683  O VAL B 715 ? O VAL B 965  
AA7 2  3  O ASN B 712 ? O ASN B 962  N CYS B 592 ? N CYS B 842  
AA7 3  4  O VAL B 591 ? O VAL B 841  N LEU B 584 ? N LEU B 834  
AA8 1  2  N LYS B 654 ? N LYS B 904  O VAL B 662 ? O VAL B 912  
AA9 1  2  N VAL C 7   ? N VAL H 5    O ALA C 25  ? O ALA H 23   
AA9 2  3  N CYS C 24  ? N CYS H 22   O LEU C 81  ? O LEU H 78   
AA9 3  4  O GLN C 84  ? O GLN H 81   N THR C 71  ? N THR H 68   
AB1 1  2  N VAL C 14  ? N VAL H 12   O THR C 125 ? O THR H 110  
AB1 2  3  O THR C 122 ? O THR H 107  N TYR C 96  ? N TYR H 90   
AB1 3  4  O TYR C 97  ? O TYR H 91   N VAL C 39  ? N VAL H 37   
AB1 4  5  N TRP C 38  ? N TRP H 36   O VAL C 50  ? O VAL H 48   
AB1 5  6  N VAL C 52  ? N VAL H 50   O ASP C 61  ? O ASP H 58   
AB2 1  2  N THR D 153 ? N THR L 5    O ARG D 172 ? O ARG L 24   
AB2 2  3  N ILE D 169 ? N ILE L 21   O LEU D 226 ? O LEU L 73   
AB2 3  4  O LYS D 227 ? O LYS L 74   N SER D 216 ? N SER L 63   
AB3 1  2  N LEU D 159 ? N LEU L 11   O LYS D 255 ? O LYS L 102  
AB3 2  3  O THR D 254 ? O THR L 101  N TYR D 239 ? N TYR L 86   
AB3 3  4  O TYR D 240 ? O TYR L 87   N TYR D 189 ? N TYR L 36   
AB3 4  5  N TRP D 188 ? N TRP L 35   O ILE D 201 ? O ILE L 48   
AB3 5  6  N SER D 202 ? N SER L 49   O TYR D 206 ? O TYR L 53   
# 
_atom_sites.entry_id                    7QQB 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.fract_transf_matrix[1][1]   0.011922 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.009149 
_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]   0.006687 
_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   . ASN A 1 9   ? 13.092  -9.732  16.651  1.00 106.94 ?  26   ASN A N   1 
ATOM   2    C CA  . ASN A 1 9   ? 13.352  -8.841  17.775  1.00 120.84 ?  26   ASN A CA  1 
ATOM   3    C C   . ASN A 1 9   ? 13.550  -9.644  19.058  1.00 118.10 ?  26   ASN A C   1 
ATOM   4    O O   . ASN A 1 9   ? 12.972  -10.720 19.220  1.00 101.61 ?  26   ASN A O   1 
ATOM   5    C CB  . ASN A 1 9   ? 12.206  -7.840  17.943  1.00 117.04 ?  26   ASN A CB  1 
ATOM   6    C CG  . ASN A 1 9   ? 12.539  -6.731  18.920  1.00 118.51 ?  26   ASN A CG  1 
ATOM   7    O OD1 . ASN A 1 9   ? 13.706  -6.495  19.235  1.00 118.71 ?  26   ASN A OD1 1 
ATOM   8    N ND2 . ASN A 1 9   ? 11.514  -6.038  19.402  1.00 112.92 ?  26   ASN A ND2 1 
ATOM   9    N N   . LEU A 1 10  ? 14.370  -9.121  19.967  1.00 120.94 ?  27   LEU A N   1 
ATOM   10   C CA  . LEU A 1 10  ? 14.672  -9.793  21.221  1.00 112.49 ?  27   LEU A CA  1 
ATOM   11   C C   . LEU A 1 10  ? 14.464  -8.834  22.385  1.00 112.34 ?  27   LEU A C   1 
ATOM   12   O O   . LEU A 1 10  ? 14.484  -7.610  22.224  1.00 105.85 ?  27   LEU A O   1 
ATOM   13   C CB  . LEU A 1 10  ? 16.107  -10.345 21.242  1.00 112.79 ?  27   LEU A CB  1 
ATOM   14   C CG  . LEU A 1 10  ? 17.262  -9.397  21.580  1.00 115.40 ?  27   LEU A CG  1 
ATOM   15   C CD1 . LEU A 1 10  ? 18.547  -10.189 21.765  1.00 104.32 ?  27   LEU A CD1 1 
ATOM   16   C CD2 . LEU A 1 10  ? 17.445  -8.332  20.510  1.00 114.27 ?  27   LEU A CD2 1 
ATOM   17   N N   . ASN A 1 11  ? 14.262  -9.412  23.568  1.00 96.40  ?  28   ASN A N   1 
ATOM   18   C CA  . ASN A 1 11  ? 13.984  -8.652  24.779  1.00 93.68  ?  28   ASN A CA  1 
ATOM   19   C C   . ASN A 1 11  ? 14.798  -9.236  25.923  1.00 93.99  ?  28   ASN A C   1 
ATOM   20   O O   . ASN A 1 11  ? 14.822  -10.456 26.106  1.00 96.75  ?  28   ASN A O   1 
ATOM   21   C CB  . ASN A 1 11  ? 12.490  -8.691  25.120  1.00 97.09  ?  28   ASN A CB  1 
ATOM   22   C CG  . ASN A 1 11  ? 11.623  -8.956  23.903  1.00 99.63  ?  28   ASN A CG  1 
ATOM   23   O OD1 . ASN A 1 11  ? 11.511  -10.093 23.444  1.00 85.91  ?  28   ASN A OD1 1 
ATOM   24   N ND2 . ASN A 1 11  ? 11.005  -7.906  23.373  1.00 104.56 ?  28   ASN A ND2 1 
ATOM   25   N N   . GLU A 1 12  ? 15.453  -8.372  26.694  1.00 87.57  ?  29   GLU A N   1 
ATOM   26   C CA  . GLU A 1 12  ? 16.330  -8.814  27.772  1.00 85.82  ?  29   GLU A CA  1 
ATOM   27   C C   . GLU A 1 12  ? 15.537  -9.000  29.060  1.00 79.06  ?  29   GLU A C   1 
ATOM   28   O O   . GLU A 1 12  ? 15.019  -8.029  29.622  1.00 83.61  ?  29   GLU A O   1 
ATOM   29   C CB  . GLU A 1 12  ? 17.461  -7.815  28.007  1.00 92.61  ?  29   GLU A CB  1 
ATOM   30   C CG  . GLU A 1 12  ? 18.421  -8.248  29.108  1.00 98.68  ?  29   GLU A CG  1 
ATOM   31   C CD  . GLU A 1 12  ? 19.118  -7.081  29.774  1.00 110.77 ?  29   GLU A CD  1 
ATOM   32   O OE1 . GLU A 1 12  ? 18.588  -5.953  29.697  1.00 114.51 ?  29   GLU A OE1 1 
ATOM   33   O OE2 . GLU A 1 12  ? 20.194  -7.292  30.375  1.00 106.49 -1 29   GLU A OE2 1 
ATOM   34   N N   . LEU A 1 13  ? 15.452  -10.242 29.527  1.00 85.69  ?  30   LEU A N   1 
ATOM   35   C CA  . LEU A 1 13  ? 14.888  -10.549 30.838  1.00 73.15  ?  30   LEU A CA  1 
ATOM   36   C C   . LEU A 1 13  ? 16.031  -10.601 31.845  1.00 69.99  ?  30   LEU A C   1 
ATOM   37   O O   . LEU A 1 13  ? 16.892  -11.484 31.773  1.00 79.49  ?  30   LEU A O   1 
ATOM   38   C CB  . LEU A 1 13  ? 14.118  -11.866 30.804  1.00 62.37  ?  30   LEU A CB  1 
ATOM   39   C CG  . LEU A 1 13  ? 13.755  -12.495 32.150  1.00 61.99  ?  30   LEU A CG  1 
ATOM   40   C CD1 . LEU A 1 13  ? 12.928  -11.539 32.995  1.00 78.41  ?  30   LEU A CD1 1 
ATOM   41   C CD2 . LEU A 1 13  ? 13.017  -13.811 31.946  1.00 71.66  ?  30   LEU A CD2 1 
ATOM   42   N N   . LYS A 1 14  ? 16.041  -9.656  32.780  1.00 71.32  ?  31   LYS A N   1 
ATOM   43   C CA  . LYS A 1 14  ? 17.122  -9.523  33.746  1.00 72.34  ?  31   LYS A CA  1 
ATOM   44   C C   . LYS A 1 14  ? 16.758  -10.237 35.041  1.00 71.68  ?  31   LYS A C   1 
ATOM   45   O O   . LYS A 1 14  ? 15.706  -9.970  35.631  1.00 76.45  ?  31   LYS A O   1 
ATOM   46   C CB  . LYS A 1 14  ? 17.427  -8.050  34.024  1.00 64.75  ?  31   LYS A CB  1 
ATOM   47   C CG  . LYS A 1 14  ? 18.850  -7.806  34.487  1.00 86.22  ?  31   LYS A CG  1 
ATOM   48   C CD  . LYS A 1 14  ? 19.099  -6.345  34.808  1.00 88.95  ?  31   LYS A CD  1 
ATOM   49   C CE  . LYS A 1 14  ? 20.568  -6.108  35.113  1.00 96.46  ?  31   LYS A CE  1 
ATOM   50   N NZ  . LYS A 1 14  ? 20.767  -5.035  36.124  1.00 93.73  1  31   LYS A NZ  1 
ATOM   51   N N   . MET A 1 15  ? 17.632  -11.140 35.475  1.00 57.90  ?  32   MET A N   1 
ATOM   52   C CA  . MET A 1 15  ? 17.470  -11.869 36.730  1.00 71.62  ?  32   MET A CA  1 
ATOM   53   C C   . MET A 1 15  ? 18.355  -11.193 37.772  1.00 61.20  ?  32   MET A C   1 
ATOM   54   O O   . MET A 1 15  ? 19.572  -11.391 37.794  1.00 66.22  ?  32   MET A O   1 
ATOM   55   C CB  . MET A 1 15  ? 17.828  -13.341 36.550  1.00 63.20  ?  32   MET A CB  1 
ATOM   56   C CG  . MET A 1 15  ? 16.990  -14.057 35.501  1.00 61.06  ?  32   MET A CG  1 
ATOM   57   S SD  . MET A 1 15  ? 15.290  -14.348 36.030  1.00 68.22  ?  32   MET A SD  1 
ATOM   58   C CE  . MET A 1 15  ? 15.508  -15.754 37.119  1.00 69.30  ?  32   MET A CE  1 
ATOM   59   N N   . GLU A 1 16  ? 17.738  -10.389 38.633  1.00 59.30  ?  33   GLU A N   1 
ATOM   60   C CA  . GLU A 1 16  ? 18.464  -9.618  39.640  1.00 65.94  ?  33   GLU A CA  1 
ATOM   61   C C   . GLU A 1 16  ? 18.752  -10.523 40.831  1.00 65.89  ?  33   GLU A C   1 
ATOM   62   O O   . GLU A 1 16  ? 17.880  -10.774 41.665  1.00 63.94  ?  33   GLU A O   1 
ATOM   63   C CB  . GLU A 1 16  ? 17.661  -8.388  40.042  1.00 73.24  ?  33   GLU A CB  1 
ATOM   64   C CG  . GLU A 1 16  ? 17.229  -7.539  38.853  1.00 77.75  ?  33   GLU A CG  1 
ATOM   65   C CD  . GLU A 1 16  ? 16.486  -6.284  39.263  1.00 82.54  ?  33   GLU A CD  1 
ATOM   66   O OE1 . GLU A 1 16  ? 16.450  -5.983  40.474  1.00 86.97  ?  33   GLU A OE1 1 
ATOM   67   O OE2 . GLU A 1 16  ? 15.938  -5.599  38.373  1.00 93.27  -1 33   GLU A OE2 1 
ATOM   68   N N   . CYS A 1 17  ? 19.998  -11.017 40.912  1.00 58.10  ?  34   CYS A N   1 
ATOM   69   C CA  . CYS A 1 17  ? 20.549  -11.982 41.849  1.00 67.07  ?  34   CYS A CA  1 
ATOM   70   C C   . CYS A 1 17  ? 21.129  -11.288 43.077  1.00 66.87  ?  34   CYS A C   1 
ATOM   71   O O   . CYS A 1 17  ? 21.630  -10.163 42.985  1.00 70.28  ?  34   CYS A O   1 
ATOM   72   C CB  . CYS A 1 17  ? 21.642  -12.805 41.174  1.00 65.71  ?  34   CYS A CB  1 
ATOM   73   S SG  . CYS A 1 17  ? 21.084  -13.748 39.739  1.00 81.92  ?  34   CYS A SG  1 
ATOM   74   N N   . PRO A 1 18  ? 21.074  -11.940 44.235  1.00 70.57  ?  35   PRO A N   1 
ATOM   75   C CA  . PRO A 1 18  ? 21.775  -11.413 45.408  1.00 67.73  ?  35   PRO A CA  1 
ATOM   76   C C   . PRO A 1 18  ? 23.276  -11.617 45.278  1.00 74.80  ?  35   PRO A C   1 
ATOM   77   O O   . PRO A 1 18  ? 23.754  -12.498 44.561  1.00 80.54  ?  35   PRO A O   1 
ATOM   78   C CB  . PRO A 1 18  ? 21.201  -12.237 46.564  1.00 72.13  ?  35   PRO A CB  1 
ATOM   79   C CG  . PRO A 1 18  ? 20.806  -13.528 45.929  1.00 62.58  ?  35   PRO A CG  1 
ATOM   80   C CD  . PRO A 1 18  ? 20.332  -13.175 44.542  1.00 72.15  ?  35   PRO A CD  1 
ATOM   81   N N   . HIS A 1 19  ? 24.028  -10.776 45.991  1.00 75.40  ?  36   HIS A N   1 
ATOM   82   C CA  . HIS A 1 19  ? 25.482  -10.896 45.953  1.00 73.26  ?  36   HIS A CA  1 
ATOM   83   C C   . HIS A 1 19  ? 25.966  -12.140 46.689  1.00 76.47  ?  36   HIS A C   1 
ATOM   84   O O   . HIS A 1 19  ? 26.999  -12.710 46.323  1.00 76.26  ?  36   HIS A O   1 
ATOM   85   C CB  . HIS A 1 19  ? 26.132  -9.640  46.533  1.00 78.30  ?  36   HIS A CB  1 
ATOM   86   C CG  . HIS A 1 19  ? 26.361  -8.558  45.522  1.00 89.23  ?  36   HIS A CG  1 
ATOM   87   N ND1 . HIS A 1 19  ? 27.511  -8.479  44.766  1.00 85.93  ?  36   HIS A ND1 1 
ATOM   88   C CD2 . HIS A 1 19  ? 25.587  -7.515  45.139  1.00 83.09  ?  36   HIS A CD2 1 
ATOM   89   C CE1 . HIS A 1 19  ? 27.436  -7.434  43.962  1.00 81.83  ?  36   HIS A CE1 1 
ATOM   90   N NE2 . HIS A 1 19  ? 26.279  -6.831  44.168  1.00 77.56  ?  36   HIS A NE2 1 
ATOM   91   N N   . THR A 1 20  ? 25.238  -12.581 47.713  1.00 73.74  ?  37   THR A N   1 
ATOM   92   C CA  . THR A 1 20  ? 25.604  -13.777 48.466  1.00 73.17  ?  37   THR A CA  1 
ATOM   93   C C   . THR A 1 20  ? 24.891  -14.965 47.836  1.00 80.64  ?  37   THR A C   1 
ATOM   94   O O   . THR A 1 20  ? 23.692  -15.169 48.042  1.00 79.98  ?  37   THR A O   1 
ATOM   95   C CB  . THR A 1 20  ? 25.249  -13.625 49.941  1.00 73.24  ?  37   THR A CB  1 
ATOM   96   O OG1 . THR A 1 20  ? 23.825  -13.677 50.102  1.00 91.42  ?  37   THR A OG1 1 
ATOM   97   C CG2 . THR A 1 20  ? 25.761  -12.294 50.477  1.00 73.58  ?  37   THR A CG2 1 
ATOM   98   N N   . ILE A 1 21  ? 25.623  -15.745 47.047  1.00 73.96  ?  38   ILE A N   1 
ATOM   99   C CA  . ILE A 1 21  ? 25.045  -16.924 46.409  1.00 76.20  ?  38   ILE A CA  1 
ATOM   100  C C   . ILE A 1 21  ? 25.314  -18.177 47.227  1.00 80.78  ?  38   ILE A C   1 
ATOM   101  O O   . ILE A 1 21  ? 24.393  -18.938 47.538  1.00 77.92  ?  38   ILE A O   1 
ATOM   102  C CB  . ILE A 1 21  ? 25.589  -17.070 44.972  1.00 86.78  ?  38   ILE A CB  1 
ATOM   103  C CG1 . ILE A 1 21  ? 25.381  -15.777 44.181  1.00 75.39  ?  38   ILE A CG1 1 
ATOM   104  C CG2 . ILE A 1 21  ? 24.928  -18.253 44.277  1.00 82.71  ?  38   ILE A CG2 1 
ATOM   105  C CD1 . ILE A 1 21  ? 23.970  -15.581 43.682  1.00 75.14  ?  38   ILE A CD1 1 
ATOM   106  N N   . GLY A 1 22  ? 26.583  -18.402 47.577  1.00 82.87  ?  39   GLY A N   1 
ATOM   107  C CA  . GLY A 1 22  ? 26.939  -19.561 48.375  1.00 70.56  ?  39   GLY A CA  1 
ATOM   108  C C   . GLY A 1 22  ? 26.274  -19.580 49.736  1.00 75.27  ?  39   GLY A C   1 
ATOM   109  O O   . GLY A 1 22  ? 25.919  -20.649 50.238  1.00 70.02  ?  39   GLY A O   1 
ATOM   110  N N   . LEU A 1 23  ? 26.099  -18.410 50.351  1.00 76.73  ?  40   LEU A N   1 
ATOM   111  C CA  . LEU A 1 23  ? 25.381  -18.280 51.610  1.00 73.00  ?  40   LEU A CA  1 
ATOM   112  C C   . LEU A 1 23  ? 23.966  -17.753 51.411  1.00 73.44  ?  40   LEU A C   1 
ATOM   113  O O   . LEU A 1 23  ? 23.333  -17.311 52.376  1.00 81.88  ?  40   LEU A O   1 
ATOM   114  C CB  . LEU A 1 23  ? 26.154  -17.371 52.567  1.00 61.56  ?  40   LEU A CB  1 
ATOM   115  C CG  . LEU A 1 23  ? 27.557  -17.858 52.928  1.00 67.41  ?  40   LEU A CG  1 
ATOM   116  C CD1 . LEU A 1 23  ? 28.232  -16.907 53.901  1.00 63.91  ?  40   LEU A CD1 1 
ATOM   117  C CD2 . LEU A 1 23  ? 27.492  -19.262 53.503  1.00 61.50  ?  40   LEU A CD2 1 
ATOM   118  N N   . GLY A 1 24  ? 23.459  -17.791 50.177  1.00 69.99  ?  41   GLY A N   1 
ATOM   119  C CA  . GLY A 1 24  ? 22.120  -17.328 49.902  1.00 72.87  ?  41   GLY A CA  1 
ATOM   120  C C   . GLY A 1 24  ? 21.070  -18.406 50.096  1.00 68.59  ?  41   GLY A C   1 
ATOM   121  O O   . GLY A 1 24  ? 21.369  -19.596 50.165  1.00 68.85  ?  41   GLY A O   1 
ATOM   122  N N   . GLN A 1 25  ? 19.817  -17.965 50.179  1.00 60.90  ?  42   GLN A N   1 
ATOM   123  C CA  . GLN A 1 25  ? 18.694  -18.857 50.416  1.00 65.12  ?  42   GLN A CA  1 
ATOM   124  C C   . GLN A 1 25  ? 17.494  -18.385 49.610  1.00 55.20  ?  42   GLN A C   1 
ATOM   125  O O   . GLN A 1 25  ? 17.339  -17.191 49.338  1.00 72.81  ?  42   GLN A O   1 
ATOM   126  C CB  . GLN A 1 25  ? 18.345  -18.924 51.908  1.00 62.61  ?  42   GLN A CB  1 
ATOM   127  C CG  . GLN A 1 25  ? 18.380  -17.576 52.607  1.00 65.19  ?  42   GLN A CG  1 
ATOM   128  C CD  . GLN A 1 25  ? 18.501  -17.703 54.114  1.00 80.71  ?  42   GLN A CD  1 
ATOM   129  O OE1 . GLN A 1 25  ? 18.133  -18.724 54.697  1.00 73.94  ?  42   GLN A OE1 1 
ATOM   130  N NE2 . GLN A 1 25  ? 19.029  -16.665 54.753  1.00 73.59  ?  42   GLN A NE2 1 
ATOM   131  N N   . GLY A 1 26  ? 16.650  -19.338 49.224  1.00 53.45  ?  43   GLY A N   1 
ATOM   132  C CA  . GLY A 1 26  ? 15.452  -19.025 48.472  1.00 64.50  ?  43   GLY A CA  1 
ATOM   133  C C   . GLY A 1 26  ? 15.618  -19.171 46.974  1.00 57.62  ?  43   GLY A C   1 
ATOM   134  O O   . GLY A 1 26  ? 16.400  -20.003 46.505  1.00 57.68  ?  43   GLY A O   1 
ATOM   135  N N   . LEU A 1 27  ? 14.886  -18.361 46.214  1.00 64.28  ?  44   LEU A N   1 
ATOM   136  C CA  . LEU A 1 27  ? 14.886  -18.428 44.762  1.00 57.47  ?  44   LEU A CA  1 
ATOM   137  C C   . LEU A 1 27  ? 15.187  -17.053 44.183  1.00 58.92  ?  44   LEU A C   1 
ATOM   138  O O   . LEU A 1 27  ? 15.258  -16.050 44.897  1.00 62.74  ?  44   LEU A O   1 
ATOM   139  C CB  . LEU A 1 27  ? 13.540  -18.938 44.227  1.00 53.24  ?  44   LEU A CB  1 
ATOM   140  C CG  . LEU A 1 27  ? 13.061  -20.308 44.708  1.00 61.28  ?  44   LEU A CG  1 
ATOM   141  C CD1 . LEU A 1 27  ? 11.689  -20.622 44.133  1.00 51.52  ?  44   LEU A CD1 1 
ATOM   142  C CD2 . LEU A 1 27  ? 14.062  -21.388 44.332  1.00 55.68  ?  44   LEU A CD2 1 
ATOM   143  N N   . VAL A 1 28  ? 15.374  -17.025 42.867  1.00 57.90  ?  45   VAL A N   1 
ATOM   144  C CA  . VAL A 1 28  ? 15.499  -15.797 42.094  1.00 60.63  ?  45   VAL A CA  1 
ATOM   145  C C   . VAL A 1 28  ? 14.438  -15.827 41.003  1.00 52.62  ?  45   VAL A C   1 
ATOM   146  O O   . VAL A 1 28  ? 14.235  -16.857 40.350  1.00 62.37  ?  45   VAL A O   1 
ATOM   147  C CB  . VAL A 1 28  ? 16.913  -15.628 41.495  1.00 69.21  ?  45   VAL A CB  1 
ATOM   148  C CG1 . VAL A 1 28  ? 17.319  -16.861 40.695  1.00 57.36  ?  45   VAL A CG1 1 
ATOM   149  C CG2 . VAL A 1 28  ? 16.986  -14.374 40.633  1.00 54.26  ?  45   VAL A CG2 1 
ATOM   150  N N   . ILE A 1 29  ? 13.750  -14.699 40.818  1.00 61.67  ?  46   ILE A N   1 
ATOM   151  C CA  . ILE A 1 29  ? 12.612  -14.620 39.912  1.00 57.72  ?  46   ILE A CA  1 
ATOM   152  C C   . ILE A 1 29  ? 12.725  -13.367 39.053  1.00 58.70  ?  46   ILE A C   1 
ATOM   153  O O   . ILE A 1 29  ? 13.246  -12.334 39.484  1.00 59.94  ?  46   ILE A O   1 
ATOM   154  C CB  . ILE A 1 29  ? 11.270  -14.639 40.683  1.00 54.30  ?  46   ILE A CB  1 
ATOM   155  C CG1 . ILE A 1 29  ? 10.087  -14.737 39.715  1.00 53.57  ?  46   ILE A CG1 1 
ATOM   156  C CG2 . ILE A 1 29  ? 11.143  -13.415 41.580  1.00 51.28  ?  46   ILE A CG2 1 
ATOM   157  C CD1 . ILE A 1 29  ? 8.735   -14.732 40.391  1.00 65.74  ?  46   ILE A CD1 1 
ATOM   158  N N   . GLY A 1 30  ? 12.242  -13.478 37.818  1.00 61.07  ?  47   GLY A N   1 
ATOM   159  C CA  . GLY A 1 30  ? 12.151  -12.344 36.919  1.00 53.13  ?  47   GLY A CA  1 
ATOM   160  C C   . GLY A 1 30  ? 10.976  -12.526 35.983  1.00 62.80  ?  47   GLY A C   1 
ATOM   161  O O   . GLY A 1 30  ? 10.457  -13.635 35.809  1.00 58.19  ?  47   GLY A O   1 
ATOM   162  N N   . SER A 1 31  ? 10.551  -11.415 35.386  1.00 54.58  ?  48   SER A N   1 
ATOM   163  C CA  . SER A 1 31  ? 9.427   -11.437 34.462  1.00 53.14  ?  48   SER A CA  1 
ATOM   164  C C   . SER A 1 31  ? 9.636   -10.371 33.399  1.00 57.45  ?  48   SER A C   1 
ATOM   165  O O   . SER A 1 31  ? 10.352  -9.389  33.607  1.00 62.54  ?  48   SER A O   1 
ATOM   166  C CB  . SER A 1 31  ? 8.092   -11.218 35.185  1.00 52.22  ?  48   SER A CB  1 
ATOM   167  O OG  . SER A 1 31  ? 8.054   -9.953  35.820  1.00 57.39  ?  48   SER A OG  1 
ATOM   168  N N   . ILE A 1 32  ? 9.004   -10.581 32.249  1.00 60.21  ?  49   ILE A N   1 
ATOM   169  C CA  . ILE A 1 32  ? 9.144   -9.644  31.137  1.00 58.38  ?  49   ILE A CA  1 
ATOM   170  C C   . ILE A 1 32  ? 7.875   -9.664  30.294  1.00 69.01  ?  49   ILE A C   1 
ATOM   171  O O   . ILE A 1 32  ? 7.251   -10.711 30.105  1.00 64.10  ?  49   ILE A O   1 
ATOM   172  C CB  . ILE A 1 32  ? 10.396  -9.962  30.286  1.00 61.72  ?  49   ILE A CB  1 
ATOM   173  C CG1 . ILE A 1 32  ? 10.605  -8.882  29.222  1.00 65.47  ?  49   ILE A CG1 1 
ATOM   174  C CG2 . ILE A 1 32  ? 10.292  -11.348 29.658  1.00 58.51  ?  49   ILE A CG2 1 
ATOM   175  C CD1 . ILE A 1 32  ? 12.026  -8.785  28.726  1.00 78.50  ?  49   ILE A CD1 1 
ATOM   176  N N   . GLU A 1 33  ? 7.498   -8.491  29.791  1.00 65.19  ?  50   GLU A N   1 
ATOM   177  C CA  . GLU A 1 33  ? 6.359   -8.354  28.898  1.00 65.19  ?  50   GLU A CA  1 
ATOM   178  C C   . GLU A 1 33  ? 6.811   -8.469  27.448  1.00 64.59  ?  50   GLU A C   1 
ATOM   179  O O   . GLU A 1 33  ? 7.817   -7.874  27.051  1.00 60.39  ?  50   GLU A O   1 
ATOM   180  C CB  . GLU A 1 33  ? 5.664   -7.010  29.116  1.00 67.39  ?  50   GLU A CB  1 
ATOM   181  C CG  . GLU A 1 33  ? 5.474   -6.631  30.581  1.00 80.66  ?  50   GLU A CG  1 
ATOM   182  C CD  . GLU A 1 33  ? 4.374   -7.427  31.263  1.00 89.62  ?  50   GLU A CD  1 
ATOM   183  O OE1 . GLU A 1 33  ? 3.574   -8.076  30.555  1.00 86.73  ?  50   GLU A OE1 1 
ATOM   184  O OE2 . GLU A 1 33  ? 4.307   -7.395  32.510  1.00 77.59  -1 50   GLU A OE2 1 
ATOM   185  N N   . LEU A 1 34  ? 6.065   -9.233  26.664  1.00 67.16  ?  51   LEU A N   1 
ATOM   186  C CA  . LEU A 1 34  ? 6.375   -9.470  25.264  1.00 72.98  ?  51   LEU A CA  1 
ATOM   187  C C   . LEU A 1 34  ? 5.416   -8.708  24.355  1.00 70.67  ?  51   LEU A C   1 
ATOM   188  O O   . LEU A 1 34  ? 4.324   -8.314  24.779  1.00 67.63  ?  51   LEU A O   1 
ATOM   189  C CB  . LEU A 1 34  ? 6.312   -10.971 24.944  1.00 73.45  ?  51   LEU A CB  1 
ATOM   190  C CG  . LEU A 1 34  ? 7.517   -11.785 25.420  1.00 71.20  ?  51   LEU A CG  1 
ATOM   191  C CD1 . LEU A 1 34  ? 7.425   -13.219 24.936  1.00 66.25  ?  51   LEU A CD1 1 
ATOM   192  C CD2 . LEU A 1 34  ? 8.810   -11.141 24.947  1.00 69.25  ?  51   LEU A CD2 1 
ATOM   193  N N   . PRO A 1 35  ? 5.801   -8.473  23.099  1.00 68.20  ?  52   PRO A N   1 
ATOM   194  C CA  . PRO A 1 35  ? 4.908   -7.775  22.174  1.00 66.17  ?  52   PRO A CA  1 
ATOM   195  C C   . PRO A 1 35  ? 3.619   -8.544  21.978  1.00 74.99  ?  52   PRO A C   1 
ATOM   196  O O   . PRO A 1 35  ? 3.579   -9.777  22.148  1.00 79.61  ?  52   PRO A O   1 
ATOM   197  C CB  . PRO A 1 35  ? 5.728   -7.714  20.877  1.00 76.23  ?  52   PRO A CB  1 
ATOM   198  C CG  . PRO A 1 35  ? 7.142   -7.765  21.336  1.00 76.73  ?  52   PRO A CG  1 
ATOM   199  C CD  . PRO A 1 35  ? 7.135   -8.692  22.513  1.00 72.43  ?  52   PRO A CD  1 
ATOM   200  N N   . PRO A 1 36  ? 2.531   -7.859  21.620  1.00 74.25  ?  53   PRO A N   1 
ATOM   201  C CA  . PRO A 1 36  ? 1.245   -8.554  21.464  1.00 71.25  ?  53   PRO A CA  1 
ATOM   202  C C   . PRO A 1 36  ? 1.220   -9.431  20.221  1.00 76.70  ?  53   PRO A C   1 
ATOM   203  O O   . PRO A 1 36  ? 1.712   -9.050  19.157  1.00 85.02  ?  53   PRO A O   1 
ATOM   204  C CB  . PRO A 1 36  ? 0.234   -7.406  21.353  1.00 74.43  ?  53   PRO A CB  1 
ATOM   205  C CG  . PRO A 1 36  ? 1.031   -6.272  20.805  1.00 82.40  ?  53   PRO A CG  1 
ATOM   206  C CD  . PRO A 1 36  ? 2.412   -6.409  21.375  1.00 76.52  ?  53   PRO A CD  1 
ATOM   207  N N   . VAL A 1 37  ? 0.632   -10.615 20.369  1.00 73.41  ?  54   VAL A N   1 
ATOM   208  C CA  . VAL A 1 37  ? 0.478   -11.559 19.267  1.00 81.01  ?  54   VAL A CA  1 
ATOM   209  C C   . VAL A 1 37  ? -1.011  -11.709 18.976  1.00 74.78  ?  54   VAL A C   1 
ATOM   210  O O   . VAL A 1 37  ? -1.836  -11.596 19.895  1.00 64.45  ?  54   VAL A O   1 
ATOM   211  C CB  . VAL A 1 37  ? 1.141   -12.911 19.591  1.00 76.92  ?  54   VAL A CB  1 
ATOM   212  C CG1 . VAL A 1 37  ? 2.440   -12.694 20.360  1.00 67.37  ?  54   VAL A CG1 1 
ATOM   213  C CG2 . VAL A 1 37  ? 0.199   -13.822 20.370  1.00 71.90  ?  54   VAL A CG2 1 
ATOM   214  N N   . PRO A 1 38  ? -1.410  -11.932 17.724  1.00 85.16  ?  55   PRO A N   1 
ATOM   215  C CA  . PRO A 1 38  ? -2.840  -12.072 17.427  1.00 72.92  ?  55   PRO A CA  1 
ATOM   216  C C   . PRO A 1 38  ? -3.434  -13.304 18.096  1.00 79.72  ?  55   PRO A C   1 
ATOM   217  O O   . PRO A 1 38  ? -2.731  -14.238 18.489  1.00 77.49  ?  55   PRO A O   1 
ATOM   218  C CB  . PRO A 1 38  ? -2.882  -12.185 15.898  1.00 75.11  ?  55   PRO A CB  1 
ATOM   219  C CG  . PRO A 1 38  ? -1.510  -12.607 15.504  1.00 92.34  ?  55   PRO A CG  1 
ATOM   220  C CD  . PRO A 1 38  ? -0.582  -11.998 16.509  1.00 84.63  ?  55   PRO A CD  1 
ATOM   221  N N   . LEU A 1 39  ? -4.764  -13.290 18.218  1.00 81.68  ?  56   LEU A N   1 
ATOM   222  C CA  . LEU A 1 39  ? -5.458  -14.310 18.998  1.00 83.81  ?  56   LEU A CA  1 
ATOM   223  C C   . LEU A 1 39  ? -5.338  -15.696 18.375  1.00 83.81  ?  56   LEU A C   1 
ATOM   224  O O   . LEU A 1 39  ? -5.407  -16.700 19.091  1.00 80.09  ?  56   LEU A O   1 
ATOM   225  C CB  . LEU A 1 39  ? -6.930  -13.928 19.155  1.00 66.96  ?  56   LEU A CB  1 
ATOM   226  C CG  . LEU A 1 39  ? -7.478  -13.902 20.582  1.00 69.20  ?  56   LEU A CG  1 
ATOM   227  C CD1 . LEU A 1 39  ? -6.622  -13.007 21.459  1.00 68.89  ?  56   LEU A CD1 1 
ATOM   228  C CD2 . LEU A 1 39  ? -8.924  -13.434 20.589  1.00 78.76  ?  56   LEU A CD2 1 
ATOM   229  N N   . ILE A 1 40  ? -5.159  -15.774 17.054  1.00 82.83  ?  57   ILE A N   1 
ATOM   230  C CA  . ILE A 1 40  ? -5.127  -17.076 16.394  1.00 86.45  ?  57   ILE A CA  1 
ATOM   231  C C   . ILE A 1 40  ? -3.870  -17.849 16.772  1.00 89.89  ?  57   ILE A C   1 
ATOM   232  O O   . ILE A 1 40  ? -3.891  -19.084 16.847  1.00 101.58 ?  57   ILE A O   1 
ATOM   233  C CB  . ILE A 1 40  ? -5.236  -16.909 14.867  1.00 87.14  ?  57   ILE A CB  1 
ATOM   234  C CG1 . ILE A 1 40  ? -6.066  -15.673 14.514  1.00 100.23 ?  57   ILE A CG1 1 
ATOM   235  C CG2 . ILE A 1 40  ? -5.847  -18.152 14.240  1.00 85.53  ?  57   ILE A CG2 1 
ATOM   236  C CD1 . ILE A 1 40  ? -5.241  -14.521 13.975  1.00 93.04  ?  57   ILE A CD1 1 
ATOM   237  N N   . GLN A 1 41  ? -2.765  -17.151 17.023  1.00 87.79  ?  58   GLN A N   1 
ATOM   238  C CA  . GLN A 1 41  ? -1.475  -17.779 17.275  1.00 84.24  ?  58   GLN A CA  1 
ATOM   239  C C   . GLN A 1 41  ? -1.273  -18.188 18.730  1.00 89.79  ?  58   GLN A C   1 
ATOM   240  O O   . GLN A 1 41  ? -0.195  -18.685 19.071  1.00 98.07  ?  58   GLN A O   1 
ATOM   241  C CB  . GLN A 1 41  ? -0.347  -16.832 16.854  1.00 86.14  ?  58   GLN A CB  1 
ATOM   242  C CG  . GLN A 1 41  ? -0.504  -16.256 15.456  1.00 86.72  ?  58   GLN A CG  1 
ATOM   243  C CD  . GLN A 1 41  ? 0.576   -15.247 15.122  1.00 82.50  ?  58   GLN A CD  1 
ATOM   244  O OE1 . GLN A 1 41  ? 1.401   -14.903 15.969  1.00 88.21  ?  58   GLN A OE1 1 
ATOM   245  N NE2 . GLN A 1 41  ? 0.575   -14.764 13.885  1.00 76.99  ?  58   GLN A NE2 1 
ATOM   246  N N   . VAL A 1 42  ? -2.279  -18.003 19.589  1.00 86.85  ?  59   VAL A N   1 
ATOM   247  C CA  . VAL A 1 42  ? -2.092  -18.237 21.019  1.00 87.95  ?  59   VAL A CA  1 
ATOM   248  C C   . VAL A 1 42  ? -1.965  -19.727 21.319  1.00 85.83  ?  59   VAL A C   1 
ATOM   249  O O   . VAL A 1 42  ? -1.072  -20.146 22.066  1.00 90.20  ?  59   VAL A O   1 
ATOM   250  C CB  . VAL A 1 42  ? -3.242  -17.599 21.819  1.00 93.90  ?  59   VAL A CB  1 
ATOM   251  C CG1 . VAL A 1 42  ? -3.141  -17.983 23.283  1.00 73.14  ?  59   VAL A CG1 1 
ATOM   252  C CG2 . VAL A 1 42  ? -3.234  -16.086 21.657  1.00 75.07  ?  59   VAL A CG2 1 
ATOM   253  N N   . GLU A 1 43  ? -2.847  -20.547 20.745  1.00 89.08  ?  60   GLU A N   1 
ATOM   254  C CA  . GLU A 1 43  ? -2.889  -21.971 21.061  1.00 96.14  ?  60   GLU A CA  1 
ATOM   255  C C   . GLU A 1 43  ? -1.618  -22.717 20.671  1.00 92.50  ?  60   GLU A C   1 
ATOM   256  O O   . GLU A 1 43  ? -1.316  -23.743 21.287  1.00 91.78  ?  60   GLU A O   1 
ATOM   257  C CB  . GLU A 1 43  ? -4.097  -22.600 20.367  1.00 98.53  ?  60   GLU A CB  1 
ATOM   258  C CG  . GLU A 1 43  ? -5.374  -21.813 20.575  1.00 111.69 ?  60   GLU A CG  1 
ATOM   259  C CD  . GLU A 1 43  ? -6.263  -21.823 19.356  1.00 123.65 ?  60   GLU A CD  1 
ATOM   260  O OE1 . GLU A 1 43  ? -6.172  -22.784 18.564  1.00 110.63 ?  60   GLU A OE1 1 
ATOM   261  O OE2 . GLU A 1 43  ? -7.047  -20.865 19.186  1.00 108.09 -1 60   GLU A OE2 1 
ATOM   262  N N   . SER A 1 44  ? -0.869  -22.234 19.677  1.00 86.11  ?  61   SER A N   1 
ATOM   263  C CA  . SER A 1 44  ? 0.353   -22.883 19.220  1.00 82.93  ?  61   SER A CA  1 
ATOM   264  C C   . SER A 1 44  ? 1.612   -22.290 19.842  1.00 84.95  ?  61   SER A C   1 
ATOM   265  O O   . SER A 1 44  ? 2.718   -22.610 19.396  1.00 95.87  ?  61   SER A O   1 
ATOM   266  C CB  . SER A 1 44  ? 0.449   -22.809 17.695  1.00 85.70  ?  61   SER A CB  1 
ATOM   267  O OG  . SER A 1 44  ? 0.211   -21.490 17.236  1.00 99.73  ?  61   SER A OG  1 
ATOM   268  N N   . LEU A 1 45  ? 1.471   -21.434 20.849  1.00 86.56  ?  62   LEU A N   1 
ATOM   269  C CA  . LEU A 1 45  ? 2.631   -20.862 21.517  1.00 85.77  ?  62   LEU A CA  1 
ATOM   270  C C   . LEU A 1 45  ? 3.332   -21.920 22.360  1.00 88.42  ?  62   LEU A C   1 
ATOM   271  O O   . LEU A 1 45  ? 2.692   -22.638 23.134  1.00 91.13  ?  62   LEU A O   1 
ATOM   272  C CB  . LEU A 1 45  ? 2.208   -19.684 22.394  1.00 80.74  ?  62   LEU A CB  1 
ATOM   273  C CG  . LEU A 1 45  ? 1.854   -18.367 21.698  1.00 74.70  ?  62   LEU A CG  1 
ATOM   274  C CD1 . LEU A 1 45  ? 1.187   -17.411 22.676  1.00 67.38  ?  62   LEU A CD1 1 
ATOM   275  C CD2 . LEU A 1 45  ? 3.096   -17.731 21.092  1.00 71.92  ?  62   LEU A CD2 1 
ATOM   276  N N   . LYS A 1 46  ? 4.651   -22.017 22.205  1.00 88.04  ?  63   LYS A N   1 
ATOM   277  C CA  . LYS A 1 46  ? 5.476   -22.920 22.997  1.00 85.07  ?  63   LYS A CA  1 
ATOM   278  C C   . LYS A 1 46  ? 6.667   -22.151 23.545  1.00 82.21  ?  63   LYS A C   1 
ATOM   279  O O   . LYS A 1 46  ? 7.336   -21.425 22.802  1.00 85.05  ?  63   LYS A O   1 
ATOM   280  C CB  . LYS A 1 46  ? 5.971   -24.112 22.171  1.00 90.98  ?  63   LYS A CB  1 
ATOM   281  C CG  . LYS A 1 46  ? 4.903   -25.107 21.759  1.00 103.85 ?  63   LYS A CG  1 
ATOM   282  C CD  . LYS A 1 46  ? 5.558   -26.388 21.266  1.00 107.69 ?  63   LYS A CD  1 
ATOM   283  C CE  . LYS A 1 46  ? 4.593   -27.258 20.481  1.00 109.93 ?  63   LYS A CE  1 
ATOM   284  N NZ  . LYS A 1 46  ? 5.276   -28.470 19.946  1.00 110.26 1  63   LYS A NZ  1 
ATOM   285  N N   . LEU A 1 47  ? 6.935   -22.318 24.837  1.00 75.53  ?  64   LEU A N   1 
ATOM   286  C CA  . LEU A 1 47  ? 8.088   -21.697 25.480  1.00 76.35  ?  64   LEU A CA  1 
ATOM   287  C C   . LEU A 1 47  ? 9.284   -22.630 25.330  1.00 77.25  ?  64   LEU A C   1 
ATOM   288  O O   . LEU A 1 47  ? 9.310   -23.717 25.916  1.00 76.28  ?  64   LEU A O   1 
ATOM   289  C CB  . LEU A 1 47  ? 7.795   -21.402 26.948  1.00 67.08  ?  64   LEU A CB  1 
ATOM   290  C CG  . LEU A 1 47  ? 8.867   -20.615 27.704  1.00 81.25  ?  64   LEU A CG  1 
ATOM   291  C CD1 . LEU A 1 47  ? 9.175   -19.310 26.986  1.00 80.41  ?  64   LEU A CD1 1 
ATOM   292  C CD2 . LEU A 1 47  ? 8.428   -20.348 29.135  1.00 72.50  ?  64   LEU A CD2 1 
ATOM   293  N N   . GLU A 1 48  ? 10.266  -22.212 24.537  1.00 79.87  ?  65   GLU A N   1 
ATOM   294  C CA  . GLU A 1 48  ? 11.470  -22.995 24.302  1.00 80.91  ?  65   GLU A CA  1 
ATOM   295  C C   . GLU A 1 48  ? 12.570  -22.543 25.254  1.00 85.47  ?  65   GLU A C   1 
ATOM   296  O O   . GLU A 1 48  ? 12.713  -21.349 25.532  1.00 78.15  ?  65   GLU A O   1 
ATOM   297  C CB  . GLU A 1 48  ? 11.937  -22.857 22.851  1.00 86.32  ?  65   GLU A CB  1 
ATOM   298  C CG  . GLU A 1 48  ? 10.847  -23.092 21.806  1.00 91.92  ?  65   GLU A CG  1 
ATOM   299  C CD  . GLU A 1 48  ? 10.585  -24.564 21.523  1.00 104.73 ?  65   GLU A CD  1 
ATOM   300  O OE1 . GLU A 1 48  ? 10.735  -25.397 22.443  1.00 101.46 ?  65   GLU A OE1 1 
ATOM   301  O OE2 . GLU A 1 48  ? 10.230  -24.889 20.369  1.00 110.52 -1 65   GLU A OE2 1 
ATOM   302  N N   . SER A 1 49  ? 13.349  -23.505 25.746  1.00 88.74  ?  66   SER A N   1 
ATOM   303  C CA  . SER A 1 49  ? 14.339  -23.225 26.779  1.00 85.06  ?  66   SER A CA  1 
ATOM   304  C C   . SER A 1 49  ? 15.723  -22.962 26.201  1.00 84.73  ?  66   SER A C   1 
ATOM   305  O O   . SER A 1 49  ? 16.141  -21.806 26.084  1.00 93.06  ?  66   SER A O   1 
ATOM   306  C CB  . SER A 1 49  ? 14.406  -24.384 27.776  1.00 99.62  ?  66   SER A CB  1 
ATOM   307  O OG  . SER A 1 49  ? 15.436  -24.176 28.727  1.00 93.65  ?  66   SER A OG  1 
ATOM   308  N N   . SER A 1 50  ? 16.442  -24.031 25.854  1.00 75.73  ?  67   SER A N   1 
ATOM   309  C CA  . SER A 1 50  ? 17.846  -23.978 25.445  1.00 88.90  ?  67   SER A CA  1 
ATOM   310  C C   . SER A 1 50  ? 18.735  -23.351 26.515  1.00 90.26  ?  67   SER A C   1 
ATOM   311  O O   . SER A 1 50  ? 19.811  -22.827 26.206  1.00 89.40  ?  67   SER A O   1 
ATOM   312  C CB  . SER A 1 50  ? 18.024  -23.234 24.116  1.00 83.47  ?  67   SER A CB  1 
ATOM   313  O OG  . SER A 1 50  ? 18.025  -21.831 24.312  1.00 84.29  ?  67   SER A OG  1 
ATOM   314  N N   . CYS A 1 51  ? 18.308  -23.396 27.773  1.00 92.38  ?  68   CYS A N   1 
ATOM   315  C CA  . CYS A 1 51  ? 19.091  -22.856 28.871  1.00 81.20  ?  68   CYS A CA  1 
ATOM   316  C C   . CYS A 1 51  ? 19.936  -23.946 29.518  1.00 81.20  ?  68   CYS A C   1 
ATOM   317  O O   . CYS A 1 51  ? 19.800  -25.137 29.231  1.00 96.31  ?  68   CYS A O   1 
ATOM   318  C CB  . CYS A 1 51  ? 18.190  -22.214 29.923  1.00 89.98  ?  68   CYS A CB  1 
ATOM   319  S SG  . CYS A 1 51  ? 17.407  -20.676 29.425  1.00 102.40 ?  68   CYS A SG  1 
ATOM   320  N N   . ASN A 1 52  ? 20.814  -23.518 30.417  1.00 85.49  ?  69   ASN A N   1 
ATOM   321  C CA  . ASN A 1 52  ? 21.669  -24.432 31.170  1.00 75.93  ?  69   ASN A CA  1 
ATOM   322  C C   . ASN A 1 52  ? 21.175  -24.559 32.610  1.00 76.83  ?  69   ASN A C   1 
ATOM   323  O O   . ASN A 1 52  ? 21.879  -24.259 33.575  1.00 79.95  ?  69   ASN A O   1 
ATOM   324  C CB  . ASN A 1 52  ? 23.120  -23.961 31.116  1.00 77.35  ?  69   ASN A CB  1 
ATOM   325  C CG  . ASN A 1 52  ? 24.080  -24.952 31.745  1.00 89.65  ?  69   ASN A CG  1 
ATOM   326  O OD1 . ASN A 1 52  ? 23.788  -26.144 31.838  1.00 116.85 ?  69   ASN A OD1 1 
ATOM   327  N ND2 . ASN A 1 52  ? 25.232  -24.460 32.188  1.00 102.55 ?  69   ASN A ND2 1 
ATOM   328  N N   . PHE A 1 53  ? 19.926  -24.996 32.748  1.00 77.20  ?  70   PHE A N   1 
ATOM   329  C CA  . PHE A 1 53  ? 19.391  -25.355 34.056  1.00 78.49  ?  70   PHE A CA  1 
ATOM   330  C C   . PHE A 1 53  ? 18.408  -26.508 33.878  1.00 79.18  ?  70   PHE A C   1 
ATOM   331  O O   . PHE A 1 53  ? 18.280  -27.080 32.791  1.00 71.15  ?  70   PHE A O   1 
ATOM   332  C CB  . PHE A 1 53  ? 18.769  -24.143 34.770  1.00 76.21  ?  70   PHE A CB  1 
ATOM   333  C CG  . PHE A 1 53  ? 17.785  -23.352 33.940  1.00 73.47  ?  70   PHE A CG  1 
ATOM   334  C CD1 . PHE A 1 53  ? 17.964  -21.988 33.763  1.00 71.04  ?  70   PHE A CD1 1 
ATOM   335  C CD2 . PHE A 1 53  ? 16.671  -23.952 33.372  1.00 69.92  ?  70   PHE A CD2 1 
ATOM   336  C CE1 . PHE A 1 53  ? 17.064  -21.243 33.024  1.00 60.28  ?  70   PHE A CE1 1 
ATOM   337  C CE2 . PHE A 1 53  ? 15.770  -23.213 32.626  1.00 75.73  ?  70   PHE A CE2 1 
ATOM   338  C CZ  . PHE A 1 53  ? 15.966  -21.856 32.456  1.00 70.12  ?  70   PHE A CZ  1 
ATOM   339  N N   . ASP A 1 54  ? 17.708  -26.845 34.957  1.00 73.50  ?  71   ASP A N   1 
ATOM   340  C CA  . ASP A 1 54  ? 16.821  -28.004 35.017  1.00 64.86  ?  71   ASP A CA  1 
ATOM   341  C C   . ASP A 1 54  ? 15.380  -27.496 34.995  1.00 60.19  ?  71   ASP A C   1 
ATOM   342  O O   . ASP A 1 54  ? 14.806  -27.161 36.032  1.00 66.04  ?  71   ASP A O   1 
ATOM   343  C CB  . ASP A 1 54  ? 17.117  -28.832 36.266  1.00 64.62  ?  71   ASP A CB  1 
ATOM   344  C CG  . ASP A 1 54  ? 16.716  -30.284 36.113  1.00 76.41  ?  71   ASP A CG  1 
ATOM   345  O OD1 . ASP A 1 54  ? 16.082  -30.626 35.093  1.00 79.27  ?  71   ASP A OD1 1 
ATOM   346  O OD2 . ASP A 1 54  ? 17.038  -31.085 37.016  1.00 82.02  -1 71   ASP A OD2 1 
ATOM   347  N N   . LEU A 1 55  ? 14.797  -27.451 33.799  1.00 60.06  ?  72   LEU A N   1 
ATOM   348  C CA  . LEU A 1 55  ? 13.472  -26.875 33.615  1.00 59.51  ?  72   LEU A CA  1 
ATOM   349  C C   . LEU A 1 55  ? 12.388  -27.866 34.021  1.00 68.47  ?  72   LEU A C   1 
ATOM   350  O O   . LEU A 1 55  ? 12.421  -29.036 33.625  1.00 81.55  ?  72   LEU A O   1 
ATOM   351  C CB  . LEU A 1 55  ? 13.276  -26.457 32.158  1.00 60.86  ?  72   LEU A CB  1 
ATOM   352  C CG  . LEU A 1 55  ? 12.012  -25.651 31.853  1.00 61.37  ?  72   LEU A CG  1 
ATOM   353  C CD1 . LEU A 1 55  ? 12.256  -24.166 32.070  1.00 67.07  ?  72   LEU A CD1 1 
ATOM   354  C CD2 . LEU A 1 55  ? 11.514  -25.922 30.441  1.00 70.87  ?  72   LEU A CD2 1 
ATOM   355  N N   . HIS A 1 56  ? 11.423  -27.391 34.807  1.00 67.74  ?  73   HIS A N   1 
ATOM   356  C CA  . HIS A 1 56  ? 10.261  -28.192 35.175  1.00 61.49  ?  73   HIS A CA  1 
ATOM   357  C C   . HIS A 1 56  ? 9.235   -28.117 34.049  1.00 60.84  ?  73   HIS A C   1 
ATOM   358  O O   . HIS A 1 56  ? 8.792   -27.024 33.678  1.00 84.57  ?  73   HIS A O   1 
ATOM   359  C CB  . HIS A 1 56  ? 9.667   -27.694 36.491  1.00 64.06  ?  73   HIS A CB  1 
ATOM   360  C CG  . HIS A 1 56  ? 8.726   -28.663 37.136  1.00 64.69  ?  73   HIS A CG  1 
ATOM   361  N ND1 . HIS A 1 56  ? 8.986   -29.254 38.354  1.00 59.71  ?  73   HIS A ND1 1 
ATOM   362  C CD2 . HIS A 1 56  ? 7.527   -29.145 36.733  1.00 64.12  ?  73   HIS A CD2 1 
ATOM   363  C CE1 . HIS A 1 56  ? 7.986   -30.056 38.674  1.00 59.48  ?  73   HIS A CE1 1 
ATOM   364  N NE2 . HIS A 1 56  ? 7.088   -30.009 37.706  1.00 60.05  ?  73   HIS A NE2 1 
ATOM   365  N N   . THR A 1 57  ? 8.856   -29.273 33.510  1.00 62.84  ?  74   THR A N   1 
ATOM   366  C CA  . THR A 1 57  ? 8.093   -29.344 32.269  1.00 65.70  ?  74   THR A CA  1 
ATOM   367  C C   . THR A 1 57  ? 6.583   -29.414 32.474  1.00 72.06  ?  74   THR A C   1 
ATOM   368  O O   . THR A 1 57  ? 5.846   -29.428 31.482  1.00 64.99  ?  74   THR A O   1 
ATOM   369  C CB  . THR A 1 57  ? 8.548   -30.555 31.445  1.00 67.99  ?  74   THR A CB  1 
ATOM   370  O OG1 . THR A 1 57  ? 8.503   -31.734 32.259  1.00 66.74  ?  74   THR A OG1 1 
ATOM   371  C CG2 . THR A 1 57  ? 9.967   -30.351 30.932  1.00 75.45  ?  74   THR A CG2 1 
ATOM   372  N N   . SER A 1 58  ? 6.104   -29.445 33.722  1.00 68.49  ?  75   SER A N   1 
ATOM   373  C CA  . SER A 1 58  ? 4.669   -29.587 33.963  1.00 64.69  ?  75   SER A CA  1 
ATOM   374  C C   . SER A 1 58  ? 3.873   -28.476 33.288  1.00 76.71  ?  75   SER A C   1 
ATOM   375  O O   . SER A 1 58  ? 2.827   -28.735 32.680  1.00 66.89  ?  75   SER A O   1 
ATOM   376  C CB  . SER A 1 58  ? 4.382   -29.607 35.464  1.00 61.66  ?  75   SER A CB  1 
ATOM   377  O OG  . SER A 1 58  ? 4.790   -30.832 36.047  1.00 72.34  ?  75   SER A OG  1 
ATOM   378  N N   . THR A 1 59  ? 4.354   -27.235 33.373  1.00 70.65  ?  76   THR A N   1 
ATOM   379  C CA  . THR A 1 59  ? 3.638   -26.115 32.774  1.00 65.39  ?  76   THR A CA  1 
ATOM   380  C C   . THR A 1 59  ? 3.592   -26.181 31.253  1.00 70.08  ?  76   THR A C   1 
ATOM   381  O O   . THR A 1 59  ? 2.816   -25.437 30.646  1.00 69.87  ?  76   THR A O   1 
ATOM   382  C CB  . THR A 1 59  ? 4.271   -24.791 33.206  1.00 63.50  ?  76   THR A CB  1 
ATOM   383  O OG1 . THR A 1 59  ? 5.663   -24.789 32.864  1.00 76.87  ?  76   THR A OG1 1 
ATOM   384  C CG2 . THR A 1 59  ? 4.121   -24.595 34.706  1.00 59.10  ?  76   THR A CG2 1 
ATOM   385  N N   . SER A 1 60  ? 4.388   -27.045 30.626  1.00 75.40  ?  77   SER A N   1 
ATOM   386  C CA  . SER A 1 60  ? 4.427   -27.148 29.174  1.00 77.42  ?  77   SER A CA  1 
ATOM   387  C C   . SER A 1 60  ? 3.413   -28.142 28.619  1.00 68.83  ?  77   SER A C   1 
ATOM   388  O O   . SER A 1 60  ? 3.507   -28.509 27.443  1.00 76.42  ?  77   SER A O   1 
ATOM   389  C CB  . SER A 1 60  ? 5.836   -27.527 28.710  1.00 65.92  ?  77   SER A CB  1 
ATOM   390  O OG  . SER A 1 60  ? 6.259   -28.742 29.303  1.00 82.69  ?  77   SER A OG  1 
ATOM   391  N N   . SER A 1 61  ? 2.454   -28.582 29.427  1.00 75.68  ?  78   SER A N   1 
ATOM   392  C CA  . SER A 1 61  ? 1.417   -29.497 28.977  1.00 78.11  ?  78   SER A CA  1 
ATOM   393  C C   . SER A 1 61  ? 0.154   -28.724 28.611  1.00 79.24  ?  78   SER A C   1 
ATOM   394  O O   . SER A 1 61  ? 0.006   -27.538 28.913  1.00 72.60  ?  78   SER A O   1 
ATOM   395  C CB  . SER A 1 61  ? 1.112   -30.543 30.055  1.00 69.30  ?  78   SER A CB  1 
ATOM   396  O OG  . SER A 1 61  ? 0.375   -29.976 31.124  1.00 83.23  ?  78   SER A OG  1 
ATOM   397  N N   . GLN A 1 62  ? -0.768  -29.420 27.951  1.00 81.99  ?  79   GLN A N   1 
ATOM   398  C CA  . GLN A 1 62  ? -2.001  -28.795 27.495  1.00 76.75  ?  79   GLN A CA  1 
ATOM   399  C C   . GLN A 1 62  ? -3.045  -28.782 28.602  1.00 79.43  ?  79   GLN A C   1 
ATOM   400  O O   . GLN A 1 62  ? -3.191  -29.750 29.353  1.00 75.46  ?  79   GLN A O   1 
ATOM   401  C CB  . GLN A 1 62  ? -2.552  -29.525 26.270  1.00 79.72  ?  79   GLN A CB  1 
ATOM   402  C CG  . GLN A 1 62  ? -1.672  -29.413 25.041  1.00 86.98  ?  79   GLN A CG  1 
ATOM   403  C CD  . GLN A 1 62  ? -2.386  -29.826 23.768  1.00 103.02 ?  79   GLN A CD  1 
ATOM   404  O OE1 . GLN A 1 62  ? -3.432  -30.474 23.810  1.00 94.82  ?  79   GLN A OE1 1 
ATOM   405  N NE2 . GLN A 1 62  ? -1.827  -29.442 22.626  1.00 115.13 ?  79   GLN A NE2 1 
ATOM   406  N N   . GLN A 1 63  ? -3.774  -27.673 28.696  1.00 83.17  ?  80   GLN A N   1 
ATOM   407  C CA  . GLN A 1 63  ? -4.859  -27.524 29.652  1.00 81.04  ?  80   GLN A CA  1 
ATOM   408  C C   . GLN A 1 63  ? -6.062  -26.914 28.950  1.00 82.13  ?  80   GLN A C   1 
ATOM   409  O O   . GLN A 1 63  ? -5.914  -26.032 28.100  1.00 80.64  ?  80   GLN A O   1 
ATOM   410  C CB  . GLN A 1 63  ? -4.445  -26.652 30.843  1.00 79.04  ?  80   GLN A CB  1 
ATOM   411  C CG  . GLN A 1 63  ? -4.606  -27.333 32.194  1.00 84.08  ?  80   GLN A CG  1 
ATOM   412  C CD  . GLN A 1 63  ? -6.043  -27.716 32.495  1.00 79.03  ?  80   GLN A CD  1 
ATOM   413  O OE1 . GLN A 1 63  ? -6.983  -27.095 31.998  1.00 76.64  ?  80   GLN A OE1 1 
ATOM   414  N NE2 . GLN A 1 63  ? -6.220  -28.746 33.315  1.00 83.79  ?  80   GLN A NE2 1 
ATOM   415  N N   . ALA A 1 64  ? -7.250  -27.391 29.309  1.00 80.54  ?  81   ALA A N   1 
ATOM   416  C CA  . ALA A 1 64  ? -8.480  -26.932 28.677  1.00 78.61  ?  81   ALA A CA  1 
ATOM   417  C C   . ALA A 1 64  ? -8.923  -25.615 29.304  1.00 80.21  ?  81   ALA A C   1 
ATOM   418  O O   . ALA A 1 64  ? -9.094  -25.527 30.525  1.00 79.40  ?  81   ALA A O   1 
ATOM   419  C CB  . ALA A 1 64  ? -9.571  -27.991 28.810  1.00 71.90  ?  81   ALA A CB  1 
ATOM   420  N N   . PHE A 1 65  ? -9.106  -24.594 28.470  1.00 78.48  ?  82   PHE A N   1 
ATOM   421  C CA  . PHE A 1 65  ? -9.593  -23.289 28.887  1.00 75.45  ?  82   PHE A CA  1 
ATOM   422  C C   . PHE A 1 65  ? -10.911 -22.999 28.189  1.00 72.60  ?  82   PHE A C   1 
ATOM   423  O O   . PHE A 1 65  ? -11.102 -23.367 27.024  1.00 68.51  ?  82   PHE A O   1 
ATOM   424  C CB  . PHE A 1 65  ? -8.584  -22.183 28.553  1.00 74.54  ?  82   PHE A CB  1 
ATOM   425  C CG  . PHE A 1 65  ? -7.508  -22.009 29.582  1.00 75.12  ?  82   PHE A CG  1 
ATOM   426  C CD1 . PHE A 1 65  ? -7.488  -20.891 30.395  1.00 65.40  ?  82   PHE A CD1 1 
ATOM   427  C CD2 . PHE A 1 65  ? -6.517  -22.963 29.737  1.00 93.84  ?  82   PHE A CD2 1 
ATOM   428  C CE1 . PHE A 1 65  ? -6.500  -20.725 31.343  1.00 75.28  ?  82   PHE A CE1 1 
ATOM   429  C CE2 . PHE A 1 65  ? -5.526  -22.803 30.686  1.00 87.86  ?  82   PHE A CE2 1 
ATOM   430  C CZ  . PHE A 1 65  ? -5.520  -21.683 31.491  1.00 70.32  ?  82   PHE A CZ  1 
ATOM   431  N N   . THR A 1 66  ? -11.819 -22.335 28.900  1.00 80.46  ?  83   THR A N   1 
ATOM   432  C CA  . THR A 1 66  ? -13.081 -21.890 28.312  1.00 84.33  ?  83   THR A CA  1 
ATOM   433  C C   . THR A 1 66  ? -12.848 -20.502 27.731  1.00 77.06  ?  83   THR A C   1 
ATOM   434  O O   . THR A 1 66  ? -13.004 -19.484 28.408  1.00 82.42  ?  83   THR A O   1 
ATOM   435  C CB  . THR A 1 66  ? -14.203 -21.895 29.345  1.00 81.00  ?  83   THR A CB  1 
ATOM   436  O OG1 . THR A 1 66  ? -14.365 -23.219 29.869  1.00 85.42  ?  83   THR A OG1 1 
ATOM   437  C CG2 . THR A 1 66  ? -15.517 -21.448 28.712  1.00 88.05  ?  83   THR A CG2 1 
ATOM   438  N N   . LYS A 1 67  ? -12.434 -20.463 26.466  1.00 73.73  ?  84   LYS A N   1 
ATOM   439  C CA  . LYS A 1 67  ? -12.268 -19.199 25.765  1.00 76.95  ?  84   LYS A CA  1 
ATOM   440  C C   . LYS A 1 67  ? -13.610 -18.489 25.667  1.00 77.66  ?  84   LYS A C   1 
ATOM   441  O O   . LYS A 1 67  ? -14.571 -19.034 25.111  1.00 81.10  ?  84   LYS A O   1 
ATOM   442  C CB  . LYS A 1 67  ? -11.677 -19.447 24.378  1.00 73.01  ?  84   LYS A CB  1 
ATOM   443  C CG  . LYS A 1 67  ? -11.673 -18.241 23.458  1.00 74.12  ?  84   LYS A CG  1 
ATOM   444  C CD  . LYS A 1 67  ? -10.794 -18.506 22.246  1.00 71.29  ?  84   LYS A CD  1 
ATOM   445  C CE  . LYS A 1 67  ? -11.279 -17.750 21.020  1.00 79.68  ?  84   LYS A CE  1 
ATOM   446  N NZ  . LYS A 1 67  ? -10.392 -17.992 19.848  1.00 74.43  1  84   LYS A NZ  1 
ATOM   447  N N   . TRP A 1 68  ? -13.668 -17.279 26.221  1.00 70.71  ?  85   TRP A N   1 
ATOM   448  C CA  . TRP A 1 68  ? -14.904 -16.519 26.383  1.00 70.30  ?  85   TRP A CA  1 
ATOM   449  C C   . TRP A 1 68  ? -14.710 -15.153 25.740  1.00 71.20  ?  85   TRP A C   1 
ATOM   450  O O   . TRP A 1 68  ? -13.979 -14.311 26.273  1.00 63.77  ?  85   TRP A O   1 
ATOM   451  C CB  . TRP A 1 68  ? -15.261 -16.383 27.865  1.00 63.07  ?  85   TRP A CB  1 
ATOM   452  C CG  . TRP A 1 68  ? -16.493 -15.582 28.141  1.00 63.04  ?  85   TRP A CG  1 
ATOM   453  C CD1 . TRP A 1 68  ? -17.597 -15.473 27.348  1.00 64.39  ?  85   TRP A CD1 1 
ATOM   454  C CD2 . TRP A 1 68  ? -16.745 -14.771 29.295  1.00 64.21  ?  85   TRP A CD2 1 
ATOM   455  N NE1 . TRP A 1 68  ? -18.523 -14.648 27.939  1.00 67.33  ?  85   TRP A NE1 1 
ATOM   456  C CE2 . TRP A 1 68  ? -18.023 -14.202 29.134  1.00 70.26  ?  85   TRP A CE2 1 
ATOM   457  C CE3 . TRP A 1 68  ? -16.013 -14.471 30.448  1.00 64.08  ?  85   TRP A CE3 1 
ATOM   458  C CZ2 . TRP A 1 68  ? -18.586 -13.350 30.083  1.00 73.53  ?  85   TRP A CZ2 1 
ATOM   459  C CZ3 . TRP A 1 68  ? -16.573 -13.626 31.389  1.00 67.26  ?  85   TRP A CZ3 1 
ATOM   460  C CH2 . TRP A 1 68  ? -17.846 -13.075 31.201  1.00 71.25  ?  85   TRP A CH2 1 
ATOM   461  N N   . THR A 1 69  ? -15.362 -14.930 24.603  1.00 70.37  ?  86   THR A N   1 
ATOM   462  C CA  . THR A 1 69  ? -15.185 -13.707 23.836  1.00 71.02  ?  86   THR A CA  1 
ATOM   463  C C   . THR A 1 69  ? -16.516 -12.993 23.647  1.00 79.84  ?  86   THR A C   1 
ATOM   464  O O   . THR A 1 69  ? -17.590 -13.558 23.868  1.00 91.02  ?  86   THR A O   1 
ATOM   465  C CB  . THR A 1 69  ? -14.556 -13.993 22.464  1.00 74.47  ?  86   THR A CB  1 
ATOM   466  O OG1 . THR A 1 69  ? -15.396 -14.891 21.727  1.00 84.93  ?  86   THR A OG1 1 
ATOM   467  C CG2 . THR A 1 69  ? -13.176 -14.612 22.627  1.00 73.45  ?  86   THR A CG2 1 
ATOM   468  N N   . TRP A 1 70  ? -16.425 -11.728 23.241  1.00 65.30  ?  87   TRP A N   1 
ATOM   469  C CA  . TRP A 1 70  ? -17.580 -10.928 22.867  1.00 66.87  ?  87   TRP A CA  1 
ATOM   470  C C   . TRP A 1 70  ? -17.321 -10.305 21.504  1.00 72.01  ?  87   TRP A C   1 
ATOM   471  O O   . TRP A 1 70  ? -16.171 -10.080 21.118  1.00 67.65  ?  87   TRP A O   1 
ATOM   472  C CB  . TRP A 1 70  ? -17.876 -9.821  23.895  1.00 63.79  ?  87   TRP A CB  1 
ATOM   473  C CG  . TRP A 1 70  ? -16.873 -8.701  23.881  1.00 63.96  ?  87   TRP A CG  1 
ATOM   474  C CD1 . TRP A 1 70  ? -15.742 -8.604  24.638  1.00 73.57  ?  87   TRP A CD1 1 
ATOM   475  C CD2 . TRP A 1 70  ? -16.913 -7.520  23.068  1.00 65.40  ?  87   TRP A CD2 1 
ATOM   476  N NE1 . TRP A 1 70  ? -15.075 -7.439  24.347  1.00 59.41  ?  87   TRP A NE1 1 
ATOM   477  C CE2 . TRP A 1 70  ? -15.772 -6.756  23.386  1.00 75.43  ?  87   TRP A CE2 1 
ATOM   478  C CE3 . TRP A 1 70  ? -17.801 -7.036  22.102  1.00 76.77  ?  87   TRP A CE3 1 
ATOM   479  C CZ2 . TRP A 1 70  ? -15.497 -5.534  22.772  1.00 70.87  ?  87   TRP A CZ2 1 
ATOM   480  C CZ3 . TRP A 1 70  ? -17.525 -5.824  21.493  1.00 73.87  ?  87   TRP A CZ3 1 
ATOM   481  C CH2 . TRP A 1 70  ? -16.384 -5.088  21.830  1.00 68.17  ?  87   TRP A CH2 1 
ATOM   482  N N   . GLU A 1 71  ? -18.400 -10.027 20.778  1.00 73.13  ?  88   GLU A N   1 
ATOM   483  C CA  . GLU A 1 71  ? -18.274 -9.351  19.494  1.00 78.31  ?  88   GLU A CA  1 
ATOM   484  C C   . GLU A 1 71  ? -19.603 -8.710  19.127  1.00 79.09  ?  88   GLU A C   1 
ATOM   485  O O   . GLU A 1 71  ? -20.671 -9.138  19.577  1.00 74.58  ?  88   GLU A O   1 
ATOM   486  C CB  . GLU A 1 71  ? -17.816 -10.310 18.388  1.00 82.90  ?  88   GLU A CB  1 
ATOM   487  C CG  . GLU A 1 71  ? -18.795 -11.424 18.068  1.00 88.44  ?  88   GLU A CG  1 
ATOM   488  C CD  . GLU A 1 71  ? -18.380 -12.222 16.848  1.00 105.25 ?  88   GLU A CD  1 
ATOM   489  O OE1 . GLU A 1 71  ? -17.440 -11.790 16.147  1.00 100.91 ?  88   GLU A OE1 1 
ATOM   490  O OE2 . GLU A 1 71  ? -18.991 -13.281 16.590  1.00 115.35 -1 88   GLU A OE2 1 
ATOM   491  N N   . VAL A 1 72  ? -19.516 -7.669  18.295  1.00 75.83  ?  89   VAL A N   1 
ATOM   492  C CA  . VAL A 1 72  ? -20.715 -7.012  17.801  1.00 82.23  ?  89   VAL A CA  1 
ATOM   493  C C   . VAL A 1 72  ? -21.519 -7.996  16.955  1.00 77.96  ?  89   VAL A C   1 
ATOM   494  O O   . VAL A 1 72  ? -20.969 -8.911  16.328  1.00 83.31  ?  89   VAL A O   1 
ATOM   495  C CB  . VAL A 1 72  ? -20.347 -5.752  16.998  1.00 70.73  ?  89   VAL A CB  1 
ATOM   496  C CG1 . VAL A 1 72  ? -19.659 -6.125  15.689  1.00 70.80  ?  89   VAL A CG1 1 
ATOM   497  C CG2 . VAL A 1 72  ? -21.575 -4.892  16.742  1.00 69.57  ?  89   VAL A CG2 1 
ATOM   498  N N   . LYS A 1 73  ? -22.838 -7.822  16.959  1.00 72.23  ?  90   LYS A N   1 
ATOM   499  C CA  . LYS A 1 73  ? -23.704 -8.680  16.162  1.00 76.10  ?  90   LYS A CA  1 
ATOM   500  C C   . LYS A 1 73  ? -23.441 -8.459  14.678  1.00 89.19  ?  90   LYS A C   1 
ATOM   501  O O   . LYS A 1 73  ? -23.370 -7.319  14.211  1.00 85.62  ?  90   LYS A O   1 
ATOM   502  C CB  . LYS A 1 73  ? -25.170 -8.410  16.493  1.00 76.18  ?  90   LYS A CB  1 
ATOM   503  C CG  . LYS A 1 73  ? -25.626 -9.027  17.804  1.00 74.44  ?  90   LYS A CG  1 
ATOM   504  C CD  . LYS A 1 73  ? -27.089 -8.731  18.082  1.00 75.14  ?  90   LYS A CD  1 
ATOM   505  C CE  . LYS A 1 73  ? -27.596 -9.542  19.263  1.00 75.09  ?  90   LYS A CE  1 
ATOM   506  N NZ  . LYS A 1 73  ? -28.969 -9.134  19.671  1.00 91.57  1  90   LYS A NZ  1 
ATOM   507  N N   . SER A 1 74  ? -23.290 -9.561  13.940  1.00 88.29  ?  91   SER A N   1 
ATOM   508  C CA  . SER A 1 74  ? -23.005 -9.465  12.512  1.00 90.37  ?  91   SER A CA  1 
ATOM   509  C C   . SER A 1 74  ? -24.154 -8.815  11.754  1.00 93.69  ?  91   SER A C   1 
ATOM   510  O O   . SER A 1 74  ? -23.926 -8.109  10.766  1.00 101.31 ?  91   SER A O   1 
ATOM   511  C CB  . SER A 1 74  ? -22.715 -10.853 11.943  1.00 84.23  ?  91   SER A CB  1 
ATOM   512  O OG  . SER A 1 74  ? -21.774 -11.546 12.745  1.00 97.95  ?  91   SER A OG  1 
ATOM   513  N N   . ASP A 1 75  ? -25.384 -9.035  12.200  1.00 100.14 ?  92   ASP A N   1 
ATOM   514  C CA  . ASP A 1 75  ? -26.574 -8.492  11.544  1.00 101.58 ?  92   ASP A CA  1 
ATOM   515  C C   . ASP A 1 75  ? -27.025 -7.194  12.204  1.00 108.55 ?  92   ASP A C   1 
ATOM   516  O O   . ASP A 1 75  ? -28.194 -7.014  12.544  1.00 120.79 ?  92   ASP A O   1 
ATOM   517  C CB  . ASP A 1 75  ? -27.687 -9.534  11.552  1.00 104.57 ?  92   ASP A CB  1 
ATOM   518  C CG  . ASP A 1 75  ? -28.058 -9.979  12.954  1.00 106.78 ?  92   ASP A CG  1 
ATOM   519  O OD1 . ASP A 1 75  ? -29.267 -10.135 13.229  1.00 107.38 ?  92   ASP A OD1 1 
ATOM   520  O OD2 . ASP A 1 75  ? -27.142 -10.149 13.787  1.00 106.99 -1 92   ASP A OD2 1 
ATOM   521  N N   . LEU A 1 76  ? -26.089 -6.268  12.388  1.00 100.36 ?  93   LEU A N   1 
ATOM   522  C CA  . LEU A 1 76  ? -26.375 -4.988  13.022  1.00 89.22  ?  93   LEU A CA  1 
ATOM   523  C C   . LEU A 1 76  ? -26.737 -3.969  11.949  1.00 85.83  ?  93   LEU A C   1 
ATOM   524  O O   . LEU A 1 76  ? -25.928 -3.685  11.059  1.00 96.94  ?  93   LEU A O   1 
ATOM   525  C CB  . LEU A 1 76  ? -25.176 -4.507  13.837  1.00 84.15  ?  93   LEU A CB  1 
ATOM   526  C CG  . LEU A 1 76  ? -25.469 -3.406  14.858  1.00 80.72  ?  93   LEU A CG  1 
ATOM   527  C CD1 . LEU A 1 76  ? -26.291 -3.962  16.011  1.00 72.96  ?  93   LEU A CD1 1 
ATOM   528  C CD2 . LEU A 1 76  ? -24.186 -2.768  15.364  1.00 77.14  ?  93   LEU A CD2 1 
ATOM   529  N N   . ALA A 1 77  ? -27.948 -3.424  12.035  1.00 84.40  ?  94   ALA A N   1 
ATOM   530  C CA  . ALA A 1 77  ? -28.392 -2.431  11.070  1.00 88.32  ?  94   ALA A CA  1 
ATOM   531  C C   . ALA A 1 77  ? -27.521 -1.180  11.148  1.00 87.56  ?  94   ALA A C   1 
ATOM   532  O O   . ALA A 1 77  ? -26.864 -0.906  12.156  1.00 88.68  ?  94   ALA A O   1 
ATOM   533  C CB  . ALA A 1 77  ? -29.858 -2.069  11.308  1.00 86.22  ?  94   ALA A CB  1 
ATOM   534  N N   . GLU A 1 78  ? -27.519 -0.420  10.056  1.00 86.89  ?  95   GLU A N   1 
ATOM   535  C CA  . GLU A 1 78  ? -26.725 0.799   9.997   1.00 96.28  ?  95   GLU A CA  1 
ATOM   536  C C   . GLU A 1 78  ? -27.218 1.809   11.026  1.00 89.60  ?  95   GLU A C   1 
ATOM   537  O O   . GLU A 1 78  ? -28.422 1.948   11.259  1.00 88.55  ?  95   GLU A O   1 
ATOM   538  C CB  . GLU A 1 78  ? -26.789 1.403   8.595   1.00 95.92  ?  95   GLU A CB  1 
ATOM   539  C CG  . GLU A 1 78  ? -26.247 0.497   7.501   1.00 105.13 ?  95   GLU A CG  1 
ATOM   540  C CD  . GLU A 1 78  ? -27.177 0.413   6.307   1.00 135.27 ?  95   GLU A CD  1 
ATOM   541  O OE1 . GLU A 1 78  ? -28.403 0.290   6.517   1.00 128.51 ?  95   GLU A OE1 1 
ATOM   542  O OE2 . GLU A 1 78  ? -26.685 0.477   5.160   1.00 135.57 -1 95   GLU A OE2 1 
ATOM   543  N N   . ASN A 1 79  ? -26.270 2.509   11.650  1.00 90.83  ?  96   ASN A N   1 
ATOM   544  C CA  . ASN A 1 79  ? -26.540 3.537   12.653  1.00 93.15  ?  96   ASN A CA  1 
ATOM   545  C C   . ASN A 1 79  ? -27.279 2.989   13.870  1.00 90.19  ?  96   ASN A C   1 
ATOM   546  O O   . ASN A 1 79  ? -27.975 3.738   14.564  1.00 93.85  ?  96   ASN A O   1 
ATOM   547  C CB  . ASN A 1 79  ? -27.319 4.712   12.051  1.00 89.32  ?  96   ASN A CB  1 
ATOM   548  C CG  . ASN A 1 79  ? -26.622 5.318   10.850  1.00 94.89  ?  96   ASN A CG  1 
ATOM   549  O OD1 . ASN A 1 79  ? -25.394 5.330   10.771  1.00 102.80 ?  96   ASN A OD1 1 
ATOM   550  N ND2 . ASN A 1 79  ? -27.405 5.824   9.904   1.00 98.46  ?  96   ASN A ND2 1 
ATOM   551  N N   . THR A 1 80  ? -27.147 1.693   14.146  1.00 77.22  ?  97   THR A N   1 
ATOM   552  C CA  . THR A 1 80  ? -27.742 1.125   15.347  1.00 76.43  ?  97   THR A CA  1 
ATOM   553  C C   . THR A 1 80  ? -27.003 1.635   16.577  1.00 79.54  ?  97   THR A C   1 
ATOM   554  O O   . THR A 1 80  ? -25.775 1.540   16.661  1.00 83.36  ?  97   THR A O   1 
ATOM   555  C CB  . THR A 1 80  ? -27.698 -0.401  15.303  1.00 78.75  ?  97   THR A CB  1 
ATOM   556  O OG1 . THR A 1 80  ? -28.380 -0.869  14.132  1.00 95.25  ?  97   THR A OG1 1 
ATOM   557  C CG2 . THR A 1 80  ? -28.365 -0.986  16.540  1.00 71.91  ?  97   THR A CG2 1 
ATOM   558  N N   . GLN A 1 81  ? -27.751 2.184   17.528  1.00 74.75  ?  98   GLN A N   1 
ATOM   559  C CA  . GLN A 1 81  ? -27.150 2.730   18.735  1.00 71.71  ?  98   GLN A CA  1 
ATOM   560  C C   . GLN A 1 81  ? -26.778 1.610   19.697  1.00 74.25  ?  98   GLN A C   1 
ATOM   561  O O   . GLN A 1 81  ? -27.520 0.637   19.860  1.00 77.75  ?  98   GLN A O   1 
ATOM   562  C CB  . GLN A 1 81  ? -28.106 3.717   19.404  1.00 69.49  ?  98   GLN A CB  1 
ATOM   563  C CG  . GLN A 1 81  ? -28.430 4.920   18.531  1.00 72.14  ?  98   GLN A CG  1 
ATOM   564  C CD  . GLN A 1 81  ? -29.363 5.901   19.206  1.00 73.88  ?  98   GLN A CD  1 
ATOM   565  O OE1 . GLN A 1 81  ? -30.580 5.720   19.202  1.00 80.25  ?  98   GLN A OE1 1 
ATOM   566  N NE2 . GLN A 1 81  ? -28.798 6.951   19.790  1.00 70.65  ?  98   GLN A NE2 1 
ATOM   567  N N   . ALA A 1 82  ? -25.615 1.753   20.328  1.00 68.31  ?  99   ALA A N   1 
ATOM   568  C CA  . ALA A 1 82  ? -25.099 0.707   21.199  1.00 64.09  ?  99   ALA A CA  1 
ATOM   569  C C   . ALA A 1 82  ? -26.008 0.511   22.406  1.00 68.56  ?  99   ALA A C   1 
ATOM   570  O O   . ALA A 1 82  ? -26.509 1.473   22.994  1.00 76.91  ?  99   ALA A O   1 
ATOM   571  C CB  . ALA A 1 82  ? -23.681 1.051   21.654  1.00 65.43  ?  99   ALA A CB  1 
ATOM   572  N N   . SER A 1 83  ? -26.223 -0.751  22.767  1.00 70.69  ?  100  SER A N   1 
ATOM   573  C CA  . SER A 1 83  ? -27.060 -1.111  23.902  1.00 64.15  ?  100  SER A CA  1 
ATOM   574  C C   . SER A 1 83  ? -26.508 -2.391  24.515  1.00 73.84  ?  100  SER A C   1 
ATOM   575  O O   . SER A 1 83  ? -25.457 -2.894  24.105  1.00 76.59  ?  100  SER A O   1 
ATOM   576  C CB  . SER A 1 83  ? -28.523 -1.273  23.474  1.00 69.84  ?  100  SER A CB  1 
ATOM   577  O OG  . SER A 1 83  ? -28.659 -2.308  22.513  1.00 73.71  ?  100  SER A OG  1 
ATOM   578  N N   . SER A 1 84  ? -27.228 -2.926  25.501  1.00 73.84  ?  101  SER A N   1 
ATOM   579  C CA  . SER A 1 84  ? -26.834 -4.189  26.108  1.00 64.80  ?  101  SER A CA  1 
ATOM   580  C C   . SER A 1 84  ? -27.071 -5.381  25.190  1.00 69.26  ?  101  SER A C   1 
ATOM   581  O O   . SER A 1 84  ? -26.534 -6.460  25.460  1.00 69.66  ?  101  SER A O   1 
ATOM   582  C CB  . SER A 1 84  ? -27.584 -4.390  27.427  1.00 64.38  ?  101  SER A CB  1 
ATOM   583  O OG  . SER A 1 84  ? -28.980 -4.500  27.209  1.00 67.67  ?  101  SER A OG  1 
ATOM   584  N N   . THR A 1 85  ? -27.845 -5.213  24.116  1.00 67.11  ?  102  THR A N   1 
ATOM   585  C CA  . THR A 1 85  ? -28.182 -6.308  23.214  1.00 72.11  ?  102  THR A CA  1 
ATOM   586  C C   . THR A 1 85  ? -27.640 -6.106  21.804  1.00 74.34  ?  102  THR A C   1 
ATOM   587  O O   . THR A 1 85  ? -27.955 -6.904  20.914  1.00 78.15  ?  102  THR A O   1 
ATOM   588  C CB  . THR A 1 85  ? -29.700 -6.500  23.153  1.00 73.91  ?  102  THR A CB  1 
ATOM   589  O OG1 . THR A 1 85  ? -30.282 -5.467  22.347  1.00 91.53  ?  102  THR A OG1 1 
ATOM   590  C CG2 . THR A 1 85  ? -30.301 -6.440  24.547  1.00 75.64  ?  102  THR A CG2 1 
ATOM   591  N N   . SER A 1 86  ? -26.844 -5.064  21.571  1.00 80.99  ?  103  SER A N   1 
ATOM   592  C CA  . SER A 1 86  ? -26.250 -4.843  20.259  1.00 75.31  ?  103  SER A CA  1 
ATOM   593  C C   . SER A 1 86  ? -25.001 -5.683  20.033  1.00 72.77  ?  103  SER A C   1 
ATOM   594  O O   . SER A 1 86  ? -24.361 -5.545  18.985  1.00 77.66  ?  103  SER A O   1 
ATOM   595  C CB  . SER A 1 86  ? -25.918 -3.361  20.071  1.00 71.89  ?  103  SER A CB  1 
ATOM   596  O OG  . SER A 1 86  ? -24.773 -2.990  20.819  1.00 79.14  ?  103  SER A OG  1 
ATOM   597  N N   . PHE A 1 87  ? -24.645 -6.542  20.984  1.00 68.90  ?  104  PHE A N   1 
ATOM   598  C CA  . PHE A 1 87  ? -23.470 -7.391  20.871  1.00 80.29  ?  104  PHE A CA  1 
ATOM   599  C C   . PHE A 1 87  ? -23.753 -8.697  21.596  1.00 73.76  ?  104  PHE A C   1 
ATOM   600  O O   . PHE A 1 87  ? -24.664 -8.784  22.424  1.00 72.43  ?  104  PHE A O   1 
ATOM   601  C CB  . PHE A 1 87  ? -22.224 -6.710  21.449  1.00 73.27  ?  104  PHE A CB  1 
ATOM   602  C CG  . PHE A 1 87  ? -22.301 -6.462  22.929  1.00 68.49  ?  104  PHE A CG  1 
ATOM   603  C CD1 . PHE A 1 87  ? -23.055 -5.416  23.434  1.00 64.65  ?  104  PHE A CD1 1 
ATOM   604  C CD2 . PHE A 1 87  ? -21.613 -7.272  23.815  1.00 71.80  ?  104  PHE A CD2 1 
ATOM   605  C CE1 . PHE A 1 87  ? -23.126 -5.187  24.795  1.00 62.59  ?  104  PHE A CE1 1 
ATOM   606  C CE2 . PHE A 1 87  ? -21.680 -7.047  25.174  1.00 67.34  ?  104  PHE A CE2 1 
ATOM   607  C CZ  . PHE A 1 87  ? -22.437 -6.003  25.665  1.00 68.51  ?  104  PHE A CZ  1 
ATOM   608  N N   . GLN A 1 88  ? -22.962 -9.716  21.278  1.00 68.86  ?  105  GLN A N   1 
ATOM   609  C CA  . GLN A 1 88  ? -23.152 -11.038 21.851  1.00 80.95  ?  105  GLN A CA  1 
ATOM   610  C C   . GLN A 1 88  ? -21.844 -11.544 22.437  1.00 68.43  ?  105  GLN A C   1 
ATOM   611  O O   . GLN A 1 88  ? -20.763 -11.013 22.165  1.00 70.26  ?  105  GLN A O   1 
ATOM   612  C CB  . GLN A 1 88  ? -23.681 -12.033 20.810  1.00 75.63  ?  105  GLN A CB  1 
ATOM   613  C CG  . GLN A 1 88  ? -25.178 -11.942 20.581  1.00 84.66  ?  105  GLN A CG  1 
ATOM   614  C CD  . GLN A 1 88  ? -25.630 -12.741 19.378  1.00 89.64  ?  105  GLN A CD  1 
ATOM   615  O OE1 . GLN A 1 88  ? -24.844 -13.012 18.471  1.00 102.80 ?  105  GLN A OE1 1 
ATOM   616  N NE2 . GLN A 1 88  ? -26.902 -13.125 19.364  1.00 100.36 ?  105  GLN A NE2 1 
ATOM   617  N N   . THR A 1 89  ? -21.966 -12.576 23.266  1.00 74.80  ?  106  THR A N   1 
ATOM   618  C CA  . THR A 1 89  ? -20.826 -13.256 23.856  1.00 75.76  ?  106  THR A CA  1 
ATOM   619  C C   . THR A 1 89  ? -20.936 -14.746 23.566  1.00 79.43  ?  106  THR A C   1 
ATOM   620  O O   . THR A 1 89  ? -22.030 -15.277 23.357  1.00 78.87  ?  106  THR A O   1 
ATOM   621  C CB  . THR A 1 89  ? -20.737 -13.014 25.372  1.00 75.59  ?  106  THR A CB  1 
ATOM   622  O OG1 . THR A 1 89  ? -19.526 -13.586 25.881  1.00 85.14  ?  106  THR A OG1 1 
ATOM   623  C CG2 . THR A 1 89  ? -21.925 -13.640 26.086  1.00 77.57  ?  106  THR A CG2 1 
ATOM   624  N N   . LYS A 1 90  ? -19.786 -15.412 23.546  1.00 80.49  ?  107  LYS A N   1 
ATOM   625  C CA  . LYS A 1 90  ? -19.726 -16.830 23.229  1.00 78.70  ?  107  LYS A CA  1 
ATOM   626  C C   . LYS A 1 90  ? -18.547 -17.448 23.962  1.00 85.49  ?  107  LYS A C   1 
ATOM   627  O O   . LYS A 1 90  ? -17.627 -16.751 24.402  1.00 81.55  ?  107  LYS A O   1 
ATOM   628  C CB  . LYS A 1 90  ? -19.612 -17.061 21.718  1.00 73.23  ?  107  LYS A CB  1 
ATOM   629  C CG  . LYS A 1 90  ? -18.618 -16.134 21.039  1.00 88.87  ?  107  LYS A CG  1 
ATOM   630  C CD  . LYS A 1 90  ? -18.684 -16.231 19.522  1.00 74.18  ?  107  LYS A CD  1 
ATOM   631  C CE  . LYS A 1 90  ? -17.950 -17.452 19.003  1.00 75.77  ?  107  LYS A CE  1 
ATOM   632  N NZ  . LYS A 1 90  ? -17.731 -17.367 17.532  1.00 97.05  1  107  LYS A NZ  1 
ATOM   633  N N   . SER A 1 91  ? -18.589 -18.771 24.096  1.00 73.27  ?  108  SER A N   1 
ATOM   634  C CA  . SER A 1 91  ? -17.549 -19.497 24.805  1.00 84.69  ?  108  SER A CA  1 
ATOM   635  C C   . SER A 1 91  ? -17.370 -20.869 24.173  1.00 91.54  ?  108  SER A C   1 
ATOM   636  O O   . SER A 1 91  ? -18.324 -21.470 23.670  1.00 92.84  ?  108  SER A O   1 
ATOM   637  C CB  . SER A 1 91  ? -17.878 -19.636 26.297  1.00 83.05  ?  108  SER A CB  1 
ATOM   638  O OG  . SER A 1 91  ? -19.152 -20.225 26.487  1.00 90.06  ?  108  SER A OG  1 
ATOM   639  N N   . SER A 1 92  ? -16.130 -21.348 24.198  1.00 89.51  ?  109  SER A N   1 
ATOM   640  C CA  . SER A 1 92  ? -15.813 -22.680 23.697  1.00 83.54  ?  109  SER A CA  1 
ATOM   641  C C   . SER A 1 92  ? -14.499 -23.135 24.312  1.00 83.19  ?  109  SER A C   1 
ATOM   642  O O   . SER A 1 92  ? -13.650 -22.316 24.662  1.00 90.19  ?  109  SER A O   1 
ATOM   643  C CB  . SER A 1 92  ? -15.724 -22.709 22.167  1.00 79.76  ?  109  SER A CB  1 
ATOM   644  O OG  . SER A 1 92  ? -14.513 -22.131 21.713  1.00 89.03  ?  109  SER A OG  1 
ATOM   645  N N   . GLU A 1 93  ? -14.337 -24.449 24.435  1.00 81.42  ?  110  GLU A N   1 
ATOM   646  C CA  . GLU A 1 93  ? -13.137 -24.998 25.050  1.00 76.71  ?  110  GLU A CA  1 
ATOM   647  C C   . GLU A 1 93  ? -12.000 -25.084 24.040  1.00 79.05  ?  110  GLU A C   1 
ATOM   648  O O   . GLU A 1 93  ? -12.210 -25.405 22.867  1.00 84.98  ?  110  GLU A O   1 
ATOM   649  C CB  . GLU A 1 93  ? -13.419 -26.378 25.644  1.00 81.67  ?  110  GLU A CB  1 
ATOM   650  C CG  . GLU A 1 93  ? -14.013 -26.338 27.045  1.00 77.13  ?  110  GLU A CG  1 
ATOM   651  C CD  . GLU A 1 93  ? -15.370 -25.665 27.088  1.00 90.13  ?  110  GLU A CD  1 
ATOM   652  O OE1 . GLU A 1 93  ? -16.141 -25.821 26.118  1.00 100.72 ?  110  GLU A OE1 1 
ATOM   653  O OE2 . GLU A 1 93  ? -15.663 -24.975 28.088  1.00 97.86  -1 110  GLU A OE2 1 
ATOM   654  N N   . VAL A 1 94  ? -10.790 -24.793 24.510  1.00 74.01  ?  111  VAL A N   1 
ATOM   655  C CA  . VAL A 1 94  ? -9.600  -24.792 23.664  1.00 75.97  ?  111  VAL A CA  1 
ATOM   656  C C   . VAL A 1 94  ? -8.401  -25.156 24.530  1.00 75.37  ?  111  VAL A C   1 
ATOM   657  O O   . VAL A 1 94  ? -8.337  -24.794 25.707  1.00 81.51  ?  111  VAL A O   1 
ATOM   658  C CB  . VAL A 1 94  ? -9.416  -23.426 22.964  1.00 90.82  ?  111  VAL A CB  1 
ATOM   659  C CG1 . VAL A 1 94  ? -9.277  -22.306 23.988  1.00 73.14  ?  111  VAL A CG1 1 
ATOM   660  C CG2 . VAL A 1 94  ? -8.225  -23.455 22.019  1.00 91.62  ?  111  VAL A CG2 1 
ATOM   661  N N   . ASN A 1 95  ? -7.455  -25.888 23.951  1.00 90.37  ?  112  ASN A N   1 
ATOM   662  C CA  . ASN A 1 95  ? -6.280  -26.346 24.681  1.00 84.21  ?  112  ASN A CA  1 
ATOM   663  C C   . ASN A 1 95  ? -5.178  -25.295 24.598  1.00 84.72  ?  112  ASN A C   1 
ATOM   664  O O   . ASN A 1 95  ? -4.721  -24.951 23.503  1.00 89.05  ?  112  ASN A O   1 
ATOM   665  C CB  . ASN A 1 95  ? -5.791  -27.685 24.131  1.00 83.36  ?  112  ASN A CB  1 
ATOM   666  C CG  . ASN A 1 95  ? -6.703  -28.835 24.508  1.00 92.52  ?  112  ASN A CG  1 
ATOM   667  O OD1 . ASN A 1 95  ? -7.800  -28.628 25.027  1.00 91.62  ?  112  ASN A OD1 1 
ATOM   668  N ND2 . ASN A 1 95  ? -6.253  -30.058 24.249  1.00 98.84  ?  112  ASN A ND2 1 
ATOM   669  N N   . LEU A 1 96  ? -4.756  -24.791 25.754  1.00 84.25  ?  113  LEU A N   1 
ATOM   670  C CA  . LEU A 1 96  ? -3.658  -23.842 25.853  1.00 79.81  ?  113  LEU A CA  1 
ATOM   671  C C   . LEU A 1 96  ? -2.451  -24.530 26.478  1.00 75.80  ?  113  LEU A C   1 
ATOM   672  O O   . LEU A 1 96  ? -2.597  -25.371 27.370  1.00 81.24  ?  113  LEU A O   1 
ATOM   673  C CB  . LEU A 1 96  ? -4.060  -22.619 26.681  1.00 77.01  ?  113  LEU A CB  1 
ATOM   674  C CG  . LEU A 1 96  ? -5.245  -21.826 26.124  1.00 72.64  ?  113  LEU A CG  1 
ATOM   675  C CD1 . LEU A 1 96  ? -5.547  -20.612 26.988  1.00 75.95  ?  113  LEU A CD1 1 
ATOM   676  C CD2 . LEU A 1 96  ? -4.981  -21.411 24.685  1.00 81.17  ?  113  LEU A CD2 1 
ATOM   677  N N   . ARG A 1 97  ? -1.261  -24.170 26.004  1.00 74.98  ?  114  ARG A N   1 
ATOM   678  C CA  . ARG A 1 97  ? -0.027  -24.829 26.409  1.00 76.84  ?  114  ARG A CA  1 
ATOM   679  C C   . ARG A 1 97  ? 1.001   -23.784 26.815  1.00 74.48  ?  114  ARG A C   1 
ATOM   680  O O   . ARG A 1 97  ? 1.211   -22.803 26.095  1.00 79.46  ?  114  ARG A O   1 
ATOM   681  C CB  . ARG A 1 97  ? 0.521   -25.703 25.273  1.00 80.19  ?  114  ARG A CB  1 
ATOM   682  C CG  . ARG A 1 97  ? 1.727   -26.541 25.656  1.00 91.29  ?  114  ARG A CG  1 
ATOM   683  C CD  . ARG A 1 97  ? 2.406   -27.137 24.430  1.00 94.30  ?  114  ARG A CD  1 
ATOM   684  N NE  . ARG A 1 97  ? 1.612   -28.181 23.785  1.00 102.06 ?  114  ARG A NE  1 
ATOM   685  C CZ  . ARG A 1 97  ? 1.733   -29.479 24.047  1.00 101.43 ?  114  ARG A CZ  1 
ATOM   686  N NH1 . ARG A 1 97  ? 2.613   -29.895 24.947  1.00 93.51  1  114  ARG A NH1 1 
ATOM   687  N NH2 . ARG A 1 97  ? 0.976   -30.361 23.409  1.00 96.92  ?  114  ARG A NH2 1 
ATOM   688  N N   . GLY A 1 98  ? 1.635   -23.994 27.968  1.00 72.36  ?  115  GLY A N   1 
ATOM   689  C CA  . GLY A 1 98  ? 2.709   -23.138 28.426  1.00 74.64  ?  115  GLY A CA  1 
ATOM   690  C C   . GLY A 1 98  ? 2.339   -22.123 29.486  1.00 63.40  ?  115  GLY A C   1 
ATOM   691  O O   . GLY A 1 98  ? 3.229   -21.418 29.976  1.00 71.34  ?  115  GLY A O   1 
ATOM   692  N N   . LEU A 1 99  ? 1.066   -22.026 29.858  1.00 72.13  ?  116  LEU A N   1 
ATOM   693  C CA  . LEU A 1 99  ? 0.644   -21.029 30.830  1.00 65.45  ?  116  LEU A CA  1 
ATOM   694  C C   . LEU A 1 99  ? 1.145   -21.383 32.227  1.00 66.61  ?  116  LEU A C   1 
ATOM   695  O O   . LEU A 1 99  ? 1.499   -22.527 32.523  1.00 77.27  ?  116  LEU A O   1 
ATOM   696  C CB  . LEU A 1 99  ? -0.878  -20.896 30.835  1.00 60.35  ?  116  LEU A CB  1 
ATOM   697  C CG  . LEU A 1 99  ? -1.470  -20.176 29.623  1.00 61.01  ?  116  LEU A CG  1 
ATOM   698  C CD1 . LEU A 1 99  ? -2.953  -20.453 29.511  1.00 73.02  ?  116  LEU A CD1 1 
ATOM   699  C CD2 . LEU A 1 99  ? -1.217  -18.679 29.715  1.00 71.82  ?  116  LEU A CD2 1 
ATOM   700  N N   . CYS A 1 100 ? 1.170   -20.371 33.095  1.00 70.06  ?  117  CYS A N   1 
ATOM   701  C CA  . CYS A 1 100 ? 1.645   -20.555 34.460  1.00 69.79  ?  117  CYS A CA  1 
ATOM   702  C C   . CYS A 1 100 ? 0.656   -21.382 35.269  1.00 75.91  ?  117  CYS A C   1 
ATOM   703  O O   . CYS A 1 100 ? -0.224  -20.837 35.944  1.00 77.98  ?  117  CYS A O   1 
ATOM   704  C CB  . CYS A 1 100 ? 1.904   -19.202 35.127  1.00 67.39  ?  117  CYS A CB  1 
ATOM   705  S SG  . CYS A 1 100 ? 3.371   -18.355 34.487  1.00 87.17  ?  117  CYS A SG  1 
ATOM   706  N N   . LEU A 1 101 ? 0.797   -22.707 35.195  1.00 71.80  ?  118  LEU A N   1 
ATOM   707  C CA  . LEU A 1 101 ? -0.054  -23.650 35.915  1.00 70.55  ?  118  LEU A CA  1 
ATOM   708  C C   . LEU A 1 101 ? 0.850   -24.622 36.674  1.00 73.41  ?  118  LEU A C   1 
ATOM   709  O O   . LEU A 1 101 ? 1.011   -25.784 36.296  1.00 71.85  ?  118  LEU A O   1 
ATOM   710  C CB  . LEU A 1 101 ? -0.997  -24.376 34.962  1.00 71.61  ?  118  LEU A CB  1 
ATOM   711  C CG  . LEU A 1 101 ? -2.318  -23.635 34.788  1.00 77.03  ?  118  LEU A CG  1 
ATOM   712  C CD1 . LEU A 1 101 ? -3.248  -24.372 33.840  1.00 75.74  ?  118  LEU A CD1 1 
ATOM   713  C CD2 . LEU A 1 101 ? -2.951  -23.458 36.155  1.00 86.86  ?  118  LEU A CD2 1 
ATOM   714  N N   . VAL A 1 102 ? 1.436   -24.133 37.757  1.00 68.15  ?  119  VAL A N   1 
ATOM   715  C CA  . VAL A 1 102 ? 2.442   -24.901 38.490  1.00 55.40  ?  119  VAL A CA  1 
ATOM   716  C C   . VAL A 1 102 ? 1.734   -25.865 39.440  1.00 68.85  ?  119  VAL A C   1 
ATOM   717  O O   . VAL A 1 102 ? 0.799   -25.451 40.144  1.00 61.65  ?  119  VAL A O   1 
ATOM   718  C CB  . VAL A 1 102 ? 3.373   -23.967 39.253  1.00 54.18  ?  119  VAL A CB  1 
ATOM   719  C CG1 . VAL A 1 102 ? 4.505   -24.752 39.880  1.00 54.29  ?  119  VAL A CG1 1 
ATOM   720  C CG2 . VAL A 1 102 ? 3.909   -22.883 38.330  1.00 59.34  ?  119  VAL A CG2 1 
ATOM   721  N N   . PRO A 1 103 ? 2.133   -27.133 39.481  1.00 57.09  ?  120  PRO A N   1 
ATOM   722  C CA  . PRO A 1 103 ? 1.575   -28.059 40.471  1.00 57.92  ?  120  PRO A CA  1 
ATOM   723  C C   . PRO A 1 103 ? 2.034   -27.688 41.869  1.00 57.06  ?  120  PRO A C   1 
ATOM   724  O O   . PRO A 1 103 ? 3.049   -26.994 42.031  1.00 58.96  ?  120  PRO A O   1 
ATOM   725  C CB  . PRO A 1 103 ? 2.141   -29.423 40.041  1.00 59.18  ?  120  PRO A CB  1 
ATOM   726  C CG  . PRO A 1 103 ? 2.581   -29.236 38.622  1.00 70.21  ?  120  PRO A CG  1 
ATOM   727  C CD  . PRO A 1 103 ? 3.025   -27.812 38.528  1.00 57.76  ?  120  PRO A CD  1 
ATOM   728  N N   . PRO A 1 104 ? 1.315   -28.123 42.903  1.00 57.68  ?  121  PRO A N   1 
ATOM   729  C CA  . PRO A 1 104 ? 1.718   -27.783 44.272  1.00 57.12  ?  121  PRO A CA  1 
ATOM   730  C C   . PRO A 1 104 ? 3.083   -28.355 44.627  1.00 58.20  ?  121  PRO A C   1 
ATOM   731  O O   . PRO A 1 104 ? 3.548   -29.330 44.032  1.00 67.62  ?  121  PRO A O   1 
ATOM   732  C CB  . PRO A 1 104 ? 0.608   -28.399 45.135  1.00 58.78  ?  121  PRO A CB  1 
ATOM   733  C CG  . PRO A 1 104 ? -0.058  -29.410 44.255  1.00 59.69  ?  121  PRO A CG  1 
ATOM   734  C CD  . PRO A 1 104 ? 0.043   -28.863 42.869  1.00 59.11  ?  121  PRO A CD  1 
ATOM   735  N N   . LEU A 1 105 ? 3.733   -27.701 45.596  1.00 61.40  ?  122  LEU A N   1 
ATOM   736  C CA  . LEU A 1 105 ? 5.021   -28.106 46.158  1.00 61.95  ?  122  LEU A CA  1 
ATOM   737  C C   . LEU A 1 105 ? 6.182   -27.918 45.187  1.00 59.14  ?  122  LEU A C   1 
ATOM   738  O O   . LEU A 1 105 ? 7.344   -28.066 45.578  1.00 62.61  ?  122  LEU A O   1 
ATOM   739  C CB  . LEU A 1 105 ? 4.971   -29.563 46.632  1.00 61.09  ?  122  LEU A CB  1 
ATOM   740  C CG  . LEU A 1 105 ? 3.969   -29.886 47.741  1.00 59.59  ?  122  LEU A CG  1 
ATOM   741  C CD1 . LEU A 1 105 ? 3.951   -31.379 48.024  1.00 62.37  ?  122  LEU A CD1 1 
ATOM   742  C CD2 . LEU A 1 105 ? 4.295   -29.102 49.002  1.00 65.26  ?  122  LEU A CD2 1 
ATOM   743  N N   . VAL A 1 106 ? 5.893   -27.584 43.927  1.00 58.71  ?  123  VAL A N   1 
ATOM   744  C CA  . VAL A 1 106 ? 6.961   -27.422 42.943  1.00 55.05  ?  123  VAL A CA  1 
ATOM   745  C C   . VAL A 1 106 ? 7.775   -26.167 43.240  1.00 59.85  ?  123  VAL A C   1 
ATOM   746  O O   . VAL A 1 106 ? 9.009   -26.211 43.304  1.00 65.02  ?  123  VAL A O   1 
ATOM   747  C CB  . VAL A 1 106 ? 6.381   -27.396 41.518  1.00 58.73  ?  123  VAL A CB  1 
ATOM   748  C CG1 . VAL A 1 106 ? 7.458   -27.006 40.514  1.00 56.54  ?  123  VAL A CG1 1 
ATOM   749  C CG2 . VAL A 1 106 ? 5.787   -28.751 41.166  1.00 65.54  ?  123  VAL A CG2 1 
ATOM   750  N N   . ILE A 1 107 ? 7.099   -25.032 43.428  1.00 65.03  ?  124  ILE A N   1 
ATOM   751  C CA  . ILE A 1 107 ? 7.813   -23.790 43.711  1.00 60.13  ?  124  ILE A CA  1 
ATOM   752  C C   . ILE A 1 107 ? 8.376   -23.806 45.126  1.00 56.30  ?  124  ILE A C   1 
ATOM   753  O O   . ILE A 1 107 ? 9.474   -23.296 45.377  1.00 64.25  ?  124  ILE A O   1 
ATOM   754  C CB  . ILE A 1 107 ? 6.893   -22.576 43.480  1.00 66.53  ?  124  ILE A CB  1 
ATOM   755  C CG1 . ILE A 1 107 ? 6.367   -22.566 42.044  1.00 60.30  ?  124  ILE A CG1 1 
ATOM   756  C CG2 . ILE A 1 107 ? 7.637   -21.282 43.770  1.00 55.43  ?  124  ILE A CG2 1 
ATOM   757  C CD1 . ILE A 1 107 ? 5.431   -21.415 41.743  1.00 52.79  ?  124  ILE A CD1 1 
ATOM   758  N N   . GLU A 1 108 ? 7.640   -24.398 46.072  1.00 61.82  ?  125  GLU A N   1 
ATOM   759  C CA  . GLU A 1 108 ? 8.101   -24.431 47.457  1.00 53.14  ?  125  GLU A CA  1 
ATOM   760  C C   . GLU A 1 108 ? 9.414   -25.194 47.589  1.00 60.99  ?  125  GLU A C   1 
ATOM   761  O O   . GLU A 1 108 ? 10.331  -24.749 48.289  1.00 66.65  ?  125  GLU A O   1 
ATOM   762  C CB  . GLU A 1 108 ? 7.035   -25.059 48.357  1.00 60.05  ?  125  GLU A CB  1 
ATOM   763  C CG  . GLU A 1 108 ? 5.714   -24.303 48.421  1.00 53.76  ?  125  GLU A CG  1 
ATOM   764  C CD  . GLU A 1 108 ? 4.739   -24.728 47.340  1.00 58.74  ?  125  GLU A CD  1 
ATOM   765  O OE1 . GLU A 1 108 ? 5.087   -24.624 46.144  1.00 65.40  ?  125  GLU A OE1 1 
ATOM   766  O OE2 . GLU A 1 108 ? 3.626   -25.175 47.689  1.00 64.36  -1 125  GLU A OE2 1 
ATOM   767  N N   . THR A 1 109 ? 9.525   -26.340 46.920  1.00 56.50  ?  126  THR A N   1 
ATOM   768  C CA  . THR A 1 109 ? 10.690  -27.205 47.032  1.00 54.37  ?  126  THR A CA  1 
ATOM   769  C C   . THR A 1 109 ? 11.703  -26.985 45.915  1.00 54.86  ?  126  THR A C   1 
ATOM   770  O O   . THR A 1 109 ? 12.609  -27.807 45.746  1.00 59.58  ?  126  THR A O   1 
ATOM   771  C CB  . THR A 1 109 ? 10.257  -28.673 47.055  1.00 58.00  ?  126  THR A CB  1 
ATOM   772  O OG1 . THR A 1 109 ? 9.678   -29.022 45.791  1.00 58.29  ?  126  THR A OG1 1 
ATOM   773  C CG2 . THR A 1 109 ? 9.231   -28.908 48.156  1.00 55.70  ?  126  THR A CG2 1 
ATOM   774  N N   . ALA A 1 110 ? 11.577  -25.893 45.154  1.00 59.08  ?  127  ALA A N   1 
ATOM   775  C CA  . ALA A 1 110 ? 12.505  -25.648 44.054  1.00 53.40  ?  127  ALA A CA  1 
ATOM   776  C C   . ALA A 1 110 ? 13.934  -25.469 44.549  1.00 55.37  ?  127  ALA A C   1 
ATOM   777  O O   . ALA A 1 110 ? 14.885  -25.796 43.829  1.00 64.47  ?  127  ALA A O   1 
ATOM   778  C CB  . ALA A 1 110 ? 12.063  -24.423 43.253  1.00 57.21  ?  127  ALA A CB  1 
ATOM   779  N N   . ALA A 1 111 ? 14.107  -24.955 45.769  1.00 60.21  ?  128  ALA A N   1 
ATOM   780  C CA  . ALA A 1 111 ? 15.449  -24.796 46.319  1.00 58.24  ?  128  ALA A CA  1 
ATOM   781  C C   . ALA A 1 111 ? 16.114  -26.147 46.558  1.00 67.80  ?  128  ALA A C   1 
ATOM   782  O O   . ALA A 1 111 ? 17.320  -26.298 46.333  1.00 64.41  ?  128  ALA A O   1 
ATOM   783  C CB  . ALA A 1 111 ? 15.390  -23.987 47.614  1.00 60.15  ?  128  ALA A CB  1 
ATOM   784  N N   . ARG A 1 112 ? 15.344  -27.141 47.007  1.00 65.49  ?  129  ARG A N   1 
ATOM   785  C CA  . ARG A 1 112 ? 15.911  -28.463 47.251  1.00 69.49  ?  129  ARG A CA  1 
ATOM   786  C C   . ARG A 1 112 ? 15.982  -29.292 45.974  1.00 70.51  ?  129  ARG A C   1 
ATOM   787  O O   . ARG A 1 112 ? 17.005  -29.931 45.706  1.00 76.04  ?  129  ARG A O   1 
ATOM   788  C CB  . ARG A 1 112 ? 15.098  -29.198 48.317  1.00 80.41  ?  129  ARG A CB  1 
ATOM   789  C CG  . ARG A 1 112 ? 15.652  -30.566 48.682  1.00 86.42  ?  129  ARG A CG  1 
ATOM   790  C CD  . ARG A 1 112 ? 14.876  -31.197 49.826  1.00 95.73  ?  129  ARG A CD  1 
ATOM   791  N NE  . ARG A 1 112 ? 15.363  -32.539 50.134  1.00 117.80 ?  129  ARG A NE  1 
ATOM   792  C CZ  . ARG A 1 112 ? 14.877  -33.309 51.102  1.00 122.51 ?  129  ARG A CZ  1 
ATOM   793  N NH1 . ARG A 1 112 ? 13.884  -32.874 51.865  1.00 120.02 1  129  ARG A NH1 1 
ATOM   794  N NH2 . ARG A 1 112 ? 15.384  -34.518 51.306  1.00 100.89 ?  129  ARG A NH2 1 
ATOM   795  N N   . THR A 1 113 ? 14.913  -29.292 45.173  1.00 69.02  ?  130  THR A N   1 
ATOM   796  C CA  . THR A 1 113 ? 14.906  -30.052 43.929  1.00 59.25  ?  130  THR A CA  1 
ATOM   797  C C   . THR A 1 113 ? 15.778  -29.426 42.849  1.00 64.10  ?  130  THR A C   1 
ATOM   798  O O   . THR A 1 113 ? 16.051  -30.089 41.842  1.00 66.10  ?  130  THR A O   1 
ATOM   799  C CB  . THR A 1 113 ? 13.475  -30.201 43.406  1.00 61.25  ?  130  THR A CB  1 
ATOM   800  O OG1 . THR A 1 113 ? 12.949  -28.912 43.067  1.00 65.94  ?  130  THR A OG1 1 
ATOM   801  C CG2 . THR A 1 113 ? 12.586  -30.845 44.459  1.00 56.63  ?  130  THR A CG2 1 
ATOM   802  N N   . ARG A 1 114 ? 16.213  -28.177 43.033  1.00 67.97  ?  131  ARG A N   1 
ATOM   803  C CA  . ARG A 1 114 ? 17.082  -27.478 42.083  1.00 63.90  ?  131  ARG A CA  1 
ATOM   804  C C   . ARG A 1 114 ? 16.435  -27.354 40.706  1.00 66.69  ?  131  ARG A C   1 
ATOM   805  O O   . ARG A 1 114 ? 17.125  -27.340 39.683  1.00 65.62  ?  131  ARG A O   1 
ATOM   806  C CB  . ARG A 1 114 ? 18.449  -28.161 41.970  1.00 72.41  ?  131  ARG A CB  1 
ATOM   807  C CG  . ARG A 1 114 ? 19.117  -28.441 43.306  1.00 69.39  ?  131  ARG A CG  1 
ATOM   808  C CD  . ARG A 1 114 ? 19.716  -27.185 43.919  1.00 82.65  ?  131  ARG A CD  1 
ATOM   809  N NE  . ARG A 1 114 ? 21.148  -27.081 43.654  1.00 93.29  ?  131  ARG A NE  1 
ATOM   810  C CZ  . ARG A 1 114 ? 21.967  -26.248 44.287  1.00 101.54 ?  131  ARG A CZ  1 
ATOM   811  N NH1 . ARG A 1 114 ? 21.497  -25.442 45.229  1.00 96.82  1  131  ARG A NH1 1 
ATOM   812  N NH2 . ARG A 1 114 ? 23.258  -26.224 43.982  1.00 82.48  ?  131  ARG A NH2 1 
ATOM   813  N N   . LYS A 1 115 ? 15.111  -27.259 40.664  1.00 65.11  ?  132  LYS A N   1 
ATOM   814  C CA  . LYS A 1 115 ? 14.384  -27.132 39.411  1.00 67.73  ?  132  LYS A CA  1 
ATOM   815  C C   . LYS A 1 115 ? 14.049  -25.674 39.124  1.00 66.01  ?  132  LYS A C   1 
ATOM   816  O O   . LYS A 1 115 ? 13.963  -24.836 40.025  1.00 64.43  ?  132  LYS A O   1 
ATOM   817  C CB  . LYS A 1 115 ? 13.104  -27.972 39.434  1.00 66.48  ?  132  LYS A CB  1 
ATOM   818  C CG  . LYS A 1 115 ? 13.325  -29.420 39.034  1.00 67.38  ?  132  LYS A CG  1 
ATOM   819  C CD  . LYS A 1 115 ? 12.246  -29.894 38.075  1.00 80.47  ?  132  LYS A CD  1 
ATOM   820  C CE  . LYS A 1 115 ? 12.637  -31.203 37.405  1.00 77.25  ?  132  LYS A CE  1 
ATOM   821  N NZ  . LYS A 1 115 ? 13.806  -31.045 36.500  1.00 77.12  1  132  LYS A NZ  1 
ATOM   822  N N   . THR A 1 116 ? 13.863  -25.382 37.839  1.00 64.80  ?  133  THR A N   1 
ATOM   823  C CA  . THR A 1 116 ? 13.575  -24.038 37.358  1.00 61.64  ?  133  THR A CA  1 
ATOM   824  C C   . THR A 1 116 ? 12.220  -24.037 36.666  1.00 67.25  ?  133  THR A C   1 
ATOM   825  O O   . THR A 1 116 ? 11.946  -24.903 35.827  1.00 60.12  ?  133  THR A O   1 
ATOM   826  C CB  . THR A 1 116 ? 14.669  -23.555 36.399  1.00 62.71  ?  133  THR A CB  1 
ATOM   827  O OG1 . THR A 1 116 ? 15.925  -23.510 37.087  1.00 66.44  ?  133  THR A OG1 1 
ATOM   828  C CG2 . THR A 1 116 ? 14.343  -22.171 35.864  1.00 66.45  ?  133  THR A CG2 1 
ATOM   829  N N   . ILE A 1 117 ? 11.376  -23.072 37.022  1.00 66.89  ?  134  ILE A N   1 
ATOM   830  C CA  . ILE A 1 117 ? 10.038  -22.931 36.462  1.00 57.39  ?  134  ILE A CA  1 
ATOM   831  C C   . ILE A 1 117 ? 10.040  -21.752 35.499  1.00 62.74  ?  134  ILE A C   1 
ATOM   832  O O   . ILE A 1 117 ? 10.495  -20.655 35.846  1.00 72.13  ?  134  ILE A O   1 
ATOM   833  C CB  . ILE A 1 117 ? 8.976   -22.741 37.562  1.00 56.30  ?  134  ILE A CB  1 
ATOM   834  C CG1 . ILE A 1 117 ? 8.877   -23.986 38.450  1.00 55.56  ?  134  ILE A CG1 1 
ATOM   835  C CG2 . ILE A 1 117 ? 7.619   -22.421 36.951  1.00 60.48  ?  134  ILE A CG2 1 
ATOM   836  C CD1 . ILE A 1 117 ? 9.789   -23.966 39.660  1.00 54.45  ?  134  ILE A CD1 1 
ATOM   837  N N   . ALA A 1 118 ? 9.534   -21.981 34.290  1.00 60.89  ?  135  ALA A N   1 
ATOM   838  C CA  . ALA A 1 118 ? 9.383   -20.930 33.293  1.00 58.84  ?  135  ALA A CA  1 
ATOM   839  C C   . ALA A 1 118 ? 8.016   -21.072 32.648  1.00 65.36  ?  135  ALA A C   1 
ATOM   840  O O   . ALA A 1 118 ? 7.669   -22.151 32.158  1.00 71.25  ?  135  ALA A O   1 
ATOM   841  C CB  . ALA A 1 118 ? 10.482  -21.001 32.227  1.00 58.05  ?  135  ALA A CB  1 
ATOM   842  N N   . CYS A 1 119 ? 7.244   -19.990 32.650  1.00 63.36  ?  136  CYS A N   1 
ATOM   843  C CA  . CYS A 1 119 ? 5.888   -20.031 32.112  1.00 62.98  ?  136  CYS A CA  1 
ATOM   844  C C   . CYS A 1 119 ? 5.502   -18.627 31.667  1.00 72.03  ?  136  CYS A C   1 
ATOM   845  O O   . CYS A 1 119 ? 6.334   -17.718 31.636  1.00 73.02  ?  136  CYS A O   1 
ATOM   846  C CB  . CYS A 1 119 ? 4.919   -20.609 33.152  1.00 55.43  ?  136  CYS A CB  1 
ATOM   847  S SG  . CYS A 1 119 ? 4.865   -19.713 34.723  1.00 81.45  ?  136  CYS A SG  1 
ATOM   848  N N   . PHE A 1 120 ? 4.231   -18.447 31.310  1.00 64.73  ?  137  PHE A N   1 
ATOM   849  C CA  . PHE A 1 120 ? 3.750   -17.133 30.912  1.00 61.77  ?  137  PHE A CA  1 
ATOM   850  C C   . PHE A 1 120 ? 2.265   -17.016 31.215  1.00 62.26  ?  137  PHE A C   1 
ATOM   851  O O   . PHE A 1 120 ? 1.547   -18.015 31.291  1.00 60.36  ?  137  PHE A O   1 
ATOM   852  C CB  . PHE A 1 120 ? 4.014   -16.852 29.423  1.00 58.62  ?  137  PHE A CB  1 
ATOM   853  C CG  . PHE A 1 120 ? 3.261   -17.754 28.482  1.00 57.39  ?  137  PHE A CG  1 
ATOM   854  C CD1 . PHE A 1 120 ? 1.998   -17.407 28.025  1.00 58.80  ?  137  PHE A CD1 1 
ATOM   855  C CD2 . PHE A 1 120 ? 3.825   -18.937 28.034  1.00 65.11  ?  137  PHE A CD2 1 
ATOM   856  C CE1 . PHE A 1 120 ? 1.307   -18.231 27.154  1.00 62.51  ?  137  PHE A CE1 1 
ATOM   857  C CE2 . PHE A 1 120 ? 3.139   -19.764 27.161  1.00 64.90  ?  137  PHE A CE2 1 
ATOM   858  C CZ  . PHE A 1 120 ? 1.879   -19.411 26.722  1.00 62.15  ?  137  PHE A CZ  1 
ATOM   859  N N   . ASP A 1 121 ? 1.822   -15.778 31.400  1.00 62.35  ?  138  ASP A N   1 
ATOM   860  C CA  . ASP A 1 121 ? 0.412   -15.441 31.534  1.00 58.71  ?  138  ASP A CA  1 
ATOM   861  C C   . ASP A 1 121 ? 0.009   -14.530 30.380  1.00 62.04  ?  138  ASP A C   1 
ATOM   862  O O   . ASP A 1 121 ? 0.854   -14.010 29.650  1.00 62.20  ?  138  ASP A O   1 
ATOM   863  C CB  . ASP A 1 121 ? 0.124   -14.772 32.884  1.00 62.33  ?  138  ASP A CB  1 
ATOM   864  C CG  . ASP A 1 121 ? -1.330  -14.892 33.295  1.00 66.89  ?  138  ASP A CG  1 
ATOM   865  O OD1 . ASP A 1 121 ? -2.128  -15.439 32.504  1.00 64.88  ?  138  ASP A OD1 1 
ATOM   866  O OD2 . ASP A 1 121 ? -1.675  -14.445 34.409  1.00 68.46  -1 138  ASP A OD2 1 
ATOM   867  N N   . LEU A 1 122 ? -1.297  -14.332 30.216  1.00 58.65  ?  139  LEU A N   1 
ATOM   868  C CA  . LEU A 1 122 ? -1.835  -13.596 29.079  1.00 61.75  ?  139  LEU A CA  1 
ATOM   869  C C   . LEU A 1 122 ? -2.651  -12.402 29.554  1.00 60.10  ?  139  LEU A C   1 
ATOM   870  O O   . LEU A 1 122 ? -3.480  -12.532 30.460  1.00 62.27  ?  139  LEU A O   1 
ATOM   871  C CB  . LEU A 1 122 ? -2.699  -14.507 28.202  1.00 60.17  ?  139  LEU A CB  1 
ATOM   872  C CG  . LEU A 1 122 ? -1.962  -15.647 27.500  1.00 58.19  ?  139  LEU A CG  1 
ATOM   873  C CD1 . LEU A 1 122 ? -2.925  -16.488 26.678  1.00 58.72  ?  139  LEU A CD1 1 
ATOM   874  C CD2 . LEU A 1 122 ? -0.844  -15.097 26.628  1.00 70.41  ?  139  LEU A CD2 1 
ATOM   875  N N   . SER A 1 123 ? -2.415  -11.244 28.935  1.00 63.09  ?  140  SER A N   1 
ATOM   876  C CA  . SER A 1 123 ? -3.230  -10.048 29.134  1.00 55.45  ?  140  SER A CA  1 
ATOM   877  C C   . SER A 1 123 ? -3.707  -9.604  27.758  1.00 58.26  ?  140  SER A C   1 
ATOM   878  O O   . SER A 1 123 ? -2.897  -9.205  26.918  1.00 59.55  ?  140  SER A O   1 
ATOM   879  C CB  . SER A 1 123 ? -2.435  -8.946  29.831  1.00 53.06  ?  140  SER A CB  1 
ATOM   880  O OG  . SER A 1 123 ? -1.966  -9.379  31.096  1.00 72.11  ?  140  SER A OG  1 
ATOM   881  N N   . CYS A 1 124 ? -5.009  -9.686  27.510  1.00 60.23  ?  141  CYS A N   1 
ATOM   882  C CA  . CYS A 1 124 ? -5.511  -9.590  26.149  1.00 60.60  ?  141  CYS A CA  1 
ATOM   883  C C   . CYS A 1 124 ? -6.640  -8.578  26.040  1.00 62.16  ?  141  CYS A C   1 
ATOM   884  O O   . CYS A 1 124 ? -7.346  -8.297  27.013  1.00 73.16  ?  141  CYS A O   1 
ATOM   885  C CB  . CYS A 1 124 ? -6.007  -10.951 25.653  1.00 69.60  ?  141  CYS A CB  1 
ATOM   886  S SG  . CYS A 1 124 ? -4.987  -12.350 26.151  1.00 68.85  ?  141  CYS A SG  1 
ATOM   887  N N   . ASN A 1 125 ? -6.802  -8.034  24.834  1.00 64.70  ?  142  ASN A N   1 
ATOM   888  C CA  . ASN A 1 125 ? -8.000  -7.319  24.441  1.00 67.35  ?  142  ASN A CA  1 
ATOM   889  C C   . ASN A 1 125 ? -8.775  -8.193  23.447  1.00 63.15  ?  142  ASN A C   1 
ATOM   890  O O   . ASN A 1 125 ? -8.682  -9.431  23.511  1.00 77.85  ?  142  ASN A O   1 
ATOM   891  C CB  . ASN A 1 125 ? -7.625  -5.929  23.922  1.00 67.65  ?  142  ASN A CB  1 
ATOM   892  C CG  . ASN A 1 125 ? -6.864  -5.945  22.595  1.00 78.51  ?  142  ASN A CG  1 
ATOM   893  O OD1 . ASN A 1 125 ? -6.656  -6.991  21.979  1.00 74.65  ?  142  ASN A OD1 1 
ATOM   894  N ND2 . ASN A 1 125 ? -6.452  -4.752  22.150  1.00 66.31  ?  142  ASN A ND2 1 
ATOM   895  N N   . GLN A 1 126 ? -9.520  -7.568  22.536  1.00 68.96  ?  143  GLN A N   1 
ATOM   896  C CA  . GLN A 1 126 ? -10.432 -8.341  21.700  1.00 72.13  ?  143  GLN A CA  1 
ATOM   897  C C   . GLN A 1 126 ? -9.703  -9.121  20.611  1.00 75.09  ?  143  GLN A C   1 
ATOM   898  O O   . GLN A 1 126 ? -10.150 -10.209 20.231  1.00 72.53  ?  143  GLN A O   1 
ATOM   899  C CB  . GLN A 1 126 ? -11.483 -7.420  21.081  1.00 65.26  ?  143  GLN A CB  1 
ATOM   900  C CG  . GLN A 1 126 ? -12.783 -8.121  20.722  1.00 63.48  ?  143  GLN A CG  1 
ATOM   901  C CD  . GLN A 1 126 ? -13.831 -7.164  20.193  1.00 79.24  ?  143  GLN A CD  1 
ATOM   902  O OE1 . GLN A 1 126 ? -13.526 -6.024  19.842  1.00 79.24  ?  143  GLN A OE1 1 
ATOM   903  N NE2 . GLN A 1 126 ? -15.077 -7.621  20.136  1.00 71.94  ?  143  GLN A NE2 1 
ATOM   904  N N   . THR A 1 127 ? -8.586  -8.597  20.099  1.00 73.79  ?  144  THR A N   1 
ATOM   905  C CA  . THR A 1 127 ? -7.934  -9.186  18.938  1.00 67.15  ?  144  THR A CA  1 
ATOM   906  C C   . THR A 1 127 ? -6.538  -9.735  19.198  1.00 69.14  ?  144  THR A C   1 
ATOM   907  O O   . THR A 1 127 ? -6.005  -10.435 18.329  1.00 71.53  ?  144  THR A O   1 
ATOM   908  C CB  . THR A 1 127 ? -7.846  -8.161  17.794  1.00 71.21  ?  144  THR A CB  1 
ATOM   909  O OG1 . THR A 1 127 ? -6.973  -7.090  18.173  1.00 81.91  ?  144  THR A OG1 1 
ATOM   910  C CG2 . THR A 1 127 ? -9.222  -7.598  17.472  1.00 76.81  ?  144  THR A CG2 1 
ATOM   911  N N   . THR A 1 128 ? -5.928  -9.449  20.346  1.00 82.67  ?  145  THR A N   1 
ATOM   912  C CA  . THR A 1 128 ? -4.555  -9.878  20.578  1.00 86.21  ?  145  THR A CA  1 
ATOM   913  C C   . THR A 1 128 ? -4.346  -10.196 22.050  1.00 80.13  ?  145  THR A C   1 
ATOM   914  O O   . THR A 1 128 ? -5.132  -9.799  22.913  1.00 77.43  ?  145  THR A O   1 
ATOM   915  C CB  . THR A 1 128 ? -3.547  -8.811  20.144  1.00 78.35  ?  145  THR A CB  1 
ATOM   916  O OG1 . THR A 1 128 ? -2.220  -9.334  20.262  1.00 97.93  ?  145  THR A OG1 1 
ATOM   917  C CG2 . THR A 1 128 ? -3.663  -7.605  21.040  1.00 74.97  ?  145  THR A CG2 1 
ATOM   918  N N   . CYS A 1 129 ? -3.257  -10.913 22.320  1.00 72.57  ?  146  CYS A N   1 
ATOM   919  C CA  . CYS A 1 129 ? -2.821  -11.247 23.668  1.00 73.88  ?  146  CYS A CA  1 
ATOM   920  C C   . CYS A 1 129 ? -1.370  -10.830 23.845  1.00 69.96  ?  146  CYS A C   1 
ATOM   921  O O   . CYS A 1 129 ? -0.539  -11.059 22.963  1.00 69.45  ?  146  CYS A O   1 
ATOM   922  C CB  . CYS A 1 129 ? -2.956  -12.749 23.953  1.00 68.49  ?  146  CYS A CB  1 
ATOM   923  S SG  . CYS A 1 129 ? -4.609  -13.305 24.401  1.00 100.36 ?  146  CYS A SG  1 
ATOM   924  N N   . GLN A 1 130 ? -1.067  -10.217 24.987  1.00 68.18  ?  147  GLN A N   1 
ATOM   925  C CA  . GLN A 1 130 ? 0.297   -9.893  25.354  1.00 68.88  ?  147  GLN A CA  1 
ATOM   926  C C   . GLN A 1 130 ? 0.770   -10.890 26.396  1.00 60.89  ?  147  GLN A C   1 
ATOM   927  O O   . GLN A 1 130 ? 0.113   -11.037 27.442  1.00 66.57  ?  147  GLN A O   1 
ATOM   928  C CB  . GLN A 1 130 ? 0.379   -8.473  25.900  1.00 62.98  ?  147  GLN A CB  1 
ATOM   929  C CG  . GLN A 1 130 ? 1.671   -8.148  26.621  1.00 80.50  ?  147  GLN A CG  1 
ATOM   930  C CD  . GLN A 1 130 ? 1.712   -6.712  27.103  1.00 92.41  ?  147  GLN A CD  1 
ATOM   931  O OE1 . GLN A 1 130 ? 1.261   -5.799  26.408  1.00 85.24  ?  147  GLN A OE1 1 
ATOM   932  N NE2 . GLN A 1 130 ? 2.245   -6.504  28.301  1.00 81.62  ?  147  GLN A NE2 1 
ATOM   933  N N   . PRO A 1 131 ? 1.863   -11.611 26.152  1.00 63.00  ?  148  PRO A N   1 
ATOM   934  C CA  . PRO A 1 131 ? 2.346   -12.585 27.135  1.00 63.58  ?  148  PRO A CA  1 
ATOM   935  C C   . PRO A 1 131 ? 3.338   -11.975 28.113  1.00 72.72  ?  148  PRO A C   1 
ATOM   936  O O   . PRO A 1 131 ? 4.178   -11.144 27.764  1.00 77.30  ?  148  PRO A O   1 
ATOM   937  C CB  . PRO A 1 131 ? 3.024   -13.654 26.262  1.00 57.96  ?  148  PRO A CB  1 
ATOM   938  C CG  . PRO A 1 131 ? 2.999   -13.117 24.829  1.00 59.41  ?  148  PRO A CG  1 
ATOM   939  C CD  . PRO A 1 131 ? 2.639   -11.671 24.906  1.00 74.70  ?  148  PRO A CD  1 
ATOM   940  N N   . THR A 1 132 ? 3.217   -12.399 29.366  1.00 65.35  ?  149  THR A N   1 
ATOM   941  C CA  . THR A 1 132 ? 4.141   -12.034 30.433  1.00 63.39  ?  149  THR A CA  1 
ATOM   942  C C   . THR A 1 132 ? 4.878   -13.302 30.842  1.00 68.69  ?  149  THR A C   1 
ATOM   943  O O   . THR A 1 132 ? 4.276   -14.214 31.418  1.00 65.51  ?  149  THR A O   1 
ATOM   944  C CB  . THR A 1 132 ? 3.403   -11.419 31.620  1.00 64.14  ?  149  THR A CB  1 
ATOM   945  O OG1 . THR A 1 132 ? 2.605   -10.318 31.169  1.00 72.93  ?  149  THR A OG1 1 
ATOM   946  C CG2 . THR A 1 132 ? 4.393   -10.926 32.665  1.00 60.27  ?  149  THR A CG2 1 
ATOM   947  N N   . VAL A 1 133 ? 6.169   -13.361 30.526  1.00 58.88  ?  150  VAL A N   1 
ATOM   948  C CA  . VAL A 1 133 ? 6.988   -14.536 30.791  1.00 60.57  ?  150  VAL A CA  1 
ATOM   949  C C   . VAL A 1 133 ? 7.600   -14.413 32.179  1.00 64.13  ?  150  VAL A C   1 
ATOM   950  O O   . VAL A 1 133 ? 8.245   -13.406 32.498  1.00 57.89  ?  150  VAL A O   1 
ATOM   951  C CB  . VAL A 1 133 ? 8.081   -14.700 29.721  1.00 63.69  ?  150  VAL A CB  1 
ATOM   952  C CG1 . VAL A 1 133 ? 9.017   -15.843 30.088  1.00 57.25  ?  150  VAL A CG1 1 
ATOM   953  C CG2 . VAL A 1 133 ? 7.454   -14.937 28.356  1.00 58.14  ?  150  VAL A CG2 1 
ATOM   954  N N   . PHE A 1 134 ? 7.386   -15.438 33.002  1.00 60.95  ?  151  PHE A N   1 
ATOM   955  C CA  . PHE A 1 134 ? 7.978   -15.562 34.325  1.00 55.57  ?  151  PHE A CA  1 
ATOM   956  C C   . PHE A 1 134 ? 9.029   -16.664 34.312  1.00 57.37  ?  151  PHE A C   1 
ATOM   957  O O   . PHE A 1 134 ? 8.827   -17.721 33.700  1.00 54.99  ?  151  PHE A O   1 
ATOM   958  C CB  . PHE A 1 134 ? 6.920   -15.890 35.383  1.00 52.02  ?  151  PHE A CB  1 
ATOM   959  C CG  . PHE A 1 134 ? 5.847   -14.852 35.518  1.00 54.13  ?  151  PHE A CG  1 
ATOM   960  C CD1 . PHE A 1 134 ? 6.011   -13.778 36.375  1.00 58.35  ?  151  PHE A CD1 1 
ATOM   961  C CD2 . PHE A 1 134 ? 4.667   -14.958 34.801  1.00 55.72  ?  151  PHE A CD2 1 
ATOM   962  C CE1 . PHE A 1 134 ? 5.025   -12.821 36.507  1.00 55.25  ?  151  PHE A CE1 1 
ATOM   963  C CE2 . PHE A 1 134 ? 3.675   -14.005 34.929  1.00 69.59  ?  151  PHE A CE2 1 
ATOM   964  C CZ  . PHE A 1 134 ? 3.855   -12.935 35.783  1.00 56.06  ?  151  PHE A CZ  1 
ATOM   965  N N   . LEU A 1 135 ? 10.140  -16.413 35.003  1.00 55.78  ?  152  LEU A N   1 
ATOM   966  C CA  . LEU A 1 135 ? 11.234  -17.371 35.127  1.00 54.40  ?  152  LEU A CA  1 
ATOM   967  C C   . LEU A 1 135 ? 11.767  -17.307 36.549  1.00 60.58  ?  152  LEU A C   1 
ATOM   968  O O   . LEU A 1 135 ? 12.190  -16.240 37.002  1.00 62.93  ?  152  LEU A O   1 
ATOM   969  C CB  . LEU A 1 135 ? 12.353  -17.068 34.127  1.00 55.07  ?  152  LEU A CB  1 
ATOM   970  C CG  . LEU A 1 135 ? 13.624  -17.908 34.271  1.00 55.32  ?  152  LEU A CG  1 
ATOM   971  C CD1 . LEU A 1 135 ? 13.372  -19.338 33.824  1.00 59.04  ?  152  LEU A CD1 1 
ATOM   972  C CD2 . LEU A 1 135 ? 14.781  -17.293 33.496  1.00 62.98  ?  152  LEU A CD2 1 
ATOM   973  N N   . MET A 1 136 ? 11.758  -18.440 37.248  1.00 62.89  ?  153  MET A N   1 
ATOM   974  C CA  . MET A 1 136 ? 12.248  -18.490 38.617  1.00 60.94  ?  153  MET A CA  1 
ATOM   975  C C   . MET A 1 136 ? 13.023  -19.779 38.836  1.00 68.75  ?  153  MET A C   1 
ATOM   976  O O   . MET A 1 136 ? 12.670  -20.827 38.291  1.00 61.34  ?  153  MET A O   1 
ATOM   977  C CB  . MET A 1 136 ? 11.100  -18.380 39.628  1.00 51.72  ?  153  MET A CB  1 
ATOM   978  C CG  . MET A 1 136 ? 10.010  -19.417 39.447  1.00 58.04  ?  153  MET A CG  1 
ATOM   979  S SD  . MET A 1 136 ? 8.573   -19.067 40.474  1.00 64.94  ?  153  MET A SD  1 
ATOM   980  C CE  . MET A 1 136 ? 7.288   -19.007 39.228  1.00 51.32  ?  153  MET A CE  1 
ATOM   981  N N   . GLY A 1 137 ? 14.082  -19.690 39.635  1.00 63.30  ?  154  GLY A N   1 
ATOM   982  C CA  . GLY A 1 137 ? 14.934  -20.829 39.889  1.00 54.02  ?  154  GLY A CA  1 
ATOM   983  C C   . GLY A 1 137 ? 15.762  -20.687 41.150  1.00 61.15  ?  154  GLY A C   1 
ATOM   984  O O   . GLY A 1 137 ? 15.636  -19.713 41.895  1.00 59.93  ?  154  GLY A O   1 
ATOM   985  N N   . PRO A 1 138 ? 16.618  -21.668 41.420  1.00 67.24  ?  155  PRO A N   1 
ATOM   986  C CA  . PRO A 1 138 ? 17.477  -21.592 42.606  1.00 68.99  ?  155  PRO A CA  1 
ATOM   987  C C   . PRO A 1 138 ? 18.477  -20.451 42.494  1.00 66.68  ?  155  PRO A C   1 
ATOM   988  O O   . PRO A 1 138 ? 18.818  -19.990 41.404  1.00 62.87  ?  155  PRO A O   1 
ATOM   989  C CB  . PRO A 1 138 ? 18.189  -22.951 42.625  1.00 59.15  ?  155  PRO A CB  1 
ATOM   990  C CG  . PRO A 1 138 ? 17.348  -23.841 41.761  1.00 54.30  ?  155  PRO A CG  1 
ATOM   991  C CD  . PRO A 1 138 ? 16.771  -22.948 40.709  1.00 60.82  ?  155  PRO A CD  1 
ATOM   992  N N   . ILE A 1 139 ? 18.945  -19.993 43.658  1.00 72.05  ?  156  ILE A N   1 
ATOM   993  C CA  . ILE A 1 139 ? 19.924  -18.909 43.696  1.00 65.29  ?  156  ILE A CA  1 
ATOM   994  C C   . ILE A 1 139 ? 21.194  -19.311 42.956  1.00 75.02  ?  156  ILE A C   1 
ATOM   995  O O   . ILE A 1 139 ? 21.790  -18.506 42.227  1.00 65.92  ?  156  ILE A O   1 
ATOM   996  C CB  . ILE A 1 139 ? 20.216  -18.509 45.155  1.00 60.16  ?  156  ILE A CB  1 
ATOM   997  C CG1 . ILE A 1 139 ? 18.961  -17.930 45.809  1.00 69.12  ?  156  ILE A CG1 1 
ATOM   998  C CG2 . ILE A 1 139 ? 21.354  -17.507 45.225  1.00 70.23  ?  156  ILE A CG2 1 
ATOM   999  C CD1 . ILE A 1 139 ? 18.524  -16.610 45.220  1.00 67.72  ?  156  ILE A CD1 1 
ATOM   1000 N N   . GLN A 1 140 ? 21.610  -20.571 43.106  1.00 74.54  ?  157  GLN A N   1 
ATOM   1001 C CA  . GLN A 1 140 ? 22.854  -21.033 42.502  1.00 66.58  ?  157  GLN A CA  1 
ATOM   1002 C C   . GLN A 1 140 ? 22.831  -20.956 40.979  1.00 68.18  ?  157  GLN A C   1 
ATOM   1003 O O   . GLN A 1 140 ? 23.896  -20.848 40.361  1.00 65.13  ?  157  GLN A O   1 
ATOM   1004 C CB  . GLN A 1 140 ? 23.148  -22.465 42.960  1.00 75.36  ?  157  GLN A CB  1 
ATOM   1005 C CG  . GLN A 1 140 ? 24.489  -23.024 42.499  1.00 84.08  ?  157  GLN A CG  1 
ATOM   1006 C CD  . GLN A 1 140 ? 25.681  -22.325 43.134  1.00 95.19  ?  157  GLN A CD  1 
ATOM   1007 O OE1 . GLN A 1 140 ? 25.531  -21.510 44.045  1.00 93.42  ?  157  GLN A OE1 1 
ATOM   1008 N NE2 . GLN A 1 140 ? 26.876  -22.649 42.654  1.00 101.73 ?  157  GLN A NE2 1 
ATOM   1009 N N   . THR A 1 141 ? 21.648  -20.989 40.357  1.00 67.28  ?  158  THR A N   1 
ATOM   1010 C CA  . THR A 1 141 ? 21.582  -20.852 38.906  1.00 66.03  ?  158  THR A CA  1 
ATOM   1011 C C   . THR A 1 141 ? 22.057  -19.484 38.432  1.00 73.10  ?  158  THR A C   1 
ATOM   1012 O O   . THR A 1 141 ? 22.302  -19.313 37.232  1.00 70.34  ?  158  THR A O   1 
ATOM   1013 C CB  . THR A 1 141 ? 20.158  -21.117 38.402  1.00 58.83  ?  158  THR A CB  1 
ATOM   1014 O OG1 . THR A 1 141 ? 20.215  -21.660 37.078  1.00 85.07  ?  158  THR A OG1 1 
ATOM   1015 C CG2 . THR A 1 141 ? 19.342  -19.834 38.366  1.00 62.24  ?  158  THR A CG2 1 
ATOM   1016 N N   . CYS A 1 142 ? 22.206  -18.516 39.340  1.00 76.42  ?  159  CYS A N   1 
ATOM   1017 C CA  . CYS A 1 142 ? 22.833  -17.244 39.001  1.00 77.32  ?  159  CYS A CA  1 
ATOM   1018 C C   . CYS A 1 142 ? 24.305  -17.397 38.637  1.00 74.39  ?  159  CYS A C   1 
ATOM   1019 O O   . CYS A 1 142 ? 24.911  -16.431 38.162  1.00 80.75  ?  159  CYS A O   1 
ATOM   1020 C CB  . CYS A 1 142 ? 22.688  -16.266 40.168  1.00 72.50  ?  159  CYS A CB  1 
ATOM   1021 S SG  . CYS A 1 142 ? 21.007  -15.657 40.422  1.00 85.65  ?  159  CYS A SG  1 
ATOM   1022 N N   . ILE A 1 143 ? 24.888  -18.579 38.848  1.00 81.38  ?  160  ILE A N   1 
ATOM   1023 C CA  . ILE A 1 143 ? 26.276  -18.852 38.510  1.00 76.90  ?  160  ILE A CA  1 
ATOM   1024 C C   . ILE A 1 143 ? 26.399  -19.949 37.461  1.00 75.37  ?  160  ILE A C   1 
ATOM   1025 O O   . ILE A 1 143 ? 27.215  -19.843 36.538  1.00 78.91  ?  160  ILE A O   1 
ATOM   1026 C CB  . ILE A 1 143 ? 27.091  -19.213 39.773  1.00 71.98  ?  160  ILE A CB  1 
ATOM   1027 C CG1 . ILE A 1 143 ? 27.171  -18.015 40.720  1.00 71.10  ?  160  ILE A CG1 1 
ATOM   1028 C CG2 . ILE A 1 143 ? 28.483  -19.702 39.401  1.00 68.49  ?  160  ILE A CG2 1 
ATOM   1029 C CD1 . ILE A 1 143 ? 27.896  -18.308 42.013  1.00 82.23  ?  160  ILE A CD1 1 
ATOM   1030 N N   . THR A 1 144 ? 25.589  -21.004 37.572  1.00 72.23  ?  161  THR A N   1 
ATOM   1031 C CA  . THR A 1 144 ? 25.677  -22.124 36.643  1.00 73.58  ?  161  THR A CA  1 
ATOM   1032 C C   . THR A 1 144 ? 25.104  -21.793 35.269  1.00 66.82  ?  161  THR A C   1 
ATOM   1033 O O   . THR A 1 144 ? 25.521  -22.394 34.273  1.00 85.39  ?  161  THR A O   1 
ATOM   1034 C CB  . THR A 1 144 ? 24.954  -23.347 37.220  1.00 71.12  ?  161  THR A CB  1 
ATOM   1035 O OG1 . THR A 1 144 ? 23.538  -23.144 37.163  1.00 80.57  ?  161  THR A OG1 1 
ATOM   1036 C CG2 . THR A 1 144 ? 25.363  -23.571 38.672  1.00 65.44  ?  161  THR A CG2 1 
ATOM   1037 N N   . THR A 1 145 ? 24.166  -20.849 35.189  1.00 78.18  ?  162  THR A N   1 
ATOM   1038 C CA  . THR A 1 145 ? 23.535  -20.475 33.927  1.00 78.32  ?  162  THR A CA  1 
ATOM   1039 C C   . THR A 1 145 ? 24.073  -19.162 33.370  1.00 89.05  ?  162  THR A C   1 
ATOM   1040 O O   . THR A 1 145 ? 24.494  -19.110 32.210  1.00 89.61  ?  162  THR A O   1 
ATOM   1041 C CB  . THR A 1 145 ? 22.013  -20.380 34.106  1.00 80.49  ?  162  THR A CB  1 
ATOM   1042 O OG1 . THR A 1 145 ? 21.544  -21.525 34.829  1.00 81.36  ?  162  THR A OG1 1 
ATOM   1043 C CG2 . THR A 1 145 ? 21.316  -20.330 32.751  1.00 81.81  ?  162  THR A CG2 1 
ATOM   1044 N N   . LYS A 1 146 ? 24.050  -18.096 34.174  1.00 87.65  ?  163  LYS A N   1 
ATOM   1045 C CA  . LYS A 1 146 ? 24.632  -16.801 33.827  1.00 92.97  ?  163  LYS A CA  1 
ATOM   1046 C C   . LYS A 1 146 ? 23.950  -16.158 32.622  1.00 89.05  ?  163  LYS A C   1 
ATOM   1047 O O   . LYS A 1 146 ? 23.401  -15.057 32.731  1.00 79.62  ?  163  LYS A O   1 
ATOM   1048 C CB  . LYS A 1 146 ? 26.135  -16.945 33.567  1.00 95.17  ?  163  LYS A CB  1 
ATOM   1049 C CG  . LYS A 1 146 ? 26.941  -15.677 33.799  1.00 105.40 ?  163  LYS A CG  1 
ATOM   1050 C CD  . LYS A 1 146 ? 27.306  -15.515 35.266  1.00 110.58 ?  163  LYS A CD  1 
ATOM   1051 C CE  . LYS A 1 146 ? 28.258  -14.347 35.472  1.00 118.45 ?  163  LYS A CE  1 
ATOM   1052 N NZ  . LYS A 1 146 ? 28.808  -14.312 36.857  1.00 114.53 1  163  LYS A NZ  1 
ATOM   1053 N N   . SER A 1 147 ? 23.986  -16.826 31.470  1.00 97.59  ?  164  SER A N   1 
ATOM   1054 C CA  . SER A 1 147 ? 23.427  -16.290 30.238  1.00 95.37  ?  164  SER A CA  1 
ATOM   1055 C C   . SER A 1 147 ? 22.661  -17.379 29.504  1.00 103.32 ?  164  SER A C   1 
ATOM   1056 O O   . SER A 1 147 ? 23.121  -18.521 29.424  1.00 98.85  ?  164  SER A O   1 
ATOM   1057 C CB  . SER A 1 147 ? 24.528  -15.725 29.330  1.00 92.04  ?  164  SER A CB  1 
ATOM   1058 O OG  . SER A 1 147 ? 24.072  -15.590 27.995  1.00 95.08  ?  164  SER A OG  1 
ATOM   1059 N N   . CYS A 1 148 ? 21.494  -17.024 28.967  1.00 108.25 ?  165  CYS A N   1 
ATOM   1060 C CA  . CYS A 1 148 ? 20.707  -17.973 28.187  1.00 103.70 ?  165  CYS A CA  1 
ATOM   1061 C C   . CYS A 1 148 ? 19.825  -17.225 27.193  1.00 101.96 ?  165  CYS A C   1 
ATOM   1062 O O   . CYS A 1 148 ? 19.824  -15.993 27.129  1.00 103.23 ?  165  CYS A O   1 
ATOM   1063 C CB  . CYS A 1 148 ? 19.848  -18.871 29.079  1.00 100.58 ?  165  CYS A CB  1 
ATOM   1064 S SG  . CYS A 1 148 ? 18.723  -19.890 28.100  1.00 147.24 ?  165  CYS A SG  1 
ATOM   1065 N N   . LEU A 1 149 ? 19.041  -17.994 26.435  1.00 90.09  ?  166  LEU A N   1 
ATOM   1066 C CA  . LEU A 1 149 ? 18.158  -17.439 25.412  1.00 90.04  ?  166  LEU A CA  1 
ATOM   1067 C C   . LEU A 1 149 ? 16.886  -18.277 25.363  1.00 89.50  ?  166  LEU A C   1 
ATOM   1068 O O   . LEU A 1 149 ? 16.904  -19.400 24.851  1.00 92.10  ?  166  LEU A O   1 
ATOM   1069 C CB  . LEU A 1 149 ? 18.850  -17.419 24.052  1.00 77.77  ?  166  LEU A CB  1 
ATOM   1070 C CG  . LEU A 1 149 ? 18.340  -16.407 23.026  1.00 79.75  ?  166  LEU A CG  1 
ATOM   1071 C CD1 . LEU A 1 149 ? 18.841  -15.012 23.365  1.00 79.37  ?  166  LEU A CD1 1 
ATOM   1072 C CD2 . LEU A 1 149 ? 18.756  -16.807 21.620  1.00 78.09  ?  166  LEU A CD2 1 
ATOM   1073 N N   . LEU A 1 150 ? 15.793  -17.733 25.889  1.00 85.93  ?  167  LEU A N   1 
ATOM   1074 C CA  . LEU A 1 150 ? 14.477  -18.349 25.798  1.00 76.95  ?  167  LEU A CA  1 
ATOM   1075 C C   . LEU A 1 150 ? 13.794  -17.956 24.491  1.00 80.98  ?  167  LEU A C   1 
ATOM   1076 O O   . LEU A 1 150 ? 14.185  -17.000 23.820  1.00 87.99  ?  167  LEU A O   1 
ATOM   1077 C CB  . LEU A 1 150 ? 13.599  -17.931 26.980  1.00 75.03  ?  167  LEU A CB  1 
ATOM   1078 C CG  . LEU A 1 150 ? 14.039  -18.312 28.393  1.00 78.43  ?  167  LEU A CG  1 
ATOM   1079 C CD1 . LEU A 1 150 ? 13.122  -17.664 29.419  1.00 70.82  ?  167  LEU A CD1 1 
ATOM   1080 C CD2 . LEU A 1 150 ? 14.047  -19.820 28.562  1.00 83.02  ?  167  LEU A CD2 1 
ATOM   1081 N N   . GLY A 1 151 ? 12.743  -18.696 24.148  1.00 71.55  ?  168  GLY A N   1 
ATOM   1082 C CA  . GLY A 1 151 ? 11.993  -18.405 22.941  1.00 67.23  ?  168  GLY A CA  1 
ATOM   1083 C C   . GLY A 1 151 ? 10.496  -18.578 23.094  1.00 79.63  ?  168  GLY A C   1 
ATOM   1084 O O   . GLY A 1 151 ? 10.038  -19.538 23.722  1.00 65.67  ?  168  GLY A O   1 
ATOM   1085 N N   . LEU A 1 152 ? 9.721   -17.656 22.526  1.00 79.39  ?  169  LEU A N   1 
ATOM   1086 C CA  . LEU A 1 152 ? 8.265   -17.755 22.553  1.00 70.20  ?  169  LEU A CA  1 
ATOM   1087 C C   . LEU A 1 152 ? 7.720   -17.132 21.279  1.00 78.20  ?  169  LEU A C   1 
ATOM   1088 O O   . LEU A 1 152 ? 7.899   -15.931 21.049  1.00 86.61  ?  169  LEU A O   1 
ATOM   1089 C CB  . LEU A 1 152 ? 7.682   -17.063 23.788  1.00 72.91  ?  169  LEU A CB  1 
ATOM   1090 C CG  . LEU A 1 152 ? 6.188   -17.290 24.033  1.00 67.73  ?  169  LEU A CG  1 
ATOM   1091 C CD1 . LEU A 1 152 ? 5.891   -18.766 24.259  1.00 66.49  ?  169  LEU A CD1 1 
ATOM   1092 C CD2 . LEU A 1 152 ? 5.695   -16.457 25.207  1.00 66.95  ?  169  LEU A CD2 1 
ATOM   1093 N N   . GLY A 1 153 ? 7.066   -17.948 20.456  1.00 84.74  ?  170  GLY A N   1 
ATOM   1094 C CA  . GLY A 1 153 ? 6.521   -17.448 19.205  1.00 83.57  ?  170  GLY A CA  1 
ATOM   1095 C C   . GLY A 1 153 ? 7.621   -16.927 18.304  1.00 86.78  ?  170  GLY A C   1 
ATOM   1096 O O   . GLY A 1 153 ? 8.610   -17.615 18.025  1.00 93.29  ?  170  GLY A O   1 
ATOM   1097 N N   . ASP A 1 154 ? 7.452   -15.690 17.843  1.00 91.13  ?  171  ASP A N   1 
ATOM   1098 C CA  . ASP A 1 154 ? 8.439   -15.017 17.011  1.00 93.81  ?  171  ASP A CA  1 
ATOM   1099 C C   . ASP A 1 154 ? 9.390   -14.147 17.824  1.00 96.70  ?  171  ASP A C   1 
ATOM   1100 O O   . ASP A 1 154 ? 10.095  -13.308 17.249  1.00 95.93  ?  171  ASP A O   1 
ATOM   1101 C CB  . ASP A 1 154 ? 7.735   -14.179 15.943  1.00 97.28  ?  171  ASP A CB  1 
ATOM   1102 C CG  . ASP A 1 154 ? 6.835   -13.112 16.539  1.00 104.03 ?  171  ASP A CG  1 
ATOM   1103 O OD1 . ASP A 1 154 ? 7.126   -11.912 16.351  1.00 109.38 ?  171  ASP A OD1 1 
ATOM   1104 O OD2 . ASP A 1 154 ? 5.844   -13.476 17.209  1.00 110.14 -1 171  ASP A OD2 1 
ATOM   1105 N N   . GLN A 1 155 ? 9.430   -14.331 19.143  1.00 95.29  ?  172  GLN A N   1 
ATOM   1106 C CA  . GLN A 1 155 ? 10.233  -13.502 20.029  1.00 85.73  ?  172  GLN A CA  1 
ATOM   1107 C C   . GLN A 1 155 ? 11.296  -14.342 20.724  1.00 82.70  ?  172  GLN A C   1 
ATOM   1108 O O   . GLN A 1 155 ? 11.049  -15.493 21.101  1.00 92.14  ?  172  GLN A O   1 
ATOM   1109 C CB  . GLN A 1 155 ? 9.353   -12.807 21.076  1.00 78.92  ?  172  GLN A CB  1 
ATOM   1110 C CG  . GLN A 1 155 ? 8.323   -11.853 20.492  1.00 78.26  ?  172  GLN A CG  1 
ATOM   1111 C CD  . GLN A 1 155 ? 8.947   -10.596 19.916  1.00 89.88  ?  172  GLN A CD  1 
ATOM   1112 O OE1 . GLN A 1 155 ? 9.962   -10.108 20.414  1.00 101.41 ?  172  GLN A OE1 1 
ATOM   1113 N NE2 . GLN A 1 155 ? 8.344   -10.067 18.858  1.00 93.57  ?  172  GLN A NE2 1 
ATOM   1114 N N   . ARG A 1 156 ? 12.481  -13.759 20.879  1.00 81.44  ?  173  ARG A N   1 
ATOM   1115 C CA  . ARG A 1 156 ? 13.557  -14.334 21.669  1.00 80.89  ?  173  ARG A CA  1 
ATOM   1116 C C   . ARG A 1 156 ? 13.774  -13.487 22.915  1.00 89.37  ?  173  ARG A C   1 
ATOM   1117 O O   . ARG A 1 156 ? 13.490  -12.285 22.926  1.00 98.09  ?  173  ARG A O   1 
ATOM   1118 C CB  . ARG A 1 156 ? 14.857  -14.422 20.864  1.00 84.68  ?  173  ARG A CB  1 
ATOM   1119 C CG  . ARG A 1 156 ? 14.808  -15.391 19.695  1.00 90.09  ?  173  ARG A CG  1 
ATOM   1120 C CD  . ARG A 1 156 ? 16.161  -15.477 19.009  1.00 103.35 ?  173  ARG A CD  1 
ATOM   1121 N NE  . ARG A 1 156 ? 16.122  -16.297 17.802  1.00 129.27 ?  173  ARG A NE  1 
ATOM   1122 C CZ  . ARG A 1 156 ? 17.153  -16.461 16.980  1.00 133.13 ?  173  ARG A CZ  1 
ATOM   1123 N NH1 . ARG A 1 156 ? 18.306  -15.858 17.236  1.00 127.89 1  173  ARG A NH1 1 
ATOM   1124 N NH2 . ARG A 1 156 ? 17.033  -17.224 15.902  1.00 132.98 ?  173  ARG A NH2 1 
ATOM   1125 N N   . ILE A 1 157 ? 14.282  -14.121 23.968  1.00 77.70  ?  174  ILE A N   1 
ATOM   1126 C CA  . ILE A 1 157 ? 14.422  -13.496 25.278  1.00 76.97  ?  174  ILE A CA  1 
ATOM   1127 C C   . ILE A 1 157 ? 15.834  -13.768 25.779  1.00 83.11  ?  174  ILE A C   1 
ATOM   1128 O O   . ILE A 1 157 ? 16.157  -14.903 26.146  1.00 81.33  ?  174  ILE A O   1 
ATOM   1129 C CB  . ILE A 1 157 ? 13.380  -14.016 26.277  1.00 66.88  ?  174  ILE A CB  1 
ATOM   1130 C CG1 . ILE A 1 157 ? 11.968  -13.630 25.829  1.00 74.62  ?  174  ILE A CG1 1 
ATOM   1131 C CG2 . ILE A 1 157 ? 13.665  -13.488 27.670  1.00 72.42  ?  174  ILE A CG2 1 
ATOM   1132 C CD1 . ILE A 1 157 ? 10.869  -14.269 26.651  1.00 74.99  ?  174  ILE A CD1 1 
ATOM   1133 N N   . GLN A 1 158 ? 16.674  -12.736 25.795  1.00 75.61  ?  175  GLN A N   1 
ATOM   1134 C CA  . GLN A 1 158 ? 18.028  -12.857 26.324  1.00 76.17  ?  175  GLN A CA  1 
ATOM   1135 C C   . GLN A 1 158 ? 17.964  -12.824 27.847  1.00 85.66  ?  175  GLN A C   1 
ATOM   1136 O O   . GLN A 1 158 ? 17.591  -11.805 28.437  1.00 87.78  ?  175  GLN A O   1 
ATOM   1137 C CB  . GLN A 1 158 ? 18.913  -11.739 25.779  1.00 78.89  ?  175  GLN A CB  1 
ATOM   1138 C CG  . GLN A 1 158 ? 20.222  -11.535 26.533  1.00 87.94  ?  175  GLN A CG  1 
ATOM   1139 C CD  . GLN A 1 158 ? 21.214  -12.667 26.330  1.00 96.36  ?  175  GLN A CD  1 
ATOM   1140 O OE1 . GLN A 1 158 ? 21.001  -13.561 25.511  1.00 100.55 ?  175  GLN A OE1 1 
ATOM   1141 N NE2 . GLN A 1 158 ? 22.312  -12.630 27.077  1.00 96.63  ?  175  GLN A NE2 1 
ATOM   1142 N N   . VAL A 1 159 ? 18.321  -13.935 28.486  1.00 81.29  ?  176  VAL A N   1 
ATOM   1143 C CA  . VAL A 1 159 ? 18.263  -14.068 29.937  1.00 81.45  ?  176  VAL A CA  1 
ATOM   1144 C C   . VAL A 1 159 ? 19.648  -13.788 30.499  1.00 77.71  ?  176  VAL A C   1 
ATOM   1145 O O   . VAL A 1 159 ? 20.612  -14.496 30.175  1.00 85.46  ?  176  VAL A O   1 
ATOM   1146 C CB  . VAL A 1 159 ? 17.773  -15.464 30.353  1.00 78.94  ?  176  VAL A CB  1 
ATOM   1147 C CG1 . VAL A 1 159 ? 17.777  -15.598 31.869  1.00 76.01  ?  176  VAL A CG1 1 
ATOM   1148 C CG2 . VAL A 1 159 ? 16.386  -15.732 29.791  1.00 65.91  ?  176  VAL A CG2 1 
ATOM   1149 N N   . ASN A 1 160 ? 19.742  -12.763 31.345  1.00 71.04  ?  177  ASN A N   1 
ATOM   1150 C CA  . ASN A 1 160 ? 20.983  -12.361 31.992  1.00 82.25  ?  177  ASN A CA  1 
ATOM   1151 C C   . ASN A 1 160 ? 20.822  -12.456 33.503  1.00 72.67  ?  177  ASN A C   1 
ATOM   1152 O O   . ASN A 1 160 ? 19.838  -11.959 34.059  1.00 68.17  ?  177  ASN A O   1 
ATOM   1153 C CB  . ASN A 1 160 ? 21.374  -10.931 31.602  1.00 84.77  ?  177  ASN A CB  1 
ATOM   1154 C CG  . ASN A 1 160 ? 21.714  -10.796 30.132  1.00 93.75  ?  177  ASN A CG  1 
ATOM   1155 O OD1 . ASN A 1 160 ? 22.272  -11.711 29.526  1.00 102.35 ?  177  ASN A OD1 1 
ATOM   1156 N ND2 . ASN A 1 160 ? 21.383  -9.649  29.551  1.00 94.97  ?  177  ASN A ND2 1 
ATOM   1157 N N   . TYR A 1 161 ? 21.790  -13.091 34.159  1.00 70.30  ?  178  TYR A N   1 
ATOM   1158 C CA  . TYR A 1 161 ? 21.847  -13.162 35.614  1.00 68.76  ?  178  TYR A CA  1 
ATOM   1159 C C   . TYR A 1 161 ? 22.915  -12.190 36.101  1.00 74.49  ?  178  TYR A C   1 
ATOM   1160 O O   . TYR A 1 161 ? 24.097  -12.352 35.779  1.00 78.60  ?  178  TYR A O   1 
ATOM   1161 C CB  . TYR A 1 161 ? 22.160  -14.583 36.086  1.00 80.75  ?  178  TYR A CB  1 
ATOM   1162 C CG  . TYR A 1 161 ? 21.104  -15.614 35.742  1.00 72.61  ?  178  TYR A CG  1 
ATOM   1163 C CD1 . TYR A 1 161 ? 21.090  -16.238 34.502  1.00 70.42  ?  178  TYR A CD1 1 
ATOM   1164 C CD2 . TYR A 1 161 ? 20.132  -15.974 36.665  1.00 69.21  ?  178  TYR A CD2 1 
ATOM   1165 C CE1 . TYR A 1 161 ? 20.131  -17.184 34.187  1.00 77.05  ?  178  TYR A CE1 1 
ATOM   1166 C CE2 . TYR A 1 161 ? 19.168  -16.917 36.358  1.00 59.46  ?  178  TYR A CE2 1 
ATOM   1167 C CZ  . TYR A 1 161 ? 19.172  -17.519 35.119  1.00 74.19  ?  178  TYR A CZ  1 
ATOM   1168 O OH  . TYR A 1 161 ? 18.215  -18.460 34.813  1.00 67.65  ?  178  TYR A OH  1 
ATOM   1169 N N   . GLU A 1 162 ? 22.503  -11.185 36.871  1.00 78.82  ?  179  GLU A N   1 
ATOM   1170 C CA  . GLU A 1 162 ? 23.409  -10.144 37.341  1.00 78.64  ?  179  GLU A CA  1 
ATOM   1171 C C   . GLU A 1 162 ? 23.219  -9.923  38.833  1.00 74.52  ?  179  GLU A C   1 
ATOM   1172 O O   . GLU A 1 162 ? 22.084  -9.818  39.309  1.00 73.85  ?  179  GLU A O   1 
ATOM   1173 C CB  . GLU A 1 162 ? 23.185  -8.833  36.580  1.00 79.19  ?  179  GLU A CB  1 
ATOM   1174 C CG  . GLU A 1 162 ? 23.611  -8.880  35.121  1.00 98.37  ?  179  GLU A CG  1 
ATOM   1175 C CD  . GLU A 1 162 ? 23.675  -7.503  34.492  1.00 107.13 ?  179  GLU A CD  1 
ATOM   1176 O OE1 . GLU A 1 162 ? 23.281  -7.364  33.314  1.00 105.60 ?  179  GLU A OE1 1 
ATOM   1177 O OE2 . GLU A 1 162 ? 24.114  -6.558  35.181  1.00 108.56 -1 179  GLU A OE2 1 
ATOM   1178 N N   . LYS A 1 163 ? 24.330  -9.850  39.565  1.00 67.49  ?  180  LYS A N   1 
ATOM   1179 C CA  . LYS A 1 163 ? 24.275  -9.557  40.991  1.00 71.43  ?  180  LYS A CA  1 
ATOM   1180 C C   . LYS A 1 163 ? 23.739  -8.147  41.212  1.00 80.17  ?  180  LYS A C   1 
ATOM   1181 O O   . LYS A 1 163 ? 24.195  -7.191  40.577  1.00 75.73  ?  180  LYS A O   1 
ATOM   1182 C CB  . LYS A 1 163 ? 25.658  -9.708  41.622  1.00 69.22  ?  180  LYS A CB  1 
ATOM   1183 C CG  . LYS A 1 163 ? 26.163  -11.142 41.693  1.00 72.18  ?  180  LYS A CG  1 
ATOM   1184 C CD  . LYS A 1 163 ? 27.429  -11.240 42.531  1.00 83.22  ?  180  LYS A CD  1 
ATOM   1185 C CE  . LYS A 1 163 ? 27.908  -12.678 42.647  1.00 92.78  ?  180  LYS A CE  1 
ATOM   1186 N NZ  . LYS A 1 163 ? 29.124  -12.785 43.500  1.00 94.23  1  180  LYS A NZ  1 
ATOM   1187 N N   . THR A 1 164 ? 22.772  -8.018  42.119  1.00 76.84  ?  181  THR A N   1 
ATOM   1188 C CA  . THR A 1 164 ? 22.065  -6.765  42.333  1.00 62.44  ?  181  THR A CA  1 
ATOM   1189 C C   . THR A 1 164 ? 21.915  -6.518  43.827  1.00 79.81  ?  181  THR A C   1 
ATOM   1190 O O   . THR A 1 164 ? 21.766  -7.455  44.615  1.00 74.91  ?  181  THR A O   1 
ATOM   1191 C CB  . THR A 1 164 ? 20.688  -6.786  41.643  1.00 72.85  ?  181  THR A CB  1 
ATOM   1192 O OG1 . THR A 1 164 ? 20.856  -7.084  40.251  1.00 79.21  ?  181  THR A OG1 1 
ATOM   1193 C CG2 . THR A 1 164 ? 19.979  -5.446  41.782  1.00 66.00  ?  181  THR A CG2 1 
ATOM   1194 N N   . TYR A 1 165 ? 21.968  -5.243  44.211  1.00 85.54  ?  182  TYR A N   1 
ATOM   1195 C CA  . TYR A 1 165 ? 21.814  -4.861  45.608  1.00 76.57  ?  182  TYR A CA  1 
ATOM   1196 C C   . TYR A 1 165 ? 20.342  -4.813  45.998  1.00 78.39  ?  182  TYR A C   1 
ATOM   1197 O O   . TYR A 1 165 ? 19.484  -4.432  45.195  1.00 80.33  ?  182  TYR A O   1 
ATOM   1198 C CB  . TYR A 1 165 ? 22.452  -3.497  45.867  1.00 88.20  ?  182  TYR A CB  1 
ATOM   1199 C CG  . TYR A 1 165 ? 23.913  -3.410  45.500  1.00 97.69  ?  182  TYR A CG  1 
ATOM   1200 C CD1 . TYR A 1 165 ? 24.864  -4.169  46.170  1.00 96.51  ?  182  TYR A CD1 1 
ATOM   1201 C CD2 . TYR A 1 165 ? 24.345  -2.553  44.495  1.00 98.26  ?  182  TYR A CD2 1 
ATOM   1202 C CE1 . TYR A 1 165 ? 26.202  -4.088  45.843  1.00 96.29  ?  182  TYR A CE1 1 
ATOM   1203 C CE2 . TYR A 1 165 ? 25.682  -2.463  44.160  1.00 105.45 ?  182  TYR A CE2 1 
ATOM   1204 C CZ  . TYR A 1 165 ? 26.606  -3.233  44.837  1.00 112.75 ?  182  TYR A CZ  1 
ATOM   1205 O OH  . TYR A 1 165 ? 27.938  -3.147  44.506  1.00 108.25 ?  182  TYR A OH  1 
ATOM   1206 N N   . CYS A 1 166 ? 20.060  -5.196  47.244  1.00 74.30  ?  183  CYS A N   1 
ATOM   1207 C CA  . CYS A 1 166 ? 18.725  -5.094  47.830  1.00 85.21  ?  183  CYS A CA  1 
ATOM   1208 C C   . CYS A 1 166 ? 17.676  -5.784  46.960  1.00 76.98  ?  183  CYS A C   1 
ATOM   1209 O O   . CYS A 1 166 ? 16.659  -5.200  46.581  1.00 83.59  ?  183  CYS A O   1 
ATOM   1210 C CB  . CYS A 1 166 ? 18.353  -3.632  48.080  1.00 78.38  ?  183  CYS A CB  1 
ATOM   1211 S SG  . CYS A 1 166 ? 17.375  -3.365  49.575  1.00 89.94  ?  183  CYS A SG  1 
ATOM   1212 N N   . VAL A 1 167 ? 17.933  -7.054  46.648  1.00 71.45  ?  184  VAL A N   1 
ATOM   1213 C CA  . VAL A 1 167 ? 17.009  -7.814  45.815  1.00 71.34  ?  184  VAL A CA  1 
ATOM   1214 C C   . VAL A 1 167 ? 15.759  -8.248  46.569  1.00 63.72  ?  184  VAL A C   1 
ATOM   1215 O O   . VAL A 1 167 ? 14.746  -8.572  45.934  1.00 63.33  ?  184  VAL A O   1 
ATOM   1216 C CB  . VAL A 1 167 ? 17.710  -9.048  45.228  1.00 77.47  ?  184  VAL A CB  1 
ATOM   1217 C CG1 . VAL A 1 167 ? 18.726  -8.627  44.184  1.00 74.27  ?  184  VAL A CG1 1 
ATOM   1218 C CG2 . VAL A 1 167 ? 18.386  -9.839  46.336  1.00 67.82  ?  184  VAL A CG2 1 
ATOM   1219 N N   . SER A 1 168 ? 15.795  -8.260  47.902  1.00 71.04  ?  185  SER A N   1 
ATOM   1220 C CA  . SER A 1 168 ? 14.688  -8.760  48.704  1.00 66.64  ?  185  SER A CA  1 
ATOM   1221 C C   . SER A 1 168 ? 13.987  -7.687  49.524  1.00 70.34  ?  185  SER A C   1 
ATOM   1222 O O   . SER A 1 168 ? 12.918  -7.961  50.082  1.00 62.52  ?  185  SER A O   1 
ATOM   1223 C CB  . SER A 1 168 ? 15.178  -9.870  49.647  1.00 61.03  ?  185  SER A CB  1 
ATOM   1224 O OG  . SER A 1 168 ? 15.888  -10.869 48.933  1.00 68.68  ?  185  SER A OG  1 
ATOM   1225 N N   . GLY A 1 169 ? 14.548  -6.486  49.616  1.00 70.47  ?  186  GLY A N   1 
ATOM   1226 C CA  . GLY A 1 169 ? 13.972  -5.418  50.412  1.00 79.96  ?  186  GLY A CA  1 
ATOM   1227 C C   . GLY A 1 169 ? 13.785  -4.158  49.588  1.00 72.33  ?  186  GLY A C   1 
ATOM   1228 O O   . GLY A 1 169 ? 13.409  -4.198  48.417  1.00 71.02  ?  186  GLY A O   1 
ATOM   1229 N N   . GLN A 1 170 ? 14.051  -3.021  50.227  1.00 64.31  ?  187  GLN A N   1 
ATOM   1230 C CA  . GLN A 1 170 ? 13.894  -1.715  49.604  1.00 70.30  ?  187  GLN A CA  1 
ATOM   1231 C C   . GLN A 1 170 ? 15.012  -0.799  50.080  1.00 69.38  ?  187  GLN A C   1 
ATOM   1232 O O   . GLN A 1 170 ? 15.471  -0.896  51.220  1.00 74.81  ?  187  GLN A O   1 
ATOM   1233 C CB  . GLN A 1 170 ? 12.527  -1.095  49.935  1.00 67.53  ?  187  GLN A CB  1 
ATOM   1234 C CG  . GLN A 1 170 ? 12.276  0.257   49.288  1.00 66.87  ?  187  GLN A CG  1 
ATOM   1235 C CD  . GLN A 1 170 ? 11.293  1.103   50.070  1.00 60.71  ?  187  GLN A CD  1 
ATOM   1236 O OE1 . GLN A 1 170 ? 10.177  0.674   50.360  1.00 66.44  ?  187  GLN A OE1 1 
ATOM   1237 N NE2 . GLN A 1 170 ? 11.710  2.312   50.426  1.00 65.40  ?  187  GLN A NE2 1 
ATOM   1238 N N   . LEU A 1 171 ? 15.455  0.087   49.193  1.00 68.26  ?  188  LEU A N   1 
ATOM   1239 C CA  . LEU A 1 171 ? 16.485  1.057   49.543  1.00 71.28  ?  188  LEU A CA  1 
ATOM   1240 C C   . LEU A 1 171 ? 15.844  2.273   50.199  1.00 67.44  ?  188  LEU A C   1 
ATOM   1241 O O   . LEU A 1 171 ? 14.999  2.941   49.592  1.00 67.57  ?  188  LEU A O   1 
ATOM   1242 C CB  . LEU A 1 171 ? 17.279  1.466   48.304  1.00 68.01  ?  188  LEU A CB  1 
ATOM   1243 C CG  . LEU A 1 171 ? 18.385  0.507   47.864  1.00 75.13  ?  188  LEU A CG  1 
ATOM   1244 C CD1 . LEU A 1 171 ? 19.051  1.016   46.600  1.00 77.53  ?  188  LEU A CD1 1 
ATOM   1245 C CD2 . LEU A 1 171 ? 19.406  0.337   48.977  1.00 73.30  ?  188  LEU A CD2 1 
ATOM   1246 N N   . ILE A 1 172 ? 16.235  2.552   51.437  1.00 69.87  ?  189  ILE A N   1 
ATOM   1247 C CA  . ILE A 1 172 ? 15.813  3.738   52.168  1.00 70.10  ?  189  ILE A CA  1 
ATOM   1248 C C   . ILE A 1 172 ? 17.041  4.623   52.325  1.00 72.90  ?  189  ILE A C   1 
ATOM   1249 O O   . ILE A 1 172 ? 17.985  4.268   53.044  1.00 75.79  ?  189  ILE A O   1 
ATOM   1250 C CB  . ILE A 1 172 ? 15.201  3.385   53.530  1.00 70.79  ?  189  ILE A CB  1 
ATOM   1251 C CG1 . ILE A 1 172 ? 14.050  2.393   53.354  1.00 68.23  ?  189  ILE A CG1 1 
ATOM   1252 C CG2 . ILE A 1 172 ? 14.721  4.642   54.239  1.00 73.68  ?  189  ILE A CG2 1 
ATOM   1253 C CD1 . ILE A 1 172 ? 13.421  1.946   54.656  1.00 72.92  ?  189  ILE A CD1 1 
ATOM   1254 N N   . GLU A 1 173 ? 17.038  5.762   51.629  1.00 73.07  ?  190  GLU A N   1 
ATOM   1255 C CA  . GLU A 1 173 ? 18.121  6.745   51.696  1.00 74.66  ?  190  GLU A CA  1 
ATOM   1256 C C   . GLU A 1 173 ? 19.487  6.096   51.480  1.00 77.09  ?  190  GLU A C   1 
ATOM   1257 O O   . GLU A 1 173 ? 20.483  6.468   52.104  1.00 80.11  ?  190  GLU A O   1 
ATOM   1258 C CB  . GLU A 1 173 ? 18.080  7.512   53.018  1.00 76.55  ?  190  GLU A CB  1 
ATOM   1259 C CG  . GLU A 1 173 ? 16.844  8.385   53.180  1.00 81.30  ?  190  GLU A CG  1 
ATOM   1260 C CD  . GLU A 1 173 ? 16.791  9.515   52.167  1.00 95.15  ?  190  GLU A CD  1 
ATOM   1261 O OE1 . GLU A 1 173 ? 17.763  10.298  52.094  1.00 82.00  ?  190  GLU A OE1 1 
ATOM   1262 O OE2 . GLU A 1 173 ? 15.781  9.615   51.438  1.00 89.44  -1 190  GLU A OE2 1 
ATOM   1263 N N   . GLY A 1 174 ? 19.532  5.105   50.589  1.00 75.86  ?  191  GLY A N   1 
ATOM   1264 C CA  . GLY A 1 174 ? 20.771  4.460   50.217  1.00 77.95  ?  191  GLY A CA  1 
ATOM   1265 C C   . GLY A 1 174 ? 21.119  3.207   50.993  1.00 79.55  ?  191  GLY A C   1 
ATOM   1266 O O   . GLY A 1 174 ? 22.096  2.534   50.639  1.00 81.19  ?  191  GLY A O   1 
ATOM   1267 N N   . ILE A 1 175 ? 20.361  2.866   52.033  1.00 79.27  ?  192  ILE A N   1 
ATOM   1268 C CA  . ILE A 1 175 ? 20.632  1.690   52.854  1.00 80.94  ?  192  ILE A CA  1 
ATOM   1269 C C   . ILE A 1 175 ? 19.529  0.668   52.607  1.00 80.01  ?  192  ILE A C   1 
ATOM   1270 O O   . ILE A 1 175 ? 18.344  1.016   52.600  1.00 75.78  ?  192  ILE A O   1 
ATOM   1271 C CB  . ILE A 1 175 ? 20.733  2.053   54.348  1.00 86.93  ?  192  ILE A CB  1 
ATOM   1272 C CG1 . ILE A 1 175 ? 22.030  2.819   54.634  1.00 86.52  ?  192  ILE A CG1 1 
ATOM   1273 C CG2 . ILE A 1 175 ? 20.660  0.806   55.216  1.00 84.47  ?  192  ILE A CG2 1 
ATOM   1274 C CD1 . ILE A 1 175 ? 21.946  4.312   54.386  1.00 86.07  ?  192  ILE A CD1 1 
ATOM   1275 N N   . CYS A 1 176 ? 19.919  -0.586  52.394  1.00 78.91  ?  193  CYS A N   1 
ATOM   1276 C CA  . CYS A 1 176 ? 18.954  -1.647  52.144  1.00 76.66  ?  193  CYS A CA  1 
ATOM   1277 C C   . CYS A 1 176 ? 18.249  -2.049  53.432  1.00 77.09  ?  193  CYS A C   1 
ATOM   1278 O O   . CYS A 1 176 ? 18.880  -2.220  54.479  1.00 79.99  ?  193  CYS A O   1 
ATOM   1279 C CB  . CYS A 1 176 ? 19.640  -2.862  51.527  1.00 82.82  ?  193  CYS A CB  1 
ATOM   1280 S SG  . CYS A 1 176 ? 18.511  -4.191  51.044  1.00 89.47  ?  193  CYS A SG  1 
ATOM   1281 N N   . PHE A 1 177 ? 16.929  -2.212  53.345  1.00 74.29  ?  194  PHE A N   1 
ATOM   1282 C CA  . PHE A 1 177 ? 16.105  -2.661  54.460  1.00 74.40  ?  194  PHE A CA  1 
ATOM   1283 C C   . PHE A 1 177 ? 15.280  -3.848  53.989  1.00 72.31  ?  194  PHE A C   1 
ATOM   1284 O O   . PHE A 1 177 ? 14.550  -3.744  52.997  1.00 74.05  ?  194  PHE A O   1 
ATOM   1285 C CB  . PHE A 1 177 ? 15.189  -1.540  54.961  1.00 73.15  ?  194  PHE A CB  1 
ATOM   1286 C CG  . PHE A 1 177 ? 15.845  -0.601  55.935  1.00 76.38  ?  194  PHE A CG  1 
ATOM   1287 C CD1 . PHE A 1 177 ? 15.616  -0.730  57.295  1.00 77.87  ?  194  PHE A CD1 1 
ATOM   1288 C CD2 . PHE A 1 177 ? 16.676  0.416   55.494  1.00 79.88  ?  194  PHE A CD2 1 
ATOM   1289 C CE1 . PHE A 1 177 ? 16.209  0.132   58.198  1.00 80.23  ?  194  PHE A CE1 1 
ATOM   1290 C CE2 . PHE A 1 177 ? 17.272  1.282   56.394  1.00 84.17  ?  194  PHE A CE2 1 
ATOM   1291 C CZ  . PHE A 1 177 ? 17.037  1.139   57.747  1.00 81.03  ?  194  PHE A CZ  1 
ATOM   1292 N N   . ASN A 1 178 ? 15.399  -4.972  54.693  1.00 73.96  ?  195  ASN A N   1 
ATOM   1293 C CA  . ASN A 1 178 ? 14.630  -6.160  54.364  1.00 73.36  ?  195  ASN A CA  1 
ATOM   1294 C C   . ASN A 1 178 ? 13.427  -6.291  55.289  1.00 71.52  ?  195  ASN A C   1 
ATOM   1295 O O   . ASN A 1 178 ? 13.441  -5.776  56.411  1.00 73.21  ?  195  ASN A O   1 
ATOM   1296 C CB  . ASN A 1 178 ? 15.495  -7.419  54.478  1.00 74.71  ?  195  ASN A CB  1 
ATOM   1297 C CG  . ASN A 1 178 ? 16.407  -7.611  53.284  1.00 76.37  ?  195  ASN A CG  1 
ATOM   1298 O OD1 . ASN A 1 178 ? 16.144  -7.093  52.198  1.00 77.36  ?  195  ASN A OD1 1 
ATOM   1299 N ND2 . ASN A 1 178 ? 17.481  -8.367  53.475  1.00 84.41  ?  195  ASN A ND2 1 
ATOM   1300 N N   . PRO A 1 179 ? 12.367  -6.965  54.838  1.00 72.74  ?  196  PRO A N   1 
ATOM   1301 C CA  . PRO A 1 179 ? 11.209  -7.182  55.713  1.00 71.77  ?  196  PRO A CA  1 
ATOM   1302 C C   . PRO A 1 179 ? 11.598  -7.935  56.976  1.00 75.08  ?  196  PRO A C   1 
ATOM   1303 O O   . PRO A 1 179 ? 12.487  -8.790  56.969  1.00 74.65  ?  196  PRO A O   1 
ATOM   1304 C CB  . PRO A 1 179 ? 10.255  -8.004  54.839  1.00 65.56  ?  196  PRO A CB  1 
ATOM   1305 C CG  . PRO A 1 179 ? 10.638  -7.656  53.439  1.00 63.88  ?  196  PRO A CG  1 
ATOM   1306 C CD  . PRO A 1 179 ? 12.125  -7.453  53.470  1.00 68.60  ?  196  PRO A CD  1 
ATOM   1307 N N   . VAL A 1 180 ? 10.920  -7.594  58.076  1.00 78.89  ?  197  VAL A N   1 
ATOM   1308 C CA  . VAL A 1 180 ? 11.199  -8.227  59.360  1.00 84.92  ?  197  VAL A CA  1 
ATOM   1309 C C   . VAL A 1 180 ? 10.949  -9.726  59.264  1.00 80.99  ?  197  VAL A C   1 
ATOM   1310 O O   . VAL A 1 180 ? 9.955   -10.177 58.680  1.00 76.23  ?  197  VAL A O   1 
ATOM   1311 C CB  . VAL A 1 180 ? 10.347  -7.580  60.465  1.00 78.92  ?  197  VAL A CB  1 
ATOM   1312 C CG1 . VAL A 1 180 ? 10.228  -8.500  61.672  1.00 90.32  ?  197  VAL A CG1 1 
ATOM   1313 C CG2 . VAL A 1 180 ? 10.946  -6.243  60.874  1.00 76.78  ?  197  VAL A CG2 1 
ATOM   1314 N N   . HIS A 1 181 ? 11.866  -10.507 59.830  1.00 96.64  ?  198  HIS A N   1 
ATOM   1315 C CA  . HIS A 1 181 ? 11.789  -11.963 59.784  1.00 110.51 ?  198  HIS A CA  1 
ATOM   1316 C C   . HIS A 1 181 ? 11.081  -12.470 61.035  1.00 109.42 ?  198  HIS A C   1 
ATOM   1317 O O   . HIS A 1 181 ? 11.632  -12.404 62.140  1.00 110.34 ?  198  HIS A O   1 
ATOM   1318 C CB  . HIS A 1 181 ? 13.185  -12.568 59.661  1.00 112.05 ?  198  HIS A CB  1 
ATOM   1319 C CG  . HIS A 1 181 ? 13.216  -14.054 59.836  1.00 123.43 ?  198  HIS A CG  1 
ATOM   1320 N ND1 . HIS A 1 181 ? 13.537  -14.655 61.034  1.00 126.74 ?  198  HIS A ND1 1 
ATOM   1321 C CD2 . HIS A 1 181 ? 12.964  -15.061 58.966  1.00 129.28 ?  198  HIS A CD2 1 
ATOM   1322 C CE1 . HIS A 1 181 ? 13.483  -15.968 60.894  1.00 127.92 ?  198  HIS A CE1 1 
ATOM   1323 N NE2 . HIS A 1 181 ? 13.138  -16.240 59.649  1.00 136.84 ?  198  HIS A NE2 1 
ATOM   1324 N N   . THR A 1 182 ? 9.862   -12.971 60.865  1.00 111.66 ?  199  THR A N   1 
ATOM   1325 C CA  . THR A 1 182 ? 9.137   -13.618 61.954  1.00 122.49 ?  199  THR A CA  1 
ATOM   1326 C C   . THR A 1 182 ? 8.127   -14.620 61.407  1.00 112.16 ?  199  THR A C   1 
ATOM   1327 O O   . THR A 1 182 ? 6.987   -14.265 61.105  1.00 102.93 ?  199  THR A O   1 
ATOM   1328 C CB  . THR A 1 182 ? 8.395   -12.603 62.844  1.00 122.93 ?  199  THR A CB  1 
ATOM   1329 O OG1 . THR A 1 182 ? 9.301   -11.581 63.277  1.00 109.65 ?  199  THR A OG1 1 
ATOM   1330 C CG2 . THR A 1 182 ? 7.817   -13.307 64.062  1.00 113.67 ?  199  THR A CG2 1 
ATOM   1331 N N   . GLN A 1 187 ? 6.735   -10.516 65.227  1.00 132.42 ?  204  GLN A N   1 
ATOM   1332 C CA  . GLN A 1 187 ? 6.251   -9.143  65.182  1.00 132.07 ?  204  GLN A CA  1 
ATOM   1333 C C   . GLN A 1 187 ? 5.947   -8.648  66.593  1.00 146.16 ?  204  GLN A C   1 
ATOM   1334 O O   . GLN A 1 187 ? 4.783   -8.506  66.968  1.00 148.27 ?  204  GLN A O   1 
ATOM   1335 C CB  . GLN A 1 187 ? 5.006   -9.044  64.299  1.00 121.03 ?  204  GLN A CB  1 
ATOM   1336 C CG  . GLN A 1 187 ? 4.686   -7.637  63.828  1.00 126.68 ?  204  GLN A CG  1 
ATOM   1337 C CD  . GLN A 1 187 ? 5.742   -7.083  62.890  1.00 114.41 ?  204  GLN A CD  1 
ATOM   1338 O OE1 . GLN A 1 187 ? 6.455   -7.835  62.224  1.00 107.90 ?  204  GLN A OE1 1 
ATOM   1339 N NE2 . GLN A 1 187 ? 5.849   -5.762  62.838  1.00 123.55 ?  204  GLN A NE2 1 
ATOM   1340 N N   . PRO A 1 188 ? 6.995   -8.389  67.381  1.00 149.42 ?  205  PRO A N   1 
ATOM   1341 C CA  . PRO A 1 188 ? 6.781   -8.018  68.785  1.00 151.22 ?  205  PRO A CA  1 
ATOM   1342 C C   . PRO A 1 188 ? 6.432   -6.550  68.967  1.00 154.12 ?  205  PRO A C   1 
ATOM   1343 O O   . PRO A 1 188 ? 5.617   -6.201  69.825  1.00 151.28 ?  205  PRO A O   1 
ATOM   1344 C CB  . PRO A 1 188 ? 8.125   -8.359  69.438  1.00 142.80 ?  205  PRO A CB  1 
ATOM   1345 C CG  . PRO A 1 188 ? 9.120   -8.146  68.344  1.00 143.51 ?  205  PRO A CG  1 
ATOM   1346 C CD  . PRO A 1 188 ? 8.427   -8.504  67.049  1.00 144.16 ?  205  PRO A CD  1 
ATOM   1347 N N   . SER A 1 189 ? 7.049   -5.677  68.173  1.00 148.73 ?  206  SER A N   1 
ATOM   1348 C CA  . SER A 1 189 ? 6.888   -4.241  68.362  1.00 145.20 ?  206  SER A CA  1 
ATOM   1349 C C   . SER A 1 189 ? 5.576   -3.755  67.764  1.00 151.88 ?  206  SER A C   1 
ATOM   1350 O O   . SER A 1 189 ? 4.647   -4.543  67.558  1.00 146.53 ?  206  SER A O   1 
ATOM   1351 C CB  . SER A 1 189 ? 8.066   -3.487  67.745  1.00 147.22 ?  206  SER A CB  1 
ATOM   1352 O OG  . SER A 1 189 ? 9.292   -3.887  68.336  1.00 127.84 ?  206  SER A OG  1 
ATOM   1353 N N   . HIS A 1 190 ? 5.488   -2.453  67.484  1.00 154.82 ?  207  HIS A N   1 
ATOM   1354 C CA  . HIS A 1 190 ? 4.269   -1.867  66.926  1.00 150.96 ?  207  HIS A CA  1 
ATOM   1355 C C   . HIS A 1 190 ? 4.442   -1.386  65.493  1.00 147.79 ?  207  HIS A C   1 
ATOM   1356 O O   . HIS A 1 190 ? 4.253   -2.152  64.539  1.00 139.85 ?  207  HIS A O   1 
ATOM   1357 C CB  . HIS A 1 190 ? 3.805   -0.694  67.779  1.00 155.84 ?  207  HIS A CB  1 
ATOM   1358 C CG  . HIS A 1 190 ? 2.325   -0.656  68.003  1.00 167.87 ?  207  HIS A CG  1 
ATOM   1359 N ND1 . HIS A 1 190 ? 1.695   0.384   68.655  1.00 174.57 ?  207  HIS A ND1 1 
ATOM   1360 C CD2 . HIS A 1 190 ? 1.349   -1.533  67.669  1.00 172.50 ?  207  HIS A CD2 1 
ATOM   1361 C CE1 . HIS A 1 190 ? 0.396   0.146   68.709  1.00 180.18 ?  207  HIS A CE1 1 
ATOM   1362 N NE2 . HIS A 1 190 ? 0.160   -1.011  68.118  1.00 182.00 ?  207  HIS A NE2 1 
ATOM   1363 N N   . THR A 1 191 ? 4.790   -0.112  65.328  1.00 149.45 ?  208  THR A N   1 
ATOM   1364 C CA  . THR A 1 191 ? 4.917   0.506   64.011  1.00 137.18 ?  208  THR A CA  1 
ATOM   1365 C C   . THR A 1 191 ? 6.261   1.203   63.893  1.00 123.91 ?  208  THR A C   1 
ATOM   1366 O O   . THR A 1 191 ? 6.571   2.102   64.681  1.00 112.66 ?  208  THR A O   1 
ATOM   1367 C CB  . THR A 1 191 ? 3.777   1.494   63.736  1.00 126.43 ?  208  THR A CB  1 
ATOM   1368 O OG1 . THR A 1 191 ? 4.164   2.375   62.678  1.00 116.13 ?  208  THR A OG1 1 
ATOM   1369 C CG2 . THR A 1 191 ? 3.427   2.310   64.982  1.00 112.74 ?  208  THR A CG2 1 
ATOM   1370 N N   . TYR A 1 192 ? 7.047   0.802   62.889  1.00 119.97 ?  209  TYR A N   1 
ATOM   1371 C CA  . TYR A 1 192 ? 8.355   1.408   62.644  1.00 113.92 ?  209  TYR A CA  1 
ATOM   1372 C C   . TYR A 1 192 ? 8.710   1.464   61.160  1.00 104.44 ?  209  TYR A C   1 
ATOM   1373 O O   . TYR A 1 192 ? 7.848   1.742   60.319  1.00 107.67 ?  209  TYR A O   1 
ATOM   1374 C CB  . TYR A 1 192 ? 9.437   0.653   63.418  1.00 110.32 ?  209  TYR A CB  1 
ATOM   1375 C CG  . TYR A 1 192 ? 9.635   1.177   64.821  1.00 118.28 ?  209  TYR A CG  1 
ATOM   1376 C CD1 . TYR A 1 192 ? 10.474  2.257   65.064  1.00 126.94 ?  209  TYR A CD1 1 
ATOM   1377 C CD2 . TYR A 1 192 ? 8.979   0.597   65.902  1.00 123.68 ?  209  TYR A CD2 1 
ATOM   1378 C CE1 . TYR A 1 192 ? 10.659  2.746   66.344  1.00 129.86 ?  209  TYR A CE1 1 
ATOM   1379 C CE2 . TYR A 1 192 ? 9.156   1.079   67.186  1.00 130.39 ?  209  TYR A CE2 1 
ATOM   1380 C CZ  . TYR A 1 192 ? 9.998   2.153   67.401  1.00 131.89 ?  209  TYR A CZ  1 
ATOM   1381 O OH  . TYR A 1 192 ? 10.178  2.636   68.677  1.00 120.46 ?  209  TYR A OH  1 
ATOM   1382 N N   . ASP A 1 193 ? 9.981   1.215   60.834  1.00 82.41  ?  210  ASP A N   1 
ATOM   1383 C CA  . ASP A 1 193 ? 10.492  1.382   59.475  1.00 72.88  ?  210  ASP A CA  1 
ATOM   1384 C C   . ASP A 1 193 ? 9.772   0.475   58.483  1.00 73.46  ?  210  ASP A C   1 
ATOM   1385 O O   . ASP A 1 193 ? 9.890   -0.753  58.550  1.00 88.13  ?  210  ASP A O   1 
ATOM   1386 C CB  . ASP A 1 193 ? 12.000  1.120   59.436  1.00 74.28  ?  210  ASP A CB  1 
ATOM   1387 C CG  . ASP A 1 193 ? 12.790  2.150   60.221  1.00 90.77  ?  210  ASP A CG  1 
ATOM   1388 O OD1 . ASP A 1 193 ? 12.444  3.349   60.148  1.00 88.49  ?  210  ASP A OD1 1 
ATOM   1389 O OD2 . ASP A 1 193 ? 13.751  1.762   60.918  1.00 94.10  -1 210  ASP A OD2 1 
ATOM   1390 N N   . ILE A 1 194 ? 9.032   1.078   57.556  1.00 65.61  ?  211  ILE A N   1 
ATOM   1391 C CA  . ILE A 1 194 ? 8.201   0.355   56.600  1.00 63.71  ?  211  ILE A CA  1 
ATOM   1392 C C   . ILE A 1 194 ? 8.883   0.365   55.240  1.00 61.54  ?  211  ILE A C   1 
ATOM   1393 O O   . ILE A 1 194 ? 9.317   1.421   54.760  1.00 70.05  ?  211  ILE A O   1 
ATOM   1394 C CB  . ILE A 1 194 ? 6.793   0.970   56.513  1.00 59.94  ?  211  ILE A CB  1 
ATOM   1395 C CG1 . ILE A 1 194 ? 5.946   0.537   57.711  1.00 64.15  ?  211  ILE A CG1 1 
ATOM   1396 C CG2 . ILE A 1 194 ? 6.114   0.599   55.201  1.00 56.63  ?  211  ILE A CG2 1 
ATOM   1397 C CD1 . ILE A 1 194 ? 4.512   1.020   57.655  1.00 73.30  ?  211  ILE A CD1 1 
ATOM   1398 N N   . VAL A 1 195 ? 8.984   -0.809  54.624  1.00 60.85  ?  212  VAL A N   1 
ATOM   1399 C CA  . VAL A 1 195 ? 9.464   -0.938  53.257  1.00 59.62  ?  212  VAL A CA  1 
ATOM   1400 C C   . VAL A 1 195 ? 8.290   -1.339  52.374  1.00 56.24  ?  212  VAL A C   1 
ATOM   1401 O O   . VAL A 1 195 ? 7.285   -1.890  52.836  1.00 57.60  ?  212  VAL A O   1 
ATOM   1402 C CB  . VAL A 1 195 ? 10.618  -1.956  53.134  1.00 61.69  ?  212  VAL A CB  1 
ATOM   1403 C CG1 . VAL A 1 195 ? 11.683  -1.675  54.177  1.00 65.22  ?  212  VAL A CG1 1 
ATOM   1404 C CG2 . VAL A 1 195 ? 10.095  -3.380  53.264  1.00 61.21  ?  212  VAL A CG2 1 
ATOM   1405 N N   . THR A 1 196 ? 8.420   -1.045  51.083  1.00 54.57  ?  213  THR A N   1 
ATOM   1406 C CA  . THR A 1 196 ? 7.408   -1.386  50.089  1.00 56.34  ?  213  THR A CA  1 
ATOM   1407 C C   . THR A 1 196 ? 8.067   -2.258  49.029  1.00 56.06  ?  213  THR A C   1 
ATOM   1408 O O   . THR A 1 196 ? 8.881   -1.773  48.236  1.00 54.51  ?  213  THR A O   1 
ATOM   1409 C CB  . THR A 1 196 ? 6.794   -0.133  49.467  1.00 59.96  ?  213  THR A CB  1 
ATOM   1410 O OG1 . THR A 1 196 ? 6.330   0.738   50.506  1.00 66.86  ?  213  THR A OG1 1 
ATOM   1411 C CG2 . THR A 1 196 ? 5.622   -0.509  48.572  1.00 56.90  ?  213  THR A CG2 1 
ATOM   1412 N N   . VAL A 1 197 ? 7.715   -3.540  49.018  1.00 59.45  ?  214  VAL A N   1 
ATOM   1413 C CA  . VAL A 1 197 ? 8.343   -4.516  48.139  1.00 55.72  ?  214  VAL A CA  1 
ATOM   1414 C C   . VAL A 1 197 ? 7.305   -5.069  47.173  1.00 59.20  ?  214  VAL A C   1 
ATOM   1415 O O   . VAL A 1 197 ? 6.107   -5.125  47.472  1.00 59.76  ?  214  VAL A O   1 
ATOM   1416 C CB  . VAL A 1 197 ? 9.009   -5.657  48.938  1.00 57.22  ?  214  VAL A CB  1 
ATOM   1417 C CG1 . VAL A 1 197 ? 10.256  -5.148  49.642  1.00 57.72  ?  214  VAL A CG1 1 
ATOM   1418 C CG2 . VAL A 1 197 ? 8.027   -6.240  49.940  1.00 53.43  ?  214  VAL A CG2 1 
ATOM   1419 N N   . MET A 1 198 ? 7.783   -5.472  46.000  1.00 50.49  ?  215  MET A N   1 
ATOM   1420 C CA  . MET A 1 198 ? 6.954   -6.089  44.976  1.00 57.21  ?  215  MET A CA  1 
ATOM   1421 C C   . MET A 1 198 ? 6.835   -7.585  45.233  1.00 57.64  ?  215  MET A C   1 
ATOM   1422 O O   . MET A 1 198 ? 7.820   -8.250  45.564  1.00 57.59  ?  215  MET A O   1 
ATOM   1423 C CB  . MET A 1 198 ? 7.556   -5.841  43.592  1.00 53.63  ?  215  MET A CB  1 
ATOM   1424 C CG  . MET A 1 198 ? 6.841   -6.525  42.437  1.00 62.18  ?  215  MET A CG  1 
ATOM   1425 S SD  . MET A 1 198 ? 7.865   -6.508  40.950  1.00 79.51  ?  215  MET A SD  1 
ATOM   1426 C CE  . MET A 1 198 ? 6.693   -7.033  39.703  1.00 79.62  ?  215  MET A CE  1 
ATOM   1427 N N   . VAL A 1 199 ? 5.622   -8.112  45.082  1.00 47.18  ?  216  VAL A N   1 
ATOM   1428 C CA  . VAL A 1 199 ? 5.376   -9.545  45.182  1.00 56.26  ?  216  VAL A CA  1 
ATOM   1429 C C   . VAL A 1 199 ? 4.754   -10.021 43.878  1.00 53.23  ?  216  VAL A C   1 
ATOM   1430 O O   . VAL A 1 199 ? 3.942   -9.317  43.268  1.00 54.18  ?  216  VAL A O   1 
ATOM   1431 C CB  . VAL A 1 199 ? 4.476   -9.906  46.383  1.00 53.28  ?  216  VAL A CB  1 
ATOM   1432 C CG1 . VAL A 1 199 ? 5.158   -9.530  47.690  1.00 56.04  ?  216  VAL A CG1 1 
ATOM   1433 C CG2 . VAL A 1 199 ? 3.112   -9.240  46.264  1.00 54.25  ?  216  VAL A CG2 1 
ATOM   1434 N N   . ARG A 1 200 ? 5.158   -11.211 43.444  1.00 59.99  ?  217  ARG A N   1 
ATOM   1435 C CA  . ARG A 1 200 ? 4.587   -11.870 42.275  1.00 51.80  ?  217  ARG A CA  1 
ATOM   1436 C C   . ARG A 1 200 ? 4.050   -13.222 42.724  1.00 53.37  ?  217  ARG A C   1 
ATOM   1437 O O   . ARG A 1 200 ? 4.825   -14.121 43.068  1.00 59.40  ?  217  ARG A O   1 
ATOM   1438 C CB  . ARG A 1 200 ? 5.623   -12.013 41.160  1.00 48.37  ?  217  ARG A CB  1 
ATOM   1439 C CG  . ARG A 1 200 ? 5.717   -10.781 40.271  1.00 50.49  ?  217  ARG A CG  1 
ATOM   1440 C CD  . ARG A 1 200 ? 6.984   -10.766 39.432  1.00 44.97  ?  217  ARG A CD  1 
ATOM   1441 N NE  . ARG A 1 200 ? 8.165   -10.460 40.232  1.00 53.73  ?  217  ARG A NE  1 
ATOM   1442 C CZ  . ARG A 1 200 ? 9.344   -10.120 39.722  1.00 51.29  ?  217  ARG A CZ  1 
ATOM   1443 N NH1 . ARG A 1 200 ? 9.501   -10.036 38.408  1.00 51.86  1  217  ARG A NH1 1 
ATOM   1444 N NH2 . ARG A 1 200 ? 10.366  -9.859  40.525  1.00 46.20  ?  217  ARG A NH2 1 
ATOM   1445 N N   . CYS A 1 201 ? 2.729   -13.357 42.734  1.00 55.72  ?  218  CYS A N   1 
ATOM   1446 C CA  . CYS A 1 201 ? 2.060   -14.547 43.235  1.00 61.83  ?  218  CYS A CA  1 
ATOM   1447 C C   . CYS A 1 201 ? 1.581   -15.420 42.083  1.00 56.12  ?  218  CYS A C   1 
ATOM   1448 O O   . CYS A 1 201 ? 1.315   -14.939 40.979  1.00 57.03  ?  218  CYS A O   1 
ATOM   1449 C CB  . CYS A 1 201 ? 0.873   -14.166 44.120  1.00 64.27  ?  218  CYS A CB  1 
ATOM   1450 S SG  . CYS A 1 201 ? 1.036   -14.542 45.888  1.00 98.70  ?  218  CYS A SG  1 
ATOM   1451 N N   . PHE A 1 202 ? 1.463   -16.716 42.361  1.00 69.28  ?  219  PHE A N   1 
ATOM   1452 C CA  . PHE A 1 202 ? 1.056   -17.703 41.372  1.00 56.86  ?  219  PHE A CA  1 
ATOM   1453 C C   . PHE A 1 202 ? 0.011   -18.619 41.990  1.00 49.89  ?  219  PHE A C   1 
ATOM   1454 O O   . PHE A 1 202 ? 0.218   -19.148 43.087  1.00 59.33  ?  219  PHE A O   1 
ATOM   1455 C CB  . PHE A 1 202 ? 2.258   -18.513 40.880  1.00 49.81  ?  219  PHE A CB  1 
ATOM   1456 C CG  . PHE A 1 202 ? 3.332   -17.675 40.249  1.00 59.80  ?  219  PHE A CG  1 
ATOM   1457 C CD1 . PHE A 1 202 ? 3.356   -17.473 38.880  1.00 49.45  ?  219  PHE A CD1 1 
ATOM   1458 C CD2 . PHE A 1 202 ? 4.315   -17.081 41.025  1.00 54.45  ?  219  PHE A CD2 1 
ATOM   1459 C CE1 . PHE A 1 202 ? 4.343   -16.700 38.295  1.00 54.03  ?  219  PHE A CE1 1 
ATOM   1460 C CE2 . PHE A 1 202 ? 5.303   -16.306 40.446  1.00 49.16  ?  219  PHE A CE2 1 
ATOM   1461 C CZ  . PHE A 1 202 ? 5.316   -16.116 39.079  1.00 56.96  ?  219  PHE A CZ  1 
ATOM   1462 N N   . LEU A 1 203 ? -1.105  -18.798 41.289  1.00 50.42  ?  220  LEU A N   1 
ATOM   1463 C CA  . LEU A 1 203 ? -2.197  -19.622 41.787  1.00 51.54  ?  220  LEU A CA  1 
ATOM   1464 C C   . LEU A 1 203 ? -1.841  -21.099 41.693  1.00 58.39  ?  220  LEU A C   1 
ATOM   1465 O O   . LEU A 1 203 ? -1.305  -21.565 40.683  1.00 55.17  ?  220  LEU A O   1 
ATOM   1466 C CB  . LEU A 1 203 ? -3.480  -19.344 41.007  1.00 51.80  ?  220  LEU A CB  1 
ATOM   1467 C CG  . LEU A 1 203 ? -4.728  -20.086 41.493  1.00 63.87  ?  220  LEU A CG  1 
ATOM   1468 C CD1 . LEU A 1 203 ? -5.089  -19.672 42.914  1.00 52.70  ?  220  LEU A CD1 1 
ATOM   1469 C CD2 . LEU A 1 203 ? -5.897  -19.857 40.550  1.00 54.25  ?  220  LEU A CD2 1 
ATOM   1470 N N   . ILE A 1 204 ? -2.150  -21.836 42.757  1.00 54.71  ?  221  ILE A N   1 
ATOM   1471 C CA  . ILE A 1 204 ? -1.869  -23.262 42.851  1.00 62.02  ?  221  ILE A CA  1 
ATOM   1472 C C   . ILE A 1 204 ? -3.169  -23.991 43.159  1.00 57.30  ?  221  ILE A C   1 
ATOM   1473 O O   . ILE A 1 204 ? -3.950  -23.549 44.009  1.00 58.04  ?  221  ILE A O   1 
ATOM   1474 C CB  . ILE A 1 204 ? -0.812  -23.560 43.933  1.00 60.57  ?  221  ILE A CB  1 
ATOM   1475 C CG1 . ILE A 1 204 ? 0.412   -22.658 43.756  1.00 54.35  ?  221  ILE A CG1 1 
ATOM   1476 C CG2 . ILE A 1 204 ? -0.411  -25.014 43.885  1.00 57.77  ?  221  ILE A CG2 1 
ATOM   1477 C CD1 . ILE A 1 204 ? 1.142   -22.858 42.449  1.00 54.84  ?  221  ILE A CD1 1 
ATOM   1478 N N   . VAL A 1 205 ? -3.399  -25.104 42.469  1.00 59.11  ?  222  VAL A N   1 
ATOM   1479 C CA  . VAL A 1 205 ? -4.582  -25.933 42.675  1.00 68.13  ?  222  VAL A CA  1 
ATOM   1480 C C   . VAL A 1 205 ? -4.192  -27.106 43.564  1.00 62.46  ?  222  VAL A C   1 
ATOM   1481 O O   . VAL A 1 205 ? -3.273  -27.866 43.236  1.00 73.52  ?  222  VAL A O   1 
ATOM   1482 C CB  . VAL A 1 205 ? -5.164  -26.423 41.339  1.00 62.36  ?  222  VAL A CB  1 
ATOM   1483 C CG1 . VAL A 1 205 ? -6.392  -27.289 41.580  1.00 64.30  ?  222  VAL A CG1 1 
ATOM   1484 C CG2 . VAL A 1 205 ? -5.503  -25.239 40.445  1.00 63.63  ?  222  VAL A CG2 1 
ATOM   1485 N N   . LYS A 1 206 ? -4.889  -27.257 44.690  1.00 69.05  ?  223  LYS A N   1 
ATOM   1486 C CA  . LYS A 1 206 ? -4.588  -28.325 45.640  1.00 74.19  ?  223  LYS A CA  1 
ATOM   1487 C C   . LYS A 1 206 ? -5.868  -28.662 46.393  1.00 68.36  ?  223  LYS A C   1 
ATOM   1488 O O   . LYS A 1 206 ? -6.356  -27.849 47.184  1.00 68.69  ?  223  LYS A O   1 
ATOM   1489 C CB  . LYS A 1 206 ? -3.474  -27.908 46.598  1.00 68.74  ?  223  LYS A CB  1 
ATOM   1490 C CG  . LYS A 1 206 ? -2.753  -29.066 47.271  1.00 71.77  ?  223  LYS A CG  1 
ATOM   1491 C CD  . LYS A 1 206 ? -3.427  -29.479 48.569  1.00 79.94  ?  223  LYS A CD  1 
ATOM   1492 C CE  . LYS A 1 206 ? -2.699  -30.646 49.218  1.00 68.67  ?  223  LYS A CE  1 
ATOM   1493 N NZ  . LYS A 1 206 ? -2.731  -31.868 48.368  1.00 83.88  1  223  LYS A NZ  1 
ATOM   1494 N N   . LYS A 1 207 ? -6.399  -29.856 46.152  1.00 71.90  ?  224  LYS A N   1 
ATOM   1495 C CA  . LYS A 1 207 ? -7.653  -30.302 46.740  1.00 77.35  ?  224  LYS A CA  1 
ATOM   1496 C C   . LYS A 1 207 ? -7.389  -31.208 47.936  1.00 72.12  ?  224  LYS A C   1 
ATOM   1497 O O   . LYS A 1 207 ? -6.388  -31.928 47.984  1.00 75.62  ?  224  LYS A O   1 
ATOM   1498 C CB  . LYS A 1 207 ? -8.498  -31.045 45.700  1.00 73.20  ?  224  LYS A CB  1 
ATOM   1499 C CG  . LYS A 1 207 ? -8.611  -30.314 44.368  1.00 90.65  ?  224  LYS A CG  1 
ATOM   1500 C CD  . LYS A 1 207 ? -9.031  -31.236 43.227  1.00 83.71  ?  224  LYS A CD  1 
ATOM   1501 C CE  . LYS A 1 207 ? -10.535 -31.474 43.199  1.00 99.21  ?  224  LYS A CE  1 
ATOM   1502 N NZ  . LYS A 1 207 ? -10.944 -32.650 44.016  1.00 99.60  1  224  LYS A NZ  1 
ATOM   1503 N N   . VAL A 1 208 ? -8.297  -31.157 48.913  1.00 82.83  ?  225  VAL A N   1 
ATOM   1504 C CA  . VAL A 1 208 ? -8.273  -32.061 50.054  1.00 79.42  ?  225  VAL A CA  1 
ATOM   1505 C C   . VAL A 1 208 ? -9.634  -32.738 50.160  1.00 92.76  ?  225  VAL A C   1 
ATOM   1506 O O   . VAL A 1 208 ? -10.625 -32.292 49.577  1.00 85.87  ?  225  VAL A O   1 
ATOM   1507 C CB  . VAL A 1 208 ? -7.911  -31.352 51.378  1.00 73.58  ?  225  VAL A CB  1 
ATOM   1508 C CG1 . VAL A 1 208 ? -6.474  -30.849 51.336  1.00 71.46  ?  225  VAL A CG1 1 
ATOM   1509 C CG2 . VAL A 1 208 ? -8.877  -30.215 51.657  1.00 82.06  ?  225  VAL A CG2 1 
ATOM   1510 N N   . THR A 1 209 ? -9.671  -33.826 50.930  1.00 79.79  ?  226  THR A N   1 
ATOM   1511 C CA  . THR A 1 209 ? -10.808 -34.739 50.878  1.00 82.81  ?  226  THR A CA  1 
ATOM   1512 C C   . THR A 1 209 ? -12.022 -34.233 51.651  1.00 92.04  ?  226  THR A C   1 
ATOM   1513 O O   . THR A 1 209 ? -13.158 -34.513 51.251  1.00 86.35  ?  226  THR A O   1 
ATOM   1514 C CB  . THR A 1 209 ? -10.395 -36.115 51.408  1.00 85.48  ?  226  THR A CB  1 
ATOM   1515 O OG1 . THR A 1 209 ? -9.109  -36.464 50.881  1.00 100.34 ?  226  THR A OG1 1 
ATOM   1516 C CG2 . THR A 1 209 ? -11.404 -37.175 50.989  1.00 88.76  ?  226  THR A CG2 1 
ATOM   1517 N N   . THR A 1 210 ? -11.824 -33.492 52.742  1.00 82.29  ?  227  THR A N   1 
ATOM   1518 C CA  . THR A 1 210 ? -12.944 -33.228 53.640  1.00 87.96  ?  227  THR A CA  1 
ATOM   1519 C C   . THR A 1 210 ? -13.094 -31.763 54.038  1.00 91.68  ?  227  THR A C   1 
ATOM   1520 O O   . THR A 1 210 ? -14.187 -31.199 53.931  1.00 114.71 ?  227  THR A O   1 
ATOM   1521 C CB  . THR A 1 210 ? -12.806 -34.085 54.901  1.00 92.77  ?  227  THR A CB  1 
ATOM   1522 O OG1 . THR A 1 210 ? -12.667 -35.462 54.529  1.00 107.36 ?  227  THR A OG1 1 
ATOM   1523 C CG2 . THR A 1 210 ? -14.031 -33.929 55.790  1.00 88.73  ?  227  THR A CG2 1 
ATOM   1524 N N   . GLY A 1 211 ? -12.016 -31.142 54.504  1.00 90.61  ?  228  GLY A N   1 
ATOM   1525 C CA  . GLY A 1 211 ? -12.126 -29.856 55.162  1.00 105.56 ?  228  GLY A CA  1 
ATOM   1526 C C   . GLY A 1 211 ? -12.398 -28.696 54.218  1.00 104.91 ?  228  GLY A C   1 
ATOM   1527 O O   . GLY A 1 211 ? -12.410 -28.818 52.993  1.00 98.58  ?  228  GLY A O   1 
ATOM   1528 N N   . ASP A 1 212 ? -12.636 -27.537 54.832  1.00 108.79 ?  229  ASP A N   1 
ATOM   1529 C CA  . ASP A 1 212 ? -12.752 -26.264 54.134  1.00 103.02 ?  229  ASP A CA  1 
ATOM   1530 C C   . ASP A 1 212 ? -11.441 -25.489 54.123  1.00 96.42  ?  229  ASP A C   1 
ATOM   1531 O O   . ASP A 1 212 ? -11.436 -24.303 53.779  1.00 97.09  ?  229  ASP A O   1 
ATOM   1532 C CB  . ASP A 1 212 ? -13.846 -25.403 54.772  1.00 102.31 ?  229  ASP A CB  1 
ATOM   1533 C CG  . ASP A 1 212 ? -15.234 -25.754 54.278  1.00 108.27 ?  229  ASP A CG  1 
ATOM   1534 O OD1 . ASP A 1 212 ? -15.363 -26.690 53.462  1.00 122.26 ?  229  ASP A OD1 1 
ATOM   1535 O OD2 . ASP A 1 212 ? -16.199 -25.084 54.703  1.00 113.02 -1 229  ASP A OD2 1 
ATOM   1536 N N   . SER A 1 213 ? -10.332 -26.135 54.491  1.00 94.88  ?  230  SER A N   1 
ATOM   1537 C CA  . SER A 1 213 ? -9.072  -25.427 54.687  1.00 91.54  ?  230  SER A CA  1 
ATOM   1538 C C   . SER A 1 213 ? -8.488  -24.878 53.392  1.00 70.98  ?  230  SER A C   1 
ATOM   1539 O O   . SER A 1 213 ? -7.683  -23.942 53.443  1.00 82.74  ?  230  SER A O   1 
ATOM   1540 C CB  . SER A 1 213 ? -8.057  -26.351 55.363  1.00 83.95  ?  230  SER A CB  1 
ATOM   1541 O OG  . SER A 1 213 ? -7.928  -27.571 54.654  1.00 69.23  ?  230  SER A OG  1 
ATOM   1542 N N   . MET A 1 214 ? -8.866  -25.430 52.242  1.00 82.10  ?  231  MET A N   1 
ATOM   1543 C CA  . MET A 1 214 ? -8.327  -24.995 50.961  1.00 67.60  ?  231  MET A CA  1 
ATOM   1544 C C   . MET A 1 214 ? -9.240  -24.021 50.227  1.00 66.24  ?  231  MET A C   1 
ATOM   1545 O O   . MET A 1 214 ? -8.872  -23.541 49.151  1.00 61.38  ?  231  MET A O   1 
ATOM   1546 C CB  . MET A 1 214 ? -8.043  -26.208 50.069  1.00 75.11  ?  231  MET A CB  1 
ATOM   1547 C CG  . MET A 1 214 ? -7.009  -27.173 50.634  1.00 82.55  ?  231  MET A CG  1 
ATOM   1548 S SD  . MET A 1 214 ? -5.412  -26.398 50.952  1.00 79.86  ?  231  MET A SD  1 
ATOM   1549 C CE  . MET A 1 214 ? -5.402  -26.361 52.743  1.00 79.72  ?  231  MET A CE  1 
ATOM   1550 N N   . LYS A 1 215 ? -10.416 -23.719 50.777  1.00 63.66  ?  232  LYS A N   1 
ATOM   1551 C CA  . LYS A 1 215 ? -11.338 -22.759 50.169  1.00 68.44  ?  232  LYS A CA  1 
ATOM   1552 C C   . LYS A 1 215 ? -10.829 -21.349 50.461  1.00 71.84  ?  232  LYS A C   1 
ATOM   1553 O O   . LYS A 1 215 ? -11.293 -20.653 51.368  1.00 65.81  ?  232  LYS A O   1 
ATOM   1554 C CB  . LYS A 1 215 ? -12.754 -22.972 50.688  1.00 67.68  ?  232  LYS A CB  1 
ATOM   1555 C CG  . LYS A 1 215 ? -13.419 -24.245 50.185  1.00 68.39  ?  232  LYS A CG  1 
ATOM   1556 C CD  . LYS A 1 215 ? -14.678 -24.557 50.979  1.00 95.41  ?  232  LYS A CD  1 
ATOM   1557 C CE  . LYS A 1 215 ? -15.575 -25.539 50.241  1.00 89.04  ?  232  LYS A CE  1 
ATOM   1558 N NZ  . LYS A 1 215 ? -14.865 -26.797 49.887  1.00 93.39  1  232  LYS A NZ  1 
ATOM   1559 N N   . ILE A 1 216 ? -9.849  -20.923 49.658  1.00 74.09  ?  233  ILE A N   1 
ATOM   1560 C CA  . ILE A 1 216 ? -9.217  -19.625 49.873  1.00 79.37  ?  233  ILE A CA  1 
ATOM   1561 C C   . ILE A 1 216 ? -10.204 -18.489 49.635  1.00 67.15  ?  233  ILE A C   1 
ATOM   1562 O O   . ILE A 1 216 ? -10.091 -17.421 50.250  1.00 64.78  ?  233  ILE A O   1 
ATOM   1563 C CB  . ILE A 1 216 ? -7.966  -19.485 48.982  1.00 57.23  ?  233  ILE A CB  1 
ATOM   1564 C CG1 . ILE A 1 216 ? -7.251  -18.160 49.263  1.00 56.42  ?  233  ILE A CG1 1 
ATOM   1565 C CG2 . ILE A 1 216 ? -8.335  -19.594 47.510  1.00 60.62  ?  233  ILE A CG2 1 
ATOM   1566 C CD1 . ILE A 1 216 ? -6.038  -17.921 48.396  1.00 54.11  ?  233  ILE A CD1 1 
ATOM   1567 N N   . GLU A 1 217 ? -11.191 -18.695 48.757  1.00 67.51  ?  234  GLU A N   1 
ATOM   1568 C CA  . GLU A 1 217 ? -12.176 -17.650 48.498  1.00 69.60  ?  234  GLU A CA  1 
ATOM   1569 C C   . GLU A 1 217 ? -13.004 -17.332 49.737  1.00 70.02  ?  234  GLU A C   1 
ATOM   1570 O O   . GLU A 1 217 ? -13.515 -16.214 49.862  1.00 72.26  ?  234  GLU A O   1 
ATOM   1571 C CB  . GLU A 1 217 ? -13.085 -18.057 47.335  1.00 66.31  ?  234  GLU A CB  1 
ATOM   1572 C CG  . GLU A 1 217 ? -13.971 -16.933 46.814  1.00 71.69  ?  234  GLU A CG  1 
ATOM   1573 C CD  . GLU A 1 217 ? -13.213 -15.629 46.646  1.00 76.89  ?  234  GLU A CD  1 
ATOM   1574 O OE1 . GLU A 1 217 ? -13.665 -14.599 47.188  1.00 66.47  ?  234  GLU A OE1 1 
ATOM   1575 O OE2 . GLU A 1 217 ? -12.157 -15.635 45.980  1.00 77.02  -1 234  GLU A OE2 1 
ATOM   1576 N N   . LYS A 1 218 ? -13.144 -18.287 50.662  1.00 66.69  ?  235  LYS A N   1 
ATOM   1577 C CA  . LYS A 1 218 ? -13.817 -17.988 51.922  1.00 73.11  ?  235  LYS A CA  1 
ATOM   1578 C C   . LYS A 1 218 ? -12.988 -17.045 52.784  1.00 71.25  ?  235  LYS A C   1 
ATOM   1579 O O   . LYS A 1 218 ? -13.547 -16.309 53.606  1.00 75.19  ?  235  LYS A O   1 
ATOM   1580 C CB  . LYS A 1 218 ? -14.119 -19.279 52.687  1.00 68.57  ?  235  LYS A CB  1 
ATOM   1581 C CG  . LYS A 1 218 ? -15.056 -20.236 51.962  1.00 76.03  ?  235  LYS A CG  1 
ATOM   1582 C CD  . LYS A 1 218 ? -15.352 -21.478 52.795  1.00 75.16  ?  235  LYS A CD  1 
ATOM   1583 C CE  . LYS A 1 218 ? -16.530 -21.270 53.735  1.00 82.88  ?  235  LYS A CE  1 
ATOM   1584 N NZ  . LYS A 1 218 ? -17.837 -21.410 53.032  1.00 81.04  1  235  LYS A NZ  1 
ATOM   1585 N N   . SER A 1 219 ? -11.663 -17.053 52.619  1.00 62.64  ?  236  SER A N   1 
ATOM   1586 C CA  . SER A 1 219 ? -10.826 -16.107 53.350  1.00 69.63  ?  236  SER A CA  1 
ATOM   1587 C C   . SER A 1 219 ? -10.982 -14.696 52.797  1.00 74.09  ?  236  SER A C   1 
ATOM   1588 O O   . SER A 1 219 ? -10.975 -13.722 53.559  1.00 74.74  ?  236  SER A O   1 
ATOM   1589 C CB  . SER A 1 219 ? -9.362  -16.545 53.302  1.00 65.73  ?  236  SER A CB  1 
ATOM   1590 O OG  . SER A 1 219 ? -9.130  -17.656 54.151  1.00 86.14  ?  236  SER A OG  1 
ATOM   1591 N N   . PHE A 1 220 ? -11.122 -14.565 51.475  1.00 71.74  ?  237  PHE A N   1 
ATOM   1592 C CA  . PHE A 1 220 ? -11.354 -13.250 50.886  1.00 64.12  ?  237  PHE A CA  1 
ATOM   1593 C C   . PHE A 1 220 ? -12.707 -12.690 51.304  1.00 73.04  ?  237  PHE A C   1 
ATOM   1594 O O   . PHE A 1 220 ? -12.819 -11.504 51.636  1.00 74.71  ?  237  PHE A O   1 
ATOM   1595 C CB  . PHE A 1 220 ? -11.260 -13.325 49.362  1.00 59.12  ?  237  PHE A CB  1 
ATOM   1596 C CG  . PHE A 1 220 ? -9.871  -13.573 48.850  1.00 57.03  ?  237  PHE A CG  1 
ATOM   1597 C CD1 . PHE A 1 220 ? -8.853  -12.671 49.110  1.00 61.37  ?  237  PHE A CD1 1 
ATOM   1598 C CD2 . PHE A 1 220 ? -9.588  -14.696 48.092  1.00 58.24  ?  237  PHE A CD2 1 
ATOM   1599 C CE1 . PHE A 1 220 ? -7.574  -12.892 48.635  1.00 51.84  ?  237  PHE A CE1 1 
ATOM   1600 C CE2 . PHE A 1 220 ? -8.311  -14.922 47.613  1.00 58.69  ?  237  PHE A CE2 1 
ATOM   1601 C CZ  . PHE A 1 220 ? -7.303  -14.018 47.886  1.00 56.48  ?  237  PHE A CZ  1 
ATOM   1602 N N   . GLU A 1 221 ? -13.747 -13.528 51.291  1.00 66.44  ?  238  GLU A N   1 
ATOM   1603 C CA  . GLU A 1 221 ? -15.070 -13.073 51.705  1.00 70.49  ?  238  GLU A CA  1 
ATOM   1604 C C   . GLU A 1 221 ? -15.087 -12.665 53.172  1.00 74.98  ?  238  GLU A C   1 
ATOM   1605 O O   . GLU A 1 221 ? -15.849 -11.772 53.559  1.00 79.28  ?  238  GLU A O   1 
ATOM   1606 C CB  . GLU A 1 221 ? -16.104 -14.167 51.437  1.00 70.15  ?  238  GLU A CB  1 
ATOM   1607 C CG  . GLU A 1 221 ? -16.257 -14.514 49.964  1.00 75.98  ?  238  GLU A CG  1 
ATOM   1608 C CD  . GLU A 1 221 ? -17.070 -15.772 49.739  1.00 86.84  ?  238  GLU A CD  1 
ATOM   1609 O OE1 . GLU A 1 221 ? -17.359 -16.089 48.566  1.00 83.03  ?  238  GLU A OE1 1 
ATOM   1610 O OE2 . GLU A 1 221 ? -17.416 -16.445 50.734  1.00 87.25  -1 238  GLU A OE2 1 
ATOM   1611 N N   . THR A 1 222 ? -14.254 -13.301 53.999  1.00 69.80  ?  239  THR A N   1 
ATOM   1612 C CA  . THR A 1 222 ? -14.129 -12.880 55.390  1.00 69.90  ?  239  THR A CA  1 
ATOM   1613 C C   . THR A 1 222 ? -13.452 -11.516 55.493  1.00 73.96  ?  239  THR A C   1 
ATOM   1614 O O   . THR A 1 222 ? -13.878 -10.664 56.282  1.00 82.41  ?  239  THR A O   1 
ATOM   1615 C CB  . THR A 1 222 ? -13.351 -13.928 56.191  1.00 78.04  ?  239  THR A CB  1 
ATOM   1616 O OG1 . THR A 1 222 ? -14.090 -15.157 56.230  1.00 76.99  ?  239  THR A OG1 1 
ATOM   1617 C CG2 . THR A 1 222 ? -13.106 -13.447 57.612  1.00 69.75  ?  239  THR A CG2 1 
ATOM   1618 N N   . LEU A 1 223 ? -12.404 -11.289 54.693  1.00 75.44  ?  240  LEU A N   1 
ATOM   1619 C CA  . LEU A 1 223 ? -11.672 -10.026 54.749  1.00 72.55  ?  240  LEU A CA  1 
ATOM   1620 C C   . LEU A 1 223 ? -12.518 -8.851  54.282  1.00 72.59  ?  240  LEU A C   1 
ATOM   1621 O O   . LEU A 1 223 ? -12.366 -7.736  54.792  1.00 78.06  ?  240  LEU A O   1 
ATOM   1622 C CB  . LEU A 1 223 ? -10.391 -10.126 53.919  1.00 61.67  ?  240  LEU A CB  1 
ATOM   1623 C CG  . LEU A 1 223 ? -9.131  -10.471 54.716  1.00 66.64  ?  240  LEU A CG  1 
ATOM   1624 C CD1 . LEU A 1 223 ? -7.943  -10.573 53.780  1.00 61.85  ?  240  LEU A CD1 1 
ATOM   1625 C CD2 . LEU A 1 223 ? -8.888  -9.422  55.795  1.00 59.49  ?  240  LEU A CD2 1 
ATOM   1626 N N   . VAL A 1 224 ? -13.398 -9.068  53.306  1.00 73.81  ?  241  VAL A N   1 
ATOM   1627 C CA  . VAL A 1 224 ? -14.336 -8.036  52.884  1.00 69.44  ?  241  VAL A CA  1 
ATOM   1628 C C   . VAL A 1 224 ? -15.653 -8.079  53.643  1.00 81.05  ?  241  VAL A C   1 
ATOM   1629 O O   . VAL A 1 224 ? -16.561 -7.303  53.316  1.00 71.63  ?  241  VAL A O   1 
ATOM   1630 C CB  . VAL A 1 224 ? -14.599 -8.124  51.368  1.00 67.61  ?  241  VAL A CB  1 
ATOM   1631 C CG1 . VAL A 1 224 ? -13.295 -7.986  50.595  1.00 57.97  ?  241  VAL A CG1 1 
ATOM   1632 C CG2 . VAL A 1 224 ? -15.280 -9.430  51.016  1.00 77.00  ?  241  VAL A CG2 1 
ATOM   1633 N N   . GLN A 1 225 ? -15.785 -8.951  54.646  1.00 75.78  ?  242  GLN A N   1 
ATOM   1634 C CA  . GLN A 1 225 ? -16.966 -8.999  55.513  1.00 76.29  ?  242  GLN A CA  1 
ATOM   1635 C C   . GLN A 1 225 ? -18.254 -9.246  54.727  1.00 75.50  ?  242  GLN A C   1 
ATOM   1636 O O   . GLN A 1 225 ? -19.296 -8.648  55.001  1.00 76.69  ?  242  GLN A O   1 
ATOM   1637 C CB  . GLN A 1 225 ? -17.075 -7.727  56.355  1.00 77.88  ?  242  GLN A CB  1 
ATOM   1638 C CG  . GLN A 1 225 ? -15.931 -7.545  57.342  1.00 82.19  ?  242  GLN A CG  1 
ATOM   1639 C CD  . GLN A 1 225 ? -15.696 -6.092  57.707  1.00 86.07  ?  242  GLN A CD  1 
ATOM   1640 O OE1 . GLN A 1 225 ? -15.891 -5.196  56.887  1.00 86.63  ?  242  GLN A OE1 1 
ATOM   1641 N NE2 . GLN A 1 225 ? -15.271 -5.853  58.943  1.00 96.06  ?  242  GLN A NE2 1 
ATOM   1642 N N   . LYS A 1 226 ? -18.185 -10.164 53.769  1.00 78.34  ?  243  LYS A N   1 
ATOM   1643 C CA  . LYS A 1 226 ? -19.333 -10.565 52.970  1.00 72.13  ?  243  LYS A CA  1 
ATOM   1644 C C   . LYS A 1 226 ? -19.841 -11.905 53.481  1.00 82.07  ?  243  LYS A C   1 
ATOM   1645 O O   . LYS A 1 226 ? -19.132 -12.915 53.400  1.00 77.42  ?  243  LYS A O   1 
ATOM   1646 C CB  . LYS A 1 226 ? -18.961 -10.661 51.492  1.00 77.02  ?  243  LYS A CB  1 
ATOM   1647 C CG  . LYS A 1 226 ? -20.104 -11.132 50.610  1.00 77.44  ?  243  LYS A CG  1 
ATOM   1648 C CD  . LYS A 1 226 ? -21.301 -10.195 50.706  1.00 73.53  ?  243  LYS A CD  1 
ATOM   1649 C CE  . LYS A 1 226 ? -22.443 -10.662 49.814  1.00 74.89  ?  243  LYS A CE  1 
ATOM   1650 N NZ  . LYS A 1 226 ? -23.530 -9.649  49.713  1.00 96.63  1  243  LYS A NZ  1 
ATOM   1651 N N   . THR A 1 227 ? -21.062 -11.910 54.000  1.00 80.83  ?  244  THR A N   1 
ATOM   1652 C CA  . THR A 1 227 ? -21.670 -13.097 54.574  1.00 83.33  ?  244  THR A CA  1 
ATOM   1653 C C   . THR A 1 227 ? -22.683 -13.699 53.609  1.00 90.60  ?  244  THR A C   1 
ATOM   1654 O O   . THR A 1 227 ? -23.318 -12.991 52.821  1.00 95.41  ?  244  THR A O   1 
ATOM   1655 C CB  . THR A 1 227 ? -22.359 -12.765 55.901  1.00 84.54  ?  244  THR A CB  1 
ATOM   1656 O OG1 . THR A 1 227 ? -23.438 -11.850 55.666  1.00 77.94  ?  244  THR A OG1 1 
ATOM   1657 C CG2 . THR A 1 227 ? -21.374 -12.136 56.874  1.00 79.17  ?  244  THR A CG2 1 
ATOM   1658 N N   . GLY A 1 228 ? -22.823 -15.022 53.674  1.00 82.95  ?  245  GLY A N   1 
ATOM   1659 C CA  . GLY A 1 228 ? -23.878 -15.724 52.976  1.00 80.19  ?  245  GLY A CA  1 
ATOM   1660 C C   . GLY A 1 228 ? -23.517 -16.317 51.631  1.00 93.84  ?  245  GLY A C   1 
ATOM   1661 O O   . GLY A 1 228 ? -24.388 -16.923 50.996  1.00 90.09  ?  245  GLY A O   1 
ATOM   1662 N N   . CYS A 1 229 ? -22.278 -16.167 51.170  1.00 90.48  ?  246  CYS A N   1 
ATOM   1663 C CA  . CYS A 1 229 ? -21.891 -16.730 49.884  1.00 87.68  ?  246  CYS A CA  1 
ATOM   1664 C C   . CYS A 1 229 ? -21.641 -18.229 50.009  1.00 87.62  ?  246  CYS A C   1 
ATOM   1665 O O   . CYS A 1 229 ? -21.080 -18.700 51.002  1.00 82.01  ?  246  CYS A O   1 
ATOM   1666 C CB  . CYS A 1 229 ? -20.637 -16.046 49.336  1.00 93.22  ?  246  CYS A CB  1 
ATOM   1667 S SG  . CYS A 1 229 ? -20.763 -14.267 49.002  1.00 94.02  ?  246  CYS A SG  1 
ATOM   1668 N N   . THR A 1 230 ? -22.068 -18.978 48.990  1.00 92.11  ?  247  THR A N   1 
ATOM   1669 C CA  . THR A 1 230 ? -21.844 -20.416 48.929  1.00 84.65  ?  247  THR A CA  1 
ATOM   1670 C C   . THR A 1 230 ? -21.131 -20.856 47.657  1.00 83.64  ?  247  THR A C   1 
ATOM   1671 O O   . THR A 1 230 ? -20.936 -22.061 47.461  1.00 77.47  ?  247  THR A O   1 
ATOM   1672 C CB  . THR A 1 230 ? -23.172 -21.180 49.048  1.00 77.13  ?  247  THR A CB  1 
ATOM   1673 O OG1 . THR A 1 230 ? -23.950 -20.982 47.860  1.00 83.67  ?  247  THR A OG1 1 
ATOM   1674 C CG2 . THR A 1 230 ? -23.968 -20.699 50.254  1.00 78.82  ?  247  THR A CG2 1 
ATOM   1675 N N   . ASP A 1 231 ? -20.742 -19.926 46.792  1.00 93.39  ?  248  ASP A N   1 
ATOM   1676 C CA  . ASP A 1 231 ? -20.061 -20.246 45.536  1.00 91.76  ?  248  ASP A CA  1 
ATOM   1677 C C   . ASP A 1 231 ? -18.553 -20.075 45.666  1.00 76.92  ?  248  ASP A C   1 
ATOM   1678 O O   . ASP A 1 231 ? -17.903 -19.441 44.834  1.00 72.02  ?  248  ASP A O   1 
ATOM   1679 C CB  . ASP A 1 231 ? -20.613 -19.385 44.407  1.00 76.63  ?  248  ASP A CB  1 
ATOM   1680 C CG  . ASP A 1 231 ? -22.056 -19.714 44.075  1.00 89.68  ?  248  ASP A CG  1 
ATOM   1681 O OD1 . ASP A 1 231 ? -22.919 -19.581 44.968  1.00 93.05  ?  248  ASP A OD1 1 
ATOM   1682 O OD2 . ASP A 1 231 ? -22.326 -20.102 42.919  1.00 89.49  -1 248  ASP A OD2 1 
ATOM   1683 N N   . ASN A 1 232 ? -17.980 -20.649 46.719  1.00 79.70  ?  249  ASN A N   1 
ATOM   1684 C CA  . ASN A 1 232 ? -16.561 -20.527 47.028  1.00 82.10  ?  249  ASN A CA  1 
ATOM   1685 C C   . ASN A 1 232 ? -15.933 -21.901 47.217  1.00 77.88  ?  249  ASN A C   1 
ATOM   1686 O O   . ASN A 1 232 ? -15.136 -22.123 48.133  1.00 77.93  ?  249  ASN A O   1 
ATOM   1687 C CB  . ASN A 1 232 ? -16.353 -19.656 48.264  1.00 77.31  ?  249  ASN A CB  1 
ATOM   1688 C CG  . ASN A 1 232 ? -17.354 -19.958 49.362  1.00 80.48  ?  249  ASN A CG  1 
ATOM   1689 O OD1 . ASN A 1 232 ? -17.784 -21.099 49.532  1.00 86.13  ?  249  ASN A OD1 1 
ATOM   1690 N ND2 . ASN A 1 232 ? -17.740 -18.930 50.109  1.00 89.53  ?  249  ASN A ND2 1 
ATOM   1691 N N   . GLY A 1 233 ? -16.281 -22.844 46.342  1.00 74.71  ?  250  GLY A N   1 
ATOM   1692 C CA  . GLY A 1 233 ? -15.817 -24.211 46.479  1.00 85.91  ?  250  GLY A CA  1 
ATOM   1693 C C   . GLY A 1 233 ? -14.430 -24.491 45.945  1.00 78.08  ?  250  GLY A C   1 
ATOM   1694 O O   . GLY A 1 233 ? -13.936 -25.609 46.119  1.00 84.92  ?  250  GLY A O   1 
ATOM   1695 N N   . PHE A 1 234 ? -13.794 -23.513 45.302  1.00 73.04  ?  251  PHE A N   1 
ATOM   1696 C CA  . PHE A 1 234 ? -12.457 -23.721 44.760  1.00 67.05  ?  251  PHE A CA  1 
ATOM   1697 C C   . PHE A 1 234 ? -11.472 -24.055 45.872  1.00 67.72  ?  251  PHE A C   1 
ATOM   1698 O O   . PHE A 1 234 ? -11.527 -23.487 46.967  1.00 68.89  ?  251  PHE A O   1 
ATOM   1699 C CB  . PHE A 1 234 ? -11.994 -22.476 44.000  1.00 73.58  ?  251  PHE A CB  1 
ATOM   1700 C CG  . PHE A 1 234 ? -10.553 -22.526 43.572  1.00 62.55  ?  251  PHE A CG  1 
ATOM   1701 C CD1 . PHE A 1 234 ? -10.182 -23.190 42.415  1.00 70.33  ?  251  PHE A CD1 1 
ATOM   1702 C CD2 . PHE A 1 234 ? -9.569  -21.903 44.324  1.00 60.41  ?  251  PHE A CD2 1 
ATOM   1703 C CE1 . PHE A 1 234 ? -8.857  -23.237 42.019  1.00 59.68  ?  251  PHE A CE1 1 
ATOM   1704 C CE2 . PHE A 1 234 ? -8.244  -21.947 43.935  1.00 57.46  ?  251  PHE A CE2 1 
ATOM   1705 C CZ  . PHE A 1 234 ? -7.888  -22.615 42.780  1.00 59.49  ?  251  PHE A CZ  1 
ATOM   1706 N N   . GLN A 1 235 ? -10.564 -24.985 45.585  1.00 72.09  ?  252  GLN A N   1 
ATOM   1707 C CA  . GLN A 1 235 ? -9.557  -25.431 46.540  1.00 68.98  ?  252  GLN A CA  1 
ATOM   1708 C C   . GLN A 1 235 ? -8.174  -25.162 45.968  1.00 64.34  ?  252  GLN A C   1 
ATOM   1709 O O   . GLN A 1 235 ? -7.807  -25.723 44.929  1.00 62.52  ?  252  GLN A O   1 
ATOM   1710 C CB  . GLN A 1 235 ? -9.728  -26.915 46.871  1.00 70.45  ?  252  GLN A CB  1 
ATOM   1711 C CG  . GLN A 1 235 ? -10.896 -27.208 47.796  1.00 73.09  ?  252  GLN A CG  1 
ATOM   1712 C CD  . GLN A 1 235 ? -10.988 -28.673 48.172  1.00 71.51  ?  252  GLN A CD  1 
ATOM   1713 O OE1 . GLN A 1 235 ? -10.909 -29.552 47.315  1.00 86.19  ?  252  GLN A OE1 1 
ATOM   1714 N NE2 . GLN A 1 235 ? -11.149 -28.943 49.462  1.00 79.76  ?  252  GLN A NE2 1 
ATOM   1715 N N   . GLY A 1 236 ? -7.413  -24.312 46.647  1.00 64.75  ?  253  GLY A N   1 
ATOM   1716 C CA  . GLY A 1 236 ? -6.079  -23.978 46.197  1.00 65.00  ?  253  GLY A CA  1 
ATOM   1717 C C   . GLY A 1 236 ? -5.478  -22.894 47.069  1.00 64.99  ?  253  GLY A C   1 
ATOM   1718 O O   . GLY A 1 236 ? -6.025  -22.535 48.114  1.00 64.79  ?  253  GLY A O   1 
ATOM   1719 N N   . TYR A 1 237 ? -4.339  -22.379 46.614  1.00 56.56  ?  254  TYR A N   1 
ATOM   1720 C CA  . TYR A 1 237 ? -3.616  -21.346 47.345  1.00 56.23  ?  254  TYR A CA  1 
ATOM   1721 C C   . TYR A 1 237 ? -2.705  -20.606 46.372  1.00 61.75  ?  254  TYR A C   1 
ATOM   1722 O O   . TYR A 1 237 ? -2.669  -20.903 45.174  1.00 57.16  ?  254  TYR A O   1 
ATOM   1723 C CB  . TYR A 1 237 ? -2.828  -21.947 48.513  1.00 54.95  ?  254  TYR A CB  1 
ATOM   1724 C CG  . TYR A 1 237 ? -1.772  -22.953 48.107  1.00 63.82  ?  254  TYR A CG  1 
ATOM   1725 C CD1 . TYR A 1 237 ? -2.075  -24.303 47.998  1.00 58.66  ?  254  TYR A CD1 1 
ATOM   1726 C CD2 . TYR A 1 237 ? -0.467  -22.554 47.844  1.00 67.71  ?  254  TYR A CD2 1 
ATOM   1727 C CE1 . TYR A 1 237 ? -1.111  -25.225 47.633  1.00 67.34  ?  254  TYR A CE1 1 
ATOM   1728 C CE2 . TYR A 1 237 ? 0.502   -23.470 47.480  1.00 59.46  ?  254  TYR A CE2 1 
ATOM   1729 C CZ  . TYR A 1 237 ? 0.176   -24.802 47.376  1.00 60.77  ?  254  TYR A CZ  1 
ATOM   1730 O OH  . TYR A 1 237 ? 1.141   -25.713 47.012  1.00 64.36  ?  254  TYR A OH  1 
ATOM   1731 N N   . TYR A 1 238 ? -1.966  -19.634 46.903  1.00 51.59  ?  255  TYR A N   1 
ATOM   1732 C CA  . TYR A 1 238 ? -1.033  -18.824 46.131  1.00 57.74  ?  255  TYR A CA  1 
ATOM   1733 C C   . TYR A 1 238 ? 0.375   -18.981 46.686  1.00 55.04  ?  255  TYR A C   1 
ATOM   1734 O O   . TYR A 1 238 ? 0.564   -19.106 47.900  1.00 52.63  ?  255  TYR A O   1 
ATOM   1735 C CB  . TYR A 1 238 ? -1.425  -17.341 46.156  1.00 53.19  ?  255  TYR A CB  1 
ATOM   1736 C CG  . TYR A 1 238 ? -2.519  -16.959 45.186  1.00 49.62  ?  255  TYR A CG  1 
ATOM   1737 C CD1 . TYR A 1 238 ? -3.844  -16.887 45.594  1.00 49.45  ?  255  TYR A CD1 1 
ATOM   1738 C CD2 . TYR A 1 238 ? -2.224  -16.661 43.862  1.00 48.42  ?  255  TYR A CD2 1 
ATOM   1739 C CE1 . TYR A 1 238 ? -4.846  -16.533 44.709  1.00 49.48  ?  255  TYR A CE1 1 
ATOM   1740 C CE2 . TYR A 1 238 ? -3.218  -16.305 42.970  1.00 48.44  ?  255  TYR A CE2 1 
ATOM   1741 C CZ  . TYR A 1 238 ? -4.528  -16.243 43.400  1.00 56.93  ?  255  TYR A CZ  1 
ATOM   1742 O OH  . TYR A 1 238 ? -5.523  -15.891 42.517  1.00 56.05  ?  255  TYR A OH  1 
ATOM   1743 N N   . VAL A 1 239 ? 1.360   -18.971 45.792  1.00 53.88  ?  256  VAL A N   1 
ATOM   1744 C CA  . VAL A 1 239 ? 2.771   -18.963 46.160  1.00 55.63  ?  256  VAL A CA  1 
ATOM   1745 C C   . VAL A 1 239 ? 3.368   -17.653 45.668  1.00 57.36  ?  256  VAL A C   1 
ATOM   1746 O O   . VAL A 1 239 ? 3.426   -17.407 44.456  1.00 64.83  ?  256  VAL A O   1 
ATOM   1747 C CB  . VAL A 1 239 ? 3.530   -20.164 45.574  1.00 52.84  ?  256  VAL A CB  1 
ATOM   1748 C CG1 . VAL A 1 239 ? 4.999   -20.088 45.948  1.00 63.28  ?  256  VAL A CG1 1 
ATOM   1749 C CG2 . VAL A 1 239 ? 2.928   -21.463 46.067  1.00 56.57  ?  256  VAL A CG2 1 
ATOM   1750 N N   . CYS A 1 240 ? 3.808   -16.816 46.603  1.00 64.98  ?  257  CYS A N   1 
ATOM   1751 C CA  . CYS A 1 240 ? 4.347   -15.500 46.298  1.00 58.12  ?  257  CYS A CA  1 
ATOM   1752 C C   . CYS A 1 240 ? 5.866   -15.496 46.413  1.00 51.73  ?  257  CYS A C   1 
ATOM   1753 O O   . CYS A 1 240 ? 6.458   -16.285 47.154  1.00 64.35  ?  257  CYS A O   1 
ATOM   1754 C CB  . CYS A 1 240 ? 3.766   -14.444 47.241  1.00 52.55  ?  257  CYS A CB  1 
ATOM   1755 S SG  . CYS A 1 240 ? 2.516   -13.324 46.552  1.00 83.34  ?  257  CYS A SG  1 
ATOM   1756 N N   . LEU A 1 241 ? 6.492   -14.586 45.670  1.00 57.77  ?  258  LEU A N   1 
ATOM   1757 C CA  . LEU A 1 241 ? 7.920   -14.321 45.773  1.00 50.67  ?  258  LEU A CA  1 
ATOM   1758 C C   . LEU A 1 241 ? 8.117   -12.821 45.919  1.00 57.58  ?  258  LEU A C   1 
ATOM   1759 O O   . LEU A 1 241 ? 7.552   -12.039 45.148  1.00 63.59  ?  258  LEU A O   1 
ATOM   1760 C CB  . LEU A 1 241 ? 8.678   -14.853 44.553  1.00 51.19  ?  258  LEU A CB  1 
ATOM   1761 C CG  . LEU A 1 241 ? 9.101   -16.322 44.629  1.00 60.89  ?  258  LEU A CG  1 
ATOM   1762 C CD1 . LEU A 1 241 ? 9.524   -16.832 43.264  1.00 61.87  ?  258  LEU A CD1 1 
ATOM   1763 C CD2 . LEU A 1 241 ? 10.229  -16.496 45.634  1.00 54.57  ?  258  LEU A CD2 1 
ATOM   1764 N N   . ILE A 1 242 ? 8.908   -12.425 46.910  1.00 62.16  ?  259  ILE A N   1 
ATOM   1765 C CA  . ILE A 1 242 ? 9.096   -11.019 47.247  1.00 51.88  ?  259  ILE A CA  1 
ATOM   1766 C C   . ILE A 1 242 ? 10.302  -10.480 46.490  1.00 60.16  ?  259  ILE A C   1 
ATOM   1767 O O   . ILE A 1 242 ? 11.371  -11.103 46.480  1.00 61.98  ?  259  ILE A O   1 
ATOM   1768 C CB  . ILE A 1 242 ? 9.271   -10.840 48.764  1.00 51.52  ?  259  ILE A CB  1 
ATOM   1769 C CG1 . ILE A 1 242 ? 8.003   -11.280 49.498  1.00 55.96  ?  259  ILE A CG1 1 
ATOM   1770 C CG2 . ILE A 1 242 ? 9.621   -9.401  49.099  1.00 56.36  ?  259  ILE A CG2 1 
ATOM   1771 C CD1 . ILE A 1 242 ? 8.071   -11.100 50.999  1.00 57.56  ?  259  ILE A CD1 1 
ATOM   1772 N N   . GLY A 1 243 ? 10.130  -9.320  45.859  1.00 54.25  ?  260  GLY A N   1 
ATOM   1773 C CA  . GLY A 1 243 ? 11.219  -8.711  45.116  1.00 45.72  ?  260  GLY A CA  1 
ATOM   1774 C C   . GLY A 1 243 ? 11.645  -9.577  43.949  1.00 56.58  ?  260  GLY A C   1 
ATOM   1775 O O   . GLY A 1 243 ? 10.820  -10.188 43.259  1.00 65.87  ?  260  GLY A O   1 
ATOM   1776 N N   . SER A 1 244 ? 12.955  -9.631  43.719  1.00 53.88  ?  261  SER A N   1 
ATOM   1777 C CA  . SER A 1 244 ? 13.525  -10.502 42.702  1.00 65.64  ?  261  SER A CA  1 
ATOM   1778 C C   . SER A 1 244 ? 14.147  -11.763 43.285  1.00 63.54  ?  261  SER A C   1 
ATOM   1779 O O   . SER A 1 244 ? 14.483  -12.677 42.524  1.00 56.82  ?  261  SER A O   1 
ATOM   1780 C CB  . SER A 1 244 ? 14.581  -9.748  41.882  1.00 49.78  ?  261  SER A CB  1 
ATOM   1781 O OG  . SER A 1 244 ? 15.719  -9.447  42.670  1.00 61.87  ?  261  SER A OG  1 
ATOM   1782 N N   . SER A 1 245 ? 14.301  -11.837 44.605  1.00 56.83  ?  262  SER A N   1 
ATOM   1783 C CA  . SER A 1 245 ? 14.925  -12.990 45.245  1.00 57.93  ?  262  SER A CA  1 
ATOM   1784 C C   . SER A 1 245 ? 14.417  -13.102 46.673  1.00 64.59  ?  262  SER A C   1 
ATOM   1785 O O   . SER A 1 245 ? 14.542  -12.150 47.450  1.00 65.42  ?  262  SER A O   1 
ATOM   1786 C CB  . SER A 1 245 ? 16.450  -12.870 45.225  1.00 60.41  ?  262  SER A CB  1 
ATOM   1787 O OG  . SER A 1 245 ? 17.048  -13.867 46.035  1.00 61.96  ?  262  SER A OG  1 
ATOM   1788 N N   . SER A 1 246 ? 13.854  -14.259 47.013  1.00 56.52  ?  263  SER A N   1 
ATOM   1789 C CA  . SER A 1 246 ? 13.369  -14.536 48.360  1.00 59.94  ?  263  SER A CA  1 
ATOM   1790 C C   . SER A 1 246 ? 13.000  -16.011 48.437  1.00 56.34  ?  263  SER A C   1 
ATOM   1791 O O   . SER A 1 246 ? 13.037  -16.735 47.439  1.00 56.25  ?  263  SER A O   1 
ATOM   1792 C CB  . SER A 1 246 ? 12.164  -13.664 48.725  1.00 52.45  ?  263  SER A CB  1 
ATOM   1793 O OG  . SER A 1 246 ? 11.019  -14.041 47.979  1.00 54.43  ?  263  SER A OG  1 
ATOM   1794 N N   . GLU A 1 247 ? 12.646  -16.446 49.643  1.00 56.99  ?  264  GLU A N   1 
ATOM   1795 C CA  . GLU A 1 247 ? 12.065  -17.767 49.808  1.00 55.88  ?  264  GLU A CA  1 
ATOM   1796 C C   . GLU A 1 247 ? 10.584  -17.733 49.435  1.00 62.51  ?  264  GLU A C   1 
ATOM   1797 O O   . GLU A 1 247 ? 9.909   -16.721 49.643  1.00 58.39  ?  264  GLU A O   1 
ATOM   1798 C CB  . GLU A 1 247 ? 12.225  -18.249 51.246  1.00 52.04  ?  264  GLU A CB  1 
ATOM   1799 C CG  . GLU A 1 247 ? 13.647  -18.625 51.628  1.00 57.57  ?  264  GLU A CG  1 
ATOM   1800 C CD  . GLU A 1 247 ? 13.767  -19.048 53.080  1.00 69.14  ?  264  GLU A CD  1 
ATOM   1801 O OE1 . GLU A 1 247 ? 12.741  -19.034 53.792  1.00 79.32  ?  264  GLU A OE1 1 
ATOM   1802 O OE2 . GLU A 1 247 ? 14.888  -19.391 53.512  1.00 88.16  -1 264  GLU A OE2 1 
ATOM   1803 N N   . PRO A 1 248 ? 10.061  -18.821 48.870  1.00 55.33  ?  265  PRO A N   1 
ATOM   1804 C CA  . PRO A 1 248 ? 8.645   -18.841 48.485  1.00 54.05  ?  265  PRO A CA  1 
ATOM   1805 C C   . PRO A 1 248 ? 7.739   -18.631 49.690  1.00 52.52  ?  265  PRO A C   1 
ATOM   1806 O O   . PRO A 1 248 ? 8.021   -19.102 50.793  1.00 59.58  ?  265  PRO A O   1 
ATOM   1807 C CB  . PRO A 1 248 ? 8.461   -20.236 47.877  1.00 60.36  ?  265  PRO A CB  1 
ATOM   1808 C CG  . PRO A 1 248 ? 9.833   -20.644 47.446  1.00 52.71  ?  265  PRO A CG  1 
ATOM   1809 C CD  . PRO A 1 248 ? 10.761  -20.051 48.464  1.00 57.63  ?  265  PRO A CD  1 
ATOM   1810 N N   . LEU A 1 249 ? 6.642   -17.912 49.466  1.00 58.68  ?  266  LEU A N   1 
ATOM   1811 C CA  . LEU A 1 249 ? 5.701   -17.554 50.518  1.00 49.43  ?  266  LEU A CA  1 
ATOM   1812 C C   . LEU A 1 249 ? 4.357   -18.214 50.245  1.00 57.18  ?  266  LEU A C   1 
ATOM   1813 O O   . LEU A 1 249 ? 3.797   -18.063 49.155  1.00 61.01  ?  266  LEU A O   1 
ATOM   1814 C CB  . LEU A 1 249 ? 5.540   -16.034 50.612  1.00 50.95  ?  266  LEU A CB  1 
ATOM   1815 C CG  . LEU A 1 249 ? 4.588   -15.513 51.690  1.00 59.76  ?  266  LEU A CG  1 
ATOM   1816 C CD1 . LEU A 1 249 ? 5.046   -15.954 53.071  1.00 64.63  ?  266  LEU A CD1 1 
ATOM   1817 C CD2 . LEU A 1 249 ? 4.473   -13.996 51.618  1.00 60.61  ?  266  LEU A CD2 1 
ATOM   1818 N N   . TYR A 1 250 ? 3.845   -18.940 51.237  1.00 57.68  ?  267  TYR A N   1 
ATOM   1819 C CA  . TYR A 1 250 ? 2.566   -19.627 51.127  1.00 52.57  ?  267  TYR A CA  1 
ATOM   1820 C C   . TYR A 1 250 ? 1.448   -18.688 51.565  1.00 56.28  ?  267  TYR A C   1 
ATOM   1821 O O   . TYR A 1 250 ? 1.483   -18.148 52.674  1.00 72.91  ?  267  TYR A O   1 
ATOM   1822 C CB  . TYR A 1 250 ? 2.565   -20.898 51.982  1.00 69.05  ?  267  TYR A CB  1 
ATOM   1823 C CG  . TYR A 1 250 ? 1.361   -21.798 51.789  1.00 61.54  ?  267  TYR A CG  1 
ATOM   1824 C CD1 . TYR A 1 250 ? 1.456   -22.971 51.051  1.00 66.26  ?  267  TYR A CD1 1 
ATOM   1825 C CD2 . TYR A 1 250 ? 0.131   -21.483 52.355  1.00 63.25  ?  267  TYR A CD2 1 
ATOM   1826 C CE1 . TYR A 1 250 ? 0.360   -23.801 50.878  1.00 58.12  ?  267  TYR A CE1 1 
ATOM   1827 C CE2 . TYR A 1 250 ? -0.969  -22.302 52.183  1.00 63.85  ?  267  TYR A CE2 1 
ATOM   1828 C CZ  . TYR A 1 250 ? -0.850  -23.459 51.444  1.00 59.23  ?  267  TYR A CZ  1 
ATOM   1829 O OH  . TYR A 1 250 ? -1.942  -24.279 51.272  1.00 61.63  ?  267  TYR A OH  1 
ATOM   1830 N N   . ILE A 1 251 ? 0.461   -18.502 50.696  1.00 59.83  ?  268  ILE A N   1 
ATOM   1831 C CA  . ILE A 1 251 ? -0.700  -17.667 50.975  1.00 60.20  ?  268  ILE A CA  1 
ATOM   1832 C C   . ILE A 1 251 ? -1.933  -18.562 50.951  1.00 63.14  ?  268  ILE A C   1 
ATOM   1833 O O   . ILE A 1 251 ? -2.222  -19.185 49.926  1.00 70.46  ?  268  ILE A O   1 
ATOM   1834 C CB  . ILE A 1 251 ? -0.846  -16.519 49.961  1.00 59.77  ?  268  ILE A CB  1 
ATOM   1835 C CG1 . ILE A 1 251 ? 0.469   -15.751 49.825  1.00 57.69  ?  268  ILE A CG1 1 
ATOM   1836 C CG2 . ILE A 1 251 ? -1.971  -15.581 50.375  1.00 58.59  ?  268  ILE A CG2 1 
ATOM   1837 C CD1 . ILE A 1 251 ? 0.959   -15.154 51.119  1.00 59.99  ?  268  ILE A CD1 1 
ATOM   1838 N N   . PRO A 1 252 ? -2.706  -18.653 52.045  1.00 67.00  ?  269  PRO A N   1 
ATOM   1839 C CA  . PRO A 1 252 ? -2.468  -17.940 53.302  1.00 67.21  ?  269  PRO A CA  1 
ATOM   1840 C C   . PRO A 1 252 ? -1.778  -18.770 54.386  1.00 63.48  ?  269  PRO A C   1 
ATOM   1841 O O   . PRO A 1 252 ? -2.062  -19.959 54.540  1.00 71.95  ?  269  PRO A O   1 
ATOM   1842 C CB  . PRO A 1 252 ? -3.881  -17.569 53.742  1.00 62.64  ?  269  PRO A CB  1 
ATOM   1843 C CG  . PRO A 1 252 ? -4.710  -18.726 53.270  1.00 54.84  ?  269  PRO A CG  1 
ATOM   1844 C CD  . PRO A 1 252 ? -4.044  -19.268 52.018  1.00 63.50  ?  269  PRO A CD  1 
ATOM   1845 N N   . THR A 1 253 ? -0.877  -18.135 55.127  1.00 70.57  ?  270  THR A N   1 
ATOM   1846 C CA  . THR A 1 253 ? -0.292  -18.700 56.336  1.00 66.30  ?  270  THR A CA  1 
ATOM   1847 C C   . THR A 1 253 ? -0.782  -17.878 57.520  1.00 82.69  ?  270  THR A C   1 
ATOM   1848 O O   . THR A 1 253 ? -0.600  -16.656 57.551  1.00 87.28  ?  270  THR A O   1 
ATOM   1849 C CB  . THR A 1 253 ? 1.236   -18.706 56.270  1.00 78.47  ?  270  THR A CB  1 
ATOM   1850 O OG1 . THR A 1 253 ? 1.667   -19.611 55.245  1.00 66.75  ?  270  THR A OG1 1 
ATOM   1851 C CG2 . THR A 1 253 ? 1.823   -19.143 57.603  1.00 65.04  ?  270  THR A CG2 1 
ATOM   1852 N N   . LEU A 1 254 ? -1.399  -18.551 58.491  1.00 88.92  ?  271  LEU A N   1 
ATOM   1853 C CA  . LEU A 1 254 ? -2.183  -17.879 59.518  1.00 93.91  ?  271  LEU A CA  1 
ATOM   1854 C C   . LEU A 1 254 ? -1.340  -17.184 60.580  1.00 91.40  ?  271  LEU A C   1 
ATOM   1855 O O   . LEU A 1 254 ? -1.886  -16.384 61.347  1.00 87.65  ?  271  LEU A O   1 
ATOM   1856 C CB  . LEU A 1 254 ? -3.127  -18.883 60.186  1.00 87.97  ?  271  LEU A CB  1 
ATOM   1857 C CG  . LEU A 1 254 ? -3.894  -19.796 59.225  1.00 86.19  ?  271  LEU A CG  1 
ATOM   1858 C CD1 . LEU A 1 254 ? -3.216  -21.157 59.111  1.00 95.04  ?  271  LEU A CD1 1 
ATOM   1859 C CD2 . LEU A 1 254 ? -5.346  -19.946 59.651  1.00 101.24 ?  271  LEU A CD2 1 
ATOM   1860 N N   . ASP A 1 255 ? -0.040  -17.461 60.650  1.00 90.82  ?  272  ASP A N   1 
ATOM   1861 C CA  . ASP A 1 255 ? 0.837   -16.828 61.627  1.00 95.24  ?  272  ASP A CA  1 
ATOM   1862 C C   . ASP A 1 255 ? 1.892   -15.939 60.986  1.00 97.72  ?  272  ASP A C   1 
ATOM   1863 O O   . ASP A 1 255 ? 2.693   -15.332 61.705  1.00 105.13 ?  272  ASP A O   1 
ATOM   1864 C CB  . ASP A 1 255 ? 1.511   -17.895 62.498  1.00 105.83 ?  272  ASP A CB  1 
ATOM   1865 C CG  . ASP A 1 255 ? 2.344   -18.869 61.687  1.00 120.63 ?  272  ASP A CG  1 
ATOM   1866 O OD1 . ASP A 1 255 ? 3.582   -18.883 61.858  1.00 123.35 ?  272  ASP A OD1 1 
ATOM   1867 O OD2 . ASP A 1 255 ? 1.758   -19.610 60.869  1.00 124.97 -1 272  ASP A OD2 1 
ATOM   1868 N N   . ASP A 1 256 ? 1.913   -15.845 59.660  1.00 87.79  ?  273  ASP A N   1 
ATOM   1869 C CA  . ASP A 1 256 ? 2.868   -15.005 58.950  1.00 81.07  ?  273  ASP A CA  1 
ATOM   1870 C C   . ASP A 1 256 ? 2.230   -13.647 58.684  1.00 80.42  ?  273  ASP A C   1 
ATOM   1871 O O   . ASP A 1 256 ? 1.196   -13.564 58.012  1.00 80.94  ?  273  ASP A O   1 
ATOM   1872 C CB  . ASP A 1 256 ? 3.291   -15.665 57.639  1.00 75.86  ?  273  ASP A CB  1 
ATOM   1873 C CG  . ASP A 1 256 ? 4.602   -15.122 57.109  1.00 74.56  ?  273  ASP A CG  1 
ATOM   1874 O OD1 . ASP A 1 256 ? 5.591   -15.884 57.076  1.00 77.15  ?  273  ASP A OD1 1 
ATOM   1875 O OD2 . ASP A 1 256 ? 4.647   -13.930 56.738  1.00 73.01  -1 273  ASP A OD2 1 
ATOM   1876 N N   . TYR A 1 257 ? 2.843   -12.584 59.215  1.00 75.85  ?  274  TYR A N   1 
ATOM   1877 C CA  . TYR A 1 257 ? 2.307   -11.245 58.994  1.00 75.18  ?  274  TYR A CA  1 
ATOM   1878 C C   . TYR A 1 257 ? 2.380   -10.854 57.524  1.00 70.98  ?  274  TYR A C   1 
ATOM   1879 O O   . TYR A 1 257 ? 1.530   -10.096 57.040  1.00 72.87  ?  274  TYR A O   1 
ATOM   1880 C CB  . TYR A 1 257 ? 3.053   -10.225 59.857  1.00 73.18  ?  274  TYR A CB  1 
ATOM   1881 C CG  . TYR A 1 257 ? 4.438   -9.884  59.355  1.00 68.45  ?  274  TYR A CG  1 
ATOM   1882 C CD1 . TYR A 1 257 ? 4.655   -8.764  58.563  1.00 67.96  ?  274  TYR A CD1 1 
ATOM   1883 C CD2 . TYR A 1 257 ? 5.528   -10.682 59.673  1.00 76.09  ?  274  TYR A CD2 1 
ATOM   1884 C CE1 . TYR A 1 257 ? 5.917   -8.450  58.100  1.00 67.92  ?  274  TYR A CE1 1 
ATOM   1885 C CE2 . TYR A 1 257 ? 6.795   -10.374 59.215  1.00 81.19  ?  274  TYR A CE2 1 
ATOM   1886 C CZ  . TYR A 1 257 ? 6.983   -9.257  58.429  1.00 64.13  ?  274  TYR A CZ  1 
ATOM   1887 O OH  . TYR A 1 257 ? 8.241   -8.947  57.970  1.00 73.40  ?  274  TYR A OH  1 
ATOM   1888 N N   . ARG A 1 258 ? 3.386   -11.354 56.802  1.00 63.20  ?  275  ARG A N   1 
ATOM   1889 C CA  . ARG A 1 258 ? 3.472   -11.093 55.370  1.00 62.18  ?  275  ARG A CA  1 
ATOM   1890 C C   . ARG A 1 258 ? 2.303   -11.726 54.626  1.00 68.23  ?  275  ARG A C   1 
ATOM   1891 O O   . ARG A 1 258 ? 1.771   -11.136 53.679  1.00 67.56  ?  275  ARG A O   1 
ATOM   1892 C CB  . ARG A 1 258 ? 4.798   -11.615 54.818  1.00 50.83  ?  275  ARG A CB  1 
ATOM   1893 C CG  . ARG A 1 258 ? 6.030   -11.111 55.548  1.00 58.14  ?  275  ARG A CG  1 
ATOM   1894 C CD  . ARG A 1 258 ? 7.243   -11.942 55.174  1.00 59.12  ?  275  ARG A CD  1 
ATOM   1895 N NE  . ARG A 1 258 ? 7.072   -13.342 55.554  1.00 78.12  ?  275  ARG A NE  1 
ATOM   1896 C CZ  . ARG A 1 258 ? 7.868   -14.328 55.156  1.00 78.42  ?  275  ARG A CZ  1 
ATOM   1897 N NH1 . ARG A 1 258 ? 8.893   -14.070 54.355  1.00 73.33  1  275  ARG A NH1 1 
ATOM   1898 N NH2 . ARG A 1 258 ? 7.637   -15.573 55.552  1.00 76.04  ?  275  ARG A NH2 1 
ATOM   1899 N N   . SER A 1 259 ? 1.887   -12.924 55.045  1.00 68.30  ?  276  SER A N   1 
ATOM   1900 C CA  . SER A 1 259 ? 0.762   -13.590 54.396  1.00 59.76  ?  276  SER A CA  1 
ATOM   1901 C C   . SER A 1 259 ? -0.531  -12.805 54.580  1.00 57.51  ?  276  SER A C   1 
ATOM   1902 O O   . SER A 1 259 ? -1.293  -12.623 53.623  1.00 56.58  ?  276  SER A O   1 
ATOM   1903 C CB  . SER A 1 259 ? 0.608   -15.009 54.942  1.00 70.40  ?  276  SER A CB  1 
ATOM   1904 O OG  . SER A 1 259 ? -0.635  -15.568 54.560  1.00 68.46  ?  276  SER A OG  1 
ATOM   1905 N N   . ALA A 1 260 ? -0.794  -12.331 55.801  1.00 52.47  ?  277  ALA A N   1 
ATOM   1906 C CA  . ALA A 1 260 ? -2.016  -11.575 56.053  1.00 60.19  ?  277  ALA A CA  1 
ATOM   1907 C C   . ALA A 1 260 ? -2.044  -10.266 55.276  1.00 64.01  ?  277  ALA A C   1 
ATOM   1908 O O   . ALA A 1 260 ? -3.112  -9.841  54.822  1.00 66.63  ?  277  ALA A O   1 
ATOM   1909 C CB  . ALA A 1 260 ? -2.162  -11.306 57.552  1.00 63.34  ?  277  ALA A CB  1 
ATOM   1910 N N   . GLU A 1 261 ? -0.888  -9.618  55.107  1.00 60.40  ?  278  GLU A N   1 
ATOM   1911 C CA  . GLU A 1 261 ? -0.837  -8.367  54.358  1.00 66.65  ?  278  GLU A CA  1 
ATOM   1912 C C   . GLU A 1 261 ? -0.963  -8.601  52.857  1.00 60.80  ?  278  GLU A C   1 
ATOM   1913 O O   . GLU A 1 261 ? -1.628  -7.824  52.164  1.00 57.57  ?  278  GLU A O   1 
ATOM   1914 C CB  . GLU A 1 261 ? 0.461   -7.620  54.679  1.00 61.78  ?  278  GLU A CB  1 
ATOM   1915 C CG  . GLU A 1 261 ? 0.582   -6.251  54.020  1.00 70.22  ?  278  GLU A CG  1 
ATOM   1916 C CD  . GLU A 1 261 ? -0.555  -5.317  54.380  1.00 79.34  ?  278  GLU A CD  1 
ATOM   1917 O OE1 . GLU A 1 261 ? -0.959  -4.510  53.515  1.00 63.64  ?  278  GLU A OE1 1 
ATOM   1918 O OE2 . GLU A 1 261 ? -1.043  -5.391  55.528  1.00 85.99  -1 278  GLU A OE2 1 
ATOM   1919 N N   . VAL A 1 262 ? -0.330  -9.657  52.336  1.00 51.83  ?  279  VAL A N   1 
ATOM   1920 C CA  . VAL A 1 262 ? -0.486  -9.993  50.922  1.00 51.69  ?  279  VAL A CA  1 
ATOM   1921 C C   . VAL A 1 262 ? -1.930  -10.379 50.627  1.00 59.39  ?  279  VAL A C   1 
ATOM   1922 O O   . VAL A 1 262 ? -2.502  -9.973  49.608  1.00 56.02  ?  279  VAL A O   1 
ATOM   1923 C CB  . VAL A 1 262 ? 0.494   -11.114 50.524  1.00 53.18  ?  279  VAL A CB  1 
ATOM   1924 C CG1 . VAL A 1 262 ? 0.153   -11.667 49.144  1.00 45.49  ?  279  VAL A CG1 1 
ATOM   1925 C CG2 . VAL A 1 262 ? 1.928   -10.605 50.546  1.00 63.26  ?  279  VAL A CG2 1 
ATOM   1926 N N   . LEU A 1 263 ? -2.543  -11.160 51.519  1.00 54.44  ?  280  LEU A N   1 
ATOM   1927 C CA  . LEU A 1 263 ? -3.940  -11.542 51.337  1.00 56.90  ?  280  LEU A CA  1 
ATOM   1928 C C   . LEU A 1 263 ? -4.855  -10.322 51.375  1.00 59.13  ?  280  LEU A C   1 
ATOM   1929 O O   . LEU A 1 263 ? -5.811  -10.229 50.595  1.00 57.13  ?  280  LEU A O   1 
ATOM   1930 C CB  . LEU A 1 263 ? -4.346  -12.553 52.410  1.00 55.24  ?  280  LEU A CB  1 
ATOM   1931 C CG  . LEU A 1 263 ? -5.619  -13.370 52.182  1.00 64.72  ?  280  LEU A CG  1 
ATOM   1932 C CD1 . LEU A 1 263 ? -5.431  -14.341 51.028  1.00 52.40  ?  280  LEU A CD1 1 
ATOM   1933 C CD2 . LEU A 1 263 ? -6.010  -14.113 53.449  1.00 70.72  ?  280  LEU A CD2 1 
ATOM   1934 N N   . SER A 1 264 ? -4.574  -9.373  52.272  1.00 51.73  ?  281  SER A N   1 
ATOM   1935 C CA  . SER A 1 264 ? -5.396  -8.170  52.367  1.00 55.36  ?  281  SER A CA  1 
ATOM   1936 C C   . SER A 1 264 ? -5.294  -7.325  51.103  1.00 56.27  ?  281  SER A C   1 
ATOM   1937 O O   . SER A 1 264 ? -6.301  -6.793  50.622  1.00 51.93  ?  281  SER A O   1 
ATOM   1938 C CB  . SER A 1 264 ? -4.988  -7.352  53.592  1.00 55.96  ?  281  SER A CB  1 
ATOM   1939 O OG  . SER A 1 264 ? -5.724  -6.144  53.668  1.00 66.84  ?  281  SER A OG  1 
ATOM   1940 N N   . ARG A 1 265 ? -4.085  -7.189  50.553  1.00 54.94  ?  282  ARG A N   1 
ATOM   1941 C CA  . ARG A 1 265 ? -3.913  -6.431  49.318  1.00 45.39  ?  282  ARG A CA  1 
ATOM   1942 C C   . ARG A 1 265 ? -4.646  -7.083  48.154  1.00 50.38  ?  282  ARG A C   1 
ATOM   1943 O O   . ARG A 1 265 ? -5.136  -6.384  47.260  1.00 62.15  ?  282  ARG A O   1 
ATOM   1944 C CB  . ARG A 1 265 ? -2.425  -6.285  49.004  1.00 56.17  ?  282  ARG A CB  1 
ATOM   1945 C CG  . ARG A 1 265 ? -1.681  -5.394  49.983  1.00 57.34  ?  282  ARG A CG  1 
ATOM   1946 C CD  . ARG A 1 265 ? -1.878  -3.930  49.642  1.00 58.71  ?  282  ARG A CD  1 
ATOM   1947 N NE  . ARG A 1 265 ? -1.713  -3.065  50.805  1.00 69.38  ?  282  ARG A NE  1 
ATOM   1948 C CZ  . ARG A 1 265 ? -1.602  -1.743  50.739  1.00 77.56  ?  282  ARG A CZ  1 
ATOM   1949 N NH1 . ARG A 1 265 ? -1.626  -1.134  49.562  1.00 69.05  1  282  ARG A NH1 1 
ATOM   1950 N NH2 . ARG A 1 265 ? -1.461  -1.030  51.849  1.00 76.68  ?  282  ARG A NH2 1 
ATOM   1951 N N   . MET A 1 266 ? -4.732  -8.415  48.145  1.00 59.06  ?  283  MET A N   1 
ATOM   1952 C CA  . MET A 1 266 ? -5.495  -9.097  47.105  1.00 54.15  ?  283  MET A CA  1 
ATOM   1953 C C   . MET A 1 266 ? -6.987  -8.832  47.250  1.00 55.81  ?  283  MET A C   1 
ATOM   1954 O O   . MET A 1 266 ? -7.690  -8.650  46.250  1.00 58.94  ?  283  MET A O   1 
ATOM   1955 C CB  . MET A 1 266 ? -5.223  -10.599 47.150  1.00 59.46  ?  283  MET A CB  1 
ATOM   1956 C CG  . MET A 1 266 ? -3.852  -11.014 46.664  1.00 47.63  ?  283  MET A CG  1 
ATOM   1957 S SD  . MET A 1 266 ? -3.667  -12.805 46.721  1.00 60.48  ?  283  MET A SD  1 
ATOM   1958 C CE  . MET A 1 266 ? -2.110  -13.006 45.868  1.00 52.80  ?  283  MET A CE  1 
ATOM   1959 N N   . ALA A 1 267 ? -7.488  -8.810  48.488  1.00 60.88  ?  284  ALA A N   1 
ATOM   1960 C CA  . ALA A 1 267 ? -8.923  -8.657  48.707  1.00 61.58  ?  284  ALA A CA  1 
ATOM   1961 C C   . ALA A 1 267 ? -9.436  -7.313  48.207  1.00 55.28  ?  284  ALA A C   1 
ATOM   1962 O O   . ALA A 1 267 ? -10.575 -7.222  47.734  1.00 60.68  ?  284  ALA A O   1 
ATOM   1963 C CB  . ALA A 1 267 ? -9.246  -8.829  50.191  1.00 65.21  ?  284  ALA A CB  1 
ATOM   1964 N N   . PHE A 1 268 ? -8.621  -6.265  48.299  1.00 61.42  ?  285  PHE A N   1 
ATOM   1965 C CA  . PHE A 1 268 ? -9.025  -4.926  47.896  1.00 62.12  ?  285  PHE A CA  1 
ATOM   1966 C C   . PHE A 1 268 ? -8.466  -4.520  46.539  1.00 55.14  ?  285  PHE A C   1 
ATOM   1967 O O   . PHE A 1 268 ? -8.793  -3.435  46.047  1.00 62.02  ?  285  PHE A O   1 
ATOM   1968 C CB  . PHE A 1 268 ? -8.609  -3.915  48.968  1.00 66.73  ?  285  PHE A CB  1 
ATOM   1969 C CG  . PHE A 1 268 ? -9.250  -4.163  50.304  1.00 77.98  ?  285  PHE A CG  1 
ATOM   1970 C CD1 . PHE A 1 268 ? -10.620 -4.352  50.403  1.00 74.39  ?  285  PHE A CD1 1 
ATOM   1971 C CD2 . PHE A 1 268 ? -8.486  -4.233  51.457  1.00 77.87  ?  285  PHE A CD2 1 
ATOM   1972 C CE1 . PHE A 1 268 ? -11.218 -4.589  51.627  1.00 72.40  ?  285  PHE A CE1 1 
ATOM   1973 C CE2 . PHE A 1 268 ? -9.078  -4.471  52.686  1.00 86.34  ?  285  PHE A CE2 1 
ATOM   1974 C CZ  . PHE A 1 268 ? -10.446 -4.650  52.770  1.00 76.63  ?  285  PHE A CZ  1 
ATOM   1975 N N   . ALA A 1 269 ? -7.638  -5.362  45.926  1.00 50.51  ?  286  ALA A N   1 
ATOM   1976 C CA  . ALA A 1 269 ? -7.169  -5.167  44.553  1.00 52.43  ?  286  ALA A CA  1 
ATOM   1977 C C   . ALA A 1 269 ? -7.081  -6.532  43.886  1.00 57.07  ?  286  ALA A C   1 
ATOM   1978 O O   . ALA A 1 269 ? -5.989  -7.060  43.645  1.00 54.59  ?  286  ALA A O   1 
ATOM   1979 C CB  . ALA A 1 269 ? -5.821  -4.444  44.529  1.00 44.67  ?  286  ALA A CB  1 
ATOM   1980 N N   . PRO A 1 270 ? -8.230  -7.139  43.573  1.00 54.15  ?  287  PRO A N   1 
ATOM   1981 C CA  . PRO A 1 270 ? -8.218  -8.533  43.096  1.00 46.05  ?  287  PRO A CA  1 
ATOM   1982 C C   . PRO A 1 270 ? -7.458  -8.735  41.798  1.00 57.80  ?  287  PRO A C   1 
ATOM   1983 O O   . PRO A 1 270 ? -6.903  -9.820  41.583  1.00 58.90  ?  287  PRO A O   1 
ATOM   1984 C CB  . PRO A 1 270 ? -9.711  -8.857  42.930  1.00 49.47  ?  287  PRO A CB  1 
ATOM   1985 C CG  . PRO A 1 270 ? -10.425 -7.848  43.782  1.00 57.00  ?  287  PRO A CG  1 
ATOM   1986 C CD  . PRO A 1 270 ? -9.597  -6.608  43.691  1.00 52.52  ?  287  PRO A CD  1 
ATOM   1987 N N   . HIS A 1 271 ? -7.410  -7.734  40.924  1.00 53.80  ?  288  HIS A N   1 
ATOM   1988 C CA  . HIS A 1 271 ? -6.706  -7.866  39.657  1.00 47.46  ?  288  HIS A CA  1 
ATOM   1989 C C   . HIS A 1 271 ? -5.254  -7.414  39.741  1.00 47.31  ?  288  HIS A C   1 
ATOM   1990 O O   . HIS A 1 271 ? -4.532  -7.500  38.740  1.00 58.79  ?  288  HIS A O   1 
ATOM   1991 C CB  . HIS A 1 271 ? -7.440  -7.083  38.562  1.00 45.07  ?  288  HIS A CB  1 
ATOM   1992 C CG  . HIS A 1 271 ? -8.735  -7.705  38.142  1.00 57.57  ?  288  HIS A CG  1 
ATOM   1993 N ND1 . HIS A 1 271 ? -8.814  -8.664  37.154  1.00 59.23  ?  288  HIS A ND1 1 
ATOM   1994 C CD2 . HIS A 1 271 ? -10.002 -7.507  38.577  1.00 53.08  ?  288  HIS A CD2 1 
ATOM   1995 C CE1 . HIS A 1 271 ? -10.074 -9.028  36.998  1.00 61.06  ?  288  HIS A CE1 1 
ATOM   1996 N NE2 . HIS A 1 271 ? -10.815 -8.341  37.849  1.00 62.42  ?  288  HIS A NE2 1 
ATOM   1997 N N   . GLY A 1 272 ? -4.810  -6.947  40.905  1.00 48.52  ?  289  GLY A N   1 
ATOM   1998 C CA  . GLY A 1 272 ? -3.437  -6.553  41.111  1.00 61.26  ?  289  GLY A CA  1 
ATOM   1999 C C   . GLY A 1 272 ? -2.978  -5.478  40.124  1.00 61.87  ?  289  GLY A C   1 
ATOM   2000 O O   . GLY A 1 272 ? -3.756  -4.690  39.564  1.00 63.79  ?  289  GLY A O   1 
ATOM   2001 N N   . GLU A 1 273 ? -1.665  -5.460  39.929  1.00 80.39  ?  290  GLU A N   1 
ATOM   2002 C CA  . GLU A 1 273 ? -1.045  -4.514  39.016  1.00 82.79  ?  290  GLU A CA  1 
ATOM   2003 C C   . GLU A 1 273 ? -1.342  -4.893  37.569  1.00 81.10  ?  290  GLU A C   1 
ATOM   2004 O O   . GLU A 1 273 ? -1.596  -6.055  37.236  1.00 78.39  ?  290  GLU A O   1 
ATOM   2005 C CB  . GLU A 1 273 ? 0.459   -4.444  39.244  1.00 84.80  ?  290  GLU A CB  1 
ATOM   2006 C CG  . GLU A 1 273 ? 0.871   -3.542  40.395  1.00 87.67  ?  290  GLU A CG  1 
ATOM   2007 C CD  . GLU A 1 273 ? 0.226   -2.168  40.315  1.00 89.84  ?  290  GLU A CD  1 
ATOM   2008 O OE1 . GLU A 1 273 ? -0.348  -1.722  41.330  1.00 90.52  ?  290  GLU A OE1 1 
ATOM   2009 O OE2 . GLU A 1 273 ? 0.288   -1.537  39.238  1.00 105.67 -1 290  GLU A OE2 1 
ATOM   2010 N N   . ASP A 1 274 ? -1.314  -3.887  36.707  1.00 83.64  ?  291  ASP A N   1 
ATOM   2011 C CA  . ASP A 1 274 ? -1.485  -4.078  35.278  1.00 82.53  ?  291  ASP A CA  1 
ATOM   2012 C C   . ASP A 1 274 ? -0.137  -4.335  34.616  1.00 83.34  ?  291  ASP A C   1 
ATOM   2013 O O   . ASP A 1 274 ? 0.927   -4.064  35.180  1.00 85.37  ?  291  ASP A O   1 
ATOM   2014 C CB  . ASP A 1 274 ? -2.155  -2.856  34.648  1.00 84.13  ?  291  ASP A CB  1 
ATOM   2015 C CG  . ASP A 1 274 ? -1.473  -1.553  35.030  1.00 101.07 ?  291  ASP A CG  1 
ATOM   2016 O OD1 . ASP A 1 274 ? -1.516  -1.183  36.224  1.00 104.60 ?  291  ASP A OD1 1 
ATOM   2017 O OD2 . ASP A 1 274 ? -0.886  -0.905  34.138  1.00 104.79 -1 291  ASP A OD2 1 
ATOM   2018 N N   . HIS A 1 275 ? -0.196  -4.869  33.399  1.00 81.04  ?  292  HIS A N   1 
ATOM   2019 C CA  . HIS A 1 275 ? 1.001   -5.085  32.597  1.00 81.73  ?  292  HIS A CA  1 
ATOM   2020 C C   . HIS A 1 275 ? 1.030   -4.086  31.447  1.00 89.28  ?  292  HIS A C   1 
ATOM   2021 O O   . HIS A 1 275 ? 1.231   -4.463  30.288  1.00 102.19 ?  292  HIS A O   1 
ATOM   2022 C CB  . HIS A 1 275 ? 1.044   -6.522  32.076  1.00 78.54  ?  292  HIS A CB  1 
ATOM   2023 C CG  . HIS A 1 275 ? 1.022   -7.555  33.160  1.00 76.66  ?  292  HIS A CG  1 
ATOM   2024 N ND1 . HIS A 1 275 ? 2.162   -8.187  33.608  1.00 76.80  ?  292  HIS A ND1 1 
ATOM   2025 C CD2 . HIS A 1 275 ? 0.000   -8.060  33.891  1.00 74.63  ?  292  HIS A CD2 1 
ATOM   2026 C CE1 . HIS A 1 275 ? 1.843   -9.040  34.565  1.00 74.92  ?  292  HIS A CE1 1 
ATOM   2027 N NE2 . HIS A 1 275 ? 0.537   -8.983  34.756  1.00 73.58  ?  292  HIS A NE2 1 
ATOM   2028 N N   . ASP A 1 276 ? 0.832   -2.811  31.769  1.00 102.67 ?  293  ASP A N   1 
ATOM   2029 C CA  . ASP A 1 276 ? 0.675   -1.781  30.753  1.00 105.81 ?  293  ASP A CA  1 
ATOM   2030 C C   . ASP A 1 276 ? 2.000   -1.470  30.066  1.00 114.19 ?  293  ASP A C   1 
ATOM   2031 O O   . ASP A 1 276 ? 3.074   -1.532  30.669  1.00 97.51  ?  293  ASP A O   1 
ATOM   2032 C CB  . ASP A 1 276 ? 0.107   -0.506  31.381  1.00 120.07 ?  293  ASP A CB  1 
ATOM   2033 C CG  . ASP A 1 276 ? -0.107  0.606   30.369  1.00 130.85 ?  293  ASP A CG  1 
ATOM   2034 O OD1 . ASP A 1 276 ? -0.191  0.307   29.158  1.00 112.54 ?  293  ASP A OD1 1 
ATOM   2035 O OD2 . ASP A 1 276 ? -0.186  1.781   30.788  1.00 148.10 -1 293  ASP A OD2 1 
ATOM   2036 N N   . ILE A 1 277 ? 1.907   -1.133  28.784  1.00 147.77 ?  294  ILE A N   1 
ATOM   2037 C CA  . ILE A 1 277 ? 3.027   -0.578  28.030  1.00 155.47 ?  294  ILE A CA  1 
ATOM   2038 C C   . ILE A 1 277 ? 2.832   0.934   28.065  1.00 157.51 ?  294  ILE A C   1 
ATOM   2039 O O   . ILE A 1 277 ? 2.138   1.519   27.231  1.00 155.64 ?  294  ILE A O   1 
ATOM   2040 C CB  . ILE A 1 277 ? 3.091   -1.132  26.607  1.00 154.39 ?  294  ILE A CB  1 
ATOM   2041 C CG1 . ILE A 1 277 ? 1.681   -1.323  26.043  1.00 150.00 ?  294  ILE A CG1 1 
ATOM   2042 C CG2 . ILE A 1 277 ? 3.858   -2.447  26.581  1.00 135.25 ?  294  ILE A CG2 1 
ATOM   2043 C CD1 . ILE A 1 277 ? 1.658   -1.840  24.625  1.00 141.00 ?  294  ILE A CD1 1 
ATOM   2044 N N   . GLU A 1 278 ? 3.450   1.580   29.053  1.00 138.15 ?  295  GLU A N   1 
ATOM   2045 C CA  . GLU A 1 278 ? 3.233   3.005   29.302  1.00 140.69 ?  295  GLU A CA  1 
ATOM   2046 C C   . GLU A 1 278 ? 3.793   3.916   28.207  1.00 164.16 ?  295  GLU A C   1 
ATOM   2047 O O   . GLU A 1 278 ? 3.824   5.134   28.443  1.00 162.10 ?  295  GLU A O   1 
ATOM   2048 C CB  . GLU A 1 278 ? 3.823   3.396   30.657  1.00 141.74 ?  295  GLU A CB  1 
ATOM   2049 C CG  . GLU A 1 278 ? 2.908   3.105   31.838  1.00 128.78 ?  295  GLU A CG  1 
ATOM   2050 C CD  . GLU A 1 278 ? 3.470   2.050   32.768  1.00 134.43 ?  295  GLU A CD  1 
ATOM   2051 O OE1 . GLU A 1 278 ? 2.690   1.467   33.552  1.00 129.59 ?  295  GLU A OE1 1 
ATOM   2052 O OE2 . GLU A 1 278 ? 4.693   1.804   32.712  1.00 123.59 -1 295  GLU A OE2 1 
ATOM   2053 N N   . LYS A 1 279 ? 4.238   3.421   27.054  1.00 163.99 ?  296  LYS A N   1 
ATOM   2054 C CA  . LYS A 1 279 ? 4.535   4.309   25.940  1.00 176.73 ?  296  LYS A CA  1 
ATOM   2055 C C   . LYS A 1 279 ? 3.257   5.014   25.500  1.00 189.89 ?  296  LYS A C   1 
ATOM   2056 O O   . LYS A 1 279 ? 2.150   4.490   25.660  1.00 190.45 ?  296  LYS A O   1 
ATOM   2057 C CB  . LYS A 1 279 ? 5.148   3.526   24.774  1.00 175.11 ?  296  LYS A CB  1 
ATOM   2058 C CG  . LYS A 1 279 ? 6.373   4.186   24.139  1.00 177.31 ?  296  LYS A CG  1 
ATOM   2059 C CD  . LYS A 1 279 ? 5.994   5.400   23.302  1.00 175.34 ?  296  LYS A CD  1 
ATOM   2060 C CE  . LYS A 1 279 ? 5.961   5.076   21.814  1.00 165.06 ?  296  LYS A CE  1 
ATOM   2061 N NZ  . LYS A 1 279 ? 7.317   5.153   21.197  1.00 146.70 1  296  LYS A NZ  1 
ATOM   2062 N N   . ASN A 1 280 ? 3.419   6.231   24.971  1.00 205.28 ?  297  ASN A N   1 
ATOM   2063 C CA  . ASN A 1 280 ? 2.321   7.123   24.595  1.00 207.80 ?  297  ASN A CA  1 
ATOM   2064 C C   . ASN A 1 280 ? 1.593   7.655   25.826  1.00 207.62 ?  297  ASN A C   1 
ATOM   2065 O O   . ASN A 1 280 ? 1.241   8.839   25.876  1.00 203.87 ?  297  ASN A O   1 
ATOM   2066 C CB  . ASN A 1 280 ? 1.332   6.426   23.652  1.00 205.05 ?  297  ASN A CB  1 
ATOM   2067 C CG  . ASN A 1 280 ? 1.993   5.917   22.388  1.00 205.71 ?  297  ASN A CG  1 
ATOM   2068 O OD1 . ASN A 1 280 ? 2.770   4.964   22.420  1.00 203.95 ?  297  ASN A OD1 1 
ATOM   2069 N ND2 . ASN A 1 280 ? 1.680   6.548   21.262  1.00 203.76 ?  297  ASN A ND2 1 
ATOM   2070 N N   . ALA A 1 281 ? 1.363   6.789   26.817  1.00 175.10 ?  298  ALA A N   1 
ATOM   2071 C CA  . ALA A 1 281 ? 0.737   7.161   28.087  1.00 159.86 ?  298  ALA A CA  1 
ATOM   2072 C C   . ALA A 1 281 ? -0.653  7.757   27.887  1.00 149.54 ?  298  ALA A C   1 
ATOM   2073 O O   . ALA A 1 281 ? -1.067  8.655   28.624  1.00 155.44 ?  298  ALA A O   1 
ATOM   2074 C CB  . ALA A 1 281 ? 1.622   8.123   28.887  1.00 166.51 ?  298  ALA A CB  1 
ATOM   2075 N N   . ILE A 1 282 ? -1.381  7.269   26.888  1.00 135.90 ?  299  ILE A N   1 
ATOM   2076 C CA  . ILE A 1 282 ? -2.753  7.687   26.631  1.00 122.32 ?  299  ILE A CA  1 
ATOM   2077 C C   . ILE A 1 282 ? -3.650  6.531   27.064  1.00 108.12 ?  299  ILE A C   1 
ATOM   2078 O O   . ILE A 1 282 ? -3.855  5.563   26.321  1.00 114.39 ?  299  ILE A O   1 
ATOM   2079 C CB  . ILE A 1 282 ? -2.970  8.079   25.162  1.00 127.63 ?  299  ILE A CB  1 
ATOM   2080 C CG1 . ILE A 1 282 ? -4.463  8.208   24.845  1.00 101.27 ?  299  ILE A CG1 1 
ATOM   2081 C CG2 . ILE A 1 282 ? -2.259  7.105   24.221  1.00 139.51 ?  299  ILE A CG2 1 
ATOM   2082 C CD1 . ILE A 1 282 ? -4.752  8.516   23.392  1.00 101.15 ?  299  ILE A CD1 1 
ATOM   2083 N N   . SER A 1 283 ? -4.172  6.615   28.286  1.00 100.63 ?  300  SER A N   1 
ATOM   2084 C CA  . SER A 1 283 ? -5.011  5.556   28.847  1.00 96.15  ?  300  SER A CA  1 
ATOM   2085 C C   . SER A 1 283 ? -6.465  5.891   28.551  1.00 95.03  ?  300  SER A C   1 
ATOM   2086 O O   . SER A 1 283 ? -7.146  6.561   29.329  1.00 95.91  ?  300  SER A O   1 
ATOM   2087 C CB  . SER A 1 283 ? -4.761  5.399   30.341  1.00 96.61  ?  300  SER A CB  1 
ATOM   2088 O OG  . SER A 1 283 ? -3.472  4.866   30.591  1.00 109.89 ?  300  SER A OG  1 
ATOM   2089 N N   . ALA A 1 284 ? -6.945  5.418   27.404  1.00 67.62  ?  301  ALA A N   1 
ATOM   2090 C CA  . ALA A 1 284 ? -8.327  5.610   26.987  1.00 74.40  ?  301  ALA A CA  1 
ATOM   2091 C C   . ALA A 1 284 ? -8.871  4.281   26.488  1.00 78.41  ?  301  ALA A C   1 
ATOM   2092 O O   . ALA A 1 284 ? -8.199  3.581   25.725  1.00 85.42  ?  301  ALA A O   1 
ATOM   2093 C CB  . ALA A 1 284 ? -8.438  6.682   25.898  1.00 68.49  ?  301  ALA A CB  1 
ATOM   2094 N N   . MET A 1 285 ? -10.079 3.933   26.927  1.00 61.69  ?  302  MET A N   1 
ATOM   2095 C CA  . MET A 1 285 ? -10.707 2.688   26.518  1.00 65.94  ?  302  MET A CA  1 
ATOM   2096 C C   . MET A 1 285 ? -12.216 2.883   26.489  1.00 67.52  ?  302  MET A C   1 
ATOM   2097 O O   . MET A 1 285 ? -12.746 3.879   26.986  1.00 64.64  ?  302  MET A O   1 
ATOM   2098 C CB  . MET A 1 285 ? -10.321 1.534   27.448  1.00 70.78  ?  302  MET A CB  1 
ATOM   2099 C CG  . MET A 1 285 ? -10.924 1.624   28.837  1.00 76.24  ?  302  MET A CG  1 
ATOM   2100 S SD  . MET A 1 285 ? -10.094 0.540   30.014  1.00 80.59  ?  302  MET A SD  1 
ATOM   2101 C CE  . MET A 1 285 ? -8.582  1.458   30.305  1.00 73.37  ?  302  MET A CE  1 
ATOM   2102 N N   . ARG A 1 286 ? -12.906 1.912   25.895  1.00 68.69  ?  303  ARG A N   1 
ATOM   2103 C CA  . ARG A 1 286 ? -14.354 1.947   25.741  1.00 62.08  ?  303  ARG A CA  1 
ATOM   2104 C C   . ARG A 1 286 ? -14.958 0.801   26.540  1.00 63.84  ?  303  ARG A C   1 
ATOM   2105 O O   . ARG A 1 286 ? -14.584 -0.360  26.344  1.00 63.41  ?  303  ARG A O   1 
ATOM   2106 C CB  . ARG A 1 286 ? -14.757 1.857   24.266  1.00 61.17  ?  303  ARG A CB  1 
ATOM   2107 C CG  . ARG A 1 286 ? -14.767 3.192   23.520  1.00 66.41  ?  303  ARG A CG  1 
ATOM   2108 C CD  . ARG A 1 286 ? -13.373 3.790   23.380  1.00 56.87  ?  303  ARG A CD  1 
ATOM   2109 N NE  . ARG A 1 286 ? -12.523 3.014   22.482  1.00 68.66  ?  303  ARG A NE  1 
ATOM   2110 C CZ  . ARG A 1 286 ? -11.207 3.171   22.379  1.00 71.19  ?  303  ARG A CZ  1 
ATOM   2111 N NH1 . ARG A 1 286 ? -10.586 4.071   23.128  1.00 69.69  1  303  ARG A NH1 1 
ATOM   2112 N NH2 . ARG A 1 286 ? -10.510 2.424   21.533  1.00 84.82  ?  303  ARG A NH2 1 
ATOM   2113 N N   . ILE A 1 287 ? -15.884 1.127   27.438  1.00 61.35  ?  304  ILE A N   1 
ATOM   2114 C CA  . ILE A 1 287 ? -16.556 0.130   28.265  1.00 60.52  ?  304  ILE A CA  1 
ATOM   2115 C C   . ILE A 1 287 ? -17.779 -0.362  27.500  1.00 60.04  ?  304  ILE A C   1 
ATOM   2116 O O   . ILE A 1 287 ? -18.767 0.363   27.356  1.00 66.88  ?  304  ILE A O   1 
ATOM   2117 C CB  . ILE A 1 287 ? -16.947 0.701   29.633  1.00 60.76  ?  304  ILE A CB  1 
ATOM   2118 C CG1 . ILE A 1 287 ? -15.709 1.198   30.383  1.00 53.24  ?  304  ILE A CG1 1 
ATOM   2119 C CG2 . ILE A 1 287 ? -17.678 -0.347  30.458  1.00 57.02  ?  304  ILE A CG2 1 
ATOM   2120 C CD1 . ILE A 1 287 ? -14.702 0.114   30.694  1.00 47.09  ?  304  ILE A CD1 1 
ATOM   2121 N N   . VAL A 1 288 ? -17.713 -1.600  27.008  1.00 71.79  ?  305  VAL A N   1 
ATOM   2122 C CA  . VAL A 1 288 ? -18.824 -2.149  26.237  1.00 63.77  ?  305  VAL A CA  1 
ATOM   2123 C C   . VAL A 1 288 ? -19.999 -2.479  27.150  1.00 63.65  ?  305  VAL A C   1 
ATOM   2124 O O   . VAL A 1 288 ? -21.162 -2.253  26.794  1.00 64.53  ?  305  VAL A O   1 
ATOM   2125 C CB  . VAL A 1 288 ? -18.356 -3.375  25.434  1.00 64.90  ?  305  VAL A CB  1 
ATOM   2126 C CG1 . VAL A 1 288 ? -19.515 -3.992  24.666  1.00 65.04  ?  305  VAL A CG1 1 
ATOM   2127 C CG2 . VAL A 1 288 ? -17.239 -2.975  24.485  1.00 58.41  ?  305  VAL A CG2 1 
ATOM   2128 N N   . GLY A 1 289 ? -19.722 -3.009  28.340  1.00 60.52  ?  306  GLY A N   1 
ATOM   2129 C CA  . GLY A 1 289 ? -20.781 -3.257  29.298  1.00 64.49  ?  306  GLY A CA  1 
ATOM   2130 C C   . GLY A 1 289 ? -20.637 -4.533  30.100  1.00 60.41  ?  306  GLY A C   1 
ATOM   2131 O O   . GLY A 1 289 ? -19.723 -5.331  29.868  1.00 65.64  ?  306  GLY A O   1 
ATOM   2132 N N   . LYS A 1 290 ? -21.545 -4.731  31.053  1.00 60.95  ?  307  LYS A N   1 
ATOM   2133 C CA  . LYS A 1 290 ? -21.521 -5.926  31.884  1.00 64.45  ?  307  LYS A CA  1 
ATOM   2134 C C   . LYS A 1 290 ? -22.028 -7.122  31.089  1.00 63.05  ?  307  LYS A C   1 
ATOM   2135 O O   . LYS A 1 290 ? -23.058 -7.039  30.412  1.00 69.74  ?  307  LYS A O   1 
ATOM   2136 C CB  . LYS A 1 290 ? -22.371 -5.708  33.135  1.00 61.15  ?  307  LYS A CB  1 
ATOM   2137 C CG  . LYS A 1 290 ? -22.090 -6.684  34.261  1.00 81.62  ?  307  LYS A CG  1 
ATOM   2138 C CD  . LYS A 1 290 ? -22.307 -6.023  35.612  1.00 80.24  ?  307  LYS A CD  1 
ATOM   2139 C CE  . LYS A 1 290 ? -21.881 -6.936  36.747  1.00 90.47  ?  307  LYS A CE  1 
ATOM   2140 N NZ  . LYS A 1 290 ? -21.888 -6.224  38.053  1.00 69.16  1  307  LYS A NZ  1 
ATOM   2141 N N   . VAL A 1 291 ? -21.296 -8.233  31.160  1.00 71.39  ?  308  VAL A N   1 
ATOM   2142 C CA  . VAL A 1 291 ? -21.599 -9.426  30.381  1.00 70.48  ?  308  VAL A CA  1 
ATOM   2143 C C   . VAL A 1 291 ? -21.504 -10.651 31.277  1.00 70.89  ?  308  VAL A C   1 
ATOM   2144 O O   . VAL A 1 291 ? -20.800 -10.650 32.291  1.00 71.38  ?  308  VAL A O   1 
ATOM   2145 C CB  . VAL A 1 291 ? -20.655 -9.578  29.166  1.00 62.12  ?  308  VAL A CB  1 
ATOM   2146 C CG1 . VAL A 1 291 ? -20.816 -8.408  28.214  1.00 61.58  ?  308  VAL A CG1 1 
ATOM   2147 C CG2 . VAL A 1 291 ? -19.211 -9.701  29.627  1.00 61.64  ?  308  VAL A CG2 1 
ATOM   2148 N N   . THR A 1 292 ? -22.227 -11.702 30.895  1.00 76.00  ?  309  THR A N   1 
ATOM   2149 C CA  . THR A 1 292 ? -22.140 -13.003 31.540  1.00 76.56  ?  309  THR A CA  1 
ATOM   2150 C C   . THR A 1 292 ? -21.861 -14.062 30.482  1.00 80.85  ?  309  THR A C   1 
ATOM   2151 O O   . THR A 1 292 ? -22.116 -13.860 29.292  1.00 81.30  ?  309  THR A O   1 
ATOM   2152 C CB  . THR A 1 292 ? -23.425 -13.357 32.306  1.00 74.21  ?  309  THR A CB  1 
ATOM   2153 O OG1 . THR A 1 292 ? -24.527 -13.422 31.393  1.00 84.70  ?  309  THR A OG1 1 
ATOM   2154 C CG2 . THR A 1 292 ? -23.718 -12.316 33.376  1.00 75.79  ?  309  THR A CG2 1 
ATOM   2155 N N   . GLY A 1 293 ? -21.329 -15.202 30.926  1.00 81.99  ?  310  GLY A N   1 
ATOM   2156 C CA  . GLY A 1 293 ? -20.953 -16.252 30.001  1.00 76.88  ?  310  GLY A CA  1 
ATOM   2157 C C   . GLY A 1 293 ? -21.080 -17.628 30.618  1.00 82.98  ?  310  GLY A C   1 
ATOM   2158 O O   . GLY A 1 293 ? -21.305 -17.781 31.821  1.00 78.04  ?  310  GLY A O   1 
ATOM   2159 N N   . LYS A 1 294 ? -20.925 -18.638 29.763  1.00 90.65  ?  311  LYS A N   1 
ATOM   2160 C CA  . LYS A 1 294 ? -21.017 -20.040 30.157  1.00 77.96  ?  311  LYS A CA  1 
ATOM   2161 C C   . LYS A 1 294 ? -19.608 -20.613 30.264  1.00 80.87  ?  311  LYS A C   1 
ATOM   2162 O O   . LYS A 1 294 ? -18.899 -20.726 29.259  1.00 79.91  ?  311  LYS A O   1 
ATOM   2163 C CB  . LYS A 1 294 ? -21.851 -20.833 29.154  1.00 85.48  ?  311  LYS A CB  1 
ATOM   2164 C CG  . LYS A 1 294 ? -23.305 -20.407 29.064  1.00 88.86  ?  311  LYS A CG  1 
ATOM   2165 C CD  . LYS A 1 294 ? -23.997 -21.088 27.893  1.00 86.65  ?  311  LYS A CD  1 
ATOM   2166 C CE  . LYS A 1 294 ? -25.481 -20.762 27.856  1.00 88.84  ?  311  LYS A CE  1 
ATOM   2167 N NZ  . LYS A 1 294 ? -26.142 -21.327 26.647  1.00 100.69 1  311  LYS A NZ  1 
ATOM   2168 N N   . ALA A 1 295 ? -19.208 -20.976 31.477  1.00 82.82  ?  312  ALA A N   1 
ATOM   2169 C CA  . ALA A 1 295 ? -17.903 -21.585 31.728  1.00 84.22  ?  312  ALA A CA  1 
ATOM   2170 C C   . ALA A 1 295 ? -18.096 -22.799 32.626  1.00 88.81  ?  312  ALA A C   1 
ATOM   2171 O O   . ALA A 1 295 ? -18.382 -22.633 33.831  1.00 77.71  ?  312  ALA A O   1 
ATOM   2172 C CB  . ALA A 1 295 ? -16.940 -20.585 32.360  1.00 79.05  ?  312  ALA A CB  1 
ATOM   2173 N N   . PRO A 1 296 ? -17.955 -24.029 32.103  1.00 94.83  ?  313  PRO A N   1 
ATOM   2174 C CA  . PRO A 1 296 ? -17.603 -24.334 30.710  1.00 93.84  ?  313  PRO A CA  1 
ATOM   2175 C C   . PRO A 1 296 ? -18.746 -24.074 29.732  1.00 91.47  ?  313  PRO A C   1 
ATOM   2176 O O   . PRO A 1 296 ? -19.890 -23.908 30.153  1.00 87.30  ?  313  PRO A O   1 
ATOM   2177 C CB  . PRO A 1 296 ? -17.262 -25.824 30.759  1.00 87.70  ?  313  PRO A CB  1 
ATOM   2178 C CG  . PRO A 1 296 ? -18.090 -26.348 31.876  1.00 85.26  ?  313  PRO A CG  1 
ATOM   2179 C CD  . PRO A 1 296 ? -18.123 -25.253 32.906  1.00 82.31  ?  313  PRO A CD  1 
ATOM   2180 N N   . SER A 1 297 ? -18.429 -24.036 28.436  1.00 90.61  ?  314  SER A N   1 
ATOM   2181 C CA  . SER A 1 297 ? -19.431 -23.728 27.424  1.00 98.58  ?  314  SER A CA  1 
ATOM   2182 C C   . SER A 1 297 ? -20.491 -24.812 27.283  1.00 98.17  ?  314  SER A C   1 
ATOM   2183 O O   . SER A 1 297 ? -21.532 -24.556 26.668  1.00 100.64 ?  314  SER A O   1 
ATOM   2184 C CB  . SER A 1 297 ? -18.754 -23.488 26.074  1.00 99.62  ?  314  SER A CB  1 
ATOM   2185 O OG  . SER A 1 297 ? -17.948 -24.590 25.702  1.00 103.58 ?  314  SER A OG  1 
ATOM   2186 N N   . THR A 1 298 ? -20.258 -26.006 27.826  1.00 99.02  ?  315  THR A N   1 
ATOM   2187 C CA  . THR A 1 298 ? -21.272 -27.052 27.829  1.00 111.29 ?  315  THR A CA  1 
ATOM   2188 C C   . THR A 1 298 ? -22.266 -26.903 28.974  1.00 107.42 ?  315  THR A C   1 
ATOM   2189 O O   . THR A 1 298 ? -23.180 -27.727 29.089  1.00 111.99 ?  315  THR A O   1 
ATOM   2190 C CB  . THR A 1 298 ? -20.612 -28.432 27.898  1.00 102.67 ?  315  THR A CB  1 
ATOM   2191 O OG1 . THR A 1 298 ? -19.849 -28.539 29.106  1.00 96.57  ?  315  THR A OG1 1 
ATOM   2192 C CG2 . THR A 1 298 ? -19.695 -28.642 26.703  1.00 97.15  ?  315  THR A CG2 1 
ATOM   2193 N N   . GLU A 1 299 ? -22.107 -25.885 29.816  1.00 102.54 ?  316  GLU A N   1 
ATOM   2194 C CA  . GLU A 1 299 ? -23.039 -25.639 30.902  1.00 103.93 ?  316  GLU A CA  1 
ATOM   2195 C C   . GLU A 1 299 ? -24.379 -25.161 30.350  1.00 103.66 ?  316  GLU A C   1 
ATOM   2196 O O   . GLU A 1 299 ? -24.468 -24.593 29.258  1.00 103.36 ?  316  GLU A O   1 
ATOM   2197 C CB  . GLU A 1 299 ? -22.470 -24.603 31.872  1.00 99.65  ?  316  GLU A CB  1 
ATOM   2198 C CG  . GLU A 1 299 ? -23.043 -24.654 33.281  1.00 103.82 ?  316  GLU A CG  1 
ATOM   2199 C CD  . GLU A 1 299 ? -22.224 -25.526 34.215  1.00 114.57 ?  316  GLU A CD  1 
ATOM   2200 O OE1 . GLU A 1 299 ? -21.285 -26.197 33.736  1.00 120.74 ?  316  GLU A OE1 1 
ATOM   2201 O OE2 . GLU A 1 299 ? -22.513 -25.537 35.431  1.00 124.51 -1 316  GLU A OE2 1 
ATOM   2202 N N   . SER A 1 300 ? -25.434 -25.395 31.128  1.00 96.56  ?  317  SER A N   1 
ATOM   2203 C CA  . SER A 1 300 ? -26.778 -24.992 30.738  1.00 109.77 ?  317  SER A CA  1 
ATOM   2204 C C   . SER A 1 300 ? -27.136 -23.581 31.190  1.00 102.25 ?  317  SER A C   1 
ATOM   2205 O O   . SER A 1 300 ? -28.185 -23.067 30.787  1.00 103.25 ?  317  SER A O   1 
ATOM   2206 C CB  . SER A 1 300 ? -27.810 -25.982 31.293  1.00 102.98 ?  317  SER A CB  1 
ATOM   2207 O OG  . SER A 1 300 ? -27.742 -26.055 32.706  1.00 114.28 ?  317  SER A OG  1 
ATOM   2208 N N   . SER A 1 301 ? -26.298 -22.945 32.006  1.00 95.70  ?  318  SER A N   1 
ATOM   2209 C CA  . SER A 1 301 ? -26.573 -21.604 32.500  1.00 103.06 ?  318  SER A CA  1 
ATOM   2210 C C   . SER A 1 301 ? -25.270 -20.822 32.590  1.00 99.09  ?  318  SER A C   1 
ATOM   2211 O O   . SER A 1 301 ? -24.175 -21.388 32.542  1.00 102.33 ?  318  SER A O   1 
ATOM   2212 C CB  . SER A 1 301 ? -27.266 -21.638 33.869  1.00 93.83  ?  318  SER A CB  1 
ATOM   2213 O OG  . SER A 1 301 ? -28.481 -22.364 33.808  1.00 115.06 ?  318  SER A OG  1 
ATOM   2214 N N   . ASP A 1 302 ? -25.403 -19.504 32.719  1.00 90.50  ?  319  ASP A N   1 
ATOM   2215 C CA  . ASP A 1 302 ? -24.234 -18.646 32.853  1.00 92.92  ?  319  ASP A CA  1 
ATOM   2216 C C   . ASP A 1 302 ? -23.559 -18.867 34.201  1.00 91.11  ?  319  ASP A C   1 
ATOM   2217 O O   . ASP A 1 302 ? -24.219 -18.948 35.240  1.00 86.31  ?  319  ASP A O   1 
ATOM   2218 C CB  . ASP A 1 302 ? -24.626 -17.178 32.696  1.00 84.59  ?  319  ASP A CB  1 
ATOM   2219 C CG  . ASP A 1 302 ? -24.799 -16.775 31.246  1.00 87.60  ?  319  ASP A CG  1 
ATOM   2220 O OD1 . ASP A 1 302 ? -24.467 -17.589 30.360  1.00 88.32  ?  319  ASP A OD1 1 
ATOM   2221 O OD2 . ASP A 1 302 ? -25.266 -15.644 30.994  1.00 96.10  -1 319  ASP A OD2 1 
ATOM   2222 N N   . THR A 1 303 ? -22.228 -18.962 34.178  1.00 76.87  ?  320  THR A N   1 
ATOM   2223 C CA  . THR A 1 303 ? -21.448 -19.223 35.378  1.00 74.99  ?  320  THR A CA  1 
ATOM   2224 C C   . THR A 1 303 ? -20.414 -18.154 35.698  1.00 82.95  ?  320  THR A C   1 
ATOM   2225 O O   . THR A 1 303 ? -19.908 -18.136 36.825  1.00 81.99  ?  320  THR A O   1 
ATOM   2226 C CB  . THR A 1 303 ? -20.724 -20.575 35.266  1.00 81.56  ?  320  THR A CB  1 
ATOM   2227 O OG1 . THR A 1 303 ? -19.997 -20.629 34.032  1.00 75.41  ?  320  THR A OG1 1 
ATOM   2228 C CG2 . THR A 1 303 ? -21.721 -21.723 35.317  1.00 84.05  ?  320  THR A CG2 1 
ATOM   2229 N N   . VAL A 1 304 ? -20.084 -17.276 34.755  1.00 69.46  ?  321  VAL A N   1 
ATOM   2230 C CA  . VAL A 1 304 ? -19.069 -16.250 34.959  1.00 73.90  ?  321  VAL A CA  1 
ATOM   2231 C C   . VAL A 1 304 ? -19.571 -14.946 34.357  1.00 70.67  ?  321  VAL A C   1 
ATOM   2232 O O   . VAL A 1 304 ? -20.270 -14.950 33.339  1.00 67.65  ?  321  VAL A O   1 
ATOM   2233 C CB  . VAL A 1 304 ? -17.715 -16.669 34.345  1.00 65.24  ?  321  VAL A CB  1 
ATOM   2234 C CG1 . VAL A 1 304 ? -17.849 -16.894 32.846  1.00 66.42  ?  321  VAL A CG1 1 
ATOM   2235 C CG2 . VAL A 1 304 ? -16.637 -15.635 34.647  1.00 66.73  ?  321  VAL A CG2 1 
ATOM   2236 N N   . GLN A 1 305 ? -19.236 -13.829 35.002  1.00 67.14  ?  322  GLN A N   1 
ATOM   2237 C CA  . GLN A 1 305 ? -19.585 -12.506 34.511  1.00 72.76  ?  322  GLN A CA  1 
ATOM   2238 C C   . GLN A 1 305 ? -18.335 -11.637 34.461  1.00 66.32  ?  322  GLN A C   1 
ATOM   2239 O O   . GLN A 1 305 ? -17.253 -12.035 34.902  1.00 68.20  ?  322  GLN A O   1 
ATOM   2240 C CB  . GLN A 1 305 ? -20.660 -11.844 35.385  1.00 62.34  ?  322  GLN A CB  1 
ATOM   2241 C CG  . GLN A 1 305 ? -20.157 -11.350 36.730  1.00 60.71  ?  322  GLN A CG  1 
ATOM   2242 C CD  . GLN A 1 305 ? -21.255 -10.733 37.572  1.00 64.58  ?  322  GLN A CD  1 
ATOM   2243 O OE1 . GLN A 1 305 ? -22.409 -11.159 37.518  1.00 77.48  ?  322  GLN A OE1 1 
ATOM   2244 N NE2 . GLN A 1 305 ? -20.902 -9.721  38.356  1.00 69.63  ?  322  GLN A NE2 1 
ATOM   2245 N N   . GLY A 1 306 ? -18.495 -10.438 33.917  1.00 69.50  ?  323  GLY A N   1 
ATOM   2246 C CA  . GLY A 1 306 ? -17.377 -9.522  33.812  1.00 56.86  ?  323  GLY A CA  1 
ATOM   2247 C C   . GLY A 1 306 ? -17.783 -8.263  33.080  1.00 61.60  ?  323  GLY A C   1 
ATOM   2248 O O   . GLY A 1 306 ? -18.968 -8.003  32.860  1.00 66.81  ?  323  GLY A O   1 
ATOM   2249 N N   . ILE A 1 307 ? -16.776 -7.480  32.703  1.00 59.25  ?  324  ILE A N   1 
ATOM   2250 C CA  . ILE A 1 307 ? -16.970 -6.227  31.980  1.00 64.01  ?  324  ILE A CA  1 
ATOM   2251 C C   . ILE A 1 307 ? -16.271 -6.346  30.634  1.00 61.55  ?  324  ILE A C   1 
ATOM   2252 O O   . ILE A 1 307 ? -15.051 -6.545  30.578  1.00 58.00  ?  324  ILE A O   1 
ATOM   2253 C CB  . ILE A 1 307 ? -16.435 -5.020  32.765  1.00 51.11  ?  324  ILE A CB  1 
ATOM   2254 C CG1 . ILE A 1 307 ? -17.166 -4.883  34.102  1.00 51.06  ?  324  ILE A CG1 1 
ATOM   2255 C CG2 . ILE A 1 307 ? -16.570 -3.749  31.942  1.00 50.36  ?  324  ILE A CG2 1 
ATOM   2256 C CD1 . ILE A 1 307 ? -18.649 -4.641  33.965  1.00 52.63  ?  324  ILE A CD1 1 
ATOM   2257 N N   . ALA A 1 308 ? -17.041 -6.233  29.556  1.00 57.75  ?  325  ALA A N   1 
ATOM   2258 C CA  . ALA A 1 308 ? -16.470 -6.214  28.219  1.00 57.99  ?  325  ALA A CA  1 
ATOM   2259 C C   . ALA A 1 308 ? -15.943 -4.821  27.901  1.00 72.47  ?  325  ALA A C   1 
ATOM   2260 O O   . ALA A 1 308 ? -16.599 -3.814  28.185  1.00 62.13  ?  325  ALA A O   1 
ATOM   2261 C CB  . ALA A 1 308 ? -17.512 -6.636  27.183  1.00 60.27  ?  325  ALA A CB  1 
ATOM   2262 N N   . PHE A 1 309 ? -14.749 -4.765  27.316  1.00 68.73  ?  326  PHE A N   1 
ATOM   2263 C CA  . PHE A 1 309 ? -14.093 -3.497  27.040  1.00 57.14  ?  326  PHE A CA  1 
ATOM   2264 C C   . PHE A 1 309 ? -13.451 -3.541  25.660  1.00 67.21  ?  326  PHE A C   1 
ATOM   2265 O O   . PHE A 1 309 ? -13.335 -4.597  25.034  1.00 59.72  ?  326  PHE A O   1 
ATOM   2266 C CB  . PHE A 1 309 ? -13.041 -3.166  28.107  1.00 54.51  ?  326  PHE A CB  1 
ATOM   2267 C CG  . PHE A 1 309 ? -11.811 -4.027  28.035  1.00 58.08  ?  326  PHE A CG  1 
ATOM   2268 C CD1 . PHE A 1 309 ? -11.784 -5.272  28.641  1.00 61.62  ?  326  PHE A CD1 1 
ATOM   2269 C CD2 . PHE A 1 309 ? -10.677 -3.588  27.368  1.00 57.30  ?  326  PHE A CD2 1 
ATOM   2270 C CE1 . PHE A 1 309 ? -10.652 -6.066  28.579  1.00 52.44  ?  326  PHE A CE1 1 
ATOM   2271 C CE2 . PHE A 1 309 ? -9.543  -4.379  27.302  1.00 61.88  ?  326  PHE A CE2 1 
ATOM   2272 C CZ  . PHE A 1 309 ? -9.531  -5.619  27.908  1.00 49.24  ?  326  PHE A CZ  1 
ATOM   2273 N N   . SER A 1 310 ? -13.026 -2.368  25.196  1.00 63.92  ?  327  SER A N   1 
ATOM   2274 C CA  . SER A 1 310 ? -12.297 -2.233  23.941  1.00 58.61  ?  327  SER A CA  1 
ATOM   2275 C C   . SER A 1 310 ? -11.146 -1.265  24.160  1.00 69.03  ?  327  SER A C   1 
ATOM   2276 O O   . SER A 1 310 ? -11.368 -0.124  24.578  1.00 67.35  ?  327  SER A O   1 
ATOM   2277 C CB  . SER A 1 310 ? -13.205 -1.743  22.815  1.00 57.74  ?  327  SER A CB  1 
ATOM   2278 O OG  . SER A 1 310 ? -12.461 -1.521  21.631  1.00 84.66  ?  327  SER A OG  1 
ATOM   2279 N N   . GLY A 1 311 ? -9.927  -1.716  23.881  1.00 65.91  ?  328  GLY A N   1 
ATOM   2280 C CA  . GLY A 1 311 ? -8.764  -0.872  24.086  1.00 63.72  ?  328  GLY A CA  1 
ATOM   2281 C C   . GLY A 1 311 ? -7.495  -1.702  24.054  1.00 58.73  ?  328  GLY A C   1 
ATOM   2282 O O   . GLY A 1 311 ? -7.496  -2.837  23.581  1.00 78.20  ?  328  GLY A O   1 
ATOM   2283 N N   . ASN A 1 312 ? -6.415  -1.114  24.560  1.00 70.61  ?  329  ASN A N   1 
ATOM   2284 C CA  . ASN A 1 312 ? -5.154  -1.829  24.624  1.00 62.96  ?  329  ASN A CA  1 
ATOM   2285 C C   . ASN A 1 312 ? -5.194  -2.873  25.739  1.00 69.08  ?  329  ASN A C   1 
ATOM   2286 O O   . ASN A 1 312 ? -5.930  -2.720  26.717  1.00 62.63  ?  329  ASN A O   1 
ATOM   2287 C CB  . ASN A 1 312 ? -3.998  -0.858  24.858  1.00 70.12  ?  329  ASN A CB  1 
ATOM   2288 C CG  . ASN A 1 312 ? -3.636  -0.068  23.615  1.00 71.58  ?  329  ASN A CG  1 
ATOM   2289 O OD1 . ASN A 1 312 ? -4.277  -0.201  22.572  1.00 87.44  ?  329  ASN A OD1 1 
ATOM   2290 N ND2 . ASN A 1 312 ? -2.608  0.767   23.723  1.00 70.77  ?  329  ASN A ND2 1 
ATOM   2291 N N   . PRO A 1 313 ? -4.423  -3.952  25.606  1.00 65.49  ?  330  PRO A N   1 
ATOM   2292 C CA  . PRO A 1 313 ? -4.368  -4.953  26.679  1.00 65.04  ?  330  PRO A CA  1 
ATOM   2293 C C   . PRO A 1 313 ? -3.821  -4.347  27.963  1.00 61.48  ?  330  PRO A C   1 
ATOM   2294 O O   . PRO A 1 313 ? -2.775  -3.694  27.966  1.00 61.13  ?  330  PRO A O   1 
ATOM   2295 C CB  . PRO A 1 313 ? -3.431  -6.028  26.115  1.00 54.20  ?  330  PRO A CB  1 
ATOM   2296 C CG  . PRO A 1 313 ? -3.491  -5.847  24.634  1.00 57.95  ?  330  PRO A CG  1 
ATOM   2297 C CD  . PRO A 1 313 ? -3.659  -4.372  24.419  1.00 70.44  ?  330  PRO A CD  1 
ATOM   2298 N N   . LEU A 1 314 ? -4.541  -4.570  29.065  1.00 62.18  ?  331  LEU A N   1 
ATOM   2299 C CA  . LEU A 1 314 ? -4.184  -3.972  30.349  1.00 53.75  ?  331  LEU A CA  1 
ATOM   2300 C C   . LEU A 1 314 ? -4.007  -5.035  31.425  1.00 62.17  ?  331  LEU A C   1 
ATOM   2301 O O   . LEU A 1 314 ? -2.877  -5.276  31.857  1.00 60.30  ?  331  LEU A O   1 
ATOM   2302 C CB  . LEU A 1 314 ? -5.233  -2.933  30.748  1.00 54.14  ?  331  LEU A CB  1 
ATOM   2303 C CG  . LEU A 1 314 ? -4.844  -1.974  31.873  1.00 62.30  ?  331  LEU A CG  1 
ATOM   2304 C CD1 . LEU A 1 314 ? -3.504  -1.323  31.572  1.00 67.22  ?  331  LEU A CD1 1 
ATOM   2305 C CD2 . LEU A 1 314 ? -5.919  -0.916  32.066  1.00 56.36  ?  331  LEU A CD2 1 
ATOM   2306 N N   . TYR A 1 315 ? -5.079  -5.682  31.872  1.00 60.64  ?  332  TYR A N   1 
ATOM   2307 C CA  . TYR A 1 315 ? -5.013  -6.639  32.966  1.00 48.48  ?  332  TYR A CA  1 
ATOM   2308 C C   . TYR A 1 315 ? -4.996  -8.072  32.443  1.00 60.61  ?  332  TYR A C   1 
ATOM   2309 O O   . TYR A 1 315 ? -5.242  -8.341  31.265  1.00 59.06  ?  332  TYR A O   1 
ATOM   2310 C CB  . TYR A 1 315 ? -6.190  -6.439  33.926  1.00 49.71  ?  332  TYR A CB  1 
ATOM   2311 C CG  . TYR A 1 315 ? -6.159  -5.120  34.660  1.00 54.38  ?  332  TYR A CG  1 
ATOM   2312 C CD1 . TYR A 1 315 ? -6.916  -4.042  34.224  1.00 52.39  ?  332  TYR A CD1 1 
ATOM   2313 C CD2 . TYR A 1 315 ? -5.368  -4.950  35.787  1.00 51.07  ?  332  TYR A CD2 1 
ATOM   2314 C CE1 . TYR A 1 315 ? -6.889  -2.833  34.892  1.00 59.23  ?  332  TYR A CE1 1 
ATOM   2315 C CE2 . TYR A 1 315 ? -5.333  -3.745  36.461  1.00 69.03  ?  332  TYR A CE2 1 
ATOM   2316 C CZ  . TYR A 1 315 ? -6.095  -2.689  36.009  1.00 57.56  ?  332  TYR A CZ  1 
ATOM   2317 O OH  . TYR A 1 315 ? -6.066  -1.486  36.677  1.00 66.45  ?  332  TYR A OH  1 
ATOM   2318 N N   . THR A 1 316 ? -4.696  -8.998  33.352  1.00 62.74  ?  333  THR A N   1 
ATOM   2319 C CA  . THR A 1 316 ? -4.669  -10.414 33.013  1.00 54.07  ?  333  THR A CA  1 
ATOM   2320 C C   . THR A 1 316 ? -6.046  -10.881 32.555  1.00 59.45  ?  333  THR A C   1 
ATOM   2321 O O   . THR A 1 316 ? -7.077  -10.416 33.050  1.00 57.69  ?  333  THR A O   1 
ATOM   2322 C CB  . THR A 1 316 ? -4.203  -11.236 34.217  1.00 48.66  ?  333  THR A CB  1 
ATOM   2323 O OG1 . THR A 1 316 ? -4.439  -12.628 33.973  1.00 80.57  ?  333  THR A OG1 1 
ATOM   2324 C CG2 . THR A 1 316 ? -4.947  -10.810 35.476  1.00 64.04  ?  333  THR A CG2 1 
ATOM   2325 N N   . SER A 1 317 ? -6.057  -11.805 31.594  1.00 60.13  ?  334  SER A N   1 
ATOM   2326 C CA  . SER A 1 317 ? -7.289  -12.305 30.999  1.00 56.12  ?  334  SER A CA  1 
ATOM   2327 C C   . SER A 1 317 ? -7.544  -13.771 31.334  1.00 62.00  ?  334  SER A C   1 
ATOM   2328 O O   . SER A 1 317 ? -8.379  -14.414 30.691  1.00 59.06  ?  334  SER A O   1 
ATOM   2329 C CB  . SER A 1 317 ? -7.258  -12.109 29.482  1.00 55.87  ?  334  SER A CB  1 
ATOM   2330 O OG  . SER A 1 317 ? -7.037  -10.750 29.147  1.00 64.49  ?  334  SER A OG  1 
ATOM   2331 N N   . THR A 1 318 ? -6.844  -14.312 32.330  1.00 53.81  ?  335  THR A N   1 
ATOM   2332 C CA  . THR A 1 318 ? -6.956  -15.717 32.689  1.00 64.03  ?  335  THR A CA  1 
ATOM   2333 C C   . THR A 1 318 ? -7.305  -15.848 34.165  1.00 62.30  ?  335  THR A C   1 
ATOM   2334 O O   . THR A 1 318 ? -6.878  -15.042 34.996  1.00 70.18  ?  335  THR A O   1 
ATOM   2335 C CB  . THR A 1 318 ? -5.654  -16.479 32.394  1.00 59.98  ?  335  THR A CB  1 
ATOM   2336 O OG1 . THR A 1 318 ? -4.579  -15.909 33.150  1.00 66.95  ?  335  THR A OG1 1 
ATOM   2337 C CG2 . THR A 1 318 ? -5.318  -16.407 30.912  1.00 59.81  ?  335  THR A CG2 1 
ATOM   2338 N N   . GLY A 1 319 ? -8.085  -16.876 34.481  1.00 67.60  ?  336  GLY A N   1 
ATOM   2339 C CA  . GLY A 1 319 ? -8.492  -17.102 35.855  1.00 64.04  ?  336  GLY A CA  1 
ATOM   2340 C C   . GLY A 1 319 ? -9.244  -18.407 35.989  1.00 58.75  ?  336  GLY A C   1 
ATOM   2341 O O   . GLY A 1 319 ? -9.446  -19.140 35.017  1.00 61.51  ?  336  GLY A O   1 
ATOM   2342 N N   . VAL A 1 320 ? -9.655  -18.692 37.224  1.00 60.31  ?  337  VAL A N   1 
ATOM   2343 C CA  . VAL A 1 320 ? -10.452 -19.871 37.540  1.00 62.45  ?  337  VAL A CA  1 
ATOM   2344 C C   . VAL A 1 320 ? -11.720 -19.426 38.252  1.00 61.53  ?  337  VAL A C   1 
ATOM   2345 O O   . VAL A 1 320 ? -11.729 -18.429 38.981  1.00 61.65  ?  337  VAL A O   1 
ATOM   2346 C CB  . VAL A 1 320 ? -9.675  -20.892 38.405  1.00 64.14  ?  337  VAL A CB  1 
ATOM   2347 C CG1 . VAL A 1 320 ? -8.331  -21.200 37.787  1.00 61.88  ?  337  VAL A CG1 1 
ATOM   2348 C CG2 . VAL A 1 320 ? -9.499  -20.381 39.831  1.00 64.71  ?  337  VAL A CG2 1 
ATOM   2349 N N   . LEU A 1 321 ? -12.801 -20.168 38.027  1.00 64.13  ?  338  LEU A N   1 
ATOM   2350 C CA  . LEU A 1 321 ? -14.023 -19.931 38.780  1.00 66.19  ?  338  LEU A CA  1 
ATOM   2351 C C   . LEU A 1 321 ? -13.817 -20.297 40.242  1.00 74.52  ?  338  LEU A C   1 
ATOM   2352 O O   . LEU A 1 321 ? -13.245 -21.342 40.563  1.00 80.28  ?  338  LEU A O   1 
ATOM   2353 C CB  . LEU A 1 321 ? -15.186 -20.744 38.209  1.00 70.45  ?  338  LEU A CB  1 
ATOM   2354 C CG  . LEU A 1 321 ? -16.006 -20.144 37.068  1.00 77.82  ?  338  LEU A CG  1 
ATOM   2355 C CD1 . LEU A 1 321 ? -15.538 -20.690 35.738  1.00 88.24  ?  338  LEU A CD1 1 
ATOM   2356 C CD2 . LEU A 1 321 ? -17.487 -20.423 37.271  1.00 74.02  ?  338  LEU A CD2 1 
ATOM   2357 N N   . THR A 1 322 ? -14.284 -19.426 41.132  1.00 69.78  ?  339  THR A N   1 
ATOM   2358 C CA  . THR A 1 322 ? -14.228 -19.705 42.560  1.00 71.02  ?  339  THR A CA  1 
ATOM   2359 C C   . THR A 1 322 ? -15.290 -20.700 43.007  1.00 71.85  ?  339  THR A C   1 
ATOM   2360 O O   . THR A 1 322 ? -15.299 -21.084 44.181  1.00 78.39  ?  339  THR A O   1 
ATOM   2361 C CB  . THR A 1 322 ? -14.380 -18.408 43.360  1.00 65.32  ?  339  THR A CB  1 
ATOM   2362 O OG1 . THR A 1 322 ? -15.743 -17.968 43.301  1.00 69.40  ?  339  THR A OG1 1 
ATOM   2363 C CG2 . THR A 1 322 ? -13.484 -17.322 42.787  1.00 59.66  ?  339  THR A CG2 1 
ATOM   2364 N N   . ALA A 1 323 ? -16.170 -21.135 42.105  1.00 75.33  ?  340  ALA A N   1 
ATOM   2365 C CA  . ALA A 1 323 ? -17.305 -21.975 42.469  1.00 79.07  ?  340  ALA A CA  1 
ATOM   2366 C C   . ALA A 1 323 ? -16.968 -23.462 42.486  1.00 82.17  ?  340  ALA A C   1 
ATOM   2367 O O   . ALA A 1 323 ? -17.464 -24.195 43.348  1.00 90.14  ?  340  ALA A O   1 
ATOM   2368 C CB  . ALA A 1 323 ? -18.471 -21.726 41.508  1.00 73.47  ?  340  ALA A CB  1 
ATOM   2369 N N   . LYS A 1 324 ? -16.141 -23.928 41.554  1.00 77.77  ?  341  LYS A N   1 
ATOM   2370 C CA  . LYS A 1 324 ? -15.841 -25.345 41.408  1.00 91.17  ?  341  LYS A CA  1 
ATOM   2371 C C   . LYS A 1 324 ? -14.432 -25.643 41.902  1.00 93.00  ?  341  LYS A C   1 
ATOM   2372 O O   . LYS A 1 324 ? -13.486 -24.914 41.587  1.00 91.66  ?  341  LYS A O   1 
ATOM   2373 C CB  . LYS A 1 324 ? -15.979 -25.786 39.948  1.00 95.21  ?  341  LYS A CB  1 
ATOM   2374 C CG  . LYS A 1 324 ? -17.344 -25.518 39.331  1.00 95.41  ?  341  LYS A CG  1 
ATOM   2375 C CD  . LYS A 1 324 ? -18.423 -26.377 39.969  1.00 97.09  ?  341  LYS A CD  1 
ATOM   2376 C CE  . LYS A 1 324 ? -19.740 -26.259 39.215  1.00 102.50 ?  341  LYS A CE  1 
ATOM   2377 N NZ  . LYS A 1 324 ? -19.622 -26.737 37.808  1.00 93.67  1  341  LYS A NZ  1 
ATOM   2378 N N   . ASP A 1 325 ? -14.295 -26.723 42.678  1.00 87.48  ?  342  ASP A N   1 
ATOM   2379 C CA  . ASP A 1 325 ? -12.968 -27.164 43.093  1.00 87.86  ?  342  ASP A CA  1 
ATOM   2380 C C   . ASP A 1 325 ? -12.234 -27.874 41.964  1.00 89.90  ?  342  ASP A C   1 
ATOM   2381 O O   . ASP A 1 325 ? -11.003 -27.798 41.888  1.00 98.25  ?  342  ASP A O   1 
ATOM   2382 C CB  . ASP A 1 325 ? -13.063 -28.067 44.326  1.00 96.65  ?  342  ASP A CB  1 
ATOM   2383 C CG  . ASP A 1 325 ? -14.085 -29.176 44.169  1.00 97.73  ?  342  ASP A CG  1 
ATOM   2384 O OD1 . ASP A 1 325 ? -14.446 -29.507 43.020  1.00 109.62 ?  342  ASP A OD1 1 
ATOM   2385 O OD2 . ASP A 1 325 ? -14.534 -29.712 45.204  1.00 109.55 -1 342  ASP A OD2 1 
ATOM   2386 N N   . ASP A 1 326 ? -12.956 -28.566 41.096  1.00 98.97  ?  343  ASP A N   1 
ATOM   2387 C CA  . ASP A 1 326 ? -12.365 -28.990 39.837  1.00 97.93  ?  343  ASP A CA  1 
ATOM   2388 C C   . ASP A 1 326 ? -12.102 -27.734 39.018  1.00 109.15 ?  343  ASP A C   1 
ATOM   2389 O O   . ASP A 1 326 ? -13.060 -27.056 38.622  1.00 118.43 ?  343  ASP A O   1 
ATOM   2390 C CB  . ASP A 1 326 ? -13.281 -29.968 39.093  1.00 124.31 ?  343  ASP A CB  1 
ATOM   2391 C CG  . ASP A 1 326 ? -14.689 -29.430 38.898  1.00 118.86 ?  343  ASP A CG  1 
ATOM   2392 O OD1 . ASP A 1 326 ? -14.996 -28.956 37.783  1.00 108.58 ?  343  ASP A OD1 1 
ATOM   2393 O OD2 . ASP A 1 326 ? -15.484 -29.475 39.861  1.00 120.54 -1 343  ASP A OD2 1 
ATOM   2394 N N   . PRO A 1 327 ? -10.847 -27.367 38.764  1.00 114.49 ?  344  PRO A N   1 
ATOM   2395 C CA  . PRO A 1 327 ? -10.558 -26.021 38.246  1.00 78.94  ?  344  PRO A CA  1 
ATOM   2396 C C   . PRO A 1 327 ? -11.137 -25.812 36.856  1.00 77.33  ?  344  PRO A C   1 
ATOM   2397 O O   . PRO A 1 327 ? -10.853 -26.566 35.922  1.00 77.83  ?  344  PRO A O   1 
ATOM   2398 C CB  . PRO A 1 327 ? -9.026  -25.970 38.239  1.00 75.80  ?  344  PRO A CB  1 
ATOM   2399 C CG  . PRO A 1 327 ? -8.603  -27.396 38.144  1.00 88.44  ?  344  PRO A CG  1 
ATOM   2400 C CD  . PRO A 1 327 ? -9.627  -28.179 38.914  1.00 97.56  ?  344  PRO A CD  1 
ATOM   2401 N N   . VAL A 1 328 ? -11.965 -24.779 36.731  1.00 85.35  ?  345  VAL A N   1 
ATOM   2402 C CA  . VAL A 1 328 ? -12.544 -24.373 35.457  1.00 81.91  ?  345  VAL A CA  1 
ATOM   2403 C C   . VAL A 1 328 ? -11.764 -23.148 34.996  1.00 75.25  ?  345  VAL A C   1 
ATOM   2404 O O   . VAL A 1 328 ? -11.996 -22.031 35.468  1.00 74.87  ?  345  VAL A O   1 
ATOM   2405 C CB  . VAL A 1 328 ? -14.042 -24.082 35.578  1.00 81.02  ?  345  VAL A CB  1 
ATOM   2406 C CG1 . VAL A 1 328 ? -14.661 -23.937 34.198  1.00 83.68  ?  345  VAL A CG1 1 
ATOM   2407 C CG2 . VAL A 1 328 ? -14.734 -25.179 36.373  1.00 75.89  ?  345  VAL A CG2 1 
ATOM   2408 N N   . TYR A 1 329 ? -10.830 -23.358 34.074  1.00 71.76  ?  346  TYR A N   1 
ATOM   2409 C CA  . TYR A 1 329 ? -9.975  -22.282 33.594  1.00 68.03  ?  346  TYR A CA  1 
ATOM   2410 C C   . TYR A 1 329 ? -10.690 -21.481 32.515  1.00 74.09  ?  346  TYR A C   1 
ATOM   2411 O O   . TYR A 1 329 ? -11.241 -22.050 31.567  1.00 72.29  ?  346  TYR A O   1 
ATOM   2412 C CB  . TYR A 1 329 ? -8.664  -22.853 33.060  1.00 69.83  ?  346  TYR A CB  1 
ATOM   2413 C CG  . TYR A 1 329 ? -7.825  -23.497 34.133  1.00 76.47  ?  346  TYR A CG  1 
ATOM   2414 C CD1 . TYR A 1 329 ? -7.045  -22.726 34.980  1.00 76.93  ?  346  TYR A CD1 1 
ATOM   2415 C CD2 . TYR A 1 329 ? -7.819  -24.872 34.308  1.00 71.64  ?  346  TYR A CD2 1 
ATOM   2416 C CE1 . TYR A 1 329 ? -6.284  -23.306 35.970  1.00 75.01  ?  346  TYR A CE1 1 
ATOM   2417 C CE2 . TYR A 1 329 ? -7.055  -25.461 35.295  1.00 78.98  ?  346  TYR A CE2 1 
ATOM   2418 C CZ  . TYR A 1 329 ? -6.288  -24.673 36.123  1.00 70.89  ?  346  TYR A CZ  1 
ATOM   2419 O OH  . TYR A 1 329 ? -5.526  -25.257 37.109  1.00 82.58  ?  346  TYR A OH  1 
ATOM   2420 N N   . VAL A 1 330 ? -10.682 -20.158 32.663  1.00 64.34  ?  347  VAL A N   1 
ATOM   2421 C CA  . VAL A 1 330 ? -11.367 -19.255 31.747  1.00 67.55  ?  347  VAL A CA  1 
ATOM   2422 C C   . VAL A 1 330 ? -10.343 -18.304 31.145  1.00 73.66  ?  347  VAL A C   1 
ATOM   2423 O O   . VAL A 1 330 ? -9.585  -17.654 31.874  1.00 60.07  ?  347  VAL A O   1 
ATOM   2424 C CB  . VAL A 1 330 ? -12.486 -18.468 32.452  1.00 68.86  ?  347  VAL A CB  1 
ATOM   2425 C CG1 . VAL A 1 330 ? -13.354 -17.753 31.428  1.00 66.77  ?  347  VAL A CG1 1 
ATOM   2426 C CG2 . VAL A 1 330 ? -13.320 -19.392 33.312  1.00 65.00  ?  347  VAL A CG2 1 
ATOM   2427 N N   . TRP A 1 331 ? -10.325 -18.229 29.819  1.00 77.19  ?  348  TRP A N   1 
ATOM   2428 C CA  . TRP A 1 331 ? -9.513  -17.273 29.077  1.00 61.54  ?  348  TRP A CA  1 
ATOM   2429 C C   . TRP A 1 331 ? -10.474 -16.321 28.376  1.00 69.07  ?  348  TRP A C   1 
ATOM   2430 O O   . TRP A 1 331 ? -11.131 -16.703 27.403  1.00 69.26  ?  348  TRP A O   1 
ATOM   2431 C CB  . TRP A 1 331 ? -8.607  -17.990 28.079  1.00 63.26  ?  348  TRP A CB  1 
ATOM   2432 C CG  . TRP A 1 331 ? -7.865  -17.080 27.153  1.00 62.16  ?  348  TRP A CG  1 
ATOM   2433 C CD1 . TRP A 1 331 ? -7.327  -15.863 27.450  1.00 66.13  ?  348  TRP A CD1 1 
ATOM   2434 C CD2 . TRP A 1 331 ? -7.586  -17.316 25.769  1.00 75.83  ?  348  TRP A CD2 1 
ATOM   2435 N NE1 . TRP A 1 331 ? -6.724  -15.328 26.336  1.00 65.70  ?  348  TRP A NE1 1 
ATOM   2436 C CE2 . TRP A 1 331 ? -6.871  -16.201 25.290  1.00 66.12  ?  348  TRP A CE2 1 
ATOM   2437 C CE3 . TRP A 1 331 ? -7.870  -18.365 24.889  1.00 68.67  ?  348  TRP A CE3 1 
ATOM   2438 C CZ2 . TRP A 1 331 ? -6.437  -16.105 23.969  1.00 64.91  ?  348  TRP A CZ2 1 
ATOM   2439 C CZ3 . TRP A 1 331 ? -7.438  -18.267 23.579  1.00 76.41  ?  348  TRP A CZ3 1 
ATOM   2440 C CH2 . TRP A 1 331 ? -6.730  -17.146 23.132  1.00 82.16  ?  348  TRP A CH2 1 
ATOM   2441 N N   . ALA A 1 332 ? -10.565 -15.087 28.876  1.00 65.51  ?  349  ALA A N   1 
ATOM   2442 C CA  . ALA A 1 332 ? -11.542 -14.107 28.405  1.00 61.36  ?  349  ALA A CA  1 
ATOM   2443 C C   . ALA A 1 332 ? -10.816 -12.899 27.825  1.00 62.31  ?  349  ALA A C   1 
ATOM   2444 O O   . ALA A 1 332 ? -10.663 -11.870 28.502  1.00 67.95  ?  349  ALA A O   1 
ATOM   2445 C CB  . ALA A 1 332 ? -12.487 -13.688 29.529  1.00 64.57  ?  349  ALA A CB  1 
ATOM   2446 N N   . PRO A 1 333 ? -10.362 -12.981 26.574  1.00 67.96  ?  350  PRO A N   1 
ATOM   2447 C CA  . PRO A 1 333 ? -9.743  -11.810 25.939  1.00 62.70  ?  350  PRO A CA  1 
ATOM   2448 C C   . PRO A 1 333 ? -10.783 -10.736 25.660  1.00 59.11  ?  350  PRO A C   1 
ATOM   2449 O O   . PRO A 1 333 ? -11.861 -11.016 25.132  1.00 67.05  ?  350  PRO A O   1 
ATOM   2450 C CB  . PRO A 1 333 ? -9.153  -12.379 24.644  1.00 70.32  ?  350  PRO A CB  1 
ATOM   2451 C CG  . PRO A 1 333 ? -9.987  -13.578 24.351  1.00 63.28  ?  350  PRO A CG  1 
ATOM   2452 C CD  . PRO A 1 333 ? -10.362 -14.156 25.686  1.00 63.12  ?  350  PRO A CD  1 
ATOM   2453 N N   . GLY A 1 334 ? -10.454 -9.499  26.025  1.00 68.88  ?  351  GLY A N   1 
ATOM   2454 C CA  . GLY A 1 334 ? -11.374 -8.396  25.851  1.00 58.68  ?  351  GLY A CA  1 
ATOM   2455 C C   . GLY A 1 334 ? -12.436 -8.272  26.919  1.00 62.43  ?  351  GLY A C   1 
ATOM   2456 O O   . GLY A 1 334 ? -13.337 -7.437  26.778  1.00 64.98  ?  351  GLY A O   1 
ATOM   2457 N N   . ILE A 1 335 ? -12.363 -9.073  27.982  1.00 60.50  ?  352  ILE A N   1 
ATOM   2458 C CA  . ILE A 1 335 ? -13.319 -9.027  29.082  1.00 62.13  ?  352  ILE A CA  1 
ATOM   2459 C C   . ILE A 1 335 ? -12.547 -9.058  30.393  1.00 65.42  ?  352  ILE A C   1 
ATOM   2460 O O   . ILE A 1 335 ? -11.718 -9.949  30.609  1.00 69.28  ?  352  ILE A O   1 
ATOM   2461 C CB  . ILE A 1 335 ? -14.320 -10.198 29.029  1.00 56.73  ?  352  ILE A CB  1 
ATOM   2462 C CG1 . ILE A 1 335 ? -15.027 -10.254 27.673  1.00 58.04  ?  352  ILE A CG1 1 
ATOM   2463 C CG2 . ILE A 1 335 ? -15.340 -10.079 30.153  1.00 55.81  ?  352  ILE A CG2 1 
ATOM   2464 C CD1 . ILE A 1 335 ? -15.918 -11.470 27.503  1.00 68.83  ?  352  ILE A CD1 1 
ATOM   2465 N N   . MET A 1 336 ? -12.815 -8.086  31.263  1.00 66.49  ?  353  MET A N   1 
ATOM   2466 C CA  . MET A 1 336 ? -12.281 -8.099  32.621  1.00 59.17  ?  353  MET A CA  1 
ATOM   2467 C C   . MET A 1 336 ? -13.201 -8.950  33.487  1.00 57.28  ?  353  MET A C   1 
ATOM   2468 O O   . MET A 1 336 ? -14.326 -8.543  33.794  1.00 65.37  ?  353  MET A O   1 
ATOM   2469 C CB  . MET A 1 336 ? -12.165 -6.681  33.173  1.00 53.56  ?  353  MET A CB  1 
ATOM   2470 C CG  . MET A 1 336 ? -11.173 -5.800  32.434  1.00 66.93  ?  353  MET A CG  1 
ATOM   2471 S SD  . MET A 1 336 ? -11.034 -4.160  33.169  1.00 59.45  ?  353  MET A SD  1 
ATOM   2472 C CE  . MET A 1 336 ? -12.713 -3.567  32.984  1.00 51.55  ?  353  MET A CE  1 
ATOM   2473 N N   . MET A 1 337 ? -12.730 -10.130 33.879  1.00 56.43  ?  354  MET A N   1 
ATOM   2474 C CA  . MET A 1 337 ? -13.576 -11.062 34.609  1.00 69.15  ?  354  MET A CA  1 
ATOM   2475 C C   . MET A 1 337 ? -13.858 -10.560 36.020  1.00 54.90  ?  354  MET A C   1 
ATOM   2476 O O   . MET A 1 337 ? -13.053 -9.846  36.626  1.00 59.95  ?  354  MET A O   1 
ATOM   2477 C CB  . MET A 1 337 ? -12.927 -12.444 34.662  1.00 68.04  ?  354  MET A CB  1 
ATOM   2478 C CG  . MET A 1 337 ? -12.848 -13.132 33.311  1.00 72.77  ?  354  MET A CG  1 
ATOM   2479 S SD  . MET A 1 337 ? -12.272 -14.832 33.433  1.00 68.98  ?  354  MET A SD  1 
ATOM   2480 C CE  . MET A 1 337 ? -10.672 -14.590 34.200  1.00 55.16  ?  354  MET A CE  1 
ATOM   2481 N N   . GLU A 1 338 ? -15.022 -10.946 36.539  1.00 56.00  ?  355  GLU A N   1 
ATOM   2482 C CA  . GLU A 1 338 ? -15.456 -10.504 37.857  1.00 53.51  ?  355  GLU A CA  1 
ATOM   2483 C C   . GLU A 1 338 ? -14.522 -11.036 38.935  1.00 59.46  ?  355  GLU A C   1 
ATOM   2484 O O   . GLU A 1 338 ? -14.379 -12.252 39.102  1.00 61.15  ?  355  GLU A O   1 
ATOM   2485 C CB  . GLU A 1 338 ? -16.887 -10.972 38.114  1.00 55.65  ?  355  GLU A CB  1 
ATOM   2486 C CG  . GLU A 1 338 ? -17.419 -10.601 39.483  1.00 72.73  ?  355  GLU A CG  1 
ATOM   2487 C CD  . GLU A 1 338 ? -17.543 -9.103  39.669  1.00 75.12  ?  355  GLU A CD  1 
ATOM   2488 O OE1 . GLU A 1 338 ? -18.390 -8.486  38.990  1.00 78.52  ?  355  GLU A OE1 1 
ATOM   2489 O OE2 . GLU A 1 338 ? -16.783 -8.543  40.487  1.00 72.91  -1 355  GLU A OE2 1 
ATOM   2490 N N   . GLY A 1 339 ? -13.889 -10.124 39.668  1.00 58.54  ?  356  GLY A N   1 
ATOM   2491 C CA  . GLY A 1 339 ? -12.968 -10.508 40.718  1.00 50.78  ?  356  GLY A CA  1 
ATOM   2492 C C   . GLY A 1 339 ? -13.301 -9.903  42.065  1.00 54.72  ?  356  GLY A C   1 
ATOM   2493 O O   . GLY A 1 339 ? -12.635 -10.197 43.062  1.00 63.70  ?  356  GLY A O   1 
ATOM   2494 N N   . ASN A 1 340 ? -14.327 -9.054  42.109  1.00 56.13  ?  357  ASN A N   1 
ATOM   2495 C CA  . ASN A 1 340 ? -14.738 -8.422  43.358  1.00 62.43  ?  357  ASN A CA  1 
ATOM   2496 C C   . ASN A 1 340 ? -15.238 -9.486  44.327  1.00 58.17  ?  357  ASN A C   1 
ATOM   2497 O O   . ASN A 1 340 ? -16.193 -10.210 44.029  1.00 67.70  ?  357  ASN A O   1 
ATOM   2498 C CB  . ASN A 1 340 ? -15.820 -7.377  43.086  1.00 53.81  ?  357  ASN A CB  1 
ATOM   2499 C CG  . ASN A 1 340 ? -16.146 -6.525  44.307  1.00 58.75  ?  357  ASN A CG  1 
ATOM   2500 O OD1 . ASN A 1 340 ? -16.212 -7.021  45.431  1.00 60.78  ?  357  ASN A OD1 1 
ATOM   2501 N ND2 . ASN A 1 340 ? -16.354 -5.231  44.084  1.00 60.81  ?  357  ASN A ND2 1 
ATOM   2502 N N   . HIS A 1 341 ? -14.593 -9.576  45.492  1.00 60.25  ?  358  HIS A N   1 
ATOM   2503 C CA  . HIS A 1 341 ? -14.935 -10.602 46.469  1.00 62.81  ?  358  HIS A CA  1 
ATOM   2504 C C   . HIS A 1 341 ? -16.240 -10.320 47.201  1.00 63.93  ?  358  HIS A C   1 
ATOM   2505 O O   . HIS A 1 341 ? -16.757 -11.221 47.870  1.00 72.53  ?  358  HIS A O   1 
ATOM   2506 C CB  . HIS A 1 341 ? -13.798 -10.758 47.482  1.00 59.40  ?  358  HIS A CB  1 
ATOM   2507 C CG  . HIS A 1 341 ? -12.490 -11.152 46.867  1.00 59.63  ?  358  HIS A CG  1 
ATOM   2508 N ND1 . HIS A 1 341 ? -12.270 -12.397 46.318  1.00 61.93  ?  358  HIS A ND1 1 
ATOM   2509 C CD2 . HIS A 1 341 ? -11.331 -10.466 46.720  1.00 61.22  ?  358  HIS A CD2 1 
ATOM   2510 C CE1 . HIS A 1 341 ? -11.034 -12.460 45.856  1.00 58.33  ?  358  HIS A CE1 1 
ATOM   2511 N NE2 . HIS A 1 341 ? -10.443 -11.302 46.088  1.00 60.41  ?  358  HIS A NE2 1 
ATOM   2512 N N   . SER A 1 342 ? -16.786 -9.107  47.094  1.00 69.56  ?  359  SER A N   1 
ATOM   2513 C CA  . SER A 1 342 ? -18.030 -8.786  47.783  1.00 67.34  ?  359  SER A CA  1 
ATOM   2514 C C   . SER A 1 342 ? -19.252 -9.406  47.118  1.00 62.63  ?  359  SER A C   1 
ATOM   2515 O O   . SER A 1 342 ? -20.297 -9.521  47.765  1.00 80.49  ?  359  SER A O   1 
ATOM   2516 C CB  . SER A 1 342 ? -18.209 -7.269  47.880  1.00 60.87  ?  359  SER A CB  1 
ATOM   2517 O OG  . SER A 1 342 ? -17.279 -6.709  48.791  1.00 70.69  ?  359  SER A OG  1 
ATOM   2518 N N   . VAL A 1 343 ? -19.155 -9.796  45.850  1.00 59.66  ?  360  VAL A N   1 
ATOM   2519 C CA  . VAL A 1 343 ? -20.239 -10.539 45.224  1.00 69.25  ?  360  VAL A CA  1 
ATOM   2520 C C   . VAL A 1 343 ? -20.155 -12.004 45.643  1.00 72.98  ?  360  VAL A C   1 
ATOM   2521 O O   . VAL A 1 343 ? -19.140 -12.472 46.163  1.00 80.05  ?  360  VAL A O   1 
ATOM   2522 C CB  . VAL A 1 343 ? -20.208 -10.390 43.691  1.00 70.34  ?  360  VAL A CB  1 
ATOM   2523 C CG1 . VAL A 1 343 ? -20.003 -8.933  43.300  1.00 58.21  ?  360  VAL A CG1 1 
ATOM   2524 C CG2 . VAL A 1 343 ? -19.128 -11.274 43.085  1.00 72.51  ?  360  VAL A CG2 1 
ATOM   2525 N N   . CYS A 1 344 ? -21.248 -12.735 45.431  1.00 74.30  ?  361  CYS A N   1 
ATOM   2526 C CA  . CYS A 1 344 ? -21.277 -14.162 45.732  1.00 80.05  ?  361  CYS A CA  1 
ATOM   2527 C C   . CYS A 1 344 ? -21.197 -15.037 44.488  1.00 80.32  ?  361  CYS A C   1 
ATOM   2528 O O   . CYS A 1 344 ? -20.557 -16.092 44.521  1.00 91.99  ?  361  CYS A O   1 
ATOM   2529 C CB  . CYS A 1 344 ? -22.543 -14.532 46.515  1.00 75.93  ?  361  CYS A CB  1 
ATOM   2530 S SG  . CYS A 1 344 ? -22.625 -13.971 48.240  1.00 103.32 ?  361  CYS A SG  1 
ATOM   2531 N N   . ASP A 1 345 ? -21.824 -14.623 43.392  1.00 74.25  ?  362  ASP A N   1 
ATOM   2532 C CA  . ASP A 1 345 ? -21.972 -15.458 42.208  1.00 74.25  ?  362  ASP A CA  1 
ATOM   2533 C C   . ASP A 1 345 ? -21.021 -15.023 41.100  1.00 69.47  ?  362  ASP A C   1 
ATOM   2534 O O   . ASP A 1 345 ? -20.759 -13.829 40.922  1.00 75.32  ?  362  ASP A O   1 
ATOM   2535 C CB  . ASP A 1 345 ? -23.413 -15.408 41.697  1.00 77.89  ?  362  ASP A CB  1 
ATOM   2536 C CG  . ASP A 1 345 ? -24.380 -16.145 42.603  1.00 100.80 ?  362  ASP A CG  1 
ATOM   2537 O OD1 . ASP A 1 345 ? -25.195 -16.939 42.087  1.00 84.20  ?  362  ASP A OD1 1 
ATOM   2538 O OD2 . ASP A 1 345 ? -24.312 -15.942 43.834  1.00 116.85 -1 362  ASP A OD2 1 
ATOM   2539 N N   . LYS A 1 346 ? -20.501 -16.009 40.364  1.00 68.69  ?  363  LYS A N   1 
ATOM   2540 C CA  . LYS A 1 346 ? -19.806 -15.803 39.093  1.00 65.89  ?  363  LYS A CA  1 
ATOM   2541 C C   . LYS A 1 346 ? -18.500 -15.023 39.241  1.00 62.80  ?  363  LYS A C   1 
ATOM   2542 O O   . LYS A 1 346 ? -18.135 -14.248 38.354  1.00 64.20  ?  363  LYS A O   1 
ATOM   2543 C CB  . LYS A 1 346 ? -20.717 -15.108 38.073  1.00 71.53  ?  363  LYS A CB  1 
ATOM   2544 C CG  . LYS A 1 346 ? -22.054 -15.800 37.862  1.00 69.68  ?  363  LYS A CG  1 
ATOM   2545 C CD  . LYS A 1 346 ? -22.908 -15.055 36.847  1.00 75.73  ?  363  LYS A CD  1 
ATOM   2546 C CE  . LYS A 1 346 ? -24.266 -15.719 36.670  1.00 73.72  ?  363  LYS A CE  1 
ATOM   2547 N NZ  . LYS A 1 346 ? -25.076 -15.693 37.921  1.00 80.65  1  363  LYS A NZ  1 
ATOM   2548 N N   . LYS A 1 347 ? -17.774 -15.229 40.333  1.00 62.01  ?  364  LYS A N   1 
ATOM   2549 C CA  . LYS A 1 347 ? -16.501 -14.563 40.570  1.00 62.83  ?  364  LYS A CA  1 
ATOM   2550 C C   . LYS A 1 347 ? -15.336 -15.476 40.197  1.00 59.20  ?  364  LYS A C   1 
ATOM   2551 O O   . LYS A 1 347 ? -15.464 -16.701 40.151  1.00 67.72  ?  364  LYS A O   1 
ATOM   2552 C CB  . LYS A 1 347 ? -16.391 -14.126 42.032  1.00 58.87  ?  364  LYS A CB  1 
ATOM   2553 C CG  . LYS A 1 347 ? -17.197 -15.000 42.974  1.00 80.57  ?  364  LYS A CG  1 
ATOM   2554 C CD  . LYS A 1 347 ? -17.402 -14.348 44.328  1.00 63.88  ?  364  LYS A CD  1 
ATOM   2555 C CE  . LYS A 1 347 ? -16.140 -14.383 45.165  1.00 64.39  ?  364  LYS A CE  1 
ATOM   2556 N NZ  . LYS A 1 347 ? -16.423 -14.053 46.589  1.00 67.32  1  364  LYS A NZ  1 
ATOM   2557 N N   . THR A 1 348 ? -14.187 -14.856 39.919  1.00 71.14  ?  365  THR A N   1 
ATOM   2558 C CA  . THR A 1 348 ? -13.000 -15.577 39.478  1.00 60.04  ?  365  THR A CA  1 
ATOM   2559 C C   . THR A 1 348 ? -11.789 -15.162 40.303  1.00 58.88  ?  365  THR A C   1 
ATOM   2560 O O   . THR A 1 348 ? -11.777 -14.113 40.951  1.00 63.35  ?  365  THR A O   1 
ATOM   2561 C CB  . THR A 1 348 ? -12.695 -15.337 37.988  1.00 59.77  ?  365  THR A CB  1 
ATOM   2562 O OG1 . THR A 1 348 ? -12.176 -14.013 37.809  1.00 65.93  ?  365  THR A OG1 1 
ATOM   2563 C CG2 . THR A 1 348 ? -13.947 -15.503 37.142  1.00 66.45  ?  365  THR A CG2 1 
ATOM   2564 N N   . LEU A 1 349 ? -10.762 -16.008 40.256  1.00 56.35  ?  366  LEU A N   1 
ATOM   2565 C CA  . LEU A 1 349 ? -9.477  -15.752 40.883  1.00 57.24  ?  366  LEU A CA  1 
ATOM   2566 C C   . LEU A 1 349 ? -8.395  -15.723 39.811  1.00 61.44  ?  366  LEU A C   1 
ATOM   2567 O O   . LEU A 1 349 ? -8.384  -16.593 38.930  1.00 64.20  ?  366  LEU A O   1 
ATOM   2568 C CB  . LEU A 1 349 ? -9.155  -16.832 41.926  1.00 58.49  ?  366  LEU A CB  1 
ATOM   2569 C CG  . LEU A 1 349 ? -9.265  -16.440 43.400  1.00 63.79  ?  366  LEU A CG  1 
ATOM   2570 C CD1 . LEU A 1 349 ? -10.433 -15.503 43.620  1.00 55.55  ?  366  LEU A CD1 1 
ATOM   2571 C CD2 . LEU A 1 349 ? -9.407  -17.685 44.265  1.00 56.41  ?  366  LEU A CD2 1 
ATOM   2572 N N   . PRO A 1 350 ? -7.483  -14.755 39.838  1.00 56.52  ?  367  PRO A N   1 
ATOM   2573 C CA  . PRO A 1 350 ? -6.484  -14.661 38.769  1.00 59.23  ?  367  PRO A CA  1 
ATOM   2574 C C   . PRO A 1 350 ? -5.423  -15.745 38.880  1.00 58.00  ?  367  PRO A C   1 
ATOM   2575 O O   . PRO A 1 350 ? -5.150  -16.279 39.958  1.00 60.30  ?  367  PRO A O   1 
ATOM   2576 C CB  . PRO A 1 350 ? -5.879  -13.270 38.974  1.00 49.34  ?  367  PRO A CB  1 
ATOM   2577 C CG  . PRO A 1 350 ? -6.042  -13.015 40.435  1.00 49.88  ?  367  PRO A CG  1 
ATOM   2578 C CD  . PRO A 1 350 ? -7.343  -13.670 40.824  1.00 50.09  ?  367  PRO A CD  1 
ATOM   2579 N N   . LEU A 1 351 ? -4.817  -16.064 37.733  1.00 59.47  ?  368  LEU A N   1 
ATOM   2580 C CA  . LEU A 1 351 ? -3.736  -17.044 37.699  1.00 56.31  ?  368  LEU A CA  1 
ATOM   2581 C C   . LEU A 1 351 ? -2.437  -16.463 38.246  1.00 58.25  ?  368  LEU A C   1 
ATOM   2582 O O   . LEU A 1 351 ? -1.691  -17.156 38.947  1.00 63.03  ?  368  LEU A O   1 
ATOM   2583 C CB  . LEU A 1 351 ? -3.532  -17.552 36.270  1.00 54.95  ?  368  LEU A CB  1 
ATOM   2584 C CG  . LEU A 1 351 ? -4.128  -18.917 35.923  1.00 59.98  ?  368  LEU A CG  1 
ATOM   2585 C CD1 . LEU A 1 351 ? -5.554  -19.035 36.430  1.00 57.56  ?  368  LEU A CD1 1 
ATOM   2586 C CD2 . LEU A 1 351 ? -4.072  -19.155 34.422  1.00 68.22  ?  368  LEU A CD2 1 
ATOM   2587 N N   . THR A 1 352 ? -2.149  -15.203 37.928  1.00 67.40  ?  369  THR A N   1 
ATOM   2588 C CA  . THR A 1 352 ? -0.990  -14.498 38.452  1.00 62.32  ?  369  THR A CA  1 
ATOM   2589 C C   . THR A 1 352 ? -1.444  -13.179 39.061  1.00 53.28  ?  369  THR A C   1 
ATOM   2590 O O   . THR A 1 352 ? -2.456  -12.605 38.651  1.00 51.38  ?  369  THR A O   1 
ATOM   2591 C CB  . THR A 1 352 ? 0.064   -14.235 37.364  1.00 66.30  ?  369  THR A CB  1 
ATOM   2592 O OG1 . THR A 1 352 ? -0.535  -13.523 36.274  1.00 64.35  ?  369  THR A OG1 1 
ATOM   2593 C CG2 . THR A 1 352 ? 0.644   -15.545 36.854  1.00 61.81  ?  369  THR A CG2 1 
ATOM   2594 N N   . TRP A 1 353 ? -0.686  -12.706 40.047  1.00 55.86  ?  370  TRP A N   1 
ATOM   2595 C CA  . TRP A 1 353 ? -1.053  -11.497 40.777  1.00 50.37  ?  370  TRP A CA  1 
ATOM   2596 C C   . TRP A 1 353 ? 0.215   -10.756 41.170  1.00 53.56  ?  370  TRP A C   1 
ATOM   2597 O O   . TRP A 1 353 ? 1.085   -11.324 41.836  1.00 59.27  ?  370  TRP A O   1 
ATOM   2598 C CB  . TRP A 1 353 ? -1.888  -11.841 42.013  1.00 51.29  ?  370  TRP A CB  1 
ATOM   2599 C CG  . TRP A 1 353 ? -2.483  -10.651 42.697  1.00 52.67  ?  370  TRP A CG  1 
ATOM   2600 C CD1 . TRP A 1 353 ? -3.712  -10.104 42.466  1.00 45.46  ?  370  TRP A CD1 1 
ATOM   2601 C CD2 . TRP A 1 353 ? -1.879  -9.861  43.727  1.00 53.95  ?  370  TRP A CD2 1 
ATOM   2602 N NE1 . TRP A 1 353 ? -3.909  -9.022  43.288  1.00 56.43  ?  370  TRP A NE1 1 
ATOM   2603 C CE2 . TRP A 1 353 ? -2.798  -8.851  44.071  1.00 54.77  ?  370  TRP A CE2 1 
ATOM   2604 C CE3 . TRP A 1 353 ? -0.650  -9.909  44.390  1.00 45.16  ?  370  TRP A CE3 1 
ATOM   2605 C CZ2 . TRP A 1 353 ? -2.527  -7.898  45.050  1.00 47.13  ?  370  TRP A CZ2 1 
ATOM   2606 C CZ3 . TRP A 1 353 ? -0.383  -8.963  45.361  1.00 47.08  ?  370  TRP A CZ3 1 
ATOM   2607 C CH2 . TRP A 1 353 ? -1.316  -7.971  45.681  1.00 57.22  ?  370  TRP A CH2 1 
ATOM   2608 N N   . THR A 1 354 ? 0.317   -9.495  40.755  1.00 67.26  ?  371  THR A N   1 
ATOM   2609 C CA  . THR A 1 354 ? 1.456   -8.643  41.067  1.00 55.23  ?  371  THR A CA  1 
ATOM   2610 C C   . THR A 1 354 ? 0.982   -7.465  41.904  1.00 55.99  ?  371  THR A C   1 
ATOM   2611 O O   . THR A 1 354 ? 0.013   -6.791  41.539  1.00 69.53  ?  371  THR A O   1 
ATOM   2612 C CB  . THR A 1 354 ? 2.140   -8.144  39.790  1.00 56.73  ?  371  THR A CB  1 
ATOM   2613 O OG1 . THR A 1 354 ? 2.838   -9.227  39.163  1.00 75.69  ?  371  THR A OG1 1 
ATOM   2614 C CG2 . THR A 1 354 ? 3.121   -7.025  40.107  1.00 55.98  ?  371  THR A CG2 1 
ATOM   2615 N N   . GLY A 1 355 ? 1.661   -7.222  43.025  1.00 56.95  ?  372  GLY A N   1 
ATOM   2616 C CA  . GLY A 1 355 ? 1.302   -6.121  43.894  1.00 55.40  ?  372  GLY A CA  1 
ATOM   2617 C C   . GLY A 1 355 ? 2.508   -5.581  44.631  1.00 51.13  ?  372  GLY A C   1 
ATOM   2618 O O   . GLY A 1 355 ? 3.607   -6.137  44.570  1.00 53.31  ?  372  GLY A O   1 
ATOM   2619 N N   . PHE A 1 356 ? 2.283   -4.473  45.330  1.00 62.79  ?  373  PHE A N   1 
ATOM   2620 C CA  . PHE A 1 356 ? 3.293   -3.839  46.165  1.00 56.40  ?  373  PHE A CA  1 
ATOM   2621 C C   . PHE A 1 356 ? 2.809   -3.861  47.607  1.00 57.74  ?  373  PHE A C   1 
ATOM   2622 O O   . PHE A 1 356 ? 1.692   -3.420  47.898  1.00 64.33  ?  373  PHE A O   1 
ATOM   2623 C CB  . PHE A 1 356 ? 3.575   -2.410  45.699  1.00 44.10  ?  373  PHE A CB  1 
ATOM   2624 C CG  . PHE A 1 356 ? 4.057   -2.328  44.281  1.00 44.63  ?  373  PHE A CG  1 
ATOM   2625 C CD1 . PHE A 1 356 ? 3.181   -2.029  43.251  1.00 51.31  ?  373  PHE A CD1 1 
ATOM   2626 C CD2 . PHE A 1 356 ? 5.386   -2.570  43.974  1.00 51.25  ?  373  PHE A CD2 1 
ATOM   2627 C CE1 . PHE A 1 356 ? 3.623   -1.962  41.943  1.00 56.24  ?  373  PHE A CE1 1 
ATOM   2628 C CE2 . PHE A 1 356 ? 5.833   -2.505  42.667  1.00 51.89  ?  373  PHE A CE2 1 
ATOM   2629 C CZ  . PHE A 1 356 ? 4.950   -2.200  41.651  1.00 49.93  ?  373  PHE A CZ  1 
ATOM   2630 N N   . ILE A 1 357 ? 3.648   -4.374  48.500  1.00 51.49  ?  374  ILE A N   1 
ATOM   2631 C CA  . ILE A 1 357 ? 3.252   -4.728  49.856  1.00 54.75  ?  374  ILE A CA  1 
ATOM   2632 C C   . ILE A 1 357 ? 4.009   -3.831  50.825  1.00 55.83  ?  374  ILE A C   1 
ATOM   2633 O O   . ILE A 1 357 ? 5.236   -3.755  50.750  1.00 63.24  ?  374  ILE A O   1 
ATOM   2634 C CB  . ILE A 1 357 ? 3.533   -6.208  50.174  1.00 55.69  ?  374  ILE A CB  1 
ATOM   2635 C CG1 . ILE A 1 357 ? 2.902   -7.108  49.112  1.00 61.88  ?  374  ILE A CG1 1 
ATOM   2636 C CG2 . ILE A 1 357 ? 3.012   -6.568  51.543  1.00 52.53  ?  374  ILE A CG2 1 
ATOM   2637 C CD1 . ILE A 1 357 ? 1.414   -6.915  48.951  1.00 65.14  ?  374  ILE A CD1 1 
ATOM   2638 N N   . PRO A 1 358 ? 3.328   -3.140  51.741  1.00 57.55  ?  375  PRO A N   1 
ATOM   2639 C CA  . PRO A 1 358 ? 4.042   -2.424  52.805  1.00 57.48  ?  375  PRO A CA  1 
ATOM   2640 C C   . PRO A 1 358 ? 4.319   -3.332  53.992  1.00 65.14  ?  375  PRO A C   1 
ATOM   2641 O O   . PRO A 1 358 ? 3.387   -3.873  54.597  1.00 66.24  ?  375  PRO A O   1 
ATOM   2642 C CB  . PRO A 1 358 ? 3.080   -1.285  53.176  1.00 45.54  ?  375  PRO A CB  1 
ATOM   2643 C CG  . PRO A 1 358 ? 1.799   -1.534  52.378  1.00 57.78  ?  375  PRO A CG  1 
ATOM   2644 C CD  . PRO A 1 358 ? 1.878   -2.916  51.817  1.00 58.63  ?  375  PRO A CD  1 
ATOM   2645 N N   . LEU A 1 359 ? 5.591   -3.513  54.333  1.00 61.72  ?  376  LEU A N   1 
ATOM   2646 C CA  . LEU A 1 359 ? 5.982   -4.408  55.408  1.00 61.74  ?  376  LEU A CA  1 
ATOM   2647 C C   . LEU A 1 359 ? 6.980   -3.726  56.330  1.00 68.96  ?  376  LEU A C   1 
ATOM   2648 O O   . LEU A 1 359 ? 7.768   -2.884  55.886  1.00 63.70  ?  376  LEU A O   1 
ATOM   2649 C CB  . LEU A 1 359 ? 6.602   -5.701  54.856  1.00 61.77  ?  376  LEU A CB  1 
ATOM   2650 C CG  . LEU A 1 359 ? 5.687   -6.597  54.022  1.00 57.92  ?  376  LEU A CG  1 
ATOM   2651 C CD1 . LEU A 1 359 ? 6.457   -7.783  53.461  1.00 67.17  ?  376  LEU A CD1 1 
ATOM   2652 C CD2 . LEU A 1 359 ? 4.502   -7.066  54.852  1.00 57.52  ?  376  LEU A CD2 1 
ATOM   2653 N N   . PRO A 1 360 ? 6.958   -4.059  57.619  1.00 62.33  ?  377  PRO A N   1 
ATOM   2654 C CA  . PRO A 1 360 ? 8.002   -3.564  58.523  1.00 65.18  ?  377  PRO A CA  1 
ATOM   2655 C C   . PRO A 1 360 ? 9.373   -4.057  58.082  1.00 71.32  ?  377  PRO A C   1 
ATOM   2656 O O   . PRO A 1 360 ? 9.540   -5.211  57.682  1.00 72.27  ?  377  PRO A O   1 
ATOM   2657 C CB  . PRO A 1 360 ? 7.602   -4.147  59.883  1.00 68.92  ?  377  PRO A CB  1 
ATOM   2658 C CG  . PRO A 1 360 ? 6.136   -4.411  59.763  1.00 73.56  ?  377  PRO A CG  1 
ATOM   2659 C CD  . PRO A 1 360 ? 5.913   -4.810  58.337  1.00 65.78  ?  377  PRO A CD  1 
ATOM   2660 N N   . GLY A 1 361 ? 10.358  -3.166  58.157  1.00 71.26  ?  378  GLY A N   1 
ATOM   2661 C CA  . GLY A 1 361 ? 11.676  -3.474  57.638  1.00 65.22  ?  378  GLY A CA  1 
ATOM   2662 C C   . GLY A 1 361 ? 12.803  -3.389  58.646  1.00 62.85  ?  378  GLY A C   1 
ATOM   2663 O O   . GLY A 1 361 ? 12.654  -2.796  59.718  1.00 74.36  ?  378  GLY A O   1 
ATOM   2664 N N   . GLU A 1 362 ? 13.941  -3.988  58.303  1.00 69.18  ?  379  GLU A N   1 
ATOM   2665 C CA  . GLU A 1 362 ? 15.140  -3.922  59.124  1.00 71.22  ?  379  GLU A CA  1 
ATOM   2666 C C   . GLU A 1 362 ? 16.357  -3.974  58.213  1.00 70.65  ?  379  GLU A C   1 
ATOM   2667 O O   . GLU A 1 362 ? 16.302  -4.527  57.112  1.00 76.73  ?  379  GLU A O   1 
ATOM   2668 C CB  . GLU A 1 362 ? 15.184  -5.055  60.158  1.00 73.06  ?  379  GLU A CB  1 
ATOM   2669 C CG  . GLU A 1 362 ? 14.981  -6.447  59.579  1.00 85.76  ?  379  GLU A CG  1 
ATOM   2670 C CD  . GLU A 1 362 ? 14.938  -7.522  60.649  1.00 98.72  ?  379  GLU A CD  1 
ATOM   2671 O OE1 . GLU A 1 362 ? 14.884  -8.718  60.291  1.00 89.29  ?  379  GLU A OE1 1 
ATOM   2672 O OE2 . GLU A 1 362 ? 14.958  -7.170  61.848  1.00 102.02 -1 379  GLU A OE2 1 
ATOM   2673 N N   . ILE A 1 363 ? 17.458  -3.387  58.685  1.00 74.26  ?  380  ILE A N   1 
ATOM   2674 C CA  . ILE A 1 363 ? 18.667  -3.284  57.877  1.00 84.71  ?  380  ILE A CA  1 
ATOM   2675 C C   . ILE A 1 363 ? 19.285  -4.664  57.686  1.00 80.85  ?  380  ILE A C   1 
ATOM   2676 O O   . ILE A 1 363 ? 19.243  -5.516  58.586  1.00 80.94  ?  380  ILE A O   1 
ATOM   2677 C CB  . ILE A 1 363 ? 19.657  -2.305  58.535  1.00 88.67  ?  380  ILE A CB  1 
ATOM   2678 C CG1 . ILE A 1 363 ? 20.960  -2.218  57.735  1.00 89.23  ?  380  ILE A CG1 1 
ATOM   2679 C CG2 . ILE A 1 363 ? 19.928  -2.704  59.981  1.00 81.22  ?  380  ILE A CG2 1 
ATOM   2680 C CD1 . ILE A 1 363 ? 21.981  -1.273  58.330  1.00 87.22  ?  380  ILE A CD1 1 
ATOM   2681 N N   . GLU A 1 364 ? 19.847  -4.898  56.501  1.00 79.44  ?  381  GLU A N   1 
ATOM   2682 C CA  . GLU A 1 364 ? 20.543  -6.147  56.200  1.00 85.67  ?  381  GLU A CA  1 
ATOM   2683 C C   . GLU A 1 364 ? 21.661  -6.419  57.201  1.00 87.39  ?  381  GLU A C   1 
ATOM   2684 O O   . GLU A 1 364 ? 22.818  -6.074  56.961  1.00 91.09  ?  381  GLU A O   1 
ATOM   2685 C CB  . GLU A 1 364 ? 21.119  -6.119  54.781  1.00 86.30  ?  381  GLU A CB  1 
ATOM   2686 C CG  . GLU A 1 364 ? 20.121  -6.447  53.683  1.00 94.22  ?  381  GLU A CG  1 
ATOM   2687 C CD  . GLU A 1 364 ? 20.788  -6.697  52.342  1.00 100.62 ?  381  GLU A CD  1 
ATOM   2688 O OE1 . GLU A 1 364 ? 21.802  -6.030  52.045  1.00 101.26 ?  381  GLU A OE1 1 
ATOM   2689 O OE2 . GLU A 1 364 ? 20.304  -7.569  51.588  1.00 92.87  -1 381  GLU A OE2 1 
ATOM   2690 N N   . GLU B 1 409 ? 28.781  38.838  84.247  1.00 119.99 ?  659  GLU B N   1 
ATOM   2691 C CA  . GLU B 1 409 ? 28.878  38.816  82.792  1.00 132.44 ?  659  GLU B CA  1 
ATOM   2692 C C   . GLU B 1 409 ? 29.017  37.388  82.274  1.00 135.24 ?  659  GLU B C   1 
ATOM   2693 O O   . GLU B 1 409 ? 29.793  36.597  82.811  1.00 133.12 ?  659  GLU B O   1 
ATOM   2694 C CB  . GLU B 1 409 ? 30.059  39.667  82.320  1.00 128.38 ?  659  GLU B CB  1 
ATOM   2695 C CG  . GLU B 1 409 ? 30.288  39.647  80.815  1.00 131.80 ?  659  GLU B CG  1 
ATOM   2696 C CD  . GLU B 1 409 ? 29.032  39.961  80.025  1.00 138.77 ?  659  GLU B CD  1 
ATOM   2697 O OE1 . GLU B 1 409 ? 28.317  39.012  79.637  1.00 134.46 ?  659  GLU B OE1 1 
ATOM   2698 O OE2 . GLU B 1 409 ? 28.756  41.158  79.796  1.00 134.65 -1 659  GLU B OE2 1 
ATOM   2699 N N   . THR B 1 410 ? 28.259  37.064  81.231  1.00 135.53 ?  660  THR B N   1 
ATOM   2700 C CA  . THR B 1 410 ? 28.322  35.735  80.647  1.00 131.13 ?  660  THR B CA  1 
ATOM   2701 C C   . THR B 1 410 ? 29.572  35.593  79.783  1.00 130.05 ?  660  THR B C   1 
ATOM   2702 O O   . THR B 1 410 ? 30.157  36.575  79.316  1.00 134.93 ?  660  THR B O   1 
ATOM   2703 C CB  . THR B 1 410 ? 27.068  35.445  79.817  1.00 129.50 ?  660  THR B CB  1 
ATOM   2704 O OG1 . THR B 1 410 ? 26.994  34.042  79.534  1.00 127.35 ?  660  THR B OG1 1 
ATOM   2705 C CG2 . THR B 1 410 ? 27.098  36.217  78.504  1.00 126.29 ?  660  THR B CG2 1 
ATOM   2706 N N   . GLN B 1 411 ? 29.988  34.344  79.583  1.00 116.93 ?  661  GLN B N   1 
ATOM   2707 C CA  . GLN B 1 411 ? 31.173  34.031  78.788  1.00 118.20 ?  661  GLN B CA  1 
ATOM   2708 C C   . GLN B 1 411 ? 30.835  32.858  77.879  1.00 116.03 ?  661  GLN B C   1 
ATOM   2709 O O   . GLN B 1 411 ? 30.605  31.743  78.358  1.00 103.30 ?  661  GLN B O   1 
ATOM   2710 C CB  . GLN B 1 411 ? 32.373  33.711  79.680  1.00 114.20 ?  661  GLN B CB  1 
ATOM   2711 C CG  . GLN B 1 411 ? 32.885  34.906  80.473  1.00 111.42 ?  661  GLN B CG  1 
ATOM   2712 C CD  . GLN B 1 411 ? 34.024  34.547  81.407  1.00 114.26 ?  661  GLN B CD  1 
ATOM   2713 O OE1 . GLN B 1 411 ? 34.254  33.375  81.705  1.00 126.76 ?  661  GLN B OE1 1 
ATOM   2714 N NE2 . GLN B 1 411 ? 34.745  35.560  81.876  1.00 103.17 ?  661  GLN B NE2 1 
ATOM   2715 N N   . ASN B 1 412 ? 30.808  33.109  76.572  1.00 118.18 ?  662  ASN B N   1 
ATOM   2716 C CA  . ASN B 1 412 ? 30.401  32.108  75.586  1.00 113.71 ?  662  ASN B CA  1 
ATOM   2717 C C   . ASN B 1 412 ? 31.584  31.198  75.279  1.00 109.85 ?  662  ASN B C   1 
ATOM   2718 O O   . ASN B 1 412 ? 32.406  31.478  74.405  1.00 106.01 ?  662  ASN B O   1 
ATOM   2719 C CB  . ASN B 1 412 ? 29.875  32.784  74.327  1.00 114.75 ?  662  ASN B CB  1 
ATOM   2720 C CG  . ASN B 1 412 ? 28.643  33.625  74.592  1.00 114.65 ?  662  ASN B CG  1 
ATOM   2721 O OD1 . ASN B 1 412 ? 28.300  33.896  75.743  1.00 112.36 ?  662  ASN B OD1 1 
ATOM   2722 N ND2 . ASN B 1 412 ? 27.969  34.041  73.527  1.00 112.11 ?  662  ASN B ND2 1 
ATOM   2723 N N   . LEU B 1 413 ? 31.664  30.087  76.005  1.00 112.22 ?  663  LEU B N   1 
ATOM   2724 C CA  . LEU B 1 413 ? 32.707  29.104  75.762  1.00 110.23 ?  663  LEU B CA  1 
ATOM   2725 C C   . LEU B 1 413 ? 32.423  28.334  74.474  1.00 108.05 ?  663  LEU B C   1 
ATOM   2726 O O   . LEU B 1 413 ? 31.287  28.260  73.999  1.00 114.32 ?  663  LEU B O   1 
ATOM   2727 C CB  . LEU B 1 413 ? 32.811  28.131  76.937  1.00 100.83 ?  663  LEU B CB  1 
ATOM   2728 C CG  . LEU B 1 413 ? 32.915  28.741  78.335  1.00 97.69  ?  663  LEU B CG  1 
ATOM   2729 C CD1 . LEU B 1 413 ? 32.690  27.677  79.397  1.00 98.39  ?  663  LEU B CD1 1 
ATOM   2730 C CD2 . LEU B 1 413 ? 34.263  29.413  78.527  1.00 96.43  ?  663  LEU B CD2 1 
ATOM   2731 N N   . ASN B 1 414 ? 33.478  27.756  73.908  1.00 103.54 ?  664  ASN B N   1 
ATOM   2732 C CA  . ASN B 1 414 ? 33.363  26.916  72.726  1.00 111.03 ?  664  ASN B CA  1 
ATOM   2733 C C   . ASN B 1 414 ? 34.143  25.627  72.939  1.00 110.85 ?  664  ASN B C   1 
ATOM   2734 O O   . ASN B 1 414 ? 35.087  25.570  73.731  1.00 100.32 ?  664  ASN B O   1 
ATOM   2735 C CB  . ASN B 1 414 ? 33.861  27.631  71.462  1.00 111.91 ?  664  ASN B CB  1 
ATOM   2736 C CG  . ASN B 1 414 ? 32.789  28.485  70.815  1.00 112.35 ?  664  ASN B CG  1 
ATOM   2737 O OD1 . ASN B 1 414 ? 31.929  27.980  70.092  1.00 110.03 ?  664  ASN B OD1 1 
ATOM   2738 N ND2 . ASN B 1 414 ? 32.834  29.787  71.070  1.00 120.13 ?  664  ASN B ND2 1 
ATOM   2739 N N   . SER B 1 415 ? 33.736  24.589  72.216  1.00 113.08 ?  665  SER B N   1 
ATOM   2740 C CA  . SER B 1 415 ? 34.355  23.283  72.377  1.00 111.75 ?  665  SER B CA  1 
ATOM   2741 C C   . SER B 1 415 ? 35.737  23.258  71.734  1.00 113.62 ?  665  SER B C   1 
ATOM   2742 O O   . SER B 1 415 ? 36.007  23.957  70.754  1.00 118.51 ?  665  SER B O   1 
ATOM   2743 C CB  . SER B 1 415 ? 33.478  22.195  71.762  1.00 121.73 ?  665  SER B CB  1 
ATOM   2744 O OG  . SER B 1 415 ? 33.590  22.198  70.350  1.00 124.65 ?  665  SER B OG  1 
ATOM   2745 N N   . GLY B 1 416 ? 36.612  22.438  72.296  1.00 113.10 ?  666  GLY B N   1 
ATOM   2746 C CA  . GLY B 1 416 ? 37.974  22.296  71.814  1.00 98.94  ?  666  GLY B CA  1 
ATOM   2747 C C   . GLY B 1 416 ? 38.953  22.253  72.970  1.00 95.81  ?  666  GLY B C   1 
ATOM   2748 O O   . GLY B 1 416 ? 38.704  22.781  74.055  1.00 105.31 ?  666  GLY B O   1 
ATOM   2749 N N   . TRP B 1 417 ? 40.093  21.609  72.739  1.00 97.68  ?  667  TRP B N   1 
ATOM   2750 C CA  . TRP B 1 417 ? 41.140  21.487  73.742  1.00 91.79  ?  667  TRP B CA  1 
ATOM   2751 C C   . TRP B 1 417 ? 42.206  22.551  73.522  1.00 100.57 ?  667  TRP B C   1 
ATOM   2752 O O   . TRP B 1 417 ? 42.554  22.873  72.382  1.00 103.72 ?  667  TRP B O   1 
ATOM   2753 C CB  . TRP B 1 417 ? 41.777  20.096  73.706  1.00 100.76 ?  667  TRP B CB  1 
ATOM   2754 C CG  . TRP B 1 417 ? 42.997  19.982  74.570  1.00 98.17  ?  667  TRP B CG  1 
ATOM   2755 C CD1 . TRP B 1 417 ? 44.298  20.079  74.168  1.00 102.02 ?  667  TRP B CD1 1 
ATOM   2756 C CD2 . TRP B 1 417 ? 43.031  19.764  75.986  1.00 102.62 ?  667  TRP B CD2 1 
ATOM   2757 N NE1 . TRP B 1 417 ? 45.139  19.929  75.244  1.00 98.76  ?  667  TRP B NE1 1 
ATOM   2758 C CE2 . TRP B 1 417 ? 44.386  19.734  76.372  1.00 100.71 ?  667  TRP B CE2 1 
ATOM   2759 C CE3 . TRP B 1 417 ? 42.047  19.588  76.965  1.00 88.94  ?  667  TRP B CE3 1 
ATOM   2760 C CZ2 . TRP B 1 417 ? 44.783  19.536  77.693  1.00 101.74 ?  667  TRP B CZ2 1 
ATOM   2761 C CZ3 . TRP B 1 417 ? 42.444  19.391  78.277  1.00 83.17  ?  667  TRP B CZ3 1 
ATOM   2762 C CH2 . TRP B 1 417 ? 43.799  19.367  78.628  1.00 89.72  ?  667  TRP B CH2 1 
ATOM   2763 N N   . THR B 1 418 ? 42.719  23.094  74.623  1.00 106.09 ?  668  THR B N   1 
ATOM   2764 C CA  . THR B 1 418 ? 43.770  24.103  74.600  1.00 98.68  ?  668  THR B CA  1 
ATOM   2765 C C   . THR B 1 418 ? 44.949  23.607  75.425  1.00 99.82  ?  668  THR B C   1 
ATOM   2766 O O   . THR B 1 418 ? 44.770  23.159  76.562  1.00 103.65 ?  668  THR B O   1 
ATOM   2767 C CB  . THR B 1 418 ? 43.260  25.443  75.144  1.00 98.91  ?  668  THR B CB  1 
ATOM   2768 O OG1 . THR B 1 418 ? 42.410  26.064  74.171  1.00 104.62 ?  668  THR B OG1 1 
ATOM   2769 C CG2 . THR B 1 418 ? 44.421  26.374  75.470  1.00 105.50 ?  668  THR B CG2 1 
ATOM   2770 N N   . ASP B 1 419 ? 46.146  23.677  74.846  1.00 103.09 ?  669  ASP B N   1 
ATOM   2771 C CA  . ASP B 1 419 ? 47.348  23.259  75.557  1.00 107.75 ?  669  ASP B CA  1 
ATOM   2772 C C   . ASP B 1 419 ? 47.596  24.163  76.757  1.00 105.72 ?  669  ASP B C   1 
ATOM   2773 O O   . ASP B 1 419 ? 47.714  25.383  76.614  1.00 107.49 ?  669  ASP B O   1 
ATOM   2774 C CB  . ASP B 1 419 ? 48.552  23.279  74.617  1.00 112.21 ?  669  ASP B CB  1 
ATOM   2775 C CG  . ASP B 1 419 ? 48.594  22.076  73.699  1.00 108.95 ?  669  ASP B CG  1 
ATOM   2776 O OD1 . ASP B 1 419 ? 48.106  21.001  74.109  1.00 111.09 ?  669  ASP B OD1 1 
ATOM   2777 O OD2 . ASP B 1 419 ? 49.118  22.203  72.573  1.00 112.78 -1 669  ASP B OD2 1 
ATOM   2778 N N   . THR B 1 420 ? 47.672  23.559  77.940  1.00 105.96 ?  670  THR B N   1 
ATOM   2779 C CA  . THR B 1 420 ? 47.943  24.273  79.177  1.00 97.85  ?  670  THR B CA  1 
ATOM   2780 C C   . THR B 1 420 ? 49.175  23.683  79.849  1.00 104.04 ?  670  THR B C   1 
ATOM   2781 O O   . THR B 1 420 ? 49.482  22.498  79.688  1.00 114.54 ?  670  THR B O   1 
ATOM   2782 C CB  . THR B 1 420 ? 46.750  24.204  80.143  1.00 103.62 ?  670  THR B CB  1 
ATOM   2783 O OG1 . THR B 1 420 ? 46.601  22.862  80.625  1.00 94.43  ?  670  THR B OG1 1 
ATOM   2784 C CG2 . THR B 1 420 ? 45.465  24.630  79.445  1.00 97.20  ?  670  THR B CG2 1 
ATOM   2785 N N   . ALA B 1 421 ? 49.883  24.521  80.604  1.00 107.12 ?  671  ALA B N   1 
ATOM   2786 C CA  . ALA B 1 421 ? 51.013  24.054  81.390  1.00 97.31  ?  671  ALA B CA  1 
ATOM   2787 C C   . ALA B 1 421 ? 50.516  23.365  82.659  1.00 105.01 ?  671  ALA B C   1 
ATOM   2788 O O   . ALA B 1 421 ? 49.315  23.309  82.942  1.00 106.09 ?  671  ALA B O   1 
ATOM   2789 C CB  . ALA B 1 421 ? 51.947  25.213  81.730  1.00 87.27  ?  671  ALA B CB  1 
ATOM   2790 N N   . HIS B 1 422 ? 51.458  22.833  83.435  1.00 99.98  ?  672  HIS B N   1 
ATOM   2791 C CA  . HIS B 1 422 ? 51.109  22.176  84.685  1.00 96.49  ?  672  HIS B CA  1 
ATOM   2792 C C   . HIS B 1 422 ? 50.446  23.162  85.640  1.00 107.30 ?  672  HIS B C   1 
ATOM   2793 O O   . HIS B 1 422 ? 50.768  24.354  85.668  1.00 110.14 ?  672  HIS B O   1 
ATOM   2794 C CB  . HIS B 1 422 ? 52.352  21.571  85.343  1.00 104.55 ?  672  HIS B CB  1 
ATOM   2795 C CG  . HIS B 1 422 ? 52.636  20.160  84.929  1.00 104.87 ?  672  HIS B CG  1 
ATOM   2796 N ND1 . HIS B 1 422 ? 53.292  19.842  83.758  1.00 105.91 ?  672  HIS B ND1 1 
ATOM   2797 C CD2 . HIS B 1 422 ? 52.361  18.981  85.537  1.00 97.27  ?  672  HIS B CD2 1 
ATOM   2798 C CE1 . HIS B 1 422 ? 53.407  18.529  83.663  1.00 102.58 ?  672  HIS B CE1 1 
ATOM   2799 N NE2 . HIS B 1 422 ? 52.849  17.983  84.729  1.00 110.14 ?  672  HIS B NE2 1 
ATOM   2800 N N   . GLY B 1 423 ? 49.504  22.659  86.415  1.00 101.55 ?  673  GLY B N   1 
ATOM   2801 C CA  . GLY B 1 423 ? 48.848  23.455  87.433  1.00 105.71 ?  673  GLY B CA  1 
ATOM   2802 C C   . GLY B 1 423 ? 47.404  23.040  87.617  1.00 103.66 ?  673  GLY B C   1 
ATOM   2803 O O   . GLY B 1 423 ? 46.799  22.370  86.783  1.00 92.59  ?  673  GLY B O   1 
ATOM   2804 N N   . SER B 1 424 ? 46.843  23.453  88.751  1.00 105.04 ?  674  SER B N   1 
ATOM   2805 C CA  . SER B 1 424 ? 45.442  23.232  89.076  1.00 95.45  ?  674  SER B CA  1 
ATOM   2806 C C   . SER B 1 424 ? 44.937  24.438  89.850  1.00 92.19  ?  674  SER B C   1 
ATOM   2807 O O   . SER B 1 424 ? 45.540  24.828  90.855  1.00 96.38  ?  674  SER B O   1 
ATOM   2808 C CB  . SER B 1 424 ? 45.252  21.952  89.897  1.00 102.05 ?  674  SER B CB  1 
ATOM   2809 O OG  . SER B 1 424 ? 45.967  22.021  91.118  1.00 107.05 ?  674  SER B OG  1 
ATOM   2810 N N   . GLY B 1 425 ? 43.837  25.022  89.383  1.00 96.93  ?  675  GLY B N   1 
ATOM   2811 C CA  . GLY B 1 425 ? 43.347  26.259  89.970  1.00 70.90  ?  675  GLY B CA  1 
ATOM   2812 C C   . GLY B 1 425 ? 42.875  26.055  91.399  1.00 68.31  ?  675  GLY B C   1 
ATOM   2813 O O   . GLY B 1 425 ? 42.117  25.123  91.694  1.00 77.85  ?  675  GLY B O   1 
ATOM   2814 N N   . VAL B 1 426 ? 43.325  26.929  92.296  1.00 71.44  ?  676  VAL B N   1 
ATOM   2815 C CA  . VAL B 1 426 ? 42.922  26.920  93.697  1.00 82.67  ?  676  VAL B CA  1 
ATOM   2816 C C   . VAL B 1 426 ? 42.159  28.207  93.977  1.00 79.95  ?  676  VAL B C   1 
ATOM   2817 O O   . VAL B 1 426 ? 42.651  29.302  93.683  1.00 80.57  ?  676  VAL B O   1 
ATOM   2818 C CB  . VAL B 1 426 ? 44.133  26.786  94.638  1.00 67.99  ?  676  VAL B CB  1 
ATOM   2819 C CG1 . VAL B 1 426 ? 43.678  26.763  96.089  1.00 75.35  ?  676  VAL B CG1 1 
ATOM   2820 C CG2 . VAL B 1 426 ? 44.929  25.534  94.302  1.00 67.81  ?  676  VAL B CG2 1 
ATOM   2821 N N   . ILE B 1 427 ? 40.963  28.073  94.542  1.00 75.11  ?  677  ILE B N   1 
ATOM   2822 C CA  . ILE B 1 427 ? 40.105  29.226  94.807  1.00 72.22  ?  677  ILE B CA  1 
ATOM   2823 C C   . ILE B 1 427 ? 39.889  29.376  96.309  1.00 75.04  ?  677  ILE B C   1 
ATOM   2824 O O   . ILE B 1 427 ? 39.208  28.543  96.924  1.00 75.23  ?  677  ILE B O   1 
ATOM   2825 C CB  . ILE B 1 427 ? 38.763  29.103  94.068  1.00 73.59  ?  677  ILE B CB  1 
ATOM   2826 C CG1 . ILE B 1 427 ? 38.982  29.140  92.554  1.00 66.90  ?  677  ILE B CG1 1 
ATOM   2827 C CG2 . ILE B 1 427 ? 37.811  30.210  94.501  1.00 70.07  ?  677  ILE B CG2 1 
ATOM   2828 C CD1 . ILE B 1 427 ? 37.699  29.179  91.749  1.00 65.99  ?  677  ILE B CD1 1 
ATOM   2829 N N   . PRO B 1 428 ? 40.449  30.410  96.938  1.00 75.22  ?  678  PRO B N   1 
ATOM   2830 C CA  . PRO B 1 428 ? 40.144  30.678  98.353  1.00 69.93  ?  678  PRO B CA  1 
ATOM   2831 C C   . PRO B 1 428 ? 38.737  31.240  98.490  1.00 71.24  ?  678  PRO B C   1 
ATOM   2832 O O   . PRO B 1 428 ? 38.411  32.279  97.912  1.00 77.16  ?  678  PRO B O   1 
ATOM   2833 C CB  . PRO B 1 428 ? 41.211  31.700  98.758  1.00 74.61  ?  678  PRO B CB  1 
ATOM   2834 C CG  . PRO B 1 428 ? 41.578  32.381  97.480  1.00 65.22  ?  678  PRO B CG  1 
ATOM   2835 C CD  . PRO B 1 428 ? 41.451  31.345  96.397  1.00 76.96  ?  678  PRO B CD  1 
ATOM   2836 N N   . MET B 1 429 ? 37.902  30.547  99.265  1.00 71.08  ?  679  MET B N   1 
ATOM   2837 C CA  . MET B 1 429 ? 36.476  30.866  99.356  1.00 78.30  ?  679  MET B CA  1 
ATOM   2838 C C   . MET B 1 429 ? 36.253  32.017  100.339 1.00 76.99  ?  679  MET B C   1 
ATOM   2839 O O   . MET B 1 429 ? 35.751  31.852  101.453 1.00 82.90  ?  679  MET B O   1 
ATOM   2840 C CB  . MET B 1 429 ? 35.681  29.630  99.754  1.00 76.55  ?  679  MET B CB  1 
ATOM   2841 C CG  . MET B 1 429 ? 35.758  28.496  98.744  1.00 70.84  ?  679  MET B CG  1 
ATOM   2842 S SD  . MET B 1 429 ? 35.064  28.942  97.140  1.00 72.28  ?  679  MET B SD  1 
ATOM   2843 C CE  . MET B 1 429 ? 33.314  28.965  97.517  1.00 65.17  ?  679  MET B CE  1 
ATOM   2844 N N   . ARG B 1 430 ? 36.635  33.217  99.897  1.00 77.36  ?  680  ARG B N   1 
ATOM   2845 C CA  . ARG B 1 430 ? 36.286  34.421  100.642 1.00 81.65  ?  680  ARG B CA  1 
ATOM   2846 C C   . ARG B 1 430 ? 34.880  34.897  100.307 1.00 81.09  ?  680  ARG B C   1 
ATOM   2847 O O   . ARG B 1 430 ? 34.211  35.493  101.158 1.00 82.49  ?  680  ARG B O   1 
ATOM   2848 C CB  . ARG B 1 430 ? 37.294  35.535  100.362 1.00 70.75  ?  680  ARG B CB  1 
ATOM   2849 C CG  . ARG B 1 430 ? 38.669  35.261  100.928 1.00 77.21  ?  680  ARG B CG  1 
ATOM   2850 C CD  . ARG B 1 430 ? 39.653  36.365  100.592 1.00 70.82  ?  680  ARG B CD  1 
ATOM   2851 N NE  . ARG B 1 430 ? 41.007  35.832  100.503 1.00 83.97  ?  680  ARG B NE  1 
ATOM   2852 C CZ  . ARG B 1 430 ? 41.786  35.591  101.552 1.00 81.87  ?  680  ARG B CZ  1 
ATOM   2853 N NH1 . ARG B 1 430 ? 41.350  35.843  102.778 1.00 72.08  1  680  ARG B NH1 1 
ATOM   2854 N NH2 . ARG B 1 430 ? 43.002  35.095  101.374 1.00 97.91  ?  680  ARG B NH2 1 
ATOM   2855 N N   . THR B 1 431 ? 34.424  34.645  99.084  1.00 80.00  ?  681  THR B N   1 
ATOM   2856 C CA  . THR B 1 431 ? 33.082  34.985  98.643  1.00 73.90  ?  681  THR B CA  1 
ATOM   2857 C C   . THR B 1 431 ? 32.461  33.773  97.964  1.00 74.11  ?  681  THR B C   1 
ATOM   2858 O O   . THR B 1 431 ? 33.105  32.736  97.780  1.00 79.85  ?  681  THR B O   1 
ATOM   2859 C CB  . THR B 1 431 ? 33.090  36.185  97.685  1.00 79.51  ?  681  THR B CB  1 
ATOM   2860 O OG1 . THR B 1 431 ? 32.190  35.936  96.598  1.00 88.93  ?  681  THR B OG1 1 
ATOM   2861 C CG2 . THR B 1 431 ? 34.489  36.426  97.134  1.00 70.26  ?  681  THR B CG2 1 
ATOM   2862 N N   . ASP B 1 432 ? 31.190  33.908  97.597  1.00 74.08  ?  682  ASP B N   1 
ATOM   2863 C CA  . ASP B 1 432 ? 30.525  32.861  96.835  1.00 57.05  ?  682  ASP B CA  1 
ATOM   2864 C C   . ASP B 1 432 ? 31.177  32.720  95.466  1.00 63.24  ?  682  ASP B C   1 
ATOM   2865 O O   . ASP B 1 432 ? 31.367  33.708  94.751  1.00 77.81  ?  682  ASP B O   1 
ATOM   2866 C CB  . ASP B 1 432 ? 29.037  33.175  96.679  1.00 60.20  ?  682  ASP B CB  1 
ATOM   2867 C CG  . ASP B 1 432 ? 28.260  33.002  97.970  1.00 67.04  ?  682  ASP B CG  1 
ATOM   2868 O OD1 . ASP B 1 432 ? 28.696  32.212  98.833  1.00 74.46  ?  682  ASP B OD1 1 
ATOM   2869 O OD2 . ASP B 1 432 ? 27.202  33.649  98.117  1.00 73.43  -1 682  ASP B OD2 1 
ATOM   2870 N N   . LEU B 1 433 ? 31.530  31.489  95.108  1.00 72.06  ?  683  LEU B N   1 
ATOM   2871 C CA  . LEU B 1 433 ? 32.068  31.210  93.784  1.00 65.67  ?  683  LEU B CA  1 
ATOM   2872 C C   . LEU B 1 433 ? 30.930  31.235  92.772  1.00 63.47  ?  683  LEU B C   1 
ATOM   2873 O O   . LEU B 1 433 ? 30.017  30.404  92.835  1.00 62.58  ?  683  LEU B O   1 
ATOM   2874 C CB  . LEU B 1 433 ? 32.784  29.861  93.768  1.00 65.81  ?  683  LEU B CB  1 
ATOM   2875 C CG  . LEU B 1 433 ? 33.299  29.390  92.407  1.00 54.46  ?  683  LEU B CG  1 
ATOM   2876 C CD1 . LEU B 1 433 ? 34.175  30.452  91.758  1.00 58.47  ?  683  LEU B CD1 1 
ATOM   2877 C CD2 . LEU B 1 433 ? 34.057  28.079  92.549  1.00 64.61  ?  683  LEU B CD2 1 
ATOM   2878 N N   . GLU B 1 434 ? 30.978  32.191  91.849  1.00 63.28  ?  684  GLU B N   1 
ATOM   2879 C CA  . GLU B 1 434 ? 29.924  32.388  90.863  1.00 71.06  ?  684  GLU B CA  1 
ATOM   2880 C C   . GLU B 1 434 ? 30.465  32.111  89.469  1.00 69.51  ?  684  GLU B C   1 
ATOM   2881 O O   . GLU B 1 434 ? 31.542  32.597  89.106  1.00 72.16  ?  684  GLU B O   1 
ATOM   2882 C CB  . GLU B 1 434 ? 29.358  33.809  90.938  1.00 69.47  ?  684  GLU B CB  1 
ATOM   2883 C CG  . GLU B 1 434 ? 28.346  34.124  89.848  1.00 78.63  ?  684  GLU B CG  1 
ATOM   2884 C CD  . GLU B 1 434 ? 27.276  35.093  90.308  1.00 100.81 ?  684  GLU B CD  1 
ATOM   2885 O OE1 . GLU B 1 434 ? 27.408  35.640  91.423  1.00 107.12 ?  684  GLU B OE1 1 
ATOM   2886 O OE2 . GLU B 1 434 ? 26.298  35.299  89.558  1.00 103.58 -1 684  GLU B OE2 1 
ATOM   2887 N N   . LEU B 1 435 ? 29.713  31.333  88.694  1.00 61.23  ?  685  LEU B N   1 
ATOM   2888 C CA  . LEU B 1 435 ? 30.060  31.015  87.317  1.00 69.13  ?  685  LEU B CA  1 
ATOM   2889 C C   . LEU B 1 435 ? 28.893  31.387  86.417  1.00 73.48  ?  685  LEU B C   1 
ATOM   2890 O O   . LEU B 1 435 ? 27.764  30.938  86.643  1.00 82.42  ?  685  LEU B O   1 
ATOM   2891 C CB  . LEU B 1 435 ? 30.395  29.528  87.153  1.00 61.69  ?  685  LEU B CB  1 
ATOM   2892 C CG  . LEU B 1 435 ? 31.522  28.964  88.018  1.00 61.32  ?  685  LEU B CG  1 
ATOM   2893 C CD1 . LEU B 1 435 ? 31.678  27.472  87.772  1.00 69.85  ?  685  LEU B CD1 1 
ATOM   2894 C CD2 . LEU B 1 435 ? 32.828  29.695  87.754  1.00 64.08  ?  685  LEU B CD2 1 
ATOM   2895 N N   . ASP B 1 436 ? 29.163  32.208  85.407  1.00 85.43  ?  686  ASP B N   1 
ATOM   2896 C CA  . ASP B 1 436 ? 28.170  32.575  84.405  1.00 91.49  ?  686  ASP B CA  1 
ATOM   2897 C C   . ASP B 1 436 ? 28.782  32.351  83.033  1.00 88.31  ?  686  ASP B C   1 
ATOM   2898 O O   . ASP B 1 436 ? 29.757  33.017  82.669  1.00 94.21  ?  686  ASP B O   1 
ATOM   2899 C CB  . ASP B 1 436 ? 27.716  34.028  84.571  1.00 103.74 ?  686  ASP B CB  1 
ATOM   2900 C CG  . ASP B 1 436 ? 26.354  34.284  83.958  1.00 100.98 ?  686  ASP B CG  1 
ATOM   2901 O OD1 . ASP B 1 436 ? 25.361  33.725  84.468  1.00 93.39  ?  686  ASP B OD1 1 
ATOM   2902 O OD2 . ASP B 1 436 ? 26.277  35.042  82.967  1.00 115.87 -1 686  ASP B OD2 1 
ATOM   2903 N N   . PHE B 1 437 ? 28.216  31.413  82.279  1.00 95.26  ?  687  PHE B N   1 
ATOM   2904 C CA  . PHE B 1 437 ? 28.792  31.009  81.007  1.00 92.76  ?  687  PHE B CA  1 
ATOM   2905 C C   . PHE B 1 437 ? 27.706  30.388  80.144  1.00 93.18  ?  687  PHE B C   1 
ATOM   2906 O O   . PHE B 1 437 ? 26.710  29.869  80.654  1.00 93.77  ?  687  PHE B O   1 
ATOM   2907 C CB  . PHE B 1 437 ? 29.942  30.015  81.208  1.00 87.29  ?  687  PHE B CB  1 
ATOM   2908 C CG  . PHE B 1 437 ? 29.535  28.760  81.931  1.00 88.40  ?  687  PHE B CG  1 
ATOM   2909 C CD1 . PHE B 1 437 ? 29.542  28.708  83.315  1.00 88.18  ?  687  PHE B CD1 1 
ATOM   2910 C CD2 . PHE B 1 437 ? 29.142  27.634  81.227  1.00 92.71  ?  687  PHE B CD2 1 
ATOM   2911 C CE1 . PHE B 1 437 ? 29.165  27.557  83.983  1.00 87.84  ?  687  PHE B CE1 1 
ATOM   2912 C CE2 . PHE B 1 437 ? 28.763  26.480  81.889  1.00 88.52  ?  687  PHE B CE2 1 
ATOM   2913 C CZ  . PHE B 1 437 ? 28.775  26.443  83.269  1.00 82.21  ?  687  PHE B CZ  1 
ATOM   2914 N N   . SER B 1 438 ? 27.914  30.445  78.832  1.00 97.04  ?  688  SER B N   1 
ATOM   2915 C CA  . SER B 1 438 ? 27.044  29.794  77.865  1.00 97.67  ?  688  SER B CA  1 
ATOM   2916 C C   . SER B 1 438 ? 27.880  28.845  77.022  1.00 101.83 ?  688  SER B C   1 
ATOM   2917 O O   . SER B 1 438 ? 28.915  29.242  76.476  1.00 112.94 ?  688  SER B O   1 
ATOM   2918 C CB  . SER B 1 438 ? 26.336  30.814  76.971  1.00 107.67 ?  688  SER B CB  1 
ATOM   2919 O OG  . SER B 1 438 ? 27.239  31.388  76.044  1.00 112.63 ?  688  SER B OG  1 
ATOM   2920 N N   . LEU B 1 439 ? 27.437  27.596  76.924  1.00 96.80  ?  689  LEU B N   1 
ATOM   2921 C CA  . LEU B 1 439 ? 28.150  26.599  76.147  1.00 106.61 ?  689  LEU B CA  1 
ATOM   2922 C C   . LEU B 1 439 ? 27.230  26.002  75.091  1.00 110.62 ?  689  LEU B C   1 
ATOM   2923 O O   . LEU B 1 439 ? 26.011  25.944  75.283  1.00 111.87 ?  689  LEU B O   1 
ATOM   2924 C CB  . LEU B 1 439 ? 28.701  25.477  77.039  1.00 109.47 ?  689  LEU B CB  1 
ATOM   2925 C CG  . LEU B 1 439 ? 27.777  24.318  77.425  1.00 99.19  ?  689  LEU B CG  1 
ATOM   2926 C CD1 . LEU B 1 439 ? 28.570  23.223  78.115  1.00 95.11  ?  689  LEU B CD1 1 
ATOM   2927 C CD2 . LEU B 1 439 ? 26.639  24.789  78.315  1.00 107.74 ?  689  LEU B CD2 1 
ATOM   2928 N N   . PRO B 1 440 ? 27.779  25.564  73.961  1.00 112.95 ?  690  PRO B N   1 
ATOM   2929 C CA  . PRO B 1 440 ? 26.945  24.930  72.937  1.00 105.09 ?  690  PRO B CA  1 
ATOM   2930 C C   . PRO B 1 440 ? 26.462  23.566  73.396  1.00 112.99 ?  690  PRO B C   1 
ATOM   2931 O O   . PRO B 1 440 ? 27.058  22.919  74.260  1.00 114.24 ?  690  PRO B O   1 
ATOM   2932 C CB  . PRO B 1 440 ? 27.884  24.802  71.730  1.00 106.24 ?  690  PRO B CB  1 
ATOM   2933 C CG  . PRO B 1 440 ? 29.074  25.660  72.047  1.00 109.84 ?  690  PRO B CG  1 
ATOM   2934 C CD  . PRO B 1 440 ? 29.182  25.683  73.535  1.00 106.29 ?  690  PRO B CD  1 
ATOM   2935 N N   . SER B 1 441 ? 25.355  23.131  72.801  1.00 112.83 ?  691  SER B N   1 
ATOM   2936 C CA  . SER B 1 441 ? 24.907  21.767  73.019  1.00 108.39 ?  691  SER B CA  1 
ATOM   2937 C C   . SER B 1 441 ? 25.878  20.794  72.355  1.00 116.79 ?  691  SER B C   1 
ATOM   2938 O O   . SER B 1 441 ? 26.763  21.183  71.586  1.00 121.05 ?  691  SER B O   1 
ATOM   2939 C CB  . SER B 1 441 ? 23.494  21.567  72.478  1.00 114.66 ?  691  SER B CB  1 
ATOM   2940 O OG  . SER B 1 441 ? 23.489  21.573  71.062  1.00 115.19 ?  691  SER B OG  1 
ATOM   2941 N N   . SER B 1 442 ? 25.705  19.509  72.666  1.00 110.82 ?  692  SER B N   1 
ATOM   2942 C CA  . SER B 1 442 ? 26.619  18.445  72.251  1.00 116.45 ?  692  SER B CA  1 
ATOM   2943 C C   . SER B 1 442 ? 28.043  18.689  72.737  1.00 108.93 ?  692  SER B C   1 
ATOM   2944 O O   . SER B 1 442 ? 28.988  18.073  72.233  1.00 111.99 ?  692  SER B O   1 
ATOM   2945 C CB  . SER B 1 442 ? 26.616  18.253  70.730  1.00 113.17 ?  692  SER B CB  1 
ATOM   2946 O OG  . SER B 1 442 ? 27.116  19.400  70.065  1.00 106.76 ?  692  SER B OG  1 
ATOM   2947 N N   . ALA B 1 443 ? 28.212  19.583  73.708  1.00 114.43 ?  693  ALA B N   1 
ATOM   2948 C CA  . ALA B 1 443 ? 29.517  19.908  74.267  1.00 106.92 ?  693  ALA B CA  1 
ATOM   2949 C C   . ALA B 1 443 ? 29.455  19.715  75.772  1.00 96.34  ?  693  ALA B C   1 
ATOM   2950 O O   . ALA B 1 443 ? 28.716  20.426  76.461  1.00 99.36  ?  693  ALA B O   1 
ATOM   2951 C CB  . ALA B 1 443 ? 29.929  21.343  73.923  1.00 109.33 ?  693  ALA B CB  1 
ATOM   2952 N N   . SER B 1 444 ? 30.218  18.753  76.278  1.00 89.17  ?  694  SER B N   1 
ATOM   2953 C CA  . SER B 1 444 ? 30.267  18.506  77.710  1.00 94.89  ?  694  SER B CA  1 
ATOM   2954 C C   . SER B 1 444 ? 31.257  19.453  78.375  1.00 100.71 ?  694  SER B C   1 
ATOM   2955 O O   . SER B 1 444 ? 32.324  19.747  77.828  1.00 100.07 ?  694  SER B O   1 
ATOM   2956 C CB  . SER B 1 444 ? 30.650  17.052  77.985  1.00 94.06  ?  694  SER B CB  1 
ATOM   2957 O OG  . SER B 1 444 ? 31.590  16.587  77.033  1.00 94.26  ?  694  SER B OG  1 
ATOM   2958 N N   . TYR B 1 445 ? 30.896  19.930  79.563  1.00 94.09  ?  695  TYR B N   1 
ATOM   2959 C CA  . TYR B 1 445 ? 31.681  20.915  80.292  1.00 83.17  ?  695  TYR B CA  1 
ATOM   2960 C C   . TYR B 1 445 ? 32.323  20.267  81.511  1.00 82.58  ?  695  TYR B C   1 
ATOM   2961 O O   . TYR B 1 445 ? 31.671  19.512  82.239  1.00 82.48  ?  695  TYR B O   1 
ATOM   2962 C CB  . TYR B 1 445 ? 30.807  22.097  80.719  1.00 79.14  ?  695  TYR B CB  1 
ATOM   2963 C CG  . TYR B 1 445 ? 31.570  23.247  81.336  1.00 79.41  ?  695  TYR B CG  1 
ATOM   2964 C CD1 . TYR B 1 445 ? 32.726  23.736  80.743  1.00 88.25  ?  695  TYR B CD1 1 
ATOM   2965 C CD2 . TYR B 1 445 ? 31.124  23.857  82.501  1.00 78.04  ?  695  TYR B CD2 1 
ATOM   2966 C CE1 . TYR B 1 445 ? 33.424  24.791  81.301  1.00 93.78  ?  695  TYR B CE1 1 
ATOM   2967 C CE2 . TYR B 1 445 ? 31.815  24.914  83.066  1.00 83.27  ?  695  TYR B CE2 1 
ATOM   2968 C CZ  . TYR B 1 445 ? 32.963  25.377  82.461  1.00 86.41  ?  695  TYR B CZ  1 
ATOM   2969 O OH  . TYR B 1 445 ? 33.656  26.429  83.016  1.00 84.91  ?  695  TYR B OH  1 
ATOM   2970 N N   . THR B 1 446 ? 33.605  20.560  81.724  1.00 78.16  ?  696  THR B N   1 
ATOM   2971 C CA  . THR B 1 446 ? 34.357  20.043  82.863  1.00 76.73  ?  696  THR B CA  1 
ATOM   2972 C C   . THR B 1 446 ? 35.048  21.215  83.548  1.00 82.00  ?  696  THR B C   1 
ATOM   2973 O O   . THR B 1 446 ? 36.030  21.752  83.026  1.00 83.08  ?  696  THR B O   1 
ATOM   2974 C CB  . THR B 1 446 ? 35.377  18.991  82.426  1.00 83.35  ?  696  THR B CB  1 
ATOM   2975 O OG1 . THR B 1 446 ? 34.718  17.970  81.667  1.00 85.79  ?  696  THR B OG1 1 
ATOM   2976 C CG2 . THR B 1 446 ? 36.041  18.360  83.642  1.00 77.04  ?  696  THR B CG2 1 
ATOM   2977 N N   . TYR B 1 447 ? 34.532  21.613  84.708  1.00 77.88  ?  697  TYR B N   1 
ATOM   2978 C CA  . TYR B 1 447 ? 35.090  22.706  85.494  1.00 67.43  ?  697  TYR B CA  1 
ATOM   2979 C C   . TYR B 1 447 ? 35.623  22.140  86.804  1.00 64.75  ?  697  TYR B C   1 
ATOM   2980 O O   . TYR B 1 447 ? 34.856  21.599  87.607  1.00 67.13  ?  697  TYR B O   1 
ATOM   2981 C CB  . TYR B 1 447 ? 34.038  23.783  85.757  1.00 63.06  ?  697  TYR B CB  1 
ATOM   2982 C CG  . TYR B 1 447 ? 34.546  24.949  86.572  1.00 65.19  ?  697  TYR B CG  1 
ATOM   2983 C CD1 . TYR B 1 447 ? 34.350  25.000  87.947  1.00 62.48  ?  697  TYR B CD1 1 
ATOM   2984 C CD2 . TYR B 1 447 ? 35.224  26.000  85.968  1.00 65.40  ?  697  TYR B CD2 1 
ATOM   2985 C CE1 . TYR B 1 447 ? 34.813  26.064  88.695  1.00 64.70  ?  697  TYR B CE1 1 
ATOM   2986 C CE2 . TYR B 1 447 ? 35.690  27.069  86.708  1.00 63.35  ?  697  TYR B CE2 1 
ATOM   2987 C CZ  . TYR B 1 447 ? 35.482  27.097  88.071  1.00 70.01  ?  697  TYR B CZ  1 
ATOM   2988 O OH  . TYR B 1 447 ? 35.946  28.161  88.811  1.00 66.90  ?  697  TYR B OH  1 
ATOM   2989 N N   . ARG B 1 448 ? 36.931  22.269  87.016  1.00 56.36  ?  698  ARG B N   1 
ATOM   2990 C CA  . ARG B 1 448 ? 37.597  21.689  88.173  1.00 63.56  ?  698  ARG B CA  1 
ATOM   2991 C C   . ARG B 1 448 ? 38.387  22.759  88.909  1.00 64.81  ?  698  ARG B C   1 
ATOM   2992 O O   . ARG B 1 448 ? 39.201  23.461  88.302  1.00 60.89  ?  698  ARG B O   1 
ATOM   2993 C CB  . ARG B 1 448 ? 38.527  20.548  87.755  1.00 57.67  ?  698  ARG B CB  1 
ATOM   2994 C CG  . ARG B 1 448 ? 37.804  19.326  87.227  1.00 74.21  ?  698  ARG B CG  1 
ATOM   2995 C CD  . ARG B 1 448 ? 38.788  18.308  86.683  1.00 73.04  ?  698  ARG B CD  1 
ATOM   2996 N NE  . ARG B 1 448 ? 39.960  18.167  87.542  1.00 75.82  ?  698  ARG B NE  1 
ATOM   2997 C CZ  . ARG B 1 448 ? 40.002  17.412  88.634  1.00 73.77  ?  698  ARG B CZ  1 
ATOM   2998 N NH1 . ARG B 1 448 ? 38.931  16.727  89.012  1.00 65.97  1  698  ARG B NH1 1 
ATOM   2999 N NH2 . ARG B 1 448 ? 41.113  17.346  89.353  1.00 70.35  ?  698  ARG B NH2 1 
ATOM   3000 N N   . ARG B 1 449 ? 38.148  22.874  90.213  1.00 62.06  ?  699  ARG B N   1 
ATOM   3001 C CA  . ARG B 1 449 ? 38.896  23.790  91.063  1.00 69.55  ?  699  ARG B CA  1 
ATOM   3002 C C   . ARG B 1 449 ? 39.084  23.148  92.429  1.00 58.74  ?  699  ARG B C   1 
ATOM   3003 O O   . ARG B 1 449 ? 38.342  22.242  92.819  1.00 63.16  ?  699  ARG B O   1 
ATOM   3004 C CB  . ARG B 1 449 ? 38.189  25.143  91.217  1.00 56.22  ?  699  ARG B CB  1 
ATOM   3005 C CG  . ARG B 1 449 ? 38.151  26.002  89.966  1.00 69.21  ?  699  ARG B CG  1 
ATOM   3006 C CD  . ARG B 1 449 ? 39.544  26.396  89.510  1.00 62.25  ?  699  ARG B CD  1 
ATOM   3007 N NE  . ARG B 1 449 ? 39.495  27.407  88.459  1.00 75.11  ?  699  ARG B NE  1 
ATOM   3008 C CZ  . ARG B 1 449 ? 39.249  27.146  87.179  1.00 72.71  ?  699  ARG B CZ  1 
ATOM   3009 N NH1 . ARG B 1 449 ? 39.027  25.900  86.783  1.00 68.42  1  699  ARG B NH1 1 
ATOM   3010 N NH2 . ARG B 1 449 ? 39.223  28.132  86.293  1.00 73.72  ?  699  ARG B NH2 1 
ATOM   3011 N N   . GLN B 1 450 ? 40.090  23.630  93.154  1.00 69.47  ?  700  GLN B N   1 
ATOM   3012 C CA  . GLN B 1 450 ? 40.295  23.268  94.552  1.00 71.71  ?  700  GLN B CA  1 
ATOM   3013 C C   . GLN B 1 450 ? 39.838  24.435  95.419  1.00 66.54  ?  700  GLN B C   1 
ATOM   3014 O O   . GLN B 1 450 ? 40.438  25.515  95.384  1.00 77.27  ?  700  GLN B O   1 
ATOM   3015 C CB  . GLN B 1 450 ? 41.756  22.923  94.831  1.00 68.08  ?  700  GLN B CB  1 
ATOM   3016 C CG  . GLN B 1 450 ? 42.197  21.591  94.255  1.00 77.70  ?  700  GLN B CG  1 
ATOM   3017 C CD  . GLN B 1 450 ? 42.836  20.693  95.297  1.00 89.01  ?  700  GLN B CD  1 
ATOM   3018 O OE1 . GLN B 1 450 ? 42.145  20.051  96.088  1.00 74.74  ?  700  GLN B OE1 1 
ATOM   3019 N NE2 . GLN B 1 450 ? 44.164  20.646  95.302  1.00 96.49  ?  700  GLN B NE2 1 
ATOM   3020 N N   . LEU B 1 451 ? 38.780  24.217  96.194  1.00 68.19  ?  701  LEU B N   1 
ATOM   3021 C CA  . LEU B 1 451 ? 38.206  25.255  97.041  1.00 73.32  ?  701  LEU B CA  1 
ATOM   3022 C C   . LEU B 1 451 ? 38.903  25.236  98.397  1.00 67.92  ?  701  LEU B C   1 
ATOM   3023 O O   . LEU B 1 451 ? 38.857  24.228  99.111  1.00 68.58  ?  701  LEU B O   1 
ATOM   3024 C CB  . LEU B 1 451 ? 36.700  25.048  97.196  1.00 72.53  ?  701  LEU B CB  1 
ATOM   3025 C CG  . LEU B 1 451 ? 35.929  24.852  95.886  1.00 56.01  ?  701  LEU B CG  1 
ATOM   3026 C CD1 . LEU B 1 451 ? 34.433  24.761  96.141  1.00 62.45  ?  701  LEU B CD1 1 
ATOM   3027 C CD2 . LEU B 1 451 ? 36.240  25.964  94.894  1.00 63.72  ?  701  LEU B CD2 1 
ATOM   3028 N N   . GLN B 1 452 ? 39.545  26.347  98.749  1.00 65.66  ?  702  GLN B N   1 
ATOM   3029 C CA  . GLN B 1 452 ? 40.378  26.435  99.939  1.00 73.29  ?  702  GLN B CA  1 
ATOM   3030 C C   . GLN B 1 452 ? 39.736  27.351  100.972 1.00 79.66  ?  702  GLN B C   1 
ATOM   3031 O O   . GLN B 1 452 ? 39.210  28.416  100.632 1.00 78.67  ?  702  GLN B O   1 
ATOM   3032 C CB  . GLN B 1 452 ? 41.777  26.949  99.584  1.00 79.03  ?  702  GLN B CB  1 
ATOM   3033 C CG  . GLN B 1 452 ? 42.754  26.969  100.746 1.00 79.63  ?  702  GLN B CG  1 
ATOM   3034 C CD  . GLN B 1 452 ? 44.099  27.549  100.358 1.00 88.29  ?  702  GLN B CD  1 
ATOM   3035 O OE1 . GLN B 1 452 ? 44.172  28.567  99.669  1.00 86.06  ?  702  GLN B OE1 1 
ATOM   3036 N NE2 . GLN B 1 452 ? 45.172  26.899  100.791 1.00 96.89  ?  702  GLN B NE2 1 
ATOM   3037 N N   . ASN B 1 453 ? 39.787  26.933  102.230 1.00 79.89  ?  703  ASN B N   1 
ATOM   3038 C CA  . ASN B 1 453 ? 39.229  27.727  103.319 1.00 83.24  ?  703  ASN B CA  1 
ATOM   3039 C C   . ASN B 1 453 ? 40.175  28.879  103.641 1.00 87.56  ?  703  ASN B C   1 
ATOM   3040 O O   . ASN B 1 453 ? 41.364  28.639  103.877 1.00 98.25  ?  703  ASN B O   1 
ATOM   3041 C CB  . ASN B 1 453 ? 39.011  26.845  104.542 1.00 86.42  ?  703  ASN B CB  1 
ATOM   3042 C CG  . ASN B 1 453 ? 38.295  27.564  105.670 1.00 93.52  ?  703  ASN B CG  1 
ATOM   3043 O OD1 . ASN B 1 453 ? 37.751  28.653  105.491 1.00 97.35  ?  703  ASN B OD1 1 
ATOM   3044 N ND2 . ASN B 1 453 ? 38.291  26.949  106.846 1.00 87.22  ?  703  ASN B ND2 1 
ATOM   3045 N N   . PRO B 1 454 ? 39.706  30.135  103.630 1.00 87.97  ?  704  PRO B N   1 
ATOM   3046 C CA  . PRO B 1 454 ? 40.601  31.257  103.969 1.00 87.22  ?  704  PRO B CA  1 
ATOM   3047 C C   . PRO B 1 454 ? 41.322  31.088  105.297 1.00 101.19 ?  704  PRO B C   1 
ATOM   3048 O O   . PRO B 1 454 ? 42.528  31.353  105.379 1.00 109.77 ?  704  PRO B O   1 
ATOM   3049 C CB  . PRO B 1 454 ? 39.648  32.459  103.985 1.00 81.68  ?  704  PRO B CB  1 
ATOM   3050 C CG  . PRO B 1 454 ? 38.586  32.092  103.014 1.00 77.90  ?  704  PRO B CG  1 
ATOM   3051 C CD  . PRO B 1 454 ? 38.394  30.603  103.154 1.00 80.03  ?  704  PRO B CD  1 
ATOM   3052 N N   . ALA B 1 455 ? 40.618  30.664  106.342 1.00 99.87  ?  705  ALA B N   1 
ATOM   3053 C CA  . ALA B 1 455 ? 41.276  30.241  107.569 1.00 89.46  ?  705  ALA B CA  1 
ATOM   3054 C C   . ALA B 1 455 ? 41.696  28.785  107.431 1.00 102.10 ?  705  ALA B C   1 
ATOM   3055 O O   . ALA B 1 455 ? 40.978  27.977  106.835 1.00 113.72 ?  705  ALA B O   1 
ATOM   3056 C CB  . ALA B 1 455 ? 40.349  30.418  108.771 1.00 83.65  ?  705  ALA B CB  1 
ATOM   3057 N N   . ASN B 1 456 ? 42.868  28.455  107.978 1.00 104.36 ?  706  ASN B N   1 
ATOM   3058 C CA  . ASN B 1 456 ? 43.461  27.132  107.800 1.00 115.30 ?  706  ASN B CA  1 
ATOM   3059 C C   . ASN B 1 456 ? 43.617  26.837  106.312 1.00 104.36 ?  706  ASN B C   1 
ATOM   3060 O O   . ASN B 1 456 ? 42.805  26.115  105.726 1.00 99.11  ?  706  ASN B O   1 
ATOM   3061 C CB  . ASN B 1 456 ? 42.614  26.054  108.487 1.00 113.14 ?  706  ASN B CB  1 
ATOM   3062 C CG  . ASN B 1 456 ? 43.309  24.701  108.546 1.00 114.97 ?  706  ASN B CG  1 
ATOM   3063 O OD1 . ASN B 1 456 ? 44.244  24.429  107.792 1.00 115.44 ?  706  ASN B OD1 1 
ATOM   3064 N ND2 . ASN B 1 456 ? 42.844  23.842  109.445 1.00 119.10 ?  706  ASN B ND2 1 
ATOM   3065 N N   . GLU B 1 457 ? 44.665  27.390  105.698 1.00 105.65 ?  707  GLU B N   1 
ATOM   3066 C CA  . GLU B 1 457 ? 44.874  27.252  104.261 1.00 103.21 ?  707  GLU B CA  1 
ATOM   3067 C C   . GLU B 1 457 ? 45.163  25.819  103.835 1.00 102.94 ?  707  GLU B C   1 
ATOM   3068 O O   . GLU B 1 457 ? 45.175  25.540  102.632 1.00 99.31  ?  707  GLU B O   1 
ATOM   3069 C CB  . GLU B 1 457 ? 46.017  28.167  103.820 1.00 104.88 ?  707  GLU B CB  1 
ATOM   3070 C CG  . GLU B 1 457 ? 45.838  29.617  104.248 1.00 112.85 ?  707  GLU B CG  1 
ATOM   3071 C CD  . GLU B 1 457 ? 47.082  30.455  104.022 1.00 135.58 ?  707  GLU B CD  1 
ATOM   3072 O OE1 . GLU B 1 457 ? 47.777  30.230  103.008 1.00 137.67 ?  707  GLU B OE1 1 
ATOM   3073 O OE2 . GLU B 1 457 ? 47.368  31.333  104.864 1.00 132.23 -1 707  GLU B OE2 1 
ATOM   3074 N N   . GLN B 1 458 ? 45.393  24.910  104.779 1.00 103.20 ?  708  GLN B N   1 
ATOM   3075 C CA  . GLN B 1 458 ? 45.621  23.505  104.475 1.00 105.30 ?  708  GLN B CA  1 
ATOM   3076 C C   . GLN B 1 458 ? 44.325  22.714  104.341 1.00 106.00 ?  708  GLN B C   1 
ATOM   3077 O O   . GLN B 1 458 ? 44.372  21.491  104.169 1.00 108.99 ?  708  GLN B O   1 
ATOM   3078 C CB  . GLN B 1 458 ? 46.522  22.879  105.540 1.00 109.15 ?  708  GLN B CB  1 
ATOM   3079 C CG  . GLN B 1 458 ? 47.991  23.249  105.387 1.00 114.50 ?  708  GLN B CG  1 
ATOM   3080 C CD  . GLN B 1 458 ? 48.779  23.063  106.669 1.00 124.08 ?  708  GLN B CD  1 
ATOM   3081 O OE1 . GLN B 1 458 ? 48.384  23.550  107.728 1.00 118.53 ?  708  GLN B OE1 1 
ATOM   3082 N NE2 . GLN B 1 458 ? 49.898  22.352  106.580 1.00 125.48 ?  708  GLN B NE2 1 
ATOM   3083 N N   . GLU B 1 459 ? 43.174  23.381  104.415 1.00 102.72 ?  709  GLU B N   1 
ATOM   3084 C CA  . GLU B 1 459 ? 41.875  22.762  104.161 1.00 91.08  ?  709  GLU B CA  1 
ATOM   3085 C C   . GLU B 1 459 ? 41.478  23.094  102.726 1.00 88.57  ?  709  GLU B C   1 
ATOM   3086 O O   . GLU B 1 459 ? 40.900  24.145  102.450 1.00 81.04  ?  709  GLU B O   1 
ATOM   3087 C CB  . GLU B 1 459 ? 40.827  23.254  105.155 1.00 97.10  ?  709  GLU B CB  1 
ATOM   3088 C CG  . GLU B 1 459 ? 40.746  22.447  106.439 1.00 101.32 ?  709  GLU B CG  1 
ATOM   3089 C CD  . GLU B 1 459 ? 39.663  22.954  107.373 1.00 108.97 ?  709  GLU B CD  1 
ATOM   3090 O OE1 . GLU B 1 459 ? 39.188  24.093  107.168 1.00 99.41  ?  709  GLU B OE1 1 
ATOM   3091 O OE2 . GLU B 1 459 ? 39.285  22.216  108.309 1.00 107.64 -1 709  GLU B OE2 1 
ATOM   3092 N N   . LYS B 1 460 ? 41.798  22.189  101.804 1.00 84.95  ?  710  LYS B N   1 
ATOM   3093 C CA  . LYS B 1 460 ? 41.455  22.342  100.398 1.00 79.23  ?  710  LYS B CA  1 
ATOM   3094 C C   . LYS B 1 460 ? 40.519  21.217  99.982  1.00 79.09  ?  710  LYS B C   1 
ATOM   3095 O O   . LYS B 1 460 ? 40.801  20.041  100.235 1.00 76.62  ?  710  LYS B O   1 
ATOM   3096 C CB  . LYS B 1 460 ? 42.708  22.355  99.516  1.00 80.04  ?  710  LYS B CB  1 
ATOM   3097 C CG  . LYS B 1 460 ? 43.510  23.642  99.631  1.00 81.09  ?  710  LYS B CG  1 
ATOM   3098 C CD  . LYS B 1 460 ? 44.487  23.822  98.478  1.00 91.40  ?  710  LYS B CD  1 
ATOM   3099 C CE  . LYS B 1 460 ? 45.741  22.986  98.665  1.00 102.92 ?  710  LYS B CE  1 
ATOM   3100 N NZ  . LYS B 1 460 ? 46.783  23.342  97.662  1.00 96.96  1  710  LYS B NZ  1 
ATOM   3101 N N   . ILE B 1 461 ? 39.409  21.582  99.349  1.00 77.64  ?  711  ILE B N   1 
ATOM   3102 C CA  . ILE B 1 461 ? 38.397  20.614  98.938  1.00 73.16  ?  711  ILE B CA  1 
ATOM   3103 C C   . ILE B 1 461 ? 38.342  20.570  97.415  1.00 70.25  ?  711  ILE B C   1 
ATOM   3104 O O   . ILE B 1 461 ? 38.480  21.612  96.756  1.00 75.08  ?  711  ILE B O   1 
ATOM   3105 C CB  . ILE B 1 461 ? 37.027  20.950  99.557  1.00 66.65  ?  711  ILE B CB  1 
ATOM   3106 C CG1 . ILE B 1 461 ? 36.553  19.797  100.439 1.00 75.21  ?  711  ILE B CG1 1 
ATOM   3107 C CG2 . ILE B 1 461 ? 35.982  21.250  98.487  1.00 71.15  ?  711  ILE B CG2 1 
ATOM   3108 C CD1 . ILE B 1 461 ? 37.622  19.256  101.349 1.00 92.25  ?  711  ILE B CD1 1 
ATOM   3109 N N   . PRO B 1 462 ? 38.181  19.394  96.815  1.00 68.20  ?  712  PRO B N   1 
ATOM   3110 C CA  . PRO B 1 462 ? 38.031  19.326  95.359  1.00 64.97  ?  712  PRO B CA  1 
ATOM   3111 C C   . PRO B 1 462 ? 36.619  19.691  94.931  1.00 60.74  ?  712  PRO B C   1 
ATOM   3112 O O   . PRO B 1 462 ? 35.633  19.299  95.561  1.00 61.73  ?  712  PRO B O   1 
ATOM   3113 C CB  . PRO B 1 462 ? 38.347  17.859  95.042  1.00 59.63  ?  712  PRO B CB  1 
ATOM   3114 C CG  . PRO B 1 462 ? 37.973  17.128  96.285  1.00 61.41  ?  712  PRO B CG  1 
ATOM   3115 C CD  . PRO B 1 462 ? 38.299  18.058  97.425  1.00 76.28  ?  712  PRO B CD  1 
ATOM   3116 N N   . PHE B 1 463 ? 36.530  20.463  93.851  1.00 63.37  ?  713  PHE B N   1 
ATOM   3117 C CA  . PHE B 1 463 ? 35.253  20.804  93.238  1.00 56.73  ?  713  PHE B CA  1 
ATOM   3118 C C   . PHE B 1 463 ? 35.319  20.444  91.764  1.00 67.11  ?  713  PHE B C   1 
ATOM   3119 O O   . PHE B 1 463 ? 36.119  21.018  91.018  1.00 68.67  ?  713  PHE B O   1 
ATOM   3120 C CB  . PHE B 1 463 ? 34.916  22.288  93.416  1.00 60.08  ?  713  PHE B CB  1 
ATOM   3121 C CG  . PHE B 1 463 ? 33.668  22.709  92.691  1.00 60.92  ?  713  PHE B CG  1 
ATOM   3122 C CD1 . PHE B 1 463 ? 32.437  22.173  93.034  1.00 56.58  ?  713  PHE B CD1 1 
ATOM   3123 C CD2 . PHE B 1 463 ? 33.725  23.642  91.668  1.00 58.91  ?  713  PHE B CD2 1 
ATOM   3124 C CE1 . PHE B 1 463 ? 31.286  22.557  92.369  1.00 51.11  ?  713  PHE B CE1 1 
ATOM   3125 C CE2 . PHE B 1 463 ? 32.578  24.032  91.000  1.00 64.06  ?  713  PHE B CE2 1 
ATOM   3126 C CZ  . PHE B 1 463 ? 31.357  23.489  91.351  1.00 63.88  ?  713  PHE B CZ  1 
ATOM   3127 N N   . HIS B 1 464 ? 34.486  19.493  91.353  1.00 69.53  ?  714  HIS B N   1 
ATOM   3128 C CA  . HIS B 1 464 ? 34.407  19.047  89.969  1.00 65.99  ?  714  HIS B CA  1 
ATOM   3129 C C   . HIS B 1 464 ? 32.974  19.212  89.489  1.00 65.61  ?  714  HIS B C   1 
ATOM   3130 O O   . HIS B 1 464 ? 32.066  18.547  90.002  1.00 66.96  ?  714  HIS B O   1 
ATOM   3131 C CB  . HIS B 1 464 ? 34.858  17.585  89.845  1.00 67.72  ?  714  HIS B CB  1 
ATOM   3132 C CG  . HIS B 1 464 ? 34.851  17.063  88.439  1.00 74.95  ?  714  HIS B CG  1 
ATOM   3133 N ND1 . HIS B 1 464 ? 35.980  16.562  87.828  1.00 79.05  ?  714  HIS B ND1 1 
ATOM   3134 C CD2 . HIS B 1 464 ? 33.851  16.943  87.534  1.00 77.16  ?  714  HIS B CD2 1 
ATOM   3135 C CE1 . HIS B 1 464 ? 35.679  16.168  86.603  1.00 79.41  ?  714  HIS B CE1 1 
ATOM   3136 N NE2 . HIS B 1 464 ? 34.393  16.388  86.400  1.00 70.67  ?  714  HIS B NE2 1 
ATOM   3137 N N   . LEU B 1 465 ? 32.774  20.097  88.520  1.00 66.22  ?  715  LEU B N   1 
ATOM   3138 C CA  . LEU B 1 465 ? 31.471  20.320  87.907  1.00 60.51  ?  715  LEU B CA  1 
ATOM   3139 C C   . LEU B 1 465 ? 31.476  19.688  86.522  1.00 67.78  ?  715  LEU B C   1 
ATOM   3140 O O   . LEU B 1 465 ? 32.211  20.132  85.633  1.00 78.70  ?  715  LEU B O   1 
ATOM   3141 C CB  . LEU B 1 465 ? 31.149  21.812  87.822  1.00 57.38  ?  715  LEU B CB  1 
ATOM   3142 C CG  . LEU B 1 465 ? 29.831  22.149  87.125  1.00 61.56  ?  715  LEU B CG  1 
ATOM   3143 C CD1 . LEU B 1 465 ? 28.654  21.508  87.848  1.00 64.35  ?  715  LEU B CD1 1 
ATOM   3144 C CD2 . LEU B 1 465 ? 29.653  23.651  87.030  1.00 58.29  ?  715  LEU B CD2 1 
ATOM   3145 N N   . GLN B 1 466 ? 30.656  18.656  86.341  1.00 68.09  ?  716  GLN B N   1 
ATOM   3146 C CA  . GLN B 1 466 ? 30.537  17.951  85.071  1.00 69.92  ?  716  GLN B CA  1 
ATOM   3147 C C   . GLN B 1 466 ? 29.131  18.161  84.530  1.00 72.77  ?  716  GLN B C   1 
ATOM   3148 O O   . GLN B 1 466 ? 28.152  17.744  85.158  1.00 73.94  ?  716  GLN B O   1 
ATOM   3149 C CB  . GLN B 1 466 ? 30.832  16.458  85.238  1.00 68.89  ?  716  GLN B CB  1 
ATOM   3150 C CG  . GLN B 1 466 ? 30.889  15.687  83.930  1.00 73.79  ?  716  GLN B CG  1 
ATOM   3151 C CD  . GLN B 1 466 ? 32.131  16.001  83.118  1.00 82.56  ?  716  GLN B CD  1 
ATOM   3152 O OE1 . GLN B 1 466 ? 33.174  16.356  83.668  1.00 81.04  ?  716  GLN B OE1 1 
ATOM   3153 N NE2 . GLN B 1 466 ? 32.025  15.872  81.801  1.00 78.29  ?  716  GLN B NE2 1 
ATOM   3154 N N   . ILE B 1 467 ? 29.033  18.808  83.374  1.00 76.56  ?  717  ILE B N   1 
ATOM   3155 C CA  . ILE B 1 467 ? 27.756  19.097  82.732  1.00 77.60  ?  717  ILE B CA  1 
ATOM   3156 C C   . ILE B 1 467 ? 27.683  18.266  81.459  1.00 86.49  ?  717  ILE B C   1 
ATOM   3157 O O   . ILE B 1 467 ? 28.442  18.499  80.509  1.00 93.91  ?  717  ILE B O   1 
ATOM   3158 C CB  . ILE B 1 467 ? 27.594  20.595  82.440  1.00 76.67  ?  717  ILE B CB  1 
ATOM   3159 C CG1 . ILE B 1 467 ? 27.513  21.376  83.754  1.00 72.29  ?  717  ILE B CG1 1 
ATOM   3160 C CG2 . ILE B 1 467 ? 26.360  20.841  81.587  1.00 80.13  ?  717  ILE B CG2 1 
ATOM   3161 C CD1 . ILE B 1 467 ? 27.461  22.874  83.577  1.00 86.17  ?  717  ILE B CD1 1 
ATOM   3162 N N   . SER B 1 468 ? 26.773  17.295  81.438  1.00 89.60  ?  718  SER B N   1 
ATOM   3163 C CA  . SER B 1 468 ? 26.655  16.405  80.295  1.00 79.88  ?  718  SER B CA  1 
ATOM   3164 C C   . SER B 1 468 ? 25.996  17.119  79.118  1.00 83.17  ?  718  SER B C   1 
ATOM   3165 O O   . SER B 1 468 ? 25.568  18.273  79.210  1.00 81.37  ?  718  SER B O   1 
ATOM   3166 C CB  . SER B 1 468 ? 25.853  15.155  80.668  1.00 85.40  ?  718  SER B CB  1 
ATOM   3167 O OG  . SER B 1 468 ? 26.497  14.428  81.698  1.00 104.33 ?  718  SER B OG  1 
ATOM   3168 N N   . LYS B 1 469 ? 25.915  16.405  77.998  1.00 95.82  ?  719  LYS B N   1 
ATOM   3169 C CA  . LYS B 1 469 ? 25.369  16.982  76.778  1.00 87.84  ?  719  LYS B CA  1 
ATOM   3170 C C   . LYS B 1 469 ? 23.892  17.316  76.947  1.00 90.94  ?  719  LYS B C   1 
ATOM   3171 O O   . LYS B 1 469 ? 23.182  16.721  77.762  1.00 90.33  ?  719  LYS B O   1 
ATOM   3172 C CB  . LYS B 1 469 ? 25.561  16.023  75.603  1.00 85.15  ?  719  LYS B CB  1 
ATOM   3173 C CG  . LYS B 1 469 ? 26.983  15.975  75.071  1.00 96.46  ?  719  LYS B CG  1 
ATOM   3174 C CD  . LYS B 1 469 ? 27.130  14.928  73.980  1.00 96.01  ?  719  LYS B CD  1 
ATOM   3175 C CE  . LYS B 1 469 ? 28.534  14.934  73.400  1.00 101.82 ?  719  LYS B CE  1 
ATOM   3176 N NZ  . LYS B 1 469 ? 28.754  13.805  72.456  1.00 102.89 1  719  LYS B NZ  1 
ATOM   3177 N N   . GLN B 1 470 ? 23.434  18.288  76.163  1.00 93.84  ?  720  GLN B N   1 
ATOM   3178 C CA  . GLN B 1 470 ? 22.052  18.742  76.228  1.00 90.97  ?  720  GLN B CA  1 
ATOM   3179 C C   . GLN B 1 470 ? 21.154  17.766  75.480  1.00 97.34  ?  720  GLN B C   1 
ATOM   3180 O O   . GLN B 1 470 ? 21.323  17.556  74.274  1.00 93.51  ?  720  GLN B O   1 
ATOM   3181 C CB  . GLN B 1 470 ? 21.921  20.143  75.637  1.00 86.02  ?  720  GLN B CB  1 
ATOM   3182 C CG  . GLN B 1 470 ? 20.490  20.661  75.588  1.00 89.03  ?  720  GLN B CG  1 
ATOM   3183 C CD  . GLN B 1 470 ? 20.140  21.293  74.253  1.00 96.12  ?  720  GLN B CD  1 
ATOM   3184 O OE1 . GLN B 1 470 ? 20.320  20.684  73.199  1.00 99.10  ?  720  GLN B OE1 1 
ATOM   3185 N NE2 . GLN B 1 470 ? 19.640  22.523  74.293  1.00 86.19  ?  720  GLN B NE2 1 
ATOM   3186 N N   . VAL B 1 471 ? 20.205  17.169  76.192  1.00 95.22  ?  721  VAL B N   1 
ATOM   3187 C CA  . VAL B 1 471 ? 19.142  16.384  75.576  1.00 87.23  ?  721  VAL B CA  1 
ATOM   3188 C C   . VAL B 1 471 ? 17.915  17.275  75.457  1.00 83.22  ?  721  VAL B C   1 
ATOM   3189 O O   . VAL B 1 471 ? 17.664  18.130  76.317  1.00 84.09  ?  721  VAL B O   1 
ATOM   3190 C CB  . VAL B 1 471 ? 18.841  15.102  76.379  1.00 83.21  ?  721  VAL B CB  1 
ATOM   3191 C CG1 . VAL B 1 471 ? 20.122  14.321  76.630  1.00 85.98  ?  721  VAL B CG1 1 
ATOM   3192 C CG2 . VAL B 1 471 ? 18.152  15.426  77.691  1.00 89.50  ?  721  VAL B CG2 1 
ATOM   3193 N N   . ILE B 1 472 ? 17.163  17.102  74.375  1.00 82.07  ?  722  ILE B N   1 
ATOM   3194 C CA  . ILE B 1 472 ? 16.009  17.941  74.076  1.00 90.12  ?  722  ILE B CA  1 
ATOM   3195 C C   . ILE B 1 472 ? 14.769  17.060  74.025  1.00 81.33  ?  722  ILE B C   1 
ATOM   3196 O O   . ILE B 1 472 ? 14.743  16.055  73.305  1.00 81.23  ?  722  ILE B O   1 
ATOM   3197 C CB  . ILE B 1 472 ? 16.200  18.720  72.760  1.00 86.86  ?  722  ILE B CB  1 
ATOM   3198 C CG1 . ILE B 1 472 ? 14.851  19.037  72.109  1.00 79.63  ?  722  ILE B CG1 1 
ATOM   3199 C CG2 . ILE B 1 472 ? 17.111  17.960  71.807  1.00 75.90  ?  722  ILE B CG2 1 
ATOM   3200 C CD1 . ILE B 1 472 ? 14.972  19.809  70.811  1.00 84.53  ?  722  ILE B CD1 1 
ATOM   3201 N N   . HIS B 1 473 ? 13.754  17.433  74.799  1.00 83.57  ?  723  HIS B N   1 
ATOM   3202 C CA  . HIS B 1 473 ? 12.494  16.707  74.872  1.00 82.39  ?  723  HIS B CA  1 
ATOM   3203 C C   . HIS B 1 473 ? 11.428  17.485  74.117  1.00 80.56  ?  723  HIS B C   1 
ATOM   3204 O O   . HIS B 1 473 ? 11.277  18.695  74.320  1.00 85.88  ?  723  HIS B O   1 
ATOM   3205 C CB  . HIS B 1 473 ? 12.067  16.498  76.327  1.00 85.05  ?  723  HIS B CB  1 
ATOM   3206 C CG  . HIS B 1 473 ? 13.175  16.037  77.221  1.00 91.80  ?  723  HIS B CG  1 
ATOM   3207 N ND1 . HIS B 1 473 ? 13.355  14.715  77.564  1.00 101.36 ?  723  HIS B ND1 1 
ATOM   3208 C CD2 . HIS B 1 473 ? 14.164  16.724  77.842  1.00 86.26  ?  723  HIS B CD2 1 
ATOM   3209 C CE1 . HIS B 1 473 ? 14.405  14.607  78.359  1.00 100.86 ?  723  HIS B CE1 1 
ATOM   3210 N NE2 . HIS B 1 473 ? 14.914  15.811  78.543  1.00 91.20  ?  723  HIS B NE2 1 
ATOM   3211 N N   . ALA B 1 474 ? 10.692  16.793  73.251  1.00 81.57  ?  724  ALA B N   1 
ATOM   3212 C CA  . ALA B 1 474 ? 9.676   17.417  72.414  1.00 81.02  ?  724  ALA B CA  1 
ATOM   3213 C C   . ALA B 1 474 ? 8.384   16.624  72.519  1.00 78.76  ?  724  ALA B C   1 
ATOM   3214 O O   . ALA B 1 474 ? 8.337   15.456  72.119  1.00 83.67  ?  724  ALA B O   1 
ATOM   3215 C CB  . ALA B 1 474 ? 10.135  17.497  70.955  1.00 63.88  ?  724  ALA B CB  1 
ATOM   3216 N N   . GLU B 1 475 ? 7.344   17.252  73.062  1.00 78.91  ?  725  GLU B N   1 
ATOM   3217 C CA  . GLU B 1 475 ? 6.010   16.668  73.015  1.00 80.56  ?  725  GLU B CA  1 
ATOM   3218 C C   . GLU B 1 475 ? 5.543   16.644  71.566  1.00 76.50  ?  725  GLU B C   1 
ATOM   3219 O O   . GLU B 1 475 ? 5.514   17.685  70.902  1.00 80.07  ?  725  GLU B O   1 
ATOM   3220 C CB  . GLU B 1 475 ? 5.045   17.472  73.883  1.00 85.38  ?  725  GLU B CB  1 
ATOM   3221 C CG  . GLU B 1 475 ? 3.974   16.636  74.563  1.00 102.72 ?  725  GLU B CG  1 
ATOM   3222 C CD  . GLU B 1 475 ? 2.836   17.477  75.109  1.00 117.10 ?  725  GLU B CD  1 
ATOM   3223 O OE1 . GLU B 1 475 ? 1.691   17.302  74.639  1.00 117.96 ?  725  GLU B OE1 1 
ATOM   3224 O OE2 . GLU B 1 475 ? 3.087   18.318  75.998  1.00 121.63 -1 725  GLU B OE2 1 
ATOM   3225 N N   . ILE B 1 476 ? 5.192   15.460  71.064  1.00 80.85  ?  726  ILE B N   1 
ATOM   3226 C CA  . ILE B 1 476 ? 4.948   15.279  69.641  1.00 80.37  ?  726  ILE B CA  1 
ATOM   3227 C C   . ILE B 1 476 ? 3.582   14.648  69.412  1.00 72.27  ?  726  ILE B C   1 
ATOM   3228 O O   . ILE B 1 476 ? 3.021   13.975  70.279  1.00 72.37  ?  726  ILE B O   1 
ATOM   3229 C CB  . ILE B 1 476 ? 6.042   14.420  68.969  1.00 78.42  ?  726  ILE B CB  1 
ATOM   3230 C CG1 . ILE B 1 476 ? 6.120   13.043  69.634  1.00 76.16  ?  726  ILE B CG1 1 
ATOM   3231 C CG2 . ILE B 1 476 ? 7.386   15.131  69.017  1.00 70.35  ?  726  ILE B CG2 1 
ATOM   3232 C CD1 . ILE B 1 476 ? 7.066   12.082  68.948  1.00 74.46  ?  726  ILE B CD1 1 
ATOM   3233 N N   . GLN B 1 477 ? 3.053   14.887  68.215  1.00 71.73  ?  727  GLN B N   1 
ATOM   3234 C CA  . GLN B 1 477 ? 1.886   14.189  67.695  1.00 72.24  ?  727  GLN B CA  1 
ATOM   3235 C C   . GLN B 1 477 ? 2.316   13.346  66.504  1.00 70.97  ?  727  GLN B C   1 
ATOM   3236 O O   . GLN B 1 477 ? 2.933   13.863  65.566  1.00 76.82  ?  727  GLN B O   1 
ATOM   3237 C CB  . GLN B 1 477 ? 0.791   15.168  67.263  1.00 79.47  ?  727  GLN B CB  1 
ATOM   3238 C CG  . GLN B 1 477 ? 0.014   15.811  68.394  1.00 84.75  ?  727  GLN B CG  1 
ATOM   3239 C CD  . GLN B 1 477 ? -1.193  16.579  67.890  1.00 92.82  ?  727  GLN B CD  1 
ATOM   3240 O OE1 . GLN B 1 477 ? -1.719  16.291  66.814  1.00 98.86  ?  727  GLN B OE1 1 
ATOM   3241 N NE2 . GLN B 1 477 ? -1.635  17.564  68.663  1.00 96.56  ?  727  GLN B NE2 1 
ATOM   3242 N N   . HIS B 1 478 ? 1.995   12.057  66.542  1.00 73.37  ?  728  HIS B N   1 
ATOM   3243 C CA  . HIS B 1 478 ? 2.293   11.164  65.428  1.00 63.88  ?  728  HIS B CA  1 
ATOM   3244 C C   . HIS B 1 478 ? 1.291   11.426  64.310  1.00 63.13  ?  728  HIS B C   1 
ATOM   3245 O O   . HIS B 1 478 ? 0.094   11.162  64.464  1.00 65.35  ?  728  HIS B O   1 
ATOM   3246 C CB  . HIS B 1 478 ? 2.251   9.709   65.883  1.00 67.26  ?  728  HIS B CB  1 
ATOM   3247 C CG  . HIS B 1 478 ? 3.297   9.364   66.896  1.00 70.00  ?  728  HIS B CG  1 
ATOM   3248 N ND1 . HIS B 1 478 ? 4.395   8.586   66.598  1.00 83.33  ?  728  HIS B ND1 1 
ATOM   3249 C CD2 . HIS B 1 478 ? 3.416   9.697   68.203  1.00 74.16  ?  728  HIS B CD2 1 
ATOM   3250 C CE1 . HIS B 1 478 ? 5.144   8.452   67.679  1.00 75.70  ?  728  HIS B CE1 1 
ATOM   3251 N NE2 . HIS B 1 478 ? 4.572   9.117   68.666  1.00 81.21  ?  728  HIS B NE2 1 
ATOM   3252 N N   . LEU B 1 479 ? 1.775   11.955  63.188  1.00 66.36  ?  729  LEU B N   1 
ATOM   3253 C CA  . LEU B 1 479 ? 0.921   12.281  62.054  1.00 68.01  ?  729  LEU B CA  1 
ATOM   3254 C C   . LEU B 1 479 ? 0.793   11.142  61.052  1.00 66.37  ?  729  LEU B C   1 
ATOM   3255 O O   . LEU B 1 479 ? -0.030  11.235  60.135  1.00 66.45  ?  729  LEU B O   1 
ATOM   3256 C CB  . LEU B 1 479 ? 1.451   13.528  61.337  1.00 61.99  ?  729  LEU B CB  1 
ATOM   3257 C CG  . LEU B 1 479 ? 1.458   14.826  62.145  1.00 68.32  ?  729  LEU B CG  1 
ATOM   3258 C CD1 . LEU B 1 479 ? 2.063   15.960  61.333  1.00 61.29  ?  729  LEU B CD1 1 
ATOM   3259 C CD2 . LEU B 1 479 ? 0.052   15.183  62.605  1.00 70.81  ?  729  LEU B CD2 1 
ATOM   3260 N N   . GLY B 1 480 ? 1.574   10.082  61.201  1.00 61.21  ?  730  GLY B N   1 
ATOM   3261 C CA  . GLY B 1 480 ? 1.540   8.973   60.275  1.00 61.94  ?  730  GLY B CA  1 
ATOM   3262 C C   . GLY B 1 480 ? 2.704   8.989   59.305  1.00 64.74  ?  730  GLY B C   1 
ATOM   3263 O O   . GLY B 1 480 ? 3.745   9.611   59.531  1.00 68.29  ?  730  GLY B O   1 
ATOM   3264 N N   . HIS B 1 481 ? 2.509   8.287   58.194  1.00 59.61  ?  731  HIS B N   1 
ATOM   3265 C CA  . HIS B 1 481 ? 3.527   8.151   57.163  1.00 58.73  ?  731  HIS B CA  1 
ATOM   3266 C C   . HIS B 1 481 ? 3.197   9.051   55.981  1.00 54.22  ?  731  HIS B C   1 
ATOM   3267 O O   . HIS B 1 481 ? 2.054   9.074   55.512  1.00 54.91  ?  731  HIS B O   1 
ATOM   3268 C CB  . HIS B 1 481 ? 3.637   6.699   56.696  1.00 55.59  ?  731  HIS B CB  1 
ATOM   3269 C CG  . HIS B 1 481 ? 4.099   5.753   57.759  1.00 65.76  ?  731  HIS B CG  1 
ATOM   3270 N ND1 . HIS B 1 481 ? 5.398   5.299   57.836  1.00 67.49  ?  731  HIS B ND1 1 
ATOM   3271 C CD2 . HIS B 1 481 ? 3.436   5.172   58.787  1.00 60.33  ?  731  HIS B CD2 1 
ATOM   3272 C CE1 . HIS B 1 481 ? 5.516   4.480   58.867  1.00 74.43  ?  731  HIS B CE1 1 
ATOM   3273 N NE2 . HIS B 1 481 ? 4.340   4.386   59.460  1.00 83.41  ?  731  HIS B NE2 1 
ATOM   3274 N N   . TRP B 1 482 ? 4.194   9.793   55.507  1.00 58.23  ?  732  TRP B N   1 
ATOM   3275 C CA  . TRP B 1 482 ? 4.066   10.505  54.245  1.00 52.99  ?  732  TRP B CA  1 
ATOM   3276 C C   . TRP B 1 482 ? 4.200   9.511   53.100  1.00 58.15  ?  732  TRP B C   1 
ATOM   3277 O O   . TRP B 1 482 ? 4.981   8.558   53.176  1.00 59.74  ?  732  TRP B O   1 
ATOM   3278 C CB  . TRP B 1 482 ? 5.127   11.598  54.129  1.00 55.84  ?  732  TRP B CB  1 
ATOM   3279 C CG  . TRP B 1 482 ? 4.799   12.645  53.110  1.00 51.35  ?  732  TRP B CG  1 
ATOM   3280 C CD1 . TRP B 1 482 ? 3.582   12.880  52.538  1.00 61.36  ?  732  TRP B CD1 1 
ATOM   3281 C CD2 . TRP B 1 482 ? 5.700   13.600  52.539  1.00 53.58  ?  732  TRP B CD2 1 
ATOM   3282 N NE1 . TRP B 1 482 ? 3.670   13.922  51.647  1.00 52.75  ?  732  TRP B NE1 1 
ATOM   3283 C CE2 . TRP B 1 482 ? 4.960   14.382  51.630  1.00 54.84  ?  732  TRP B CE2 1 
ATOM   3284 C CE3 . TRP B 1 482 ? 7.061   13.870  52.709  1.00 50.57  ?  732  TRP B CE3 1 
ATOM   3285 C CZ2 . TRP B 1 482 ? 5.535   15.416  50.895  1.00 50.83  ?  732  TRP B CZ2 1 
ATOM   3286 C CZ3 . TRP B 1 482 ? 7.630   14.896  51.978  1.00 60.49  ?  732  TRP B CZ3 1 
ATOM   3287 C CH2 . TRP B 1 482 ? 6.868   15.657  51.083  1.00 56.05  ?  732  TRP B CH2 1 
ATOM   3288 N N   . MET B 1 483 ? 3.431   9.730   52.037  1.00 57.93  ?  733  MET B N   1 
ATOM   3289 C CA  . MET B 1 483 ? 3.308   8.747   50.970  1.00 57.86  ?  733  MET B CA  1 
ATOM   3290 C C   . MET B 1 483 ? 3.562   9.394   49.617  1.00 55.12  ?  733  MET B C   1 
ATOM   3291 O O   . MET B 1 483 ? 2.991   10.444  49.307  1.00 57.89  ?  733  MET B O   1 
ATOM   3292 C CB  . MET B 1 483 ? 1.922   8.095   50.994  1.00 64.04  ?  733  MET B CB  1 
ATOM   3293 C CG  . MET B 1 483 ? 1.580   7.437   52.323  1.00 60.41  ?  733  MET B CG  1 
ATOM   3294 S SD  . MET B 1 483 ? 2.206   5.755   52.484  1.00 63.12  ?  733  MET B SD  1 
ATOM   3295 C CE  . MET B 1 483 ? 1.150   4.893   51.323  1.00 53.61  ?  733  MET B CE  1 
ATOM   3296 N N   . ASP B 1 484 ? 4.420   8.762   48.822  1.00 51.91  ?  734  ASP B N   1 
ATOM   3297 C CA  . ASP B 1 484 ? 4.647   9.143   47.438  1.00 50.32  ?  734  ASP B CA  1 
ATOM   3298 C C   . ASP B 1 484 ? 3.632   8.441   46.544  1.00 57.41  ?  734  ASP B C   1 
ATOM   3299 O O   . ASP B 1 484 ? 3.134   7.362   46.871  1.00 60.08  ?  734  ASP B O   1 
ATOM   3300 C CB  . ASP B 1 484 ? 6.071   8.780   47.010  1.00 53.02  ?  734  ASP B CB  1 
ATOM   3301 C CG  . ASP B 1 484 ? 6.402   9.255   45.610  1.00 62.51  ?  734  ASP B CG  1 
ATOM   3302 O OD1 . ASP B 1 484 ? 5.696   10.150  45.097  1.00 57.87  ?  734  ASP B OD1 1 
ATOM   3303 O OD2 . ASP B 1 484 ? 7.367   8.728   45.017  1.00 67.40  -1 734  ASP B OD2 1 
ATOM   3304 N N   . GLY B 1 485 ? 3.324   9.064   45.406  1.00 61.33  ?  735  GLY B N   1 
ATOM   3305 C CA  . GLY B 1 485 ? 2.333   8.510   44.505  1.00 49.96  ?  735  GLY B CA  1 
ATOM   3306 C C   . GLY B 1 485 ? 2.680   8.773   43.056  1.00 57.24  ?  735  GLY B C   1 
ATOM   3307 O O   . GLY B 1 485 ? 3.597   9.533   42.737  1.00 57.53  ?  735  GLY B O   1 
ATOM   3308 N N   . THR B 1 486 ? 1.923   8.124   42.174  1.00 57.05  ?  736  THR B N   1 
ATOM   3309 C CA  . THR B 1 486 ? 2.097   8.257   40.735  1.00 50.66  ?  736  THR B CA  1 
ATOM   3310 C C   . THR B 1 486 ? 0.815   8.796   40.118  1.00 56.82  ?  736  THR B C   1 
ATOM   3311 O O   . THR B 1 486 ? -0.262  8.221   40.309  1.00 64.75  ?  736  THR B O   1 
ATOM   3312 C CB  . THR B 1 486 ? 2.464   6.916   40.092  1.00 54.40  ?  736  THR B CB  1 
ATOM   3313 O OG1 . THR B 1 486 ? 3.675   6.421   40.675  1.00 63.47  ?  736  THR B OG1 1 
ATOM   3314 C CG2 . THR B 1 486 ? 2.662   7.084   38.592  1.00 53.14  ?  736  THR B CG2 1 
ATOM   3315 N N   . PHE B 1 487 ? 0.937   9.900   39.387  1.00 53.85  ?  737  PHE B N   1 
ATOM   3316 C CA  . PHE B 1 487 ? -0.195  10.536  38.722  1.00 55.44  ?  737  PHE B CA  1 
ATOM   3317 C C   . PHE B 1 487 ? -0.555  9.730   37.478  1.00 50.85  ?  737  PHE B C   1 
ATOM   3318 O O   . PHE B 1 487 ? 0.230   9.663   36.527  1.00 54.42  ?  737  PHE B O   1 
ATOM   3319 C CB  . PHE B 1 487 ? 0.167   11.977  38.365  1.00 60.20  ?  737  PHE B CB  1 
ATOM   3320 C CG  . PHE B 1 487 ? -1.011  12.849  38.032  1.00 52.60  ?  737  PHE B CG  1 
ATOM   3321 C CD1 . PHE B 1 487 ? -1.574  12.828  36.767  1.00 58.30  ?  737  PHE B CD1 1 
ATOM   3322 C CD2 . PHE B 1 487 ? -1.535  13.716  38.976  1.00 61.37  ?  737  PHE B CD2 1 
ATOM   3323 C CE1 . PHE B 1 487 ? -2.650  13.640  36.456  1.00 60.27  ?  737  PHE B CE1 1 
ATOM   3324 C CE2 . PHE B 1 487 ? -2.605  14.533  38.671  1.00 59.54  ?  737  PHE B CE2 1 
ATOM   3325 C CZ  . PHE B 1 487 ? -3.164  14.495  37.409  1.00 56.99  ?  737  PHE B CZ  1 
ATOM   3326 N N   . ASN B 1 488 ? -1.735  9.113   37.481  1.00 50.52  ?  738  ASN B N   1 
ATOM   3327 C CA  . ASN B 1 488 ? -2.207  8.314   36.356  1.00 50.88  ?  738  ASN B CA  1 
ATOM   3328 C C   . ASN B 1 488 ? -3.545  8.853   35.869  1.00 52.31  ?  738  ASN B C   1 
ATOM   3329 O O   . ASN B 1 488 ? -4.492  8.982   36.652  1.00 56.41  ?  738  ASN B O   1 
ATOM   3330 C CB  . ASN B 1 488 ? -2.336  6.836   36.737  1.00 57.24  ?  738  ASN B CB  1 
ATOM   3331 C CG  . ASN B 1 488 ? -0.997  6.125   36.769  1.00 53.87  ?  738  ASN B CG  1 
ATOM   3332 O OD1 . ASN B 1 488 ? -0.040  6.554   36.126  1.00 62.86  ?  738  ASN B OD1 1 
ATOM   3333 N ND2 . ASN B 1 488 ? -0.925  5.028   37.514  1.00 70.03  ?  738  ASN B ND2 1 
ATOM   3334 N N   . LEU B 1 489 ? -3.614  9.156   34.576  1.00 51.32  ?  739  LEU B N   1 
ATOM   3335 C CA  . LEU B 1 489 ? -4.801  9.713   33.940  1.00 57.51  ?  739  LEU B CA  1 
ATOM   3336 C C   . LEU B 1 489 ? -5.465  8.635   33.094  1.00 52.87  ?  739  LEU B C   1 
ATOM   3337 O O   . LEU B 1 489 ? -4.802  7.990   32.275  1.00 60.68  ?  739  LEU B O   1 
ATOM   3338 C CB  . LEU B 1 489 ? -4.428  10.919  33.075  1.00 52.10  ?  739  LEU B CB  1 
ATOM   3339 C CG  . LEU B 1 489 ? -5.530  11.852  32.577  1.00 54.69  ?  739  LEU B CG  1 
ATOM   3340 C CD1 . LEU B 1 489 ? -6.185  12.575  33.739  1.00 68.86  ?  739  LEU B CD1 1 
ATOM   3341 C CD2 . LEU B 1 489 ? -4.951  12.846  31.585  1.00 53.35  ?  739  LEU B CD2 1 
ATOM   3342 N N   . LYS B 1 490 ? -6.768  8.439   33.292  1.00 51.20  ?  740  LYS B N   1 
ATOM   3343 C CA  . LYS B 1 490 ? -7.509  7.420   32.564  1.00 58.81  ?  740  LYS B CA  1 
ATOM   3344 C C   . LYS B 1 490 ? -8.845  7.972   32.093  1.00 51.40  ?  740  LYS B C   1 
ATOM   3345 O O   . LYS B 1 490 ? -9.516  8.708   32.821  1.00 55.77  ?  740  LYS B O   1 
ATOM   3346 C CB  . LYS B 1 490 ? -7.746  6.170   33.423  1.00 57.46  ?  740  LYS B CB  1 
ATOM   3347 C CG  . LYS B 1 490 ? -6.551  5.239   33.519  1.00 67.97  ?  740  LYS B CG  1 
ATOM   3348 C CD  . LYS B 1 490 ? -6.980  3.851   33.966  1.00 67.26  ?  740  LYS B CD  1 
ATOM   3349 C CE  . LYS B 1 490 ? -5.812  2.879   33.962  1.00 70.77  ?  740  LYS B CE  1 
ATOM   3350 N NZ  . LYS B 1 490 ? -4.752  3.285   34.926  1.00 92.89  1  740  LYS B NZ  1 
ATOM   3351 N N   . THR B 1 491 ? -9.227  7.599   30.873  1.00 51.97  ?  741  THR B N   1 
ATOM   3352 C CA  . THR B 1 491 ? -10.505 7.973   30.283  1.00 60.25  ?  741  THR B CA  1 
ATOM   3353 C C   . THR B 1 491 ? -11.252 6.708   29.885  1.00 52.15  ?  741  THR B C   1 
ATOM   3354 O O   . THR B 1 491 ? -10.696 5.846   29.197  1.00 64.69  ?  741  THR B O   1 
ATOM   3355 C CB  . THR B 1 491 ? -10.310 8.877   29.062  1.00 56.45  ?  741  THR B CB  1 
ATOM   3356 O OG1 . THR B 1 491 ? -9.595  10.057  29.447  1.00 64.00  ?  741  THR B OG1 1 
ATOM   3357 C CG2 . THR B 1 491 ? -11.655 9.272   28.471  1.00 53.33  ?  741  THR B CG2 1 
ATOM   3358 N N   . ALA B 1 492 ? -12.506 6.600   30.318  1.00 51.75  ?  742  ALA B N   1 
ATOM   3359 C CA  . ALA B 1 492 ? -13.340 5.435   30.034  1.00 51.76  ?  742  ALA B CA  1 
ATOM   3360 C C   . ALA B 1 492 ? -14.660 5.911   29.444  1.00 54.16  ?  742  ALA B C   1 
ATOM   3361 O O   . ALA B 1 492 ? -15.492 6.483   30.156  1.00 57.23  ?  742  ALA B O   1 
ATOM   3362 C CB  . ALA B 1 492 ? -13.575 4.605   31.296  1.00 51.16  ?  742  ALA B CB  1 
ATOM   3363 N N   . PHE B 1 493 ? -14.852 5.673   28.150  1.00 52.67  ?  743  PHE B N   1 
ATOM   3364 C CA  . PHE B 1 493 ? -16.086 6.037   27.467  1.00 53.62  ?  743  PHE B CA  1 
ATOM   3365 C C   . PHE B 1 493 ? -17.029 4.841   27.458  1.00 58.83  ?  743  PHE B C   1 
ATOM   3366 O O   . PHE B 1 493 ? -16.732 3.815   26.837  1.00 67.40  ?  743  PHE B O   1 
ATOM   3367 C CB  . PHE B 1 493 ? -15.804 6.507   26.041  1.00 54.02  ?  743  PHE B CB  1 
ATOM   3368 C CG  . PHE B 1 493 ? -17.045 6.760   25.230  1.00 59.84  ?  743  PHE B CG  1 
ATOM   3369 C CD1 . PHE B 1 493 ? -17.341 5.981   24.125  1.00 68.45  ?  743  PHE B CD1 1 
ATOM   3370 C CD2 . PHE B 1 493 ? -17.922 7.771   25.583  1.00 64.00  ?  743  PHE B CD2 1 
ATOM   3371 C CE1 . PHE B 1 493 ? -18.485 6.213   23.381  1.00 63.41  ?  743  PHE B CE1 1 
ATOM   3372 C CE2 . PHE B 1 493 ? -19.068 8.006   24.845  1.00 59.97  ?  743  PHE B CE2 1 
ATOM   3373 C CZ  . PHE B 1 493 ? -19.349 7.226   23.743  1.00 55.66  ?  743  PHE B CZ  1 
ATOM   3374 N N   . HIS B 1 494 ? -18.159 4.972   28.147  1.00 53.70  ?  744  HIS B N   1 
ATOM   3375 C CA  . HIS B 1 494 ? -19.172 3.928   28.144  1.00 56.13  ?  744  HIS B CA  1 
ATOM   3376 C C   . HIS B 1 494 ? -19.956 3.977   26.838  1.00 55.60  ?  744  HIS B C   1 
ATOM   3377 O O   . HIS B 1 494 ? -20.400 5.048   26.412  1.00 62.33  ?  744  HIS B O   1 
ATOM   3378 C CB  . HIS B 1 494 ? -20.112 4.092   29.338  1.00 52.70  ?  744  HIS B CB  1 
ATOM   3379 C CG  . HIS B 1 494 ? -19.461 3.827   30.661  1.00 64.58  ?  744  HIS B CG  1 
ATOM   3380 N ND1 . HIS B 1 494 ? -18.465 4.629   31.176  1.00 66.37  ?  744  HIS B ND1 1 
ATOM   3381 C CD2 . HIS B 1 494 ? -19.664 2.848   31.573  1.00 58.85  ?  744  HIS B CD2 1 
ATOM   3382 C CE1 . HIS B 1 494 ? -18.082 4.155   32.348  1.00 67.57  ?  744  HIS B CE1 1 
ATOM   3383 N NE2 . HIS B 1 494 ? -18.795 3.075   32.613  1.00 68.47  ?  744  HIS B NE2 1 
ATOM   3384 N N   . CYS B 1 495 ? -20.112 2.818   26.194  1.00 58.79  ?  745  CYS B N   1 
ATOM   3385 C CA  . CYS B 1 495 ? -20.881 2.764   24.956  1.00 60.53  ?  745  CYS B CA  1 
ATOM   3386 C C   . CYS B 1 495 ? -22.359 3.052   25.187  1.00 54.12  ?  745  CYS B C   1 
ATOM   3387 O O   . CYS B 1 495 ? -23.059 3.428   24.240  1.00 61.44  ?  745  CYS B O   1 
ATOM   3388 C CB  . CYS B 1 495 ? -20.706 1.401   24.279  1.00 57.17  ?  745  CYS B CB  1 
ATOM   3389 S SG  . CYS B 1 495 ? -19.005 0.999   23.772  1.00 68.21  ?  745  CYS B SG  1 
ATOM   3390 N N   . TYR B 1 496 ? -22.845 2.893   26.417  1.00 53.52  ?  746  TYR B N   1 
ATOM   3391 C CA  . TYR B 1 496 ? -24.218 3.244   26.752  1.00 53.56  ?  746  TYR B CA  1 
ATOM   3392 C C   . TYR B 1 496 ? -24.326 3.411   28.260  1.00 52.98  ?  746  TYR B C   1 
ATOM   3393 O O   . TYR B 1 496 ? -23.451 2.980   29.016  1.00 52.53  ?  746  TYR B O   1 
ATOM   3394 C CB  . TYR B 1 496 ? -25.214 2.190   26.250  1.00 54.01  ?  746  TYR B CB  1 
ATOM   3395 C CG  . TYR B 1 496 ? -25.139 0.858   26.968  1.00 66.78  ?  746  TYR B CG  1 
ATOM   3396 C CD1 . TYR B 1 496 ? -25.936 0.597   28.076  1.00 57.78  ?  746  TYR B CD1 1 
ATOM   3397 C CD2 . TYR B 1 496 ? -24.279 -0.141  26.533  1.00 60.59  ?  746  TYR B CD2 1 
ATOM   3398 C CE1 . TYR B 1 496 ? -25.872 -0.618  28.734  1.00 67.02  ?  746  TYR B CE1 1 
ATOM   3399 C CE2 . TYR B 1 496 ? -24.210 -1.359  27.184  1.00 63.37  ?  746  TYR B CE2 1 
ATOM   3400 C CZ  . TYR B 1 496 ? -25.009 -1.591  28.283  1.00 60.57  ?  746  TYR B CZ  1 
ATOM   3401 O OH  . TYR B 1 496 ? -24.943 -2.801  28.933  1.00 70.28  ?  746  TYR B OH  1 
ATOM   3402 N N   . GLY B 1 497 ? -25.413 4.048   28.685  1.00 54.75  ?  747  GLY B N   1 
ATOM   3403 C CA  . GLY B 1 497 ? -25.702 4.184   30.097  1.00 52.77  ?  747  GLY B CA  1 
ATOM   3404 C C   . GLY B 1 497 ? -24.762 5.132   30.828  1.00 53.73  ?  747  GLY B C   1 
ATOM   3405 O O   . GLY B 1 497 ? -23.999 5.901   30.242  1.00 52.78  ?  747  GLY B O   1 
ATOM   3406 N N   . SER B 1 498 ? -24.839 5.054   32.152  1.00 59.22  ?  748  SER B N   1 
ATOM   3407 C CA  . SER B 1 498 ? -24.063 5.910   33.032  1.00 55.93  ?  748  SER B CA  1 
ATOM   3408 C C   . SER B 1 498 ? -22.678 5.318   33.286  1.00 61.49  ?  748  SER B C   1 
ATOM   3409 O O   . SER B 1 498 ? -22.365 4.193   32.890  1.00 65.96  ?  748  SER B O   1 
ATOM   3410 C CB  . SER B 1 498 ? -24.801 6.120   34.354  1.00 64.73  ?  748  SER B CB  1 
ATOM   3411 O OG  . SER B 1 498 ? -24.987 4.892   35.037  1.00 75.37  ?  748  SER B OG  1 
ATOM   3412 N N   . CYS B 1 499 ? -21.843 6.102   33.962  1.00 63.70  ?  749  CYS B N   1 
ATOM   3413 C CA  . CYS B 1 499 ? -20.495 5.684   34.323  1.00 67.82  ?  749  CYS B CA  1 
ATOM   3414 C C   . CYS B 1 499 ? -20.540 4.969   35.669  1.00 64.23  ?  749  CYS B C   1 
ATOM   3415 O O   . CYS B 1 499 ? -20.894 5.574   36.687  1.00 66.30  ?  749  CYS B O   1 
ATOM   3416 C CB  . CYS B 1 499 ? -19.559 6.890   34.378  1.00 65.43  ?  749  CYS B CB  1 
ATOM   3417 S SG  . CYS B 1 499 ? -20.402 8.478   34.188  1.00 119.36 ?  749  CYS B SG  1 
ATOM   3418 N N   . GLU B 1 500 ? -20.179 3.689   35.672  1.00 62.02  ?  750  GLU B N   1 
ATOM   3419 C CA  . GLU B 1 500 ? -20.283 2.879   36.877  1.00 55.88  ?  750  GLU B CA  1 
ATOM   3420 C C   . GLU B 1 500 ? -19.205 3.259   37.888  1.00 54.20  ?  750  GLU B C   1 
ATOM   3421 O O   . GLU B 1 500 ? -18.083 3.625   37.529  1.00 58.46  ?  750  GLU B O   1 
ATOM   3422 C CB  . GLU B 1 500 ? -20.174 1.395   36.530  1.00 67.06  ?  750  GLU B CB  1 
ATOM   3423 C CG  . GLU B 1 500 ? -21.227 0.905   35.546  1.00 54.45  ?  750  GLU B CG  1 
ATOM   3424 C CD  . GLU B 1 500 ? -22.629 0.942   36.123  1.00 72.80  ?  750  GLU B CD  1 
ATOM   3425 O OE1 . GLU B 1 500 ? -23.595 0.740   35.357  1.00 85.07  ?  750  GLU B OE1 1 
ATOM   3426 O OE2 . GLU B 1 500 ? -22.767 1.172   37.343  1.00 85.21  -1 750  GLU B OE2 1 
ATOM   3427 N N   . LYS B 1 501 ? -19.559 3.160   39.167  1.00 54.08  ?  751  LYS B N   1 
ATOM   3428 C CA  . LYS B 1 501 ? -18.672 3.513   40.267  1.00 53.19  ?  751  LYS B CA  1 
ATOM   3429 C C   . LYS B 1 501 ? -18.190 2.249   40.967  1.00 53.97  ?  751  LYS B C   1 
ATOM   3430 O O   . LYS B 1 501 ? -18.999 1.386   41.324  1.00 56.84  ?  751  LYS B O   1 
ATOM   3431 C CB  . LYS B 1 501 ? -19.378 4.430   41.268  1.00 50.58  ?  751  LYS B CB  1 
ATOM   3432 C CG  . LYS B 1 501 ? -19.822 5.758   40.683  1.00 58.91  ?  751  LYS B CG  1 
ATOM   3433 C CD  . LYS B 1 501 ? -18.671 6.457   39.980  1.00 60.75  ?  751  LYS B CD  1 
ATOM   3434 C CE  . LYS B 1 501 ? -19.060 7.863   39.555  1.00 67.46  ?  751  LYS B CE  1 
ATOM   3435 N NZ  . LYS B 1 501 ? -20.307 7.871   38.744  1.00 72.21  1  751  LYS B NZ  1 
ATOM   3436 N N   . TYR B 1 502 ? -16.873 2.154   41.164  1.00 55.47  ?  752  TYR B N   1 
ATOM   3437 C CA  . TYR B 1 502 ? -16.243 1.011   41.829  1.00 52.06  ?  752  TYR B CA  1 
ATOM   3438 C C   . TYR B 1 502 ? -16.613 -0.302  41.140  1.00 56.00  ?  752  TYR B C   1 
ATOM   3439 O O   . TYR B 1 502 ? -16.983 -1.289  41.780  1.00 59.69  ?  752  TYR B O   1 
ATOM   3440 C CB  . TYR B 1 502 ? -16.597 0.977   43.317  1.00 54.85  ?  752  TYR B CB  1 
ATOM   3441 C CG  . TYR B 1 502 ? -16.031 2.145   44.094  1.00 52.64  ?  752  TYR B CG  1 
ATOM   3442 C CD1 . TYR B 1 502 ? -14.694 2.170   44.468  1.00 60.86  ?  752  TYR B CD1 1 
ATOM   3443 C CD2 . TYR B 1 502 ? -16.832 3.223   44.448  1.00 59.65  ?  752  TYR B CD2 1 
ATOM   3444 C CE1 . TYR B 1 502 ? -14.170 3.238   45.175  1.00 64.11  ?  752  TYR B CE1 1 
ATOM   3445 C CE2 . TYR B 1 502 ? -16.316 4.295   45.156  1.00 51.41  ?  752  TYR B CE2 1 
ATOM   3446 C CZ  . TYR B 1 502 ? -14.985 4.296   45.517  1.00 56.96  ?  752  TYR B CZ  1 
ATOM   3447 O OH  . TYR B 1 502 ? -14.467 5.358   46.220  1.00 71.44  ?  752  TYR B OH  1 
ATOM   3448 N N   . ALA B 1 503 ? -16.509 -0.304  39.813  1.00 52.75  ?  753  ALA B N   1 
ATOM   3449 C CA  . ALA B 1 503 ? -16.787 -1.484  39.011  1.00 51.35  ?  753  ALA B CA  1 
ATOM   3450 C C   . ALA B 1 503 ? -15.595 -1.932  38.181  1.00 53.97  ?  753  ALA B C   1 
ATOM   3451 O O   . ALA B 1 503 ? -15.695 -2.943  37.475  1.00 66.17  ?  753  ALA B O   1 
ATOM   3452 C CB  . ALA B 1 503 ? -17.987 -1.230  38.087  1.00 54.07  ?  753  ALA B CB  1 
ATOM   3453 N N   . TYR B 1 504 ? -14.477 -1.224  38.249  1.00 54.05  ?  754  TYR B N   1 
ATOM   3454 C CA  . TYR B 1 504 ? -13.303 -1.490  37.434  1.00 52.30  ?  754  TYR B CA  1 
ATOM   3455 C C   . TYR B 1 504 ? -12.064 -1.523  38.314  1.00 51.23  ?  754  TYR B C   1 
ATOM   3456 O O   . TYR B 1 504 ? -12.049 -0.937  39.402  1.00 55.52  ?  754  TYR B O   1 
ATOM   3457 C CB  . TYR B 1 504 ? -13.151 -0.423  36.341  1.00 52.70  ?  754  TYR B CB  1 
ATOM   3458 C CG  . TYR B 1 504 ? -14.450 -0.076  35.647  1.00 56.82  ?  754  TYR B CG  1 
ATOM   3459 C CD1 . TYR B 1 504 ? -15.136 -1.024  34.899  1.00 51.16  ?  754  TYR B CD1 1 
ATOM   3460 C CD2 . TYR B 1 504 ? -14.988 1.201   35.736  1.00 53.85  ?  754  TYR B CD2 1 
ATOM   3461 C CE1 . TYR B 1 504 ? -16.324 -0.711  34.264  1.00 53.45  ?  754  TYR B CE1 1 
ATOM   3462 C CE2 . TYR B 1 504 ? -16.175 1.523   35.102  1.00 50.46  ?  754  TYR B CE2 1 
ATOM   3463 C CZ  . TYR B 1 504 ? -16.839 0.564   34.368  1.00 59.61  ?  754  TYR B CZ  1 
ATOM   3464 O OH  . TYR B 1 504 ? -18.020 0.877   33.736  1.00 61.64  ?  754  TYR B OH  1 
ATOM   3465 N N   . PRO B 1 505 ? -11.005 -2.210  37.874  1.00 55.32  ?  755  PRO B N   1 
ATOM   3466 C CA  . PRO B 1 505 ? -9.822  -2.361  38.738  1.00 52.66  ?  755  PRO B CA  1 
ATOM   3467 C C   . PRO B 1 505 ? -9.119  -1.055  39.075  1.00 53.90  ?  755  PRO B C   1 
ATOM   3468 O O   . PRO B 1 505 ? -8.556  -0.940  40.171  1.00 51.26  ?  755  PRO B O   1 
ATOM   3469 C CB  . PRO B 1 505 ? -8.914  -3.293  37.923  1.00 56.16  ?  755  PRO B CB  1 
ATOM   3470 C CG  . PRO B 1 505 ? -9.843  -4.030  37.017  1.00 52.85  ?  755  PRO B CG  1 
ATOM   3471 C CD  . PRO B 1 505 ? -10.913 -3.047  36.664  1.00 52.17  ?  755  PRO B CD  1 
ATOM   3472 N N   . TRP B 1 506 ? -9.123  -0.067  38.176  1.00 58.36  ?  756  TRP B N   1 
ATOM   3473 C CA  . TRP B 1 506 ? -8.419  1.177   38.470  1.00 56.40  ?  756  TRP B CA  1 
ATOM   3474 C C   . TRP B 1 506 ? -9.101  1.988   39.564  1.00 50.01  ?  756  TRP B C   1 
ATOM   3475 O O   . TRP B 1 506 ? -8.466  2.873   40.148  1.00 54.14  ?  756  TRP B O   1 
ATOM   3476 C CB  . TRP B 1 506 ? -8.264  2.025   37.203  1.00 62.19  ?  756  TRP B CB  1 
ATOM   3477 C CG  . TRP B 1 506 ? -9.528  2.251   36.431  1.00 62.76  ?  756  TRP B CG  1 
ATOM   3478 C CD1 . TRP B 1 506 ? -10.449 3.237   36.633  1.00 50.28  ?  756  TRP B CD1 1 
ATOM   3479 C CD2 . TRP B 1 506 ? -9.998  1.486   35.314  1.00 54.36  ?  756  TRP B CD2 1 
ATOM   3480 N NE1 . TRP B 1 506 ? -11.468 3.128   35.718  1.00 50.05  ?  756  TRP B NE1 1 
ATOM   3481 C CE2 . TRP B 1 506 ? -11.215 2.061   34.896  1.00 50.50  ?  756  TRP B CE2 1 
ATOM   3482 C CE3 . TRP B 1 506 ? -9.510  0.369   34.630  1.00 56.14  ?  756  TRP B CE3 1 
ATOM   3483 C CZ2 . TRP B 1 506 ? -11.950 1.557   33.825  1.00 54.39  ?  756  TRP B CZ2 1 
ATOM   3484 C CZ3 . TRP B 1 506 ? -10.242 -0.131  33.569  1.00 55.76  ?  756  TRP B CZ3 1 
ATOM   3485 C CH2 . TRP B 1 506 ? -11.449 0.461   33.178  1.00 58.86  ?  756  TRP B CH2 1 
ATOM   3486 N N   . GLN B 1 507 ? -10.366 1.704   39.862  1.00 50.02  ?  757  GLN B N   1 
ATOM   3487 C CA  . GLN B 1 507 ? -11.067 2.358   40.958  1.00 49.81  ?  757  GLN B CA  1 
ATOM   3488 C C   . GLN B 1 507 ? -10.757 1.731   42.313  1.00 53.85  ?  757  GLN B C   1 
ATOM   3489 O O   . GLN B 1 507 ? -11.382 2.104   43.313  1.00 55.17  ?  757  GLN B O   1 
ATOM   3490 C CB  . GLN B 1 507 ? -12.574 2.346   40.692  1.00 49.83  ?  757  GLN B CB  1 
ATOM   3491 C CG  . GLN B 1 507 ? -12.987 3.281   39.562  1.00 56.90  ?  757  GLN B CG  1 
ATOM   3492 C CD  . GLN B 1 507 ? -14.333 2.929   38.965  1.00 53.36  ?  757  GLN B CD  1 
ATOM   3493 O OE1 . GLN B 1 507 ? -14.769 1.779   39.023  1.00 52.34  ?  757  GLN B OE1 1 
ATOM   3494 N NE2 . GLN B 1 507 ? -14.999 3.919   38.382  1.00 49.61  ?  757  GLN B NE2 1 
ATOM   3495 N N   . THR B 1 508 ? -9.818  0.787   42.366  1.00 50.52  ?  758  THR B N   1 
ATOM   3496 C CA  . THR B 1 508 ? -9.275  0.287   43.621  1.00 50.95  ?  758  THR B CA  1 
ATOM   3497 C C   . THR B 1 508 ? -8.084  1.102   44.100  1.00 50.70  ?  758  THR B C   1 
ATOM   3498 O O   . THR B 1 508 ? -7.495  0.765   45.133  1.00 51.09  ?  758  THR B O   1 
ATOM   3499 C CB  . THR B 1 508 ? -8.852  -1.179  43.480  1.00 55.03  ?  758  THR B CB  1 
ATOM   3500 O OG1 . THR B 1 508 ? -7.722  -1.268  42.603  1.00 51.69  ?  758  THR B OG1 1 
ATOM   3501 C CG2 . THR B 1 508 ? -9.992  -2.016  42.918  1.00 57.17  ?  758  THR B CG2 1 
ATOM   3502 N N   . ALA B 1 509 ? -7.718  2.157   43.373  1.00 50.17  ?  759  ALA B N   1 
ATOM   3503 C CA  . ALA B 1 509 ? -6.542  2.944   43.713  1.00 49.98  ?  759  ALA B CA  1 
ATOM   3504 C C   . ALA B 1 509 ? -6.671  3.528   45.113  1.00 56.03  ?  759  ALA B C   1 
ATOM   3505 O O   . ALA B 1 509 ? -7.775  3.700   45.640  1.00 49.96  ?  759  ALA B O   1 
ATOM   3506 C CB  . ALA B 1 509 ? -6.339  4.067   42.694  1.00 49.56  ?  759  ALA B CB  1 
ATOM   3507 N N   . GLY B 1 510 ? -5.518  3.816   45.723  1.00 58.97  ?  760  GLY B N   1 
ATOM   3508 C CA  . GLY B 1 510 ? -5.522  4.396   47.056  1.00 54.88  ?  760  GLY B CA  1 
ATOM   3509 C C   . GLY B 1 510 ? -6.415  5.614   47.148  1.00 58.26  ?  760  GLY B C   1 
ATOM   3510 O O   . GLY B 1 510 ? -7.212  5.749   48.079  1.00 53.58  ?  760  GLY B O   1 
ATOM   3511 N N   . CYS B 1 511 ? -6.320  6.500   46.159  1.00 57.09  ?  761  CYS B N   1 
ATOM   3512 C CA  . CYS B 1 511 ? -7.181  7.670   46.095  1.00 67.82  ?  761  CYS B CA  1 
ATOM   3513 C C   . CYS B 1 511 ? -7.247  8.174   44.662  1.00 58.76  ?  761  CYS B C   1 
ATOM   3514 O O   . CYS B 1 511 ? -6.293  8.031   43.893  1.00 50.64  ?  761  CYS B O   1 
ATOM   3515 C CB  . CYS B 1 511 ? -6.693  8.774   47.031  1.00 60.59  ?  761  CYS B CB  1 
ATOM   3516 S SG  . CYS B 1 511 ? -7.398  8.641   48.673  1.00 104.14 ?  761  CYS B SG  1 
ATOM   3517 N N   . PHE B 1 512 ? -8.385  8.776   44.321  1.00 58.86  ?  762  PHE B N   1 
ATOM   3518 C CA  . PHE B 1 512 ? -8.642  9.200   42.954  1.00 50.98  ?  762  PHE B CA  1 
ATOM   3519 C C   . PHE B 1 512 ? -9.806  10.180  42.942  1.00 51.46  ?  762  PHE B C   1 
ATOM   3520 O O   . PHE B 1 512 ? -10.568 10.282  43.907  1.00 53.10  ?  762  PHE B O   1 
ATOM   3521 C CB  . PHE B 1 512 ? -8.942  8.000   42.051  1.00 51.63  ?  762  PHE B CB  1 
ATOM   3522 C CG  . PHE B 1 512 ? -10.205 7.272   42.409  1.00 48.84  ?  762  PHE B CG  1 
ATOM   3523 C CD1 . PHE B 1 512 ? -10.198 6.272   43.365  1.00 53.77  ?  762  PHE B CD1 1 
ATOM   3524 C CD2 . PHE B 1 512 ? -11.400 7.586   41.784  1.00 48.88  ?  762  PHE B CD2 1 
ATOM   3525 C CE1 . PHE B 1 512 ? -11.362 5.600   43.693  1.00 60.11  ?  762  PHE B CE1 1 
ATOM   3526 C CE2 . PHE B 1 512 ? -12.565 6.920   42.109  1.00 49.06  ?  762  PHE B CE2 1 
ATOM   3527 C CZ  . PHE B 1 512 ? -12.546 5.925   43.063  1.00 53.33  ?  762  PHE B CZ  1 
ATOM   3528 N N   . VAL B 1 513 ? -9.927  10.902  41.830  1.00 48.81  ?  763  VAL B N   1 
ATOM   3529 C CA  . VAL B 1 513 ? -11.045 11.806  41.579  1.00 49.52  ?  763  VAL B CA  1 
ATOM   3530 C C   . VAL B 1 513 ? -11.495 11.602  40.140  1.00 49.18  ?  763  VAL B C   1 
ATOM   3531 O O   . VAL B 1 513 ? -10.666 11.586  39.223  1.00 49.45  ?  763  VAL B O   1 
ATOM   3532 C CB  . VAL B 1 513 ? -10.672 13.284  41.819  1.00 55.15  ?  763  VAL B CB  1 
ATOM   3533 C CG1 . VAL B 1 513 ? -11.867 14.184  41.539  1.00 49.67  ?  763  VAL B CG1 1 
ATOM   3534 C CG2 . VAL B 1 513 ? -10.170 13.492  43.240  1.00 66.11  ?  763  VAL B CG2 1 
ATOM   3535 N N   . GLU B 1 514 ? -12.800 11.448  39.939  1.00 49.33  ?  764  GLU B N   1 
ATOM   3536 C CA  . GLU B 1 514 ? -13.365 11.226  38.617  1.00 54.89  ?  764  GLU B CA  1 
ATOM   3537 C C   . GLU B 1 514 ? -14.377 12.314  38.284  1.00 52.91  ?  764  GLU B C   1 
ATOM   3538 O O   . GLU B 1 514 ? -15.026 12.877  39.171  1.00 54.48  ?  764  GLU B O   1 
ATOM   3539 C CB  . GLU B 1 514 ? -14.042 9.852   38.518  1.00 49.41  ?  764  GLU B CB  1 
ATOM   3540 C CG  . GLU B 1 514 ? -13.149 8.682   38.895  1.00 55.36  ?  764  GLU B CG  1 
ATOM   3541 C CD  . GLU B 1 514 ? -13.860 7.347   38.768  1.00 58.14  ?  764  GLU B CD  1 
ATOM   3542 O OE1 . GLU B 1 514 ? -13.388 6.489   37.991  1.00 49.27  ?  764  GLU B OE1 1 
ATOM   3543 O OE2 . GLU B 1 514 ? -14.896 7.161   39.441  1.00 55.17  -1 764  GLU B OE2 1 
ATOM   3544 N N   . LYS B 1 515 ? -14.506 12.603  36.990  1.00 50.33  ?  765  LYS B N   1 
ATOM   3545 C CA  . LYS B 1 515 ? -15.513 13.526  36.485  1.00 50.92  ?  765  LYS B CA  1 
ATOM   3546 C C   . LYS B 1 515 ? -16.332 12.823  35.415  1.00 55.48  ?  765  LYS B C   1 
ATOM   3547 O O   . LYS B 1 515 ? -15.772 12.173  34.526  1.00 56.29  ?  765  LYS B O   1 
ATOM   3548 C CB  . LYS B 1 515 ? -14.882 14.800  35.916  1.00 62.13  ?  765  LYS B CB  1 
ATOM   3549 C CG  . LYS B 1 515 ? -15.895 15.741  35.282  1.00 52.28  ?  765  LYS B CG  1 
ATOM   3550 C CD  . LYS B 1 515 ? -15.406 17.178  35.274  1.00 67.47  ?  765  LYS B CD  1 
ATOM   3551 C CE  . LYS B 1 515 ? -16.513 18.125  34.837  1.00 53.89  ?  765  LYS B CE  1 
ATOM   3552 N NZ  . LYS B 1 515 ? -16.147 19.551  35.057  1.00 83.98  1  765  LYS B NZ  1 
ATOM   3553 N N   . ASP B 1 516 ? -17.652 12.959  35.501  1.00 51.95  ?  766  ASP B N   1 
ATOM   3554 C CA  . ASP B 1 516 ? -18.578 12.303  34.588  1.00 58.53  ?  766  ASP B CA  1 
ATOM   3555 C C   . ASP B 1 516 ? -19.075 13.313  33.561  1.00 52.43  ?  766  ASP B C   1 
ATOM   3556 O O   . ASP B 1 516 ? -19.732 14.297  33.920  1.00 59.83  ?  766  ASP B O   1 
ATOM   3557 C CB  . ASP B 1 516 ? -19.749 11.694  35.357  1.00 51.92  ?  766  ASP B CB  1 
ATOM   3558 C CG  . ASP B 1 516 ? -19.299 10.707  36.417  1.00 62.02  ?  766  ASP B CG  1 
ATOM   3559 O OD1 . ASP B 1 516 ? -18.161 10.202  36.318  1.00 57.21  ?  766  ASP B OD1 1 
ATOM   3560 O OD2 . ASP B 1 516 ? -20.088 10.429  37.345  1.00 75.61  -1 766  ASP B OD2 1 
ATOM   3561 N N   . TYR B 1 517 ? -18.767 13.066  32.291  1.00 52.73  ?  767  TYR B N   1 
ATOM   3562 C CA  . TYR B 1 517 ? -19.175 13.935  31.195  1.00 53.68  ?  767  TYR B CA  1 
ATOM   3563 C C   . TYR B 1 517 ? -20.374 13.333  30.477  1.00 59.03  ?  767  TYR B C   1 
ATOM   3564 O O   . TYR B 1 517 ? -20.388 12.135  30.176  1.00 64.12  ?  767  TYR B O   1 
ATOM   3565 C CB  . TYR B 1 517 ? -18.026 14.145  30.207  1.00 54.08  ?  767  TYR B CB  1 
ATOM   3566 C CG  . TYR B 1 517 ? -16.990 15.147  30.662  1.00 55.24  ?  767  TYR B CG  1 
ATOM   3567 C CD1 . TYR B 1 517 ? -15.875 14.747  31.384  1.00 53.48  ?  767  TYR B CD1 1 
ATOM   3568 C CD2 . TYR B 1 517 ? -17.127 16.497  30.367  1.00 59.72  ?  767  TYR B CD2 1 
ATOM   3569 C CE1 . TYR B 1 517 ? -14.926 15.663  31.800  1.00 66.46  ?  767  TYR B CE1 1 
ATOM   3570 C CE2 . TYR B 1 517 ? -16.183 17.420  30.778  1.00 55.37  ?  767  TYR B CE2 1 
ATOM   3571 C CZ  . TYR B 1 517 ? -15.085 16.997  31.494  1.00 54.97  ?  767  TYR B CZ  1 
ATOM   3572 O OH  . TYR B 1 517 ? -14.143 17.911  31.907  1.00 69.12  ?  767  TYR B OH  1 
ATOM   3573 N N   . GLU B 1 518 ? -21.375 14.165  30.204  1.00 55.17  ?  768  GLU B N   1 
ATOM   3574 C CA  . GLU B 1 518 ? -22.508 13.726  29.407  1.00 55.19  ?  768  GLU B CA  1 
ATOM   3575 C C   . GLU B 1 518 ? -22.081 13.507  27.959  1.00 57.31  ?  768  GLU B C   1 
ATOM   3576 O O   . GLU B 1 518 ? -21.095 14.073  27.479  1.00 71.77  ?  768  GLU B O   1 
ATOM   3577 C CB  . GLU B 1 518 ? -23.640 14.753  29.458  1.00 56.08  ?  768  GLU B CB  1 
ATOM   3578 C CG  . GLU B 1 518 ? -24.149 15.068  30.851  1.00 59.28  ?  768  GLU B CG  1 
ATOM   3579 C CD  . GLU B 1 518 ? -25.342 16.006  30.828  1.00 72.96  ?  768  GLU B CD  1 
ATOM   3580 O OE1 . GLU B 1 518 ? -25.920 16.205  29.739  1.00 73.61  ?  768  GLU B OE1 1 
ATOM   3581 O OE2 . GLU B 1 518 ? -25.700 16.545  31.896  1.00 68.66  -1 768  GLU B OE2 1 
ATOM   3582 N N   . TYR B 1 519 ? -22.840 12.668  27.261  1.00 55.86  ?  769  TYR B N   1 
ATOM   3583 C CA  . TYR B 1 519 ? -22.631 12.476  25.833  1.00 56.59  ?  769  TYR B CA  1 
ATOM   3584 C C   . TYR B 1 519 ? -23.296 13.620  25.079  1.00 65.35  ?  769  TYR B C   1 
ATOM   3585 O O   . TYR B 1 519 ? -24.506 13.833  25.207  1.00 81.89  ?  769  TYR B O   1 
ATOM   3586 C CB  . TYR B 1 519 ? -23.189 11.132  25.373  1.00 58.12  ?  769  TYR B CB  1 
ATOM   3587 C CG  . TYR B 1 519 ? -23.067 10.920  23.882  1.00 62.36  ?  769  TYR B CG  1 
ATOM   3588 C CD1 . TYR B 1 519 ? -21.854 10.564  23.309  1.00 57.32  ?  769  TYR B CD1 1 
ATOM   3589 C CD2 . TYR B 1 519 ? -24.161 11.087  23.044  1.00 61.55  ?  769  TYR B CD2 1 
ATOM   3590 C CE1 . TYR B 1 519 ? -21.734 10.376  21.946  1.00 58.31  ?  769  TYR B CE1 1 
ATOM   3591 C CE2 . TYR B 1 519 ? -24.051 10.901  21.680  1.00 69.64  ?  769  TYR B CE2 1 
ATOM   3592 C CZ  . TYR B 1 519 ? -22.835 10.545  21.136  1.00 64.19  ?  769  TYR B CZ  1 
ATOM   3593 O OH  . TYR B 1 519 ? -22.719 10.358  19.778  1.00 72.77  ?  769  TYR B OH  1 
ATOM   3594 N N   . GLU B 1 520 ? -22.508 14.359  24.305  1.00 65.20  ?  770  GLU B N   1 
ATOM   3595 C CA  . GLU B 1 520 ? -23.007 15.481  23.520  1.00 74.52  ?  770  GLU B CA  1 
ATOM   3596 C C   . GLU B 1 520 ? -23.013 15.080  22.049  1.00 73.36  ?  770  GLU B C   1 
ATOM   3597 O O   . GLU B 1 520 ? -21.952 14.893  21.443  1.00 72.83  ?  770  GLU B O   1 
ATOM   3598 C CB  . GLU B 1 520 ? -22.169 16.738  23.757  1.00 71.23  ?  770  GLU B CB  1 
ATOM   3599 C CG  . GLU B 1 520 ? -20.664 16.543  23.658  1.00 71.82  ?  770  GLU B CG  1 
ATOM   3600 C CD  . GLU B 1 520 ? -19.911 17.858  23.677  1.00 95.74  ?  770  GLU B CD  1 
ATOM   3601 O OE1 . GLU B 1 520 ? -18.959 17.991  24.476  1.00 98.42  ?  770  GLU B OE1 1 
ATOM   3602 O OE2 . GLU B 1 520 ? -20.278 18.762  22.897  1.00 106.04 -1 770  GLU B OE2 1 
ATOM   3603 N N   . SER B 1 521 ? -24.209 14.929  21.486  1.00 80.13  ?  771  SER B N   1 
ATOM   3604 C CA  . SER B 1 521 ? -24.330 14.691  20.057  1.00 80.89  ?  771  SER B CA  1 
ATOM   3605 C C   . SER B 1 521 ? -23.828 15.906  19.286  1.00 86.89  ?  771  SER B C   1 
ATOM   3606 O O   . SER B 1 521 ? -23.945 17.048  19.737  1.00 90.83  ?  771  SER B O   1 
ATOM   3607 C CB  . SER B 1 521 ? -25.783 14.392  19.688  1.00 84.86  ?  771  SER B CB  1 
ATOM   3608 O OG  . SER B 1 521 ? -26.352 13.454  20.586  1.00 76.34  ?  771  SER B OG  1 
ATOM   3609 N N   . GLY B 1 522 ? -23.257 15.651  18.112  1.00 89.47  ?  772  GLY B N   1 
ATOM   3610 C CA  . GLY B 1 522 ? -22.673 16.711  17.320  1.00 93.09  ?  772  GLY B CA  1 
ATOM   3611 C C   . GLY B 1 522 ? -21.248 17.064  17.677  1.00 85.29  ?  772  GLY B C   1 
ATOM   3612 O O   . GLY B 1 522 ? -20.652 17.916  17.005  1.00 92.56  ?  772  GLY B O   1 
ATOM   3613 N N   . TRP B 1 523 ? -20.682 16.451  18.719  1.00 84.38  ?  773  TRP B N   1 
ATOM   3614 C CA  . TRP B 1 523 ? -19.272 16.663  19.025  1.00 88.94  ?  773  TRP B CA  1 
ATOM   3615 C C   . TRP B 1 523 ? -18.377 16.033  17.966  1.00 85.57  ?  773  TRP B C   1 
ATOM   3616 O O   . TRP B 1 523 ? -17.284 16.544  17.695  1.00 94.51  ?  773  TRP B O   1 
ATOM   3617 C CB  . TRP B 1 523 ? -18.947 16.098  20.409  1.00 88.33  ?  773  TRP B CB  1 
ATOM   3618 C CG  . TRP B 1 523 ? -17.526 16.310  20.842  1.00 90.04  ?  773  TRP B CG  1 
ATOM   3619 C CD1 . TRP B 1 523 ? -16.721 17.369  20.532  1.00 90.01  ?  773  TRP B CD1 1 
ATOM   3620 C CD2 . TRP B 1 523 ? -16.738 15.434  21.657  1.00 79.64  ?  773  TRP B CD2 1 
ATOM   3621 N NE1 . TRP B 1 523 ? -15.484 17.207  21.107  1.00 87.53  ?  773  TRP B NE1 1 
ATOM   3622 C CE2 . TRP B 1 523 ? -15.468 16.027  21.802  1.00 73.84  ?  773  TRP B CE2 1 
ATOM   3623 C CE3 . TRP B 1 523 ? -16.984 14.207  22.280  1.00 72.28  ?  773  TRP B CE3 1 
ATOM   3624 C CZ2 . TRP B 1 523 ? -14.449 15.436  22.544  1.00 77.75  ?  773  TRP B CZ2 1 
ATOM   3625 C CZ3 . TRP B 1 523 ? -15.971 13.621  23.016  1.00 69.71  ?  773  TRP B CZ3 1 
ATOM   3626 C CH2 . TRP B 1 523 ? -14.719 14.235  23.140  1.00 78.70  ?  773  TRP B CH2 1 
ATOM   3627 N N   . GLY B 1 524 ? -18.821 14.934  17.358  1.00 78.77  ?  774  GLY B N   1 
ATOM   3628 C CA  . GLY B 1 524 ? -18.089 14.281  16.299  1.00 81.67  ?  774  GLY B CA  1 
ATOM   3629 C C   . GLY B 1 524 ? -17.155 13.177  16.746  1.00 89.30  ?  774  GLY B C   1 
ATOM   3630 O O   . GLY B 1 524 ? -16.784 12.331  15.924  1.00 100.23 ?  774  GLY B O   1 
ATOM   3631 N N   . CYS B 1 525 ? -16.766 13.154  18.019  1.00 87.94  ?  775  CYS B N   1 
ATOM   3632 C CA  . CYS B 1 525 ? -15.828 12.155  18.527  1.00 83.57  ?  775  CYS B CA  1 
ATOM   3633 C C   . CYS B 1 525 ? -16.607 10.895  18.881  1.00 80.85  ?  775  CYS B C   1 
ATOM   3634 O O   . CYS B 1 525 ? -17.026 10.693  20.021  1.00 94.68  ?  775  CYS B O   1 
ATOM   3635 C CB  . CYS B 1 525 ? -15.067 12.695  19.731  1.00 77.96  ?  775  CYS B CB  1 
ATOM   3636 S SG  . CYS B 1 525 ? -13.412 12.012  19.933  1.00 93.15  ?  775  CYS B SG  1 
ATOM   3637 N N   . ASN B 1 526 ? -16.800 10.035  17.889  1.00 68.53  ?  776  ASN B N   1 
ATOM   3638 C CA  . ASN B 1 526 ? -17.531 8.783   18.072  1.00 80.63  ?  776  ASN B CA  1 
ATOM   3639 C C   . ASN B 1 526 ? -16.613 7.606   17.779  1.00 72.74  ?  776  ASN B C   1 
ATOM   3640 O O   . ASN B 1 526 ? -16.209 7.415   16.615  1.00 69.04  ?  776  ASN B O   1 
ATOM   3641 C CB  . ASN B 1 526 ? -18.763 8.741   17.169  1.00 78.52  ?  776  ASN B CB  1 
ATOM   3642 C CG  . ASN B 1 526 ? -19.661 9.949   17.352  1.00 77.56  ?  776  ASN B CG  1 
ATOM   3643 O OD1 . ASN B 1 526 ? -20.486 9.992   18.265  1.00 87.27  ?  776  ASN B OD1 1 
ATOM   3644 N ND2 . ASN B 1 526 ? -19.507 10.939  16.480  1.00 89.08  ?  776  ASN B ND2 1 
ATOM   3645 N N   . PRO B 1 527 ? -16.253 6.801   18.775  1.00 70.65  ?  777  PRO B N   1 
ATOM   3646 C CA  . PRO B 1 527 ? -15.352 5.673   18.521  1.00 64.46  ?  777  PRO B CA  1 
ATOM   3647 C C   . PRO B 1 527 ? -16.024 4.599   17.681  1.00 70.84  ?  777  PRO B C   1 
ATOM   3648 O O   . PRO B 1 527 ? -17.234 4.376   17.761  1.00 77.43  ?  777  PRO B O   1 
ATOM   3649 C CB  . PRO B 1 527 ? -15.025 5.157   19.926  1.00 69.28  ?  777  PRO B CB  1 
ATOM   3650 C CG  . PRO B 1 527 ? -16.196 5.565   20.750  1.00 65.69  ?  777  PRO B CG  1 
ATOM   3651 C CD  . PRO B 1 527 ? -16.659 6.880   20.188  1.00 73.08  ?  777  PRO B CD  1 
ATOM   3652 N N   . ALA B 1 528 ? -15.213 3.928   16.868  1.00 64.07  ?  778  ALA B N   1 
ATOM   3653 C CA  . ALA B 1 528 ? -15.701 2.915   15.943  1.00 70.73  ?  778  ALA B CA  1 
ATOM   3654 C C   . ALA B 1 528 ? -15.660 1.505   16.517  1.00 75.58  ?  778  ALA B C   1 
ATOM   3655 O O   . ALA B 1 528 ? -16.031 0.558   15.815  1.00 79.48  ?  778  ALA B O   1 
ATOM   3656 C CB  . ALA B 1 528 ? -14.894 2.961   14.642  1.00 73.17  ?  778  ALA B CB  1 
ATOM   3657 N N   . ASP B 1 529 ? -15.226 1.336   17.764  1.00 71.49  ?  779  ASP B N   1 
ATOM   3658 C CA  . ASP B 1 529 ? -15.121 0.015   18.367  1.00 64.93  ?  779  ASP B CA  1 
ATOM   3659 C C   . ASP B 1 529 ? -16.222 -0.278  19.379  1.00 68.28  ?  779  ASP B C   1 
ATOM   3660 O O   . ASP B 1 529 ? -16.190 -1.335  20.016  1.00 82.75  ?  779  ASP B O   1 
ATOM   3661 C CB  . ASP B 1 529 ? -13.746 -0.163  19.022  1.00 63.05  ?  779  ASP B CB  1 
ATOM   3662 C CG  . ASP B 1 529 ? -13.370 0.997   19.922  1.00 74.99  ?  779  ASP B CG  1 
ATOM   3663 O OD1 . ASP B 1 529 ? -14.126 1.991   19.965  1.00 72.30  ?  779  ASP B OD1 1 
ATOM   3664 O OD2 . ASP B 1 529 ? -12.315 0.914   20.585  1.00 73.26  -1 779  ASP B OD2 1 
ATOM   3665 N N   . CYS B 1 530 ? -17.189 0.623   19.550  1.00 69.67  ?  780  CYS B N   1 
ATOM   3666 C CA  . CYS B 1 530 ? -18.373 0.259   20.310  1.00 78.57  ?  780  CYS B CA  1 
ATOM   3667 C C   . CYS B 1 530 ? -19.277 -0.631  19.460  1.00 66.75  ?  780  CYS B C   1 
ATOM   3668 O O   . CYS B 1 530 ? -19.276 -0.534  18.230  1.00 75.30  ?  780  CYS B O   1 
ATOM   3669 C CB  . CYS B 1 530 ? -19.146 1.501   20.752  1.00 61.93  ?  780  CYS B CB  1 
ATOM   3670 S SG  . CYS B 1 530 ? -18.556 2.299   22.270  1.00 80.69  ?  780  CYS B SG  1 
ATOM   3671 N N   . PRO B 1 531 ? -20.050 -1.517  20.088  1.00 64.76  ?  781  PRO B N   1 
ATOM   3672 C CA  . PRO B 1 531 ? -21.013 -2.317  19.321  1.00 66.97  ?  781  PRO B CA  1 
ATOM   3673 C C   . PRO B 1 531 ? -22.184 -1.472  18.847  1.00 68.63  ?  781  PRO B C   1 
ATOM   3674 O O   . PRO B 1 531 ? -23.314 -1.637  19.316  1.00 75.40  ?  781  PRO B O   1 
ATOM   3675 C CB  . PRO B 1 531 ? -21.453 -3.391  20.322  1.00 65.52  ?  781  PRO B CB  1 
ATOM   3676 C CG  . PRO B 1 531 ? -21.270 -2.746  21.652  1.00 69.46  ?  781  PRO B CG  1 
ATOM   3677 C CD  . PRO B 1 531 ? -20.050 -1.873  21.518  1.00 76.24  ?  781  PRO B CD  1 
ATOM   3678 N N   . GLY B 1 532 ? -21.916 -0.559  17.913  1.00 71.23  ?  782  GLY B N   1 
ATOM   3679 C CA  . GLY B 1 532 ? -22.895 0.406   17.462  1.00 69.04  ?  782  GLY B CA  1 
ATOM   3680 C C   . GLY B 1 532 ? -22.428 1.829   17.722  1.00 71.98  ?  782  GLY B C   1 
ATOM   3681 O O   . GLY B 1 532 ? -21.224 2.115   17.731  1.00 82.91  ?  782  GLY B O   1 
ATOM   3682 N N   . VAL B 1 533 ? -23.395 2.716   17.938  1.00 75.28  ?  783  VAL B N   1 
ATOM   3683 C CA  . VAL B 1 533 ? -23.117 4.125   18.195  1.00 59.43  ?  783  VAL B CA  1 
ATOM   3684 C C   . VAL B 1 533 ? -23.058 4.329   19.705  1.00 60.57  ?  783  VAL B C   1 
ATOM   3685 O O   . VAL B 1 533 ? -24.066 4.188   20.401  1.00 73.50  ?  783  VAL B O   1 
ATOM   3686 C CB  . VAL B 1 533 ? -24.171 5.033   17.552  1.00 60.64  ?  783  VAL B CB  1 
ATOM   3687 C CG1 . VAL B 1 533 ? -23.850 6.493   17.833  1.00 67.68  ?  783  VAL B CG1 1 
ATOM   3688 C CG2 . VAL B 1 533 ? -24.247 4.778   16.056  1.00 66.15  ?  783  VAL B CG2 1 
ATOM   3689 N N   . GLY B 1 534 ? -21.874 4.663   20.211  1.00 60.13  ?  784  GLY B N   1 
ATOM   3690 C CA  . GLY B 1 534 ? -21.723 4.901   21.637  1.00 60.11  ?  784  GLY B CA  1 
ATOM   3691 C C   . GLY B 1 534 ? -22.406 6.193   22.048  1.00 64.80  ?  784  GLY B C   1 
ATOM   3692 O O   . GLY B 1 534 ? -22.203 7.245   21.430  1.00 62.49  ?  784  GLY B O   1 
ATOM   3693 N N   . THR B 1 535 ? -23.231 6.118   23.095  1.00 59.19  ?  785  THR B N   1 
ATOM   3694 C CA  . THR B 1 535 ? -23.976 7.272   23.583  1.00 56.08  ?  785  THR B CA  1 
ATOM   3695 C C   . THR B 1 535 ? -23.915 7.411   25.100  1.00 59.34  ?  785  THR B C   1 
ATOM   3696 O O   . THR B 1 535 ? -24.675 8.203   25.667  1.00 55.23  ?  785  THR B O   1 
ATOM   3697 C CB  . THR B 1 535 ? -25.443 7.201   23.138  1.00 56.58  ?  785  THR B CB  1 
ATOM   3698 O OG1 . THR B 1 535 ? -26.002 5.939   23.526  1.00 82.96  ?  785  THR B OG1 1 
ATOM   3699 C CG2 . THR B 1 535 ? -25.562 7.365   21.628  1.00 58.29  ?  785  THR B CG2 1 
ATOM   3700 N N   . GLY B 1 536 ? -23.035 6.670   25.770  1.00 58.10  ?  786  GLY B N   1 
ATOM   3701 C CA  . GLY B 1 536 ? -22.973 6.669   27.215  1.00 53.66  ?  786  GLY B CA  1 
ATOM   3702 C C   . GLY B 1 536 ? -22.070 7.755   27.771  1.00 61.30  ?  786  GLY B C   1 
ATOM   3703 O O   . GLY B 1 536 ? -21.638 8.675   27.075  1.00 57.12  ?  786  GLY B O   1 
ATOM   3704 N N   . CYS B 1 537 ? -21.783 7.627   29.063  1.00 54.89  ?  787  CYS B N   1 
ATOM   3705 C CA  . CYS B 1 537 ? -20.991 8.613   29.781  1.00 54.04  ?  787  CYS B CA  1 
ATOM   3706 C C   . CYS B 1 537 ? -19.501 8.421   29.524  1.00 65.02  ?  787  CYS B C   1 
ATOM   3707 O O   . CYS B 1 537 ? -19.031 7.314   29.246  1.00 70.59  ?  787  CYS B O   1 
ATOM   3708 C CB  . CYS B 1 537 ? -21.266 8.522   31.282  1.00 54.63  ?  787  CYS B CB  1 
ATOM   3709 S SG  . CYS B 1 537 ? -19.910 9.111   32.322  1.00 72.15  ?  787  CYS B SG  1 
ATOM   3710 N N   . THR B 1 538 ? -18.757 9.522   29.625  1.00 62.36  ?  788  THR B N   1 
ATOM   3711 C CA  . THR B 1 538 ? -17.301 9.517   29.537  1.00 55.56  ?  788  THR B CA  1 
ATOM   3712 C C   . THR B 1 538 ? -16.752 9.770   30.936  1.00 54.63  ?  788  THR B C   1 
ATOM   3713 O O   . THR B 1 538 ? -16.897 10.872  31.476  1.00 63.33  ?  788  THR B O   1 
ATOM   3714 C CB  . THR B 1 538 ? -16.802 10.572  28.552  1.00 54.44  ?  788  THR B CB  1 
ATOM   3715 O OG1 . THR B 1 538 ? -17.417 10.365  27.275  1.00 54.88  ?  788  THR B OG1 1 
ATOM   3716 C CG2 . THR B 1 538 ? -15.292 10.485  28.402  1.00 53.44  ?  788  THR B CG2 1 
ATOM   3717 N N   . ALA B 1 539 ? -16.130 8.749   31.522  1.00 57.81  ?  789  ALA B N   1 
ATOM   3718 C CA  . ALA B 1 539 ? -15.621 8.812   32.891  1.00 60.55  ?  789  ALA B CA  1 
ATOM   3719 C C   . ALA B 1 539 ? -14.137 9.159   32.846  1.00 61.16  ?  789  ALA B C   1 
ATOM   3720 O O   . ALA B 1 539 ? -13.295 8.308   32.549  1.00 69.89  ?  789  ALA B O   1 
ATOM   3721 C CB  . ALA B 1 539 ? -15.864 7.495   33.619  1.00 52.97  ?  789  ALA B CB  1 
ATOM   3722 N N   . CYS B 1 540 ? -13.821 10.415  33.145  1.00 56.47  ?  790  CYS B N   1 
ATOM   3723 C CA  . CYS B 1 540 ? -12.448 10.887  33.226  1.00 58.77  ?  790  CYS B CA  1 
ATOM   3724 C C   . CYS B 1 540 ? -12.008 10.919  34.682  1.00 54.51  ?  790  CYS B C   1 
ATOM   3725 O O   . CYS B 1 540 ? -12.760 11.358  35.556  1.00 63.77  ?  790  CYS B O   1 
ATOM   3726 C CB  . CYS B 1 540 ? -12.316 12.278  32.608  1.00 55.27  ?  790  CYS B CB  1 
ATOM   3727 S SG  . CYS B 1 540 ? -12.783 12.351  30.872  1.00 62.88  ?  790  CYS B SG  1 
ATOM   3728 N N   . GLY B 1 541 ? -10.793 10.457  34.940  1.00 50.24  ?  791  GLY B N   1 
ATOM   3729 C CA  . GLY B 1 541 ? -10.320 10.341  36.308  1.00 49.76  ?  791  GLY B CA  1 
ATOM   3730 C C   . GLY B 1 541 ? -8.819  10.467  36.413  1.00 49.81  ?  791  GLY B C   1 
ATOM   3731 O O   . GLY B 1 541 ? -8.079  10.163  35.471  1.00 50.17  ?  791  GLY B O   1 
ATOM   3732 N N   . VAL B 1 542 ? -8.371  10.937  37.574  1.00 51.30  ?  792  VAL B N   1 
ATOM   3733 C CA  . VAL B 1 542 ? -6.968  10.922  37.969  1.00 49.50  ?  792  VAL B CA  1 
ATOM   3734 C C   . VAL B 1 542 ? -6.823  9.906   39.090  1.00 49.15  ?  792  VAL B C   1 
ATOM   3735 O O   . VAL B 1 542 ? -7.570  9.954   40.073  1.00 49.91  ?  792  VAL B O   1 
ATOM   3736 C CB  . VAL B 1 542 ? -6.491  12.308  38.430  1.00 57.48  ?  792  VAL B CB  1 
ATOM   3737 C CG1 . VAL B 1 542 ? -5.108  12.202  39.046  1.00 55.79  ?  792  VAL B CG1 1 
ATOM   3738 C CG2 . VAL B 1 542 ? -6.500  13.291  37.272  1.00 60.95  ?  792  VAL B CG2 1 
ATOM   3739 N N   . TYR B 1 543 ? -5.863  8.995   38.952  1.00 53.61  ?  793  TYR B N   1 
ATOM   3740 C CA  . TYR B 1 543 ? -5.708  7.884   39.882  1.00 52.41  ?  793  TYR B CA  1 
ATOM   3741 C C   . TYR B 1 543 ? -4.286  7.875   40.420  1.00 52.68  ?  793  TYR B C   1 
ATOM   3742 O O   . TYR B 1 543 ? -3.326  7.823   39.643  1.00 54.30  ?  793  TYR B O   1 
ATOM   3743 C CB  . TYR B 1 543 ? -6.046  6.554   39.199  1.00 50.66  ?  793  TYR B CB  1 
ATOM   3744 C CG  . TYR B 1 543 ? -7.423  6.549   38.568  1.00 49.30  ?  793  TYR B CG  1 
ATOM   3745 C CD1 . TYR B 1 543 ? -7.619  7.018   37.276  1.00 49.53  ?  793  TYR B CD1 1 
ATOM   3746 C CD2 . TYR B 1 543 ? -8.528  6.086   39.268  1.00 49.14  ?  793  TYR B CD2 1 
ATOM   3747 C CE1 . TYR B 1 543 ? -8.875  7.024   36.700  1.00 49.56  ?  793  TYR B CE1 1 
ATOM   3748 C CE2 . TYR B 1 543 ? -9.788  6.090   38.699  1.00 50.07  ?  793  TYR B CE2 1 
ATOM   3749 C CZ  . TYR B 1 543 ? -9.955  6.559   37.415  1.00 49.33  ?  793  TYR B CZ  1 
ATOM   3750 O OH  . TYR B 1 543 ? -11.207 6.562   36.844  1.00 49.41  ?  793  TYR B OH  1 
ATOM   3751 N N   . LEU B 1 544 ? -4.153  7.932   41.743  1.00 49.72  ?  794  LEU B N   1 
ATOM   3752 C CA  . LEU B 1 544 ? -2.852  7.891   42.404  1.00 54.17  ?  794  LEU B CA  1 
ATOM   3753 C C   . LEU B 1 544 ? -2.504  6.436   42.697  1.00 53.95  ?  794  LEU B C   1 
ATOM   3754 O O   . LEU B 1 544 ? -3.067  5.827   43.612  1.00 59.95  ?  794  LEU B O   1 
ATOM   3755 C CB  . LEU B 1 544 ? -2.871  8.722   43.685  1.00 49.04  ?  794  LEU B CB  1 
ATOM   3756 C CG  . LEU B 1 544 ? -3.257  10.194  43.532  1.00 55.49  ?  794  LEU B CG  1 
ATOM   3757 C CD1 . LEU B 1 544 ? -3.136  10.921  44.863  1.00 48.71  ?  794  LEU B CD1 1 
ATOM   3758 C CD2 . LEU B 1 544 ? -2.408  10.869  42.464  1.00 49.44  ?  794  LEU B CD2 1 
ATOM   3759 N N   . ASP B 1 545 ? -1.576  5.883   41.924  1.00 60.39  ?  795  ASP B N   1 
ATOM   3760 C CA  . ASP B 1 545 ? -1.203  4.481   42.022  1.00 50.34  ?  795  ASP B CA  1 
ATOM   3761 C C   . ASP B 1 545 ? 0.188   4.335   42.626  1.00 51.41  ?  795  ASP B C   1 
ATOM   3762 O O   . ASP B 1 545 ? 0.985   5.277   42.647  1.00 58.32  ?  795  ASP B O   1 
ATOM   3763 C CB  . ASP B 1 545 ? -1.248  3.808   40.645  1.00 50.74  ?  795  ASP B CB  1 
ATOM   3764 C CG  . ASP B 1 545 ? -2.604  3.938   39.978  1.00 53.21  ?  795  ASP B CG  1 
ATOM   3765 O OD1 . ASP B 1 545 ? -3.627  3.891   40.693  1.00 66.33  ?  795  ASP B OD1 1 
ATOM   3766 O OD2 . ASP B 1 545 ? -2.648  4.091   38.739  1.00 55.11  -1 795  ASP B OD2 1 
ATOM   3767 N N   . LYS B 1 546 ? 0.462   3.126   43.121  1.00 59.92  ?  796  LYS B N   1 
ATOM   3768 C CA  . LYS B 1 546 ? 1.761   2.759   43.687  1.00 51.77  ?  796  LYS B CA  1 
ATOM   3769 C C   . LYS B 1 546 ? 2.168   3.719   44.808  1.00 51.43  ?  796  LYS B C   1 
ATOM   3770 O O   . LYS B 1 546 ? 3.201   4.390   44.751  1.00 51.76  ?  796  LYS B O   1 
ATOM   3771 C CB  . LYS B 1 546 ? 2.836   2.695   42.597  1.00 52.28  ?  796  LYS B CB  1 
ATOM   3772 C CG  . LYS B 1 546 ? 2.451   1.865   41.383  1.00 52.70  ?  796  LYS B CG  1 
ATOM   3773 C CD  . LYS B 1 546 ? 3.670   1.547   40.530  1.00 56.40  ?  796  LYS B CD  1 
ATOM   3774 C CE  . LYS B 1 546 ? 3.274   1.078   39.140  1.00 85.45  ?  796  LYS B CE  1 
ATOM   3775 N NZ  . LYS B 1 546 ? 2.704   2.192   38.329  1.00 95.52  1  796  LYS B NZ  1 
ATOM   3776 N N   . LEU B 1 547 ? 1.329   3.771   45.839  1.00 57.22  ?  797  LEU B N   1 
ATOM   3777 C CA  . LEU B 1 547 ? 1.602   4.603   47.004  1.00 51.93  ?  797  LEU B CA  1 
ATOM   3778 C C   . LEU B 1 547 ? 2.631   3.912   47.891  1.00 59.85  ?  797  LEU B C   1 
ATOM   3779 O O   . LEU B 1 547 ? 2.420   2.775   48.325  1.00 59.58  ?  797  LEU B O   1 
ATOM   3780 C CB  . LEU B 1 547 ? 0.314   4.875   47.777  1.00 51.19  ?  797  LEU B CB  1 
ATOM   3781 C CG  . LEU B 1 547 ? -0.816  5.572   47.015  1.00 50.10  ?  797  LEU B CG  1 
ATOM   3782 C CD1 . LEU B 1 547 ? -2.065  5.661   47.877  1.00 50.04  ?  797  LEU B CD1 1 
ATOM   3783 C CD2 . LEU B 1 547 ? -0.382  6.954   46.551  1.00 55.63  ?  797  LEU B CD2 1 
ATOM   3784 N N   . LYS B 1 548 ? 3.744   4.593   48.159  1.00 60.26  ?  798  LYS B N   1 
ATOM   3785 C CA  . LYS B 1 548 ? 4.806   4.062   49.000  1.00 57.76  ?  798  LYS B CA  1 
ATOM   3786 C C   . LYS B 1 548 ? 5.057   5.000   50.172  1.00 57.01  ?  798  LYS B C   1 
ATOM   3787 O O   . LYS B 1 548 ? 4.994   6.223   50.024  1.00 57.84  ?  798  LYS B O   1 
ATOM   3788 C CB  . LYS B 1 548 ? 6.113   3.877   48.218  1.00 58.77  ?  798  LYS B CB  1 
ATOM   3789 C CG  . LYS B 1 548 ? 5.948   3.378   46.795  1.00 69.62  ?  798  LYS B CG  1 
ATOM   3790 C CD  . LYS B 1 548 ? 7.260   2.822   46.259  1.00 81.14  ?  798  LYS B CD  1 
ATOM   3791 C CE  . LYS B 1 548 ? 8.434   3.745   46.563  1.00 81.72  ?  798  LYS B CE  1 
ATOM   3792 N NZ  . LYS B 1 548 ? 8.311   5.067   45.887  1.00 97.07  1  798  LYS B NZ  1 
ATOM   3793 N N   . SER B 1 549 ? 5.350   4.419   51.332  1.00 58.81  ?  799  SER B N   1 
ATOM   3794 C CA  . SER B 1 549 ? 5.750   5.213   52.486  1.00 52.81  ?  799  SER B CA  1 
ATOM   3795 C C   . SER B 1 549 ? 7.162   5.747   52.283  1.00 62.07  ?  799  SER B C   1 
ATOM   3796 O O   . SER B 1 549 ? 8.075   4.998   51.923  1.00 54.38  ?  799  SER B O   1 
ATOM   3797 C CB  . SER B 1 549 ? 5.678   4.371   53.760  1.00 56.30  ?  799  SER B CB  1 
ATOM   3798 O OG  . SER B 1 549 ? 6.251   5.057   54.860  1.00 59.11  ?  799  SER B OG  1 
ATOM   3799 N N   . VAL B 1 550 ? 7.342   7.048   52.510  1.00 52.41  ?  800  VAL B N   1 
ATOM   3800 C CA  . VAL B 1 550 ? 8.644   7.689   52.374  1.00 56.67  ?  800  VAL B CA  1 
ATOM   3801 C C   . VAL B 1 550 ? 9.179   8.205   53.696  1.00 59.55  ?  800  VAL B C   1 
ATOM   3802 O O   . VAL B 1 550 ? 10.282  8.770   53.725  1.00 65.72  ?  800  VAL B O   1 
ATOM   3803 C CB  . VAL B 1 550 ? 8.610   8.824   51.333  1.00 57.47  ?  800  VAL B CB  1 
ATOM   3804 C CG1 . VAL B 1 550 ? 8.389   8.258   49.938  1.00 54.92  ?  800  VAL B CG1 1 
ATOM   3805 C CG2 . VAL B 1 550 ? 7.531   9.836   51.683  1.00 51.27  ?  800  VAL B CG2 1 
ATOM   3806 N N   . GLY B 1 551 ? 8.447   8.036   54.783  1.00 63.78  ?  801  GLY B N   1 
ATOM   3807 C CA  . GLY B 1 551 ? 8.941   8.437   56.087  1.00 65.00  ?  801  GLY B CA  1 
ATOM   3808 C C   . GLY B 1 551 ? 7.809   8.841   57.005  1.00 59.21  ?  801  GLY B C   1 
ATOM   3809 O O   . GLY B 1 551 ? 6.665   9.021   56.592  1.00 61.59  ?  801  GLY B O   1 
ATOM   3810 N N   . LYS B 1 552 ? 8.156   8.985   58.281  1.00 63.68  ?  802  LYS B N   1 
ATOM   3811 C CA  . LYS B 1 552 ? 7.214   9.383   59.316  1.00 64.06  ?  802  LYS B CA  1 
ATOM   3812 C C   . LYS B 1 552 ? 7.305   10.884  59.566  1.00 65.65  ?  802  LYS B C   1 
ATOM   3813 O O   . LYS B 1 552 ? 8.363   11.497  59.402  1.00 67.26  ?  802  LYS B O   1 
ATOM   3814 C CB  . LYS B 1 552 ? 7.479   8.630   60.622  1.00 63.21  ?  802  LYS B CB  1 
ATOM   3815 C CG  . LYS B 1 552 ? 7.619   7.125   60.472  1.00 66.34  ?  802  LYS B CG  1 
ATOM   3816 C CD  . LYS B 1 552 ? 7.562   6.442   61.830  1.00 69.64  ?  802  LYS B CD  1 
ATOM   3817 C CE  . LYS B 1 552 ? 7.938   4.972   61.740  1.00 88.81  ?  802  LYS B CE  1 
ATOM   3818 N NZ  . LYS B 1 552 ? 9.395   4.782   61.499  1.00 88.47  1  802  LYS B NZ  1 
ATOM   3819 N N   . ALA B 1 553 ? 6.182   11.468  59.974  1.00 58.33  ?  803  ALA B N   1 
ATOM   3820 C CA  . ALA B 1 553 ? 6.094   12.889  60.277  1.00 61.99  ?  803  ALA B CA  1 
ATOM   3821 C C   . ALA B 1 553 ? 5.588   13.083  61.700  1.00 67.77  ?  803  ALA B C   1 
ATOM   3822 O O   . ALA B 1 553 ? 4.682   12.374  62.149  1.00 64.58  ?  803  ALA B O   1 
ATOM   3823 C CB  . ALA B 1 553 ? 5.171   13.611  59.291  1.00 56.65  ?  803  ALA B CB  1 
ATOM   3824 N N   . PHE B 1 554 ? 6.178   14.048  62.405  1.00 63.70  ?  804  PHE B N   1 
ATOM   3825 C CA  . PHE B 1 554 ? 5.797   14.372  63.772  1.00 65.67  ?  804  PHE B CA  1 
ATOM   3826 C C   . PHE B 1 554 ? 5.641   15.878  63.915  1.00 60.79  ?  804  PHE B C   1 
ATOM   3827 O O   . PHE B 1 554 ? 6.460   16.645  63.400  1.00 66.59  ?  804  PHE B O   1 
ATOM   3828 C CB  . PHE B 1 554 ? 6.836   13.870  64.783  1.00 62.65  ?  804  PHE B CB  1 
ATOM   3829 C CG  . PHE B 1 554 ? 7.204   12.425  64.610  1.00 70.60  ?  804  PHE B CG  1 
ATOM   3830 C CD1 . PHE B 1 554 ? 6.417   11.426  65.157  1.00 76.45  ?  804  PHE B CD1 1 
ATOM   3831 C CD2 . PHE B 1 554 ? 8.343   12.067  63.909  1.00 68.56  ?  804  PHE B CD2 1 
ATOM   3832 C CE1 . PHE B 1 554 ? 6.757   10.096  65.002  1.00 69.29  ?  804  PHE B CE1 1 
ATOM   3833 C CE2 . PHE B 1 554 ? 8.687   10.738  63.751  1.00 68.88  ?  804  PHE B CE2 1 
ATOM   3834 C CZ  . PHE B 1 554 ? 7.893   9.752   64.299  1.00 66.03  ?  804  PHE B CZ  1 
ATOM   3835 N N   . LYS B 1 555 ? 4.596   16.298  64.622  1.00 65.63  ?  805  LYS B N   1 
ATOM   3836 C CA  . LYS B 1 555 ? 4.344   17.708  64.892  1.00 69.61  ?  805  LYS B CA  1 
ATOM   3837 C C   . LYS B 1 555 ? 4.755   18.036  66.321  1.00 72.71  ?  805  LYS B C   1 
ATOM   3838 O O   . LYS B 1 555 ? 4.370   17.332  67.260  1.00 78.04  ?  805  LYS B O   1 
ATOM   3839 C CB  . LYS B 1 555 ? 2.870   18.052  64.673  1.00 70.58  ?  805  LYS B CB  1 
ATOM   3840 C CG  . LYS B 1 555 ? 2.528   19.505  64.961  1.00 86.20  ?  805  LYS B CG  1 
ATOM   3841 C CD  . LYS B 1 555 ? 1.350   19.959  64.119  1.00 98.02  ?  805  LYS B CD  1 
ATOM   3842 C CE  . LYS B 1 555 ? 1.680   19.853  62.638  1.00 94.37  ?  805  LYS B CE  1 
ATOM   3843 N NZ  . LYS B 1 555 ? 0.497   20.125  61.777  1.00 89.30  1  805  LYS B NZ  1 
ATOM   3844 N N   . ILE B 1 556 ? 5.529   19.105  66.481  1.00 80.23  ?  806  ILE B N   1 
ATOM   3845 C CA  . ILE B 1 556 ? 6.066   19.476  67.787  1.00 74.80  ?  806  ILE B CA  1 
ATOM   3846 C C   . ILE B 1 556 ? 4.993   20.224  68.568  1.00 74.00  ?  806  ILE B C   1 
ATOM   3847 O O   . ILE B 1 556 ? 4.517   21.280  68.137  1.00 79.95  ?  806  ILE B O   1 
ATOM   3848 C CB  . ILE B 1 556 ? 7.337   20.326  67.642  1.00 76.71  ?  806  ILE B CB  1 
ATOM   3849 C CG1 . ILE B 1 556 ? 8.466   19.494  67.028  1.00 71.02  ?  806  ILE B CG1 1 
ATOM   3850 C CG2 . ILE B 1 556 ? 7.764   20.883  68.989  1.00 71.12  ?  806  ILE B CG2 1 
ATOM   3851 C CD1 . ILE B 1 556 ? 9.766   20.252  66.857  1.00 58.06  ?  806  ILE B CD1 1 
ATOM   3852 N N   . VAL B 1 557 ? 4.605   19.675  69.718  1.00 75.23  ?  807  VAL B N   1 
ATOM   3853 C CA  . VAL B 1 557 ? 3.610   20.340  70.553  1.00 80.39  ?  807  VAL B CA  1 
ATOM   3854 C C   . VAL B 1 557 ? 4.286   21.329  71.493  1.00 80.90  ?  807  VAL B C   1 
ATOM   3855 O O   . VAL B 1 557 ? 3.866   22.486  71.612  1.00 80.17  ?  807  VAL B O   1 
ATOM   3856 C CB  . VAL B 1 557 ? 2.775   19.301  71.325  1.00 84.05  ?  807  VAL B CB  1 
ATOM   3857 C CG1 . VAL B 1 557 ? 1.774   19.995  72.233  1.00 77.46  ?  807  VAL B CG1 1 
ATOM   3858 C CG2 . VAL B 1 557 ? 2.073   18.362  70.350  1.00 77.82  ?  807  VAL B CG2 1 
ATOM   3859 N N   . SER B 1 558 ? 5.346   20.889  72.167  1.00 77.51  ?  808  SER B N   1 
ATOM   3860 C CA  . SER B 1 558 ? 6.107   21.743  73.066  1.00 74.34  ?  808  SER B CA  1 
ATOM   3861 C C   . SER B 1 558 ? 7.544   21.239  73.111  1.00 76.49  ?  808  SER B C   1 
ATOM   3862 O O   . SER B 1 558 ? 7.864   20.161  72.602  1.00 77.97  ?  808  SER B O   1 
ATOM   3863 C CB  . SER B 1 558 ? 5.486   21.777  74.469  1.00 77.54  ?  808  SER B CB  1 
ATOM   3864 O OG  . SER B 1 558 ? 5.484   20.492  75.066  1.00 95.32  ?  808  SER B OG  1 
ATOM   3865 N N   . LEU B 1 559 ? 8.414   22.036  73.729  1.00 79.81  ?  809  LEU B N   1 
ATOM   3866 C CA  . LEU B 1 559 ? 9.838   21.741  73.782  1.00 83.47  ?  809  LEU B CA  1 
ATOM   3867 C C   . LEU B 1 559 ? 10.381  22.036  75.173  1.00 91.39  ?  809  LEU B C   1 
ATOM   3868 O O   . LEU B 1 559 ? 9.971   23.004  75.819  1.00 75.66  ?  809  LEU B O   1 
ATOM   3869 C CB  . LEU B 1 559 ? 10.609  22.552  72.733  1.00 84.07  ?  809  LEU B CB  1 
ATOM   3870 C CG  . LEU B 1 559 ? 10.485  22.070  71.286  1.00 84.93  ?  809  LEU B CG  1 
ATOM   3871 C CD1 . LEU B 1 559 ? 10.763  23.202  70.313  1.00 78.68  ?  809  LEU B CD1 1 
ATOM   3872 C CD2 . LEU B 1 559 ? 11.432  20.908  71.031  1.00 74.70  ?  809  LEU B CD2 1 
ATOM   3873 N N   . ARG B 1 560 ? 11.310  21.193  75.618  1.00 85.76  ?  810  ARG B N   1 
ATOM   3874 C CA  . ARG B 1 560 ? 11.951  21.331  76.917  1.00 85.67  ?  810  ARG B CA  1 
ATOM   3875 C C   . ARG B 1 560 ? 13.382  20.826  76.803  1.00 86.07  ?  810  ARG B C   1 
ATOM   3876 O O   . ARG B 1 560 ? 13.638  19.822  76.133  1.00 94.24  ?  810  ARG B O   1 
ATOM   3877 C CB  . ARG B 1 560 ? 11.183  20.561  77.999  1.00 92.58  ?  810  ARG B CB  1 
ATOM   3878 C CG  . ARG B 1 560 ? 11.929  20.380  79.310  1.00 98.57  ?  810  ARG B CG  1 
ATOM   3879 C CD  . ARG B 1 560 ? 11.015  19.796  80.374  1.00 96.94  ?  810  ARG B CD  1 
ATOM   3880 N NE  . ARG B 1 560 ? 10.134  18.768  79.827  1.00 100.02 ?  810  ARG B NE  1 
ATOM   3881 C CZ  . ARG B 1 560 ? 10.409  17.468  79.823  1.00 107.87 ?  810  ARG B CZ  1 
ATOM   3882 N NH1 . ARG B 1 560 ? 11.547  17.026  80.341  1.00 99.19  1  810  ARG B NH1 1 
ATOM   3883 N NH2 . ARG B 1 560 ? 9.543   16.608  79.303  1.00 98.24  ?  810  ARG B NH2 1 
ATOM   3884 N N   . TYR B 1 561 ? 14.309  21.526  77.455  1.00 90.17  ?  811  TYR B N   1 
ATOM   3885 C CA  . TYR B 1 561 ? 15.736  21.259  77.317  1.00 89.83  ?  811  TYR B CA  1 
ATOM   3886 C C   . TYR B 1 561 ? 16.343  21.045  78.694  1.00 87.24  ?  811  TYR B C   1 
ATOM   3887 O O   . TYR B 1 561 ? 16.220  21.907  79.571  1.00 87.84  ?  811  TYR B O   1 
ATOM   3888 C CB  . TYR B 1 561 ? 16.435  22.409  76.588  1.00 84.57  ?  811  TYR B CB  1 
ATOM   3889 C CG  . TYR B 1 561 ? 15.730  22.804  75.311  1.00 87.41  ?  811  TYR B CG  1 
ATOM   3890 C CD1 . TYR B 1 561 ? 14.749  23.787  75.312  1.00 74.20  ?  811  TYR B CD1 1 
ATOM   3891 C CD2 . TYR B 1 561 ? 16.030  22.179  74.109  1.00 90.67  ?  811  TYR B CD2 1 
ATOM   3892 C CE1 . TYR B 1 561 ? 14.094  24.143  74.150  1.00 83.67  ?  811  TYR B CE1 1 
ATOM   3893 C CE2 . TYR B 1 561 ? 15.382  22.530  72.943  1.00 87.40  ?  811  TYR B CE2 1 
ATOM   3894 C CZ  . TYR B 1 561 ? 14.414  23.511  72.969  1.00 83.41  ?  811  TYR B CZ  1 
ATOM   3895 O OH  . TYR B 1 561 ? 13.763  23.861  71.810  1.00 79.63  ?  811  TYR B OH  1 
ATOM   3896 N N   . THR B 1 562 ? 16.992  19.896  78.882  1.00 81.64  ?  812  THR B N   1 
ATOM   3897 C CA  . THR B 1 562 ? 17.624  19.548  80.145  1.00 85.87  ?  812  THR B CA  1 
ATOM   3898 C C   . THR B 1 562 ? 19.083  19.181  79.910  1.00 88.68  ?  812  THR B C   1 
ATOM   3899 O O   . THR B 1 562 ? 19.461  18.731  78.824  1.00 84.70  ?  812  THR B O   1 
ATOM   3900 C CB  . THR B 1 562 ? 16.916  18.372  80.840  1.00 80.50  ?  812  THR B CB  1 
ATOM   3901 O OG1 . THR B 1 562 ? 17.342  17.139  80.249  1.00 81.07  ?  812  THR B OG1 1 
ATOM   3902 C CG2 . THR B 1 562 ? 15.405  18.491  80.705  1.00 94.41  ?  812  THR B CG2 1 
ATOM   3903 N N   . ARG B 1 563 ? 19.899  19.380  80.943  1.00 77.72  ?  813  ARG B N   1 
ATOM   3904 C CA  . ARG B 1 563 ? 21.295  18.964  80.933  1.00 84.25  ?  813  ARG B CA  1 
ATOM   3905 C C   . ARG B 1 563 ? 21.619  18.307  82.265  1.00 78.87  ?  813  ARG B C   1 
ATOM   3906 O O   . ARG B 1 563 ? 21.253  18.827  83.322  1.00 85.19  ?  813  ARG B O   1 
ATOM   3907 C CB  . ARG B 1 563 ? 22.240  20.146  80.679  1.00 82.61  ?  813  ARG B CB  1 
ATOM   3908 C CG  . ARG B 1 563 ? 22.025  20.820  79.336  1.00 87.96  ?  813  ARG B CG  1 
ATOM   3909 C CD  . ARG B 1 563 ? 23.263  21.559  78.859  1.00 84.28  ?  813  ARG B CD  1 
ATOM   3910 N NE  . ARG B 1 563 ? 24.379  20.656  78.593  1.00 93.35  ?  813  ARG B NE  1 
ATOM   3911 C CZ  . ARG B 1 563 ? 25.344  20.902  77.713  1.00 94.89  ?  813  ARG B CZ  1 
ATOM   3912 N NH1 . ARG B 1 563 ? 25.325  22.018  76.998  1.00 96.00  1  813  ARG B NH1 1 
ATOM   3913 N NH2 . ARG B 1 563 ? 26.324  20.025  77.539  1.00 100.46 ?  813  ARG B NH2 1 
ATOM   3914 N N   . LYS B 1 564 ? 22.299  17.166  82.207  1.00 82.63  ?  814  LYS B N   1 
ATOM   3915 C CA  . LYS B 1 564 ? 22.647  16.417  83.408  1.00 77.53  ?  814  LYS B CA  1 
ATOM   3916 C C   . LYS B 1 564 ? 23.819  17.092  84.108  1.00 76.00  ?  814  LYS B C   1 
ATOM   3917 O O   . LYS B 1 564 ? 24.903  17.225  83.529  1.00 74.75  ?  814  LYS B O   1 
ATOM   3918 C CB  . LYS B 1 564 ? 22.990  14.974  83.047  1.00 78.04  ?  814  LYS B CB  1 
ATOM   3919 C CG  . LYS B 1 564 ? 23.179  14.052  84.238  1.00 78.85  ?  814  LYS B CG  1 
ATOM   3920 C CD  . LYS B 1 564 ? 23.893  12.780  83.816  1.00 86.64  ?  814  LYS B CD  1 
ATOM   3921 C CE  . LYS B 1 564 ? 23.255  12.175  82.575  1.00 110.03 ?  814  LYS B CE  1 
ATOM   3922 N NZ  . LYS B 1 564 ? 24.172  11.222  81.893  1.00 99.04  1  814  LYS B NZ  1 
ATOM   3923 N N   . ALA B 1 565 ? 23.603  17.515  85.349  1.00 67.72  ?  815  ALA B N   1 
ATOM   3924 C CA  . ALA B 1 565 ? 24.629  18.174  86.147  1.00 65.34  ?  815  ALA B CA  1 
ATOM   3925 C C   . ALA B 1 565 ? 25.158  17.194  87.186  1.00 70.96  ?  815  ALA B C   1 
ATOM   3926 O O   . ALA B 1 565 ? 24.397  16.702  88.026  1.00 78.40  ?  815  ALA B O   1 
ATOM   3927 C CB  . ALA B 1 565 ? 24.074  19.428  86.821  1.00 78.67  ?  815  ALA B CB  1 
ATOM   3928 N N   . CYS B 1 566 ? 26.456  16.909  87.122  1.00 66.85  ?  816  CYS B N   1 
ATOM   3929 C CA  . CYS B 1 566 ? 27.133  16.058  88.091  1.00 68.02  ?  816  CYS B CA  1 
ATOM   3930 C C   . CYS B 1 566 ? 28.182  16.883  88.819  1.00 73.96  ?  816  CYS B C   1 
ATOM   3931 O O   . CYS B 1 566 ? 28.933  17.635  88.188  1.00 72.59  ?  816  CYS B O   1 
ATOM   3932 C CB  . CYS B 1 566 ? 27.781  14.850  87.413  1.00 64.25  ?  816  CYS B CB  1 
ATOM   3933 S SG  . CYS B 1 566 ? 26.632  13.569  86.850  1.00 81.45  ?  816  CYS B SG  1 
ATOM   3934 N N   . ILE B 1 567 ? 28.235  16.740  90.142  1.00 66.81  ?  817  ILE B N   1 
ATOM   3935 C CA  . ILE B 1 567 ? 29.076  17.570  90.994  1.00 69.16  ?  817  ILE B CA  1 
ATOM   3936 C C   . ILE B 1 567 ? 29.854  16.675  91.948  1.00 67.65  ?  817  ILE B C   1 
ATOM   3937 O O   . ILE B 1 567 ? 29.283  15.766  92.559  1.00 73.42  ?  817  ILE B O   1 
ATOM   3938 C CB  . ILE B 1 567 ? 28.241  18.599  91.782  1.00 69.15  ?  817  ILE B CB  1 
ATOM   3939 C CG1 . ILE B 1 567 ? 27.480  19.516  90.824  1.00 66.81  ?  817  ILE B CG1 1 
ATOM   3940 C CG2 . ILE B 1 567 ? 29.129  19.411  92.714  1.00 58.81  ?  817  ILE B CG2 1 
ATOM   3941 C CD1 . ILE B 1 567 ? 26.410  20.337  91.492  1.00 59.99  ?  817  ILE B CD1 1 
ATOM   3942 N N   . GLN B 1 568 ? 31.155  16.934  92.070  1.00 69.12  ?  818  GLN B N   1 
ATOM   3943 C CA  . GLN B 1 568 ? 32.013  16.293  93.062  1.00 66.24  ?  818  GLN B CA  1 
ATOM   3944 C C   . GLN B 1 568 ? 32.541  17.381  93.988  1.00 71.70  ?  818  GLN B C   1 
ATOM   3945 O O   . GLN B 1 568 ? 33.436  18.145  93.608  1.00 79.58  ?  818  GLN B O   1 
ATOM   3946 C CB  . GLN B 1 568 ? 33.162  15.537  92.396  1.00 65.71  ?  818  GLN B CB  1 
ATOM   3947 C CG  . GLN B 1 568 ? 34.153  14.919  93.374  1.00 65.38  ?  818  GLN B CG  1 
ATOM   3948 C CD  . GLN B 1 568 ? 33.616  13.669  94.041  1.00 73.27  ?  818  GLN B CD  1 
ATOM   3949 O OE1 . GLN B 1 568 ? 32.919  12.869  93.417  1.00 77.72  ?  818  GLN B OE1 1 
ATOM   3950 N NE2 . GLN B 1 568 ? 33.938  13.493  95.318  1.00 71.07  ?  818  GLN B NE2 1 
ATOM   3951 N N   . LEU B 1 569 ? 31.985  17.460  95.195  1.00 64.60  ?  819  LEU B N   1 
ATOM   3952 C CA  . LEU B 1 569 ? 32.372  18.463  96.184  1.00 66.40  ?  819  LEU B CA  1 
ATOM   3953 C C   . LEU B 1 569 ? 33.003  17.743  97.370  1.00 68.61  ?  819  LEU B C   1 
ATOM   3954 O O   . LEU B 1 569 ? 32.296  17.145  98.188  1.00 73.14  ?  819  LEU B O   1 
ATOM   3955 C CB  . LEU B 1 569 ? 31.172  19.298  96.623  1.00 71.71  ?  819  LEU B CB  1 
ATOM   3956 C CG  . LEU B 1 569 ? 31.480  20.378  97.661  1.00 56.41  ?  819  LEU B CG  1 
ATOM   3957 C CD1 . LEU B 1 569 ? 32.333  21.485  97.056  1.00 61.27  ?  819  LEU B CD1 1 
ATOM   3958 C CD2 . LEU B 1 569 ? 30.199  20.941  98.258  1.00 61.37  ?  819  LEU B CD2 1 
ATOM   3959 N N   . GLY B 1 570 ? 34.326  17.812  97.467  1.00 69.57  ?  820  GLY B N   1 
ATOM   3960 C CA  . GLY B 1 570 ? 35.010  17.120  98.548  1.00 75.00  ?  820  GLY B CA  1 
ATOM   3961 C C   . GLY B 1 570 ? 34.830  15.623  98.416  1.00 75.99  ?  820  GLY B C   1 
ATOM   3962 O O   . GLY B 1 570 ? 35.096  15.030  97.364  1.00 79.84  ?  820  GLY B O   1 
ATOM   3963 N N   . THR B 1 571 ? 34.364  14.999  99.493  1.00 74.50  ?  821  THR B N   1 
ATOM   3964 C CA  . THR B 1 571 ? 34.074  13.573  99.510  1.00 68.73  ?  821  THR B CA  1 
ATOM   3965 C C   . THR B 1 571 ? 32.637  13.258  99.113  1.00 77.18  ?  821  THR B C   1 
ATOM   3966 O O   . THR B 1 571 ? 32.227  12.095  99.186  1.00 77.18  ?  821  THR B O   1 
ATOM   3967 C CB  . THR B 1 571 ? 34.367  12.990  100.896 1.00 72.73  ?  821  THR B CB  1 
ATOM   3968 O OG1 . THR B 1 571 ? 33.750  11.703  101.019 1.00 108.06 ?  821  THR B OG1 1 
ATOM   3969 C CG2 . THR B 1 571 ? 33.839  13.911  101.987 1.00 92.57  ?  821  THR B CG2 1 
ATOM   3970 N N   . GLU B 1 572 ? 31.868  14.259  98.695  1.00 82.16  ?  822  GLU B N   1 
ATOM   3971 C CA  . GLU B 1 572 ? 30.476  14.077  98.312  1.00 70.56  ?  822  GLU B CA  1 
ATOM   3972 C C   . GLU B 1 572 ? 30.326  14.160  96.798  1.00 68.09  ?  822  GLU B C   1 
ATOM   3973 O O   . GLU B 1 572 ? 31.111  14.821  96.112  1.00 71.42  ?  822  GLU B O   1 
ATOM   3974 C CB  . GLU B 1 572 ? 29.578  15.119  98.984  1.00 69.39  ?  822  GLU B CB  1 
ATOM   3975 C CG  . GLU B 1 572 ? 29.564  15.034  100.501 1.00 74.93  ?  822  GLU B CG  1 
ATOM   3976 C CD  . GLU B 1 572 ? 28.535  15.953  101.127 1.00 81.48  ?  822  GLU B CD  1 
ATOM   3977 O OE1 . GLU B 1 572 ? 28.341  15.880  102.359 1.00 84.65  ?  822  GLU B OE1 1 
ATOM   3978 O OE2 . GLU B 1 572 ? 27.917  16.745  100.385 1.00 82.68  -1 822  GLU B OE2 1 
ATOM   3979 N N   . GLN B 1 573 ? 29.301  13.482  96.286  1.00 65.39  ?  823  GLN B N   1 
ATOM   3980 C CA  . GLN B 1 573 ? 29.054  13.411  94.853  1.00 62.92  ?  823  GLN B CA  1 
ATOM   3981 C C   . GLN B 1 573 ? 27.556  13.295  94.615  1.00 61.80  ?  823  GLN B C   1 
ATOM   3982 O O   . GLN B 1 573 ? 26.853  12.629  95.379  1.00 67.36  ?  823  GLN B O   1 
ATOM   3983 C CB  . GLN B 1 573 ? 29.789  12.220  94.225  1.00 75.86  ?  823  GLN B CB  1 
ATOM   3984 C CG  . GLN B 1 573 ? 29.521  12.021  92.743  1.00 83.07  ?  823  GLN B CG  1 
ATOM   3985 C CD  . GLN B 1 573 ? 30.195  10.779  92.195  1.00 90.19  ?  823  GLN B CD  1 
ATOM   3986 O OE1 . GLN B 1 573 ? 31.024  10.162  92.864  1.00 87.74  ?  823  GLN B OE1 1 
ATOM   3987 N NE2 . GLN B 1 573 ? 29.838  10.404  90.972  1.00 94.30  ?  823  GLN B NE2 1 
ATOM   3988 N N   . THR B 1 574 ? 27.074  13.950  93.560  1.00 67.03  ?  824  THR B N   1 
ATOM   3989 C CA  . THR B 1 574 ? 25.666  13.858  93.200  1.00 70.02  ?  824  THR B CA  1 
ATOM   3990 C C   . THR B 1 574 ? 25.505  14.175  91.720  1.00 65.53  ?  824  THR B C   1 
ATOM   3991 O O   . THR B 1 574 ? 26.321  14.887  91.128  1.00 70.74  ?  824  THR B O   1 
ATOM   3992 C CB  . THR B 1 574 ? 24.799  14.801  94.045  1.00 67.13  ?  824  THR B CB  1 
ATOM   3993 O OG1 . THR B 1 574 ? 23.415  14.499  93.834  1.00 84.74  ?  824  THR B OG1 1 
ATOM   3994 C CG2 . THR B 1 574 ? 25.053  16.254  93.669  1.00 71.31  ?  824  THR B CG2 1 
ATOM   3995 N N   . CYS B 1 575 ? 24.448  13.621  91.130  1.00 72.07  ?  825  CYS B N   1 
ATOM   3996 C CA  . CYS B 1 575 ? 24.079  13.891  89.746  1.00 81.39  ?  825  CYS B CA  1 
ATOM   3997 C C   . CYS B 1 575 ? 22.579  14.125  89.689  1.00 77.45  ?  825  CYS B C   1 
ATOM   3998 O O   . CYS B 1 575 ? 21.807  13.324  90.224  1.00 86.70  ?  825  CYS B O   1 
ATOM   3999 C CB  . CYS B 1 575 ? 24.459  12.731  88.816  1.00 68.54  ?  825  CYS B CB  1 
ATOM   4000 S SG  . CYS B 1 575 ? 26.227  12.477  88.517  1.00 88.75  ?  825  CYS B SG  1 
ATOM   4001 N N   . LYS B 1 576 ? 22.169  15.214  89.043  1.00 69.85  ?  826  LYS B N   1 
ATOM   4002 C CA  . LYS B 1 576 ? 20.757  15.546  88.920  1.00 76.20  ?  826  LYS B CA  1 
ATOM   4003 C C   . LYS B 1 576 ? 20.512  16.215  87.576  1.00 73.12  ?  826  LYS B C   1 
ATOM   4004 O O   . LYS B 1 576 ? 21.325  17.024  87.121  1.00 77.30  ?  826  LYS B O   1 
ATOM   4005 C CB  . LYS B 1 576 ? 20.295  16.465  90.059  1.00 73.04  ?  826  LYS B CB  1 
ATOM   4006 C CG  . LYS B 1 576 ? 20.108  15.765  91.397  1.00 89.19  ?  826  LYS B CG  1 
ATOM   4007 C CD  . LYS B 1 576 ? 18.749  15.088  91.483  1.00 94.86  ?  826  LYS B CD  1 
ATOM   4008 C CE  . LYS B 1 576 ? 18.818  13.802  92.295  1.00 100.66 ?  826  LYS B CE  1 
ATOM   4009 N NZ  . LYS B 1 576 ? 19.527  13.986  93.592  1.00 89.33  1  826  LYS B NZ  1 
ATOM   4010 N N   . ASN B 1 577 ? 19.392  15.867  86.946  1.00 79.01  ?  827  ASN B N   1 
ATOM   4011 C CA  . ASN B 1 577 ? 18.977  16.526  85.716  1.00 80.87  ?  827  ASN B CA  1 
ATOM   4012 C C   . ASN B 1 577 ? 18.389  17.892  86.039  1.00 82.33  ?  827  ASN B C   1 
ATOM   4013 O O   . ASN B 1 577 ? 17.561  18.022  86.947  1.00 97.22  ?  827  ASN B O   1 
ATOM   4014 C CB  . ASN B 1 577 ? 17.953  15.676  84.963  1.00 80.60  ?  827  ASN B CB  1 
ATOM   4015 C CG  . ASN B 1 577 ? 18.598  14.676  84.024  1.00 91.80  ?  827  ASN B CG  1 
ATOM   4016 O OD1 . ASN B 1 577 ? 19.013  15.025  82.919  1.00 97.08  ?  827  ASN B OD1 1 
ATOM   4017 N ND2 . ASN B 1 577 ? 18.678  13.422  84.456  1.00 99.13  ?  827  ASN B ND2 1 
ATOM   4018 N N   . VAL B 1 578 ? 18.821  18.911  85.302  1.00 86.67  ?  828  VAL B N   1 
ATOM   4019 C CA  . VAL B 1 578 ? 18.341  20.273  85.489  1.00 90.40  ?  828  VAL B CA  1 
ATOM   4020 C C   . VAL B 1 578 ? 17.705  20.747  84.191  1.00 86.22  ?  828  VAL B C   1 
ATOM   4021 O O   . VAL B 1 578 ? 18.180  20.420  83.098  1.00 89.49  ?  828  VAL B O   1 
ATOM   4022 C CB  . VAL B 1 578 ? 19.472  21.228  85.937  1.00 74.14  ?  828  VAL B CB  1 
ATOM   4023 C CG1 . VAL B 1 578 ? 20.255  20.616  87.084  1.00 79.01  ?  828  VAL B CG1 1 
ATOM   4024 C CG2 . VAL B 1 578 ? 20.404  21.578  84.782  1.00 75.78  ?  828  VAL B CG2 1 
ATOM   4025 N N   . ASP B 1 579 ? 16.604  21.486  84.314  1.00 89.87  ?  829  ASP B N   1 
ATOM   4026 C CA  . ASP B 1 579 ? 16.028  22.178  83.169  1.00 90.25  ?  829  ASP B CA  1 
ATOM   4027 C C   . ASP B 1 579 ? 15.774  23.632  83.540  1.00 96.90  ?  829  ASP B C   1 
ATOM   4028 O O   . ASP B 1 579 ? 16.291  24.116  84.553  1.00 104.67 ?  829  ASP B O   1 
ATOM   4029 C CB  . ASP B 1 579 ? 14.738  21.504  82.691  1.00 97.40  ?  829  ASP B CB  1 
ATOM   4030 C CG  . ASP B 1 579 ? 13.628  21.557  83.721  1.00 105.32 ?  829  ASP B CG  1 
ATOM   4031 O OD1 . ASP B 1 579 ? 13.574  20.656  84.584  1.00 112.05 ?  829  ASP B OD1 1 
ATOM   4032 O OD2 . ASP B 1 579 ? 12.815  22.504  83.670  1.00 106.61 -1 829  ASP B OD2 1 
ATOM   4033 N N   . SER B 1 580 ? 14.979  24.335  82.732  1.00 97.12  ?  830  SER B N   1 
ATOM   4034 C CA  . SER B 1 580 ? 14.767  25.760  82.965  1.00 102.22 ?  830  SER B CA  1 
ATOM   4035 C C   . SER B 1 580 ? 13.992  26.007  84.254  1.00 113.75 ?  830  SER B C   1 
ATOM   4036 O O   . SER B 1 580 ? 14.323  26.924  85.016  1.00 109.00 ?  830  SER B O   1 
ATOM   4037 C CB  . SER B 1 580 ? 14.041  26.382  81.773  1.00 103.38 ?  830  SER B CB  1 
ATOM   4038 O OG  . SER B 1 580 ? 14.790  26.219  80.581  1.00 108.76 ?  830  SER B OG  1 
ATOM   4039 N N   . ASN B 1 581 ? 12.967  25.200  84.521  1.00 114.99 ?  831  ASN B N   1 
ATOM   4040 C CA  . ASN B 1 581 ? 12.103  25.410  85.675  1.00 114.95 ?  831  ASN B CA  1 
ATOM   4041 C C   . ASN B 1 581 ? 12.515  24.603  86.899  1.00 109.35 ?  831  ASN B C   1 
ATOM   4042 O O   . ASN B 1 581 ? 11.925  24.791  87.969  1.00 117.70 ?  831  ASN B O   1 
ATOM   4043 C CB  . ASN B 1 581 ? 10.652  25.074  85.314  1.00 113.80 ?  831  ASN B CB  1 
ATOM   4044 C CG  . ASN B 1 581 ? 10.064  26.039  84.304  1.00 118.23 ?  831  ASN B CG  1 
ATOM   4045 O OD1 . ASN B 1 581 ? 10.319  27.242  84.358  1.00 124.35 ?  831  ASN B OD1 1 
ATOM   4046 N ND2 . ASN B 1 581 ? 9.274   25.515  83.374  1.00 108.57 ?  831  ASN B ND2 1 
ATOM   4047 N N   . ASP B 1 582 ? 13.506  23.715  86.778  1.00 112.90 ?  832  ASP B N   1 
ATOM   4048 C CA  . ASP B 1 582 ? 13.936  22.853  87.883  1.00 111.47 ?  832  ASP B CA  1 
ATOM   4049 C C   . ASP B 1 582 ? 15.445  23.017  88.055  1.00 109.79 ?  832  ASP B C   1 
ATOM   4050 O O   . ASP B 1 582 ? 16.228  22.153  87.652  1.00 101.29 ?  832  ASP B O   1 
ATOM   4051 C CB  . ASP B 1 582 ? 13.545  21.395  87.624  1.00 118.45 ?  832  ASP B CB  1 
ATOM   4052 C CG  . ASP B 1 582 ? 13.785  20.497  88.826  1.00 121.91 ?  832  ASP B CG  1 
ATOM   4053 O OD1 . ASP B 1 582 ? 14.182  21.011  89.895  1.00 115.97 ?  832  ASP B OD1 1 
ATOM   4054 O OD2 . ASP B 1 582 ? 13.572  19.273  88.697  1.00 119.23 -1 832  ASP B OD2 1 
ATOM   4055 N N   . CYS B 1 583 ? 15.849  24.132  88.659  1.00 109.61 ?  833  CYS B N   1 
ATOM   4056 C CA  . CYS B 1 583 ? 17.253  24.331  88.982  1.00 92.74  ?  833  CYS B CA  1 
ATOM   4057 C C   . CYS B 1 583 ? 17.696  23.343  90.054  1.00 84.06  ?  833  CYS B C   1 
ATOM   4058 O O   . CYS B 1 583 ? 16.916  22.939  90.922  1.00 88.16  ?  833  CYS B O   1 
ATOM   4059 C CB  . CYS B 1 583 ? 17.505  25.756  89.474  1.00 83.58  ?  833  CYS B CB  1 
ATOM   4060 S SG  . CYS B 1 583 ? 17.464  27.072  88.237  1.00 116.45 ?  833  CYS B SG  1 
ATOM   4061 N N   . LEU B 1 584 ? 18.965  22.951  89.986  1.00 77.78  ?  834  LEU B N   1 
ATOM   4062 C CA  . LEU B 1 584 ? 19.562  22.131  91.031  1.00 73.30  ?  834  LEU B CA  1 
ATOM   4063 C C   . LEU B 1 584 ? 19.910  23.021  92.216  1.00 78.86  ?  834  LEU B C   1 
ATOM   4064 O O   . LEU B 1 584 ? 20.716  23.948  92.085  1.00 74.31  ?  834  LEU B O   1 
ATOM   4065 C CB  . LEU B 1 584 ? 20.805  21.414  90.513  1.00 63.65  ?  834  LEU B CB  1 
ATOM   4066 C CG  . LEU B 1 584 ? 21.530  20.543  91.539  1.00 71.32  ?  834  LEU B CG  1 
ATOM   4067 C CD1 . LEU B 1 584 ? 20.590  19.489  92.103  1.00 63.89  ?  834  LEU B CD1 1 
ATOM   4068 C CD2 . LEU B 1 584 ? 22.759  19.898  90.921  1.00 66.98  ?  834  LEU B CD2 1 
ATOM   4069 N N   . VAL B 1 585 ? 19.303  22.749  93.366  1.00 76.23  ?  835  VAL B N   1 
ATOM   4070 C CA  . VAL B 1 585 ? 19.513  23.537  94.574  1.00 62.95  ?  835  VAL B CA  1 
ATOM   4071 C C   . VAL B 1 585 ? 19.979  22.575  95.660  1.00 70.00  ?  835  VAL B C   1 
ATOM   4072 O O   . VAL B 1 585 ? 19.184  21.803  96.209  1.00 66.58  ?  835  VAL B O   1 
ATOM   4073 C CB  . VAL B 1 585 ? 18.253  24.298  95.003  1.00 72.18  ?  835  VAL B CB  1 
ATOM   4074 C CG1 . VAL B 1 585 ? 18.477  24.977  96.344  1.00 60.91  ?  835  VAL B CG1 1 
ATOM   4075 C CG2 . VAL B 1 585 ? 17.868  25.319  93.944  1.00 71.53  ?  835  VAL B CG2 1 
ATOM   4076 N N   . THR B 1 586 ? 21.269  22.613  95.970  1.00 71.32  ?  836  THR B N   1 
ATOM   4077 C CA  . THR B 1 586 ? 21.843  21.897  97.098  1.00 60.25  ?  836  THR B CA  1 
ATOM   4078 C C   . THR B 1 586 ? 22.249  22.904  98.169  1.00 72.40  ?  836  THR B C   1 
ATOM   4079 O O   . THR B 1 586 ? 22.142  24.121  97.985  1.00 83.28  ?  836  THR B O   1 
ATOM   4080 C CB  . THR B 1 586 ? 23.031  21.042  96.652  1.00 66.02  ?  836  THR B CB  1 
ATOM   4081 O OG1 . THR B 1 586 ? 24.086  21.890  96.180  1.00 70.95  ?  836  THR B OG1 1 
ATOM   4082 C CG2 . THR B 1 586 ? 22.614  20.096  95.534  1.00 66.25  ?  836  THR B CG2 1 
ATOM   4083 N N   . THR B 1 587 ? 22.717  22.386  99.306  1.00 70.32  ?  837  THR B N   1 
ATOM   4084 C CA  . THR B 1 587 ? 23.083  23.263  100.413 1.00 72.74  ?  837  THR B CA  1 
ATOM   4085 C C   . THR B 1 587 ? 24.271  24.151  100.064 1.00 65.75  ?  837  THR B C   1 
ATOM   4086 O O   . THR B 1 587 ? 24.351  25.289  100.542 1.00 72.69  ?  837  THR B O   1 
ATOM   4087 C CB  . THR B 1 587 ? 23.390  22.440  101.664 1.00 67.32  ?  837  THR B CB  1 
ATOM   4088 O OG1 . THR B 1 587 ? 24.576  21.666  101.451 1.00 84.32  ?  837  THR B OG1 1 
ATOM   4089 C CG2 . THR B 1 587 ? 22.236  21.503  101.983 1.00 69.62  ?  837  THR B CG2 1 
ATOM   4090 N N   . SER B 1 588 ? 25.191  23.663  99.233  1.00 65.77  ?  838  SER B N   1 
ATOM   4091 C CA  . SER B 1 588 ? 26.396  24.407  98.891  1.00 60.25  ?  838  SER B CA  1 
ATOM   4092 C C   . SER B 1 588 ? 26.478  24.822  97.431  1.00 64.62  ?  838  SER B C   1 
ATOM   4093 O O   . SER B 1 588 ? 27.135  25.819  97.128  1.00 67.13  ?  838  SER B O   1 
ATOM   4094 C CB  . SER B 1 588 ? 27.644  23.584  99.236  1.00 63.76  ?  838  SER B CB  1 
ATOM   4095 O OG  . SER B 1 588 ? 27.754  23.385  100.635 1.00 78.49  ?  838  SER B OG  1 
ATOM   4096 N N   . VAL B 1 589 ? 25.837  24.092  96.520  1.00 62.54  ?  839  VAL B N   1 
ATOM   4097 C CA  . VAL B 1 589 ? 25.948  24.344  95.089  1.00 64.87  ?  839  VAL B CA  1 
ATOM   4098 C C   . VAL B 1 589 ? 24.558  24.559  94.507  1.00 66.48  ?  839  VAL B C   1 
ATOM   4099 O O   . VAL B 1 589 ? 23.609  23.852  94.863  1.00 66.64  ?  839  VAL B O   1 
ATOM   4100 C CB  . VAL B 1 589 ? 26.665  23.186  94.363  1.00 57.50  ?  839  VAL B CB  1 
ATOM   4101 C CG1 . VAL B 1 589 ? 26.988  23.577  92.930  1.00 63.47  ?  839  VAL B CG1 1 
ATOM   4102 C CG2 . VAL B 1 589 ? 27.929  22.786  95.109  1.00 63.74  ?  839  VAL B CG2 1 
ATOM   4103 N N   . LYS B 1 590 ? 24.444  25.537  93.610  1.00 66.13  ?  840  LYS B N   1 
ATOM   4104 C CA  . LYS B 1 590 ? 23.218  25.789  92.863  1.00 69.36  ?  840  LYS B CA  1 
ATOM   4105 C C   . LYS B 1 590 ? 23.560  25.867  91.383  1.00 67.17  ?  840  LYS B C   1 
ATOM   4106 O O   . LYS B 1 590 ? 24.378  26.698  90.978  1.00 73.75  ?  840  LYS B O   1 
ATOM   4107 C CB  . LYS B 1 590 ? 22.533  27.081  93.317  1.00 63.93  ?  840  LYS B CB  1 
ATOM   4108 C CG  . LYS B 1 590 ? 21.206  27.336  92.617  1.00 70.21  ?  840  LYS B CG  1 
ATOM   4109 C CD  . LYS B 1 590 ? 21.055  28.785  92.178  1.00 83.52  ?  840  LYS B CD  1 
ATOM   4110 C CE  . LYS B 1 590 ? 20.833  29.711  93.361  1.00 78.79  ?  840  LYS B CE  1 
ATOM   4111 N NZ  . LYS B 1 590 ? 20.571  31.109  92.918  1.00 75.71  1  840  LYS B NZ  1 
ATOM   4112 N N   . VAL B 1 591 ? 22.935  25.007  90.583  1.00 67.51  ?  841  VAL B N   1 
ATOM   4113 C CA  . VAL B 1 591 ? 23.118  24.988  89.136  1.00 70.04  ?  841  VAL B CA  1 
ATOM   4114 C C   . VAL B 1 591 ? 21.787  25.357  88.495  1.00 75.15  ?  841  VAL B C   1 
ATOM   4115 O O   . VAL B 1 591 ? 20.796  24.630  88.641  1.00 76.49  ?  841  VAL B O   1 
ATOM   4116 C CB  . VAL B 1 591 ? 23.610  23.619  88.641  1.00 68.70  ?  841  VAL B CB  1 
ATOM   4117 C CG1 . VAL B 1 591 ? 23.948  23.678  87.158  1.00 70.32  ?  841  VAL B CG1 1 
ATOM   4118 C CG2 . VAL B 1 591 ? 24.813  23.161  89.453  1.00 66.54  ?  841  VAL B CG2 1 
ATOM   4119 N N   . CYS B 1 592 ? 21.763  26.485  87.789  1.00 73.20  ?  842  CYS B N   1 
ATOM   4120 C CA  . CYS B 1 592 ? 20.553  27.007  87.165  1.00 76.64  ?  842  CYS B CA  1 
ATOM   4121 C C   . CYS B 1 592 ? 20.763  27.113  85.662  1.00 77.41  ?  842  CYS B C   1 
ATOM   4122 O O   . CYS B 1 592 ? 21.651  27.842  85.207  1.00 88.06  ?  842  CYS B O   1 
ATOM   4123 C CB  . CYS B 1 592 ? 20.183  28.377  87.738  1.00 81.39  ?  842  CYS B CB  1 
ATOM   4124 S SG  . CYS B 1 592 ? 18.830  28.402  88.944  1.00 115.13 ?  842  CYS B SG  1 
ATOM   4125 N N   . LEU B 1 593 ? 19.944  26.394  84.897  1.00 90.70  ?  843  LEU B N   1 
ATOM   4126 C CA  . LEU B 1 593 ? 19.879  26.560  83.445  1.00 82.01  ?  843  LEU B CA  1 
ATOM   4127 C C   . LEU B 1 593 ? 18.855  27.653  83.164  1.00 94.53  ?  843  LEU B C   1 
ATOM   4128 O O   . LEU B 1 593 ? 17.646  27.422  83.245  1.00 97.33  ?  843  LEU B O   1 
ATOM   4129 C CB  . LEU B 1 593 ? 19.506  25.248  82.764  1.00 77.98  ?  843  LEU B CB  1 
ATOM   4130 C CG  . LEU B 1 593 ? 19.232  25.324  81.260  1.00 86.00  ?  843  LEU B CG  1 
ATOM   4131 C CD1 . LEU B 1 593 ? 20.483  25.749  80.507  1.00 94.86  ?  843  LEU B CD1 1 
ATOM   4132 C CD2 . LEU B 1 593 ? 18.706  23.998  80.734  1.00 83.52  ?  843  LEU B CD2 1 
ATOM   4133 N N   . ILE B 1 594 ? 19.335  28.849  82.832  1.00 87.50  ?  844  ILE B N   1 
ATOM   4134 C CA  . ILE B 1 594 ? 18.449  30.006  82.774  1.00 90.48  ?  844  ILE B CA  1 
ATOM   4135 C C   . ILE B 1 594 ? 17.754  30.156  81.421  1.00 92.18  ?  844  ILE B C   1 
ATOM   4136 O O   . ILE B 1 594 ? 16.633  30.673  81.362  1.00 107.77 ?  844  ILE B O   1 
ATOM   4137 C CB  . ILE B 1 594 ? 19.219  31.287  83.143  1.00 94.77  ?  844  ILE B CB  1 
ATOM   4138 C CG1 . ILE B 1 594 ? 20.196  31.682  82.036  1.00 105.12 ?  844  ILE B CG1 1 
ATOM   4139 C CG2 . ILE B 1 594 ? 19.972  31.098  84.449  1.00 81.22  ?  844  ILE B CG2 1 
ATOM   4140 C CD1 . ILE B 1 594 ? 20.844  33.029  82.263  1.00 95.15  ?  844  ILE B CD1 1 
ATOM   4141 N N   . GLY B 1 595 ? 18.378  29.714  80.332  1.00 82.69  ?  845  GLY B N   1 
ATOM   4142 C CA  . GLY B 1 595 ? 17.783  29.897  79.022  1.00 97.01  ?  845  GLY B CA  1 
ATOM   4143 C C   . GLY B 1 595 ? 18.351  28.938  78.004  1.00 95.13  ?  845  GLY B C   1 
ATOM   4144 O O   . GLY B 1 595 ? 19.434  28.371  78.186  1.00 99.17  ?  845  GLY B O   1 
ATOM   4145 N N   . THR B 1 596 ? 17.602  28.764  76.916  1.00 86.26  ?  846  THR B N   1 
ATOM   4146 C CA  . THR B 1 596 ? 18.001  27.866  75.838  1.00 97.24  ?  846  THR B CA  1 
ATOM   4147 C C   . THR B 1 596 ? 17.481  28.423  74.522  1.00 90.80  ?  846  THR B C   1 
ATOM   4148 O O   . THR B 1 596 ? 16.277  28.658  74.381  1.00 89.08  ?  846  THR B O   1 
ATOM   4149 C CB  . THR B 1 596 ? 17.463  26.449  76.065  1.00 101.54 ?  846  THR B CB  1 
ATOM   4150 O OG1 . THR B 1 596 ? 17.764  26.027  77.401  1.00 93.69  ?  846  THR B OG1 1 
ATOM   4151 C CG2 . THR B 1 596 ? 18.095  25.476  75.081  1.00 88.13  ?  846  THR B CG2 1 
ATOM   4152 N N   . VAL B 1 597 ? 18.385  28.637  73.569  1.00 89.05  ?  847  VAL B N   1 
ATOM   4153 C CA  . VAL B 1 597 ? 18.031  29.067  72.221  1.00 98.82  ?  847  VAL B CA  1 
ATOM   4154 C C   . VAL B 1 597 ? 18.019  27.843  71.318  1.00 97.83  ?  847  VAL B C   1 
ATOM   4155 O O   . VAL B 1 597 ? 18.900  26.978  71.412  1.00 104.55 ?  847  VAL B O   1 
ATOM   4156 C CB  . VAL B 1 597 ? 19.004  30.145  71.703  1.00 105.88 ?  847  VAL B CB  1 
ATOM   4157 C CG1 . VAL B 1 597 ? 20.443  29.687  71.858  1.00 102.38 ?  847  VAL B CG1 1 
ATOM   4158 C CG2 . VAL B 1 597 ? 18.700  30.495  70.252  1.00 95.77  ?  847  VAL B CG2 1 
ATOM   4159 N N   . SER B 1 598 ? 17.016  27.760  70.448  1.00 95.96  ?  848  SER B N   1 
ATOM   4160 C CA  . SER B 1 598 ? 16.770  26.554  69.675  1.00 90.54  ?  848  SER B CA  1 
ATOM   4161 C C   . SER B 1 598 ? 16.554  26.875  68.205  1.00 87.64  ?  848  SER B C   1 
ATOM   4162 O O   . SER B 1 598 ? 16.094  27.962  67.846  1.00 97.90  ?  848  SER B O   1 
ATOM   4163 C CB  . SER B 1 598 ? 15.548  25.799  70.205  1.00 94.49  ?  848  SER B CB  1 
ATOM   4164 O OG  . SER B 1 598 ? 15.289  24.643  69.429  1.00 77.01  ?  848  SER B OG  1 
ATOM   4165 N N   . LYS B 1 599 ? 16.894  25.904  67.356  1.00 77.89  ?  849  LYS B N   1 
ATOM   4166 C CA  . LYS B 1 599 ? 16.503  25.930  65.955  1.00 80.42  ?  849  LYS B CA  1 
ATOM   4167 C C   . LYS B 1 599 ? 15.111  25.358  65.737  1.00 84.95  ?  849  LYS B C   1 
ATOM   4168 O O   . LYS B 1 599 ? 14.513  25.596  64.681  1.00 85.82  ?  849  LYS B O   1 
ATOM   4169 C CB  . LYS B 1 599 ? 17.511  25.145  65.105  1.00 74.10  ?  849  LYS B CB  1 
ATOM   4170 C CG  . LYS B 1 599 ? 17.177  23.668  64.952  1.00 85.81  ?  849  LYS B CG  1 
ATOM   4171 C CD  . LYS B 1 599 ? 18.372  22.856  64.481  1.00 89.99  ?  849  LYS B CD  1 
ATOM   4172 C CE  . LYS B 1 599 ? 18.948  23.392  63.182  1.00 96.78  ?  849  LYS B CE  1 
ATOM   4173 N NZ  . LYS B 1 599 ? 20.139  22.607  62.752  1.00 97.39  1  849  LYS B NZ  1 
ATOM   4174 N N   . PHE B 1 600 ? 14.587  24.617  66.711  1.00 81.82  ?  850  PHE B N   1 
ATOM   4175 C CA  . PHE B 1 600 ? 13.266  24.014  66.633  1.00 83.50  ?  850  PHE B CA  1 
ATOM   4176 C C   . PHE B 1 600 ? 12.253  24.900  67.343  1.00 76.44  ?  850  PHE B C   1 
ATOM   4177 O O   . PHE B 1 600 ? 12.547  25.484  68.391  1.00 76.97  ?  850  PHE B O   1 
ATOM   4178 C CB  . PHE B 1 600 ? 13.259  22.616  67.259  1.00 82.13  ?  850  PHE B CB  1 
ATOM   4179 C CG  . PHE B 1 600 ? 14.326  21.703  66.725  1.00 77.76  ?  850  PHE B CG  1 
ATOM   4180 C CD1 . PHE B 1 600 ? 14.107  20.955  65.580  1.00 76.00  ?  850  PHE B CD1 1 
ATOM   4181 C CD2 . PHE B 1 600 ? 15.545  21.585  67.373  1.00 74.25  ?  850  PHE B CD2 1 
ATOM   4182 C CE1 . PHE B 1 600 ? 15.086  20.112  65.088  1.00 65.55  ?  850  PHE B CE1 1 
ATOM   4183 C CE2 . PHE B 1 600 ? 16.529  20.743  66.885  1.00 81.89  ?  850  PHE B CE2 1 
ATOM   4184 C CZ  . PHE B 1 600 ? 16.298  20.006  65.741  1.00 73.73  ?  850  PHE B CZ  1 
ATOM   4185 N N   . GLN B 1 601 ? 11.064  24.995  66.771  1.00 73.57  ?  851  GLN B N   1 
ATOM   4186 C CA  . GLN B 1 601 ? 9.972   25.792  67.302  1.00 74.82  ?  851  GLN B CA  1 
ATOM   4187 C C   . GLN B 1 601 ? 8.740   24.921  67.455  1.00 75.86  ?  851  GLN B C   1 
ATOM   4188 O O   . GLN B 1 601 ? 8.604   23.899  66.775  1.00 75.95  ?  851  GLN B O   1 
ATOM   4189 C CB  . GLN B 1 601 ? 9.659   26.984  66.386  1.00 81.77  ?  851  GLN B CB  1 
ATOM   4190 C CG  . GLN B 1 601 ? 10.773  28.011  66.299  1.00 88.94  ?  851  GLN B CG  1 
ATOM   4191 C CD  . GLN B 1 601 ? 11.034  28.694  67.624  1.00 97.11  ?  851  GLN B CD  1 
ATOM   4192 O OE1 . GLN B 1 601 ? 10.104  28.997  68.374  1.00 95.13  ?  851  GLN B OE1 1 
ATOM   4193 N NE2 . GLN B 1 601 ? 12.304  28.936  67.925  1.00 100.41 ?  851  GLN B NE2 1 
ATOM   4194 N N   . PRO B 1 602 ? 7.828   25.287  68.355  1.00 77.79  ?  852  PRO B N   1 
ATOM   4195 C CA  . PRO B 1 602 ? 6.542   24.590  68.418  1.00 76.62  ?  852  PRO B CA  1 
ATOM   4196 C C   . PRO B 1 602 ? 5.791   24.711  67.101  1.00 74.31  ?  852  PRO B C   1 
ATOM   4197 O O   . PRO B 1 602 ? 5.999   25.637  66.314  1.00 73.74  ?  852  PRO B O   1 
ATOM   4198 C CB  . PRO B 1 602 ? 5.801   25.309  69.552  1.00 76.74  ?  852  PRO B CB  1 
ATOM   4199 C CG  . PRO B 1 602 ? 6.892   25.864  70.404  1.00 82.37  ?  852  PRO B CG  1 
ATOM   4200 C CD  . PRO B 1 602 ? 7.989   26.250  69.457  1.00 81.00  ?  852  PRO B CD  1 
ATOM   4201 N N   . SER B 1 603 ? 4.908   23.740  66.869  1.00 81.26  ?  853  SER B N   1 
ATOM   4202 C CA  . SER B 1 603 ? 4.107   23.569  65.659  1.00 79.10  ?  853  SER B CA  1 
ATOM   4203 C C   . SER B 1 603 ? 4.947   23.180  64.447  1.00 78.79  ?  853  SER B C   1 
ATOM   4204 O O   . SER B 1 603 ? 4.387   22.997  63.360  1.00 83.26  ?  853  SER B O   1 
ATOM   4205 C CB  . SER B 1 603 ? 3.279   24.819  65.317  1.00 80.64  ?  853  SER B CB  1 
ATOM   4206 O OG  . SER B 1 603 ? 2.364   24.551  64.269  1.00 104.71 ?  853  SER B OG  1 
ATOM   4207 N N   . ASP B 1 604 ? 6.265   23.046  64.590  1.00 70.87  ?  854  ASP B N   1 
ATOM   4208 C CA  . ASP B 1 604 ? 7.080   22.513  63.508  1.00 73.69  ?  854  ASP B CA  1 
ATOM   4209 C C   . ASP B 1 604 ? 6.739   21.049  63.259  1.00 77.67  ?  854  ASP B C   1 
ATOM   4210 O O   . ASP B 1 604 ? 6.366   20.310  64.175  1.00 78.58  ?  854  ASP B O   1 
ATOM   4211 C CB  . ASP B 1 604 ? 8.570   22.640  63.834  1.00 68.14  ?  854  ASP B CB  1 
ATOM   4212 C CG  . ASP B 1 604 ? 9.081   24.061  63.710  1.00 81.54  ?  854  ASP B CG  1 
ATOM   4213 O OD1 . ASP B 1 604 ? 8.286   24.953  63.347  1.00 82.69  ?  854  ASP B OD1 1 
ATOM   4214 O OD2 . ASP B 1 604 ? 10.282  24.283  63.975  1.00 65.54  -1 854  ASP B OD2 1 
ATOM   4215 N N   . THR B 1 605 ? 6.869   20.632  62.004  1.00 79.94  ?  855  THR B N   1 
ATOM   4216 C CA  . THR B 1 605 ? 6.666   19.243  61.613  1.00 68.42  ?  855  THR B CA  1 
ATOM   4217 C C   . THR B 1 605 ? 8.021   18.625  61.297  1.00 71.50  ?  855  THR B C   1 
ATOM   4218 O O   . THR B 1 605 ? 8.755   19.133  60.442  1.00 64.15  ?  855  THR B O   1 
ATOM   4219 C CB  . THR B 1 605 ? 5.729   19.132  60.410  1.00 60.30  ?  855  THR B CB  1 
ATOM   4220 O OG1 . THR B 1 605 ? 4.415   19.562  60.785  1.00 63.65  ?  855  THR B OG1 1 
ATOM   4221 C CG2 . THR B 1 605 ? 5.663   17.692  59.921  1.00 66.67  ?  855  THR B CG2 1 
ATOM   4222 N N   . LEU B 1 606 ? 8.351   17.539  61.991  1.00 67.76  ?  856  LEU B N   1 
ATOM   4223 C CA  . LEU B 1 606 ? 9.606   16.827  61.791  1.00 65.40  ?  856  LEU B CA  1 
ATOM   4224 C C   . LEU B 1 606 ? 9.354   15.620  60.896  1.00 65.74  ?  856  LEU B C   1 
ATOM   4225 O O   . LEU B 1 606 ? 8.549   14.747  61.236  1.00 71.50  ?  856  LEU B O   1 
ATOM   4226 C CB  . LEU B 1 606 ? 10.206  16.387  63.127  1.00 64.15  ?  856  LEU B CB  1 
ATOM   4227 C CG  . LEU B 1 606 ? 10.461  17.475  64.172  1.00 71.60  ?  856  LEU B CG  1 
ATOM   4228 C CD1 . LEU B 1 606 ? 11.145  16.889  65.399  1.00 59.06  ?  856  LEU B CD1 1 
ATOM   4229 C CD2 . LEU B 1 606 ? 11.284  18.611  63.584  1.00 72.85  ?  856  LEU B CD2 1 
ATOM   4230 N N   . LEU B 1 607 ? 10.040  15.575  59.758  1.00 65.97  ?  857  LEU B N   1 
ATOM   4231 C CA  . LEU B 1 607 ? 9.937   14.474  58.811  1.00 61.05  ?  857  LEU B CA  1 
ATOM   4232 C C   . LEU B 1 607 ? 11.210  13.643  58.868  1.00 64.28  ?  857  LEU B C   1 
ATOM   4233 O O   . LEU B 1 607 ? 12.316  14.193  58.849  1.00 66.22  ?  857  LEU B O   1 
ATOM   4234 C CB  . LEU B 1 607 ? 9.705   14.994  57.390  1.00 61.26  ?  857  LEU B CB  1 
ATOM   4235 C CG  . LEU B 1 607 ? 9.717   13.949  56.273  1.00 56.13  ?  857  LEU B CG  1 
ATOM   4236 C CD1 . LEU B 1 607 ? 8.546   12.988  56.413  1.00 53.74  ?  857  LEU B CD1 1 
ATOM   4237 C CD2 . LEU B 1 607 ? 9.710   14.621  54.910  1.00 57.17  ?  857  LEU B CD2 1 
ATOM   4238 N N   . PHE B 1 608 ? 11.054  12.323  58.939  1.00 63.22  ?  858  PHE B N   1 
ATOM   4239 C CA  . PHE B 1 608 ? 12.178  11.392  59.018  1.00 60.23  ?  858  PHE B CA  1 
ATOM   4240 C C   . PHE B 1 608 ? 12.123  10.464  57.809  1.00 64.39  ?  858  PHE B C   1 
ATOM   4241 O O   . PHE B 1 608 ? 11.299  9.546   57.761  1.00 70.38  ?  858  PHE B O   1 
ATOM   4242 C CB  . PHE B 1 608 ? 12.148  10.606  60.326  1.00 66.83  ?  858  PHE B CB  1 
ATOM   4243 C CG  . PHE B 1 608 ? 12.521  11.422  61.530  1.00 66.26  ?  858  PHE B CG  1 
ATOM   4244 C CD1 . PHE B 1 608 ? 13.836  11.481  61.962  1.00 71.76  ?  858  PHE B CD1 1 
ATOM   4245 C CD2 . PHE B 1 608 ? 11.559  12.133  62.227  1.00 69.50  ?  858  PHE B CD2 1 
ATOM   4246 C CE1 . PHE B 1 608 ? 14.185  12.233  63.067  1.00 67.60  ?  858  PHE B CE1 1 
ATOM   4247 C CE2 . PHE B 1 608 ? 11.901  12.887  63.334  1.00 66.56  ?  858  PHE B CE2 1 
ATOM   4248 C CZ  . PHE B 1 608 ? 13.216  12.937  63.754  1.00 67.42  ?  858  PHE B CZ  1 
ATOM   4249 N N   . LEU B 1 609 ? 13.009  10.702  56.837  1.00 67.32  ?  859  LEU B N   1 
ATOM   4250 C CA  . LEU B 1 609 ? 13.042  9.869   55.639  1.00 63.08  ?  859  LEU B CA  1 
ATOM   4251 C C   . LEU B 1 609 ? 13.429  8.432   55.961  1.00 63.17  ?  859  LEU B C   1 
ATOM   4252 O O   . LEU B 1 609 ? 12.968  7.500   55.292  1.00 78.40  ?  859  LEU B O   1 
ATOM   4253 C CB  . LEU B 1 609 ? 14.011  10.462  54.614  1.00 60.01  ?  859  LEU B CB  1 
ATOM   4254 C CG  . LEU B 1 609 ? 13.456  11.424  53.557  1.00 59.58  ?  859  LEU B CG  1 
ATOM   4255 C CD1 . LEU B 1 609 ? 12.631  10.673  52.523  1.00 78.26  ?  859  LEU B CD1 1 
ATOM   4256 C CD2 . LEU B 1 609 ? 12.637  12.536  54.191  1.00 59.96  ?  859  LEU B CD2 1 
ATOM   4257 N N   . GLY B 1 610 ? 14.269  8.231   56.972  1.00 71.72  ?  860  GLY B N   1 
ATOM   4258 C CA  . GLY B 1 610 ? 14.673  6.907   57.378  1.00 72.64  ?  860  GLY B CA  1 
ATOM   4259 C C   . GLY B 1 610 ? 14.557  6.718   58.877  1.00 67.47  ?  860  GLY B C   1 
ATOM   4260 O O   . GLY B 1 610 ? 13.639  7.236   59.521  1.00 75.15  ?  860  GLY B O   1 
ATOM   4261 N N   . PRO B 1 611 ? 15.486  5.962   59.461  1.00 70.31  ?  861  PRO B N   1 
ATOM   4262 C CA  . PRO B 1 611 ? 15.489  5.792   60.918  1.00 78.18  ?  861  PRO B CA  1 
ATOM   4263 C C   . PRO B 1 611 ? 15.710  7.118   61.633  1.00 79.66  ?  861  PRO B C   1 
ATOM   4264 O O   . PRO B 1 611 ? 16.129  8.115   61.041  1.00 76.33  ?  861  PRO B O   1 
ATOM   4265 C CB  . PRO B 1 611 ? 16.655  4.826   61.163  1.00 74.44  ?  861  PRO B CB  1 
ATOM   4266 C CG  . PRO B 1 611 ? 16.842  4.117   59.857  1.00 76.64  ?  861  PRO B CG  1 
ATOM   4267 C CD  . PRO B 1 611 ? 16.507  5.130   58.804  1.00 81.36  ?  861  PRO B CD  1 
ATOM   4268 N N   . LEU B 1 612 ? 15.417  7.116   62.937  1.00 79.64  ?  862  LEU B N   1 
ATOM   4269 C CA  . LEU B 1 612 ? 15.505  8.346   63.719  1.00 78.11  ?  862  LEU B CA  1 
ATOM   4270 C C   . LEU B 1 612 ? 16.927  8.894   63.744  1.00 86.94  ?  862  LEU B C   1 
ATOM   4271 O O   . LEU B 1 612 ? 17.136  10.101  63.580  1.00 85.66  ?  862  LEU B O   1 
ATOM   4272 C CB  . LEU B 1 612 ? 15.005  8.100   65.143  1.00 68.99  ?  862  LEU B CB  1 
ATOM   4273 C CG  . LEU B 1 612 ? 13.495  7.955   65.322  1.00 59.99  ?  862  LEU B CG  1 
ATOM   4274 C CD1 . LEU B 1 612 ? 13.153  7.724   66.786  1.00 63.74  ?  862  LEU B CD1 1 
ATOM   4275 C CD2 . LEU B 1 612 ? 12.775  9.184   64.787  1.00 67.03  ?  862  LEU B CD2 1 
ATOM   4276 N N   . GLU B 1 613 ? 17.916  8.026   63.942  1.00 86.44  ?  863  GLU B N   1 
ATOM   4277 C CA  . GLU B 1 613 ? 19.305  8.454   64.050  1.00 82.94  ?  863  GLU B CA  1 
ATOM   4278 C C   . GLU B 1 613 ? 19.947  8.759   62.700  1.00 81.12  ?  863  GLU B C   1 
ATOM   4279 O O   . GLU B 1 613 ? 21.174  8.892   62.635  1.00 88.23  ?  863  GLU B O   1 
ATOM   4280 C CB  . GLU B 1 613 ? 20.131  7.395   64.788  1.00 84.91  ?  863  GLU B CB  1 
ATOM   4281 C CG  . GLU B 1 613 ? 20.249  6.061   64.065  1.00 98.72  ?  863  GLU B CG  1 
ATOM   4282 C CD  . GLU B 1 613 ? 19.038  5.168   64.269  1.00 105.25 ?  863  GLU B CD  1 
ATOM   4283 O OE1 . GLU B 1 613 ? 18.141  5.546   65.053  1.00 100.82 ?  863  GLU B OE1 1 
ATOM   4284 O OE2 . GLU B 1 613 ? 18.985  4.086   63.647  1.00 100.83 -1 863  GLU B OE2 1 
ATOM   4285 N N   . GLN B 1 614 ? 19.161  8.881   61.631  1.00 71.79  ?  864  GLN B N   1 
ATOM   4286 C CA  . GLN B 1 614 ? 19.685  9.211   60.313  1.00 74.48  ?  864  GLN B CA  1 
ATOM   4287 C C   . GLN B 1 614 ? 19.442  10.665  59.927  1.00 79.27  ?  864  GLN B C   1 
ATOM   4288 O O   . GLN B 1 614 ? 19.858  11.083  58.842  1.00 78.85  ?  864  GLN B O   1 
ATOM   4289 C CB  . GLN B 1 614 ? 19.075  8.285   59.254  1.00 79.56  ?  864  GLN B CB  1 
ATOM   4290 C CG  . GLN B 1 614 ? 19.970  8.052   58.044  1.00 76.07  ?  864  GLN B CG  1 
ATOM   4291 C CD  . GLN B 1 614 ? 19.268  7.304   56.927  1.00 95.08  ?  864  GLN B CD  1 
ATOM   4292 O OE1 . GLN B 1 614 ? 18.040  7.244   56.881  1.00 94.79  ?  864  GLN B OE1 1 
ATOM   4293 N NE2 . GLN B 1 614 ? 20.048  6.729   56.018  1.00 82.88  ?  864  GLN B NE2 1 
ATOM   4294 N N   . GLY B 1 615 ? 18.786  11.439  60.778  1.00 75.40  ?  865  GLY B N   1 
ATOM   4295 C CA  . GLY B 1 615 ? 18.510  12.835  60.510  1.00 77.07  ?  865  GLY B CA  1 
ATOM   4296 C C   . GLY B 1 615 ? 17.043  13.075  60.193  1.00 67.84  ?  865  GLY B C   1 
ATOM   4297 O O   . GLY B 1 615 ? 16.239  12.153  60.052  1.00 77.53  ?  865  GLY B O   1 
ATOM   4298 N N   . GLY B 1 616 ? 16.708  14.359  60.079  1.00 74.37  ?  866  GLY B N   1 
ATOM   4299 C CA  . GLY B 1 616 ? 15.348  14.764  59.800  1.00 69.55  ?  866  GLY B CA  1 
ATOM   4300 C C   . GLY B 1 616 ? 15.301  16.071  59.039  1.00 64.26  ?  866  GLY B C   1 
ATOM   4301 O O   . GLY B 1 616 ? 16.326  16.707  58.783  1.00 67.65  ?  866  GLY B O   1 
ATOM   4302 N N   . LEU B 1 617 ? 14.083  16.465  58.671  1.00 66.67  ?  867  LEU B N   1 
ATOM   4303 C CA  . LEU B 1 617 ? 13.826  17.718  57.981  1.00 64.82  ?  867  LEU B CA  1 
ATOM   4304 C C   . LEU B 1 617 ? 12.726  18.474  58.712  1.00 72.78  ?  867  LEU B C   1 
ATOM   4305 O O   . LEU B 1 617 ? 11.824  17.872  59.301  1.00 69.49  ?  867  LEU B O   1 
ATOM   4306 C CB  . LEU B 1 617 ? 13.420  17.487  56.517  1.00 67.47  ?  867  LEU B CB  1 
ATOM   4307 C CG  . LEU B 1 617 ? 14.480  16.888  55.590  1.00 68.69  ?  867  LEU B CG  1 
ATOM   4308 C CD1 . LEU B 1 617 ? 13.875  16.569  54.234  1.00 58.17  ?  867  LEU B CD1 1 
ATOM   4309 C CD2 . LEU B 1 617 ? 15.664  17.831  55.440  1.00 71.06  ?  867  LEU B CD2 1 
ATOM   4310 N N   . ILE B 1 618 ? 12.810  19.800  58.673  1.00 72.70  ?  868  ILE B N   1 
ATOM   4311 C CA  . ILE B 1 618 ? 11.872  20.677  59.362  1.00 72.89  ?  868  ILE B CA  1 
ATOM   4312 C C   . ILE B 1 618 ? 10.966  21.327  58.327  1.00 65.53  ?  868  ILE B C   1 
ATOM   4313 O O   . ILE B 1 618 ? 11.447  21.901  57.343  1.00 80.23  ?  868  ILE B O   1 
ATOM   4314 C CB  . ILE B 1 618 ? 12.603  21.741  60.199  1.00 65.57  ?  868  ILE B CB  1 
ATOM   4315 C CG1 . ILE B 1 618 ? 13.522  21.072  61.223  1.00 73.34  ?  868  ILE B CG1 1 
ATOM   4316 C CG2 . ILE B 1 618 ? 11.604  22.654  60.892  1.00 63.93  ?  868  ILE B CG2 1 
ATOM   4317 C CD1 . ILE B 1 618 ? 14.262  22.051  62.109  1.00 77.28  ?  868  ILE B CD1 1 
ATOM   4318 N N   . PHE B 1 619 ? 9.657   21.238  58.551  1.00 60.89  ?  869  PHE B N   1 
ATOM   4319 C CA  . PHE B 1 619 ? 8.656   21.827  57.670  1.00 68.39  ?  869  PHE B CA  1 
ATOM   4320 C C   . PHE B 1 619 ? 7.839   22.838  58.460  1.00 78.78  ?  869  PHE B C   1 
ATOM   4321 O O   . PHE B 1 619 ? 7.181   22.478  59.442  1.00 70.39  ?  869  PHE B O   1 
ATOM   4322 C CB  . PHE B 1 619 ? 7.745   20.754  57.071  1.00 64.19  ?  869  PHE B CB  1 
ATOM   4323 C CG  . PHE B 1 619 ? 8.404   19.918  56.014  1.00 67.16  ?  869  PHE B CG  1 
ATOM   4324 C CD1 . PHE B 1 619 ? 8.157   20.156  54.672  1.00 66.27  ?  869  PHE B CD1 1 
ATOM   4325 C CD2 . PHE B 1 619 ? 9.271   18.895  56.359  1.00 77.11  ?  869  PHE B CD2 1 
ATOM   4326 C CE1 . PHE B 1 619 ? 8.761   19.387  53.696  1.00 75.69  ?  869  PHE B CE1 1 
ATOM   4327 C CE2 . PHE B 1 619 ? 9.880   18.125  55.387  1.00 61.35  ?  869  PHE B CE2 1 
ATOM   4328 C CZ  . PHE B 1 619 ? 9.624   18.371  54.053  1.00 59.03  ?  869  PHE B CZ  1 
ATOM   4329 N N   . LYS B 1 620 ? 7.885   24.101  58.033  1.00 77.00  ?  870  LYS B N   1 
ATOM   4330 C CA  . LYS B 1 620 ? 7.054   25.127  58.650  1.00 69.59  ?  870  LYS B CA  1 
ATOM   4331 C C   . LYS B 1 620 ? 5.622   25.079  58.135  1.00 72.10  ?  870  LYS B C   1 
ATOM   4332 O O   . LYS B 1 620 ? 4.686   25.362  58.891  1.00 87.46  ?  870  LYS B O   1 
ATOM   4333 C CB  . LYS B 1 620 ? 7.654   26.512  58.402  1.00 79.04  ?  870  LYS B CB  1 
ATOM   4334 C CG  . LYS B 1 620 ? 8.966   26.770  59.126  1.00 66.61  ?  870  LYS B CG  1 
ATOM   4335 C CD  . LYS B 1 620 ? 8.743   27.005  60.611  1.00 67.61  ?  870  LYS B CD  1 
ATOM   4336 C CE  . LYS B 1 620 ? 10.038  27.396  61.307  1.00 73.84  ?  870  LYS B CE  1 
ATOM   4337 N NZ  . LYS B 1 620 ? 9.806   27.842  62.710  1.00 90.45  1  870  LYS B NZ  1 
ATOM   4338 N N   . GLN B 1 621 ? 5.434   24.726  56.867  1.00 76.37  ?  871  GLN B N   1 
ATOM   4339 C CA  . GLN B 1 621 ? 4.113   24.610  56.254  1.00 78.50  ?  871  GLN B CA  1 
ATOM   4340 C C   . GLN B 1 621 ? 3.878   23.142  55.908  1.00 78.74  ?  871  GLN B C   1 
ATOM   4341 O O   . GLN B 1 621 ? 4.364   22.648  54.886  1.00 89.65  ?  871  GLN B O   1 
ATOM   4342 C CB  . GLN B 1 621 ? 4.004   25.499  55.019  1.00 85.24  ?  871  GLN B CB  1 
ATOM   4343 C CG  . GLN B 1 621 ? 3.971   26.989  55.326  1.00 98.57  ?  871  GLN B CG  1 
ATOM   4344 C CD  . GLN B 1 621 ? 2.675   27.420  55.988  1.00 100.11 ?  871  GLN B CD  1 
ATOM   4345 O OE1 . GLN B 1 621 ? 1.586   27.177  55.466  1.00 104.37 ?  871  GLN B OE1 1 
ATOM   4346 N NE2 . GLN B 1 621 ? 2.785   28.060  57.147  1.00 100.08 ?  871  GLN B NE2 1 
ATOM   4347 N N   . TRP B 1 622 ? 3.137   22.450  56.768  1.00 75.49  ?  872  TRP B N   1 
ATOM   4348 C CA  . TRP B 1 622 ? 2.730   21.070  56.548  1.00 74.33  ?  872  TRP B CA  1 
ATOM   4349 C C   . TRP B 1 622 ? 1.215   21.034  56.406  1.00 65.69  ?  872  TRP B C   1 
ATOM   4350 O O   . TRP B 1 622 ? 0.500   21.678  57.181  1.00 68.95  ?  872  TRP B O   1 
ATOM   4351 C CB  . TRP B 1 622 ? 3.189   20.171  57.706  1.00 70.36  ?  872  TRP B CB  1 
ATOM   4352 C CG  . TRP B 1 622 ? 3.082   18.696  57.443  1.00 71.64  ?  872  TRP B CG  1 
ATOM   4353 C CD1 . TRP B 1 622 ? 2.061   17.870  57.815  1.00 75.48  ?  872  TRP B CD1 1 
ATOM   4354 C CD2 . TRP B 1 622 ? 4.038   17.870  56.763  1.00 62.39  ?  872  TRP B CD2 1 
ATOM   4355 N NE1 . TRP B 1 622 ? 2.319   16.584  57.406  1.00 66.28  ?  872  TRP B NE1 1 
ATOM   4356 C CE2 . TRP B 1 622 ? 3.526   16.557  56.757  1.00 63.02  ?  872  TRP B CE2 1 
ATOM   4357 C CE3 . TRP B 1 622 ? 5.275   18.114  56.157  1.00 68.72  ?  872  TRP B CE3 1 
ATOM   4358 C CZ2 . TRP B 1 622 ? 4.208   15.492  56.171  1.00 53.69  ?  872  TRP B CZ2 1 
ATOM   4359 C CZ3 . TRP B 1 622 ? 5.950   17.054  55.573  1.00 65.87  ?  872  TRP B CZ3 1 
ATOM   4360 C CH2 . TRP B 1 622 ? 5.413   15.760  55.584  1.00 60.73  ?  872  TRP B CH2 1 
ATOM   4361 N N   . CYS B 1 623 ? 0.730   20.295  55.407  1.00 67.73  ?  873  CYS B N   1 
ATOM   4362 C CA  . CYS B 1 623 ? -0.696  20.302  55.095  1.00 74.81  ?  873  CYS B CA  1 
ATOM   4363 C C   . CYS B 1 623 ? -1.520  19.862  56.299  1.00 80.43  ?  873  CYS B C   1 
ATOM   4364 O O   . CYS B 1 623 ? -1.147  18.941  57.031  1.00 69.59  ?  873  CYS B O   1 
ATOM   4365 C CB  . CYS B 1 623 ? -0.994  19.396  53.898  1.00 67.68  ?  873  CYS B CB  1 
ATOM   4366 S SG  . CYS B 1 623 ? -2.196  18.083  54.245  1.00 103.73 ?  873  CYS B SG  1 
ATOM   4367 N N   . THR B 1 624 ? -2.643  20.548  56.510  1.00 83.07  ?  874  THR B N   1 
ATOM   4368 C CA  . THR B 1 624 ? -3.537  20.251  57.622  1.00 78.42  ?  874  THR B CA  1 
ATOM   4369 C C   . THR B 1 624 ? -4.987  20.230  57.157  1.00 81.42  ?  874  THR B C   1 
ATOM   4370 O O   . THR B 1 624 ? -5.533  19.166  56.845  1.00 81.16  ?  874  THR B O   1 
ATOM   4371 C CB  . THR B 1 624 ? -3.370  21.276  58.747  1.00 78.67  ?  874  THR B CB  1 
ATOM   4372 O OG1 . THR B 1 624 ? -3.586  22.595  58.230  1.00 84.54  ?  874  THR B OG1 1 
ATOM   4373 C CG2 . THR B 1 624 ? -1.978  21.194  59.357  1.00 63.84  ?  874  THR B CG2 1 
ATOM   4374 N N   . THR B 1 625 ? -5.617  21.405  57.103  1.00 73.93  ?  875  THR B N   1 
ATOM   4375 C CA  . THR B 1 625 ? -7.035  21.483  56.769  1.00 84.51  ?  875  THR B CA  1 
ATOM   4376 C C   . THR B 1 625 ? -7.265  21.352  55.268  1.00 85.44  ?  875  THR B C   1 
ATOM   4377 O O   . THR B 1 625 ? -8.098  20.552  54.828  1.00 91.36  ?  875  THR B O   1 
ATOM   4378 C CB  . THR B 1 625 ? -7.623  22.799  57.284  1.00 97.41  ?  875  THR B CB  1 
ATOM   4379 O OG1 . THR B 1 625 ? -7.170  23.881  56.462  1.00 93.71  ?  875  THR B OG1 1 
ATOM   4380 C CG2 . THR B 1 625 ? -7.185  23.048  58.720  1.00 79.30  ?  875  THR B CG2 1 
ATOM   4381 N N   . THR B 1 626 ? -6.546  22.137  54.468  1.00 91.84  ?  876  THR B N   1 
ATOM   4382 C CA  . THR B 1 626 ? -6.659  22.108  53.014  1.00 90.52  ?  876  THR B CA  1 
ATOM   4383 C C   . THR B 1 626 ? -5.401  21.454  52.456  1.00 93.35  ?  876  THR B C   1 
ATOM   4384 O O   . THR B 1 626 ? -4.318  22.048  52.493  1.00 99.98  ?  876  THR B O   1 
ATOM   4385 C CB  . THR B 1 626 ? -6.842  23.513  52.445  1.00 104.06 ?  876  THR B CB  1 
ATOM   4386 O OG1 . THR B 1 626 ? -5.597  24.220  52.500  1.00 102.63 ?  876  THR B OG1 1 
ATOM   4387 C CG2 . THR B 1 626 ? -7.885  24.278  53.247  1.00 97.58  ?  876  THR B CG2 1 
ATOM   4388 N N   . CYS B 1 627 ? -5.547  20.239  51.937  1.00 84.99  ?  877  CYS B N   1 
ATOM   4389 C CA  . CYS B 1 627 ? -4.429  19.442  51.453  1.00 71.69  ?  877  CYS B CA  1 
ATOM   4390 C C   . CYS B 1 627 ? -4.545  19.270  49.944  1.00 62.66  ?  877  CYS B C   1 
ATOM   4391 O O   . CYS B 1 627 ? -5.589  18.838  49.444  1.00 64.09  ?  877  CYS B O   1 
ATOM   4392 C CB  . CYS B 1 627 ? -4.405  18.079  52.146  1.00 72.15  ?  877  CYS B CB  1 
ATOM   4393 S SG  . CYS B 1 627 ? -2.767  17.384  52.425  1.00 118.53 ?  877  CYS B SG  1 
ATOM   4394 N N   . GLN B 1 628 ? -3.476  19.607  49.226  1.00 63.49  ?  878  GLN B N   1 
ATOM   4395 C CA  . GLN B 1 628 ? -3.463  19.569  47.771  1.00 63.09  ?  878  GLN B CA  1 
ATOM   4396 C C   . GLN B 1 628 ? -2.306  18.704  47.287  1.00 61.91  ?  878  GLN B C   1 
ATOM   4397 O O   . GLN B 1 628 ? -1.244  18.657  47.913  1.00 60.24  ?  878  GLN B O   1 
ATOM   4398 C CB  . GLN B 1 628 ? -3.347  20.982  47.181  1.00 64.23  ?  878  GLN B CB  1 
ATOM   4399 C CG  . GLN B 1 628 ? -4.300  21.989  47.807  1.00 70.56  ?  878  GLN B CG  1 
ATOM   4400 C CD  . GLN B 1 628 ? -5.296  22.549  46.814  1.00 85.10  ?  878  GLN B CD  1 
ATOM   4401 O OE1 . GLN B 1 628 ? -4.929  22.949  45.710  1.00 94.17  ?  878  GLN B OE1 1 
ATOM   4402 N NE2 . GLN B 1 628 ? -6.566  22.578  47.201  1.00 96.88  ?  878  GLN B NE2 1 
ATOM   4403 N N   . PHE B 1 629 ? -2.523  18.021  46.164  1.00 61.45  ?  879  PHE B N   1 
ATOM   4404 C CA  . PHE B 1 629 ? -1.504  17.143  45.602  1.00 57.88  ?  879  PHE B CA  1 
ATOM   4405 C C   . PHE B 1 629 ? -0.271  17.946  45.213  1.00 55.66  ?  879  PHE B C   1 
ATOM   4406 O O   . PHE B 1 629 ? -0.329  18.811  44.334  1.00 64.76  ?  879  PHE B O   1 
ATOM   4407 C CB  . PHE B 1 629 ? -2.066  16.394  44.394  1.00 53.24  ?  879  PHE B CB  1 
ATOM   4408 C CG  . PHE B 1 629 ? -1.134  15.362  43.832  1.00 54.59  ?  879  PHE B CG  1 
ATOM   4409 C CD1 . PHE B 1 629 ? -0.703  14.305  44.617  1.00 53.52  ?  879  PHE B CD1 1 
ATOM   4410 C CD2 . PHE B 1 629 ? -0.695  15.439  42.521  1.00 52.32  ?  879  PHE B CD2 1 
ATOM   4411 C CE1 . PHE B 1 629 ? 0.156   13.351  44.109  1.00 55.58  ?  879  PHE B CE1 1 
ATOM   4412 C CE2 . PHE B 1 629 ? 0.165   14.486  42.006  1.00 57.60  ?  879  PHE B CE2 1 
ATOM   4413 C CZ  . PHE B 1 629 ? 0.589   13.440  42.802  1.00 57.89  ?  879  PHE B CZ  1 
ATOM   4414 N N   . GLY B 1 630 ? 0.849   17.657  45.872  1.00 58.61  ?  880  GLY B N   1 
ATOM   4415 C CA  . GLY B 1 630 ? 2.078   18.418  45.722  1.00 53.79  ?  880  GLY B CA  1 
ATOM   4416 C C   . GLY B 1 630 ? 2.517   19.140  46.979  1.00 54.40  ?  880  GLY B C   1 
ATOM   4417 O O   . GLY B 1 630 ? 3.689   19.526  47.083  1.00 66.56  ?  880  GLY B O   1 
ATOM   4418 N N   . ASP B 1 631 ? 1.614   19.333  47.942  1.00 54.76  ?  881  ASP B N   1 
ATOM   4419 C CA  . ASP B 1 631 ? 1.951   19.992  49.194  1.00 59.17  ?  881  ASP B CA  1 
ATOM   4420 C C   . ASP B 1 631 ? 2.742   19.054  50.104  1.00 62.35  ?  881  ASP B C   1 
ATOM   4421 O O   . ASP B 1 631 ? 2.628   17.830  49.996  1.00 54.99  ?  881  ASP B O   1 
ATOM   4422 C CB  . ASP B 1 631 ? 0.685   20.448  49.913  1.00 64.08  ?  881  ASP B CB  1 
ATOM   4423 C CG  . ASP B 1 631 ? -0.038  21.552  49.173  1.00 73.52  ?  881  ASP B CG  1 
ATOM   4424 O OD1 . ASP B 1 631 ? 0.543   22.099  48.213  1.00 67.24  ?  881  ASP B OD1 1 
ATOM   4425 O OD2 . ASP B 1 631 ? -1.185  21.872  49.550  1.00 77.88  -1 881  ASP B OD2 1 
ATOM   4426 N N   . PRO B 1 632 ? 3.565   19.608  51.002  1.00 63.34  ?  882  PRO B N   1 
ATOM   4427 C CA  . PRO B 1 632 ? 4.212   18.772  52.022  1.00 59.86  ?  882  PRO B CA  1 
ATOM   4428 C C   . PRO B 1 632 ? 3.186   18.097  52.919  1.00 67.44  ?  882  PRO B C   1 
ATOM   4429 O O   . PRO B 1 632 ? 2.486   18.767  53.685  1.00 65.42  ?  882  PRO B O   1 
ATOM   4430 C CB  . PRO B 1 632 ? 5.078   19.771  52.802  1.00 64.82  ?  882  PRO B CB  1 
ATOM   4431 C CG  . PRO B 1 632 ? 5.292   20.908  51.854  1.00 62.12  ?  882  PRO B CG  1 
ATOM   4432 C CD  . PRO B 1 632 ? 4.033   21.004  51.050  1.00 58.36  ?  882  PRO B CD  1 
ATOM   4433 N N   . GLY B 1 633 ? 3.083   16.774  52.824  1.00 62.12  ?  883  GLY B N   1 
ATOM   4434 C CA  . GLY B 1 633 ? 2.067   16.040  53.548  1.00 55.17  ?  883  GLY B CA  1 
ATOM   4435 C C   . GLY B 1 633 ? 0.781   15.813  52.792  1.00 57.27  ?  883  GLY B C   1 
ATOM   4436 O O   . GLY B 1 633 ? -0.267  15.639  53.425  1.00 61.18  ?  883  GLY B O   1 
ATOM   4437 N N   . ASP B 1 634 ? 0.823   15.806  51.457  1.00 53.12  ?  884  ASP B N   1 
ATOM   4438 C CA  . ASP B 1 634 ? -0.400  15.656  50.675  1.00 55.18  ?  884  ASP B CA  1 
ATOM   4439 C C   . ASP B 1 634 ? -1.061  14.307  50.932  1.00 65.61  ?  884  ASP B C   1 
ATOM   4440 O O   . ASP B 1 634 ? -2.258  14.237  51.233  1.00 61.02  ?  884  ASP B O   1 
ATOM   4441 C CB  . ASP B 1 634 ? -0.098  15.846  49.187  1.00 56.01  ?  884  ASP B CB  1 
ATOM   4442 C CG  . ASP B 1 634 ? 1.192   15.177  48.763  1.00 59.10  ?  884  ASP B CG  1 
ATOM   4443 O OD1 . ASP B 1 634 ? 1.784   14.446  49.584  1.00 58.55  ?  884  ASP B OD1 1 
ATOM   4444 O OD2 . ASP B 1 634 ? 1.620   15.391  47.609  1.00 56.82  -1 884  ASP B OD2 1 
ATOM   4445 N N   . ILE B 1 635 ? -0.294  13.225  50.833  1.00 56.84  ?  885  ILE B N   1 
ATOM   4446 C CA  . ILE B 1 635 ? -0.798  11.872  51.036  1.00 58.17  ?  885  ILE B CA  1 
ATOM   4447 C C   . ILE B 1 635 ? -0.235  11.354  52.351  1.00 53.91  ?  885  ILE B C   1 
ATOM   4448 O O   . ILE B 1 635 ? 0.987   11.246  52.511  1.00 62.95  ?  885  ILE B O   1 
ATOM   4449 C CB  . ILE B 1 635 ? -0.421  10.948  49.869  1.00 54.59  ?  885  ILE B CB  1 
ATOM   4450 C CG1 . ILE B 1 635 ? -0.655  11.658  48.534  1.00 58.74  ?  885  ILE B CG1 1 
ATOM   4451 C CG2 . ILE B 1 635 ? -1.228  9.666   49.926  1.00 51.70  ?  885  ILE B CG2 1 
ATOM   4452 C CD1 . ILE B 1 635 ? -0.228  10.850  47.328  1.00 50.97  ?  885  ILE B CD1 1 
ATOM   4453 N N   . MET B 1 636 ? -1.122  11.032  53.291  1.00 55.22  ?  886  MET B N   1 
ATOM   4454 C CA  . MET B 1 636 ? -0.731  10.552  54.609  1.00 57.44  ?  886  MET B CA  1 
ATOM   4455 C C   . MET B 1 636 ? -1.416  9.226   54.902  1.00 59.27  ?  886  MET B C   1 
ATOM   4456 O O   . MET B 1 636 ? -2.613  9.064   54.644  1.00 60.46  ?  886  MET B O   1 
ATOM   4457 C CB  . MET B 1 636 ? -1.083  11.571  55.700  1.00 53.90  ?  886  MET B CB  1 
ATOM   4458 C CG  . MET B 1 636 ? -0.379  12.908  55.553  1.00 54.37  ?  886  MET B CG  1 
ATOM   4459 S SD  . MET B 1 636 ? 1.414   12.775  55.691  1.00 74.51  ?  886  MET B SD  1 
ATOM   4460 C CE  . MET B 1 636 ? 1.590   12.217  57.383  1.00 60.44  ?  886  MET B CE  1 
ATOM   4461 N N   . SER B 1 637 ? -0.650  8.283   55.447  1.00 59.76  ?  887  SER B N   1 
ATOM   4462 C CA  . SER B 1 637 ? -1.163  6.979   55.853  1.00 67.14  ?  887  SER B CA  1 
ATOM   4463 C C   . SER B 1 637 ? -1.297  6.966   57.372  1.00 63.14  ?  887  SER B C   1 
ATOM   4464 O O   . SER B 1 637 ? -0.296  6.877   58.090  1.00 61.67  ?  887  SER B O   1 
ATOM   4465 C CB  . SER B 1 637 ? -0.242  5.859   55.373  1.00 67.70  ?  887  SER B CB  1 
ATOM   4466 O OG  . SER B 1 637 ? -0.767  4.588   55.716  1.00 67.37  ?  887  SER B OG  1 
ATOM   4467 N N   . THR B 1 638 ? -2.529  7.054   57.855  1.00 68.70  ?  888  THR B N   1 
ATOM   4468 C CA  . THR B 1 638 ? -2.832  7.132   59.275  1.00 82.07  ?  888  THR B CA  1 
ATOM   4469 C C   . THR B 1 638 ? -3.362  5.800   59.787  1.00 83.80  ?  888  THR B C   1 
ATOM   4470 O O   . THR B 1 638 ? -3.795  4.949   59.004  1.00 78.66  ?  888  THR B O   1 
ATOM   4471 C CB  . THR B 1 638 ? -3.865  8.236   59.533  1.00 79.12  ?  888  THR B CB  1 
ATOM   4472 O OG1 . THR B 1 638 ? -5.120  7.867   58.948  1.00 77.51  ?  888  THR B OG1 1 
ATOM   4473 C CG2 . THR B 1 638 ? -3.397  9.550   58.927  1.00 68.60  ?  888  THR B CG2 1 
ATOM   4474 N N   . PRO B 1 639 ? -3.326  5.576   61.107  1.00 86.04  ?  889  PRO B N   1 
ATOM   4475 C CA  . PRO B 1 639 ? -3.921  4.340   61.645  1.00 83.21  ?  889  PRO B CA  1 
ATOM   4476 C C   . PRO B 1 639 ? -5.393  4.182   61.307  1.00 88.29  ?  889  PRO B C   1 
ATOM   4477 O O   . PRO B 1 639 ? -5.854  3.056   61.080  1.00 96.13  ?  889  PRO B O   1 
ATOM   4478 C CB  . PRO B 1 639 ? -3.696  4.478   63.157  1.00 85.84  ?  889  PRO B CB  1 
ATOM   4479 C CG  . PRO B 1 639 ? -2.497  5.351   63.275  1.00 93.39  ?  889  PRO B CG  1 
ATOM   4480 C CD  . PRO B 1 639 ? -2.594  6.330   62.140  1.00 84.01  ?  889  PRO B CD  1 
ATOM   4481 N N   . VAL B 1 640 ? -6.149  5.282   61.267  1.00 93.03  ?  890  VAL B N   1 
ATOM   4482 C CA  . VAL B 1 640 ? -7.560  5.195   60.904  1.00 85.64  ?  890  VAL B CA  1 
ATOM   4483 C C   . VAL B 1 640 ? -7.712  4.841   59.430  1.00 88.73  ?  890  VAL B C   1 
ATOM   4484 O O   . VAL B 1 640 ? -8.663  4.148   59.045  1.00 92.59  ?  890  VAL B O   1 
ATOM   4485 C CB  . VAL B 1 640 ? -8.286  6.509   61.264  1.00 84.75  ?  890  VAL B CB  1 
ATOM   4486 C CG1 . VAL B 1 640 ? -7.303  7.524   61.833  1.00 85.97  ?  890  VAL B CG1 1 
ATOM   4487 C CG2 . VAL B 1 640 ? -9.023  7.089   60.059  1.00 82.12  ?  890  VAL B CG2 1 
ATOM   4488 N N   . GLY B 1 641 ? -6.782  5.279   58.591  1.00 87.59  ?  891  GLY B N   1 
ATOM   4489 C CA  . GLY B 1 641 ? -6.851  4.972   57.175  1.00 73.99  ?  891  GLY B CA  1 
ATOM   4490 C C   . GLY B 1 641 ? -6.003  5.946   56.375  1.00 71.63  ?  891  GLY B C   1 
ATOM   4491 O O   . GLY B 1 641 ? -5.069  6.552   56.896  1.00 71.31  ?  891  GLY B O   1 
ATOM   4492 N N   . MET B 1 642 ? -6.362  6.076   55.101  1.00 66.01  ?  892  MET B N   1 
ATOM   4493 C CA  . MET B 1 642 ? -5.633  6.917   54.162  1.00 62.33  ?  892  MET B CA  1 
ATOM   4494 C C   . MET B 1 642 ? -6.258  8.308   54.133  1.00 66.84  ?  892  MET B C   1 
ATOM   4495 O O   . MET B 1 642 ? -7.448  8.451   53.832  1.00 81.88  ?  892  MET B O   1 
ATOM   4496 C CB  . MET B 1 642 ? -5.652  6.293   52.768  1.00 69.26  ?  892  MET B CB  1 
ATOM   4497 C CG  . MET B 1 642 ? -4.616  6.850   51.811  1.00 64.74  ?  892  MET B CG  1 
ATOM   4498 S SD  . MET B 1 642 ? -3.154  5.803   51.714  1.00 75.56  ?  892  MET B SD  1 
ATOM   4499 C CE  . MET B 1 642 ? -1.895  6.949   52.249  1.00 66.86  ?  892  MET B CE  1 
ATOM   4500 N N   . LYS B 1 643 ? -5.461  9.325   54.449  1.00 66.93  ?  893  LYS B N   1 
ATOM   4501 C CA  . LYS B 1 643 ? -5.876  10.716  54.327  1.00 71.98  ?  893  LYS B CA  1 
ATOM   4502 C C   . LYS B 1 643 ? -5.306  11.267  53.026  1.00 64.50  ?  893  LYS B C   1 
ATOM   4503 O O   . LYS B 1 643 ? -4.089  11.228  52.812  1.00 68.32  ?  893  LYS B O   1 
ATOM   4504 C CB  . LYS B 1 643 ? -5.405  11.545  55.522  1.00 72.50  ?  893  LYS B CB  1 
ATOM   4505 C CG  . LYS B 1 643 ? -5.937  12.971  55.528  1.00 79.11  ?  893  LYS B CG  1 
ATOM   4506 C CD  . LYS B 1 643 ? -7.457  12.995  55.601  1.00 90.04  ?  893  LYS B CD  1 
ATOM   4507 C CE  . LYS B 1 643 ? -7.955  12.600  56.984  1.00 107.05 ?  893  LYS B CE  1 
ATOM   4508 N NZ  . LYS B 1 643 ? -7.628  13.635  58.005  1.00 112.20 1  893  LYS B NZ  1 
ATOM   4509 N N   . CYS B 1 644 ? -6.179  11.782  52.166  1.00 58.51  ?  894  CYS B N   1 
ATOM   4510 C CA  . CYS B 1 644 ? -5.768  12.091  50.810  1.00 65.01  ?  894  CYS B CA  1 
ATOM   4511 C C   . CYS B 1 644 ? -5.996  13.556  50.468  1.00 64.97  ?  894  CYS B C   1 
ATOM   4512 O O   . CYS B 1 644 ? -6.887  14.203  51.027  1.00 67.34  ?  894  CYS B O   1 
ATOM   4513 C CB  . CYS B 1 644 ? -6.527  11.219  49.810  1.00 72.08  ?  894  CYS B CB  1 
ATOM   4514 S SG  . CYS B 1 644 ? -6.011  9.517   49.846  1.00 80.92  ?  894  CYS B SG  1 
ATOM   4515 N N   . PRO B 1 645 ? -5.214  14.099  49.539  1.00 66.78  ?  895  PRO B N   1 
ATOM   4516 C CA  . PRO B 1 645 ? -5.361  15.504  49.164  1.00 70.90  ?  895  PRO B CA  1 
ATOM   4517 C C   . PRO B 1 645 ? -6.343  15.685  48.016  1.00 59.20  ?  895  PRO B C   1 
ATOM   4518 O O   . PRO B 1 645 ? -6.712  14.743  47.312  1.00 69.40  ?  895  PRO B O   1 
ATOM   4519 C CB  . PRO B 1 645 ? -3.941  15.877  48.720  1.00 62.00  ?  895  PRO B CB  1 
ATOM   4520 C CG  . PRO B 1 645 ? -3.452  14.615  48.068  1.00 66.05  ?  895  PRO B CG  1 
ATOM   4521 C CD  . PRO B 1 645 ? -4.089  13.463  48.827  1.00 61.45  ?  895  PRO B CD  1 
ATOM   4522 N N   . GLU B 1 646 ? -6.765  16.932  47.841  1.00 70.64  ?  896  GLU B N   1 
ATOM   4523 C CA  . GLU B 1 646 ? -7.498  17.292  46.639  1.00 65.79  ?  896  GLU B CA  1 
ATOM   4524 C C   . GLU B 1 646 ? -6.546  17.329  45.453  1.00 60.55  ?  896  GLU B C   1 
ATOM   4525 O O   . GLU B 1 646 ? -5.418  17.818  45.555  1.00 66.85  ?  896  GLU B O   1 
ATOM   4526 C CB  . GLU B 1 646 ? -8.187  18.645  46.809  1.00 72.11  ?  896  GLU B CB  1 
ATOM   4527 C CG  . GLU B 1 646 ? -9.548  18.557  47.475  1.00 95.69  ?  896  GLU B CG  1 
ATOM   4528 C CD  . GLU B 1 646 ? -10.421 17.479  46.859  1.00 108.27 ?  896  GLU B CD  1 
ATOM   4529 O OE1 . GLU B 1 646 ? -11.125 16.777  47.617  1.00 109.25 ?  896  GLU B OE1 1 
ATOM   4530 O OE2 . GLU B 1 646 ? -10.395 17.327  45.619  1.00 109.50 -1 896  GLU B OE2 1 
ATOM   4531 N N   . LEU B 1 647 ? -6.999  16.788  44.325  1.00 65.34  ?  897  LEU B N   1 
ATOM   4532 C CA  . LEU B 1 647 ? -6.209  16.790  43.096  1.00 78.16  ?  897  LEU B CA  1 
ATOM   4533 C C   . LEU B 1 647 ? -6.499  18.095  42.367  1.00 66.22  ?  897  LEU B C   1 
ATOM   4534 O O   . LEU B 1 647 ? -7.377  18.175  41.507  1.00 76.82  ?  897  LEU B O   1 
ATOM   4535 C CB  . LEU B 1 647 ? -6.527  15.564  42.250  1.00 62.79  ?  897  LEU B CB  1 
ATOM   4536 C CG  . LEU B 1 647 ? -6.015  14.262  42.872  1.00 57.06  ?  897  LEU B CG  1 
ATOM   4537 C CD1 . LEU B 1 647 ? -6.641  13.049  42.206  1.00 63.97  ?  897  LEU B CD1 1 
ATOM   4538 C CD2 . LEU B 1 647 ? -4.496  14.194  42.790  1.00 60.55  ?  897  LEU B CD2 1 
ATOM   4539 N N   . SER B 1 648 ? -5.747  19.132  42.732  1.00 63.40  ?  898  SER B N   1 
ATOM   4540 C CA  . SER B 1 648 ? -5.976  20.466  42.193  1.00 73.63  ?  898  SER B CA  1 
ATOM   4541 C C   . SER B 1 648 ? -5.788  20.480  40.683  1.00 71.82  ?  898  SER B C   1 
ATOM   4542 O O   . SER B 1 648 ? -4.807  19.944  40.158  1.00 78.27  ?  898  SER B O   1 
ATOM   4543 C CB  . SER B 1 648 ? -5.031  21.468  42.857  1.00 73.08  ?  898  SER B CB  1 
ATOM   4544 O OG  . SER B 1 648 ? -3.691  21.004  42.839  1.00 93.24  ?  898  SER B OG  1 
ATOM   4545 N N   . GLY B 1 649 ? -6.735  21.093  39.988  1.00 71.44  ?  899  GLY B N   1 
ATOM   4546 C CA  . GLY B 1 649 ? -6.717  21.181  38.548  1.00 59.33  ?  899  GLY B CA  1 
ATOM   4547 C C   . GLY B 1 649 ? -8.114  21.022  37.996  1.00 63.21  ?  899  GLY B C   1 
ATOM   4548 O O   . GLY B 1 649 ? -9.101  21.154  38.718  1.00 76.05  ?  899  GLY B O   1 
ATOM   4549 N N   . SER B 1 650 ? -8.188  20.735  36.699  1.00 65.69  ?  900  SER B N   1 
ATOM   4550 C CA  . SER B 1 650 ? -9.467  20.553  36.031  1.00 67.12  ?  900  SER B CA  1 
ATOM   4551 C C   . SER B 1 650 ? -9.289  19.605  34.855  1.00 60.30  ?  900  SER B C   1 
ATOM   4552 O O   . SER B 1 650 ? -8.180  19.408  34.351  1.00 63.57  ?  900  SER B O   1 
ATOM   4553 C CB  . SER B 1 650 ? -10.049 21.886  35.549  1.00 63.15  ?  900  SER B CB  1 
ATOM   4554 O OG  . SER B 1 650 ? -9.296  22.417  34.473  1.00 78.45  ?  900  SER B OG  1 
ATOM   4555 N N   . PHE B 1 651 ? -10.402 19.024  34.421  1.00 66.32  ?  901  PHE B N   1 
ATOM   4556 C CA  . PHE B 1 651 ? -10.421 18.120  33.283  1.00 59.71  ?  901  PHE B CA  1 
ATOM   4557 C C   . PHE B 1 651 ? -10.811 18.867  32.015  1.00 69.84  ?  901  PHE B C   1 
ATOM   4558 O O   . PHE B 1 651 ? -11.541 19.862  32.053  1.00 69.33  ?  901  PHE B O   1 
ATOM   4559 C CB  . PHE B 1 651 ? -11.393 16.960  33.517  1.00 59.60  ?  901  PHE B CB  1 
ATOM   4560 C CG  . PHE B 1 651 ? -10.918 15.963  34.535  1.00 58.46  ?  901  PHE B CG  1 
ATOM   4561 C CD1 . PHE B 1 651 ? -9.885  15.090  34.238  1.00 57.29  ?  901  PHE B CD1 1 
ATOM   4562 C CD2 . PHE B 1 651 ? -11.512 15.889  35.783  1.00 58.76  ?  901  PHE B CD2 1 
ATOM   4563 C CE1 . PHE B 1 651 ? -9.447  14.168  35.171  1.00 59.48  ?  901  PHE B CE1 1 
ATOM   4564 C CE2 . PHE B 1 651 ? -11.079 14.968  36.720  1.00 57.86  ?  901  PHE B CE2 1 
ATOM   4565 C CZ  . PHE B 1 651 ? -10.046 14.107  36.413  1.00 56.69  ?  901  PHE B CZ  1 
ATOM   4566 N N   . ARG B 1 652 ? -10.311 18.372  30.885  1.00 66.30  ?  902  ARG B N   1 
ATOM   4567 C CA  . ARG B 1 652 ? -10.636 18.906  29.568  1.00 67.12  ?  902  ARG B CA  1 
ATOM   4568 C C   . ARG B 1 652 ? -10.943 17.739  28.643  1.00 67.17  ?  902  ARG B C   1 
ATOM   4569 O O   . ARG B 1 652 ? -10.091 16.869  28.435  1.00 67.98  ?  902  ARG B O   1 
ATOM   4570 C CB  . ARG B 1 652 ? -9.488  19.753  29.013  1.00 63.73  ?  902  ARG B CB  1 
ATOM   4571 C CG  . ARG B 1 652 ? -9.679  21.247  29.203  1.00 70.59  ?  902  ARG B CG  1 
ATOM   4572 C CD  . ARG B 1 652 ? -8.396  22.026  28.948  1.00 63.35  ?  902  ARG B CD  1 
ATOM   4573 N NE  . ARG B 1 652 ? -7.688  21.578  27.752  1.00 67.38  ?  902  ARG B NE  1 
ATOM   4574 C CZ  . ARG B 1 652 ? -6.550  20.891  27.771  1.00 65.90  ?  902  ARG B CZ  1 
ATOM   4575 N NH1 . ARG B 1 652 ? -5.984  20.573  28.927  1.00 60.89  1  902  ARG B NH1 1 
ATOM   4576 N NH2 . ARG B 1 652 ? -5.975  20.523  26.634  1.00 82.15  ?  902  ARG B NH2 1 
ATOM   4577 N N   . LYS B 1 653 ? -12.157 17.717  28.100  1.00 67.32  ?  903  LYS B N   1 
ATOM   4578 C CA  . LYS B 1 653 ? -12.590 16.639  27.218  1.00 74.46  ?  903  LYS B CA  1 
ATOM   4579 C C   . LYS B 1 653 ? -12.057 16.906  25.816  1.00 75.93  ?  903  LYS B C   1 
ATOM   4580 O O   . LYS B 1 653 ? -12.518 17.828  25.133  1.00 85.54  ?  903  LYS B O   1 
ATOM   4581 C CB  . LYS B 1 653 ? -14.112 16.533  27.216  1.00 79.25  ?  903  LYS B CB  1 
ATOM   4582 C CG  . LYS B 1 653 ? -14.639 15.141  26.921  1.00 65.79  ?  903  LYS B CG  1 
ATOM   4583 C CD  . LYS B 1 653 ? -15.982 15.191  26.209  1.00 76.38  ?  903  LYS B CD  1 
ATOM   4584 C CE  . LYS B 1 653 ? -16.937 16.168  26.867  1.00 67.26  ?  903  LYS B CE  1 
ATOM   4585 N NZ  . LYS B 1 653 ? -18.242 16.224  26.155  1.00 67.57  1  903  LYS B NZ  1 
ATOM   4586 N N   . LYS B 1 654 ? -11.090 16.107  25.384  1.00 72.91  ?  904  LYS B N   1 
ATOM   4587 C CA  . LYS B 1 654 ? -10.477 16.243  24.071  1.00 84.21  ?  904  LYS B CA  1 
ATOM   4588 C C   . LYS B 1 654 ? -10.873 15.066  23.186  1.00 81.46  ?  904  LYS B C   1 
ATOM   4589 O O   . LYS B 1 654 ? -11.579 14.144  23.606  1.00 75.96  ?  904  LYS B O   1 
ATOM   4590 C CB  . LYS B 1 654 ? -8.955  16.352  24.195  1.00 72.76  ?  904  LYS B CB  1 
ATOM   4591 C CG  . LYS B 1 654 ? -8.459  17.619  24.885  1.00 72.82  ?  904  LYS B CG  1 
ATOM   4592 C CD  . LYS B 1 654 ? -8.019  18.687  23.884  1.00 80.47  ?  904  LYS B CD  1 
ATOM   4593 C CE  . LYS B 1 654 ? -9.200  19.426  23.272  1.00 77.78  ?  904  LYS B CE  1 
ATOM   4594 N NZ  . LYS B 1 654 ? -8.759  20.498  22.337  1.00 68.03  1  904  LYS B NZ  1 
ATOM   4595 N N   . CYS B 1 655 ? -10.404 15.105  21.941  1.00 79.21  ?  905  CYS B N   1 
ATOM   4596 C CA  . CYS B 1 655 ? -10.686 14.063  20.962  1.00 65.34  ?  905  CYS B CA  1 
ATOM   4597 C C   . CYS B 1 655 ? -9.390  13.690  20.261  1.00 75.23  ?  905  CYS B C   1 
ATOM   4598 O O   . CYS B 1 655 ? -8.716  14.558  19.696  1.00 85.05  ?  905  CYS B O   1 
ATOM   4599 C CB  . CYS B 1 655 ? -11.732 14.526  19.946  1.00 69.69  ?  905  CYS B CB  1 
ATOM   4600 S SG  . CYS B 1 655 ? -12.256 13.236  18.798  1.00 84.07  ?  905  CYS B SG  1 
ATOM   4601 N N   . ALA B 1 656 ? -9.046  12.406  20.295  1.00 79.20  ?  906  ALA B N   1 
ATOM   4602 C CA  . ALA B 1 656 ? -7.835  11.901  19.663  1.00 76.27  ?  906  ALA B CA  1 
ATOM   4603 C C   . ALA B 1 656 ? -8.197  11.170  18.377  1.00 85.48  ?  906  ALA B C   1 
ATOM   4604 O O   . ALA B 1 656 ? -9.092  10.318  18.373  1.00 81.48  ?  906  ALA B O   1 
ATOM   4605 C CB  . ALA B 1 656 ? -7.072  10.970  20.606  1.00 70.76  ?  906  ALA B CB  1 
ATOM   4606 N N   . PHE B 1 657 ? -7.505  11.516  17.291  1.00 81.78  ?  907  PHE B N   1 
ATOM   4607 C CA  . PHE B 1 657 ? -7.682  10.897  15.977  1.00 84.51  ?  907  PHE B CA  1 
ATOM   4608 C C   . PHE B 1 657 ? -9.108  11.033  15.453  1.00 84.63  ?  907  PHE B C   1 
ATOM   4609 O O   . PHE B 1 657 ? -9.539  10.233  14.615  1.00 90.66  ?  907  PHE B O   1 
ATOM   4610 C CB  . PHE B 1 657 ? -7.272  9.419   15.999  1.00 80.46  ?  907  PHE B CB  1 
ATOM   4611 C CG  . PHE B 1 657 ? -6.028  9.147   16.793  1.00 83.45  ?  907  PHE B CG  1 
ATOM   4612 C CD1 . PHE B 1 657 ? -6.095  8.460   17.995  1.00 84.21  ?  907  PHE B CD1 1 
ATOM   4613 C CD2 . PHE B 1 657 ? -4.794  9.585   16.345  1.00 90.45  ?  907  PHE B CD2 1 
ATOM   4614 C CE1 . PHE B 1 657 ? -4.953  8.209   18.730  1.00 87.97  ?  907  PHE B CE1 1 
ATOM   4615 C CE2 . PHE B 1 657 ? -3.647  9.339   17.076  1.00 96.36  ?  907  PHE B CE2 1 
ATOM   4616 C CZ  . PHE B 1 657 ? -3.727  8.649   18.270  1.00 92.92  ?  907  PHE B CZ  1 
ATOM   4617 N N   . ALA B 1 658 ? -9.848  12.035  15.936  1.00 82.83  ?  908  ALA B N   1 
ATOM   4618 C CA  . ALA B 1 658 ? -11.243 12.262  15.550  1.00 80.94  ?  908  ALA B CA  1 
ATOM   4619 C C   . ALA B 1 658 ? -12.108 11.027  15.787  1.00 83.52  ?  908  ALA B C   1 
ATOM   4620 O O   . ALA B 1 658 ? -13.126 10.831  15.117  1.00 79.41  ?  908  ALA B O   1 
ATOM   4621 C CB  . ALA B 1 658 ? -11.351 12.721  14.093  1.00 68.41  ?  908  ALA B CB  1 
ATOM   4622 N N   . THR B 1 659 ? -11.717 10.188  16.747  1.00 78.31  ?  909  THR B N   1 
ATOM   4623 C CA  . THR B 1 659 ? -12.406 8.924   16.971  1.00 81.64  ?  909  THR B CA  1 
ATOM   4624 C C   . THR B 1 659 ? -12.653 8.674   18.453  1.00 74.93  ?  909  THR B C   1 
ATOM   4625 O O   . THR B 1 659 ? -13.803 8.540   18.884  1.00 75.41  ?  909  THR B O   1 
ATOM   4626 C CB  . THR B 1 659 ? -11.600 7.764   16.378  1.00 84.40  ?  909  THR B CB  1 
ATOM   4627 O OG1 . THR B 1 659 ? -11.151 8.114   15.063  1.00 98.34  ?  909  THR B OG1 1 
ATOM   4628 C CG2 . THR B 1 659 ? -12.458 6.511   16.293  1.00 81.60  ?  909  THR B CG2 1 
ATOM   4629 N N   . THR B 1 660 ? -11.580 8.615   19.243  1.00 66.28  ?  910  THR B N   1 
ATOM   4630 C CA  . THR B 1 660 ? -11.681 8.181   20.632  1.00 76.82  ?  910  THR B CA  1 
ATOM   4631 C C   . THR B 1 660 ? -11.668 9.373   21.574  1.00 72.28  ?  910  THR B C   1 
ATOM   4632 O O   . THR B 1 660 ? -10.774 10.227  21.473  1.00 77.36  ?  910  THR B O   1 
ATOM   4633 C CB  . THR B 1 660 ? -10.532 7.238   20.980  1.00 70.99  ?  910  THR B CB  1 
ATOM   4634 O OG1 . THR B 1 660 ? -9.941  7.638   22.223  1.00 86.64  ?  910  THR B OG1 1 
ATOM   4635 C CG2 . THR B 1 660 ? -9.472  7.259   19.887  1.00 67.30  ?  910  THR B CG2 1 
ATOM   4636 N N   . PRO B 1 661 ? -12.631 9.468   22.490  1.00 73.71  ?  911  PRO B N   1 
ATOM   4637 C CA  . PRO B 1 661 ? -12.600 10.547  23.487  1.00 73.46  ?  911  PRO B CA  1 
ATOM   4638 C C   . PRO B 1 661 ? -11.497 10.311  24.509  1.00 69.48  ?  911  PRO B C   1 
ATOM   4639 O O   . PRO B 1 661 ? -11.398 9.233   25.100  1.00 62.32  ?  911  PRO B O   1 
ATOM   4640 C CB  . PRO B 1 661 ? -13.990 10.479  24.134  1.00 65.24  ?  911  PRO B CB  1 
ATOM   4641 C CG  . PRO B 1 661 ? -14.827 9.659   23.194  1.00 63.70  ?  911  PRO B CG  1 
ATOM   4642 C CD  . PRO B 1 661 ? -13.882 8.696   22.552  1.00 76.06  ?  911  PRO B CD  1 
ATOM   4643 N N   . VAL B 1 662 ? -10.659 11.327  24.707  1.00 71.53  ?  912  VAL B N   1 
ATOM   4644 C CA  . VAL B 1 662 ? -9.584  11.291  25.691  1.00 65.40  ?  912  VAL B CA  1 
ATOM   4645 C C   . VAL B 1 662 ? -9.655  12.565  26.520  1.00 70.79  ?  912  VAL B C   1 
ATOM   4646 O O   . VAL B 1 662 ? -9.988  13.636  26.001  1.00 69.50  ?  912  VAL B O   1 
ATOM   4647 C CB  . VAL B 1 662 ? -8.196  11.148  25.028  1.00 70.88  ?  912  VAL B CB  1 
ATOM   4648 C CG1 . VAL B 1 662 ? -7.122  10.906  26.080  1.00 73.20  ?  912  VAL B CG1 1 
ATOM   4649 C CG2 . VAL B 1 662 ? -8.200  10.023  24.004  1.00 87.21  ?  912  VAL B CG2 1 
ATOM   4650 N N   . CYS B 1 663 ? -9.347  12.448  27.807  1.00 65.26  ?  913  CYS B N   1 
ATOM   4651 C CA  . CYS B 1 663 ? -9.339  13.578  28.721  1.00 63.66  ?  913  CYS B CA  1 
ATOM   4652 C C   . CYS B 1 663 ? -7.912  14.005  29.032  1.00 69.80  ?  913  CYS B C   1 
ATOM   4653 O O   . CYS B 1 663 ? -6.988  13.186  29.052  1.00 76.34  ?  913  CYS B O   1 
ATOM   4654 C CB  . CYS B 1 663 ? -10.063 13.235  30.022  1.00 61.31  ?  913  CYS B CB  1 
ATOM   4655 S SG  . CYS B 1 663 ? -11.715 13.922  30.167  1.00 88.40  ?  913  CYS B SG  1 
ATOM   4656 N N   . GLN B 1 664 ? -7.745  15.301  29.276  1.00 61.54  ?  914  GLN B N   1 
ATOM   4657 C CA  . GLN B 1 664 ? -6.475  15.864  29.702  1.00 67.88  ?  914  GLN B CA  1 
ATOM   4658 C C   . GLN B 1 664 ? -6.689  16.654  30.984  1.00 60.86  ?  914  GLN B C   1 
ATOM   4659 O O   . GLN B 1 664 ? -7.813  17.031  31.327  1.00 59.97  ?  914  GLN B O   1 
ATOM   4660 C CB  . GLN B 1 664 ? -5.858  16.750  28.611  1.00 62.03  ?  914  GLN B CB  1 
ATOM   4661 C CG  . GLN B 1 664 ? -5.364  15.964  27.407  1.00 63.57  ?  914  GLN B CG  1 
ATOM   4662 C CD  . GLN B 1 664 ? -4.847  16.853  26.294  1.00 83.22  ?  914  GLN B CD  1 
ATOM   4663 O OE1 . GLN B 1 664 ? -5.118  18.054  26.264  1.00 81.82  ?  914  GLN B OE1 1 
ATOM   4664 N NE2 . GLN B 1 664 ? -4.096  16.265  25.369  1.00 83.56  ?  914  GLN B NE2 1 
ATOM   4665 N N   . PHE B 1 665 ? -5.593  16.898  31.698  1.00 56.73  ?  915  PHE B N   1 
ATOM   4666 C CA  . PHE B 1 665 ? -5.643  17.500  33.022  1.00 66.67  ?  915  PHE B CA  1 
ATOM   4667 C C   . PHE B 1 665 ? -4.703  18.695  33.076  1.00 57.42  ?  915  PHE B C   1 
ATOM   4668 O O   . PHE B 1 665 ? -3.542  18.596  32.667  1.00 57.00  ?  915  PHE B O   1 
ATOM   4669 C CB  . PHE B 1 665 ? -5.270  16.473  34.097  1.00 55.60  ?  915  PHE B CB  1 
ATOM   4670 C CG  . PHE B 1 665 ? -5.532  16.939  35.499  1.00 59.61  ?  915  PHE B CG  1 
ATOM   4671 C CD1 . PHE B 1 665 ? -6.799  16.843  36.050  1.00 59.07  ?  915  PHE B CD1 1 
ATOM   4672 C CD2 . PHE B 1 665 ? -4.509  17.463  36.271  1.00 62.10  ?  915  PHE B CD2 1 
ATOM   4673 C CE1 . PHE B 1 665 ? -7.042  17.267  37.341  1.00 61.51  ?  915  PHE B CE1 1 
ATOM   4674 C CE2 . PHE B 1 665 ? -4.745  17.889  37.564  1.00 64.64  ?  915  PHE B CE2 1 
ATOM   4675 C CZ  . PHE B 1 665 ? -6.013  17.789  38.100  1.00 62.16  ?  915  PHE B CZ  1 
ATOM   4676 N N   . ASP B 1 666 ? -5.209  19.818  33.580  1.00 62.00  ?  916  ASP B N   1 
ATOM   4677 C CA  . ASP B 1 666 ? -4.438  21.048  33.729  1.00 59.07  ?  916  ASP B CA  1 
ATOM   4678 C C   . ASP B 1 666 ? -4.202  21.285  35.215  1.00 58.83  ?  916  ASP B C   1 
ATOM   4679 O O   . ASP B 1 666 ? -5.121  21.682  35.938  1.00 59.42  ?  916  ASP B O   1 
ATOM   4680 C CB  . ASP B 1 666 ? -5.166  22.231  33.095  1.00 60.75  ?  916  ASP B CB  1 
ATOM   4681 C CG  . ASP B 1 666 ? -5.337  22.075  31.598  1.00 65.59  ?  916  ASP B CG  1 
ATOM   4682 O OD1 . ASP B 1 666 ? -4.413  21.546  30.945  1.00 68.00  ?  916  ASP B OD1 1 
ATOM   4683 O OD2 . ASP B 1 666 ? -6.398  22.478  31.076  1.00 73.32  -1 916  ASP B OD2 1 
ATOM   4684 N N   . GLY B 1 667 ? -2.980  21.044  35.663  1.00 59.31  ?  917  GLY B N   1 
ATOM   4685 C CA  . GLY B 1 667 ? -2.644  21.218  37.060  1.00 57.90  ?  917  GLY B CA  1 
ATOM   4686 C C   . GLY B 1 667 ? -1.378  20.457  37.401  1.00 58.87  ?  917  GLY B C   1 
ATOM   4687 O O   . GLY B 1 667 ? -0.652  19.993  36.522  1.00 61.65  ?  917  GLY B O   1 
ATOM   4688 N N   . ASN B 1 668 ? -1.138  20.338  38.703  1.00 56.40  ?  918  ASN B N   1 
ATOM   4689 C CA  . ASN B 1 668 ? 0.064   19.668  39.178  1.00 63.40  ?  918  ASN B CA  1 
ATOM   4690 C C   . ASN B 1 668 ? -0.066  18.157  39.023  1.00 60.85  ?  918  ASN B C   1 
ATOM   4691 O O   . ASN B 1 668 ? -1.101  17.572  39.359  1.00 54.02  ?  918  ASN B O   1 
ATOM   4692 C CB  . ASN B 1 668 ? 0.327   20.026  40.639  1.00 59.54  ?  918  ASN B CB  1 
ATOM   4693 C CG  . ASN B 1 668 ? 1.530   19.303  41.208  1.00 60.64  ?  918  ASN B CG  1 
ATOM   4694 O OD1 . ASN B 1 668 ? 2.494   19.021  40.495  1.00 66.08  ?  918  ASN B OD1 1 
ATOM   4695 N ND2 . ASN B 1 668 ? 1.478   18.992  42.496  1.00 70.08  ?  918  ASN B ND2 1 
ATOM   4696 N N   . THR B 1 669 ? 0.989   17.526  38.507  1.00 61.90  ?  919  THR B N   1 
ATOM   4697 C CA  . THR B 1 669 ? 1.054   16.074  38.393  1.00 58.47  ?  919  THR B CA  1 
ATOM   4698 C C   . THR B 1 669 ? 2.258   15.494  39.123  1.00 57.94  ?  919  THR B C   1 
ATOM   4699 O O   . THR B 1 669 ? 2.577   14.314  38.932  1.00 64.02  ?  919  THR B O   1 
ATOM   4700 C CB  . THR B 1 669 ? 1.086   15.646  36.922  1.00 53.25  ?  919  THR B CB  1 
ATOM   4701 O OG1 . THR B 1 669 ? 2.269   16.160  36.298  1.00 57.18  ?  919  THR B OG1 1 
ATOM   4702 C CG2 . THR B 1 669 ? -0.137  16.169  36.184  1.00 58.64  ?  919  THR B CG2 1 
ATOM   4703 N N   . ILE B 1 670 ? 2.935   16.288  39.948  1.00 56.06  ?  920  ILE B N   1 
ATOM   4704 C CA  . ILE B 1 670 ? 4.110   15.853  40.694  1.00 58.01  ?  920  ILE B CA  1 
ATOM   4705 C C   . ILE B 1 670 ? 3.736   15.779  42.167  1.00 62.25  ?  920  ILE B C   1 
ATOM   4706 O O   . ILE B 1 670 ? 3.180   16.735  42.721  1.00 67.72  ?  920  ILE B O   1 
ATOM   4707 C CB  . ILE B 1 670 ? 5.300   16.802  40.473  1.00 61.93  ?  920  ILE B CB  1 
ATOM   4708 C CG1 . ILE B 1 670 ? 5.447   17.135  38.987  1.00 66.55  ?  920  ILE B CG1 1 
ATOM   4709 C CG2 . ILE B 1 670 ? 6.580   16.176  40.998  1.00 55.82  ?  920  ILE B CG2 1 
ATOM   4710 C CD1 . ILE B 1 670 ? 6.501   18.185  38.696  1.00 55.39  ?  920  ILE B CD1 1 
ATOM   4711 N N   . SER B 1 671 ? 4.041   14.648  42.798  1.00 67.76  ?  921  SER B N   1 
ATOM   4712 C CA  . SER B 1 671 ? 3.676   14.441  44.190  1.00 55.62  ?  921  SER B CA  1 
ATOM   4713 C C   . SER B 1 671 ? 4.471   15.371  45.103  1.00 51.89  ?  921  SER B C   1 
ATOM   4714 O O   . SER B 1 671 ? 5.512   15.917  44.729  1.00 56.61  ?  921  SER B O   1 
ATOM   4715 C CB  . SER B 1 671 ? 3.910   12.986  44.598  1.00 61.97  ?  921  SER B CB  1 
ATOM   4716 O OG  . SER B 1 671 ? 5.290   12.664  44.570  1.00 60.93  ?  921  SER B OG  1 
ATOM   4717 N N   . GLY B 1 672 ? 3.960   15.542  46.324  1.00 52.63  ?  922  GLY B N   1 
ATOM   4718 C CA  . GLY B 1 672 ? 4.635   16.401  47.283  1.00 52.43  ?  922  GLY B CA  1 
ATOM   4719 C C   . GLY B 1 672 ? 6.023   15.907  47.640  1.00 58.71  ?  922  GLY B C   1 
ATOM   4720 O O   . GLY B 1 672 ? 6.941   16.705  47.850  1.00 63.63  ?  922  GLY B O   1 
ATOM   4721 N N   . TYR B 1 673 ? 6.198   14.585  47.715  1.00 51.70  ?  923  TYR B N   1 
ATOM   4722 C CA  . TYR B 1 673 ? 7.513   14.035  48.024  1.00 51.78  ?  923  TYR B CA  1 
ATOM   4723 C C   . TYR B 1 673 ? 8.512   14.328  46.913  1.00 52.25  ?  923  TYR B C   1 
ATOM   4724 O O   . TYR B 1 673 ? 9.665   14.680  47.186  1.00 52.84  ?  923  TYR B O   1 
ATOM   4725 C CB  . TYR B 1 673 ? 7.416   12.529  48.270  1.00 53.14  ?  923  TYR B CB  1 
ATOM   4726 C CG  . TYR B 1 673 ? 8.763   11.844  48.320  1.00 51.55  ?  923  TYR B CG  1 
ATOM   4727 C CD1 . TYR B 1 673 ? 9.570   11.938  49.444  1.00 51.85  ?  923  TYR B CD1 1 
ATOM   4728 C CD2 . TYR B 1 673 ? 9.232   11.111  47.239  1.00 51.69  ?  923  TYR B CD2 1 
ATOM   4729 C CE1 . TYR B 1 673 ? 10.805  11.320  49.492  1.00 52.29  ?  923  TYR B CE1 1 
ATOM   4730 C CE2 . TYR B 1 673 ? 10.465  10.490  47.278  1.00 52.20  ?  923  TYR B CE2 1 
ATOM   4731 C CZ  . TYR B 1 673 ? 11.247  10.597  48.406  1.00 62.34  ?  923  TYR B CZ  1 
ATOM   4732 O OH  . TYR B 1 673 ? 12.477  9.977   48.448  1.00 65.21  ?  923  TYR B OH  1 
ATOM   4733 N N   . LYS B 1 674 ? 8.091   14.185  45.654  1.00 52.16  ?  924  LYS B N   1 
ATOM   4734 C CA  . LYS B 1 674 ? 9.002   14.441  44.544  1.00 52.79  ?  924  LYS B CA  1 
ATOM   4735 C C   . LYS B 1 674 ? 9.333   15.922  44.415  1.00 55.82  ?  924  LYS B C   1 
ATOM   4736 O O   . LYS B 1 674 ? 10.451  16.273  44.022  1.00 56.07  ?  924  LYS B O   1 
ATOM   4737 C CB  . LYS B 1 674 ? 8.408   13.910  43.240  1.00 59.17  ?  924  LYS B CB  1 
ATOM   4738 C CG  . LYS B 1 674 ? 8.247   12.398  43.197  1.00 56.31  ?  924  LYS B CG  1 
ATOM   4739 C CD  . LYS B 1 674 ? 7.793   11.931  41.821  1.00 77.41  ?  924  LYS B CD  1 
ATOM   4740 C CE  . LYS B 1 674 ? 7.683   10.415  41.750  1.00 62.01  ?  924  LYS B CE  1 
ATOM   4741 N NZ  . LYS B 1 674 ? 6.556   9.888   42.567  1.00 69.03  1  924  LYS B NZ  1 
ATOM   4742 N N   . ARG B 1 675 ? 8.383   16.804  44.737  1.00 53.71  ?  925  ARG B N   1 
ATOM   4743 C CA  . ARG B 1 675 ? 8.676   18.233  44.708  1.00 54.82  ?  925  ARG B CA  1 
ATOM   4744 C C   . ARG B 1 675 ? 9.564   18.641  45.876  1.00 61.69  ?  925  ARG B C   1 
ATOM   4745 O O   . ARG B 1 675 ? 10.297  19.632  45.777  1.00 60.74  ?  925  ARG B O   1 
ATOM   4746 C CB  . ARG B 1 675 ? 7.375   19.039  44.704  1.00 58.43  ?  925  ARG B CB  1 
ATOM   4747 C CG  . ARG B 1 675 ? 6.454   18.690  43.543  1.00 65.43  ?  925  ARG B CG  1 
ATOM   4748 C CD  . ARG B 1 675 ? 5.195   19.545  43.504  1.00 74.13  ?  925  ARG B CD  1 
ATOM   4749 N NE  . ARG B 1 675 ? 5.398   20.799  42.783  1.00 60.06  ?  925  ARG B NE  1 
ATOM   4750 C CZ  . ARG B 1 675 ? 5.356   22.002  43.346  1.00 78.66  ?  925  ARG B CZ  1 
ATOM   4751 N NH1 . ARG B 1 675 ? 5.109   22.121  44.643  1.00 74.64  1  925  ARG B NH1 1 
ATOM   4752 N NH2 . ARG B 1 675 ? 5.553   23.087  42.608  1.00 85.27  ?  925  ARG B NH2 1 
ATOM   4753 N N   . MET B 1 676 ? 9.519   17.892  46.981  1.00 55.75  ?  926  MET B N   1 
ATOM   4754 C CA  . MET B 1 676 ? 10.439  18.148  48.085  1.00 58.88  ?  926  MET B CA  1 
ATOM   4755 C C   . MET B 1 676 ? 11.849  17.685  47.740  1.00 67.73  ?  926  MET B C   1 
ATOM   4756 O O   . MET B 1 676 ? 12.830  18.358  48.078  1.00 72.93  ?  926  MET B O   1 
ATOM   4757 C CB  . MET B 1 676 ? 9.939   17.458  49.356  1.00 55.53  ?  926  MET B CB  1 
ATOM   4758 C CG  . MET B 1 676 ? 10.831  17.645  50.581  1.00 59.72  ?  926  MET B CG  1 
ATOM   4759 S SD  . MET B 1 676 ? 12.161  16.430  50.731  1.00 74.08  ?  926  MET B SD  1 
ATOM   4760 C CE  . MET B 1 676 ? 11.223  14.912  50.886  1.00 55.65  ?  926  MET B CE  1 
ATOM   4761 N N   . ILE B 1 677 ? 11.967  16.534  47.072  1.00 61.70  ?  927  ILE B N   1 
ATOM   4762 C CA  . ILE B 1 677 ? 13.279  16.008  46.699  1.00 63.24  ?  927  ILE B CA  1 
ATOM   4763 C C   . ILE B 1 677 ? 13.995  16.971  45.761  1.00 61.58  ?  927  ILE B C   1 
ATOM   4764 O O   . ILE B 1 677 ? 15.207  17.192  45.879  1.00 72.82  ?  927  ILE B O   1 
ATOM   4765 C CB  . ILE B 1 677 ? 13.129  14.607  46.076  1.00 62.65  ?  927  ILE B CB  1 
ATOM   4766 C CG1 . ILE B 1 677 ? 12.876  13.562  47.165  1.00 58.02  ?  927  ILE B CG1 1 
ATOM   4767 C CG2 . ILE B 1 677 ? 14.354  14.239  45.254  1.00 57.83  ?  927  ILE B CG2 1 
ATOM   4768 C CD1 . ILE B 1 677 ? 14.014  13.425  48.154  1.00 74.71  ?  927  ILE B CD1 1 
ATOM   4769 N N   . ALA B 1 678 ? 13.256  17.574  44.827  1.00 62.71  ?  928  ALA B N   1 
ATOM   4770 C CA  . ALA B 1 678 ? 13.866  18.490  43.870  1.00 64.33  ?  928  ALA B CA  1 
ATOM   4771 C C   . ALA B 1 678 ? 14.334  19.786  44.518  1.00 69.97  ?  928  ALA B C   1 
ATOM   4772 O O   . ALA B 1 678 ? 15.145  20.502  43.921  1.00 87.36  ?  928  ALA B O   1 
ATOM   4773 C CB  . ALA B 1 678 ? 12.884  18.799  42.739  1.00 63.61  ?  928  ALA B CB  1 
ATOM   4774 N N   . THR B 1 679 ? 13.842  20.108  45.713  1.00 76.15  ?  929  THR B N   1 
ATOM   4775 C CA  . THR B 1 679 ? 14.223  21.313  46.441  1.00 70.69  ?  929  THR B CA  1 
ATOM   4776 C C   . THR B 1 679 ? 14.632  20.968  47.866  1.00 74.03  ?  929  THR B C   1 
ATOM   4777 O O   . THR B 1 679 ? 14.268  21.661  48.821  1.00 78.63  ?  929  THR B O   1 
ATOM   4778 C CB  . THR B 1 679 ? 13.089  22.336  46.449  1.00 81.01  ?  929  THR B CB  1 
ATOM   4779 O OG1 . THR B 1 679 ? 11.976  21.810  47.182  1.00 66.31  ?  929  THR B OG1 1 
ATOM   4780 C CG2 . THR B 1 679 ? 12.644  22.663  45.030  1.00 69.23  ?  929  THR B CG2 1 
ATOM   4781 N N   . LYS B 1 680 ? 15.402  19.890  48.029  1.00 79.58  ?  930  LYS B N   1 
ATOM   4782 C CA  . LYS B 1 680 ? 15.738  19.407  49.365  1.00 73.63  ?  930  LYS B CA  1 
ATOM   4783 C C   . LYS B 1 680 ? 16.668  20.359  50.106  1.00 76.62  ?  930  LYS B C   1 
ATOM   4784 O O   . LYS B 1 680 ? 16.555  20.501  51.328  1.00 78.01  ?  930  LYS B O   1 
ATOM   4785 C CB  . LYS B 1 680 ? 16.372  18.018  49.269  1.00 74.50  ?  930  LYS B CB  1 
ATOM   4786 C CG  . LYS B 1 680 ? 16.462  17.277  50.591  1.00 60.71  ?  930  LYS B CG  1 
ATOM   4787 C CD  . LYS B 1 680 ? 16.978  15.867  50.383  1.00 74.57  ?  930  LYS B CD  1 
ATOM   4788 C CE  . LYS B 1 680 ? 16.875  15.036  51.649  1.00 71.44  ?  930  LYS B CE  1 
ATOM   4789 N NZ  . LYS B 1 680 ? 17.266  13.618  51.406  1.00 92.85  1  930  LYS B NZ  1 
ATOM   4790 N N   . ASP B 1 681 ? 17.581  21.023  49.392  1.00 79.65  ?  931  ASP B N   1 
ATOM   4791 C CA  . ASP B 1 681 ? 18.517  21.943  50.029  1.00 86.58  ?  931  ASP B CA  1 
ATOM   4792 C C   . ASP B 1 681 ? 17.829  23.151  50.649  1.00 81.16  ?  931  ASP B C   1 
ATOM   4793 O O   . ASP B 1 681 ? 18.461  23.866  51.435  1.00 83.76  ?  931  ASP B O   1 
ATOM   4794 C CB  . ASP B 1 681 ? 19.562  22.411  49.014  1.00 92.47  ?  931  ASP B CB  1 
ATOM   4795 C CG  . ASP B 1 681 ? 20.356  21.263  48.423  1.00 101.04 ?  931  ASP B CG  1 
ATOM   4796 O OD1 . ASP B 1 681 ? 20.667  20.310  49.167  1.00 99.23  ?  931  ASP B OD1 1 
ATOM   4797 O OD2 . ASP B 1 681 ? 20.664  21.311  47.212  1.00 111.93 -1 931  ASP B OD2 1 
ATOM   4798 N N   . SER B 1 682 ? 16.563  23.398  50.321  1.00 84.83  ?  932  SER B N   1 
ATOM   4799 C CA  . SER B 1 682 ? 15.819  24.530  50.854  1.00 82.42  ?  932  SER B CA  1 
ATOM   4800 C C   . SER B 1 682 ? 15.149  24.228  52.188  1.00 85.08  ?  932  SER B C   1 
ATOM   4801 O O   . SER B 1 682 ? 14.482  25.108  52.741  1.00 86.07  ?  932  SER B O   1 
ATOM   4802 C CB  . SER B 1 682 ? 14.762  24.984  49.842  1.00 80.95  ?  932  SER B CB  1 
ATOM   4803 O OG  . SER B 1 682 ? 15.347  25.276  48.585  1.00 87.34  ?  932  SER B OG  1 
ATOM   4804 N N   . PHE B 1 683 ? 15.305  23.017  52.717  1.00 84.11  ?  933  PHE B N   1 
ATOM   4805 C CA  . PHE B 1 683 ? 14.664  22.608  53.959  1.00 79.62  ?  933  PHE B CA  1 
ATOM   4806 C C   . PHE B 1 683 ? 15.709  22.445  55.054  1.00 78.11  ?  933  PHE B C   1 
ATOM   4807 O O   . PHE B 1 683 ? 16.770  21.855  54.825  1.00 89.26  ?  933  PHE B O   1 
ATOM   4808 C CB  . PHE B 1 683 ? 13.887  21.304  53.769  1.00 75.75  ?  933  PHE B CB  1 
ATOM   4809 C CG  . PHE B 1 683 ? 12.704  21.435  52.855  1.00 73.84  ?  933  PHE B CG  1 
ATOM   4810 C CD1 . PHE B 1 683 ? 12.783  21.027  51.534  1.00 69.02  ?  933  PHE B CD1 1 
ATOM   4811 C CD2 . PHE B 1 683 ? 11.513  21.974  53.315  1.00 65.35  ?  933  PHE B CD2 1 
ATOM   4812 C CE1 . PHE B 1 683 ? 11.695  21.149  50.689  1.00 64.53  ?  933  PHE B CE1 1 
ATOM   4813 C CE2 . PHE B 1 683 ? 10.422  22.100  52.477  1.00 74.57  ?  933  PHE B CE2 1 
ATOM   4814 C CZ  . PHE B 1 683 ? 10.513  21.686  51.162  1.00 74.80  ?  933  PHE B CZ  1 
ATOM   4815 N N   . GLN B 1 684 ? 15.401  22.968  56.239  1.00 76.79  ?  934  GLN B N   1 
ATOM   4816 C CA  . GLN B 1 684 ? 16.299  22.859  57.382  1.00 80.78  ?  934  GLN B CA  1 
ATOM   4817 C C   . GLN B 1 684 ? 16.427  21.402  57.807  1.00 78.43  ?  934  GLN B C   1 
ATOM   4818 O O   . GLN B 1 684 ? 15.448  20.782  58.235  1.00 74.63  ?  934  GLN B O   1 
ATOM   4819 C CB  . GLN B 1 684 ? 15.782  23.712  58.538  1.00 82.55  ?  934  GLN B CB  1 
ATOM   4820 C CG  . GLN B 1 684 ? 16.456  25.067  58.681  1.00 99.14  ?  934  GLN B CG  1 
ATOM   4821 C CD  . GLN B 1 684 ? 17.788  24.984  59.403  1.00 108.96 ?  934  GLN B CD  1 
ATOM   4822 O OE1 . GLN B 1 684 ? 18.275  23.896  59.712  1.00 103.61 ?  934  GLN B OE1 1 
ATOM   4823 N NE2 . GLN B 1 684 ? 18.383  26.139  59.682  1.00 109.00 ?  934  GLN B NE2 1 
ATOM   4824 N N   . SER B 1 685 ? 17.631  20.855  57.687  1.00 76.95  ?  935  SER B N   1 
ATOM   4825 C CA  . SER B 1 685 ? 17.935  19.512  58.152  1.00 78.76  ?  935  SER B CA  1 
ATOM   4826 C C   . SER B 1 685 ? 18.598  19.575  59.523  1.00 81.31  ?  935  SER B C   1 
ATOM   4827 O O   . SER B 1 685 ? 19.053  20.630  59.973  1.00 74.84  ?  935  SER B O   1 
ATOM   4828 C CB  . SER B 1 685 ? 18.838  18.782  57.154  1.00 71.19  ?  935  SER B CB  1 
ATOM   4829 O OG  . SER B 1 685 ? 20.029  19.512  56.911  1.00 88.37  ?  935  SER B OG  1 
ATOM   4830 N N   . PHE B 1 686 ? 18.639  18.426  60.192  1.00 71.17  ?  936  PHE B N   1 
ATOM   4831 C CA  . PHE B 1 686 ? 19.252  18.345  61.510  1.00 74.95  ?  936  PHE B CA  1 
ATOM   4832 C C   . PHE B 1 686 ? 19.666  16.906  61.779  1.00 73.56  ?  936  PHE B C   1 
ATOM   4833 O O   . PHE B 1 686 ? 18.954  15.970  61.409  1.00 86.26  ?  936  PHE B O   1 
ATOM   4834 C CB  . PHE B 1 686 ? 18.301  18.846  62.606  1.00 76.44  ?  936  PHE B CB  1 
ATOM   4835 C CG  . PHE B 1 686 ? 17.024  18.060  62.717  1.00 73.24  ?  936  PHE B CG  1 
ATOM   4836 C CD1 . PHE B 1 686 ? 15.934  18.368  61.919  1.00 72.28  ?  936  PHE B CD1 1 
ATOM   4837 C CD2 . PHE B 1 686 ? 16.907  17.023  63.628  1.00 71.37  ?  936  PHE B CD2 1 
ATOM   4838 C CE1 . PHE B 1 686 ? 14.757  17.650  62.021  1.00 77.17  ?  936  PHE B CE1 1 
ATOM   4839 C CE2 . PHE B 1 686 ? 15.732  16.302  63.734  1.00 66.90  ?  936  PHE B CE2 1 
ATOM   4840 C CZ  . PHE B 1 686 ? 14.656  16.616  62.930  1.00 66.76  ?  936  PHE B CZ  1 
ATOM   4841 N N   . ASN B 1 687 ? 20.819  16.745  62.417  1.00 81.21  ?  937  ASN B N   1 
ATOM   4842 C CA  . ASN B 1 687 ? 21.339  15.437  62.780  1.00 89.77  ?  937  ASN B CA  1 
ATOM   4843 C C   . ASN B 1 687 ? 20.842  15.034  64.167  1.00 79.65  ?  937  ASN B C   1 
ATOM   4844 O O   . ASN B 1 687 ? 20.479  15.874  64.994  1.00 80.41  ?  937  ASN B O   1 
ATOM   4845 C CB  . ASN B 1 687 ? 22.868  15.442  62.728  1.00 85.78  ?  937  ASN B CB  1 
ATOM   4846 C CG  . ASN B 1 687 ? 23.403  15.495  61.303  1.00 91.55  ?  937  ASN B CG  1 
ATOM   4847 O OD1 . ASN B 1 687 ? 23.043  14.668  60.466  1.00 91.26  ?  937  ASN B OD1 1 
ATOM   4848 N ND2 . ASN B 1 687 ? 24.261  16.474  61.021  1.00 97.45  ?  937  ASN B ND2 1 
ATOM   4849 N N   . VAL B 1 688 ? 20.818  13.724  64.407  1.00 85.19  ?  938  VAL B N   1 
ATOM   4850 C CA  . VAL B 1 688 ? 20.223  13.150  65.609  1.00 80.74  ?  938  VAL B CA  1 
ATOM   4851 C C   . VAL B 1 688 ? 21.159  12.092  66.179  1.00 88.37  ?  938  VAL B C   1 
ATOM   4852 O O   . VAL B 1 688 ? 21.710  11.271  65.437  1.00 101.34 ?  938  VAL B O   1 
ATOM   4853 C CB  . VAL B 1 688 ? 18.834  12.540  65.313  1.00 72.69  ?  938  VAL B CB  1 
ATOM   4854 C CG1 . VAL B 1 688 ? 18.307  11.776  66.517  1.00 71.14  ?  938  VAL B CG1 1 
ATOM   4855 C CG2 . VAL B 1 688 ? 17.850  13.624  64.899  1.00 73.40  ?  938  VAL B CG2 1 
ATOM   4856 N N   . THR B 1 689 ? 21.337  12.115  67.501  1.00 86.31  ?  939  THR B N   1 
ATOM   4857 C CA  . THR B 1 689 ? 22.105  11.105  68.217  1.00 83.87  ?  939  THR B CA  1 
ATOM   4858 C C   . THR B 1 689 ? 21.328  10.637  69.438  1.00 86.63  ?  939  THR B C   1 
ATOM   4859 O O   . THR B 1 689 ? 20.680  11.438  70.118  1.00 87.23  ?  939  THR B O   1 
ATOM   4860 C CB  . THR B 1 689 ? 23.477  11.634  68.658  1.00 84.37  ?  939  THR B CB  1 
ATOM   4861 O OG1 . THR B 1 689 ? 23.353  12.994  69.092  1.00 89.88  ?  939  THR B OG1 1 
ATOM   4862 C CG2 . THR B 1 689 ? 24.479  11.545  67.517  1.00 88.66  ?  939  THR B CG2 1 
ATOM   4863 N N   . GLU B 1 690 ? 21.412  9.334   69.710  1.00 84.33  ?  940  GLU B N   1 
ATOM   4864 C CA  . GLU B 1 690 ? 20.733  8.650   70.807  1.00 92.13  ?  940  GLU B CA  1 
ATOM   4865 C C   . GLU B 1 690 ? 19.261  9.035   70.877  1.00 87.21  ?  940  GLU B C   1 
ATOM   4866 O O   . GLU B 1 690 ? 18.835  9.690   71.837  1.00 84.73  ?  940  GLU B O   1 
ATOM   4867 C CB  . GLU B 1 690 ? 21.424  8.956   72.142  1.00 91.43  ?  940  GLU B CB  1 
ATOM   4868 C CG  . GLU B 1 690 ? 22.825  8.382   72.253  1.00 90.86  ?  940  GLU B CG  1 
ATOM   4869 C CD  . GLU B 1 690 ? 23.279  8.235   73.691  1.00 112.82 ?  940  GLU B CD  1 
ATOM   4870 O OE1 . GLU B 1 690 ? 22.582  8.739   74.598  1.00 111.11 ?  940  GLU B OE1 1 
ATOM   4871 O OE2 . GLU B 1 690 ? 24.336  7.605   73.912  1.00 124.63 -1 940  GLU B OE2 1 
ATOM   4872 N N   . PRO B 1 691 ? 18.456  8.647   69.896  1.00 83.80  ?  941  PRO B N   1 
ATOM   4873 C CA  . PRO B 1 691 ? 17.037  8.998   69.933  1.00 85.44  ?  941  PRO B CA  1 
ATOM   4874 C C   . PRO B 1 691 ? 16.232  8.028   70.782  1.00 89.32  ?  941  PRO B C   1 
ATOM   4875 O O   . PRO B 1 691 ? 16.536  6.836   70.876  1.00 93.14  ?  941  PRO B O   1 
ATOM   4876 C CB  . PRO B 1 691 ? 16.620  8.916   68.459  1.00 85.67  ?  941  PRO B CB  1 
ATOM   4877 C CG  . PRO B 1 691 ? 17.498  7.849   67.903  1.00 90.31  ?  941  PRO B CG  1 
ATOM   4878 C CD  . PRO B 1 691 ? 18.813  7.943   68.649  1.00 83.35  ?  941  PRO B CD  1 
ATOM   4879 N N   . HIS B 1 692 ? 15.189  8.566   71.411  1.00 86.82  ?  942  HIS B N   1 
ATOM   4880 C CA  . HIS B 1 692 ? 14.249  7.777   72.199  1.00 81.36  ?  942  HIS B CA  1 
ATOM   4881 C C   . HIS B 1 692 ? 12.859  8.353   71.983  1.00 83.04  ?  942  HIS B C   1 
ATOM   4882 O O   . HIS B 1 692 ? 12.627  9.531   72.268  1.00 80.28  ?  942  HIS B O   1 
ATOM   4883 C CB  . HIS B 1 692 ? 14.613  7.788   73.687  1.00 84.89  ?  942  HIS B CB  1 
ATOM   4884 C CG  . HIS B 1 692 ? 15.966  7.221   73.985  1.00 94.93  ?  942  HIS B CG  1 
ATOM   4885 N ND1 . HIS B 1 692 ? 16.160  5.900   74.328  1.00 101.38 ?  942  HIS B ND1 1 
ATOM   4886 C CD2 . HIS B 1 692 ? 17.191  7.796   73.995  1.00 96.00  ?  942  HIS B CD2 1 
ATOM   4887 C CE1 . HIS B 1 692 ? 17.448  5.686   74.533  1.00 103.60 ?  942  HIS B CE1 1 
ATOM   4888 N NE2 . HIS B 1 692 ? 18.095  6.820   74.338  1.00 103.17 ?  942  HIS B NE2 1 
ATOM   4889 N N   . ILE B 1 693 ? 11.940  7.531   71.484  1.00 84.36  ?  943  ILE B N   1 
ATOM   4890 C CA  . ILE B 1 693 ? 10.609  7.989   71.109  1.00 84.64  ?  943  ILE B CA  1 
ATOM   4891 C C   . ILE B 1 693 ? 9.565   7.146   71.828  1.00 82.07  ?  943  ILE B C   1 
ATOM   4892 O O   . ILE B 1 693 ? 9.743   5.936   72.011  1.00 85.10  ?  943  ILE B O   1 
ATOM   4893 C CB  . ILE B 1 693 ? 10.404  7.939   69.577  1.00 80.11  ?  943  ILE B CB  1 
ATOM   4894 C CG1 . ILE B 1 693 ? 9.076   8.590   69.184  1.00 69.77  ?  943  ILE B CG1 1 
ATOM   4895 C CG2 . ILE B 1 693 ? 10.487  6.507   69.058  1.00 70.03  ?  943  ILE B CG2 1 
ATOM   4896 C CD1 . ILE B 1 693 ? 8.888   8.741   67.691  1.00 69.78  ?  943  ILE B CD1 1 
ATOM   4897 N N   . SER B 1 694 ? 8.489   7.794   72.256  1.00 82.75  ?  944  SER B N   1 
ATOM   4898 C CA  . SER B 1 694 ? 7.324   7.134   72.824  1.00 73.90  ?  944  SER B CA  1 
ATOM   4899 C C   . SER B 1 694 ? 6.099   7.516   71.995  1.00 80.09  ?  944  SER B C   1 
ATOM   4900 O O   . SER B 1 694 ? 6.212   8.100   70.913  1.00 86.30  ?  944  SER B O   1 
ATOM   4901 C CB  . SER B 1 694 ? 7.150   7.509   74.298  1.00 85.20  ?  944  SER B CB  1 
ATOM   4902 O OG  . SER B 1 694 ? 6.656   8.830   74.433  1.00 79.45  ?  944  SER B OG  1 
ATOM   4903 N N   . ALA B 1 695 ? 4.919   7.188   72.513  1.00 83.71  ?  945  ALA B N   1 
ATOM   4904 C CA  . ALA B 1 695 ? 3.675   7.561   71.854  1.00 75.69  ?  945  ALA B CA  1 
ATOM   4905 C C   . ALA B 1 695 ? 3.321   9.030   72.044  1.00 85.98  ?  945  ALA B C   1 
ATOM   4906 O O   . ALA B 1 695 ? 2.330   9.490   71.467  1.00 75.07  ?  945  ALA B O   1 
ATOM   4907 C CB  . ALA B 1 695 ? 2.526   6.687   72.362  1.00 92.40  ?  945  ALA B CB  1 
ATOM   4908 N N   . SER B 1 696 ? 4.103   9.775   72.827  1.00 82.48  ?  946  SER B N   1 
ATOM   4909 C CA  . SER B 1 696 ? 3.769   11.160  73.135  1.00 83.74  ?  946  SER B CA  1 
ATOM   4910 C C   . SER B 1 696 ? 4.953   12.115  73.149  1.00 87.30  ?  946  SER B C   1 
ATOM   4911 O O   . SER B 1 696 ? 4.729   13.322  73.278  1.00 88.94  ?  946  SER B O   1 
ATOM   4912 C CB  . SER B 1 696 ? 3.055   11.241  74.493  1.00 84.24  ?  946  SER B CB  1 
ATOM   4913 O OG  . SER B 1 696 ? 3.830   10.639  75.516  1.00 95.77  ?  946  SER B OG  1 
ATOM   4914 N N   . SER B 1 697 ? 6.191   11.641  73.021  1.00 88.31  ?  947  SER B N   1 
ATOM   4915 C CA  . SER B 1 697 ? 7.342   12.528  73.100  1.00 75.05  ?  947  SER B CA  1 
ATOM   4916 C C   . SER B 1 697 ? 8.494   11.951  72.289  1.00 72.86  ?  947  SER B C   1 
ATOM   4917 O O   . SER B 1 697 ? 8.562   10.746  72.036  1.00 81.03  ?  947  SER B O   1 
ATOM   4918 C CB  . SER B 1 697 ? 7.773   12.757  74.554  1.00 78.98  ?  947  SER B CB  1 
ATOM   4919 O OG  . SER B 1 697 ? 8.078   11.531  75.195  1.00 86.61  ?  947  SER B OG  1 
ATOM   4920 N N   . LEU B 1 698 ? 9.401   12.837  71.884  1.00 74.59  ?  948  LEU B N   1 
ATOM   4921 C CA  . LEU B 1 698 ? 10.611  12.467  71.163  1.00 65.90  ?  948  LEU B CA  1 
ATOM   4922 C C   . LEU B 1 698 ? 11.810  13.059  71.886  1.00 77.86  ?  948  LEU B C   1 
ATOM   4923 O O   . LEU B 1 698 ? 11.806  14.245  72.230  1.00 82.76  ?  948  LEU B O   1 
ATOM   4924 C CB  . LEU B 1 698 ? 10.569  12.955  69.711  1.00 78.23  ?  948  LEU B CB  1 
ATOM   4925 C CG  . LEU B 1 698 ? 11.808  12.650  68.866  1.00 70.69  ?  948  LEU B CG  1 
ATOM   4926 C CD1 . LEU B 1 698 ? 12.059  11.152  68.798  1.00 73.15  ?  948  LEU B CD1 1 
ATOM   4927 C CD2 . LEU B 1 698 ? 11.667  13.239  67.470  1.00 58.58  ?  948  LEU B CD2 1 
ATOM   4928 N N   . GLU B 1 699 ? 12.830  12.235  72.111  1.00 87.20  ?  949  GLU B N   1 
ATOM   4929 C CA  . GLU B 1 699 ? 13.999  12.617  72.892  1.00 77.19  ?  949  GLU B CA  1 
ATOM   4930 C C   . GLU B 1 699 ? 15.253  12.279  72.102  1.00 79.89  ?  949  GLU B C   1 
ATOM   4931 O O   . GLU B 1 699 ? 15.425  11.134  71.673  1.00 81.78  ?  949  GLU B O   1 
ATOM   4932 C CB  . GLU B 1 699 ? 14.005  11.891  74.241  1.00 77.78  ?  949  GLU B CB  1 
ATOM   4933 C CG  . GLU B 1 699 ? 14.790  12.580  75.338  1.00 88.44  ?  949  GLU B CG  1 
ATOM   4934 C CD  . GLU B 1 699 ? 14.745  11.808  76.643  1.00 109.08 ?  949  GLU B CD  1 
ATOM   4935 O OE1 . GLU B 1 699 ? 15.690  11.036  76.913  1.00 106.70 ?  949  GLU B OE1 1 
ATOM   4936 O OE2 . GLU B 1 699 ? 13.756  11.961  77.391  1.00 116.97 -1 949  GLU B OE2 1 
ATOM   4937 N N   . TRP B 1 700 ? 16.123  13.267  71.909  1.00 76.80  ?  950  TRP B N   1 
ATOM   4938 C CA  . TRP B 1 700 ? 17.356  13.042  71.164  1.00 85.75  ?  950  TRP B CA  1 
ATOM   4939 C C   . TRP B 1 700 ? 18.389  14.078  71.583  1.00 84.69  ?  950  TRP B C   1 
ATOM   4940 O O   . TRP B 1 700 ? 18.104  14.996  72.355  1.00 82.72  ?  950  TRP B O   1 
ATOM   4941 C CB  . TRP B 1 700 ? 17.110  13.082  69.651  1.00 86.51  ?  950  TRP B CB  1 
ATOM   4942 C CG  . TRP B 1 700 ? 16.996  14.461  69.064  1.00 78.59  ?  950  TRP B CG  1 
ATOM   4943 C CD1 . TRP B 1 700 ? 17.991  15.183  68.468  1.00 77.90  ?  950  TRP B CD1 1 
ATOM   4944 C CD2 . TRP B 1 700 ? 15.819  15.276  69.002  1.00 75.15  ?  950  TRP B CD2 1 
ATOM   4945 N NE1 . TRP B 1 700 ? 17.507  16.397  68.044  1.00 72.89  ?  950  TRP B NE1 1 
ATOM   4946 C CE2 . TRP B 1 700 ? 16.177  16.479  68.361  1.00 77.14  ?  950  TRP B CE2 1 
ATOM   4947 C CE3 . TRP B 1 700 ? 14.499  15.107  69.431  1.00 73.57  ?  950  TRP B CE3 1 
ATOM   4948 C CZ2 . TRP B 1 700 ? 15.262  17.507  68.137  1.00 66.69  ?  950  TRP B CZ2 1 
ATOM   4949 C CZ3 . TRP B 1 700 ? 13.592  16.129  69.208  1.00 67.59  ?  950  TRP B CZ3 1 
ATOM   4950 C CH2 . TRP B 1 700 ? 13.978  17.312  68.566  1.00 64.89  ?  950  TRP B CH2 1 
ATOM   4951 N N   . ILE B 1 701 ? 19.604  13.909  71.065  1.00 84.43  ?  951  ILE B N   1 
ATOM   4952 C CA  . ILE B 1 701 ? 20.724  14.802  71.338  1.00 82.49  ?  951  ILE B CA  1 
ATOM   4953 C C   . ILE B 1 701 ? 21.213  15.357  70.009  1.00 88.17  ?  951  ILE B C   1 
ATOM   4954 O O   . ILE B 1 701 ? 21.640  14.595  69.133  1.00 90.25  ?  951  ILE B O   1 
ATOM   4955 C CB  . ILE B 1 701 ? 21.865  14.085  72.079  1.00 88.80  ?  951  ILE B CB  1 
ATOM   4956 C CG1 . ILE B 1 701 ? 21.344  13.406  73.347  1.00 92.52  ?  951  ILE B CG1 1 
ATOM   4957 C CG2 . ILE B 1 701 ? 22.980  15.066  72.417  1.00 82.11  ?  951  ILE B CG2 1 
ATOM   4958 C CD1 . ILE B 1 701 ? 22.419  12.686  74.139  1.00 82.93  ?  951  ILE B CD1 1 
ATOM   4959 N N   . ASP B 1 702 ? 21.150  16.673  69.858  1.00 87.72  ?  952  ASP B N   1 
ATOM   4960 C CA  . ASP B 1 702 ? 21.656  17.315  68.650  1.00 87.13  ?  952  ASP B CA  1 
ATOM   4961 C C   . ASP B 1 702 ? 23.180  17.330  68.677  1.00 92.95  ?  952  ASP B C   1 
ATOM   4962 O O   . ASP B 1 702 ? 23.769  17.789  69.659  1.00 100.88 ?  952  ASP B O   1 
ATOM   4963 C CB  . ASP B 1 702 ? 21.115  18.737  68.532  1.00 93.14  ?  952  ASP B CB  1 
ATOM   4964 C CG  . ASP B 1 702 ? 21.611  19.455  67.289  1.00 95.49  ?  952  ASP B CG  1 
ATOM   4965 O OD1 . ASP B 1 702 ? 22.806  19.815  67.233  1.00 96.94  ?  952  ASP B OD1 1 
ATOM   4966 O OD2 . ASP B 1 702 ? 20.801  19.656  66.361  1.00 107.95 -1 952  ASP B OD2 1 
ATOM   4967 N N   . PRO B 1 703 ? 23.848  16.839  67.631  1.00 96.87  ?  953  PRO B N   1 
ATOM   4968 C CA  . PRO B 1 703 ? 25.314  16.779  67.649  1.00 96.53  ?  953  PRO B CA  1 
ATOM   4969 C C   . PRO B 1 703 ? 25.978  17.835  66.776  1.00 100.91 ?  953  PRO B C   1 
ATOM   4970 O O   . PRO B 1 703 ? 27.184  17.759  66.521  1.00 106.93 ?  953  PRO B O   1 
ATOM   4971 C CB  . PRO B 1 703 ? 25.601  15.368  67.117  1.00 87.19  ?  953  PRO B CB  1 
ATOM   4972 C CG  . PRO B 1 703 ? 24.291  14.925  66.412  1.00 87.86  ?  953  PRO B CG  1 
ATOM   4973 C CD  . PRO B 1 703 ? 23.305  16.058  66.512  1.00 91.49  ?  953  PRO B CD  1 
ATOM   4974 N N   . ASP B 1 704 ? 25.210  18.824  66.313  1.00 103.70 ?  954  ASP B N   1 
ATOM   4975 C CA  . ASP B 1 704 ? 25.699  19.814  65.360  1.00 99.83  ?  954  ASP B CA  1 
ATOM   4976 C C   . ASP B 1 704 ? 25.826  21.209  65.961  1.00 100.87 ?  954  ASP B C   1 
ATOM   4977 O O   . ASP B 1 704 ? 25.894  22.193  65.214  1.00 107.05 ?  954  ASP B O   1 
ATOM   4978 C CB  . ASP B 1 704 ? 24.790  19.858  64.129  1.00 110.05 ?  954  ASP B CB  1 
ATOM   4979 C CG  . ASP B 1 704 ? 25.126  18.783  63.114  1.00 106.94 ?  954  ASP B CG  1 
ATOM   4980 O OD1 . ASP B 1 704 ? 25.997  17.935  63.404  1.00 99.43  ?  954  ASP B OD1 1 
ATOM   4981 O OD2 . ASP B 1 704 ? 24.520  18.794  62.022  1.00 102.42 -1 954  ASP B OD2 1 
ATOM   4982 N N   . SER B 1 705 ? 25.859  21.317  67.292  1.00 105.60 ?  955  SER B N   1 
ATOM   4983 C CA  . SER B 1 705 ? 25.972  22.612  67.976  1.00 111.86 ?  955  SER B CA  1 
ATOM   4984 C C   . SER B 1 705 ? 24.836  23.553  67.592  1.00 115.24 ?  955  SER B C   1 
ATOM   4985 O O   . SER B 1 705 ? 24.970  24.776  67.672  1.00 107.76 ?  955  SER B O   1 
ATOM   4986 C CB  . SER B 1 705 ? 27.323  23.272  67.701  1.00 105.16 ?  955  SER B CB  1 
ATOM   4987 O OG  . SER B 1 705 ? 27.308  24.642  68.068  1.00 124.40 ?  955  SER B OG  1 
ATOM   4988 N N   . SER B 1 706 ? 23.707  22.987  67.160  1.00 108.30 ?  956  SER B N   1 
ATOM   4989 C CA  . SER B 1 706 ? 22.569  23.809  66.772  1.00 108.52 ?  956  SER B CA  1 
ATOM   4990 C C   . SER B 1 706 ? 21.902  24.466  67.970  1.00 113.96 ?  956  SER B C   1 
ATOM   4991 O O   . SER B 1 706 ? 21.220  25.483  67.805  1.00 119.57 ?  956  SER B O   1 
ATOM   4992 C CB  . SER B 1 706 ? 21.549  22.965  66.009  1.00 116.94 ?  956  SER B CB  1 
ATOM   4993 O OG  . SER B 1 706 ? 22.116  22.425  64.829  1.00 121.62 ?  956  SER B OG  1 
ATOM   4994 N N   . LEU B 1 707 ? 22.084  23.913  69.164  1.00 120.65 ?  957  LEU B N   1 
ATOM   4995 C CA  . LEU B 1 707 ? 21.479  24.430  70.379  1.00 120.19 ?  957  LEU B CA  1 
ATOM   4996 C C   . LEU B 1 707 ? 22.553  25.067  71.252  1.00 120.06 ?  957  LEU B C   1 
ATOM   4997 O O   . LEU B 1 707 ? 23.718  24.662  71.225  1.00 121.82 ?  957  LEU B O   1 
ATOM   4998 C CB  . LEU B 1 707 ? 20.767  23.320  71.166  1.00 122.60 ?  957  LEU B CB  1 
ATOM   4999 C CG  . LEU B 1 707 ? 19.505  22.603  70.660  1.00 115.27 ?  957  LEU B CG  1 
ATOM   5000 C CD1 . LEU B 1 707 ? 18.335  23.556  70.592  1.00 111.30 ?  957  LEU B CD1 1 
ATOM   5001 C CD2 . LEU B 1 707 ? 19.705  21.907  69.319  1.00 115.15 ?  957  LEU B CD2 1 
ATOM   5002 N N   . ARG B 1 708 ? 22.153  26.073  72.027  1.00 123.51 ?  958  ARG B N   1 
ATOM   5003 C CA  . ARG B 1 708 ? 23.063  26.733  72.954  1.00 117.37 ?  958  ARG B CA  1 
ATOM   5004 C C   . ARG B 1 708 ? 22.344  26.981  74.271  1.00 112.85 ?  958  ARG B C   1 
ATOM   5005 O O   . ARG B 1 708 ? 21.195  27.433  74.279  1.00 106.13 ?  958  ARG B O   1 
ATOM   5006 C CB  . ARG B 1 708 ? 23.594  28.053  72.379  1.00 107.39 ?  958  ARG B CB  1 
ATOM   5007 C CG  . ARG B 1 708 ? 24.259  28.949  73.413  1.00 110.62 ?  958  ARG B CG  1 
ATOM   5008 C CD  . ARG B 1 708 ? 25.038  30.080  72.767  1.00 113.02 ?  958  ARG B CD  1 
ATOM   5009 N NE  . ARG B 1 708 ? 26.182  29.587  72.006  1.00 102.87 ?  958  ARG B NE  1 
ATOM   5010 C CZ  . ARG B 1 708 ? 27.347  29.242  72.547  1.00 107.20 ?  958  ARG B CZ  1 
ATOM   5011 N NH1 . ARG B 1 708 ? 28.334  28.806  71.779  1.00 110.71 1  958  ARG B NH1 1 
ATOM   5012 N NH2 . ARG B 1 708 ? 27.524  29.330  73.858  1.00 114.33 ?  958  ARG B NH2 1 
ATOM   5013 N N   . ASP B 1 709 ? 23.022  26.684  75.374  1.00 122.10 ?  959  ASP B N   1 
ATOM   5014 C CA  . ASP B 1 709 ? 22.466  26.817  76.710  1.00 114.11 ?  959  ASP B CA  1 
ATOM   5015 C C   . ASP B 1 709 ? 23.196  27.909  77.482  1.00 112.89 ?  959  ASP B C   1 
ATOM   5016 O O   . ASP B 1 709 ? 24.333  28.269  77.169  1.00 114.78 ?  959  ASP B O   1 
ATOM   5017 C CB  . ASP B 1 709 ? 22.561  25.488  77.467  1.00 116.67 ?  959  ASP B CB  1 
ATOM   5018 C CG  . ASP B 1 709 ? 22.154  24.304  76.614  1.00 121.89 ?  959  ASP B CG  1 
ATOM   5019 O OD1 . ASP B 1 709 ? 21.084  24.372  75.974  1.00 122.20 ?  959  ASP B OD1 1 
ATOM   5020 O OD2 . ASP B 1 709 ? 22.913  23.313  76.572  1.00 122.23 -1 959  ASP B OD2 1 
ATOM   5021 N N   . HIS B 1 710 ? 22.520  28.436  78.502  1.00 97.83  ?  960  HIS B N   1 
ATOM   5022 C CA  . HIS B 1 710 ? 23.087  29.439  79.396  1.00 92.59  ?  960  HIS B CA  1 
ATOM   5023 C C   . HIS B 1 710 ? 22.933  28.934  80.822  1.00 93.09  ?  960  HIS B C   1 
ATOM   5024 O O   . HIS B 1 710 ? 21.809  28.716  81.286  1.00 91.01  ?  960  HIS B O   1 
ATOM   5025 C CB  . HIS B 1 710 ? 22.397  30.796  79.214  1.00 94.50  ?  960  HIS B CB  1 
ATOM   5026 C CG  . HIS B 1 710 ? 23.091  31.930  79.905  1.00 97.45  ?  960  HIS B CG  1 
ATOM   5027 N ND1 . HIS B 1 710 ? 22.878  33.249  79.564  1.00 111.90 ?  960  HIS B ND1 1 
ATOM   5028 C CD2 . HIS B 1 710 ? 23.988  31.946  80.920  1.00 98.31  ?  960  HIS B CD2 1 
ATOM   5029 C CE1 . HIS B 1 710 ? 23.616  34.027  80.336  1.00 104.87 ?  960  HIS B CE1 1 
ATOM   5030 N NE2 . HIS B 1 710 ? 24.298  33.261  81.168  1.00 100.99 ?  960  HIS B NE2 1 
ATOM   5031 N N   . ILE B 1 711 ? 24.056  28.747  81.512  1.00 81.85  ?  961  ILE B N   1 
ATOM   5032 C CA  . ILE B 1 711 ? 24.085  28.093  82.814  1.00 81.87  ?  961  ILE B CA  1 
ATOM   5033 C C   . ILE B 1 711 ? 24.703  29.036  83.837  1.00 83.03  ?  961  ILE B C   1 
ATOM   5034 O O   . ILE B 1 711 ? 25.651  29.768  83.531  1.00 86.32  ?  961  ILE B O   1 
ATOM   5035 C CB  . ILE B 1 711 ? 24.864  26.762  82.751  1.00 86.98  ?  961  ILE B CB  1 
ATOM   5036 C CG1 . ILE B 1 711 ? 24.306  25.879  81.633  1.00 91.35  ?  961  ILE B CG1 1 
ATOM   5037 C CG2 . ILE B 1 711 ? 24.794  26.028  84.082  1.00 83.36  ?  961  ILE B CG2 1 
ATOM   5038 C CD1 . ILE B 1 711 ? 24.951  24.516  81.549  1.00 96.71  ?  961  ILE B CD1 1 
ATOM   5039 N N   . ASN B 1 712 ? 24.157  29.018  85.052  1.00 79.36  ?  962  ASN B N   1 
ATOM   5040 C CA  . ASN B 1 712 ? 24.663  29.804  86.169  1.00 72.61  ?  962  ASN B CA  1 
ATOM   5041 C C   . ASN B 1 712 ? 24.950  28.863  87.330  1.00 67.70  ?  962  ASN B C   1 
ATOM   5042 O O   . ASN B 1 712 ? 24.122  28.005  87.653  1.00 76.28  ?  962  ASN B O   1 
ATOM   5043 C CB  . ASN B 1 712 ? 23.658  30.882  86.587  1.00 80.10  ?  962  ASN B CB  1 
ATOM   5044 C CG  . ASN B 1 712 ? 24.279  31.951  87.462  1.00 77.50  ?  962  ASN B CG  1 
ATOM   5045 O OD1 . ASN B 1 712 ? 24.362  31.802  88.681  1.00 82.24  ?  962  ASN B OD1 1 
ATOM   5046 N ND2 . ASN B 1 712 ? 24.716  33.040  86.841  1.00 84.87  ?  962  ASN B ND2 1 
ATOM   5047 N N   . VAL B 1 713 ? 26.118  29.019  87.950  1.00 59.76  ?  963  VAL B N   1 
ATOM   5048 C CA  . VAL B 1 713 ? 26.564  28.140  89.026  1.00 63.03  ?  963  VAL B CA  1 
ATOM   5049 C C   . VAL B 1 713 ? 26.988  28.994  90.213  1.00 59.96  ?  963  VAL B C   1 
ATOM   5050 O O   . VAL B 1 713 ? 27.757  29.948  90.054  1.00 66.54  ?  963  VAL B O   1 
ATOM   5051 C CB  . VAL B 1 713 ? 27.721  27.227  88.577  1.00 66.06  ?  963  VAL B CB  1 
ATOM   5052 C CG1 . VAL B 1 713 ? 28.179  26.341  89.725  1.00 64.59  ?  963  VAL B CG1 1 
ATOM   5053 C CG2 . VAL B 1 713 ? 27.298  26.383  87.384  1.00 63.89  ?  963  VAL B CG2 1 
ATOM   5054 N N   . ILE B 1 714 ? 26.493  28.646  91.399  1.00 69.76  ?  964  ILE B N   1 
ATOM   5055 C CA  . ILE B 1 714 ? 26.817  29.348  92.636  1.00 67.70  ?  964  ILE B CA  1 
ATOM   5056 C C   . ILE B 1 714 ? 27.290  28.321  93.655  1.00 56.74  ?  964  ILE B C   1 
ATOM   5057 O O   . ILE B 1 714 ? 26.550  27.388  93.988  1.00 70.29  ?  964  ILE B O   1 
ATOM   5058 C CB  . ILE B 1 714 ? 25.616  30.133  93.189  1.00 67.19  ?  964  ILE B CB  1 
ATOM   5059 C CG1 . ILE B 1 714 ? 25.223  31.260  92.234  1.00 65.73  ?  964  ILE B CG1 1 
ATOM   5060 C CG2 . ILE B 1 714 ? 25.938  30.694  94.568  1.00 58.49  ?  964  ILE B CG2 1 
ATOM   5061 C CD1 . ILE B 1 714 ? 26.234  32.373  92.172  1.00 62.27  ?  964  ILE B CD1 1 
ATOM   5062 N N   . VAL B 1 715 ? 28.512  28.492  94.147  1.00 60.89  ?  965  VAL B N   1 
ATOM   5063 C CA  . VAL B 1 715 ? 29.052  27.683  95.234  1.00 61.77  ?  965  VAL B CA  1 
ATOM   5064 C C   . VAL B 1 715 ? 29.081  28.554  96.481  1.00 66.34  ?  965  VAL B C   1 
ATOM   5065 O O   . VAL B 1 715 ? 29.727  29.610  96.494  1.00 62.73  ?  965  VAL B O   1 
ATOM   5066 C CB  . VAL B 1 715 ? 30.450  27.138  94.904  1.00 65.15  ?  965  VAL B CB  1 
ATOM   5067 C CG1 . VAL B 1 715 ? 30.977  26.304  96.061  1.00 56.32  ?  965  VAL B CG1 1 
ATOM   5068 C CG2 . VAL B 1 715 ? 30.411  26.318  93.623  1.00 59.13  ?  965  VAL B CG2 1 
ATOM   5069 N N   . GLY B 1 716 ? 28.377  28.117  97.524  1.00 66.49  ?  966  GLY B N   1 
ATOM   5070 C CA  . GLY B 1 716 ? 28.285  28.916  98.731  1.00 56.27  ?  966  GLY B CA  1 
ATOM   5071 C C   . GLY B 1 716 ? 29.638  29.129  99.381  1.00 63.29  ?  966  GLY B C   1 
ATOM   5072 O O   . GLY B 1 716 ? 30.522  28.270  99.336  1.00 70.64  ?  966  GLY B O   1 
ATOM   5073 N N   . ARG B 1 717 ? 29.795  30.303  99.996  1.00 66.58  ?  967  ARG B N   1 
ATOM   5074 C CA  . ARG B 1 717 ? 31.073  30.656  100.607 1.00 63.68  ?  967  ARG B CA  1 
ATOM   5075 C C   . ARG B 1 717 ? 31.349  29.819  101.850 1.00 68.46  ?  967  ARG B C   1 
ATOM   5076 O O   . ARG B 1 717 ? 32.496  29.429  102.099 1.00 73.80  ?  967  ARG B O   1 
ATOM   5077 C CB  . ARG B 1 717 ? 31.092  32.147  100.943 1.00 66.78  ?  967  ARG B CB  1 
ATOM   5078 C CG  . ARG B 1 717 ? 32.312  32.608  101.723 1.00 89.63  ?  967  ARG B CG  1 
ATOM   5079 C CD  . ARG B 1 717 ? 31.889  33.281  103.016 1.00 79.25  ?  967  ARG B CD  1 
ATOM   5080 N NE  . ARG B 1 717 ? 30.927  34.352  102.774 1.00 96.00  ?  967  ARG B NE  1 
ATOM   5081 C CZ  . ARG B 1 717 ? 30.119  34.854  103.702 1.00 84.30  ?  967  ARG B CZ  1 
ATOM   5082 N NH1 . ARG B 1 717 ? 30.150  34.376  104.938 1.00 67.82  1  967  ARG B NH1 1 
ATOM   5083 N NH2 . ARG B 1 717 ? 29.274  35.828  103.391 1.00 87.01  ?  967  ARG B NH2 1 
ATOM   5084 N N   . ASP B 1 718 ? 30.315  29.526  102.639 1.00 73.24  ?  968  ASP B N   1 
ATOM   5085 C CA  . ASP B 1 718 ? 30.490  28.801  103.900 1.00 75.44  ?  968  ASP B CA  1 
ATOM   5086 C C   . ASP B 1 718 ? 30.345  27.297  103.669 1.00 73.11  ?  968  ASP B C   1 
ATOM   5087 O O   . ASP B 1 718 ? 29.347  26.663  104.019 1.00 83.53  ?  968  ASP B O   1 
ATOM   5088 C CB  . ASP B 1 718 ? 29.505  29.304  104.948 1.00 82.03  ?  968  ASP B CB  1 
ATOM   5089 C CG  . ASP B 1 718 ? 29.987  30.562  105.643 1.00 83.68  ?  968  ASP B CG  1 
ATOM   5090 O OD1 . ASP B 1 718 ? 29.441  31.650  105.364 1.00 96.97  ?  968  ASP B OD1 1 
ATOM   5091 O OD2 . ASP B 1 718 ? 30.924  30.461  106.463 1.00 95.71  -1 968  ASP B OD2 1 
ATOM   5092 N N   . LEU B 1 719 ? 31.386  26.727  103.069 1.00 81.02  ?  969  LEU B N   1 
ATOM   5093 C CA  . LEU B 1 719 ? 31.463  25.283  102.912 1.00 67.68  ?  969  LEU B CA  1 
ATOM   5094 C C   . LEU B 1 719 ? 31.802  24.622  104.243 1.00 72.27  ?  969  LEU B C   1 
ATOM   5095 O O   . LEU B 1 719 ? 32.483  25.199  105.095 1.00 89.23  ?  969  LEU B O   1 
ATOM   5096 C CB  . LEU B 1 719 ? 32.515  24.913  101.866 1.00 64.98  ?  969  LEU B CB  1 
ATOM   5097 C CG  . LEU B 1 719 ? 32.219  25.281  100.412 1.00 60.93  ?  969  LEU B CG  1 
ATOM   5098 C CD1 . LEU B 1 719 ? 33.507  25.322  99.611  1.00 66.36  ?  969  LEU B CD1 1 
ATOM   5099 C CD2 . LEU B 1 719 ? 31.242  24.289  99.801  1.00 61.91  ?  969  LEU B CD2 1 
ATOM   5100 N N   . SER B 1 720 ? 31.314  23.395  104.418 1.00 79.07  ?  970  SER B N   1 
ATOM   5101 C CA  . SER B 1 720 ? 31.614  22.604  105.610 1.00 78.22  ?  970  SER B CA  1 
ATOM   5102 C C   . SER B 1 720 ? 32.938  21.885  105.372 1.00 79.02  ?  970  SER B C   1 
ATOM   5103 O O   . SER B 1 720 ? 32.997  20.680  105.115 1.00 89.29  ?  970  SER B O   1 
ATOM   5104 C CB  . SER B 1 720 ? 30.482  21.630  105.912 1.00 75.26  ?  970  SER B CB  1 
ATOM   5105 O OG  . SER B 1 720 ? 29.256  22.314  106.116 1.00 78.19  ?  970  SER B OG  1 
ATOM   5106 N N   . PHE B 1 721 ? 34.026  22.656  105.466 1.00 83.24  ?  971  PHE B N   1 
ATOM   5107 C CA  . PHE B 1 721 ? 35.348  22.129  105.139 1.00 84.84  ?  971  PHE B CA  1 
ATOM   5108 C C   . PHE B 1 721 ? 35.721  20.955  106.035 1.00 95.75  ?  971  PHE B C   1 
ATOM   5109 O O   . PHE B 1 721 ? 36.349  19.993  105.579 1.00 90.17  ?  971  PHE B O   1 
ATOM   5110 C CB  . PHE B 1 721 ? 36.399  23.232  105.253 1.00 73.55  ?  971  PHE B CB  1 
ATOM   5111 C CG  . PHE B 1 721 ? 36.304  24.279  104.180 1.00 78.35  ?  971  PHE B CG  1 
ATOM   5112 C CD1 . PHE B 1 721 ? 35.578  25.440  104.387 1.00 78.12  ?  971  PHE B CD1 1 
ATOM   5113 C CD2 . PHE B 1 721 ? 36.948  24.105  102.967 1.00 74.30  ?  971  PHE B CD2 1 
ATOM   5114 C CE1 . PHE B 1 721 ? 35.493  26.406  103.401 1.00 78.81  ?  971  PHE B CE1 1 
ATOM   5115 C CE2 . PHE B 1 721 ? 36.867  25.066  101.978 1.00 74.34  ?  971  PHE B CE2 1 
ATOM   5116 C CZ  . PHE B 1 721 ? 36.138  26.218  102.195 1.00 79.71  ?  971  PHE B CZ  1 
ATOM   5117 N N   . GLN B 1 722 ? 35.340  21.014  107.313 1.00 92.06  ?  972  GLN B N   1 
ATOM   5118 C CA  . GLN B 1 722 ? 35.729  19.961  108.246 1.00 92.08  ?  972  GLN B CA  1 
ATOM   5119 C C   . GLN B 1 722 ? 35.063  18.636  107.897 1.00 95.67  ?  972  GLN B C   1 
ATOM   5120 O O   . GLN B 1 722 ? 35.707  17.581  107.936 1.00 98.69  ?  972  GLN B O   1 
ATOM   5121 C CB  . GLN B 1 722 ? 35.388  20.381  109.676 1.00 102.33 ?  972  GLN B CB  1 
ATOM   5122 C CG  . GLN B 1 722 ? 36.448  20.016  110.705 1.00 103.40 ?  972  GLN B CG  1 
ATOM   5123 C CD  . GLN B 1 722 ? 36.476  18.534  111.023 1.00 114.60 ?  972  GLN B CD  1 
ATOM   5124 O OE1 . GLN B 1 722 ? 35.459  17.949  111.396 1.00 121.80 ?  972  GLN B OE1 1 
ATOM   5125 N NE2 . GLN B 1 722 ? 37.644  17.918  110.877 1.00 107.44 ?  972  GLN B NE2 1 
ATOM   5126 N N   . ASP B 1 723 ? 33.776  18.668  107.545 1.00 90.68  ?  973  ASP B N   1 
ATOM   5127 C CA  . ASP B 1 723 ? 33.064  17.449  107.189 1.00 94.88  ?  973  ASP B CA  1 
ATOM   5128 C C   . ASP B 1 723 ? 33.359  16.990  105.767 1.00 94.97  ?  973  ASP B C   1 
ATOM   5129 O O   . ASP B 1 723 ? 33.170  15.808  105.460 1.00 100.32 ?  973  ASP B O   1 
ATOM   5130 C CB  . ASP B 1 723 ? 31.556  17.651  107.363 1.00 90.04  ?  973  ASP B CB  1 
ATOM   5131 C CG  . ASP B 1 723 ? 30.777  16.354  107.256 1.00 95.39  ?  973  ASP B CG  1 
ATOM   5132 O OD1 . ASP B 1 723 ? 30.827  15.549  108.211 1.00 100.54 ?  973  ASP B OD1 1 
ATOM   5133 O OD2 . ASP B 1 723 ? 30.116  16.137  106.218 1.00 83.78  -1 973  ASP B OD2 1 
ATOM   5134 N N   . LEU B 1 724 ? 33.815  17.889  104.896 1.00 95.94  ?  974  LEU B N   1 
ATOM   5135 C CA  . LEU B 1 724 ? 34.128  17.536  103.518 1.00 95.14  ?  974  LEU B CA  1 
ATOM   5136 C C   . LEU B 1 724 ? 35.571  17.087  103.328 1.00 99.80  ?  974  LEU B C   1 
ATOM   5137 O O   . LEU B 1 724 ? 35.913  16.606  102.243 1.00 92.58  ?  974  LEU B O   1 
ATOM   5138 C CB  . LEU B 1 724 ? 33.837  18.722  102.589 1.00 76.77  ?  974  LEU B CB  1 
ATOM   5139 C CG  . LEU B 1 724 ? 32.367  19.100  102.393 1.00 74.14  ?  974  LEU B CG  1 
ATOM   5140 C CD1 . LEU B 1 724 ? 32.242  20.373  101.568 1.00 68.05  ?  974  LEU B CD1 1 
ATOM   5141 C CD2 . LEU B 1 724 ? 31.602  17.959  101.741 1.00 77.54  ?  974  LEU B CD2 1 
ATOM   5142 N N   . SER B 1 725 ? 36.420  17.227  104.350 1.00 96.79  ?  975  SER B N   1 
ATOM   5143 C CA  . SER B 1 725 ? 37.823  16.838  104.262 1.00 97.47  ?  975  SER B CA  1 
ATOM   5144 C C   . SER B 1 725 ? 38.192  15.766  105.281 1.00 100.57 ?  975  SER B C   1 
ATOM   5145 O O   . SER B 1 725 ? 39.362  15.657  105.659 1.00 100.54 ?  975  SER B O   1 
ATOM   5146 C CB  . SER B 1 725 ? 38.732  18.056  104.437 1.00 92.47  ?  975  SER B CB  1 
ATOM   5147 O OG  . SER B 1 725 ? 38.572  18.635  105.720 1.00 106.73 ?  975  SER B OG  1 
ATOM   5148 N N   . GLU B 1 726 ? 37.219  14.975  105.736 1.00 107.39 ?  976  GLU B N   1 
ATOM   5149 C CA  . GLU B 1 726 ? 37.485  13.929  106.717 1.00 113.14 ?  976  GLU B CA  1 
ATOM   5150 C C   . GLU B 1 726 ? 38.481  12.913  106.175 1.00 115.94 ?  976  GLU B C   1 
ATOM   5151 O O   . GLU B 1 726 ? 39.637  12.876  106.610 1.00 120.60 ?  976  GLU B O   1 
ATOM   5152 C CB  . GLU B 1 726 ? 36.185  13.234  107.128 1.00 114.42 ?  976  GLU B CB  1 
ATOM   5153 C CG  . GLU B 1 726 ? 35.351  14.020  108.130 1.00 119.48 ?  976  GLU B CG  1 
ATOM   5154 C CD  . GLU B 1 726 ? 36.002  14.100  109.499 1.00 130.12 ?  976  GLU B CD  1 
ATOM   5155 O OE1 . GLU B 1 726 ? 35.334  14.558  110.450 1.00 136.26 ?  976  GLU B OE1 1 
ATOM   5156 O OE2 . GLU B 1 726 ? 37.180  13.701  109.626 1.00 124.05 -1 976  GLU B OE2 1 
ATOM   5157 N N   . THR B 1 727 ? 38.043  12.082  105.229 1.00 103.48 ?  977  THR B N   1 
ATOM   5158 C CA  . THR B 1 727 ? 38.904  11.115  104.551 1.00 95.83  ?  977  THR B CA  1 
ATOM   5159 C C   . THR B 1 727 ? 38.970  11.513  103.083 1.00 94.35  ?  977  THR B C   1 
ATOM   5160 O O   . THR B 1 727 ? 38.157  11.049  102.268 1.00 95.10  ?  977  THR B O   1 
ATOM   5161 C CB  . THR B 1 727 ? 38.382  9.689   104.714 1.00 116.44 ?  977  THR B CB  1 
ATOM   5162 O OG1 . THR B 1 727 ? 37.185  9.525   103.943 1.00 123.99 ?  977  THR B OG1 1 
ATOM   5163 C CG2 . THR B 1 727 ? 38.079  9.397   106.176 1.00 97.35  ?  977  THR B CG2 1 
ATOM   5164 N N   . PRO B 1 728 ? 39.911  12.379  102.704 1.00 96.36  ?  978  PRO B N   1 
ATOM   5165 C CA  . PRO B 1 728 ? 39.983  12.823  101.308 1.00 89.46  ?  978  PRO B CA  1 
ATOM   5166 C C   . PRO B 1 728 ? 40.264  11.660  100.368 1.00 101.78 ?  978  PRO B C   1 
ATOM   5167 O O   . PRO B 1 728 ? 41.041  10.756  100.681 1.00 100.01 ?  978  PRO B O   1 
ATOM   5168 C CB  . PRO B 1 728 ? 41.138  13.832  101.315 1.00 89.87  ?  978  PRO B CB  1 
ATOM   5169 C CG  . PRO B 1 728 ? 41.276  14.253  102.743 1.00 97.49  ?  978  PRO B CG  1 
ATOM   5170 C CD  . PRO B 1 728 ? 40.911  13.048  103.552 1.00 95.35  ?  978  PRO B CD  1 
ATOM   5171 N N   . CYS B 1 729 ? 39.610  11.688  99.210  1.00 90.32  ?  979  CYS B N   1 
ATOM   5172 C CA  . CYS B 1 729 ? 39.801  10.642  98.213  1.00 88.32  ?  979  CYS B CA  1 
ATOM   5173 C C   . CYS B 1 729 ? 41.228  10.696  97.682  1.00 108.17 ?  979  CYS B C   1 
ATOM   5174 O O   . CYS B 1 729 ? 41.639  11.697  97.084  1.00 99.98  ?  979  CYS B O   1 
ATOM   5175 C CB  . CYS B 1 729 ? 38.794  10.801  97.077  1.00 80.18  ?  979  CYS B CB  1 
ATOM   5176 S SG  . CYS B 1 729 ? 37.078  10.945  97.627  1.00 105.02 ?  979  CYS B SG  1 
ATOM   5177 N N   . GLN B 1 730 ? 41.982  9.625   97.905  1.00 111.83 ?  980  GLN B N   1 
ATOM   5178 C CA  . GLN B 1 730 ? 43.381  9.539   97.506  1.00 106.31 ?  980  GLN B CA  1 
ATOM   5179 C C   . GLN B 1 730 ? 43.503  8.611   96.307  1.00 104.03 ?  980  GLN B C   1 
ATOM   5180 O O   . GLN B 1 730 ? 43.116  7.441   96.385  1.00 109.31 ?  980  GLN B O   1 
ATOM   5181 C CB  . GLN B 1 730 ? 44.250  9.037   98.659  1.00 110.42 ?  980  GLN B CB  1 
ATOM   5182 C CG  . GLN B 1 730 ? 44.465  10.061  99.756  1.00 115.86 ?  980  GLN B CG  1 
ATOM   5183 C CD  . GLN B 1 730 ? 45.221  11.280  99.265  1.00 131.35 ?  980  GLN B CD  1 
ATOM   5184 O OE1 . GLN B 1 730 ? 46.007  11.199  98.320  1.00 137.09 ?  980  GLN B OE1 1 
ATOM   5185 N NE2 . GLN B 1 730 ? 44.984  12.421  99.902  1.00 123.33 ?  980  GLN B NE2 1 
ATOM   5186 N N   . VAL B 1 731 ? 44.045  9.132   95.209  1.00 95.64  ?  981  VAL B N   1 
ATOM   5187 C CA  . VAL B 1 731 ? 44.272  8.351   94.001  1.00 104.17 ?  981  VAL B CA  1 
ATOM   5188 C C   . VAL B 1 731 ? 45.772  8.241   93.766  1.00 116.63 ?  981  VAL B C   1 
ATOM   5189 O O   . VAL B 1 731 ? 46.551  9.129   94.135  1.00 102.56 ?  981  VAL B O   1 
ATOM   5190 C CB  . VAL B 1 731 ? 43.558  8.960   92.773  1.00 92.89  ?  981  VAL B CB  1 
ATOM   5191 C CG1 . VAL B 1 731 ? 42.127  9.343   93.124  1.00 91.05  ?  981  VAL B CG1 1 
ATOM   5192 C CG2 . VAL B 1 731 ? 44.324  10.160  92.231  1.00 84.03  ?  981  VAL B CG2 1 
ATOM   5193 N N   . ASP B 1 732 ? 46.180  7.124   93.166  1.00 107.84 ?  982  ASP B N   1 
ATOM   5194 C CA  . ASP B 1 732 ? 47.567  6.886   92.798  1.00 100.98 ?  982  ASP B CA  1 
ATOM   5195 C C   . ASP B 1 732 ? 47.622  6.527   91.321  1.00 100.92 ?  982  ASP B C   1 
ATOM   5196 O O   . ASP B 1 732 ? 46.787  5.762   90.829  1.00 100.38 ?  982  ASP B O   1 
ATOM   5197 C CB  . ASP B 1 732 ? 48.195  5.764   93.634  1.00 107.49 ?  982  ASP B CB  1 
ATOM   5198 C CG  . ASP B 1 732 ? 49.655  6.024   93.954  1.00 131.51 ?  982  ASP B CG  1 
ATOM   5199 O OD1 . ASP B 1 732 ? 50.116  5.583   95.028  1.00 137.23 ?  982  ASP B OD1 1 
ATOM   5200 O OD2 . ASP B 1 732 ? 50.333  6.690   93.142  1.00 129.80 -1 982  ASP B OD2 1 
ATOM   5201 N N   . LEU B 1 733 ? 48.604  7.084   90.616  1.00 106.22 ?  983  LEU B N   1 
ATOM   5202 C CA  . LEU B 1 733 ? 48.690  6.973   89.166  1.00 106.62 ?  983  LEU B CA  1 
ATOM   5203 C C   . LEU B 1 733 ? 49.975  6.262   88.769  1.00 107.19 ?  983  LEU B C   1 
ATOM   5204 O O   . LEU B 1 733 ? 51.050  6.566   89.298  1.00 111.93 ?  983  LEU B O   1 
ATOM   5205 C CB  . LEU B 1 733 ? 48.627  8.356   88.509  1.00 100.56 ?  983  LEU B CB  1 
ATOM   5206 C CG  . LEU B 1 733 ? 47.253  8.888   88.090  1.00 105.17 ?  983  LEU B CG  1 
ATOM   5207 C CD1 . LEU B 1 733 ? 46.254  8.838   89.233  1.00 109.92 ?  983  LEU B CD1 1 
ATOM   5208 C CD2 . LEU B 1 733 ? 47.378  10.306  87.563  1.00 112.30 ?  983  LEU B CD2 1 
ATOM   5209 N N   . THR B 1 734 ? 49.858  5.310   87.843  1.00 116.48 ?  984  THR B N   1 
ATOM   5210 C CA  . THR B 1 734 ? 51.002  4.613   87.264  1.00 114.29 ?  984  THR B CA  1 
ATOM   5211 C C   . THR B 1 734 ? 50.822  4.579   85.754  1.00 113.90 ?  984  THR B C   1 
ATOM   5212 O O   . THR B 1 734 ? 49.805  4.079   85.262  1.00 116.19 ?  984  THR B O   1 
ATOM   5213 C CB  . THR B 1 734 ? 51.136  3.185   87.808  1.00 119.79 ?  984  THR B CB  1 
ATOM   5214 O OG1 . THR B 1 734 ? 50.097  2.363   87.262  1.00 129.57 ?  984  THR B OG1 1 
ATOM   5215 C CG2 . THR B 1 734 ? 51.047  3.162   89.329  1.00 114.20 ?  984  THR B CG2 1 
ATOM   5216 N N   . THR B 1 735 ? 51.802  5.106   85.022  1.00 111.72 ?  985  THR B N   1 
ATOM   5217 C CA  . THR B 1 735 ? 51.760  5.067   83.565  1.00 116.62 ?  985  THR B CA  1 
ATOM   5218 C C   . THR B 1 735 ? 52.193  3.690   83.078  1.00 126.44 ?  985  THR B C   1 
ATOM   5219 O O   . THR B 1 735 ? 53.250  3.188   83.472  1.00 123.33 ?  985  THR B O   1 
ATOM   5220 C CB  . THR B 1 735 ? 52.657  6.153   82.971  1.00 112.57 ?  985  THR B CB  1 
ATOM   5221 O OG1 . THR B 1 735 ? 52.288  7.427   83.513  1.00 122.49 ?  985  THR B OG1 1 
ATOM   5222 C CG2 . THR B 1 735 ? 52.510  6.195   81.458  1.00 120.04 ?  985  THR B CG2 1 
ATOM   5223 N N   . THR B 1 736 ? 51.375  3.079   82.220  1.00 116.00 ?  986  THR B N   1 
ATOM   5224 C CA  . THR B 1 736 ? 51.586  1.694   81.811  1.00 123.67 ?  986  THR B CA  1 
ATOM   5225 C C   . THR B 1 736 ? 51.817  1.553   80.312  1.00 122.20 ?  986  THR B C   1 
ATOM   5226 O O   . THR B 1 736 ? 52.854  1.021   79.905  1.00 121.46 ?  986  THR B O   1 
ATOM   5227 C CB  . THR B 1 736 ? 50.394  0.832   82.248  1.00 120.53 ?  986  THR B CB  1 
ATOM   5228 O OG1 . THR B 1 736 ? 49.188  1.356   81.679  1.00 128.65 ?  986  THR B OG1 1 
ATOM   5229 C CG2 . THR B 1 736 ? 50.272  0.822   83.764  1.00 124.01 ?  986  THR B CG2 1 
ATOM   5230 N N   . SER B 1 737 ? 50.884  2.004   79.476  1.00 125.96 ?  987  SER B N   1 
ATOM   5231 C CA  . SER B 1 737 ? 50.948  1.768   78.041  1.00 119.07 ?  987  SER B CA  1 
ATOM   5232 C C   . SER B 1 737 ? 50.702  3.068   77.287  1.00 116.12 ?  987  SER B C   1 
ATOM   5233 O O   . SER B 1 737 ? 50.241  4.065   77.849  1.00 115.23 ?  987  SER B O   1 
ATOM   5234 C CB  . SER B 1 737 ? 49.929  0.705   77.609  1.00 119.38 ?  987  SER B CB  1 
ATOM   5235 O OG  . SER B 1 737 ? 49.974  -0.421  78.468  1.00 127.76 ?  987  SER B OG  1 
ATOM   5236 N N   . ILE B 1 738 ? 51.017  3.042   75.992  1.00 117.22 ?  988  ILE B N   1 
ATOM   5237 C CA  . ILE B 1 738 ? 50.803  4.190   75.117  1.00 120.21 ?  988  ILE B CA  1 
ATOM   5238 C C   . ILE B 1 738 ? 50.685  3.717   73.673  1.00 119.14 ?  988  ILE B C   1 
ATOM   5239 O O   . ILE B 1 738 ? 51.535  2.968   73.177  1.00 119.53 ?  988  ILE B O   1 
ATOM   5240 C CB  . ILE B 1 738 ? 51.929  5.232   75.273  1.00 113.55 ?  988  ILE B CB  1 
ATOM   5241 C CG1 . ILE B 1 738 ? 51.797  6.330   74.215  1.00 118.15 ?  988  ILE B CG1 1 
ATOM   5242 C CG2 . ILE B 1 738 ? 53.299  4.570   75.203  1.00 114.63 ?  988  ILE B CG2 1 
ATOM   5243 C CD1 . ILE B 1 738 ? 52.860  7.403   74.314  1.00 118.51 ?  988  ILE B CD1 1 
ATOM   5244 N N   . ASP B 1 739 ? 49.626  4.144   72.993  1.00 120.13 ?  989  ASP B N   1 
ATOM   5245 C CA  . ASP B 1 739 ? 49.395  3.826   71.593  1.00 118.48 ?  989  ASP B CA  1 
ATOM   5246 C C   . ASP B 1 739 ? 49.470  5.100   70.759  1.00 118.27 ?  989  ASP B C   1 
ATOM   5247 O O   . ASP B 1 739 ? 49.486  6.216   71.284  1.00 122.50 ?  989  ASP B O   1 
ATOM   5248 C CB  . ASP B 1 739 ? 48.040  3.126   71.413  1.00 123.68 ?  989  ASP B CB  1 
ATOM   5249 C CG  . ASP B 1 739 ? 47.881  2.499   70.039  1.00 141.02 ?  989  ASP B CG  1 
ATOM   5250 O OD1 . ASP B 1 739 ? 47.617  3.245   69.071  1.00 146.69 ?  989  ASP B OD1 1 
ATOM   5251 O OD2 . ASP B 1 739 ? 48.039  1.264   69.927  1.00 127.73 -1 989  ASP B OD2 1 
ATOM   5252 N N   . GLY B 1 740 ? 49.524  4.923   69.442  1.00 128.69 ?  990  GLY B N   1 
ATOM   5253 C CA  . GLY B 1 740 ? 49.683  6.053   68.553  1.00 129.74 ?  990  GLY B CA  1 
ATOM   5254 C C   . GLY B 1 740 ? 51.106  6.590   68.586  1.00 137.77 ?  990  GLY B C   1 
ATOM   5255 O O   . GLY B 1 740 ? 52.017  6.008   69.175  1.00 140.21 ?  990  GLY B O   1 
ATOM   5256 N N   . ALA B 1 741 ? 51.282  7.731   67.931  1.00 137.75 ?  991  ALA B N   1 
ATOM   5257 C CA  . ALA B 1 741 ? 52.567  8.414   67.872  1.00 144.31 ?  991  ALA B CA  1 
ATOM   5258 C C   . ALA B 1 741 ? 52.425  9.828   68.430  1.00 143.79 ?  991  ALA B C   1 
ATOM   5259 O O   . ALA B 1 741 ? 51.365  10.226  68.919  1.00 144.83 ?  991  ALA B O   1 
ATOM   5260 C CB  . ALA B 1 741 ? 53.111  8.435   66.441  1.00 153.51 ?  991  ALA B CB  1 
ATOM   5261 N N   . TRP B 1 742 ? 53.512  10.593  68.343  1.00 141.52 ?  992  TRP B N   1 
ATOM   5262 C CA  . TRP B 1 742 ? 53.570  11.903  68.980  1.00 142.23 ?  992  TRP B CA  1 
ATOM   5263 C C   . TRP B 1 742 ? 53.162  13.018  68.025  1.00 147.44 ?  992  TRP B C   1 
ATOM   5264 O O   . TRP B 1 742 ? 52.390  12.795  67.086  1.00 154.58 ?  992  TRP B O   1 
ATOM   5265 C CB  . TRP B 1 742 ? 54.979  12.160  69.527  1.00 133.82 ?  992  TRP B CB  1 
ATOM   5266 C CG  . TRP B 1 742 ? 56.059  12.350  68.482  1.00 141.08 ?  992  TRP B CG  1 
ATOM   5267 C CD1 . TRP B 1 742 ? 55.922  12.289  67.121  1.00 153.25 ?  992  TRP B CD1 1 
ATOM   5268 C CD2 . TRP B 1 742 ? 57.439  12.641  68.727  1.00 153.94 ?  992  TRP B CD2 1 
ATOM   5269 N NE1 . TRP B 1 742 ? 57.127  12.525  66.512  1.00 149.78 ?  992  TRP B NE1 1 
ATOM   5270 C CE2 . TRP B 1 742 ? 58.076  12.741  67.474  1.00 146.08 ?  992  TRP B CE2 1 
ATOM   5271 C CE3 . TRP B 1 742 ? 58.198  12.824  69.885  1.00 161.10 ?  992  TRP B CE3 1 
ATOM   5272 C CZ2 . TRP B 1 742 ? 59.434  13.017  67.348  1.00 137.70 ?  992  TRP B CZ2 1 
ATOM   5273 C CZ3 . TRP B 1 742 ? 59.544  13.093  69.756  1.00 153.89 ?  992  TRP B CZ3 1 
ATOM   5274 C CH2 . TRP B 1 742 ? 60.149  13.190  68.498  1.00 141.87 ?  992  TRP B CH2 1 
ATOM   5275 N N   . GLY B 1 743 ? 53.681  14.218  68.260  1.00 138.79 ?  993  GLY B N   1 
ATOM   5276 C CA  . GLY B 1 743 ? 53.485  15.327  67.349  1.00 134.35 ?  993  GLY B CA  1 
ATOM   5277 C C   . GLY B 1 743 ? 52.068  15.870  67.381  1.00 146.66 ?  993  GLY B C   1 
ATOM   5278 O O   . GLY B 1 743 ? 51.175  15.364  68.059  1.00 145.04 ?  993  GLY B O   1 
ATOM   5279 N N   . SER B 1 744 ? 51.875  16.940  66.615  1.00 151.72 ?  994  SER B N   1 
ATOM   5280 C CA  . SER B 1 744 ? 50.581  17.593  66.490  1.00 150.48 ?  994  SER B CA  1 
ATOM   5281 C C   . SER B 1 744 ? 49.733  17.005  65.369  1.00 154.28 ?  994  SER B C   1 
ATOM   5282 O O   . SER B 1 744 ? 48.727  17.612  64.987  1.00 149.58 ?  994  SER B O   1 
ATOM   5283 C CB  . SER B 1 744 ? 50.769  19.094  66.259  1.00 146.37 ?  994  SER B CB  1 
ATOM   5284 O OG  . SER B 1 744 ? 51.364  19.344  64.998  1.00 148.39 ?  994  SER B OG  1 
ATOM   5285 N N   . GLY B 1 745 ? 50.107  15.843  64.842  1.00 150.72 ?  995  GLY B N   1 
ATOM   5286 C CA  . GLY B 1 745 ? 49.419  15.295  63.691  1.00 151.41 ?  995  GLY B CA  1 
ATOM   5287 C C   . GLY B 1 745 ? 48.548  14.088  63.974  1.00 156.46 ?  995  GLY B C   1 
ATOM   5288 O O   . GLY B 1 745 ? 47.329  14.139  63.783  1.00 149.74 ?  995  GLY B O   1 
ATOM   5289 N N   . VAL B 1 746 ? 49.156  12.998  64.434  1.00 166.45 ?  996  VAL B N   1 
ATOM   5290 C CA  . VAL B 1 746 ? 48.438  11.732  64.521  1.00 161.72 ?  996  VAL B CA  1 
ATOM   5291 C C   . VAL B 1 746 ? 47.691  11.564  65.844  1.00 152.42 ?  996  VAL B C   1 
ATOM   5292 O O   . VAL B 1 746 ? 46.697  10.832  65.898  1.00 158.81 ?  996  VAL B O   1 
ATOM   5293 C CB  . VAL B 1 746 ? 49.408  10.562  64.287  1.00 156.59 ?  996  VAL B CB  1 
ATOM   5294 C CG1 . VAL B 1 746 ? 50.212  10.783  63.014  1.00 155.09 ?  996  VAL B CG1 1 
ATOM   5295 C CG2 . VAL B 1 746 ? 50.330  10.388  65.478  1.00 152.75 ?  996  VAL B CG2 1 
ATOM   5296 N N   . GLY B 1 747 ? 48.141  12.216  66.914  1.00 135.76 ?  997  GLY B N   1 
ATOM   5297 C CA  . GLY B 1 747 ? 47.541  12.011  68.219  1.00 129.26 ?  997  GLY B CA  1 
ATOM   5298 C C   . GLY B 1 747 ? 47.918  10.674  68.826  1.00 126.58 ?  997  GLY B C   1 
ATOM   5299 O O   . GLY B 1 747 ? 48.380  9.775   68.117  1.00 142.11 ?  997  GLY B O   1 
ATOM   5300 N N   . PHE B 1 748 ? 47.725  10.520  70.135  1.00 115.55 ?  998  PHE B N   1 
ATOM   5301 C CA  . PHE B 1 748 ? 48.120  9.301   70.825  1.00 120.56 ?  998  PHE B CA  1 
ATOM   5302 C C   . PHE B 1 748 ? 47.063  8.926   71.855  1.00 119.74 ?  998  PHE B C   1 
ATOM   5303 O O   . PHE B 1 748 ? 46.176  9.715   72.191  1.00 113.18 ?  998  PHE B O   1 
ATOM   5304 C CB  . PHE B 1 748 ? 49.491  9.454   71.500  1.00 121.24 ?  998  PHE B CB  1 
ATOM   5305 C CG  . PHE B 1 748 ? 49.504  10.435  72.640  1.00 116.13 ?  998  PHE B CG  1 
ATOM   5306 C CD1 . PHE B 1 748 ? 49.691  11.787  72.406  1.00 120.80 ?  998  PHE B CD1 1 
ATOM   5307 C CD2 . PHE B 1 748 ? 49.338  10.002  73.946  1.00 115.53 ?  998  PHE B CD2 1 
ATOM   5308 C CE1 . PHE B 1 748 ? 49.705  12.690  73.452  1.00 117.29 ?  998  PHE B CE1 1 
ATOM   5309 C CE2 . PHE B 1 748 ? 49.350  10.900  74.996  1.00 108.33 ?  998  PHE B CE2 1 
ATOM   5310 C CZ  . PHE B 1 748 ? 49.534  12.246  74.749  1.00 107.66 ?  998  PHE B CZ  1 
ATOM   5311 N N   . ASN B 1 749 ? 47.174  7.698   72.355  1.00 124.47 ?  999  ASN B N   1 
ATOM   5312 C CA  . ASN B 1 749 ? 46.332  7.188   73.428  1.00 122.28 ?  999  ASN B CA  1 
ATOM   5313 C C   . ASN B 1 749 ? 47.217  6.744   74.584  1.00 119.55 ?  999  ASN B C   1 
ATOM   5314 O O   . ASN B 1 749 ? 48.260  6.117   74.373  1.00 121.16 ?  999  ASN B O   1 
ATOM   5315 C CB  . ASN B 1 749 ? 45.462  6.020   72.948  1.00 125.45 ?  999  ASN B CB  1 
ATOM   5316 C CG  . ASN B 1 749 ? 44.603  5.436   74.057  1.00 123.63 ?  999  ASN B CG  1 
ATOM   5317 O OD1 . ASN B 1 749 ? 43.468  5.864   74.268  1.00 124.84 ?  999  ASN B OD1 1 
ATOM   5318 N ND2 . ASN B 1 749 ? 45.140  4.450   74.768  1.00 124.79 ?  999  ASN B ND2 1 
ATOM   5319 N N   . LEU B 1 750 ? 46.799  7.071   75.804  1.00 115.90 ?  1000 LEU B N   1 
ATOM   5320 C CA  . LEU B 1 750 ? 47.565  6.763   77.006  1.00 112.65 ?  1000 LEU B CA  1 
ATOM   5321 C C   . LEU B 1 750 ? 46.716  5.899   77.926  1.00 106.56 ?  1000 LEU B C   1 
ATOM   5322 O O   . LEU B 1 750 ? 45.633  6.317   78.351  1.00 113.84 ?  1000 LEU B O   1 
ATOM   5323 C CB  . LEU B 1 750 ? 48.003  8.046   77.720  1.00 112.39 ?  1000 LEU B CB  1 
ATOM   5324 C CG  . LEU B 1 750 ? 49.396  8.071   78.359  1.00 112.51 ?  1000 LEU B CG  1 
ATOM   5325 C CD1 . LEU B 1 750 ? 49.648  9.412   79.032  1.00 98.38  ?  1000 LEU B CD1 1 
ATOM   5326 C CD2 . LEU B 1 750 ? 49.580  6.933   79.350  1.00 121.64 ?  1000 LEU B CD2 1 
ATOM   5327 N N   . ILE B 1 751 ? 47.208  4.701   78.231  1.00 113.67 ?  1001 ILE B N   1 
ATOM   5328 C CA  . ILE B 1 751 ? 46.574  3.802   79.189  1.00 124.94 ?  1001 ILE B CA  1 
ATOM   5329 C C   . ILE B 1 751 ? 47.213  4.019   80.552  1.00 116.46 ?  1001 ILE B C   1 
ATOM   5330 O O   . ILE B 1 751 ? 48.440  4.121   80.667  1.00 113.60 ?  1001 ILE B O   1 
ATOM   5331 C CB  . ILE B 1 751 ? 46.705  2.334   78.739  1.00 118.76 ?  1001 ILE B CB  1 
ATOM   5332 C CG1 . ILE B 1 751 ? 46.007  2.124   77.395  1.00 110.16 ?  1001 ILE B CG1 1 
ATOM   5333 C CG2 . ILE B 1 751 ? 46.139  1.391   79.796  1.00 114.75 ?  1001 ILE B CG2 1 
ATOM   5334 C CD1 . ILE B 1 751 ? 46.027  0.692   76.914  1.00 114.88 ?  1001 ILE B CD1 1 
ATOM   5335 N N   . CYS B 1 752 ? 46.385  4.089   81.592  1.00 116.99 ?  1002 CYS B N   1 
ATOM   5336 C CA  . CYS B 1 752 ? 46.890  4.357   82.931  1.00 117.67 ?  1002 CYS B CA  1 
ATOM   5337 C C   . CYS B 1 752 ? 46.053  3.630   83.970  1.00 118.02 ?  1002 CYS B C   1 
ATOM   5338 O O   . CYS B 1 752 ? 44.821  3.701   83.946  1.00 116.29 ?  1002 CYS B O   1 
ATOM   5339 C CB  . CYS B 1 752 ? 46.901  5.859   83.222  1.00 122.83 ?  1002 CYS B CB  1 
ATOM   5340 S SG  . CYS B 1 752 ? 48.559  6.541   83.250  1.00 163.35 ?  1002 CYS B SG  1 
ATOM   5341 N N   . SER B 1 753 ? 46.735  2.937   84.879  1.00 115.67 ?  1003 SER B N   1 
ATOM   5342 C CA  . SER B 1 753 ? 46.098  2.297   86.022  1.00 118.35 ?  1003 SER B CA  1 
ATOM   5343 C C   . SER B 1 753 ? 45.987  3.324   87.142  1.00 110.13 ?  1003 SER B C   1 
ATOM   5344 O O   . SER B 1 753 ? 47.001  3.769   87.690  1.00 109.11 ?  1003 SER B O   1 
ATOM   5345 C CB  . SER B 1 753 ? 46.898  1.076   86.471  1.00 124.32 ?  1003 SER B CB  1 
ATOM   5346 O OG  . SER B 1 753 ? 46.325  0.489   87.626  1.00 121.42 ?  1003 SER B OG  1 
ATOM   5347 N N   . VAL B 1 754 ? 44.757  3.702   87.478  1.00 112.79 ?  1004 VAL B N   1 
ATOM   5348 C CA  . VAL B 1 754 ? 44.479  4.666   88.535  1.00 104.27 ?  1004 VAL B CA  1 
ATOM   5349 C C   . VAL B 1 754 ? 43.869  3.919   89.710  1.00 106.06 ?  1004 VAL B C   1 
ATOM   5350 O O   . VAL B 1 754 ? 42.869  3.208   89.550  1.00 113.28 ?  1004 VAL B O   1 
ATOM   5351 C CB  . VAL B 1 754 ? 43.545  5.786   88.047  1.00 100.53 ?  1004 VAL B CB  1 
ATOM   5352 C CG1 . VAL B 1 754 ? 43.174  6.702   89.201  1.00 105.01 ?  1004 VAL B CG1 1 
ATOM   5353 C CG2 . VAL B 1 754 ? 44.206  6.574   86.927  1.00 105.66 ?  1004 VAL B CG2 1 
ATOM   5354 N N   . SER B 1 755 ? 44.470  4.076   90.886  1.00 104.38 ?  1005 SER B N   1 
ATOM   5355 C CA  . SER B 1 755 ? 44.035  3.384   92.095  1.00 105.36 ?  1005 SER B CA  1 
ATOM   5356 C C   . SER B 1 755 ? 43.625  4.422   93.131  1.00 104.99 ?  1005 SER B C   1 
ATOM   5357 O O   . SER B 1 755 ? 44.478  5.124   93.685  1.00 106.39 ?  1005 SER B O   1 
ATOM   5358 C CB  . SER B 1 755 ? 45.141  2.479   92.635  1.00 110.63 ?  1005 SER B CB  1 
ATOM   5359 O OG  . SER B 1 755 ? 44.691  1.740   93.758  1.00 123.22 ?  1005 SER B OG  1 
ATOM   5360 N N   . LEU B 1 756 ? 42.325  4.519   93.390  1.00 98.79  ?  1006 LEU B N   1 
ATOM   5361 C CA  . LEU B 1 756 ? 41.800  5.396   94.424  1.00 104.84 ?  1006 LEU B CA  1 
ATOM   5362 C C   . LEU B 1 756 ? 41.567  4.605   95.705  1.00 106.53 ?  1006 LEU B C   1 
ATOM   5363 O O   . LEU B 1 756 ? 41.275  3.406   95.673  1.00 108.78 ?  1006 LEU B O   1 
ATOM   5364 C CB  . LEU B 1 756 ? 40.496  6.070   93.983  1.00 106.33 ?  1006 LEU B CB  1 
ATOM   5365 C CG  . LEU B 1 756 ? 39.201  5.266   94.117  1.00 108.13 ?  1006 LEU B CG  1 
ATOM   5366 C CD1 . LEU B 1 756 ? 37.984  6.143   93.872  1.00 96.46  ?  1006 LEU B CD1 1 
ATOM   5367 C CD2 . LEU B 1 756 ? 39.213  4.099   93.159  1.00 101.68 ?  1006 LEU B CD2 1 
ATOM   5368 N N   . THR B 1 757 ? 41.711  5.286   96.837  1.00 114.37 ?  1007 THR B N   1 
ATOM   5369 C CA  . THR B 1 757 ? 41.562  4.669   98.146  1.00 112.47 ?  1007 THR B CA  1 
ATOM   5370 C C   . THR B 1 757 ? 40.543  5.449   98.965  1.00 119.79 ?  1007 THR B C   1 
ATOM   5371 O O   . THR B 1 757 ? 40.035  6.492   98.541  1.00 115.98 ?  1007 THR B O   1 
ATOM   5372 C CB  . THR B 1 757 ? 42.901  4.605   98.898  1.00 114.28 ?  1007 THR B CB  1 
ATOM   5373 O OG1 . THR B 1 757 ? 43.321  5.930   99.246  1.00 127.59 ?  1007 THR B OG1 1 
ATOM   5374 C CG2 . THR B 1 757 ? 43.973  3.951   98.037  1.00 103.01 ?  1007 THR B CG2 1 
ATOM   5375 N N   . GLU B 1 758 ? 40.245  4.916   100.152 1.00 126.59 ?  1008 GLU B N   1 
ATOM   5376 C CA  . GLU B 1 758 ? 39.391  5.561   101.147 1.00 121.21 ?  1008 GLU B CA  1 
ATOM   5377 C C   . GLU B 1 758 ? 37.960  5.757   100.654 1.00 117.03 ?  1008 GLU B C   1 
ATOM   5378 O O   . GLU B 1 758 ? 37.014  5.277   101.288 1.00 117.44 ?  1008 GLU B O   1 
ATOM   5379 C CB  . GLU B 1 758 ? 39.993  6.904   101.578 1.00 119.14 ?  1008 GLU B CB  1 
ATOM   5380 C CG  . GLU B 1 758 ? 41.495  6.859   101.865 1.00 123.14 ?  1008 GLU B CG  1 
ATOM   5381 C CD  . GLU B 1 758 ? 41.853  6.007   103.071 1.00 129.60 ?  1008 GLU B CD  1 
ATOM   5382 O OE1 . GLU B 1 758 ? 42.644  6.480   103.916 1.00 122.96 ?  1008 GLU B OE1 1 
ATOM   5383 O OE2 . GLU B 1 758 ? 41.349  4.868   103.177 1.00 126.76 -1 1008 GLU B OE2 1 
ATOM   5384 N N   . CYS B 1 759 ? 37.785  6.459   99.538  1.00 116.63 ?  1009 CYS B N   1 
ATOM   5385 C CA  . CYS B 1 759 ? 36.452  6.762   99.037  1.00 116.20 ?  1009 CYS B CA  1 
ATOM   5386 C C   . CYS B 1 759 ? 35.882  5.594   98.241  1.00 114.10 ?  1009 CYS B C   1 
ATOM   5387 O O   . CYS B 1 759 ? 36.614  4.803   97.640  1.00 109.93 ?  1009 CYS B O   1 
ATOM   5388 C CB  . CYS B 1 759 ? 36.481  8.018   98.166  1.00 105.35 ?  1009 CYS B CB  1 
ATOM   5389 S SG  . CYS B 1 759 ? 36.899  9.526   99.068  1.00 123.69 ?  1009 CYS B SG  1 
ATOM   5390 N N   . SER B 1 760 ? 34.550  5.494   98.245  1.00 117.92 ?  1010 SER B N   1 
ATOM   5391 C CA  . SER B 1 760 ? 33.866  4.472   97.460  1.00 108.67 ?  1010 SER B CA  1 
ATOM   5392 C C   . SER B 1 760 ? 33.861  4.829   95.978  1.00 108.36 ?  1010 SER B C   1 
ATOM   5393 O O   . SER B 1 760 ? 34.176  3.990   95.127  1.00 94.21  ?  1010 SER B O   1 
ATOM   5394 C CB  . SER B 1 760 ? 32.436  4.287   97.973  1.00 98.49  ?  1010 SER B CB  1 
ATOM   5395 O OG  . SER B 1 760 ? 31.689  3.441   97.116  1.00 107.24 ?  1010 SER B OG  1 
ATOM   5396 N N   . THR B 1 761 ? 33.499  6.068   95.655  1.00 111.52 ?  1011 THR B N   1 
ATOM   5397 C CA  . THR B 1 761 ? 33.534  6.569   94.290  1.00 98.75  ?  1011 THR B CA  1 
ATOM   5398 C C   . THR B 1 761 ? 34.149  7.960   94.297  1.00 90.98  ?  1011 THR B C   1 
ATOM   5399 O O   . THR B 1 761 ? 34.279  8.599   95.344  1.00 105.10 ?  1011 THR B O   1 
ATOM   5400 C CB  . THR B 1 761 ? 32.137  6.596   93.656  1.00 97.73  ?  1011 THR B CB  1 
ATOM   5401 O OG1 . THR B 1 761 ? 31.169  6.987   94.638  1.00 95.85  ?  1011 THR B OG1 1 
ATOM   5402 C CG2 . THR B 1 761 ? 31.774  5.226   93.100  1.00 98.44  ?  1011 THR B CG2 1 
ATOM   5403 N N   . PHE B 1 762 ? 34.531  8.430   93.111  1.00 86.59  ?  1012 PHE B N   1 
ATOM   5404 C CA  . PHE B 1 762 ? 35.179  9.734   92.992  1.00 83.41  ?  1012 PHE B CA  1 
ATOM   5405 C C   . PHE B 1 762 ? 35.106  10.193  91.546  1.00 90.37  ?  1012 PHE B C   1 
ATOM   5406 O O   . PHE B 1 762 ? 35.600  9.500   90.651  1.00 90.30  ?  1012 PHE B O   1 
ATOM   5407 C CB  . PHE B 1 762 ? 36.632  9.663   93.465  1.00 83.58  ?  1012 PHE B CB  1 
ATOM   5408 C CG  . PHE B 1 762 ? 37.295  11.004  93.595  1.00 77.59  ?  1012 PHE B CG  1 
ATOM   5409 C CD1 . PHE B 1 762 ? 36.720  12.001  94.363  1.00 76.56  ?  1012 PHE B CD1 1 
ATOM   5410 C CD2 . PHE B 1 762 ? 38.499  11.262  92.962  1.00 78.87  ?  1012 PHE B CD2 1 
ATOM   5411 C CE1 . PHE B 1 762 ? 37.329  13.236  94.490  1.00 86.85  ?  1012 PHE B CE1 1 
ATOM   5412 C CE2 . PHE B 1 762 ? 39.114  12.494  93.086  1.00 85.32  ?  1012 PHE B CE2 1 
ATOM   5413 C CZ  . PHE B 1 762 ? 38.528  13.482  93.851  1.00 84.15  ?  1012 PHE B CZ  1 
ATOM   5414 N N   . LEU B 1 763 ? 34.493  11.353  91.321  1.00 87.12  ?  1013 LEU B N   1 
ATOM   5415 C CA  . LEU B 1 763 ? 34.434  11.965  89.999  1.00 78.53  ?  1013 LEU B CA  1 
ATOM   5416 C C   . LEU B 1 763 ? 35.576  12.965  89.866  1.00 84.42  ?  1013 LEU B C   1 
ATOM   5417 O O   . LEU B 1 763 ? 35.647  13.938  90.624  1.00 91.22  ?  1013 LEU B O   1 
ATOM   5418 C CB  . LEU B 1 763 ? 33.088  12.653  89.779  1.00 75.98  ?  1013 LEU B CB  1 
ATOM   5419 C CG  . LEU B 1 763 ? 32.973  13.528  88.529  1.00 76.98  ?  1013 LEU B CG  1 
ATOM   5420 C CD1 . LEU B 1 763 ? 33.147  12.699  87.265  1.00 71.57  ?  1013 LEU B CD1 1 
ATOM   5421 C CD2 . LEU B 1 763 ? 31.647  14.272  88.511  1.00 68.11  ?  1013 LEU B CD2 1 
ATOM   5422 N N   . THR B 1 764 ? 36.464  12.725  88.908  1.00 79.25  ?  1014 THR B N   1 
ATOM   5423 C CA  . THR B 1 764 ? 37.619  13.588  88.695  1.00 76.41  ?  1014 THR B CA  1 
ATOM   5424 C C   . THR B 1 764 ? 38.059  13.449  87.242  1.00 83.98  ?  1014 THR B C   1 
ATOM   5425 O O   . THR B 1 764 ? 37.372  12.828  86.423  1.00 83.87  ?  1014 THR B O   1 
ATOM   5426 C CB  . THR B 1 764 ? 38.752  13.240  89.666  1.00 74.22  ?  1014 THR B CB  1 
ATOM   5427 O OG1 . THR B 1 764 ? 39.856  14.127  89.453  1.00 74.44  ?  1014 THR B OG1 1 
ATOM   5428 C CG2 . THR B 1 764 ? 39.212  11.805  89.455  1.00 75.44  ?  1014 THR B CG2 1 
ATOM   5429 N N   . SER B 1 765 ? 39.213  14.030  86.922  1.00 78.03  ?  1015 SER B N   1 
ATOM   5430 C CA  . SER B 1 765 ? 39.776  13.977  85.583  1.00 81.06  ?  1015 SER B CA  1 
ATOM   5431 C C   . SER B 1 765 ? 41.256  13.638  85.665  1.00 80.62  ?  1015 SER B C   1 
ATOM   5432 O O   . SER B 1 765 ? 41.971  14.143  86.535  1.00 84.62  ?  1015 SER B O   1 
ATOM   5433 C CB  . SER B 1 765 ? 39.594  15.307  84.844  1.00 75.94  ?  1015 SER B CB  1 
ATOM   5434 O OG  . SER B 1 765 ? 38.238  15.713  84.853  1.00 86.52  ?  1015 SER B OG  1 
ATOM   5435 N N   . ILE B 1 766 ? 41.707  12.780  84.756  1.00 86.62  ?  1016 ILE B N   1 
ATOM   5436 C CA  . ILE B 1 766 ? 43.119  12.460  84.599  1.00 89.84  ?  1016 ILE B CA  1 
ATOM   5437 C C   . ILE B 1 766 ? 43.609  13.128  83.322  1.00 88.53  ?  1016 ILE B C   1 
ATOM   5438 O O   . ILE B 1 766 ? 42.892  13.166  82.315  1.00 84.01  ?  1016 ILE B O   1 
ATOM   5439 C CB  . ILE B 1 766 ? 43.361  10.938  84.562  1.00 95.64  ?  1016 ILE B CB  1 
ATOM   5440 C CG1 . ILE B 1 766 ? 42.701  10.264  85.766  1.00 86.43  ?  1016 ILE B CG1 1 
ATOM   5441 C CG2 . ILE B 1 766 ? 44.851  10.636  84.571  1.00 93.26  ?  1016 ILE B CG2 1 
ATOM   5442 C CD1 . ILE B 1 766 ? 43.340  10.625  87.091  1.00 103.69 ?  1016 ILE B CD1 1 
ATOM   5443 N N   . LYS B 1 767 ? 44.826  13.661  83.367  1.00 88.46  ?  1017 LYS B N   1 
ATOM   5444 C CA  . LYS B 1 767 ? 45.373  14.465  82.287  1.00 93.51  ?  1017 LYS B CA  1 
ATOM   5445 C C   . LYS B 1 767 ? 46.601  13.785  81.694  1.00 97.07  ?  1017 LYS B C   1 
ATOM   5446 O O   . LYS B 1 767 ? 47.253  12.961  82.339  1.00 101.61 ?  1017 LYS B O   1 
ATOM   5447 C CB  . LYS B 1 767 ? 45.727  15.869  82.792  1.00 82.68  ?  1017 LYS B CB  1 
ATOM   5448 C CG  . LYS B 1 767 ? 45.089  17.005  82.011  1.00 90.10  ?  1017 LYS B CG  1 
ATOM   5449 C CD  . LYS B 1 767 ? 44.886  18.235  82.887  1.00 86.84  ?  1017 LYS B CD  1 
ATOM   5450 C CE  . LYS B 1 767 ? 46.087  18.490  83.785  1.00 75.34  ?  1017 LYS B CE  1 
ATOM   5451 N NZ  . LYS B 1 767 ? 45.947  19.744  84.573  1.00 91.79  1  1017 LYS B NZ  1 
ATOM   5452 N N   . ALA B 1 768 ? 46.911  14.139  80.448  1.00 88.26  ?  1018 ALA B N   1 
ATOM   5453 C CA  . ALA B 1 768 ? 48.052  13.587  79.718  1.00 89.89  ?  1018 ALA B CA  1 
ATOM   5454 C C   . ALA B 1 768 ? 49.068  14.707  79.504  1.00 113.33 ?  1018 ALA B C   1 
ATOM   5455 O O   . ALA B 1 768 ? 48.987  15.466  78.537  1.00 113.67 ?  1018 ALA B O   1 
ATOM   5456 C CB  . ALA B 1 768 ? 47.614  12.973  78.395  1.00 89.28  ?  1018 ALA B CB  1 
ATOM   5457 N N   . CYS B 1 769 ? 50.028  14.802  80.417  1.00 114.17 ?  1019 CYS B N   1 
ATOM   5458 C CA  . CYS B 1 769 ? 51.087  15.796  80.356  1.00 109.17 ?  1019 CYS B CA  1 
ATOM   5459 C C   . CYS B 1 769 ? 52.373  15.185  79.811  1.00 111.63 ?  1019 CYS B C   1 
ATOM   5460 O O   . CYS B 1 769 ? 52.522  13.966  79.698  1.00 109.70 ?  1019 CYS B O   1 
ATOM   5461 C CB  . CYS B 1 769 ? 51.356  16.387  81.743  1.00 115.61 ?  1019 CYS B CB  1 
ATOM   5462 S SG  . CYS B 1 769 ? 50.419  17.860  82.220  1.00 151.35 ?  1019 CYS B SG  1 
ATOM   5463 N N   . ASP B 1 770 ? 53.313  16.065  79.471  1.00 111.85 ?  1020 ASP B N   1 
ATOM   5464 C CA  . ASP B 1 770 ? 54.702  15.658  79.315  1.00 117.68 ?  1020 ASP B CA  1 
ATOM   5465 C C   . ASP B 1 770 ? 55.522  16.367  80.386  1.00 111.73 ?  1020 ASP B C   1 
ATOM   5466 O O   . ASP B 1 770 ? 55.038  16.568  81.504  1.00 111.43 ?  1020 ASP B O   1 
ATOM   5467 C CB  . ASP B 1 770 ? 55.223  15.953  77.901  1.00 115.75 ?  1020 ASP B CB  1 
ATOM   5468 C CG  . ASP B 1 770 ? 55.269  17.440  77.570  1.00 118.87 ?  1020 ASP B CG  1 
ATOM   5469 O OD1 . ASP B 1 770 ? 54.778  18.266  78.367  1.00 117.14 ?  1020 ASP B OD1 1 
ATOM   5470 O OD2 . ASP B 1 770 ? 55.812  17.781  76.498  1.00 110.57 -1 1020 ASP B OD2 1 
ATOM   5471 N N   . SER B 1 771 ? 56.751  16.765  80.060  1.00 119.39 ?  1021 SER B N   1 
ATOM   5472 C CA  . SER B 1 771 ? 57.566  17.475  81.038  1.00 114.95 ?  1021 SER B CA  1 
ATOM   5473 C C   . SER B 1 771 ? 57.077  18.902  81.259  1.00 110.32 ?  1021 SER B C   1 
ATOM   5474 O O   . SER B 1 771 ? 57.278  19.461  82.343  1.00 109.25 ?  1021 SER B O   1 
ATOM   5475 C CB  . SER B 1 771 ? 59.029  17.477  80.595  1.00 112.97 ?  1021 SER B CB  1 
ATOM   5476 O OG  . SER B 1 771 ? 59.163  17.997  79.283  1.00 109.51 ?  1021 SER B OG  1 
ATOM   5477 N N   . ALA B 1 772 ? 56.427  19.502  80.264  1.00 112.39 ?  1022 ALA B N   1 
ATOM   5478 C CA  . ALA B 1 772 ? 56.102  20.923  80.317  1.00 105.30 ?  1022 ALA B CA  1 
ATOM   5479 C C   . ALA B 1 772 ? 54.617  21.229  80.202  1.00 102.51 ?  1022 ALA B C   1 
ATOM   5480 O O   . ALA B 1 772 ? 54.136  22.145  80.873  1.00 112.91 ?  1022 ALA B O   1 
ATOM   5481 C CB  . ALA B 1 772 ? 56.859  21.677  79.214  1.00 111.06 ?  1022 ALA B CB  1 
ATOM   5482 N N   . MET B 1 773 ? 53.873  20.503  79.370  1.00 107.02 ?  1023 MET B N   1 
ATOM   5483 C CA  . MET B 1 773 ? 52.478  20.838  79.118  1.00 109.99 ?  1023 MET B CA  1 
ATOM   5484 C C   . MET B 1 773 ? 51.629  19.577  79.052  1.00 110.22 ?  1023 MET B C   1 
ATOM   5485 O O   . MET B 1 773 ? 52.126  18.473  78.823  1.00 115.91 ?  1023 MET B O   1 
ATOM   5486 C CB  . MET B 1 773 ? 52.313  21.636  77.817  1.00 107.91 ?  1023 MET B CB  1 
ATOM   5487 C CG  . MET B 1 773 ? 52.633  23.115  77.941  1.00 106.05 ?  1023 MET B CG  1 
ATOM   5488 S SD  . MET B 1 773 ? 52.201  24.033  76.451  1.00 124.28 ?  1023 MET B SD  1 
ATOM   5489 C CE  . MET B 1 773 ? 52.409  25.719  77.019  1.00 124.55 ?  1023 MET B CE  1 
ATOM   5490 N N   . CYS B 1 774 ? 50.328  19.764  79.253  1.00 114.25 ?  1024 CYS B N   1 
ATOM   5491 C CA  . CYS B 1 774 ? 49.343  18.703  79.107  1.00 106.69 ?  1024 CYS B CA  1 
ATOM   5492 C C   . CYS B 1 774 ? 48.647  18.828  77.760  1.00 103.66 ?  1024 CYS B C   1 
ATOM   5493 O O   . CYS B 1 774 ? 48.275  19.928  77.340  1.00 97.86  ?  1024 CYS B O   1 
ATOM   5494 C CB  . CYS B 1 774 ? 48.311  18.751  80.233  1.00 98.96  ?  1024 CYS B CB  1 
ATOM   5495 S SG  . CYS B 1 774 ? 48.544  17.522  81.534  1.00 121.02 ?  1024 CYS B SG  1 
ATOM   5496 N N   . TYR B 1 775 ? 48.465  17.692  77.090  1.00 103.24 ?  1025 TYR B N   1 
ATOM   5497 C CA  . TYR B 1 775 ? 47.916  17.669  75.745  1.00 108.22 ?  1025 TYR B CA  1 
ATOM   5498 C C   . TYR B 1 775 ? 46.536  17.034  75.659  1.00 108.80 ?  1025 TYR B C   1 
ATOM   5499 O O   . TYR B 1 775 ? 45.903  17.116  74.601  1.00 109.33 ?  1025 TYR B O   1 
ATOM   5500 C CB  . TYR B 1 775 ? 48.879  16.933  74.801  1.00 106.54 ?  1025 TYR B CB  1 
ATOM   5501 C CG  . TYR B 1 775 ? 50.293  17.474  74.841  1.00 114.56 ?  1025 TYR B CG  1 
ATOM   5502 C CD1 . TYR B 1 775 ? 51.246  16.921  75.688  1.00 107.80 ?  1025 TYR B CD1 1 
ATOM   5503 C CD2 . TYR B 1 775 ? 50.673  18.543  74.036  1.00 118.18 ?  1025 TYR B CD2 1 
ATOM   5504 C CE1 . TYR B 1 775 ? 52.535  17.413  75.728  1.00 110.69 ?  1025 TYR B CE1 1 
ATOM   5505 C CE2 . TYR B 1 775 ? 51.962  19.041  74.068  1.00 113.55 ?  1025 TYR B CE2 1 
ATOM   5506 C CZ  . TYR B 1 775 ? 52.888  18.473  74.917  1.00 110.61 ?  1025 TYR B CZ  1 
ATOM   5507 O OH  . TYR B 1 775 ? 54.172  18.965  74.954  1.00 117.78 ?  1025 TYR B OH  1 
ATOM   5508 N N   . GLY B 1 776 ? 46.052  16.413  76.733  1.00 102.30 ?  1026 GLY B N   1 
ATOM   5509 C CA  . GLY B 1 776 ? 44.730  15.814  76.732  1.00 94.45  ?  1026 GLY B CA  1 
ATOM   5510 C C   . GLY B 1 776 ? 44.285  15.509  78.144  1.00 90.62  ?  1026 GLY B C   1 
ATOM   5511 O O   . GLY B 1 776 ? 45.076  15.537  79.090  1.00 90.76  ?  1026 GLY B O   1 
ATOM   5512 N N   . SER B 1 777 ? 42.993  15.214  78.277  1.00 84.24  ?  1027 SER B N   1 
ATOM   5513 C CA  . SER B 1 777 ? 42.420  14.894  79.575  1.00 79.20  ?  1027 SER B CA  1 
ATOM   5514 C C   . SER B 1 777 ? 41.217  13.981  79.391  1.00 86.22  ?  1027 SER B C   1 
ATOM   5515 O O   . SER B 1 777 ? 40.537  14.021  78.362  1.00 88.83  ?  1027 SER B O   1 
ATOM   5516 C CB  . SER B 1 777 ? 42.002  16.154  80.342  1.00 86.02  ?  1027 SER B CB  1 
ATOM   5517 O OG  . SER B 1 777 ? 40.710  16.586  79.950  1.00 89.95  ?  1027 SER B OG  1 
ATOM   5518 N N   . THR B 1 778 ? 40.961  13.162  80.409  1.00 87.65  ?  1028 THR B N   1 
ATOM   5519 C CA  . THR B 1 778 ? 39.818  12.261  80.433  1.00 80.31  ?  1028 THR B CA  1 
ATOM   5520 C C   . THR B 1 778 ? 39.198  12.296  81.820  1.00 85.64  ?  1028 THR B C   1 
ATOM   5521 O O   . THR B 1 778 ? 39.904  12.138  82.820  1.00 89.32  ?  1028 THR B O   1 
ATOM   5522 C CB  . THR B 1 778 ? 40.227  10.826  80.071  1.00 91.94  ?  1028 THR B CB  1 
ATOM   5523 O OG1 . THR B 1 778 ? 40.569  10.759  78.680  1.00 98.35  ?  1028 THR B OG1 1 
ATOM   5524 C CG2 . THR B 1 778 ? 39.093  9.854   80.359  1.00 84.48  ?  1028 THR B CG2 1 
ATOM   5525 N N   . THR B 1 779 ? 37.887  12.510  81.878  1.00 85.04  ?  1029 THR B N   1 
ATOM   5526 C CA  . THR B 1 779 ? 37.147  12.563  83.132  1.00 89.21  ?  1029 THR B CA  1 
ATOM   5527 C C   . THR B 1 779 ? 36.314  11.298  83.273  1.00 82.87  ?  1029 THR B C   1 
ATOM   5528 O O   . THR B 1 779 ? 35.649  10.878  82.320  1.00 87.30  ?  1029 THR B O   1 
ATOM   5529 C CB  . THR B 1 779 ? 36.246  13.799  83.191  1.00 73.47  ?  1029 THR B CB  1 
ATOM   5530 O OG1 . THR B 1 779 ? 34.890  13.419  82.929  1.00 74.01  ?  1029 THR B OG1 1 
ATOM   5531 C CG2 . THR B 1 779 ? 36.682  14.828  82.156  1.00 79.26  ?  1029 THR B CG2 1 
ATOM   5532 N N   . ALA B 1 780 ? 36.350  10.694  84.460  1.00 80.85  ?  1030 ALA B N   1 
ATOM   5533 C CA  . ALA B 1 780 ? 35.638  9.446   84.694  1.00 95.41  ?  1030 ALA B CA  1 
ATOM   5534 C C   . ALA B 1 780 ? 35.292  9.324   86.170  1.00 84.41  ?  1030 ALA B C   1 
ATOM   5535 O O   . ALA B 1 780 ? 35.934  9.926   87.034  1.00 79.71  ?  1030 ALA B O   1 
ATOM   5536 C CB  . ALA B 1 780 ? 36.462  8.236   84.237  1.00 87.52  ?  1030 ALA B CB  1 
ATOM   5537 N N   . ASN B 1 781 ? 34.259  8.530   86.446  1.00 92.45  ?  1031 ASN B N   1 
ATOM   5538 C CA  . ASN B 1 781 ? 33.821  8.248   87.811  1.00 94.02  ?  1031 ASN B CA  1 
ATOM   5539 C C   . ASN B 1 781 ? 34.565  7.007   88.290  1.00 93.73  ?  1031 ASN B C   1 
ATOM   5540 O O   . ASN B 1 781 ? 34.243  5.884   87.894  1.00 95.49  ?  1031 ASN B O   1 
ATOM   5541 C CB  . ASN B 1 781 ? 32.310  8.051   87.863  1.00 101.13 ?  1031 ASN B CB  1 
ATOM   5542 C CG  . ASN B 1 781 ? 31.729  8.317   89.242  1.00 105.12 ?  1031 ASN B CG  1 
ATOM   5543 O OD1 . ASN B 1 781 ? 30.618  8.831   89.367  1.00 110.48 ?  1031 ASN B OD1 1 
ATOM   5544 N ND2 . ASN B 1 781 ? 32.481  7.976   90.283  1.00 104.03 ?  1031 ASN B ND2 1 
ATOM   5545 N N   . LEU B 1 782 ? 35.560  7.209   89.148  1.00 92.81  ?  1032 LEU B N   1 
ATOM   5546 C CA  . LEU B 1 782 ? 36.384  6.109   89.628  1.00 87.41  ?  1032 LEU B CA  1 
ATOM   5547 C C   . LEU B 1 782 ? 35.623  5.284   90.658  1.00 103.08 ?  1032 LEU B C   1 
ATOM   5548 O O   . LEU B 1 782 ? 35.055  5.830   91.608  1.00 102.84 ?  1032 LEU B O   1 
ATOM   5549 C CB  . LEU B 1 782 ? 37.682  6.642   90.234  1.00 89.96  ?  1032 LEU B CB  1 
ATOM   5550 C CG  . LEU B 1 782 ? 38.552  7.511   89.325  1.00 83.48  ?  1032 LEU B CG  1 
ATOM   5551 C CD1 . LEU B 1 782 ? 39.816  7.944   90.049  1.00 83.21  ?  1032 LEU B CD1 1 
ATOM   5552 C CD2 . LEU B 1 782 ? 38.891  6.773   88.040  1.00 85.55  ?  1032 LEU B CD2 1 
ATOM   5553 N N   . VAL B 1 783 ? 35.610  3.968   90.462  1.00 100.89 ?  1033 VAL B N   1 
ATOM   5554 C CA  . VAL B 1 783 ? 35.007  3.027   91.400  1.00 94.67  ?  1033 VAL B CA  1 
ATOM   5555 C C   . VAL B 1 783 ? 36.114  2.443   92.265  1.00 96.88  ?  1033 VAL B C   1 
ATOM   5556 O O   . VAL B 1 783 ? 37.229  2.206   91.784  1.00 103.71 ?  1033 VAL B O   1 
ATOM   5557 C CB  . VAL B 1 783 ? 34.225  1.926   90.656  1.00 105.73 ?  1033 VAL B CB  1 
ATOM   5558 C CG1 . VAL B 1 783 ? 35.116  1.233   89.636  1.00 101.12 ?  1033 VAL B CG1 1 
ATOM   5559 C CG2 . VAL B 1 783 ? 33.634  0.918   91.635  1.00 118.78 ?  1033 VAL B CG2 1 
ATOM   5560 N N   . ARG B 1 784 ? 35.804  2.211   93.543  1.00 106.50 ?  1034 ARG B N   1 
ATOM   5561 C CA  . ARG B 1 784 ? 36.804  1.824   94.534  1.00 107.03 ?  1034 ARG B CA  1 
ATOM   5562 C C   . ARG B 1 784 ? 37.655  0.656   94.054  1.00 112.53 ?  1034 ARG B C   1 
ATOM   5563 O O   . ARG B 1 784 ? 37.141  -0.327  93.512  1.00 118.36 ?  1034 ARG B O   1 
ATOM   5564 C CB  . ARG B 1 784 ? 36.115  1.467   95.852  1.00 108.95 ?  1034 ARG B CB  1 
ATOM   5565 C CG  . ARG B 1 784 ? 37.074  1.245   97.007  1.00 107.10 ?  1034 ARG B CG  1 
ATOM   5566 C CD  . ARG B 1 784 ? 36.382  1.469   98.339  1.00 113.63 ?  1034 ARG B CD  1 
ATOM   5567 N NE  . ARG B 1 784 ? 37.342  1.699   99.413  1.00 124.88 ?  1034 ARG B NE  1 
ATOM   5568 C CZ  . ARG B 1 784 ? 37.036  2.255   100.580 1.00 129.17 ?  1034 ARG B CZ  1 
ATOM   5569 N NH1 . ARG B 1 784 ? 35.792  2.645   100.824 1.00 116.74 1  1034 ARG B NH1 1 
ATOM   5570 N NH2 . ARG B 1 784 ? 37.975  2.429   101.500 1.00 127.29 ?  1034 ARG B NH2 1 
ATOM   5571 N N   . GLY B 1 785 ? 38.966  0.777   94.251  1.00 117.91 ?  1035 GLY B N   1 
ATOM   5572 C CA  . GLY B 1 785 ? 39.901  -0.238  93.810  1.00 115.87 ?  1035 GLY B CA  1 
ATOM   5573 C C   . GLY B 1 785 ? 40.814  0.242   92.701  1.00 116.43 ?  1035 GLY B C   1 
ATOM   5574 O O   . GLY B 1 785 ? 41.372  1.341   92.776  1.00 104.37 ?  1035 GLY B O   1 
ATOM   5575 N N   . GLN B 1 786 ? 40.971  -0.575  91.664  1.00 122.68 ?  1036 GLN B N   1 
ATOM   5576 C CA  . GLN B 1 786 ? 41.810  -0.247  90.522  1.00 116.28 ?  1036 GLN B CA  1 
ATOM   5577 C C   . GLN B 1 786 ? 40.945  0.223   89.359  1.00 114.98 ?  1036 GLN B C   1 
ATOM   5578 O O   . GLN B 1 786 ? 39.874  -0.335  89.102  1.00 110.83 ?  1036 GLN B O   1 
ATOM   5579 C CB  . GLN B 1 786 ? 42.653  -1.457  90.106  1.00 112.05 ?  1036 GLN B CB  1 
ATOM   5580 C CG  . GLN B 1 786 ? 43.406  -1.296  88.793  1.00 116.04 ?  1036 GLN B CG  1 
ATOM   5581 C CD  . GLN B 1 786 ? 42.618  -1.810  87.600  1.00 127.11 ?  1036 GLN B CD  1 
ATOM   5582 O OE1 . GLN B 1 786 ? 42.548  -1.157  86.559  1.00 123.45 ?  1036 GLN B OE1 1 
ATOM   5583 N NE2 . GLN B 1 786 ? 42.021  -2.987  87.749  1.00 125.99 ?  1036 GLN B NE2 1 
ATOM   5584 N N   . ASN B 1 787 ? 41.413  1.258   88.664  1.00 113.17 ?  1037 ASN B N   1 
ATOM   5585 C CA  . ASN B 1 787 ? 40.728  1.801   87.500  1.00 106.82 ?  1037 ASN B CA  1 
ATOM   5586 C C   . ASN B 1 787 ? 41.704  1.909   86.340  1.00 108.20 ?  1037 ASN B C   1 
ATOM   5587 O O   . ASN B 1 787 ? 42.873  2.257   86.530  1.00 117.66 ?  1037 ASN B O   1 
ATOM   5588 C CB  . ASN B 1 787 ? 40.123  3.179   87.797  1.00 100.75 ?  1037 ASN B CB  1 
ATOM   5589 C CG  . ASN B 1 787 ? 38.961  3.108   88.765  1.00 98.75  ?  1037 ASN B CG  1 
ATOM   5590 O OD1 . ASN B 1 787 ? 37.799  3.151   88.361  1.00 94.82  ?  1037 ASN B OD1 1 
ATOM   5591 N ND2 . ASN B 1 787 ? 39.269  2.995   90.051  1.00 95.81  ?  1037 ASN B ND2 1 
ATOM   5592 N N   . THR B 1 788 ? 41.218  1.608   85.139  1.00 102.83 ?  1038 THR B N   1 
ATOM   5593 C CA  . THR B 1 788 ? 41.994  1.735   83.911  1.00 102.35 ?  1038 THR B CA  1 
ATOM   5594 C C   . THR B 1 788 ? 41.353  2.830   83.067  1.00 101.91 ?  1038 THR B C   1 
ATOM   5595 O O   . THR B 1 788 ? 40.217  2.679   82.604  1.00 103.84 ?  1038 THR B O   1 
ATOM   5596 C CB  . THR B 1 788 ? 42.044  0.413   83.148  1.00 106.90 ?  1038 THR B CB  1 
ATOM   5597 O OG1 . THR B 1 788 ? 42.439  -0.639  84.036  1.00 109.86 ?  1038 THR B OG1 1 
ATOM   5598 C CG2 . THR B 1 788 ? 43.042  0.500   82.003  1.00 107.98 ?  1038 THR B CG2 1 
ATOM   5599 N N   . VAL B 1 789 ? 42.075  3.931   82.873  1.00 107.95 ?  1039 VAL B N   1 
ATOM   5600 C CA  . VAL B 1 789 ? 41.573  5.082   82.135  1.00 106.19 ?  1039 VAL B CA  1 
ATOM   5601 C C   . VAL B 1 789 ? 42.410  5.267   80.876  1.00 105.11 ?  1039 VAL B C   1 
ATOM   5602 O O   . VAL B 1 789 ? 43.626  5.045   80.885  1.00 103.00 ?  1039 VAL B O   1 
ATOM   5603 C CB  . VAL B 1 789 ? 41.579  6.363   82.999  1.00 99.43  ?  1039 VAL B CB  1 
ATOM   5604 C CG1 . VAL B 1 789 ? 40.707  6.174   84.232  1.00 89.53  ?  1039 VAL B CG1 1 
ATOM   5605 C CG2 . VAL B 1 789 ? 42.996  6.747   83.400  1.00 113.28 ?  1039 VAL B CG2 1 
ATOM   5606 N N   . HIS B 1 790 ? 41.749  5.658   79.790  1.00 103.65 ?  1040 HIS B N   1 
ATOM   5607 C CA  . HIS B 1 790 ? 42.400  5.933   78.517  1.00 105.36 ?  1040 HIS B CA  1 
ATOM   5608 C C   . HIS B 1 790 ? 42.300  7.423   78.224  1.00 102.67 ?  1040 HIS B C   1 
ATOM   5609 O O   . HIS B 1 790 ? 41.224  8.014   78.358  1.00 93.19  ?  1040 HIS B O   1 
ATOM   5610 C CB  . HIS B 1 790 ? 41.763  5.125   77.383  1.00 111.79 ?  1040 HIS B CB  1 
ATOM   5611 C CG  . HIS B 1 790 ? 41.844  3.642   77.575  1.00 114.77 ?  1040 HIS B CG  1 
ATOM   5612 N ND1 . HIS B 1 790 ? 42.726  2.848   76.875  1.00 115.60 ?  1040 HIS B ND1 1 
ATOM   5613 C CD2 . HIS B 1 790 ? 41.149  2.809   78.385  1.00 115.64 ?  1040 HIS B CD2 1 
ATOM   5614 C CE1 . HIS B 1 790 ? 42.572  1.589   77.247  1.00 110.13 ?  1040 HIS B CE1 1 
ATOM   5615 N NE2 . HIS B 1 790 ? 41.622  1.539   78.163  1.00 115.34 ?  1040 HIS B NE2 1 
ATOM   5616 N N   . ILE B 1 791 ? 43.420  8.027   77.830  1.00 116.14 ?  1041 ILE B N   1 
ATOM   5617 C CA  . ILE B 1 791 ? 43.495  9.459   77.566  1.00 105.58 ?  1041 ILE B CA  1 
ATOM   5618 C C   . ILE B 1 791 ? 44.002  9.665   76.145  1.00 107.81 ?  1041 ILE B C   1 
ATOM   5619 O O   . ILE B 1 791 ? 44.983  9.037   75.734  1.00 104.62 ?  1041 ILE B O   1 
ATOM   5620 C CB  . ILE B 1 791 ? 44.409  10.180  78.573  1.00 94.45  ?  1041 ILE B CB  1 
ATOM   5621 C CG1 . ILE B 1 791 ? 44.115  9.718   80.001  1.00 91.20  ?  1041 ILE B CG1 1 
ATOM   5622 C CG2 . ILE B 1 791 ? 44.225  11.686  78.464  1.00 86.65  ?  1041 ILE B CG2 1 
ATOM   5623 C CD1 . ILE B 1 791 ? 45.054  10.300  81.024  1.00 95.11  ?  1041 ILE B CD1 1 
ATOM   5624 N N   . VAL B 1 792 ? 43.338  10.550  75.404  1.00 109.83 ?  1042 VAL B N   1 
ATOM   5625 C CA  . VAL B 1 792 ? 43.730  10.916  74.047  1.00 105.01 ?  1042 VAL B CA  1 
ATOM   5626 C C   . VAL B 1 792 ? 44.353  12.304  74.090  1.00 104.89 ?  1042 VAL B C   1 
ATOM   5627 O O   . VAL B 1 792 ? 43.766  13.238  74.650  1.00 108.44 ?  1042 VAL B O   1 
ATOM   5628 C CB  . VAL B 1 792 ? 42.531  10.872  73.084  1.00 104.20 ?  1042 VAL B CB  1 
ATOM   5629 C CG1 . VAL B 1 792 ? 42.747  11.814  71.909  1.00 109.16 ?  1042 VAL B CG1 1 
ATOM   5630 C CG2 . VAL B 1 792 ? 42.301  9.453   72.592  1.00 100.95 ?  1042 VAL B CG2 1 
ATOM   5631 N N   . GLY B 1 793 ? 45.544  12.435  73.507  1.00 128.20 ?  1043 GLY B N   1 
ATOM   5632 C CA  . GLY B 1 793 ? 46.248  13.702  73.478  1.00 124.02 ?  1043 GLY B CA  1 
ATOM   5633 C C   . GLY B 1 793 ? 46.856  13.996  72.121  1.00 126.77 ?  1043 GLY B C   1 
ATOM   5634 O O   . GLY B 1 793 ? 46.646  13.249  71.162  1.00 137.75 ?  1043 GLY B O   1 
ATOM   5635 N N   . LYS B 1 794 ? 47.620  15.086  72.040  1.00 107.45 ?  1044 LYS B N   1 
ATOM   5636 C CA  . LYS B 1 794 ? 48.221  15.513  70.778  1.00 119.91 ?  1044 LYS B CA  1 
ATOM   5637 C C   . LYS B 1 794 ? 49.369  16.463  71.078  1.00 122.90 ?  1044 LYS B C   1 
ATOM   5638 O O   . LYS B 1 794 ? 49.144  17.547  71.625  1.00 122.72 ?  1044 LYS B O   1 
ATOM   5639 C CB  . LYS B 1 794 ? 47.183  16.190  69.883  1.00 117.23 ?  1044 LYS B CB  1 
ATOM   5640 C CG  . LYS B 1 794 ? 47.776  17.059  68.788  1.00 138.40 ?  1044 LYS B CG  1 
ATOM   5641 C CD  . LYS B 1 794 ? 46.738  18.024  68.242  1.00 136.31 ?  1044 LYS B CD  1 
ATOM   5642 C CE  . LYS B 1 794 ? 47.390  19.169  67.490  1.00 138.74 ?  1044 LYS B CE  1 
ATOM   5643 N NZ  . LYS B 1 794 ? 46.398  20.169  67.009  1.00 133.49 1  1044 LYS B NZ  1 
ATOM   5644 N N   . GLY B 1 795 ? 50.582  16.069  70.713  1.00 125.37 ?  1045 GLY B N   1 
ATOM   5645 C CA  . GLY B 1 795 ? 51.772  16.864  70.944  1.00 122.68 ?  1045 GLY B CA  1 
ATOM   5646 C C   . GLY B 1 795 ? 52.893  16.037  71.541  1.00 125.09 ?  1045 GLY B C   1 
ATOM   5647 O O   . GLY B 1 795 ? 52.730  14.873  71.898  1.00 127.12 ?  1045 GLY B O   1 
ATOM   5648 N N   . GLY B 1 796 ? 54.055  16.675  71.637  1.00 129.65 ?  1046 GLY B N   1 
ATOM   5649 C CA  . GLY B 1 796 ? 55.227  16.045  72.223  1.00 137.61 ?  1046 GLY B CA  1 
ATOM   5650 C C   . GLY B 1 796 ? 56.465  16.172  71.357  1.00 149.99 ?  1046 GLY B C   1 
ATOM   5651 O O   . GLY B 1 796 ? 56.392  16.239  70.127  1.00 150.83 ?  1046 GLY B O   1 
ATOM   5652 N N   . HIS B 1 797 ? 57.626  16.208  72.011  1.00 157.82 ?  1047 HIS B N   1 
ATOM   5653 C CA  . HIS B 1 797 ? 58.904  16.353  71.327  1.00 162.27 ?  1047 HIS B CA  1 
ATOM   5654 C C   . HIS B 1 797 ? 59.926  15.438  71.992  1.00 168.11 ?  1047 HIS B C   1 
ATOM   5655 O O   . HIS B 1 797 ? 59.671  14.861  73.052  1.00 166.26 ?  1047 HIS B O   1 
ATOM   5656 C CB  . HIS B 1 797 ? 59.367  17.815  71.326  1.00 155.21 ?  1047 HIS B CB  1 
ATOM   5657 C CG  . HIS B 1 797 ? 58.333  18.766  70.807  1.00 160.01 ?  1047 HIS B CG  1 
ATOM   5658 N ND1 . HIS B 1 797 ? 57.664  18.561  69.620  1.00 161.56 ?  1047 HIS B ND1 1 
ATOM   5659 C CD2 . HIS B 1 797 ? 57.843  19.920  71.320  1.00 156.99 ?  1047 HIS B CD2 1 
ATOM   5660 C CE1 . HIS B 1 797 ? 56.810  19.549  69.421  1.00 154.59 ?  1047 HIS B CE1 1 
ATOM   5661 N NE2 . HIS B 1 797 ? 56.900  20.388  70.438  1.00 153.62 ?  1047 HIS B NE2 1 
ATOM   5662 N N   . SER B 1 798 ? 61.088  15.304  71.349  1.00 177.33 ?  1048 SER B N   1 
ATOM   5663 C CA  . SER B 1 798 ? 62.070  14.285  71.715  1.00 182.52 ?  1048 SER B CA  1 
ATOM   5664 C C   . SER B 1 798 ? 62.399  14.324  73.200  1.00 196.02 ?  1048 SER B C   1 
ATOM   5665 O O   . SER B 1 798 ? 62.960  15.303  73.700  1.00 209.45 ?  1048 SER B O   1 
ATOM   5666 C CB  . SER B 1 798 ? 63.341  14.466  70.883  1.00 184.58 ?  1048 SER B CB  1 
ATOM   5667 O OG  . SER B 1 798 ? 63.100  14.166  69.519  1.00 181.56 ?  1048 SER B OG  1 
ATOM   5668 N N   . GLY B 1 799 ? 62.046  13.248  73.900  1.00 180.57 ?  1049 GLY B N   1 
ATOM   5669 C CA  . GLY B 1 799 ? 62.232  13.157  75.331  1.00 178.49 ?  1049 GLY B CA  1 
ATOM   5670 C C   . GLY B 1 799 ? 61.001  13.458  76.157  1.00 171.18 ?  1049 GLY B C   1 
ATOM   5671 O O   . GLY B 1 799 ? 61.060  13.339  77.386  1.00 179.00 ?  1049 GLY B O   1 
ATOM   5672 N N   . SER B 1 800 ? 59.891  13.846  75.527  1.00 173.06 ?  1050 SER B N   1 
ATOM   5673 C CA  . SER B 1 800 ? 58.655  14.149  76.248  1.00 162.78 ?  1050 SER B CA  1 
ATOM   5674 C C   . SER B 1 800 ? 57.973  12.834  76.612  1.00 151.38 ?  1050 SER B C   1 
ATOM   5675 O O   . SER B 1 800 ? 57.093  12.328  75.911  1.00 148.62 ?  1050 SER B O   1 
ATOM   5676 C CB  . SER B 1 800 ? 57.745  15.043  75.417  1.00 158.12 ?  1050 SER B CB  1 
ATOM   5677 O OG  . SER B 1 800 ? 57.506  14.475  74.140  1.00 153.23 ?  1050 SER B OG  1 
ATOM   5678 N N   . LYS B 1 801 ? 58.401  12.271  77.738  1.00 136.79 ?  1051 LYS B N   1 
ATOM   5679 C CA  . LYS B 1 801 ? 57.789  11.058  78.266  1.00 120.59 ?  1051 LYS B CA  1 
ATOM   5680 C C   . LYS B 1 801 ? 56.377  11.377  78.738  1.00 123.35 ?  1051 LYS B C   1 
ATOM   5681 O O   . LYS B 1 801 ? 56.191  12.114  79.712  1.00 120.16 ?  1051 LYS B O   1 
ATOM   5682 C CB  . LYS B 1 801 ? 58.633  10.496  79.405  1.00 116.83 ?  1051 LYS B CB  1 
ATOM   5683 C CG  . LYS B 1 801 ? 60.064  10.167  79.023  1.00 122.84 ?  1051 LYS B CG  1 
ATOM   5684 C CD  . LYS B 1 801 ? 60.777  9.443   80.152  1.00 114.48 ?  1051 LYS B CD  1 
ATOM   5685 C CE  . LYS B 1 801 ? 62.209  9.104   79.774  1.00 118.64 ?  1051 LYS B CE  1 
ATOM   5686 N NZ  . LYS B 1 801 ? 62.883  8.301   80.831  1.00 120.97 1  1051 LYS B NZ  1 
ATOM   5687 N N   . PHE B 1 802 ? 55.379  10.833  78.049  1.00 118.47 ?  1052 PHE B N   1 
ATOM   5688 C CA  . PHE B 1 802 ? 53.995  11.102  78.411  1.00 102.61 ?  1052 PHE B CA  1 
ATOM   5689 C C   . PHE B 1 802 ? 53.625  10.368  79.691  1.00 105.44 ?  1052 PHE B C   1 
ATOM   5690 O O   . PHE B 1 802 ? 53.955  9.193   79.875  1.00 113.62 ?  1052 PHE B O   1 
ATOM   5691 C CB  . PHE B 1 802 ? 53.057  10.691  77.279  1.00 100.20 ?  1052 PHE B CB  1 
ATOM   5692 C CG  . PHE B 1 802 ? 53.345  11.383  75.983  1.00 107.40 ?  1052 PHE B CG  1 
ATOM   5693 C CD1 . PHE B 1 802 ? 52.839  12.647  75.732  1.00 106.76 ?  1052 PHE B CD1 1 
ATOM   5694 C CD2 . PHE B 1 802 ? 54.128  10.774  75.019  1.00 115.72 ?  1052 PHE B CD2 1 
ATOM   5695 C CE1 . PHE B 1 802 ? 53.107  13.287  74.542  1.00 116.49 ?  1052 PHE B CE1 1 
ATOM   5696 C CE2 . PHE B 1 802 ? 54.400  11.408  73.827  1.00 112.75 ?  1052 PHE B CE2 1 
ATOM   5697 C CZ  . PHE B 1 802 ? 53.889  12.665  73.588  1.00 125.54 ?  1052 PHE B CZ  1 
ATOM   5698 N N   . MET B 1 803 ? 52.935  11.073  80.581  1.00 108.29 ?  1053 MET B N   1 
ATOM   5699 C CA  . MET B 1 803 ? 52.518  10.522  81.859  1.00 110.20 ?  1053 MET B CA  1 
ATOM   5700 C C   . MET B 1 803 ? 51.112  11.010  82.173  1.00 104.83 ?  1053 MET B C   1 
ATOM   5701 O O   . MET B 1 803 ? 50.579  11.910  81.517  1.00 96.07  ?  1053 MET B O   1 
ATOM   5702 C CB  . MET B 1 803 ? 53.497  10.903  82.976  1.00 101.45 ?  1053 MET B CB  1 
ATOM   5703 C CG  . MET B 1 803 ? 54.058  12.310  82.852  1.00 109.72 ?  1053 MET B CG  1 
ATOM   5704 S SD  . MET B 1 803 ? 55.364  12.638  84.051  1.00 121.47 ?  1053 MET B SD  1 
ATOM   5705 C CE  . MET B 1 803 ? 55.987  14.204  83.448  1.00 116.09 ?  1053 MET B CE  1 
ATOM   5706 N N   . CYS B 1 804 ? 50.509  10.399  83.185  1.00 99.59  ?  1054 CYS B N   1 
ATOM   5707 C CA  . CYS B 1 804 ? 49.165  10.744  83.621  1.00 102.61 ?  1054 CYS B CA  1 
ATOM   5708 C C   . CYS B 1 804 ? 49.252  11.580  84.888  1.00 110.43 ?  1054 CYS B C   1 
ATOM   5709 O O   . CYS B 1 804 ? 49.946  11.204  85.838  1.00 111.03 ?  1054 CYS B O   1 
ATOM   5710 C CB  . CYS B 1 804 ? 48.338  9.484   83.861  1.00 115.42 ?  1054 CYS B CB  1 
ATOM   5711 S SG  . CYS B 1 804 ? 48.343  8.384   82.441  1.00 114.82 ?  1054 CYS B SG  1 
ATOM   5712 N N   . CYS B 1 805 ? 48.554  12.711  84.895  1.00 110.47 ?  1055 CYS B N   1 
ATOM   5713 C CA  . CYS B 1 805 ? 48.617  13.662  85.994  1.00 104.52 ?  1055 CYS B CA  1 
ATOM   5714 C C   . CYS B 1 805 ? 47.217  13.929  86.523  1.00 103.01 ?  1055 CYS B C   1 
ATOM   5715 O O   . CYS B 1 805 ? 46.311  14.268  85.755  1.00 102.16 ?  1055 CYS B O   1 
ATOM   5716 C CB  . CYS B 1 805 ? 49.271  14.972  85.548  1.00 105.05 ?  1055 CYS B CB  1 
ATOM   5717 S SG  . CYS B 1 805 ? 50.941  14.797  84.874  1.00 117.39 ?  1055 CYS B SG  1 
ATOM   5718 N N   . HIS B 1 806 ? 47.045  13.765  87.832  1.00 103.91 ?  1056 HIS B N   1 
ATOM   5719 C CA  . HIS B 1 806 ? 45.826  14.159  88.528  1.00 96.77  ?  1056 HIS B CA  1 
ATOM   5720 C C   . HIS B 1 806 ? 46.092  15.521  89.159  1.00 93.53  ?  1056 HIS B C   1 
ATOM   5721 O O   . HIS B 1 806 ? 46.820  15.618  90.153  1.00 98.59  ?  1056 HIS B O   1 
ATOM   5722 C CB  . HIS B 1 806 ? 45.436  13.119  89.576  1.00 90.14  ?  1056 HIS B CB  1 
ATOM   5723 C CG  . HIS B 1 806 ? 44.143  13.414  90.270  1.00 90.80  ?  1056 HIS B CG  1 
ATOM   5724 N ND1 . HIS B 1 806 ? 44.033  13.474  91.643  1.00 84.48  ?  1056 HIS B ND1 1 
ATOM   5725 C CD2 . HIS B 1 806 ? 42.905  13.665  89.783  1.00 89.46  ?  1056 HIS B CD2 1 
ATOM   5726 C CE1 . HIS B 1 806 ? 42.783  13.748  91.971  1.00 88.79  ?  1056 HIS B CE1 1 
ATOM   5727 N NE2 . HIS B 1 806 ? 42.078  13.869  90.861  1.00 79.99  ?  1056 HIS B NE2 1 
ATOM   5728 N N   . ASP B 1 807 ? 45.511  16.569  88.569  1.00 94.54  ?  1057 ASP B N   1 
ATOM   5729 C CA  . ASP B 1 807 ? 45.821  17.951  88.923  1.00 93.05  ?  1057 ASP B CA  1 
ATOM   5730 C C   . ASP B 1 807 ? 47.308  18.226  88.735  1.00 100.24 ?  1057 ASP B C   1 
ATOM   5731 O O   . ASP B 1 807 ? 47.726  18.721  87.683  1.00 99.63  ?  1057 ASP B O   1 
ATOM   5732 C CB  . ASP B 1 807 ? 45.389  18.263  90.359  1.00 86.47  ?  1057 ASP B CB  1 
ATOM   5733 C CG  . ASP B 1 807 ? 43.887  18.397  90.499  1.00 86.78  ?  1057 ASP B CG  1 
ATOM   5734 O OD1 . ASP B 1 807 ? 43.199  18.473  89.459  1.00 73.47  ?  1057 ASP B OD1 1 
ATOM   5735 O OD2 . ASP B 1 807 ? 43.396  18.427  91.648  1.00 87.15  -1 1057 ASP B OD2 1 
ATOM   5736 N N   . THR B 1 808 ? 48.116  17.908  89.748  1.00 96.73  ?  1058 THR B N   1 
ATOM   5737 C CA  . THR B 1 808 ? 49.562  18.046  89.654  1.00 98.54  ?  1058 THR B CA  1 
ATOM   5738 C C   . THR B 1 808 ? 50.323  16.773  89.997  1.00 104.81 ?  1058 THR B C   1 
ATOM   5739 O O   . THR B 1 808 ? 51.533  16.718  89.750  1.00 104.31 ?  1058 THR B O   1 
ATOM   5740 C CB  . THR B 1 808 ? 50.060  19.182  90.562  1.00 96.12  ?  1058 THR B CB  1 
ATOM   5741 O OG1 . THR B 1 808 ? 49.453  19.066  91.855  1.00 105.25 ?  1058 THR B OG1 1 
ATOM   5742 C CG2 . THR B 1 808 ? 49.717  20.538  89.960  1.00 88.28  ?  1058 THR B CG2 1 
ATOM   5743 N N   . LYS B 1 809 ? 49.663  15.757  90.551  1.00 103.35 ?  1059 LYS B N   1 
ATOM   5744 C CA  . LYS B 1 809 ? 50.307  14.486  90.863  1.00 99.93  ?  1059 LYS B CA  1 
ATOM   5745 C C   . LYS B 1 809 ? 50.449  13.677  89.580  1.00 104.88 ?  1059 LYS B C   1 
ATOM   5746 O O   . LYS B 1 809 ? 49.456  13.182  89.037  1.00 110.03 ?  1059 LYS B O   1 
ATOM   5747 C CB  . LYS B 1 809 ? 49.491  13.717  91.898  1.00 100.31 ?  1059 LYS B CB  1 
ATOM   5748 C CG  . LYS B 1 809 ? 50.247  13.350  93.162  1.00 102.40 ?  1059 LYS B CG  1 
ATOM   5749 C CD  . LYS B 1 809 ? 49.449  12.358  93.994  1.00 101.77 ?  1059 LYS B CD  1 
ATOM   5750 C CE  . LYS B 1 809 ? 50.029  12.202  95.390  1.00 112.97 ?  1059 LYS B CE  1 
ATOM   5751 N NZ  . LYS B 1 809 ? 49.884  13.452  96.187  1.00 108.48 1  1059 LYS B NZ  1 
ATOM   5752 N N   . CYS B 1 810 ? 51.678  13.537  89.093  1.00 100.04 ?  1060 CYS B N   1 
ATOM   5753 C CA  . CYS B 1 810 ? 51.962  12.754  87.901  1.00 105.25 ?  1060 CYS B CA  1 
ATOM   5754 C C   . CYS B 1 810 ? 52.668  11.460  88.287  1.00 110.32 ?  1060 CYS B C   1 
ATOM   5755 O O   . CYS B 1 810 ? 53.372  11.396  89.299  1.00 111.37 ?  1060 CYS B O   1 
ATOM   5756 C CB  . CYS B 1 810 ? 52.827  13.542  86.913  1.00 99.89  ?  1060 CYS B CB  1 
ATOM   5757 S SG  . CYS B 1 810 ? 52.175  15.165  86.445  1.00 128.74 ?  1060 CYS B SG  1 
ATOM   5758 N N   . SER B 1 811 ? 52.471  10.428  87.471  1.00 109.07 ?  1061 SER B N   1 
ATOM   5759 C CA  . SER B 1 811 ? 53.097  9.141   87.736  1.00 115.29 ?  1061 SER B CA  1 
ATOM   5760 C C   . SER B 1 811 ? 54.612  9.247   87.603  1.00 116.74 ?  1061 SER B C   1 
ATOM   5761 O O   . SER B 1 811 ? 55.137  10.060  86.837  1.00 116.81 ?  1061 SER B O   1 
ATOM   5762 C CB  . SER B 1 811 ? 52.565  8.074   86.781  1.00 112.89 ?  1061 SER B CB  1 
ATOM   5763 O OG  . SER B 1 811 ? 53.128  8.220   85.490  1.00 115.18 ?  1061 SER B OG  1 
ATOM   5764 N N   . SER B 1 812 ? 55.317  8.407   88.365  1.00 118.56 ?  1062 SER B N   1 
ATOM   5765 C CA  . SER B 1 812 ? 56.775  8.447   88.355  1.00 118.23 ?  1062 SER B CA  1 
ATOM   5766 C C   . SER B 1 812 ? 57.333  8.019   87.004  1.00 122.87 ?  1062 SER B C   1 
ATOM   5767 O O   . SER B 1 812 ? 58.350  8.556   86.548  1.00 125.13 ?  1062 SER B O   1 
ATOM   5768 C CB  . SER B 1 812 ? 57.332  7.563   89.470  1.00 113.13 ?  1062 SER B CB  1 
ATOM   5769 O OG  . SER B 1 812 ? 56.958  6.209   89.282  1.00 119.76 ?  1062 SER B OG  1 
ATOM   5770 N N   . THR B 1 813 ? 56.684  7.064   86.348  1.00 137.23 ?  1063 THR B N   1 
ATOM   5771 C CA  . THR B 1 813 ? 57.155  6.561   85.068  1.00 139.23 ?  1063 THR B CA  1 
ATOM   5772 C C   . THR B 1 813 ? 56.631  7.424   83.928  1.00 130.18 ?  1063 THR B C   1 
ATOM   5773 O O   . THR B 1 813 ? 55.536  7.988   83.999  1.00 126.89 ?  1063 THR B O   1 
ATOM   5774 C CB  . THR B 1 813 ? 56.718  5.111   84.857  1.00 142.43 ?  1063 THR B CB  1 
ATOM   5775 O OG1 . THR B 1 813 ? 55.383  5.085   84.337  1.00 144.53 ?  1063 THR B OG1 1 
ATOM   5776 C CG2 . THR B 1 813 ? 56.752  4.352   86.173  1.00 138.85 ?  1063 THR B CG2 1 
ATOM   5777 N N   . GLY B 1 814 ? 57.428  7.524   82.877  1.00 121.94 ?  1064 GLY B N   1 
ATOM   5778 C CA  . GLY B 1 814 ? 57.041  8.273   81.693  1.00 117.10 ?  1064 GLY B CA  1 
ATOM   5779 C C   . GLY B 1 814 ? 57.338  7.488   80.436  1.00 115.64 ?  1064 GLY B C   1 
ATOM   5780 O O   . GLY B 1 814 ? 58.363  6.815   80.338  1.00 127.27 ?  1064 GLY B O   1 
ATOM   5781 N N   . LEU B 1 815 ? 56.427  7.582   79.470  1.00 113.93 ?  1065 LEU B N   1 
ATOM   5782 C CA  . LEU B 1 815 ? 56.499  6.807   78.237  1.00 115.85 ?  1065 LEU B CA  1 
ATOM   5783 C C   . LEU B 1 815 ? 56.556  7.745   77.040  1.00 116.21 ?  1065 LEU B C   1 
ATOM   5784 O O   . LEU B 1 815 ? 55.784  8.706   76.960  1.00 114.51 ?  1065 LEU B O   1 
ATOM   5785 C CB  . LEU B 1 815 ? 55.298  5.865   78.114  1.00 113.13 ?  1065 LEU B CB  1 
ATOM   5786 C CG  . LEU B 1 815 ? 55.450  4.427   78.621  1.00 114.06 ?  1065 LEU B CG  1 
ATOM   5787 C CD1 . LEU B 1 815 ? 56.093  4.367   79.999  1.00 114.15 ?  1065 LEU B CD1 1 
ATOM   5788 C CD2 . LEU B 1 815 ? 54.097  3.740   78.646  1.00 116.33 ?  1065 LEU B CD2 1 
ATOM   5789 N N   . VAL B 1 816 ? 57.467  7.458   76.111  1.00 124.17 ?  1066 VAL B N   1 
ATOM   5790 C CA  . VAL B 1 816 ? 57.594  8.239   74.890  1.00 130.18 ?  1066 VAL B CA  1 
ATOM   5791 C C   . VAL B 1 816 ? 56.777  7.576   73.787  1.00 133.71 ?  1066 VAL B C   1 
ATOM   5792 O O   . VAL B 1 816 ? 56.507  6.374   73.813  1.00 136.14 ?  1066 VAL B O   1 
ATOM   5793 C CB  . VAL B 1 816 ? 59.069  8.397   74.465  1.00 125.35 ?  1066 VAL B CB  1 
ATOM   5794 C CG1 . VAL B 1 816 ? 59.851  9.138   75.537  1.00 129.05 ?  1066 VAL B CG1 1 
ATOM   5795 C CG2 . VAL B 1 816 ? 59.691  7.034   74.195  1.00 121.97 ?  1066 VAL B CG2 1 
ATOM   5796 N N   . ALA B 1 817 ? 56.381  8.374   72.801  1.00 134.90 ?  1067 ALA B N   1 
ATOM   5797 C CA  . ALA B 1 817 ? 55.583  7.898   71.686  1.00 136.21 ?  1067 ALA B CA  1 
ATOM   5798 C C   . ALA B 1 817 ? 56.489  7.562   70.504  1.00 141.06 ?  1067 ALA B C   1 
ATOM   5799 O O   . ALA B 1 817 ? 57.711  7.443   70.637  1.00 139.69 ?  1067 ALA B O   1 
ATOM   5800 C CB  . ALA B 1 817 ? 54.524  8.938   71.317  1.00 137.65 ?  1067 ALA B CB  1 
ATOM   5801 N N   . ALA B 1 818 ? 55.886  7.403   69.331  1.00 149.66 ?  1068 ALA B N   1 
ATOM   5802 C CA  . ALA B 1 818 ? 56.592  7.033   68.118  1.00 163.27 ?  1068 ALA B CA  1 
ATOM   5803 C C   . ALA B 1 818 ? 56.633  8.222   67.160  1.00 165.82 ?  1068 ALA B C   1 
ATOM   5804 O O   . ALA B 1 818 ? 56.235  9.342   67.503  1.00 165.31 ?  1068 ALA B O   1 
ATOM   5805 C CB  . ALA B 1 818 ? 55.931  5.806   67.485  1.00 163.21 ?  1068 ALA B CB  1 
ATOM   5806 N N   . ALA B 1 819 ? 57.134  7.975   65.936  1.00 162.80 ?  1069 ALA B N   1 
ATOM   5807 C CA  . ALA B 1 819 ? 57.250  8.963   64.876  1.00 159.83 ?  1069 ALA B CA  1 
ATOM   5808 C C   . ALA B 1 819 ? 55.938  9.076   64.101  1.00 166.28 ?  1069 ALA B C   1 
ATOM   5809 O O   . ALA B 1 819 ? 55.175  8.109   64.018  1.00 163.45 ?  1069 ALA B O   1 
ATOM   5810 C CB  . ALA B 1 819 ? 58.381  8.586   63.920  1.00 159.48 ?  1069 ALA B CB  1 
ATOM   5811 N N   . PRO B 1 820 ? 55.641  10.256  63.521  1.00 167.24 ?  1070 PRO B N   1 
ATOM   5812 C CA  . PRO B 1 820 ? 54.386  10.486  62.792  1.00 163.15 ?  1070 PRO B CA  1 
ATOM   5813 C C   . PRO B 1 820 ? 54.150  9.492   61.657  1.00 161.40 ?  1070 PRO B C   1 
ATOM   5814 O O   . PRO B 1 820 ? 55.120  8.969   61.113  1.00 166.45 ?  1070 PRO B O   1 
ATOM   5815 C CB  . PRO B 1 820 ? 54.561  11.903  62.234  1.00 164.13 ?  1070 PRO B CB  1 
ATOM   5816 C CG  . PRO B 1 820 ? 55.527  12.552  63.155  1.00 159.32 ?  1070 PRO B CG  1 
ATOM   5817 C CD  . PRO B 1 820 ? 56.479  11.467  63.556  1.00 161.40 ?  1070 PRO B CD  1 
ATOM   5818 N N   . SER B 1 833 ? 37.513  16.549  69.035  1.00 115.06 ?  1083 SER B N   1 
ATOM   5819 C CA  . SER B 1 833 ? 36.439  16.339  69.998  1.00 130.21 ?  1083 SER B CA  1 
ATOM   5820 C C   . SER B 1 833 ? 35.633  17.617  70.196  1.00 136.75 ?  1083 SER B C   1 
ATOM   5821 O O   . SER B 1 833 ? 35.970  18.667  69.648  1.00 130.85 ?  1083 SER B O   1 
ATOM   5822 C CB  . SER B 1 833 ? 37.001  15.861  71.339  1.00 118.03 ?  1083 SER B CB  1 
ATOM   5823 O OG  . SER B 1 833 ? 37.708  16.900  71.995  1.00 114.97 ?  1083 SER B OG  1 
ATOM   5824 N N   . ASP B 1 834 ? 34.569  17.524  70.987  1.00 143.64 ?  1084 ASP B N   1 
ATOM   5825 C CA  . ASP B 1 834 ? 33.695  18.653  71.286  1.00 145.66 ?  1084 ASP B CA  1 
ATOM   5826 C C   . ASP B 1 834 ? 33.464  18.760  72.787  1.00 145.90 ?  1084 ASP B C   1 
ATOM   5827 O O   . ASP B 1 834 ? 32.332  18.780  73.273  1.00 134.91 ?  1084 ASP B O   1 
ATOM   5828 C CB  . ASP B 1 834 ? 32.375  18.529  70.527  1.00 151.91 ?  1084 ASP B CB  1 
ATOM   5829 C CG  . ASP B 1 834 ? 31.749  17.150  70.656  1.00 157.94 ?  1084 ASP B CG  1 
ATOM   5830 O OD1 . ASP B 1 834 ? 32.105  16.409  71.598  1.00 148.11 ?  1084 ASP B OD1 1 
ATOM   5831 O OD2 . ASP B 1 834 ? 30.902  16.802  69.805  1.00 164.23 -1 1084 ASP B OD2 1 
ATOM   5832 N N   . LYS B 1 835 ? 34.555  18.830  73.546  1.00 133.06 ?  1085 LYS B N   1 
ATOM   5833 C CA  . LYS B 1 835 ? 34.503  18.914  74.997  1.00 114.23 ?  1085 LYS B CA  1 
ATOM   5834 C C   . LYS B 1 835 ? 35.169  20.203  75.459  1.00 99.84  ?  1085 LYS B C   1 
ATOM   5835 O O   . LYS B 1 835 ? 36.029  20.757  74.768  1.00 108.01 ?  1085 LYS B O   1 
ATOM   5836 C CB  . LYS B 1 835 ? 35.194  17.708  75.650  1.00 110.39 ?  1085 LYS B CB  1 
ATOM   5837 C CG  . LYS B 1 835 ? 35.108  16.415  74.845  1.00 110.38 ?  1085 LYS B CG  1 
ATOM   5838 C CD  . LYS B 1 835 ? 33.681  15.905  74.735  1.00 131.30 ?  1085 LYS B CD  1 
ATOM   5839 C CE  . LYS B 1 835 ? 33.609  14.637  73.897  1.00 133.43 ?  1085 LYS B CE  1 
ATOM   5840 N NZ  . LYS B 1 835 ? 34.037  14.870  72.489  1.00 129.40 1  1085 LYS B NZ  1 
ATOM   5841 N N   . ILE B 1 836 ? 34.767  20.679  76.634  1.00 95.41  ?  1086 ILE B N   1 
ATOM   5842 C CA  . ILE B 1 836 ? 35.325  21.888  77.230  1.00 94.28  ?  1086 ILE B CA  1 
ATOM   5843 C C   . ILE B 1 836 ? 35.950  21.517  78.568  1.00 86.48  ?  1086 ILE B C   1 
ATOM   5844 O O   . ILE B 1 836 ? 35.291  20.907  79.419  1.00 85.67  ?  1086 ILE B O   1 
ATOM   5845 C CB  . ILE B 1 836 ? 34.261  22.986  77.409  1.00 88.23  ?  1086 ILE B CB  1 
ATOM   5846 C CG1 . ILE B 1 836 ? 33.597  23.310  76.069  1.00 95.83  ?  1086 ILE B CG1 1 
ATOM   5847 C CG2 . ILE B 1 836 ? 34.889  24.238  78.003  1.00 76.93  ?  1086 ILE B CG2 1 
ATOM   5848 C CD1 . ILE B 1 836 ? 32.589  24.438  76.143  1.00 104.98 ?  1086 ILE B CD1 1 
ATOM   5849 N N   . PHE B 1 837 ? 37.214  21.889  78.751  1.00 76.39  ?  1087 PHE B N   1 
ATOM   5850 C CA  . PHE B 1 837 ? 37.957  21.596  79.968  1.00 75.37  ?  1087 PHE B CA  1 
ATOM   5851 C C   . PHE B 1 837 ? 38.464  22.895  80.578  1.00 87.79  ?  1087 PHE B C   1 
ATOM   5852 O O   . PHE B 1 837 ? 38.975  23.767  79.867  1.00 85.86  ?  1087 PHE B O   1 
ATOM   5853 C CB  . PHE B 1 837 ? 39.127  20.648  79.681  1.00 80.99  ?  1087 PHE B CB  1 
ATOM   5854 C CG  . PHE B 1 837 ? 39.725  20.030  80.912  1.00 75.77  ?  1087 PHE B CG  1 
ATOM   5855 C CD1 . PHE B 1 837 ? 39.099  18.967  81.542  1.00 70.21  ?  1087 PHE B CD1 1 
ATOM   5856 C CD2 . PHE B 1 837 ? 40.916  20.504  81.434  1.00 70.56  ?  1087 PHE B CD2 1 
ATOM   5857 C CE1 . PHE B 1 837 ? 39.646  18.392  82.673  1.00 69.82  ?  1087 PHE B CE1 1 
ATOM   5858 C CE2 . PHE B 1 837 ? 41.470  19.933  82.564  1.00 72.13  ?  1087 PHE B CE2 1 
ATOM   5859 C CZ  . PHE B 1 837 ? 40.833  18.876  83.185  1.00 72.54  ?  1087 PHE B CZ  1 
ATOM   5860 N N   . ASP B 1 838 ? 38.316  23.022  81.898  1.00 82.73  ?  1088 ASP B N   1 
ATOM   5861 C CA  . ASP B 1 838 ? 38.702  24.248  82.603  1.00 77.43  ?  1088 ASP B CA  1 
ATOM   5862 C C   . ASP B 1 838 ? 39.102  23.851  84.026  1.00 75.55  ?  1088 ASP B C   1 
ATOM   5863 O O   . ASP B 1 838 ? 38.260  23.786  84.924  1.00 81.59  ?  1088 ASP B O   1 
ATOM   5864 C CB  . ASP B 1 838 ? 37.569  25.265  82.598  1.00 80.03  ?  1088 ASP B CB  1 
ATOM   5865 C CG  . ASP B 1 838 ? 38.006  26.643  83.074  1.00 78.37  ?  1088 ASP B CG  1 
ATOM   5866 O OD1 . ASP B 1 838 ? 39.005  26.744  83.818  1.00 73.59  ?  1088 ASP B OD1 1 
ATOM   5867 O OD2 . ASP B 1 838 ? 37.340  27.633  82.704  1.00 78.39  -1 1088 ASP B OD2 1 
ATOM   5868 N N   . ASP B 1 839 ? 40.395  23.592  84.216  1.00 69.83  ?  1089 ASP B N   1 
ATOM   5869 C CA  . ASP B 1 839 ? 40.938  23.262  85.527  1.00 73.97  ?  1089 ASP B CA  1 
ATOM   5870 C C   . ASP B 1 839 ? 41.802  24.382  86.094  1.00 72.90  ?  1089 ASP B C   1 
ATOM   5871 O O   . ASP B 1 839 ? 42.509  24.169  87.085  1.00 80.40  ?  1089 ASP B O   1 
ATOM   5872 C CB  . ASP B 1 839 ? 41.733  21.955  85.458  1.00 74.90  ?  1089 ASP B CB  1 
ATOM   5873 C CG  . ASP B 1 839 ? 43.064  22.117  84.753  1.00 81.36  ?  1089 ASP B CG  1 
ATOM   5874 O OD1 . ASP B 1 839 ? 44.110  21.869  85.392  1.00 88.58  ?  1089 ASP B OD1 1 
ATOM   5875 O OD2 . ASP B 1 839 ? 43.065  22.504  83.565  1.00 96.56  -1 1089 ASP B OD2 1 
ATOM   5876 N N   . GLY B 1 840 ? 41.762  25.568  85.490  1.00 77.32  ?  1090 GLY B N   1 
ATOM   5877 C CA  . GLY B 1 840 ? 42.493  26.714  85.986  1.00 79.92  ?  1090 GLY B CA  1 
ATOM   5878 C C   . GLY B 1 840 ? 43.984  26.695  85.744  1.00 88.54  ?  1090 GLY B C   1 
ATOM   5879 O O   . GLY B 1 840 ? 44.694  27.543  86.297  1.00 97.78  ?  1090 GLY B O   1 
ATOM   5880 N N   . ALA B 1 841 ? 44.483  25.760  84.940  1.00 91.40  ?  1091 ALA B N   1 
ATOM   5881 C CA  . ALA B 1 841 ? 45.909  25.685  84.682  1.00 94.27  ?  1091 ALA B CA  1 
ATOM   5882 C C   . ALA B 1 841 ? 46.352  26.848  83.794  1.00 92.96  ?  1091 ALA B C   1 
ATOM   5883 O O   . ALA B 1 841 ? 45.579  27.337  82.966  1.00 92.51  ?  1091 ALA B O   1 
ATOM   5884 C CB  . ALA B 1 841 ? 46.262  24.356  84.017  1.00 93.56  ?  1091 ALA B CB  1 
ATOM   5885 N N   . PRO B 1 842 ? 47.590  27.318  83.958  1.00 94.38  ?  1092 PRO B N   1 
ATOM   5886 C CA  . PRO B 1 842 ? 48.069  28.423  83.118  1.00 98.65  ?  1092 PRO B CA  1 
ATOM   5887 C C   . PRO B 1 842 ? 48.159  28.009  81.655  1.00 103.55 ?  1092 PRO B C   1 
ATOM   5888 O O   . PRO B 1 842 ? 48.470  26.863  81.327  1.00 109.74 ?  1092 PRO B O   1 
ATOM   5889 C CB  . PRO B 1 842 ? 49.453  28.740  83.700  1.00 98.75  ?  1092 PRO B CB  1 
ATOM   5890 C CG  . PRO B 1 842 ? 49.439  28.156  85.081  1.00 84.72  ?  1092 PRO B CG  1 
ATOM   5891 C CD  . PRO B 1 842 ? 48.563  26.946  84.997  1.00 99.60  ?  1092 PRO B CD  1 
ATOM   5892 N N   . GLU B 1 843 ? 47.882  28.964  80.771  1.00 113.40 ?  1093 GLU B N   1 
ATOM   5893 C CA  . GLU B 1 843 ? 47.940  28.717  79.333  1.00 121.08 ?  1093 GLU B CA  1 
ATOM   5894 C C   . GLU B 1 843 ? 49.368  28.847  78.818  1.00 119.29 ?  1093 GLU B C   1 
ATOM   5895 O O   . GLU B 1 843 ? 50.258  29.291  79.541  1.00 112.91 ?  1093 GLU B O   1 
ATOM   5896 C CB  . GLU B 1 843 ? 47.023  29.682  78.579  1.00 131.73 ?  1093 GLU B CB  1 
ATOM   5897 C CG  . GLU B 1 843 ? 45.596  29.714  79.098  1.00 134.29 ?  1093 GLU B CG  1 
ATOM   5898 C CD  . GLU B 1 843 ? 44.689  30.597  78.264  1.00 145.17 ?  1093 GLU B CD  1 
ATOM   5899 O OE1 . GLU B 1 843 ? 44.144  30.105  77.253  1.00 139.13 ?  1093 GLU B OE1 1 
ATOM   5900 O OE2 . GLU B 1 843 ? 44.531  31.786  78.616  1.00 145.35 -1 1093 GLU B OE2 1 
ATOM   5901 N N   . GLN C 2 3   ? -31.803 -11.132 37.610  1.00 107.36 ?  1    GLN H N   1 
ATOM   5902 C CA  . GLN C 2 3   ? -32.541 -10.723 36.422  1.00 110.46 ?  1    GLN H CA  1 
ATOM   5903 C C   . GLN C 2 3   ? -33.076 -9.305  36.578  1.00 96.48  ?  1    GLN H C   1 
ATOM   5904 O O   . GLN C 2 3   ? -32.949 -8.698  37.641  1.00 94.91  ?  1    GLN H O   1 
ATOM   5905 C CB  . GLN C 2 3   ? -33.700 -11.682 36.147  1.00 113.85 ?  1    GLN H CB  1 
ATOM   5906 C CG  . GLN C 2 3   ? -34.882 -11.496 37.085  1.00 110.16 ?  1    GLN H CG  1 
ATOM   5907 C CD  . GLN C 2 3   ? -36.107 -12.270 36.641  1.00 117.54 ?  1    GLN H CD  1 
ATOM   5908 O OE1 . GLN C 2 3   ? -35.998 -13.371 36.101  1.00 118.69 ?  1    GLN H OE1 1 
ATOM   5909 N NE2 . GLN C 2 3   ? -37.283 -11.692 36.858  1.00 112.88 ?  1    GLN H NE2 1 
ATOM   5910 N N   . VAL C 2 4   ? -33.682 -8.786  35.514  1.00 93.27  ?  2    VAL H N   1 
ATOM   5911 C CA  . VAL C 2 4   ? -34.308 -7.471  35.520  1.00 91.95  ?  2    VAL H CA  1 
ATOM   5912 C C   . VAL C 2 4   ? -35.819 -7.656  35.515  1.00 96.24  ?  2    VAL H C   1 
ATOM   5913 O O   . VAL C 2 4   ? -36.346 -8.545  34.835  1.00 102.73 ?  2    VAL H O   1 
ATOM   5914 C CB  . VAL C 2 4   ? -33.846 -6.611  34.326  1.00 79.11  ?  2    VAL H CB  1 
ATOM   5915 C CG1 . VAL C 2 4   ? -32.340 -6.419  34.367  1.00 88.73  ?  2    VAL H CG1 1 
ATOM   5916 C CG2 . VAL C 2 4   ? -34.266 -7.237  33.004  1.00 81.50  ?  2    VAL H CG2 1 
ATOM   5917 N N   . GLN C 2 5   ? -36.513 -6.828  36.291  1.00 92.54  ?  3    GLN H N   1 
ATOM   5918 C CA  . GLN C 2 5   ? -37.967 -6.884  36.365  1.00 87.39  ?  3    GLN H CA  1 
ATOM   5919 C C   . GLN C 2 5   ? -38.470 -5.634  37.070  1.00 91.16  ?  3    GLN H C   1 
ATOM   5920 O O   . GLN C 2 5   ? -37.732 -4.975  37.809  1.00 94.37  ?  3    GLN H O   1 
ATOM   5921 C CB  . GLN C 2 5   ? -38.455 -8.141  37.095  1.00 93.95  ?  3    GLN H CB  1 
ATOM   5922 C CG  . GLN C 2 5   ? -38.203 -8.135  38.594  1.00 100.37 ?  3    GLN H CG  1 
ATOM   5923 C CD  . GLN C 2 5   ? -38.678 -9.408  39.267  1.00 103.02 ?  3    GLN H CD  1 
ATOM   5924 O OE1 . GLN C 2 5   ? -38.905 -10.423 38.610  1.00 106.64 ?  3    GLN H OE1 1 
ATOM   5925 N NE2 . GLN C 2 5   ? -38.833 -9.358  40.585  1.00 98.54  ?  3    GLN H NE2 1 
ATOM   5926 N N   . LEU C 2 6   ? -39.740 -5.322  36.829  1.00 95.45  ?  4    LEU H N   1 
ATOM   5927 C CA  . LEU C 2 6   ? -40.415 -4.186  37.441  1.00 89.71  ?  4    LEU H CA  1 
ATOM   5928 C C   . LEU C 2 6   ? -41.715 -4.676  38.059  1.00 85.80  ?  4    LEU H C   1 
ATOM   5929 O O   . LEU C 2 6   ? -42.491 -5.374  37.399  1.00 100.43 ?  4    LEU H O   1 
ATOM   5930 C CB  . LEU C 2 6   ? -40.696 -3.088  36.410  1.00 91.53  ?  4    LEU H CB  1 
ATOM   5931 C CG  . LEU C 2 6   ? -39.499 -2.575  35.606  1.00 86.83  ?  4    LEU H CG  1 
ATOM   5932 C CD1 . LEU C 2 6   ? -39.969 -1.856  34.354  1.00 77.62  ?  4    LEU H CD1 1 
ATOM   5933 C CD2 . LEU C 2 6   ? -38.631 -1.658  36.453  1.00 97.79  ?  4    LEU H CD2 1 
ATOM   5934 N N   . VAL C 2 7   ? -41.947 -4.320  39.319  1.00 87.62  ?  5    VAL H N   1 
ATOM   5935 C CA  . VAL C 2 7   ? -43.152 -4.715  40.039  1.00 98.16  ?  5    VAL H CA  1 
ATOM   5936 C C   . VAL C 2 7   ? -43.848 -3.458  40.543  1.00 94.25  ?  5    VAL H C   1 
ATOM   5937 O O   . VAL C 2 7   ? -43.217 -2.601  41.173  1.00 98.29  ?  5    VAL H O   1 
ATOM   5938 C CB  . VAL C 2 7   ? -42.837 -5.682  41.197  1.00 94.38  ?  5    VAL H CB  1 
ATOM   5939 C CG1 . VAL C 2 7   ? -42.494 -7.060  40.653  1.00 83.02  ?  5    VAL H CG1 1 
ATOM   5940 C CG2 . VAL C 2 7   ? -41.692 -5.156  42.050  1.00 105.78 ?  5    VAL H CG2 1 
ATOM   5941 N N   . GLU C 2 8   ? -45.139 -3.344  40.251  1.00 92.60  ?  6    GLU H N   1 
ATOM   5942 C CA  . GLU C 2 8   ? -45.941 -2.211  40.684  1.00 101.10 ?  6    GLU H CA  1 
ATOM   5943 C C   . GLU C 2 8   ? -46.747 -2.573  41.925  1.00 98.50  ?  6    GLU H C   1 
ATOM   5944 O O   . GLU C 2 8   ? -46.988 -3.745  42.224  1.00 96.55  ?  6    GLU H O   1 
ATOM   5945 C CB  . GLU C 2 8   ? -46.882 -1.742  39.571  1.00 101.56 ?  6    GLU H CB  1 
ATOM   5946 C CG  . GLU C 2 8   ? -46.177 -1.174  38.352  1.00 92.47  ?  6    GLU H CG  1 
ATOM   5947 C CD  . GLU C 2 8   ? -46.067 -2.175  37.221  1.00 102.38 ?  6    GLU H CD  1 
ATOM   5948 O OE1 . GLU C 2 8   ? -46.127 -1.752  36.047  1.00 83.29  ?  6    GLU H OE1 1 
ATOM   5949 O OE2 . GLU C 2 8   ? -45.930 -3.385  37.504  1.00 98.57  -1 6    GLU H OE2 1 
ATOM   5950 N N   . SER C 2 9   ? -47.166 -1.538  42.647  1.00 94.21  ?  7    SER H N   1 
ATOM   5951 C CA  . SER C 2 9   ? -47.950 -1.708  43.862  1.00 106.36 ?  7    SER H CA  1 
ATOM   5952 C C   . SER C 2 9   ? -48.605 -0.373  44.194  1.00 108.21 ?  7    SER H C   1 
ATOM   5953 O O   . SER C 2 9   ? -48.379 0.637   43.521  1.00 97.63  ?  7    SER H O   1 
ATOM   5954 C CB  . SER C 2 9   ? -47.080 -2.216  45.014  1.00 105.83 ?  7    SER H CB  1 
ATOM   5955 O OG  . SER C 2 9   ? -45.999 -1.334  45.263  1.00 103.98 ?  7    SER H OG  1 
ATOM   5956 N N   . GLY C 2 10  ? -49.430 -0.377  45.239  1.00 110.14 ?  8    GLY H N   1 
ATOM   5957 C CA  . GLY C 2 10  ? -50.096 0.825   45.692  1.00 109.64 ?  8    GLY H CA  1 
ATOM   5958 C C   . GLY C 2 10  ? -51.416 1.131   45.016  1.00 108.82 ?  8    GLY H C   1 
ATOM   5959 O O   . GLY C 2 10  ? -52.070 2.112   45.394  1.00 95.90  ?  8    GLY H O   1 
ATOM   5960 N N   . GLY C 2 11  ? -51.832 0.333   44.035  1.00 108.53 ?  9    GLY H N   1 
ATOM   5961 C CA  . GLY C 2 11  ? -53.084 0.598   43.357  1.00 100.71 ?  9    GLY H CA  1 
ATOM   5962 C C   . GLY C 2 11  ? -54.284 0.289   44.232  1.00 121.26 ?  9    GLY H C   1 
ATOM   5963 O O   . GLY C 2 11  ? -54.238 -0.557  45.123  1.00 109.63 ?  9    GLY H O   1 
ATOM   5964 N N   . GLY C 2 12  ? -55.372 0.991   43.967  1.00 120.19 ?  10   GLY H N   1 
ATOM   5965 C CA  . GLY C 2 12  ? -56.571 0.815   44.752  1.00 123.39 ?  10   GLY H CA  1 
ATOM   5966 C C   . GLY C 2 12  ? -57.752 1.455   44.067  1.00 124.25 ?  10   GLY H C   1 
ATOM   5967 O O   . GLY C 2 12  ? -57.754 1.654   42.852  1.00 125.79 ?  10   GLY H O   1 
ATOM   5968 N N   . VAL C 2 13  ? -58.762 1.781   44.871  1.00 128.78 ?  11   VAL H N   1 
ATOM   5969 C CA  . VAL C 2 13  ? -59.984 2.415   44.387  1.00 124.50 ?  11   VAL H CA  1 
ATOM   5970 C C   . VAL C 2 13  ? -60.442 3.428   45.425  1.00 120.63 ?  11   VAL H C   1 
ATOM   5971 O O   . VAL C 2 13  ? -60.675 3.068   46.585  1.00 117.98 ?  11   VAL H O   1 
ATOM   5972 C CB  . VAL C 2 13  ? -61.109 1.399   44.119  1.00 122.84 ?  11   VAL H CB  1 
ATOM   5973 C CG1 . VAL C 2 13  ? -62.441 2.112   44.018  1.00 116.24 ?  11   VAL H CG1 1 
ATOM   5974 C CG2 . VAL C 2 13  ? -60.831 0.610   42.852  1.00 131.70 ?  11   VAL H CG2 1 
ATOM   5975 N N   . VAL C 2 14  ? -60.578 4.690   45.012  1.00 124.96 ?  12   VAL H N   1 
ATOM   5976 C CA  . VAL C 2 14  ? -61.051 5.759   45.888  1.00 127.39 ?  12   VAL H CA  1 
ATOM   5977 C C   . VAL C 2 14  ? -62.031 6.651   45.134  1.00 120.69 ?  12   VAL H C   1 
ATOM   5978 O O   . VAL C 2 14  ? -62.410 6.358   43.995  1.00 117.68 ?  12   VAL H O   1 
ATOM   5979 C CB  . VAL C 2 14  ? -59.881 6.591   46.447  1.00 131.10 ?  12   VAL H CB  1 
ATOM   5980 C CG1 . VAL C 2 14  ? -59.087 5.786   47.466  1.00 130.00 ?  12   VAL H CG1 1 
ATOM   5981 C CG2 . VAL C 2 14  ? -58.981 7.066   45.312  1.00 110.34 ?  12   VAL H CG2 1 
ATOM   5982 N N   . GLN C 2 15  ? -62.437 7.753   45.766  1.00 116.96 ?  13   GLN H N   1 
ATOM   5983 C CA  . GLN C 2 15  ? -63.391 8.708   45.226  1.00 116.18 ?  13   GLN H CA  1 
ATOM   5984 C C   . GLN C 2 15  ? -62.671 9.855   44.532  1.00 125.12 ?  13   GLN H C   1 
ATOM   5985 O O   . GLN C 2 15  ? -61.490 10.109  44.790  1.00 130.18 ?  13   GLN H O   1 
ATOM   5986 C CB  . GLN C 2 15  ? -64.275 9.248   46.348  1.00 115.87 ?  13   GLN H CB  1 
ATOM   5987 C CG  . GLN C 2 15  ? -65.060 8.181   47.094  1.00 107.36 ?  13   GLN H CG  1 
ATOM   5988 C CD  . GLN C 2 15  ? -65.853 8.748   48.255  1.00 112.14 ?  13   GLN H CD  1 
ATOM   5989 O OE1 . GLN C 2 15  ? -67.083 8.800   48.217  1.00 108.57 ?  13   GLN H OE1 1 
ATOM   5990 N NE2 . GLN C 2 15  ? -65.151 9.172   49.299  1.00 117.24 ?  13   GLN H NE2 1 
ATOM   5991 N N   . PRO C 2 16  ? -63.353 10.564  43.630  1.00 131.83 ?  14   PRO H N   1 
ATOM   5992 C CA  . PRO C 2 16  ? -62.727 11.725  42.985  1.00 111.88 ?  14   PRO H CA  1 
ATOM   5993 C C   . PRO C 2 16  ? -62.345 12.789  44.003  1.00 115.31 ?  14   PRO H C   1 
ATOM   5994 O O   . PRO C 2 16  ? -63.078 13.057  44.957  1.00 114.73 ?  14   PRO H O   1 
ATOM   5995 C CB  . PRO C 2 16  ? -63.813 12.226  42.026  1.00 102.30 ?  14   PRO H CB  1 
ATOM   5996 C CG  . PRO C 2 16  ? -64.654 11.027  41.753  1.00 125.88 ?  14   PRO H CG  1 
ATOM   5997 C CD  . PRO C 2 16  ? -64.661 10.241  43.032  1.00 131.83 ?  14   PRO H CD  1 
ATOM   5998 N N   . GLY C 2 17  ? -61.177 13.396  43.789  1.00 111.77 ?  15   GLY H N   1 
ATOM   5999 C CA  . GLY C 2 17  ? -60.671 14.427  44.666  1.00 114.21 ?  15   GLY H CA  1 
ATOM   6000 C C   . GLY C 2 17  ? -59.736 13.948  45.754  1.00 125.38 ?  15   GLY H C   1 
ATOM   6001 O O   . GLY C 2 17  ? -59.073 14.780  46.387  1.00 121.63 ?  15   GLY H O   1 
ATOM   6002 N N   . ARG C 2 18  ? -59.654 12.640  45.992  1.00 121.81 ?  16   ARG H N   1 
ATOM   6003 C CA  . ARG C 2 18  ? -58.799 12.114  47.049  1.00 127.59 ?  16   ARG H CA  1 
ATOM   6004 C C   . ARG C 2 18  ? -57.358 11.974  46.575  1.00 130.69 ?  16   ARG H C   1 
ATOM   6005 O O   . ARG C 2 18  ? -56.909 12.727  45.704  1.00 126.92 ?  16   ARG H O   1 
ATOM   6006 C CB  . ARG C 2 18  ? -59.330 10.769  47.549  1.00 127.78 ?  16   ARG H CB  1 
ATOM   6007 C CG  . ARG C 2 18  ? -60.678 10.867  48.239  1.00 121.62 ?  16   ARG H CG  1 
ATOM   6008 C CD  . ARG C 2 18  ? -60.790 9.869   49.377  1.00 126.44 ?  16   ARG H CD  1 
ATOM   6009 N NE  . ARG C 2 18  ? -61.866 10.220  50.299  1.00 131.09 ?  16   ARG H NE  1 
ATOM   6010 C CZ  . ARG C 2 18  ? -62.044 9.654   51.488  1.00 126.33 ?  16   ARG H CZ  1 
ATOM   6011 N NH1 . ARG C 2 18  ? -61.213 8.707   51.903  1.00 122.28 1  16   ARG H NH1 1 
ATOM   6012 N NH2 . ARG C 2 18  ? -63.049 10.036  52.264  1.00 119.97 ?  16   ARG H NH2 1 
ATOM   6013 N N   . SER C 2 19  ? -56.628 11.013  47.137  1.00 126.53 ?  17   SER H N   1 
ATOM   6014 C CA  . SER C 2 19  ? -55.218 10.837  46.826  1.00 120.42 ?  17   SER H CA  1 
ATOM   6015 C C   . SER C 2 19  ? -54.889 9.355   46.721  1.00 118.74 ?  17   SER H C   1 
ATOM   6016 O O   . SER C 2 19  ? -55.576 8.500   47.285  1.00 124.19 ?  17   SER H O   1 
ATOM   6017 C CB  . SER C 2 19  ? -54.322 11.497  47.884  1.00 125.23 ?  17   SER H CB  1 
ATOM   6018 O OG  . SER C 2 19  ? -52.976 11.075  47.742  1.00 116.27 ?  17   SER H OG  1 
ATOM   6019 N N   . LEU C 2 20  ? -53.821 9.067   45.981  1.00 124.08 ?  18   LEU H N   1 
ATOM   6020 C CA  . LEU C 2 20  ? -53.283 7.720   45.856  1.00 115.83 ?  18   LEU H CA  1 
ATOM   6021 C C   . LEU C 2 20  ? -51.851 7.828   45.356  1.00 107.57 ?  18   LEU H C   1 
ATOM   6022 O O   . LEU C 2 20  ? -51.512 8.747   44.607  1.00 107.06 ?  18   LEU H O   1 
ATOM   6023 C CB  . LEU C 2 20  ? -54.114 6.851   44.905  1.00 115.40 ?  18   LEU H CB  1 
ATOM   6024 C CG  . LEU C 2 20  ? -54.649 5.525   45.449  1.00 113.88 ?  18   LEU H CG  1 
ATOM   6025 C CD1 . LEU C 2 20  ? -55.201 4.665   44.321  1.00 97.19  ?  18   LEU H CD1 1 
ATOM   6026 C CD2 . LEU C 2 20  ? -53.571 4.785   46.219  1.00 108.16 ?  18   LEU H CD2 1 
ATOM   6027 N N   . ARG C 2 21  ? -51.015 6.883   45.779  1.00 110.20 ?  19   ARG H N   1 
ATOM   6028 C CA  . ARG C 2 21  ? -49.607 6.862   45.401  1.00 101.69 ?  19   ARG H CA  1 
ATOM   6029 C C   . ARG C 2 21  ? -49.234 5.465   44.933  1.00 96.99  ?  19   ARG H C   1 
ATOM   6030 O O   . ARG C 2 21  ? -49.420 4.491   45.668  1.00 107.61 ?  19   ARG H O   1 
ATOM   6031 C CB  . ARG C 2 21  ? -48.712 7.291   46.567  1.00 98.20  ?  19   ARG H CB  1 
ATOM   6032 C CG  . ARG C 2 21  ? -47.235 7.020   46.336  1.00 96.80  ?  19   ARG H CG  1 
ATOM   6033 C CD  . ARG C 2 21  ? -46.375 7.722   47.370  1.00 109.55 ?  19   ARG H CD  1 
ATOM   6034 N NE  . ARG C 2 21  ? -45.552 6.790   48.134  1.00 117.40 ?  19   ARG H NE  1 
ATOM   6035 C CZ  . ARG C 2 21  ? -44.615 7.163   49.000  1.00 126.20 ?  19   ARG H CZ  1 
ATOM   6036 N NH1 . ARG C 2 21  ? -44.379 8.451   49.209  1.00 121.71 1  19   ARG H NH1 1 
ATOM   6037 N NH2 . ARG C 2 21  ? -43.911 6.249   49.655  1.00 128.90 ?  19   ARG H NH2 1 
ATOM   6038 N N   . LEU C 2 22  ? -48.712 5.372   43.716  1.00 97.55  ?  20   LEU H N   1 
ATOM   6039 C CA  . LEU C 2 22  ? -48.216 4.116   43.181  1.00 87.23  ?  20   LEU H CA  1 
ATOM   6040 C C   . LEU C 2 22  ? -46.713 4.003   43.414  1.00 95.97  ?  20   LEU H C   1 
ATOM   6041 O O   . LEU C 2 22  ? -46.014 4.997   43.627  1.00 102.56 ?  20   LEU H O   1 
ATOM   6042 C CB  . LEU C 2 22  ? -48.524 4.003   41.687  1.00 89.05  ?  20   LEU H CB  1 
ATOM   6043 C CG  . LEU C 2 22  ? -49.974 4.244   41.265  1.00 97.70  ?  20   LEU H CG  1 
ATOM   6044 C CD1 . LEU C 2 22  ? -50.130 4.067   39.763  1.00 96.06  ?  20   LEU H CD1 1 
ATOM   6045 C CD2 . LEU C 2 22  ? -50.922 3.325   42.019  1.00 92.10  ?  20   LEU H CD2 1 
ATOM   6046 N N   . SER C 2 23  ? -46.219 2.769   43.373  1.00 104.55 ?  21   SER H N   1 
ATOM   6047 C CA  . SER C 2 23  ? -44.799 2.505   43.542  1.00 91.61  ?  21   SER H CA  1 
ATOM   6048 C C   . SER C 2 23  ? -44.359 1.465   42.524  1.00 90.04  ?  21   SER H C   1 
ATOM   6049 O O   . SER C 2 23  ? -45.128 0.578   42.147  1.00 93.32  ?  21   SER H O   1 
ATOM   6050 C CB  . SER C 2 23  ? -44.473 2.020   44.961  1.00 84.82  ?  21   SER H CB  1 
ATOM   6051 O OG  . SER C 2 23  ? -45.026 0.738   45.199  1.00 99.89  ?  21   SER H OG  1 
ATOM   6052 N N   . CYS C 2 24  ? -43.110 1.587   42.080  1.00 92.41  ?  22   CYS H N   1 
ATOM   6053 C CA  . CYS C 2 24  ? -42.535 0.667   41.103  1.00 91.82  ?  22   CYS H CA  1 
ATOM   6054 C C   . CYS C 2 24  ? -41.132 0.300   41.564  1.00 91.94  ?  22   CYS H C   1 
ATOM   6055 O O   . CYS C 2 24  ? -40.217 1.125   41.487  1.00 92.34  ?  22   CYS H O   1 
ATOM   6056 C CB  . CYS C 2 24  ? -42.506 1.285   39.705  1.00 93.64  ?  22   CYS H CB  1 
ATOM   6057 S SG  . CYS C 2 24  ? -41.631 0.288   38.478  1.00 89.75  ?  22   CYS H SG  1 
ATOM   6058 N N   . ALA C 2 25  ? -40.963 -0.932  42.037  1.00 86.24  ?  23   ALA H N   1 
ATOM   6059 C CA  . ALA C 2 25  ? -39.674 -1.409  42.519  1.00 82.17  ?  23   ALA H CA  1 
ATOM   6060 C C   . ALA C 2 25  ? -38.895 -2.024  41.363  1.00 83.61  ?  23   ALA H C   1 
ATOM   6061 O O   . ALA C 2 25  ? -39.346 -3.000  40.753  1.00 83.62  ?  23   ALA H O   1 
ATOM   6062 C CB  . ALA C 2 25  ? -39.857 -2.425  43.646  1.00 84.67  ?  23   ALA H CB  1 
ATOM   6063 N N   . ALA C 2 26  ? -37.734 -1.453  41.064  1.00 85.97  ?  24   ALA H N   1 
ATOM   6064 C CA  . ALA C 2 26  ? -36.858 -1.946  40.013  1.00 82.26  ?  24   ALA H CA  1 
ATOM   6065 C C   . ALA C 2 26  ? -35.718 -2.761  40.612  1.00 79.60  ?  24   ALA H C   1 
ATOM   6066 O O   . ALA C 2 26  ? -35.348 -2.597  41.777  1.00 81.89  ?  24   ALA H O   1 
ATOM   6067 C CB  . ALA C 2 26  ? -36.297 -0.789  39.184  1.00 83.34  ?  24   ALA H CB  1 
ATOM   6068 N N   . SER C 2 27  ? -35.161 -3.648  39.791  1.00 90.65  ?  25   SER H N   1 
ATOM   6069 C CA  . SER C 2 27  ? -34.082 -4.521  40.229  1.00 78.48  ?  25   SER H CA  1 
ATOM   6070 C C   . SER C 2 27  ? -33.412 -5.130  39.006  1.00 85.04  ?  25   SER H C   1 
ATOM   6071 O O   . SER C 2 27  ? -34.084 -5.472  38.031  1.00 74.93  ?  25   SER H O   1 
ATOM   6072 C CB  . SER C 2 27  ? -34.601 -5.623  41.162  1.00 76.07  ?  25   SER H CB  1 
ATOM   6073 O OG  . SER C 2 27  ? -35.756 -6.247  40.627  1.00 88.49  ?  25   SER H OG  1 
ATOM   6074 N N   . GLY C 2 28  ? -32.085 -5.250  39.064  1.00 81.59  ?  26   GLY H N   1 
ATOM   6075 C CA  . GLY C 2 28  ? -31.315 -5.885  38.017  1.00 73.10  ?  26   GLY H CA  1 
ATOM   6076 C C   . GLY C 2 28  ? -30.635 -4.940  37.049  1.00 93.32  ?  26   GLY H C   1 
ATOM   6077 O O   . GLY C 2 28  ? -29.839 -5.400  36.222  1.00 89.10  ?  26   GLY H O   1 
ATOM   6078 N N   . PHE C 2 29  ? -30.919 -3.642  37.122  1.00 83.96  ?  27   PHE H N   1 
ATOM   6079 C CA  . PHE C 2 29  ? -30.322 -2.693  36.196  1.00 85.92  ?  27   PHE H CA  1 
ATOM   6080 C C   . PHE C 2 29  ? -30.096 -1.369  36.907  1.00 101.50 ?  27   PHE H C   1 
ATOM   6081 O O   . PHE C 2 29  ? -30.771 -1.041  37.887  1.00 99.94  ?  27   PHE H O   1 
ATOM   6082 C CB  . PHE C 2 29  ? -31.193 -2.497  34.949  1.00 78.96  ?  27   PHE H CB  1 
ATOM   6083 C CG  . PHE C 2 29  ? -32.532 -1.874  35.232  1.00 86.55  ?  27   PHE H CG  1 
ATOM   6084 C CD1 . PHE C 2 29  ? -32.723 -0.510  35.075  1.00 81.54  ?  27   PHE H CD1 1 
ATOM   6085 C CD2 . PHE C 2 29  ? -33.602 -2.652  35.643  1.00 79.62  ?  27   PHE H CD2 1 
ATOM   6086 C CE1 . PHE C 2 29  ? -33.952 0.066   35.329  1.00 71.41  ?  27   PHE H CE1 1 
ATOM   6087 C CE2 . PHE C 2 29  ? -34.836 -2.080  35.900  1.00 78.14  ?  27   PHE H CE2 1 
ATOM   6088 C CZ  . PHE C 2 29  ? -35.011 -0.719  35.743  1.00 93.88  ?  27   PHE H CZ  1 
ATOM   6089 N N   . THR C 2 30  ? -29.131 -0.610  36.395  1.00 108.60 ?  28   THR H N   1 
ATOM   6090 C CA  . THR C 2 30  ? -28.806 0.685   36.976  1.00 112.25 ?  28   THR H CA  1 
ATOM   6091 C C   . THR C 2 30  ? -29.949 1.668   36.751  1.00 108.29 ?  28   THR H C   1 
ATOM   6092 O O   . THR C 2 30  ? -30.413 1.851   35.621  1.00 110.70 ?  28   THR H O   1 
ATOM   6093 C CB  . THR C 2 30  ? -27.515 1.229   36.366  1.00 116.10 ?  28   THR H CB  1 
ATOM   6094 O OG1 . THR C 2 30  ? -26.510 0.208   36.386  1.00 129.70 ?  28   THR H OG1 1 
ATOM   6095 C CG2 . THR C 2 30  ? -27.021 2.430   37.156  1.00 103.65 ?  28   THR H CG2 1 
ATOM   6096 N N   . PHE C 2 31  ? -30.401 2.302   37.832  1.00 99.59  ?  29   PHE H N   1 
ATOM   6097 C CA  . PHE C 2 31  ? -31.518 3.233   37.772  1.00 97.32  ?  29   PHE H CA  1 
ATOM   6098 C C   . PHE C 2 31  ? -31.149 4.575   37.147  1.00 104.62 ?  29   PHE H C   1 
ATOM   6099 O O   . PHE C 2 31  ? -32.052 5.341   36.791  1.00 102.66 ?  29   PHE H O   1 
ATOM   6100 C CB  . PHE C 2 31  ? -32.081 3.456   39.181  1.00 109.55 ?  29   PHE H CB  1 
ATOM   6101 C CG  . PHE C 2 31  ? -33.575 3.604   39.219  1.00 108.94 ?  29   PHE H CG  1 
ATOM   6102 C CD1 . PHE C 2 31  ? -34.167 4.666   39.883  1.00 102.17 ?  29   PHE H CD1 1 
ATOM   6103 C CD2 . PHE C 2 31  ? -34.387 2.683   38.582  1.00 94.05  ?  29   PHE H CD2 1 
ATOM   6104 C CE1 . PHE C 2 31  ? -35.543 4.800   39.914  1.00 103.23 ?  29   PHE H CE1 1 
ATOM   6105 C CE2 . PHE C 2 31  ? -35.761 2.811   38.608  1.00 89.79  ?  29   PHE H CE2 1 
ATOM   6106 C CZ  . PHE C 2 31  ? -36.340 3.871   39.275  1.00 95.95  ?  29   PHE H CZ  1 
ATOM   6107 N N   . SER C 2 32  ? -29.858 4.874   36.998  1.00 105.69 ?  30   SER H N   1 
ATOM   6108 C CA  . SER C 2 32  ? -29.399 6.124   36.403  1.00 79.97  ?  30   SER H CA  1 
ATOM   6109 C C   . SER C 2 32  ? -29.042 5.988   34.928  1.00 78.56  ?  30   SER H C   1 
ATOM   6110 O O   . SER C 2 32  ? -28.703 6.991   34.293  1.00 84.88  ?  30   SER H O   1 
ATOM   6111 C CB  . SER C 2 32  ? -28.191 6.665   37.172  1.00 81.69  ?  30   SER H CB  1 
ATOM   6112 O OG  . SER C 2 32  ? -27.116 5.742   37.145  1.00 77.74  ?  30   SER H OG  1 
ATOM   6113 N N   . SER C 2 33  ? -29.098 4.778   34.372  1.00 76.42  ?  31   SER H N   1 
ATOM   6114 C CA  . SER C 2 33  ? -28.816 4.565   32.960  1.00 56.96  ?  31   SER H CA  1 
ATOM   6115 C C   . SER C 2 33  ? -30.070 4.485   32.102  1.00 61.82  ?  31   SER H C   1 
ATOM   6116 O O   . SER C 2 33  ? -29.983 4.681   30.885  1.00 64.23  ?  31   SER H O   1 
ATOM   6117 C CB  . SER C 2 33  ? -27.998 3.281   32.767  1.00 58.36  ?  31   SER H CB  1 
ATOM   6118 O OG  . SER C 2 33  ? -26.738 3.368   33.409  1.00 70.80  ?  31   SER H OG  1 
ATOM   6119 N N   . TYR C 2 34  ? -31.224 4.207   32.701  1.00 69.27  ?  32   TYR H N   1 
ATOM   6120 C CA  . TYR C 2 34  ? -32.473 4.037   31.975  1.00 73.15  ?  32   TYR H CA  1 
ATOM   6121 C C   . TYR C 2 34  ? -33.493 5.067   32.435  1.00 61.86  ?  32   TYR H C   1 
ATOM   6122 O O   . TYR C 2 34  ? -33.537 5.428   33.615  1.00 68.40  ?  32   TYR H O   1 
ATOM   6123 C CB  . TYR C 2 34  ? -33.046 2.628   32.179  1.00 65.40  ?  32   TYR H CB  1 
ATOM   6124 C CG  . TYR C 2 34  ? -32.192 1.518   31.611  1.00 62.28  ?  32   TYR H CG  1 
ATOM   6125 C CD1 . TYR C 2 34  ? -31.116 1.007   32.324  1.00 71.80  ?  32   TYR H CD1 1 
ATOM   6126 C CD2 . TYR C 2 34  ? -32.470 0.973   30.365  1.00 70.13  ?  32   TYR H CD2 1 
ATOM   6127 C CE1 . TYR C 2 34  ? -30.335 -0.011  31.808  1.00 70.87  ?  32   TYR H CE1 1 
ATOM   6128 C CE2 . TYR C 2 34  ? -31.696 -0.044  29.841  1.00 71.35  ?  32   TYR H CE2 1 
ATOM   6129 C CZ  . TYR C 2 34  ? -30.631 -0.532  30.566  1.00 68.53  ?  32   TYR H CZ  1 
ATOM   6130 O OH  . TYR C 2 34  ? -29.858 -1.544  30.047  1.00 83.40  ?  32   TYR H OH  1 
ATOM   6131 N N   . ALA C 2 35  ? -34.311 5.536   31.498  1.00 65.32  ?  33   ALA H N   1 
ATOM   6132 C CA  . ALA C 2 35  ? -35.467 6.346   31.844  1.00 68.08  ?  33   ALA H CA  1 
ATOM   6133 C C   . ALA C 2 35  ? -36.609 5.447   32.297  1.00 72.17  ?  33   ALA H C   1 
ATOM   6134 O O   . ALA C 2 35  ? -36.724 4.294   31.872  1.00 75.16  ?  33   ALA H O   1 
ATOM   6135 C CB  . ALA C 2 35  ? -35.909 7.199   30.654  1.00 61.92  ?  33   ALA H CB  1 
ATOM   6136 N N   . MET C 2 36  ? -37.457 5.981   33.171  1.00 65.93  ?  34   MET H N   1 
ATOM   6137 C CA  . MET C 2 36  ? -38.560 5.229   33.756  1.00 67.70  ?  34   MET H CA  1 
ATOM   6138 C C   . MET C 2 36  ? -39.871 5.913   33.399  1.00 75.22  ?  34   MET H C   1 
ATOM   6139 O O   . MET C 2 36  ? -40.084 7.077   33.753  1.00 71.61  ?  34   MET H O   1 
ATOM   6140 C CB  . MET C 2 36  ? -38.399 5.120   35.273  1.00 71.02  ?  34   MET H CB  1 
ATOM   6141 C CG  . MET C 2 36  ? -37.152 4.366   35.707  1.00 76.86  ?  34   MET H CG  1 
ATOM   6142 S SD  . MET C 2 36  ? -37.170 2.637   35.194  1.00 84.41  ?  34   MET H SD  1 
ATOM   6143 C CE  . MET C 2 36  ? -38.626 2.048   36.052  1.00 80.03  ?  34   MET H CE  1 
ATOM   6144 N N   . HIS C 2 37  ? -40.746 5.188   32.707  1.00 78.22  ?  35   HIS H N   1 
ATOM   6145 C CA  . HIS C 2 37  ? -42.009 5.722   32.224  1.00 72.74  ?  35   HIS H CA  1 
ATOM   6146 C C   . HIS C 2 37  ? -43.178 5.161   33.024  1.00 78.54  ?  35   HIS H C   1 
ATOM   6147 O O   . HIS C 2 37  ? -43.097 4.071   33.600  1.00 82.97  ?  35   HIS H O   1 
ATOM   6148 C CB  . HIS C 2 37  ? -42.219 5.394   30.742  1.00 77.08  ?  35   HIS H CB  1 
ATOM   6149 C CG  . HIS C 2 37  ? -41.229 6.042   29.826  1.00 76.47  ?  35   HIS H CG  1 
ATOM   6150 N ND1 . HIS C 2 37  ? -41.577 7.042   28.944  1.00 77.54  ?  35   HIS H ND1 1 
ATOM   6151 C CD2 . HIS C 2 37  ? -39.905 5.825   29.644  1.00 69.58  ?  35   HIS H CD2 1 
ATOM   6152 C CE1 . HIS C 2 37  ? -40.510 7.415   28.260  1.00 75.27  ?  35   HIS H CE1 1 
ATOM   6153 N NE2 . HIS C 2 37  ? -39.481 6.694   28.668  1.00 80.91  ?  35   HIS H NE2 1 
ATOM   6154 N N   . TRP C 2 38  ? -44.268 5.924   33.050  1.00 82.20  ?  36   TRP H N   1 
ATOM   6155 C CA  . TRP C 2 38  ? -45.563 5.458   33.530  1.00 68.88  ?  36   TRP H CA  1 
ATOM   6156 C C   . TRP C 2 38  ? -46.534 5.502   32.361  1.00 68.32  ?  36   TRP H C   1 
ATOM   6157 O O   . TRP C 2 38  ? -46.711 6.554   31.738  1.00 72.99  ?  36   TRP H O   1 
ATOM   6158 C CB  . TRP C 2 38  ? -46.079 6.317   34.687  1.00 76.77  ?  36   TRP H CB  1 
ATOM   6159 C CG  . TRP C 2 38  ? -45.414 6.055   36.004  1.00 75.50  ?  36   TRP H CG  1 
ATOM   6160 C CD1 . TRP C 2 38  ? -44.436 6.803   36.590  1.00 81.22  ?  36   TRP H CD1 1 
ATOM   6161 C CD2 . TRP C 2 38  ? -45.687 4.974   36.904  1.00 83.76  ?  36   TRP H CD2 1 
ATOM   6162 N NE1 . TRP C 2 38  ? -44.081 6.254   37.799  1.00 90.60  ?  36   TRP H NE1 1 
ATOM   6163 C CE2 . TRP C 2 38  ? -44.833 5.129   38.014  1.00 85.76  ?  36   TRP H CE2 1 
ATOM   6164 C CE3 . TRP C 2 38  ? -46.568 3.888   36.878  1.00 91.72  ?  36   TRP H CE3 1 
ATOM   6165 C CZ2 . TRP C 2 38  ? -44.835 4.241   39.088  1.00 83.21  ?  36   TRP H CZ2 1 
ATOM   6166 C CZ3 . TRP C 2 38  ? -46.568 3.007   37.945  1.00 90.71  ?  36   TRP H CZ3 1 
ATOM   6167 C CH2 . TRP C 2 38  ? -45.707 3.189   39.034  1.00 94.28  ?  36   TRP H CH2 1 
ATOM   6168 N N   . VAL C 2 39  ? -47.150 4.364   32.054  1.00 78.48  ?  37   VAL H N   1 
ATOM   6169 C CA  . VAL C 2 39  ? -48.116 4.259   30.968  1.00 80.57  ?  37   VAL H CA  1 
ATOM   6170 C C   . VAL C 2 39  ? -49.370 3.588   31.507  1.00 79.56  ?  37   VAL H C   1 
ATOM   6171 O O   . VAL C 2 39  ? -49.294 2.504   32.096  1.00 93.34  ?  37   VAL H O   1 
ATOM   6172 C CB  . VAL C 2 39  ? -47.553 3.472   29.768  1.00 84.11  ?  37   VAL H CB  1 
ATOM   6173 C CG1 . VAL C 2 39  ? -48.625 3.286   28.706  1.00 80.02  ?  37   VAL H CG1 1 
ATOM   6174 C CG2 . VAL C 2 39  ? -46.343 4.186   29.184  1.00 67.94  ?  37   VAL H CG2 1 
ATOM   6175 N N   . ARG C 2 40  ? -50.517 4.231   31.309  1.00 73.74  ?  38   ARG H N   1 
ATOM   6176 C CA  . ARG C 2 40  ? -51.794 3.726   31.786  1.00 81.92  ?  38   ARG H CA  1 
ATOM   6177 C C   . ARG C 2 40  ? -52.647 3.254   30.616  1.00 85.33  ?  38   ARG H C   1 
ATOM   6178 O O   . ARG C 2 40  ? -52.394 3.590   29.455  1.00 86.67  ?  38   ARG H O   1 
ATOM   6179 C CB  . ARG C 2 40  ? -52.546 4.796   32.586  1.00 82.70  ?  38   ARG H CB  1 
ATOM   6180 C CG  . ARG C 2 40  ? -53.046 5.964   31.752  1.00 78.65  ?  38   ARG H CG  1 
ATOM   6181 C CD  . ARG C 2 40  ? -53.648 7.041   32.637  1.00 79.93  ?  38   ARG H CD  1 
ATOM   6182 N NE  . ARG C 2 40  ? -54.202 8.153   31.870  1.00 94.14  ?  38   ARG H NE  1 
ATOM   6183 C CZ  . ARG C 2 40  ? -54.677 9.269   32.414  1.00 85.66  ?  38   ARG H CZ  1 
ATOM   6184 N NH1 . ARG C 2 40  ? -54.661 9.426   33.730  1.00 87.18  1  38   ARG H NH1 1 
ATOM   6185 N NH2 . ARG C 2 40  ? -55.164 10.231  31.642  1.00 101.20 ?  38   ARG H NH2 1 
ATOM   6186 N N   . GLN C 2 41  ? -53.669 2.463   30.939  1.00 83.97  ?  39   GLN H N   1 
ATOM   6187 C CA  . GLN C 2 41  ? -54.574 1.902   29.936  1.00 102.37 ?  39   GLN H CA  1 
ATOM   6188 C C   . GLN C 2 41  ? -55.977 1.869   30.534  1.00 101.80 ?  39   GLN H C   1 
ATOM   6189 O O   . GLN C 2 41  ? -56.276 1.020   31.379  1.00 104.39 ?  39   GLN H O   1 
ATOM   6190 C CB  . GLN C 2 41  ? -54.125 0.512   29.501  1.00 90.24  ?  39   GLN H CB  1 
ATOM   6191 C CG  . GLN C 2 41  ? -55.061 -0.157  28.509  1.00 90.42  ?  39   GLN H CG  1 
ATOM   6192 C CD  . GLN C 2 41  ? -54.576 -1.527  28.082  1.00 102.76 ?  39   GLN H CD  1 
ATOM   6193 O OE1 . GLN C 2 41  ? -54.294 -2.388  28.916  1.00 98.18  ?  39   GLN H OE1 1 
ATOM   6194 N NE2 . GLN C 2 41  ? -54.469 -1.735  26.774  1.00 92.00  ?  39   GLN H NE2 1 
ATOM   6195 N N   . ALA C 2 42  ? -56.827 2.797   30.100  1.00 94.91  ?  40   ALA H N   1 
ATOM   6196 C CA  . ALA C 2 42  ? -58.201 2.827   30.572  1.00 97.69  ?  40   ALA H CA  1 
ATOM   6197 C C   . ALA C 2 42  ? -58.920 1.541   30.164  1.00 105.29 ?  40   ALA H C   1 
ATOM   6198 O O   . ALA C 2 42  ? -58.559 0.911   29.164  1.00 110.70 ?  40   ALA H O   1 
ATOM   6199 C CB  . ALA C 2 42  ? -58.932 4.045   30.010  1.00 104.82 ?  40   ALA H CB  1 
ATOM   6200 N N   . PRO C 2 43  ? -59.936 1.115   30.936  1.00 112.24 ?  41   PRO H N   1 
ATOM   6201 C CA  . PRO C 2 43  ? -60.640 -0.137  30.616  1.00 97.57  ?  41   PRO H CA  1 
ATOM   6202 C C   . PRO C 2 43  ? -61.186 -0.176  29.197  1.00 97.65  ?  41   PRO H C   1 
ATOM   6203 O O   . PRO C 2 43  ? -61.973 0.687   28.797  1.00 103.74 ?  41   PRO H O   1 
ATOM   6204 C CB  . PRO C 2 43  ? -61.771 -0.172  31.651  1.00 93.09  ?  41   PRO H CB  1 
ATOM   6205 C CG  . PRO C 2 43  ? -61.241 0.605   32.800  1.00 99.12  ?  41   PRO H CG  1 
ATOM   6206 C CD  . PRO C 2 43  ? -60.407 1.703   32.203  1.00 106.34 ?  41   PRO H CD  1 
ATOM   6207 N N   . GLY C 2 44  ? -60.762 -1.178  28.427  1.00 113.49 ?  42   GLY H N   1 
ATOM   6208 C CA  . GLY C 2 44  ? -61.203 -1.339  27.058  1.00 119.29 ?  42   GLY H CA  1 
ATOM   6209 C C   . GLY C 2 44  ? -60.645 -0.336  26.075  1.00 109.35 ?  42   GLY H C   1 
ATOM   6210 O O   . GLY C 2 44  ? -61.028 -0.370  24.900  1.00 113.09 ?  42   GLY H O   1 
ATOM   6211 N N   . LYS C 2 45  ? -59.756 0.551   26.506  1.00 106.83 ?  43   LYS H N   1 
ATOM   6212 C CA  . LYS C 2 45  ? -59.201 1.590   25.652  1.00 116.01 ?  43   LYS H CA  1 
ATOM   6213 C C   . LYS C 2 45  ? -57.749 1.268   25.302  1.00 108.60 ?  43   LYS H C   1 
ATOM   6214 O O   . LYS C 2 45  ? -57.200 0.236   25.699  1.00 113.14 ?  43   LYS H O   1 
ATOM   6215 C CB  . LYS C 2 45  ? -59.309 2.957   26.330  1.00 110.83 ?  43   LYS H CB  1 
ATOM   6216 C CG  . LYS C 2 45  ? -60.697 3.296   26.846  1.00 108.58 ?  43   LYS H CG  1 
ATOM   6217 C CD  . LYS C 2 45  ? -61.753 3.179   25.755  1.00 110.16 ?  43   LYS H CD  1 
ATOM   6218 C CE  . LYS C 2 45  ? -61.478 4.137   24.603  1.00 116.25 ?  43   LYS H CE  1 
ATOM   6219 N NZ  . LYS C 2 45  ? -61.450 5.556   25.053  1.00 117.85 1  43   LYS H NZ  1 
ATOM   6220 N N   . GLY C 2 46  ? -57.125 2.175   24.554  1.00 103.06 ?  44   GLY H N   1 
ATOM   6221 C CA  . GLY C 2 46  ? -55.743 2.014   24.145  1.00 99.69  ?  44   GLY H CA  1 
ATOM   6222 C C   . GLY C 2 46  ? -54.756 2.350   25.241  1.00 98.49  ?  44   GLY H C   1 
ATOM   6223 O O   . GLY C 2 46  ? -55.039 2.212   26.438  1.00 107.97 ?  44   GLY H O   1 
ATOM   6224 N N   . LEU C 2 47  ? -53.585 2.817   24.821  1.00 93.22  ?  45   LEU H N   1 
ATOM   6225 C CA  . LEU C 2 47  ? -52.458 3.094   25.701  1.00 90.32  ?  45   LEU H CA  1 
ATOM   6226 C C   . LEU C 2 47  ? -52.232 4.598   25.793  1.00 97.53  ?  45   LEU H C   1 
ATOM   6227 O O   . LEU C 2 47  ? -52.340 5.308   24.789  1.00 87.04  ?  45   LEU H O   1 
ATOM   6228 C CB  . LEU C 2 47  ? -51.191 2.408   25.178  1.00 88.32  ?  45   LEU H CB  1 
ATOM   6229 C CG  . LEU C 2 47  ? -50.432 1.400   26.045  1.00 95.38  ?  45   LEU H CG  1 
ATOM   6230 C CD1 . LEU C 2 47  ? -51.358 0.655   26.999  1.00 87.38  ?  45   LEU H CD1 1 
ATOM   6231 C CD2 . LEU C 2 47  ? -49.691 0.419   25.151  1.00 86.49  ?  45   LEU H CD2 1 
ATOM   6232 N N   . GLU C 2 48  ? -51.921 5.083   26.997  1.00 92.37  ?  46   GLU H N   1 
ATOM   6233 C CA  . GLU C 2 48  ? -51.699 6.507   27.234  1.00 84.87  ?  46   GLU H CA  1 
ATOM   6234 C C   . GLU C 2 48  ? -50.456 6.699   28.090  1.00 79.02  ?  46   GLU H C   1 
ATOM   6235 O O   . GLU C 2 48  ? -50.366 6.153   29.194  1.00 82.31  ?  46   GLU H O   1 
ATOM   6236 C CB  . GLU C 2 48  ? -52.911 7.154   27.912  1.00 79.78  ?  46   GLU H CB  1 
ATOM   6237 C CG  . GLU C 2 48  ? -52.842 8.669   27.935  1.00 81.63  ?  46   GLU H CG  1 
ATOM   6238 C CD  . GLU C 2 48  ? -53.962 9.300   28.735  1.00 89.08  ?  46   GLU H CD  1 
ATOM   6239 O OE1 . GLU C 2 48  ? -54.729 8.555   29.380  1.00 91.77  ?  46   GLU H OE1 1 
ATOM   6240 O OE2 . GLU C 2 48  ? -54.075 10.545  28.720  1.00 95.30  -1 46   GLU H OE2 1 
ATOM   6241 N N   . TRP C 2 49  ? -49.509 7.485   27.584  1.00 76.46  ?  47   TRP H N   1 
ATOM   6242 C CA  . TRP C 2 49  ? -48.315 7.823   28.345  1.00 78.97  ?  47   TRP H CA  1 
ATOM   6243 C C   . TRP C 2 49  ? -48.646 8.844   29.428  1.00 77.02  ?  47   TRP H C   1 
ATOM   6244 O O   . TRP C 2 49  ? -49.432 9.770   29.211  1.00 71.23  ?  47   TRP H O   1 
ATOM   6245 C CB  . TRP C 2 49  ? -47.239 8.371   27.412  1.00 80.81  ?  47   TRP H CB  1 
ATOM   6246 C CG  . TRP C 2 49  ? -46.017 8.860   28.117  1.00 76.61  ?  47   TRP H CG  1 
ATOM   6247 C CD1 . TRP C 2 49  ? -44.964 8.109   28.548  1.00 68.34  ?  47   TRP H CD1 1 
ATOM   6248 C CD2 . TRP C 2 49  ? -45.714 10.216  28.466  1.00 79.92  ?  47   TRP H CD2 1 
ATOM   6249 N NE1 . TRP C 2 49  ? -44.025 8.912   29.147  1.00 69.86  ?  47   TRP H NE1 1 
ATOM   6250 C CE2 . TRP C 2 49  ? -44.462 10.210  29.111  1.00 74.31  ?  47   TRP H CE2 1 
ATOM   6251 C CE3 . TRP C 2 49  ? -46.380 11.434  28.298  1.00 86.29  ?  47   TRP H CE3 1 
ATOM   6252 C CZ2 . TRP C 2 49  ? -43.862 11.373  29.586  1.00 72.27  ?  47   TRP H CZ2 1 
ATOM   6253 C CZ3 . TRP C 2 49  ? -45.783 12.587  28.771  1.00 77.44  ?  47   TRP H CZ3 1 
ATOM   6254 C CH2 . TRP C 2 49  ? -44.537 12.548  29.407  1.00 83.15  ?  47   TRP H CH2 1 
ATOM   6255 N N   . VAL C 2 50  ? -48.037 8.677   30.600  1.00 73.00  ?  48   VAL H N   1 
ATOM   6256 C CA  . VAL C 2 50  ? -48.376 9.511   31.749  1.00 70.05  ?  48   VAL H CA  1 
ATOM   6257 C C   . VAL C 2 50  ? -47.217 10.430  32.110  1.00 80.87  ?  48   VAL H C   1 
ATOM   6258 O O   . VAL C 2 50  ? -47.336 11.657  32.011  1.00 87.91  ?  48   VAL H O   1 
ATOM   6259 C CB  . VAL C 2 50  ? -48.783 8.649   32.955  1.00 76.79  ?  48   VAL H CB  1 
ATOM   6260 C CG1 . VAL C 2 50  ? -49.156 9.532   34.137  1.00 73.26  ?  48   VAL H CG1 1 
ATOM   6261 C CG2 . VAL C 2 50  ? -49.942 7.734   32.580  1.00 77.43  ?  48   VAL H CG2 1 
ATOM   6262 N N   . ALA C 2 51  ? -46.093 9.850   32.528  1.00 74.93  ?  49   ALA H N   1 
ATOM   6263 C CA  . ALA C 2 51  ? -44.955 10.637  32.982  1.00 80.50  ?  49   ALA H CA  1 
ATOM   6264 C C   . ALA C 2 51  ? -43.665 9.881   32.685  1.00 72.27  ?  49   ALA H C   1 
ATOM   6265 O O   . ALA C 2 51  ? -43.682 8.752   32.185  1.00 74.23  ?  49   ALA H O   1 
ATOM   6266 C CB  . ALA C 2 51  ? -45.072 10.966  34.473  1.00 78.31  ?  49   ALA H CB  1 
ATOM   6267 N N   . VAL C 2 52  ? -42.538 10.518  33.005  1.00 68.39  ?  50   VAL H N   1 
ATOM   6268 C CA  . VAL C 2 52  ? -41.220 9.932   32.783  1.00 71.06  ?  50   VAL H CA  1 
ATOM   6269 C C   . VAL C 2 52  ? -40.209 10.680  33.640  1.00 66.28  ?  50   VAL H C   1 
ATOM   6270 O O   . VAL C 2 52  ? -40.390 11.859  33.956  1.00 75.58  ?  50   VAL H O   1 
ATOM   6271 C CB  . VAL C 2 52  ? -40.833 9.971   31.282  1.00 77.38  ?  50   VAL H CB  1 
ATOM   6272 C CG1 . VAL C 2 52  ? -40.590 11.403  30.824  1.00 69.38  ?  50   VAL H CG1 1 
ATOM   6273 C CG2 . VAL C 2 52  ? -39.608 9.106   31.022  1.00 65.59  ?  50   VAL H CG2 1 
ATOM   6274 N N   . THR C 2 53  ? -39.144 9.980   34.028  1.00 65.30  ?  51   THR H N   1 
ATOM   6275 C CA  . THR C 2 53  ? -37.982 10.577  34.669  1.00 70.08  ?  51   THR H CA  1 
ATOM   6276 C C   . THR C 2 53  ? -36.732 9.971   34.048  1.00 67.06  ?  51   THR H C   1 
ATOM   6277 O O   . THR C 2 53  ? -36.712 8.783   33.715  1.00 69.14  ?  51   THR H O   1 
ATOM   6278 C CB  . THR C 2 53  ? -37.985 10.352  36.190  1.00 71.37  ?  51   THR H CB  1 
ATOM   6279 O OG1 . THR C 2 53  ? -36.770 10.863  36.753  1.00 84.99  ?  51   THR H OG1 1 
ATOM   6280 C CG2 . THR C 2 53  ? -38.106 8.871   36.518  1.00 63.29  ?  51   THR H CG2 1 
ATOM   6281 N N   . TRP C 2 54  ? -35.697 10.790  33.876  1.00 63.62  ?  52   TRP H N   1 
ATOM   6282 C CA  . TRP C 2 54  ? -34.484 10.327  33.219  1.00 65.48  ?  52   TRP H CA  1 
ATOM   6283 C C   . TRP C 2 54  ? -33.288 11.102  33.752  1.00 63.49  ?  52   TRP H C   1 
ATOM   6284 O O   . TRP C 2 54  ? -33.431 12.063  34.513  1.00 74.90  ?  52   TRP H O   1 
ATOM   6285 C CB  . TRP C 2 54  ? -34.590 10.458  31.695  1.00 57.05  ?  52   TRP H CB  1 
ATOM   6286 C CG  . TRP C 2 54  ? -34.520 11.864  31.183  1.00 67.98  ?  52   TRP H CG  1 
ATOM   6287 C CD1 . TRP C 2 54  ? -33.421 12.499  30.681  1.00 70.27  ?  52   TRP H CD1 1 
ATOM   6288 C CD2 . TRP C 2 54  ? -35.596 12.808  31.109  1.00 72.46  ?  52   TRP H CD2 1 
ATOM   6289 N NE1 . TRP C 2 54  ? -33.744 13.780  30.304  1.00 66.93  ?  52   TRP H NE1 1 
ATOM   6290 C CE2 . TRP C 2 54  ? -35.074 13.995  30.556  1.00 70.59  ?  52   TRP H CE2 1 
ATOM   6291 C CE3 . TRP C 2 54  ? -36.949 12.765  31.459  1.00 63.86  ?  52   TRP H CE3 1 
ATOM   6292 C CZ2 . TRP C 2 54  ? -35.857 15.128  30.344  1.00 67.12  ?  52   TRP H CZ2 1 
ATOM   6293 C CZ3 . TRP C 2 54  ? -37.725 13.892  31.249  1.00 79.05  ?  52   TRP H CZ3 1 
ATOM   6294 C CH2 . TRP C 2 54  ? -37.177 15.058  30.697  1.00 74.75  ?  52   TRP H CH2 1 
ATOM   6295 N N   . PHE C 2 55  A -32.098 10.668  33.327  1.00 65.53  ?  52   PHE H N   1 
ATOM   6296 C CA  . PHE C 2 55  A -30.829 11.202  33.810  1.00 67.48  ?  52   PHE H CA  1 
ATOM   6297 C C   . PHE C 2 55  A -30.802 11.152  35.332  1.00 80.19  ?  52   PHE H C   1 
ATOM   6298 O O   . PHE C 2 55  A -30.962 12.182  35.996  1.00 75.58  ?  52   PHE H O   1 
ATOM   6299 C CB  . PHE C 2 55  A -30.608 12.628  33.299  1.00 67.16  ?  52   PHE H CB  1 
ATOM   6300 C CG  . PHE C 2 55  A -29.163 13.029  33.235  1.00 68.83  ?  52   PHE H CG  1 
ATOM   6301 C CD1 . PHE C 2 55  A -28.293 12.389  32.369  1.00 59.86  ?  52   PHE H CD1 1 
ATOM   6302 C CD2 . PHE C 2 55  A -28.676 14.050  34.033  1.00 74.85  ?  52   PHE H CD2 1 
ATOM   6303 C CE1 . PHE C 2 55  A -26.963 12.754  32.305  1.00 65.41  ?  52   PHE H CE1 1 
ATOM   6304 C CE2 . PHE C 2 55  A -27.345 14.420  33.973  1.00 67.48  ?  52   PHE H CE2 1 
ATOM   6305 C CZ  . PHE C 2 55  A -26.489 13.771  33.109  1.00 66.85  ?  52   PHE H CZ  1 
ATOM   6306 N N   . ASP C 2 56  ? -30.589 9.954   35.882  1.00 85.70  ?  53   ASP H N   1 
ATOM   6307 C CA  . ASP C 2 56  ? -30.845 9.673   37.290  1.00 90.30  ?  53   ASP H CA  1 
ATOM   6308 C C   . ASP C 2 56  ? -32.274 10.094  37.612  1.00 101.12 ?  53   ASP H C   1 
ATOM   6309 O O   . ASP C 2 56  ? -33.217 9.637   36.958  1.00 100.06 ?  53   ASP H O   1 
ATOM   6310 C CB  . ASP C 2 56  ? -29.832 10.381  38.195  1.00 97.58  ?  53   ASP H CB  1 
ATOM   6311 C CG  . ASP C 2 56  ? -29.455 9.550   39.408  1.00 97.97  ?  53   ASP H CG  1 
ATOM   6312 O OD1 . ASP C 2 56  ? -29.987 8.428   39.547  1.00 102.50 ?  53   ASP H OD1 1 
ATOM   6313 O OD2 . ASP C 2 56  ? -28.625 10.016  40.218  1.00 87.94  -1 53   ASP H OD2 1 
ATOM   6314 N N   . VAL C 2 57  ? -32.453 10.958  38.611  1.00 121.23 ?  54   VAL H N   1 
ATOM   6315 C CA  . VAL C 2 57  ? -33.754 11.572  38.859  1.00 119.28 ?  54   VAL H CA  1 
ATOM   6316 C C   . VAL C 2 57  ? -33.556 13.071  39.047  1.00 109.28 ?  54   VAL H C   1 
ATOM   6317 O O   . VAL C 2 57  ? -33.644 13.590  40.166  1.00 110.91 ?  54   VAL H O   1 
ATOM   6318 C CB  . VAL C 2 57  ? -34.473 10.949  40.072  1.00 125.38 ?  54   VAL H CB  1 
ATOM   6319 C CG1 . VAL C 2 57  ? -35.908 11.460  40.157  1.00 109.60 ?  54   VAL H CG1 1 
ATOM   6320 C CG2 . VAL C 2 57  ? -34.464 9.430   39.990  1.00 114.26 ?  54   VAL H CG2 1 
ATOM   6321 N N   . SER C 2 58  ? -33.268 13.773  37.950  1.00 94.96  ?  55   SER H N   1 
ATOM   6322 C CA  . SER C 2 58  ? -33.145 15.223  37.960  1.00 95.18  ?  55   SER H CA  1 
ATOM   6323 C C   . SER C 2 58  ? -34.068 15.918  36.971  1.00 92.38  ?  55   SER H C   1 
ATOM   6324 O O   . SER C 2 58  ? -34.386 17.095  37.177  1.00 91.06  ?  55   SER H O   1 
ATOM   6325 C CB  . SER C 2 58  ? -31.696 15.643  37.665  1.00 97.40  ?  55   SER H CB  1 
ATOM   6326 O OG  . SER C 2 58  ? -31.244 15.095  36.439  1.00 81.64  ?  55   SER H OG  1 
ATOM   6327 N N   . LYS C 2 59  ? -34.507 15.233  35.919  1.00 86.86  ?  56   LYS H N   1 
ATOM   6328 C CA  . LYS C 2 59  ? -35.425 15.779  34.931  1.00 68.00  ?  56   LYS H CA  1 
ATOM   6329 C C   . LYS C 2 59  ? -36.692 14.936  34.905  1.00 71.69  ?  56   LYS H C   1 
ATOM   6330 O O   . LYS C 2 59  ? -36.631 13.707  35.013  1.00 83.47  ?  56   LYS H O   1 
ATOM   6331 C CB  . LYS C 2 59  ? -34.785 15.806  33.540  1.00 68.37  ?  56   LYS H CB  1 
ATOM   6332 C CG  . LYS C 2 59  ? -33.413 16.459  33.485  1.00 66.32  ?  56   LYS H CG  1 
ATOM   6333 C CD  . LYS C 2 59  ? -33.515 17.974  33.503  1.00 74.27  ?  56   LYS H CD  1 
ATOM   6334 C CE  . LYS C 2 59  ? -32.145 18.620  33.357  1.00 73.78  ?  56   LYS H CE  1 
ATOM   6335 N NZ  . LYS C 2 59  ? -31.249 18.281  34.497  1.00 86.93  1  56   LYS H NZ  1 
ATOM   6336 N N   . LYS C 2 60  ? -37.840 15.598  34.765  1.00 77.41  ?  57   LYS H N   1 
ATOM   6337 C CA  . LYS C 2 60  ? -39.131 14.926  34.763  1.00 67.91  ?  57   LYS H CA  1 
ATOM   6338 C C   . LYS C 2 60  ? -40.052 15.593  33.751  1.00 76.74  ?  57   LYS H C   1 
ATOM   6339 O O   . LYS C 2 60  ? -39.947 16.795  33.492  1.00 75.49  ?  57   LYS H O   1 
ATOM   6340 C CB  . LYS C 2 60  ? -39.784 14.949  36.155  1.00 68.07  ?  57   LYS H CB  1 
ATOM   6341 C CG  . LYS C 2 60  ? -38.946 14.309  37.254  1.00 74.38  ?  57   LYS H CG  1 
ATOM   6342 C CD  . LYS C 2 60  ? -39.393 14.761  38.634  1.00 91.92  ?  57   LYS H CD  1 
ATOM   6343 C CE  . LYS C 2 60  ? -38.417 14.301  39.706  1.00 88.42  ?  57   LYS H CE  1 
ATOM   6344 N NZ  . LYS C 2 60  ? -38.778 14.830  41.050  1.00 92.19  1  57   LYS H NZ  1 
ATOM   6345 N N   . ASP C 2 61  ? -40.959 14.800  33.181  1.00 68.16  ?  58   ASP H N   1 
ATOM   6346 C CA  . ASP C 2 61  ? -41.955 15.309  32.249  1.00 77.06  ?  58   ASP H CA  1 
ATOM   6347 C C   . ASP C 2 61  ? -43.279 14.596  32.488  1.00 73.44  ?  58   ASP H C   1 
ATOM   6348 O O   . ASP C 2 61  ? -43.326 13.497  33.045  1.00 87.34  ?  58   ASP H O   1 
ATOM   6349 C CB  . ASP C 2 61  ? -41.520 15.136  30.788  1.00 74.57  ?  58   ASP H CB  1 
ATOM   6350 C CG  . ASP C 2 61  ? -41.447 16.456  30.045  1.00 91.69  ?  58   ASP H CG  1 
ATOM   6351 O OD1 . ASP C 2 61  ? -40.415 16.721  29.393  1.00 89.33  ?  58   ASP H OD1 1 
ATOM   6352 O OD2 . ASP C 2 61  ? -42.416 17.241  30.133  1.00 84.34  -1 58   ASP H OD2 1 
ATOM   6353 N N   . TYR C 2 62  ? -44.361 15.242  32.056  1.00 80.69  ?  59   TYR H N   1 
ATOM   6354 C CA  . TYR C 2 62  ? -45.707 14.736  32.274  1.00 81.21  ?  59   TYR H CA  1 
ATOM   6355 C C   . TYR C 2 62  ? -46.550 14.986  31.032  1.00 87.93  ?  59   TYR H C   1 
ATOM   6356 O O   . TYR C 2 62  ? -46.184 15.770  30.153  1.00 89.48  ?  59   TYR H O   1 
ATOM   6357 C CB  . TYR C 2 62  ? -46.375 15.397  33.490  1.00 77.93  ?  59   TYR H CB  1 
ATOM   6358 C CG  . TYR C 2 62  ? -45.560 15.342  34.764  1.00 74.66  ?  59   TYR H CG  1 
ATOM   6359 C CD1 . TYR C 2 62  ? -44.558 16.272  35.012  1.00 73.47  ?  59   TYR H CD1 1 
ATOM   6360 C CD2 . TYR C 2 62  ? -45.805 14.373  35.725  1.00 73.30  ?  59   TYR H CD2 1 
ATOM   6361 C CE1 . TYR C 2 62  ? -43.814 16.227  36.174  1.00 74.39  ?  59   TYR H CE1 1 
ATOM   6362 C CE2 . TYR C 2 62  ? -45.068 14.323  36.893  1.00 83.91  ?  59   TYR H CE2 1 
ATOM   6363 C CZ  . TYR C 2 62  ? -44.073 15.253  37.111  1.00 82.12  ?  59   TYR H CZ  1 
ATOM   6364 O OH  . TYR C 2 62  ? -43.334 15.208  38.272  1.00 86.68  ?  59   TYR H OH  1 
ATOM   6365 N N   . ALA C 2 63  ? -47.691 14.304  30.972  1.00 79.13  ?  60   ALA H N   1 
ATOM   6366 C CA  . ALA C 2 63  ? -48.654 14.530  29.908  1.00 83.36  ?  60   ALA H CA  1 
ATOM   6367 C C   . ALA C 2 63  ? -49.559 15.709  30.255  1.00 91.36  ?  60   ALA H C   1 
ATOM   6368 O O   . ALA C 2 63  ? -49.709 16.088  31.420  1.00 97.57  ?  60   ALA H O   1 
ATOM   6369 C CB  . ALA C 2 63  ? -49.489 13.273  29.661  1.00 85.34  ?  60   ALA H CB  1 
ATOM   6370 N N   . ASP C 2 64  ? -50.169 16.291  29.219  1.00 88.60  ?  61   ASP H N   1 
ATOM   6371 C CA  . ASP C 2 64  ? -50.984 17.487  29.419  1.00 100.03 ?  61   ASP H CA  1 
ATOM   6372 C C   . ASP C 2 64  ? -52.205 17.193  30.279  1.00 101.25 ?  61   ASP H C   1 
ATOM   6373 O O   . ASP C 2 64  ? -52.582 18.005  31.133  1.00 102.48 ?  61   ASP H O   1 
ATOM   6374 C CB  . ASP C 2 64  ? -51.414 18.070  28.072  1.00 97.15  ?  61   ASP H CB  1 
ATOM   6375 C CG  . ASP C 2 64  ? -50.244 18.579  27.257  1.00 107.04 ?  61   ASP H CG  1 
ATOM   6376 O OD1 . ASP C 2 64  ? -49.908 17.946  26.233  1.00 111.63 ?  61   ASP H OD1 1 
ATOM   6377 O OD2 . ASP C 2 64  ? -49.654 19.609  27.647  1.00 125.06 -1 61   ASP H OD2 1 
ATOM   6378 N N   . SER C 2 65  ? -52.837 16.037  30.073  1.00 109.28 ?  62   SER H N   1 
ATOM   6379 C CA  . SER C 2 65  ? -54.051 15.697  30.803  1.00 118.41 ?  62   SER H CA  1 
ATOM   6380 C C   . SER C 2 65  ? -53.817 15.491  32.294  1.00 114.05 ?  62   SER H C   1 
ATOM   6381 O O   . SER C 2 65  ? -54.793 15.367  33.042  1.00 110.37 ?  62   SER H O   1 
ATOM   6382 C CB  . SER C 2 65  ? -54.680 14.435  30.207  1.00 116.56 ?  62   SER H CB  1 
ATOM   6383 O OG  . SER C 2 65  ? -53.760 13.356  30.216  1.00 114.23 ?  62   SER H OG  1 
ATOM   6384 N N   . VAL C 2 66  ? -52.563 15.445  32.744  1.00 106.43 ?  63   VAL H N   1 
ATOM   6385 C CA  . VAL C 2 66  ? -52.265 15.106  34.130  1.00 104.65 ?  63   VAL H CA  1 
ATOM   6386 C C   . VAL C 2 66  ? -51.312 16.124  34.746  1.00 105.96 ?  63   VAL H C   1 
ATOM   6387 O O   . VAL C 2 66  ? -51.073 16.107  35.959  1.00 103.78 ?  63   VAL H O   1 
ATOM   6388 C CB  . VAL C 2 66  ? -51.673 13.688  34.239  1.00 107.66 ?  63   VAL H CB  1 
ATOM   6389 C CG1 . VAL C 2 66  ? -51.984 13.108  35.588  1.00 104.92 ?  63   VAL H CG1 1 
ATOM   6390 C CG2 . VAL C 2 66  ? -52.202 12.778  33.137  1.00 113.08 ?  63   VAL H CG2 1 
ATOM   6391 N N   . LYS C 2 67  ? -50.765 17.014  33.919  1.00 110.16 ?  64   LYS H N   1 
ATOM   6392 C CA  . LYS C 2 67  ? -49.717 17.923  34.374  1.00 98.93  ?  64   LYS H CA  1 
ATOM   6393 C C   . LYS C 2 67  ? -50.208 18.793  35.525  1.00 105.05 ?  64   LYS H C   1 
ATOM   6394 O O   . LYS C 2 67  ? -51.264 19.427  35.438  1.00 108.15 ?  64   LYS H O   1 
ATOM   6395 C CB  . LYS C 2 67  ? -49.240 18.794  33.212  1.00 92.58  ?  64   LYS H CB  1 
ATOM   6396 C CG  . LYS C 2 67  ? -47.918 19.501  33.463  1.00 95.24  ?  64   LYS H CG  1 
ATOM   6397 C CD  . LYS C 2 67  ? -47.186 19.758  32.154  1.00 102.67 ?  64   LYS H CD  1 
ATOM   6398 C CE  . LYS C 2 67  ? -45.858 20.461  32.380  1.00 101.79 ?  64   LYS H CE  1 
ATOM   6399 N NZ  . LYS C 2 67  ? -46.044 21.858  32.862  1.00 110.56 1  64   LYS H NZ  1 
ATOM   6400 N N   . GLY C 2 68  ? -49.434 18.814  36.610  1.00 96.02  ?  65   GLY H N   1 
ATOM   6401 C CA  . GLY C 2 68  ? -49.789 19.544  37.804  1.00 100.27 ?  65   GLY H CA  1 
ATOM   6402 C C   . GLY C 2 68  ? -50.529 18.736  38.848  1.00 106.36 ?  65   GLY H C   1 
ATOM   6403 O O   . GLY C 2 68  ? -50.565 19.144  40.015  1.00 114.73 ?  65   GLY H O   1 
ATOM   6404 N N   . ARG C 2 69  ? -51.119 17.604  38.467  1.00 107.63 ?  66   ARG H N   1 
ATOM   6405 C CA  . ARG C 2 69  ? -51.863 16.760  39.393  1.00 105.21 ?  66   ARG H CA  1 
ATOM   6406 C C   . ARG C 2 69  ? -51.044 15.587  39.914  1.00 109.50 ?  66   ARG H C   1 
ATOM   6407 O O   . ARG C 2 69  ? -51.145 15.247  41.097  1.00 103.77 ?  66   ARG H O   1 
ATOM   6408 C CB  . ARG C 2 69  ? -53.141 16.242  38.723  1.00 97.09  ?  66   ARG H CB  1 
ATOM   6409 C CG  . ARG C 2 69  ? -53.979 17.345  38.090  1.00 103.08 ?  66   ARG H CG  1 
ATOM   6410 C CD  . ARG C 2 69  ? -55.409 16.906  37.804  1.00 104.65 ?  66   ARG H CD  1 
ATOM   6411 N NE  . ARG C 2 69  ? -55.487 15.840  36.810  1.00 112.38 ?  66   ARG H NE  1 
ATOM   6412 C CZ  . ARG C 2 69  ? -55.781 14.576  37.093  1.00 107.37 ?  66   ARG H CZ  1 
ATOM   6413 N NH1 . ARG C 2 69  ? -56.030 14.215  38.344  1.00 107.74 1  66   ARG H NH1 1 
ATOM   6414 N NH2 . ARG C 2 69  ? -55.831 13.673  36.123  1.00 110.62 ?  66   ARG H NH2 1 
ATOM   6415 N N   . PHE C 2 70  ? -50.231 14.962  39.067  1.00 97.40  ?  67   PHE H N   1 
ATOM   6416 C CA  . PHE C 2 70  ? -49.336 13.900  39.497  1.00 98.13  ?  67   PHE H CA  1 
ATOM   6417 C C   . PHE C 2 70  ? -47.923 14.448  39.647  1.00 88.66  ?  67   PHE H C   1 
ATOM   6418 O O   . PHE C 2 70  ? -47.547 15.432  39.005  1.00 93.84  ?  67   PHE H O   1 
ATOM   6419 C CB  . PHE C 2 70  ? -49.313 12.726  38.509  1.00 91.58  ?  67   PHE H CB  1 
ATOM   6420 C CG  . PHE C 2 70  ? -50.615 11.971  38.397  1.00 92.69  ?  67   PHE H CG  1 
ATOM   6421 C CD1 . PHE C 2 70  ? -50.672 10.797  37.662  1.00 102.37 ?  67   PHE H CD1 1 
ATOM   6422 C CD2 . PHE C 2 70  ? -51.776 12.432  38.999  1.00 98.37  ?  67   PHE H CD2 1 
ATOM   6423 C CE1 . PHE C 2 70  ? -51.856 10.098  37.533  1.00 109.73 ?  67   PHE H CE1 1 
ATOM   6424 C CE2 . PHE C 2 70  ? -52.963 11.737  38.873  1.00 105.00 ?  67   PHE H CE2 1 
ATOM   6425 C CZ  . PHE C 2 70  ? -53.003 10.569  38.140  1.00 109.10 ?  67   PHE H CZ  1 
ATOM   6426 N N   . THR C 2 71  ? -47.141 13.795  40.502  1.00 90.82  ?  68   THR H N   1 
ATOM   6427 C CA  . THR C 2 71  ? -45.726 14.111  40.666  1.00 93.09  ?  68   THR H CA  1 
ATOM   6428 C C   . THR C 2 71  ? -44.957 12.802  40.720  1.00 91.91  ?  68   THR H C   1 
ATOM   6429 O O   . THR C 2 71  ? -45.221 11.964  41.587  1.00 97.60  ?  68   THR H O   1 
ATOM   6430 C CB  . THR C 2 71  ? -45.473 14.935  41.933  1.00 88.59  ?  68   THR H CB  1 
ATOM   6431 O OG1 . THR C 2 71  ? -46.202 16.167  41.859  1.00 111.22 ?  68   THR H OG1 1 
ATOM   6432 C CG2 . THR C 2 71  ? -43.989 15.237  42.080  1.00 82.32  ?  68   THR H CG2 1 
ATOM   6433 N N   . ILE C 2 72  ? -44.019 12.621  39.795  1.00 93.24  ?  69   ILE H N   1 
ATOM   6434 C CA  . ILE C 2 72  ? -43.246 11.388  39.709  1.00 94.19  ?  69   ILE H CA  1 
ATOM   6435 C C   . ILE C 2 72  ? -41.988 11.552  40.557  1.00 91.93  ?  69   ILE H C   1 
ATOM   6436 O O   . ILE C 2 72  ? -41.072 12.301  40.205  1.00 96.20  ?  69   ILE H O   1 
ATOM   6437 C CB  . ILE C 2 72  ? -42.916 11.026  38.253  1.00 87.71  ?  69   ILE H CB  1 
ATOM   6438 C CG1 . ILE C 2 72  ? -41.952 9.840   38.195  1.00 93.51  ?  69   ILE H CG1 1 
ATOM   6439 C CG2 . ILE C 2 72  ? -42.369 12.225  37.483  1.00 96.59  ?  69   ILE H CG2 1 
ATOM   6440 C CD1 . ILE C 2 72  ? -41.702 9.337   36.790  1.00 88.96  ?  69   ILE H CD1 1 
ATOM   6441 N N   . SER C 2 73  ? -41.953 10.859  41.691  1.00 105.03 ?  70   SER H N   1 
ATOM   6442 C CA  . SER C 2 73  ? -40.814 10.912  42.599  1.00 98.21  ?  70   SER H CA  1 
ATOM   6443 C C   . SER C 2 73  ? -39.830 9.789   42.298  1.00 102.51 ?  70   SER H C   1 
ATOM   6444 O O   . SER C 2 73  ? -40.163 8.832   41.602  1.00 107.08 ?  70   SER H O   1 
ATOM   6445 C CB  . SER C 2 73  ? -41.283 10.826  44.053  1.00 101.18 ?  70   SER H CB  1 
ATOM   6446 O OG  . SER C 2 73  ? -40.217 10.446  44.907  1.00 107.60 ?  70   SER H OG  1 
ATOM   6447 N N   . LYS C 2 78  ? -33.599 2.404   47.820  1.00 99.99  ?  75   LYS H N   1 
ATOM   6448 C CA  . LYS C 2 78  ? -34.552 1.309   47.684  1.00 98.85  ?  75   LYS H CA  1 
ATOM   6449 C C   . LYS C 2 78  ? -34.654 0.862   46.231  1.00 98.54  ?  75   LYS H C   1 
ATOM   6450 O O   . LYS C 2 78  ? -35.141 -0.231  45.941  1.00 108.99 ?  75   LYS H O   1 
ATOM   6451 C CB  . LYS C 2 78  ? -35.933 1.727   48.187  1.00 97.26  ?  75   LYS H CB  1 
ATOM   6452 C CG  . LYS C 2 78  ? -35.924 2.706   49.345  1.00 100.35 ?  75   LYS H CG  1 
ATOM   6453 C CD  . LYS C 2 78  ? -37.272 3.402   49.448  1.00 103.33 ?  75   LYS H CD  1 
ATOM   6454 C CE  . LYS C 2 78  ? -37.403 4.187   50.739  1.00 102.57 ?  75   LYS H CE  1 
ATOM   6455 N NZ  . LYS C 2 78  ? -37.496 3.278   51.914  1.00 95.92  1  75   LYS H NZ  1 
ATOM   6456 N N   . ASN C 2 79  ? -34.201 1.732   45.325  1.00 100.27 ?  76   ASN H N   1 
ATOM   6457 C CA  . ASN C 2 79  ? -34.266 1.489   43.883  1.00 95.83  ?  76   ASN H CA  1 
ATOM   6458 C C   . ASN C 2 79  ? -35.710 1.304   43.421  1.00 87.11  ?  76   ASN H C   1 
ATOM   6459 O O   . ASN C 2 79  ? -36.007 0.473   42.561  1.00 87.33  ?  76   ASN H O   1 
ATOM   6460 C CB  . ASN C 2 79  ? -33.401 0.291   43.482  1.00 91.01  ?  76   ASN H CB  1 
ATOM   6461 C CG  . ASN C 2 79  ? -32.851 0.413   42.075  1.00 98.47  ?  76   ASN H CG  1 
ATOM   6462 O OD1 . ASN C 2 79  ? -33.575 0.747   41.137  1.00 104.56 ?  76   ASN H OD1 1 
ATOM   6463 N ND2 . ASN C 2 79  ? -31.559 0.150   41.923  1.00 104.73 ?  76   ASN H ND2 1 
ATOM   6464 N N   . THR C 2 80  ? -36.617 2.086   44.001  1.00 91.56  ?  77   THR H N   1 
ATOM   6465 C CA  . THR C 2 80  ? -38.026 2.058   43.641  1.00 94.55  ?  77   THR H CA  1 
ATOM   6466 C C   . THR C 2 80  ? -38.440 3.409   43.074  1.00 105.91 ?  77   THR H C   1 
ATOM   6467 O O   . THR C 2 80  ? -37.849 4.445   43.396  1.00 104.80 ?  77   THR H O   1 
ATOM   6468 C CB  . THR C 2 80  ? -38.916 1.718   44.845  1.00 98.27  ?  77   THR H CB  1 
ATOM   6469 O OG1 . THR C 2 80  ? -39.031 2.865   45.695  1.00 105.98 ?  77   THR H OG1 1 
ATOM   6470 C CG2 . THR C 2 80  ? -38.325 0.564   45.640  1.00 88.26  ?  77   THR H CG2 1 
ATOM   6471 N N   . LEU C 2 81  ? -39.465 3.388   42.228  1.00 118.45 ?  78   LEU H N   1 
ATOM   6472 C CA  . LEU C 2 81  ? -40.012 4.587   41.612  1.00 111.51 ?  78   LEU H CA  1 
ATOM   6473 C C   . LEU C 2 81  ? -41.429 4.821   42.118  1.00 115.61 ?  78   LEU H C   1 
ATOM   6474 O O   . LEU C 2 81  ? -42.228 3.884   42.205  1.00 123.89 ?  78   LEU H O   1 
ATOM   6475 C CB  . LEU C 2 81  ? -40.020 4.466   40.086  1.00 106.06 ?  78   LEU H CB  1 
ATOM   6476 C CG  . LEU C 2 81  ? -40.437 5.711   39.301  1.00 103.93 ?  78   LEU H CG  1 
ATOM   6477 C CD1 . LEU C 2 81  ? -39.321 6.744   39.297  1.00 106.63 ?  78   LEU H CD1 1 
ATOM   6478 C CD2 . LEU C 2 81  ? -40.843 5.344   37.884  1.00 95.67  ?  78   LEU H CD2 1 
ATOM   6479 N N   . TYR C 2 82  ? -41.739 6.072   42.443  1.00 94.18  ?  79   TYR H N   1 
ATOM   6480 C CA  . TYR C 2 82  ? -43.035 6.438   42.990  1.00 92.08  ?  79   TYR H CA  1 
ATOM   6481 C C   . TYR C 2 82  ? -43.794 7.335   42.020  1.00 91.69  ?  79   TYR H C   1 
ATOM   6482 O O   . TYR C 2 82  ? -43.217 7.950   41.120  1.00 102.18 ?  79   TYR H O   1 
ATOM   6483 C CB  . TYR C 2 82  ? -42.882 7.148   44.339  1.00 99.68  ?  79   TYR H CB  1 
ATOM   6484 C CG  . TYR C 2 82  ? -42.232 6.305   45.411  1.00 105.30 ?  79   TYR H CG  1 
ATOM   6485 C CD1 . TYR C 2 82  ? -40.858 6.346   45.618  1.00 98.42  ?  79   TYR H CD1 1 
ATOM   6486 C CD2 . TYR C 2 82  ? -42.992 5.470   46.221  1.00 114.96 ?  79   TYR H CD2 1 
ATOM   6487 C CE1 . TYR C 2 82  ? -40.260 5.579   46.599  1.00 110.15 ?  79   TYR H CE1 1 
ATOM   6488 C CE2 . TYR C 2 82  ? -42.404 4.698   47.204  1.00 111.16 ?  79   TYR H CE2 1 
ATOM   6489 C CZ  . TYR C 2 82  ? -41.038 4.756   47.388  1.00 117.29 ?  79   TYR H CZ  1 
ATOM   6490 O OH  . TYR C 2 82  ? -40.447 3.989   48.367  1.00 95.70  ?  79   TYR H OH  1 
ATOM   6491 N N   . LEU C 2 83  ? -45.112 7.398   42.220  1.00 89.02  ?  80   LEU H N   1 
ATOM   6492 C CA  . LEU C 2 83  ? -45.978 8.263   41.418  1.00 93.09  ?  80   LEU H CA  1 
ATOM   6493 C C   . LEU C 2 83  ? -47.122 8.722   42.318  1.00 95.93  ?  80   LEU H C   1 
ATOM   6494 O O   . LEU C 2 83  ? -48.073 7.970   42.551  1.00 104.24 ?  80   LEU H O   1 
ATOM   6495 C CB  . LEU C 2 83  ? -46.493 7.543   40.179  1.00 89.67  ?  80   LEU H CB  1 
ATOM   6496 C CG  . LEU C 2 83  ? -47.516 8.309   39.336  1.00 93.80  ?  80   LEU H CG  1 
ATOM   6497 C CD1 . LEU C 2 83  ? -46.975 9.673   38.927  1.00 93.77  ?  80   LEU H CD1 1 
ATOM   6498 C CD2 . LEU C 2 83  ? -47.924 7.504   38.110  1.00 94.61  ?  80   LEU H CD2 1 
ATOM   6499 N N   . GLN C 2 84  ? -47.021 9.951   42.818  1.00 86.94  ?  81   GLN H N   1 
ATOM   6500 C CA  . GLN C 2 84  ? -48.052 10.518  43.677  1.00 103.39 ?  81   GLN H CA  1 
ATOM   6501 C C   . GLN C 2 84  ? -49.175 11.079  42.814  1.00 102.56 ?  81   GLN H C   1 
ATOM   6502 O O   . GLN C 2 84  ? -48.946 11.973  41.993  1.00 94.91  ?  81   GLN H O   1 
ATOM   6503 C CB  . GLN C 2 84  ? -47.463 11.608  44.570  1.00 96.90  ?  81   GLN H CB  1 
ATOM   6504 C CG  . GLN C 2 84  ? -48.351 12.004  45.738  1.00 107.08 ?  81   GLN H CG  1 
ATOM   6505 C CD  . GLN C 2 84  ? -48.176 11.092  46.936  1.00 110.88 ?  81   GLN H CD  1 
ATOM   6506 O OE1 . GLN C 2 84  ? -49.141 10.519  47.444  1.00 105.31 ?  81   GLN H OE1 1 
ATOM   6507 N NE2 . GLN C 2 84  ? -46.938 10.957  47.400  1.00 112.54 ?  81   GLN H NE2 1 
ATOM   6508 N N   . MET C 2 85  ? -50.384 10.558  42.999  1.00 99.11  ?  82   MET H N   1 
ATOM   6509 C CA  . MET C 2 85  ? -51.556 10.962  42.226  1.00 101.27 ?  82   MET H CA  1 
ATOM   6510 C C   . MET C 2 85  ? -52.457 11.789  43.140  1.00 110.76 ?  82   MET H C   1 
ATOM   6511 O O   . MET C 2 85  ? -53.242 11.239  43.917  1.00 115.82 ?  82   MET H O   1 
ATOM   6512 C CB  . MET C 2 85  ? -52.277 9.738   41.666  1.00 106.21 ?  82   MET H CB  1 
ATOM   6513 C CG  . MET C 2 85  ? -51.384 8.852   40.806  1.00 90.55  ?  82   MET H CG  1 
ATOM   6514 S SD  . MET C 2 85  ? -51.987 7.164   40.594  1.00 105.14 ?  82   MET H SD  1 
ATOM   6515 C CE  . MET C 2 85  ? -53.313 7.391   39.413  1.00 91.40  ?  82   MET H CE  1 
ATOM   6516 N N   . ASN C 2 86  A -52.336 13.110  43.047  1.00 108.42 ?  82   ASN H N   1 
ATOM   6517 C CA  . ASN C 2 86  A -53.103 14.034  43.871  1.00 110.04 ?  82   ASN H CA  1 
ATOM   6518 C C   . ASN C 2 86  A -54.250 14.639  43.073  1.00 113.72 ?  82   ASN H C   1 
ATOM   6519 O O   . ASN C 2 86  A -54.149 14.837  41.859  1.00 113.65 ?  82   ASN H O   1 
ATOM   6520 C CB  . ASN C 2 86  A -52.210 15.149  44.418  1.00 105.31 ?  82   ASN H CB  1 
ATOM   6521 C CG  . ASN C 2 86  A -51.337 14.685  45.564  1.00 115.63 ?  82   ASN H CG  1 
ATOM   6522 O OD1 . ASN C 2 86  A -51.256 13.491  45.854  1.00 105.29 ?  82   ASN H OD1 1 
ATOM   6523 N ND2 . ASN C 2 86  A -50.676 15.629  46.224  1.00 117.62 ?  82   ASN H ND2 1 
ATOM   6524 N N   . SER C 2 87  B -55.343 14.940  43.778  1.00 115.25 ?  82   SER H N   1 
ATOM   6525 C CA  . SER C 2 87  B -56.557 15.478  43.163  1.00 109.18 ?  82   SER H CA  1 
ATOM   6526 C C   . SER C 2 87  B -57.018 14.595  42.009  1.00 115.17 ?  82   SER H C   1 
ATOM   6527 O O   . SER C 2 87  B -57.431 15.078  40.953  1.00 117.91 ?  82   SER H O   1 
ATOM   6528 C CB  . SER C 2 87  B -56.348 16.921  42.698  1.00 113.94 ?  82   SER H CB  1 
ATOM   6529 O OG  . SER C 2 87  B -57.467 17.385  41.963  1.00 110.50 ?  82   SER H OG  1 
ATOM   6530 N N   . LEU C 2 88  C -56.936 13.282  42.213  1.00 126.53 ?  82   LEU H N   1 
ATOM   6531 C CA  . LEU C 2 88  C -57.225 12.314  41.158  1.00 124.45 ?  82   LEU H CA  1 
ATOM   6532 C C   . LEU C 2 88  C -58.695 12.405  40.773  1.00 112.36 ?  82   LEU H C   1 
ATOM   6533 O O   . LEU C 2 88  C -59.572 11.875  41.457  1.00 105.52 ?  82   LEU H O   1 
ATOM   6534 C CB  . LEU C 2 88  C -56.852 10.905  41.605  1.00 113.40 ?  82   LEU H CB  1 
ATOM   6535 C CG  . LEU C 2 88  C -56.783 10.592  43.100  1.00 117.44 ?  82   LEU H CG  1 
ATOM   6536 C CD1 . LEU C 2 88  C -58.154 10.309  43.691  1.00 129.26 ?  82   LEU H CD1 1 
ATOM   6537 C CD2 . LEU C 2 88  C -55.863 9.415   43.314  1.00 115.84 ?  82   LEU H CD2 1 
ATOM   6538 N N   . ARG C 2 89  ? -58.966 13.088  39.667  1.00 122.88 ?  83   ARG H N   1 
ATOM   6539 C CA  . ARG C 2 89  ? -60.319 13.171  39.152  1.00 119.39 ?  83   ARG H CA  1 
ATOM   6540 C C   . ARG C 2 89  ? -60.727 11.825  38.548  1.00 119.77 ?  83   ARG H C   1 
ATOM   6541 O O   . ARG C 2 89  ? -59.919 10.904  38.407  1.00 119.78 ?  83   ARG H O   1 
ATOM   6542 C CB  . ARG C 2 89  ? -60.416 14.312  38.142  1.00 134.31 ?  83   ARG H CB  1 
ATOM   6543 C CG  . ARG C 2 89  ? -59.795 15.606  38.663  1.00 139.34 ?  83   ARG H CG  1 
ATOM   6544 C CD  . ARG C 2 89  ? -59.688 16.679  37.594  1.00 134.10 ?  83   ARG H CD  1 
ATOM   6545 N NE  . ARG C 2 89  ? -59.049 16.185  36.379  1.00 139.78 ?  83   ARG H NE  1 
ATOM   6546 C CZ  . ARG C 2 89  ? -59.693 15.967  35.238  1.00 153.21 ?  83   ARG H CZ  1 
ATOM   6547 N NH1 . ARG C 2 89  ? -60.994 16.211  35.158  1.00 160.30 1  83   ARG H NH1 1 
ATOM   6548 N NH2 . ARG C 2 89  ? -59.039 15.515  34.177  1.00 144.22 ?  83   ARG H NH2 1 
ATOM   6549 N N   . ALA C 2 90  ? -62.004 11.715  38.188  1.00 133.32 ?  84   ALA H N   1 
ATOM   6550 C CA  . ALA C 2 90  ? -62.608 10.418  37.901  1.00 131.48 ?  84   ALA H CA  1 
ATOM   6551 C C   . ALA C 2 90  ? -62.232 9.839   36.540  1.00 120.60 ?  84   ALA H C   1 
ATOM   6552 O O   . ALA C 2 90  ? -62.626 8.706   36.248  1.00 129.43 ?  84   ALA H O   1 
ATOM   6553 C CB  . ALA C 2 90  ? -64.132 10.520  38.004  1.00 125.17 ?  84   ALA H CB  1 
ATOM   6554 N N   . GLU C 2 91  ? -61.487 10.562  35.707  1.00 126.52 ?  85   GLU H N   1 
ATOM   6555 C CA  . GLU C 2 91  ? -61.167 10.098  34.363  1.00 127.63 ?  85   GLU H CA  1 
ATOM   6556 C C   . GLU C 2 91  ? -59.795 9.440   34.266  1.00 117.00 ?  85   GLU H C   1 
ATOM   6557 O O   . GLU C 2 91  ? -59.345 9.135   33.157  1.00 110.24 ?  85   GLU H O   1 
ATOM   6558 C CB  . GLU C 2 91  ? -61.260 11.253  33.362  1.00 140.13 ?  85   GLU H CB  1 
ATOM   6559 C CG  . GLU C 2 91  ? -60.803 12.594  33.904  1.00 132.67 ?  85   GLU H CG  1 
ATOM   6560 C CD  . GLU C 2 91  ? -61.914 13.332  34.619  1.00 142.07 ?  85   GLU H CD  1 
ATOM   6561 O OE1 . GLU C 2 91  ? -62.843 13.818  33.940  1.00 155.25 ?  85   GLU H OE1 1 
ATOM   6562 O OE2 . GLU C 2 91  ? -61.869 13.411  35.863  1.00 138.30 -1 85   GLU H OE2 1 
ATOM   6563 N N   . ASP C 2 92  ? -59.122 9.211   35.391  1.00 101.95 ?  86   ASP H N   1 
ATOM   6564 C CA  . ASP C 2 92  ? -57.835 8.531   35.391  1.00 98.85  ?  86   ASP H CA  1 
ATOM   6565 C C   . ASP C 2 92  ? -57.963 7.029   35.613  1.00 114.45 ?  86   ASP H C   1 
ATOM   6566 O O   . ASP C 2 92  ? -56.947 6.358   35.821  1.00 110.57 ?  86   ASP H O   1 
ATOM   6567 C CB  . ASP C 2 92  ? -56.914 9.135   36.454  1.00 111.23 ?  86   ASP H CB  1 
ATOM   6568 C CG  . ASP C 2 92  ? -56.848 10.646  36.377  1.00 105.79 ?  86   ASP H CG  1 
ATOM   6569 O OD1 . ASP C 2 92  ? -57.325 11.310  37.321  1.00 104.84 ?  86   ASP H OD1 1 
ATOM   6570 O OD2 . ASP C 2 92  ? -56.332 11.169  35.366  1.00 101.35 -1 86   ASP H OD2 1 
ATOM   6571 N N   . THR C 2 93  ? -59.183 6.492   35.578  1.00 120.10 ?  87   THR H N   1 
ATOM   6572 C CA  . THR C 2 93  ? -59.391 5.061   35.766  1.00 112.68 ?  87   THR H CA  1 
ATOM   6573 C C   . THR C 2 93  ? -58.669 4.273   34.683  1.00 107.64 ?  87   THR H C   1 
ATOM   6574 O O   . THR C 2 93  ? -58.982 4.401   33.494  1.00 111.39 ?  87   THR H O   1 
ATOM   6575 C CB  . THR C 2 93  ? -60.885 4.740   35.750  1.00 119.06 ?  87   THR H CB  1 
ATOM   6576 O OG1 . THR C 2 93  ? -61.491 5.208   36.962  1.00 121.08 ?  87   THR H OG1 1 
ATOM   6577 C CG2 . THR C 2 93  ? -61.109 3.240   35.616  1.00 107.67 ?  87   THR H CG2 1 
ATOM   6578 N N   . ALA C 2 94  ? -57.705 3.455   35.097  1.00 109.01 ?  88   ALA H N   1 
ATOM   6579 C CA  . ALA C 2 94  ? -56.858 2.719   34.169  1.00 103.60 ?  88   ALA H CA  1 
ATOM   6580 C C   . ALA C 2 94  ? -56.014 1.732   34.960  1.00 96.09  ?  88   ALA H C   1 
ATOM   6581 O O   . ALA C 2 94  ? -55.960 1.776   36.192  1.00 89.59  ?  88   ALA H O   1 
ATOM   6582 C CB  . ALA C 2 94  ? -55.963 3.662   33.360  1.00 93.14  ?  88   ALA H CB  1 
ATOM   6583 N N   . VAL C 2 95  ? -55.357 0.836   34.232  1.00 87.10  ?  89   VAL H N   1 
ATOM   6584 C CA  . VAL C 2 95  ? -54.295 0.001   34.779  1.00 100.90 ?  89   VAL H CA  1 
ATOM   6585 C C   . VAL C 2 95  ? -52.973 0.669   34.428  1.00 95.32  ?  89   VAL H C   1 
ATOM   6586 O O   . VAL C 2 95  ? -52.672 0.893   33.249  1.00 91.62  ?  89   VAL H O   1 
ATOM   6587 C CB  . VAL C 2 95  ? -54.365 -1.439  34.243  1.00 96.10  ?  89   VAL H CB  1 
ATOM   6588 C CG1 . VAL C 2 95  ? -54.666 -1.451  32.752  1.00 96.89  ?  89   VAL H CG1 1 
ATOM   6589 C CG2 . VAL C 2 95  ? -53.066 -2.177  34.536  1.00 87.00  ?  89   VAL H CG2 1 
ATOM   6590 N N   . TYR C 2 96  ? -52.193 1.011   35.446  1.00 95.61  ?  90   TYR H N   1 
ATOM   6591 C CA  . TYR C 2 96  ? -50.972 1.783   35.268  1.00 82.42  ?  90   TYR H CA  1 
ATOM   6592 C C   . TYR C 2 96  ? -49.769 0.853   35.219  1.00 84.78  ?  90   TYR H C   1 
ATOM   6593 O O   . TYR C 2 96  ? -49.569 0.037   36.125  1.00 91.62  ?  90   TYR H O   1 
ATOM   6594 C CB  . TYR C 2 96  ? -50.809 2.807   36.391  1.00 82.49  ?  90   TYR H CB  1 
ATOM   6595 C CG  . TYR C 2 96  ? -51.693 4.025   36.239  1.00 93.99  ?  90   TYR H CG  1 
ATOM   6596 C CD1 . TYR C 2 96  ? -53.075 3.906   36.220  1.00 86.29  ?  90   TYR H CD1 1 
ATOM   6597 C CD2 . TYR C 2 96  ? -51.145 5.296   36.119  1.00 81.08  ?  90   TYR H CD2 1 
ATOM   6598 C CE1 . TYR C 2 96  ? -53.888 5.014   36.085  1.00 97.26  ?  90   TYR H CE1 1 
ATOM   6599 C CE2 . TYR C 2 96  ? -51.952 6.412   35.983  1.00 81.32  ?  90   TYR H CE2 1 
ATOM   6600 C CZ  . TYR C 2 96  ? -53.322 6.264   35.967  1.00 98.09  ?  90   TYR H CZ  1 
ATOM   6601 O OH  . TYR C 2 96  ? -54.132 7.369   35.832  1.00 88.01  ?  90   TYR H OH  1 
ATOM   6602 N N   . TYR C 2 97  ? -48.972 0.983   34.166  1.00 92.05  ?  91   TYR H N   1 
ATOM   6603 C CA  . TYR C 2 97  ? -47.790 0.161   33.965  1.00 90.51  ?  91   TYR H CA  1 
ATOM   6604 C C   . TYR C 2 97  ? -46.526 0.954   34.273  1.00 82.90  ?  91   TYR H C   1 
ATOM   6605 O O   . TYR C 2 97  ? -46.500 2.185   34.201  1.00 84.47  ?  91   TYR H O   1 
ATOM   6606 C CB  . TYR C 2 97  ? -47.731 -0.364  32.529  1.00 91.82  ?  91   TYR H CB  1 
ATOM   6607 C CG  . TYR C 2 97  ? -48.863 -1.293  32.160  1.00 82.58  ?  91   TYR H CG  1 
ATOM   6608 C CD1 . TYR C 2 97  ? -48.715 -2.669  32.258  1.00 92.05  ?  91   TYR H CD1 1 
ATOM   6609 C CD2 . TYR C 2 97  ? -50.079 -0.794  31.709  1.00 94.39  ?  91   TYR H CD2 1 
ATOM   6610 C CE1 . TYR C 2 97  ? -49.745 -3.524  31.919  1.00 95.40  ?  91   TYR H CE1 1 
ATOM   6611 C CE2 . TYR C 2 97  ? -51.115 -1.642  31.369  1.00 98.18  ?  91   TYR H CE2 1 
ATOM   6612 C CZ  . TYR C 2 97  ? -50.943 -3.005  31.476  1.00 94.52  ?  91   TYR H CZ  1 
ATOM   6613 O OH  . TYR C 2 97  ? -51.971 -3.852  31.137  1.00 91.90  ?  91   TYR H OH  1 
ATOM   6614 N N   . CYS C 2 98  ? -45.471 0.223   34.620  1.00 88.20  ?  92   CYS H N   1 
ATOM   6615 C CA  . CYS C 2 98  ? -44.150 0.787   34.859  1.00 78.89  ?  92   CYS H CA  1 
ATOM   6616 C C   . CYS C 2 98  ? -43.181 0.191   33.850  1.00 79.22  ?  92   CYS H C   1 
ATOM   6617 O O   . CYS C 2 98  ? -43.072 -1.035  33.739  1.00 80.85  ?  92   CYS H O   1 
ATOM   6618 C CB  . CYS C 2 98  ? -43.682 0.501   36.286  1.00 84.78  ?  92   CYS H CB  1 
ATOM   6619 S SG  . CYS C 2 98  ? -42.068 1.181   36.709  1.00 118.51 ?  92   CYS H SG  1 
ATOM   6620 N N   . ALA C 2 99  ? -42.483 1.054   33.115  1.00 80.01  ?  93   ALA H N   1 
ATOM   6621 C CA  . ALA C 2 99  ? -41.598 0.604   32.053  1.00 76.94  ?  93   ALA H CA  1 
ATOM   6622 C C   . ALA C 2 99  ? -40.291 1.382   32.098  1.00 79.94  ?  93   ALA H C   1 
ATOM   6623 O O   . ALA C 2 99  ? -40.225 2.506   32.603  1.00 81.57  ?  93   ALA H O   1 
ATOM   6624 C CB  . ALA C 2 99  ? -42.255 0.753   30.674  1.00 75.62  ?  93   ALA H CB  1 
ATOM   6625 N N   . ARG C 2 100 ? -39.247 0.760   31.559  1.00 71.51  ?  94   ARG H N   1 
ATOM   6626 C CA  . ARG C 2 100 ? -37.936 1.370   31.419  1.00 68.52  ?  94   ARG H CA  1 
ATOM   6627 C C   . ARG C 2 100 ? -37.555 1.417   29.946  1.00 69.39  ?  94   ARG H C   1 
ATOM   6628 O O   . ARG C 2 100 ? -38.122 0.704   29.116  1.00 73.74  ?  94   ARG H O   1 
ATOM   6629 C CB  . ARG C 2 100 ? -36.862 0.590   32.185  1.00 70.63  ?  94   ARG H CB  1 
ATOM   6630 C CG  . ARG C 2 100 ? -36.351 -0.598  31.392  1.00 72.68  ?  94   ARG H CG  1 
ATOM   6631 C CD  . ARG C 2 100 ? -35.037 -1.152  31.903  1.00 76.57  ?  94   ARG H CD  1 
ATOM   6632 N NE  . ARG C 2 100 ? -34.392 -1.952  30.865  1.00 79.42  ?  94   ARG H NE  1 
ATOM   6633 C CZ  . ARG C 2 100 ? -33.397 -2.804  31.079  1.00 74.53  ?  94   ARG H CZ  1 
ATOM   6634 N NH1 . ARG C 2 100 ? -32.925 -2.985  32.303  1.00 75.11  1  94   ARG H NH1 1 
ATOM   6635 N NH2 . ARG C 2 100 ? -32.878 -3.483  30.065  1.00 75.71  ?  94   ARG H NH2 1 
ATOM   6636 N N   . ASN C 2 101 ? -36.572 2.258   29.632  1.00 66.25  ?  95   ASN H N   1 
ATOM   6637 C CA  . ASN C 2 101 ? -36.002 2.293   28.293  1.00 62.00  ?  95   ASN H CA  1 
ATOM   6638 C C   . ASN C 2 101 ? -34.646 2.977   28.366  1.00 61.95  ?  95   ASN H C   1 
ATOM   6639 O O   . ASN C 2 101 ? -34.411 3.824   29.232  1.00 69.35  ?  95   ASN H O   1 
ATOM   6640 C CB  . ASN C 2 101 ? -36.922 3.012   27.297  1.00 72.77  ?  95   ASN H CB  1 
ATOM   6641 C CG  . ASN C 2 101 ? -36.792 4.518   27.363  1.00 64.96  ?  95   ASN H CG  1 
ATOM   6642 O OD1 . ASN C 2 101 ? -37.195 5.146   28.341  1.00 67.10  ?  95   ASN H OD1 1 
ATOM   6643 N ND2 . ASN C 2 101 ? -36.239 5.109   26.311  1.00 58.80  ?  95   ASN H ND2 1 
ATOM   6644 N N   . LEU C 2 102 ? -33.756 2.594   27.455  1.00 65.80  ?  96   LEU H N   1 
ATOM   6645 C CA  . LEU C 2 102 ? -32.402 3.127   27.428  1.00 61.70  ?  96   LEU H CA  1 
ATOM   6646 C C   . LEU C 2 102 ? -32.365 4.437   26.652  1.00 62.02  ?  96   LEU H C   1 
ATOM   6647 O O   . LEU C 2 102 ? -32.966 4.558   25.581  1.00 60.98  ?  96   LEU H O   1 
ATOM   6648 C CB  . LEU C 2 102 ? -31.436 2.120   26.803  1.00 58.73  ?  96   LEU H CB  1 
ATOM   6649 C CG  . LEU C 2 102 ? -29.944 2.434   26.924  1.00 61.00  ?  96   LEU H CG  1 
ATOM   6650 C CD1 . LEU C 2 102 ? -29.560 2.636   28.380  1.00 61.57  ?  96   LEU H CD1 1 
ATOM   6651 C CD2 . LEU C 2 102 ? -29.108 1.326   26.303  1.00 58.18  ?  96   LEU H CD2 1 
ATOM   6652 N N   . ILE C 2 103 ? -31.657 5.422   27.207  1.00 64.77  ?  97   ILE H N   1 
ATOM   6653 C CA  . ILE C 2 103 ? -31.529 6.737   26.598  1.00 61.52  ?  97   ILE H CA  1 
ATOM   6654 C C   . ILE C 2 103 ? -30.055 7.112   26.542  1.00 59.19  ?  97   ILE H C   1 
ATOM   6655 O O   . ILE C 2 103 ? -29.218 6.563   27.263  1.00 64.92  ?  97   ILE H O   1 
ATOM   6656 C CB  . ILE C 2 103 ? -32.319 7.820   27.363  1.00 62.08  ?  97   ILE H CB  1 
ATOM   6657 C CG1 . ILE C 2 103 ? -31.649 8.108   28.709  1.00 67.79  ?  97   ILE H CG1 1 
ATOM   6658 C CG2 . ILE C 2 103 ? -33.764 7.387   27.563  1.00 63.10  ?  97   ILE H CG2 1 
ATOM   6659 C CD1 . ILE C 2 103 ? -32.127 9.377   29.374  1.00 64.22  ?  97   ILE H CD1 1 
ATOM   6660 N N   . ARG C 2 104 ? -29.743 8.058   25.659  1.00 60.05  ?  98   ARG H N   1 
ATOM   6661 C CA  . ARG C 2 104 ? -28.408 8.637   25.632  1.00 57.93  ?  98   ARG H CA  1 
ATOM   6662 C C   . ARG C 2 104 ? -28.139 9.355   26.948  1.00 55.35  ?  98   ARG H C   1 
ATOM   6663 O O   . ARG C 2 104 ? -29.037 9.965   27.537  1.00 68.03  ?  98   ARG H O   1 
ATOM   6664 C CB  . ARG C 2 104 ? -28.270 9.608   24.457  1.00 53.30  ?  98   ARG H CB  1 
ATOM   6665 C CG  . ARG C 2 104 ? -28.647 9.016   23.103  1.00 61.77  ?  98   ARG H CG  1 
ATOM   6666 C CD  . ARG C 2 104 ? -28.866 10.106  22.062  1.00 65.81  ?  98   ARG H CD  1 
ATOM   6667 N NE  . ARG C 2 104 ? -27.647 10.459  21.339  1.00 71.29  ?  98   ARG H NE  1 
ATOM   6668 C CZ  . ARG C 2 104 ? -27.488 10.314  20.027  1.00 61.27  ?  98   ARG H CZ  1 
ATOM   6669 N NH1 . ARG C 2 104 ? -28.476 9.831   19.285  1.00 49.96  1  98   ARG H NH1 1 
ATOM   6670 N NH2 . ARG C 2 104 ? -26.346 10.663  19.451  1.00 70.12  ?  98   ARG H NH2 1 
ATOM   6671 N N   . TYR C 2 105 ? -26.897 9.275   27.418  1.00 53.15  ?  99   TYR H N   1 
ATOM   6672 C CA  . TYR C 2 105 ? -26.538 9.836   28.720  1.00 62.01  ?  99   TYR H CA  1 
ATOM   6673 C C   . TYR C 2 105 ? -26.419 11.349  28.589  1.00 66.16  ?  99   TYR H C   1 
ATOM   6674 O O   . TYR C 2 105 ? -25.343 11.895  28.337  1.00 55.11  ?  99   TYR H O   1 
ATOM   6675 C CB  . TYR C 2 105 ? -25.247 9.218   29.241  1.00 53.79  ?  99   TYR H CB  1 
ATOM   6676 C CG  . TYR C 2 105 ? -24.907 9.647   30.650  1.00 56.18  ?  99   TYR H CG  1 
ATOM   6677 C CD1 . TYR C 2 105 ? -25.471 9.008   31.745  1.00 55.61  ?  99   TYR H CD1 1 
ATOM   6678 C CD2 . TYR C 2 105 ? -24.027 10.695  30.886  1.00 57.50  ?  99   TYR H CD2 1 
ATOM   6679 C CE1 . TYR C 2 105 ? -25.167 9.398   33.034  1.00 56.34  ?  99   TYR H CE1 1 
ATOM   6680 C CE2 . TYR C 2 105 ? -23.717 11.092  32.172  1.00 54.73  ?  99   TYR H CE2 1 
ATOM   6681 C CZ  . TYR C 2 105 ? -24.290 10.440  33.242  1.00 55.89  ?  99   TYR H CZ  1 
ATOM   6682 O OH  . TYR C 2 105 ? -23.983 10.832  34.524  1.00 72.70  ?  99   TYR H OH  1 
ATOM   6683 N N   . SER C 2 106 ? -27.544 12.037  28.770  1.00 60.12  ?  100  SER H N   1 
ATOM   6684 C CA  . SER C 2 106 ? -27.563 13.492  28.758  1.00 68.29  ?  100  SER H CA  1 
ATOM   6685 C C   . SER C 2 106 ? -28.864 13.966  29.384  1.00 70.83  ?  100  SER H C   1 
ATOM   6686 O O   . SER C 2 106 ? -29.814 13.194  29.548  1.00 57.42  ?  100  SER H O   1 
ATOM   6687 C CB  . SER C 2 106 ? -27.421 14.055  27.340  1.00 65.48  ?  100  SER H CB  1 
ATOM   6688 O OG  . SER C 2 106 ? -28.692 14.272  26.751  1.00 77.52  ?  100  SER H OG  1 
ATOM   6689 N N   . GLY C 2 107 A -28.894 15.254  29.734  1.00 73.74  ?  100  GLY H N   1 
ATOM   6690 C CA  . GLY C 2 107 A -30.121 15.858  30.219  1.00 61.24  ?  100  GLY H CA  1 
ATOM   6691 C C   . GLY C 2 107 A -31.205 15.958  29.168  1.00 60.34  ?  100  GLY H C   1 
ATOM   6692 O O   . GLY C 2 107 A -32.383 16.087  29.517  1.00 65.16  ?  100  GLY H O   1 
ATOM   6693 N N   . SER C 2 108 B -30.832 15.901  27.890  1.00 67.29  ?  100  SER H N   1 
ATOM   6694 C CA  . SER C 2 108 B -31.788 15.914  26.789  1.00 64.82  ?  100  SER H CA  1 
ATOM   6695 C C   . SER C 2 108 B -32.214 14.481  26.485  1.00 61.48  ?  100  SER H C   1 
ATOM   6696 O O   . SER C 2 108 B -31.386 13.654  26.086  1.00 78.37  ?  100  SER H O   1 
ATOM   6697 C CB  . SER C 2 108 B -31.178 16.571  25.551  1.00 71.08  ?  100  SER H CB  1 
ATOM   6698 O OG  . SER C 2 108 B -30.649 17.852  25.852  1.00 70.45  ?  100  SER H OG  1 
ATOM   6699 N N   . TYR C 2 109 C -33.501 14.192  26.673  1.00 69.20  ?  100  TYR H N   1 
ATOM   6700 C CA  . TYR C 2 109 C -34.026 12.844  26.480  1.00 58.42  ?  100  TYR H CA  1 
ATOM   6701 C C   . TYR C 2 109 C -33.965 12.459  25.008  1.00 69.55  ?  100  TYR H C   1 
ATOM   6702 O O   . TYR C 2 109 C -34.501 13.168  24.150  1.00 67.55  ?  100  TYR H O   1 
ATOM   6703 C CB  . TYR C 2 109 C -35.465 12.763  26.992  1.00 56.70  ?  100  TYR H CB  1 
ATOM   6704 C CG  . TYR C 2 109 C -36.141 11.424  26.763  1.00 59.63  ?  100  TYR H CG  1 
ATOM   6705 C CD1 . TYR C 2 109 C -36.774 11.134  25.558  1.00 58.92  ?  100  TYR H CD1 1 
ATOM   6706 C CD2 . TYR C 2 109 C -36.152 10.452  27.754  1.00 66.10  ?  100  TYR H CD2 1 
ATOM   6707 C CE1 . TYR C 2 109 C -37.385 9.913   25.345  1.00 67.08  ?  100  TYR H CE1 1 
ATOM   6708 C CE2 . TYR C 2 109 C -36.766 9.230   27.550  1.00 64.54  ?  100  TYR H CE2 1 
ATOM   6709 C CZ  . TYR C 2 109 C -37.379 8.967   26.346  1.00 66.64  ?  100  TYR H CZ  1 
ATOM   6710 O OH  . TYR C 2 109 C -37.988 7.750   26.149  1.00 60.67  ?  100  TYR H OH  1 
ATOM   6711 N N   . PHE C 2 110 D -33.327 11.325  24.715  1.00 77.00  ?  100  PHE H N   1 
ATOM   6712 C CA  . PHE C 2 110 D -33.315 10.794  23.360  1.00 70.49  ?  100  PHE H CA  1 
ATOM   6713 C C   . PHE C 2 110 D -33.073 9.306   23.534  1.00 69.95  ?  100  PHE H C   1 
ATOM   6714 O O   . PHE C 2 110 D -32.047 8.925   24.123  1.00 69.08  ?  100  PHE H O   1 
ATOM   6715 C CB  . PHE C 2 110 D -32.255 11.378  22.428  1.00 65.15  ?  100  PHE H CB  1 
ATOM   6716 C CG  . PHE C 2 110 D -32.504 11.067  20.977  1.00 68.57  ?  100  PHE H CG  1 
ATOM   6717 C CD1 . PHE C 2 110 D -33.258 11.931  20.207  1.00 72.24  ?  100  PHE H CD1 1 
ATOM   6718 C CD2 . PHE C 2 110 D -32.020 9.902   20.392  1.00 67.09  ?  100  PHE H CD2 1 
ATOM   6719 C CE1 . PHE C 2 110 D -33.513 11.662  18.880  1.00 71.75  ?  100  PHE H CE1 1 
ATOM   6720 C CE2 . PHE C 2 110 D -32.274 9.624   19.051  1.00 68.10  ?  100  PHE H CE2 1 
ATOM   6721 C CZ  . PHE C 2 110 D -33.023 10.511  18.298  1.00 77.09  ?  100  PHE H CZ  1 
ATOM   6722 N N   . PRO C 2 111 E -33.969 8.463   23.039  1.00 69.89  ?  100  PRO H N   1 
ATOM   6723 C CA  . PRO C 2 111 E -33.841 7.028   23.281  1.00 65.79  ?  100  PRO H CA  1 
ATOM   6724 C C   . PRO C 2 111 E -32.829 6.365   22.358  1.00 69.91  ?  100  PRO H C   1 
ATOM   6725 O O   . PRO C 2 111 E -32.554 6.828   21.248  1.00 61.50  ?  100  PRO H O   1 
ATOM   6726 C CB  . PRO C 2 111 E -35.254 6.511   23.006  1.00 59.67  ?  100  PRO H CB  1 
ATOM   6727 C CG  . PRO C 2 111 E -35.759 7.439   21.942  1.00 63.99  ?  100  PRO H CG  1 
ATOM   6728 C CD  . PRO C 2 111 E -35.181 8.796   22.273  1.00 64.05  ?  100  PRO H CD  1 
ATOM   6729 N N   . VAL C 2 112 F -32.278 5.246   22.835  1.00 63.19  ?  100  VAL H N   1 
ATOM   6730 C CA  . VAL C 2 112 F -31.447 4.385   21.998  1.00 63.65  ?  100  VAL H CA  1 
ATOM   6731 C C   . VAL C 2 112 F -32.295 3.195   21.567  1.00 63.95  ?  100  VAL H C   1 
ATOM   6732 O O   . VAL C 2 112 F -32.110 2.650   20.473  1.00 82.64  ?  100  VAL H O   1 
ATOM   6733 C CB  . VAL C 2 112 F -30.156 3.946   22.720  1.00 62.84  ?  100  VAL H CB  1 
ATOM   6734 C CG1 . VAL C 2 112 F -29.936 4.769   23.978  1.00 59.22  ?  100  VAL H CG1 1 
ATOM   6735 C CG2 . VAL C 2 112 F -30.163 2.451   23.029  1.00 61.42  ?  100  VAL H CG2 1 
ATOM   6736 N N   . HIS C 2 113 G -33.241 2.797   22.417  1.00 62.71  ?  100  HIS H N   1 
ATOM   6737 C CA  . HIS C 2 113 G -34.251 1.814   22.050  1.00 74.99  ?  100  HIS H CA  1 
ATOM   6738 C C   . HIS C 2 113 G -35.485 2.055   22.908  1.00 70.53  ?  100  HIS H C   1 
ATOM   6739 O O   . HIS C 2 113 G -35.454 2.815   23.880  1.00 64.72  ?  100  HIS H O   1 
ATOM   6740 C CB  . HIS C 2 113 G -33.731 0.372   22.185  1.00 60.06  ?  100  HIS H CB  1 
ATOM   6741 C CG  . HIS C 2 113 G -33.381 -0.034  23.585  1.00 63.75  ?  100  HIS H CG  1 
ATOM   6742 N ND1 . HIS C 2 113 G -34.317 -0.135  24.592  1.00 65.71  ?  100  HIS H ND1 1 
ATOM   6743 C CD2 . HIS C 2 113 G -32.198 -0.397  24.136  1.00 60.45  ?  100  HIS H CD2 1 
ATOM   6744 C CE1 . HIS C 2 113 G -33.724 -0.525  25.706  1.00 61.45  ?  100  HIS H CE1 1 
ATOM   6745 N NE2 . HIS C 2 113 G -32.438 -0.693  25.456  1.00 60.87  ?  100  HIS H NE2 1 
ATOM   6746 N N   . GLY C 2 114 H -36.580 1.400   22.533  1.00 70.10  ?  100  GLY H N   1 
ATOM   6747 C CA  . GLY C 2 114 H -37.857 1.609   23.179  1.00 64.22  ?  100  GLY H CA  1 
ATOM   6748 C C   . GLY C 2 114 H -37.962 0.904   24.519  1.00 71.38  ?  100  GLY H C   1 
ATOM   6749 O O   . GLY C 2 114 H -37.007 0.329   25.042  1.00 65.10  ?  100  GLY H O   1 
ATOM   6750 N N   . MET C 2 115 I -39.169 0.959   25.080  1.00 68.33  ?  100  MET H N   1 
ATOM   6751 C CA  . MET C 2 115 I -39.445 0.331   26.368  1.00 72.56  ?  100  MET H CA  1 
ATOM   6752 C C   . MET C 2 115 I -39.418 -1.185  26.208  1.00 79.76  ?  100  MET H C   1 
ATOM   6753 O O   . MET C 2 115 I -40.338 -1.772  25.629  1.00 78.86  ?  100  MET H O   1 
ATOM   6754 C CB  . MET C 2 115 I -40.792 0.803   26.908  1.00 77.19  ?  100  MET H CB  1 
ATOM   6755 C CG  . MET C 2 115 I -40.942 2.316   26.971  1.00 78.50  ?  100  MET H CG  1 
ATOM   6756 S SD  . MET C 2 115 I -42.531 2.837   27.648  1.00 80.00  ?  100  MET H SD  1 
ATOM   6757 C CE  . MET C 2 115 I -42.741 4.417   26.833  1.00 69.31  ?  100  MET H CE  1 
ATOM   6758 N N   . ASP C 2 116 ? -38.371 -1.824  26.731  1.00 77.42  ?  101  ASP H N   1 
ATOM   6759 C CA  . ASP C 2 116 ? -38.149 -3.245  26.494  1.00 72.43  ?  101  ASP H CA  1 
ATOM   6760 C C   . ASP C 2 116 ? -38.788 -4.137  27.553  1.00 77.26  ?  101  ASP H C   1 
ATOM   6761 O O   . ASP C 2 116 ? -39.412 -5.146  27.211  1.00 81.24  ?  101  ASP H O   1 
ATOM   6762 C CB  . ASP C 2 116 ? -36.647 -3.536  26.405  1.00 70.20  ?  101  ASP H CB  1 
ATOM   6763 C CG  . ASP C 2 116 ? -35.873 -2.992  27.590  1.00 78.66  ?  101  ASP H CG  1 
ATOM   6764 O OD1 . ASP C 2 116 ? -36.484 -2.323  28.450  1.00 89.53  ?  101  ASP H OD1 1 
ATOM   6765 O OD2 . ASP C 2 116 ? -34.649 -3.233  27.661  1.00 70.76  -1 101  ASP H OD2 1 
ATOM   6766 N N   . VAL C 2 117 ? -38.643 -3.799  28.832  1.00 72.12  ?  102  VAL H N   1 
ATOM   6767 C CA  . VAL C 2 117 ? -39.204 -4.589  29.923  1.00 82.17  ?  102  VAL H CA  1 
ATOM   6768 C C   . VAL C 2 117 ? -40.226 -3.737  30.664  1.00 78.73  ?  102  VAL H C   1 
ATOM   6769 O O   . VAL C 2 117 ? -39.952 -2.579  31.000  1.00 86.92  ?  102  VAL H O   1 
ATOM   6770 C CB  . VAL C 2 117 ? -38.112 -5.110  30.878  1.00 71.74  ?  102  VAL H CB  1 
ATOM   6771 C CG1 . VAL C 2 117 ? -37.103 -4.027  31.185  1.00 82.68  ?  102  VAL H CG1 1 
ATOM   6772 C CG2 . VAL C 2 117 ? -38.731 -5.646  32.165  1.00 89.58  ?  102  VAL H CG2 1 
ATOM   6773 N N   . TRP C 2 118 ? -41.401 -4.310  30.908  1.00 91.88  ?  103  TRP H N   1 
ATOM   6774 C CA  . TRP C 2 118 ? -42.508 -3.641  31.569  1.00 81.82  ?  103  TRP H CA  1 
ATOM   6775 C C   . TRP C 2 118 ? -42.840 -4.356  32.873  1.00 77.73  ?  103  TRP H C   1 
ATOM   6776 O O   . TRP C 2 118 ? -42.415 -5.487  33.118  1.00 86.45  ?  103  TRP H O   1 
ATOM   6777 C CB  . TRP C 2 118 ? -43.749 -3.602  30.666  1.00 79.23  ?  103  TRP H CB  1 
ATOM   6778 C CG  . TRP C 2 118 ? -43.571 -2.845  29.381  1.00 79.28  ?  103  TRP H CG  1 
ATOM   6779 C CD1 . TRP C 2 118 ? -42.586 -3.021  28.450  1.00 80.24  ?  103  TRP H CD1 1 
ATOM   6780 C CD2 . TRP C 2 118 ? -44.421 -1.810  28.872  1.00 78.12  ?  103  TRP H CD2 1 
ATOM   6781 N NE1 . TRP C 2 118 ? -42.762 -2.149  27.403  1.00 86.58  ?  103  TRP H NE1 1 
ATOM   6782 C CE2 . TRP C 2 118 ? -43.883 -1.396  27.637  1.00 86.22  ?  103  TRP H CE2 1 
ATOM   6783 C CE3 . TRP C 2 118 ? -45.581 -1.189  29.344  1.00 72.95  ?  103  TRP H CE3 1 
ATOM   6784 C CZ2 . TRP C 2 118 ? -44.466 -0.389  26.868  1.00 91.73  ?  103  TRP H CZ2 1 
ATOM   6785 C CZ3 . TRP C 2 118 ? -46.157 -0.191  28.581  1.00 86.22  ?  103  TRP H CZ3 1 
ATOM   6786 C CH2 . TRP C 2 118 ? -45.600 0.199   27.357  1.00 84.35  ?  103  TRP H CH2 1 
ATOM   6787 N N   . GLY C 2 119 ? -43.618 -3.673  33.715  1.00 81.12  ?  104  GLY H N   1 
ATOM   6788 C CA  . GLY C 2 119 ? -44.172 -4.291  34.900  1.00 84.94  ?  104  GLY H CA  1 
ATOM   6789 C C   . GLY C 2 119 ? -45.474 -5.015  34.605  1.00 85.44  ?  104  GLY H C   1 
ATOM   6790 O O   . GLY C 2 119 ? -46.096 -4.825  33.561  1.00 94.33  ?  104  GLY H O   1 
ATOM   6791 N N   . GLN C 2 120 ? -45.882 -5.864  35.550  1.00 105.51 ?  105  GLN H N   1 
ATOM   6792 C CA  . GLN C 2 120 ? -47.125 -6.606  35.377  1.00 113.18 ?  105  GLN H CA  1 
ATOM   6793 C C   . GLN C 2 120 ? -48.345 -5.697  35.433  1.00 109.47 ?  105  GLN H C   1 
ATOM   6794 O O   . GLN C 2 120 ? -49.419 -6.090  34.963  1.00 108.06 ?  105  GLN H O   1 
ATOM   6795 C CB  . GLN C 2 120 ? -47.240 -7.710  36.430  1.00 100.21 ?  105  GLN H CB  1 
ATOM   6796 C CG  . GLN C 2 120 ? -47.912 -7.290  37.732  1.00 105.48 ?  105  GLN H CG  1 
ATOM   6797 C CD  . GLN C 2 120 ? -47.052 -6.370  38.579  1.00 112.75 ?  105  GLN H CD  1 
ATOM   6798 O OE1 . GLN C 2 120 ? -45.908 -6.071  38.234  1.00 118.27 ?  105  GLN H OE1 1 
ATOM   6799 N NE2 . GLN C 2 120 ? -47.601 -5.920  39.701  1.00 109.28 ?  105  GLN H NE2 1 
ATOM   6800 N N   . GLY C 2 121 ? -48.206 -4.504  35.987  1.00 94.14  ?  106  GLY H N   1 
ATOM   6801 C CA  . GLY C 2 121 ? -49.281 -3.535  36.015  1.00 85.93  ?  106  GLY H CA  1 
ATOM   6802 C C   . GLY C 2 121 ? -50.023 -3.530  37.338  1.00 100.55 ?  106  GLY H C   1 
ATOM   6803 O O   . GLY C 2 121 ? -50.109 -4.542  38.044  1.00 100.10 ?  106  GLY H O   1 
ATOM   6804 N N   . THR C 2 122 ? -50.567 -2.367  37.685  1.00 100.73 ?  107  THR H N   1 
ATOM   6805 C CA  . THR C 2 122 ? -51.410 -2.206  38.858  1.00 95.72  ?  107  THR H CA  1 
ATOM   6806 C C   . THR C 2 122 ? -52.690 -1.490  38.451  1.00 108.55 ?  107  THR H C   1 
ATOM   6807 O O   . THR C 2 122 ? -52.693 -0.664  37.534  1.00 107.18 ?  107  THR H O   1 
ATOM   6808 C CB  . THR C 2 122 ? -50.695 -1.427  39.975  1.00 98.59  ?  107  THR H CB  1 
ATOM   6809 O OG1 . THR C 2 122 ? -51.587 -1.242  41.081  1.00 96.48  ?  107  THR H OG1 1 
ATOM   6810 C CG2 . THR C 2 122 ? -50.223 -0.070  39.472  1.00 92.39  ?  107  THR H CG2 1 
ATOM   6811 N N   . THR C 2 123 ? -53.782 -1.818  39.136  1.00 111.03 ?  108  THR H N   1 
ATOM   6812 C CA  . THR C 2 123 ? -55.110 -1.340  38.776  1.00 107.99 ?  108  THR H CA  1 
ATOM   6813 C C   . THR C 2 123 ? -55.561 -0.267  39.757  1.00 109.82 ?  108  THR H C   1 
ATOM   6814 O O   . THR C 2 123 ? -55.479 -0.459  40.975  1.00 111.25 ?  108  THR H O   1 
ATOM   6815 C CB  . THR C 2 123 ? -56.119 -2.492  38.762  1.00 111.36 ?  108  THR H CB  1 
ATOM   6816 O OG1 . THR C 2 123 ? -55.576 -3.595  38.026  1.00 110.40 ?  108  THR H OG1 1 
ATOM   6817 C CG2 . THR C 2 123 ? -57.421 -2.051  38.112  1.00 107.98 ?  108  THR H CG2 1 
ATOM   6818 N N   . VAL C 2 124 ? -56.039 0.857   39.224  1.00 112.11 ?  109  VAL H N   1 
ATOM   6819 C CA  . VAL C 2 124 ? -56.604 1.930   40.034  1.00 119.75 ?  109  VAL H CA  1 
ATOM   6820 C C   . VAL C 2 124 ? -57.823 2.488   39.311  1.00 118.32 ?  109  VAL H C   1 
ATOM   6821 O O   . VAL C 2 124 ? -57.719 2.941   38.166  1.00 112.80 ?  109  VAL H O   1 
ATOM   6822 C CB  . VAL C 2 124 ? -55.588 3.048   40.332  1.00 109.55 ?  109  VAL H CB  1 
ATOM   6823 C CG1 . VAL C 2 124 ? -54.715 3.309   39.127  1.00 100.37 ?  109  VAL H CG1 1 
ATOM   6824 C CG2 . VAL C 2 124 ? -56.304 4.322   40.765  1.00 100.21 ?  109  VAL H CG2 1 
ATOM   6825 N N   . THR C 2 125 ? -58.975 2.446   39.974  1.00 126.92 ?  110  THR H N   1 
ATOM   6826 C CA  . THR C 2 125 ? -60.232 2.944   39.434  1.00 136.54 ?  110  THR H CA  1 
ATOM   6827 C C   . THR C 2 125 ? -60.815 3.961   40.405  1.00 131.48 ?  110  THR H C   1 
ATOM   6828 O O   . THR C 2 125 ? -60.863 3.712   41.614  1.00 128.50 ?  110  THR H O   1 
ATOM   6829 C CB  . THR C 2 125 ? -61.226 1.798   39.204  1.00 131.53 ?  110  THR H CB  1 
ATOM   6830 O OG1 . THR C 2 125 ? -60.729 0.925   38.182  1.00 130.43 ?  110  THR H OG1 1 
ATOM   6831 C CG2 . THR C 2 125 ? -62.589 2.338   38.791  1.00 130.81 ?  110  THR H CG2 1 
ATOM   6832 N N   . VAL C 2 126 ? -61.250 5.103   39.880  1.00 145.96 ?  111  VAL H N   1 
ATOM   6833 C CA  . VAL C 2 126 ? -61.841 6.168   40.683  1.00 149.45 ?  111  VAL H CA  1 
ATOM   6834 C C   . VAL C 2 126 ? -63.176 6.539   40.050  1.00 149.26 ?  111  VAL H C   1 
ATOM   6835 O O   . VAL C 2 126 ? -63.210 7.177   38.991  1.00 161.55 ?  111  VAL H O   1 
ATOM   6836 C CB  . VAL C 2 126 ? -60.925 7.394   40.791  1.00 152.83 ?  111  VAL H CB  1 
ATOM   6837 C CG1 . VAL C 2 126 ? -61.656 8.545   41.462  1.00 144.44 ?  111  VAL H CG1 1 
ATOM   6838 C CG2 . VAL C 2 126 ? -59.663 7.044   41.566  1.00 151.58 ?  111  VAL H CG2 1 
ATOM   6839 N N   . SER C 2 127 ? -64.272 6.140   40.694  1.00 138.67 ?  112  SER H N   1 
ATOM   6840 C CA  . SER C 2 127 ? -65.614 6.442   40.202  1.00 143.83 ?  112  SER H CA  1 
ATOM   6841 C C   . SER C 2 127 ? -66.585 6.313   41.363  1.00 148.63 ?  112  SER H C   1 
ATOM   6842 O O   . SER C 2 127 ? -66.634 5.263   42.012  1.00 149.35 ?  112  SER H O   1 
ATOM   6843 C CB  . SER C 2 127 ? -66.007 5.502   39.060  1.00 148.11 ?  112  SER H CB  1 
ATOM   6844 O OG  . SER C 2 127 ? -65.115 5.621   37.965  1.00 148.70 ?  112  SER H OG  1 
ATOM   6845 N N   . SER C 2 128 ? -67.350 7.367   41.626  1.00 157.09 ?  113  SER H N   1 
ATOM   6846 C CA  . SER C 2 128 ? -68.299 7.356   42.733  1.00 156.40 ?  113  SER H CA  1 
ATOM   6847 C C   . SER C 2 128 ? -69.571 8.121   42.382  1.00 152.51 ?  113  SER H C   1 
ATOM   6848 O O   . SER C 2 128 ? -69.513 9.248   41.890  1.00 158.10 ?  113  SER H O   1 
ATOM   6849 C CB  . SER C 2 128 ? -67.661 7.949   43.990  1.00 160.31 ?  113  SER H CB  1 
ATOM   6850 O OG  . SER C 2 128 ? -66.475 7.254   44.335  1.00 157.80 ?  113  SER H OG  1 
ATOM   6851 N N   . ASP D 2 149 ? -51.218 20.997  16.935  1.00 113.77 ?  1    ASP L N   1 
ATOM   6852 C CA  . ASP D 2 149 ? -51.108 19.795  17.753  1.00 116.23 ?  1    ASP L CA  1 
ATOM   6853 C C   . ASP D 2 149 ? -50.494 18.642  16.962  1.00 125.33 ?  1    ASP L C   1 
ATOM   6854 O O   . ASP D 2 149 ? -49.988 18.835  15.857  1.00 120.60 ?  1    ASP L O   1 
ATOM   6855 C CB  . ASP D 2 149 ? -52.472 19.397  18.298  1.00 116.23 ?  1    ASP L CB  1 
ATOM   6856 N N   . ILE D 2 150 ? -50.548 17.443  17.537  1.00 119.28 ?  2    ILE L N   1 
ATOM   6857 C CA  . ILE D 2 150 ? -49.941 16.255  16.942  1.00 114.72 ?  2    ILE L CA  1 
ATOM   6858 C C   . ILE D 2 150 ? -50.741 15.036  17.378  1.00 113.31 ?  2    ILE L C   1 
ATOM   6859 O O   . ILE D 2 150 ? -51.056 14.881  18.562  1.00 117.42 ?  2    ILE L O   1 
ATOM   6860 C CB  . ILE D 2 150 ? -48.456 16.119  17.341  1.00 117.95 ?  2    ILE L CB  1 
ATOM   6861 C CG1 . ILE D 2 150 ? -48.001 14.656  17.302  1.00 106.79 ?  2    ILE L CG1 1 
ATOM   6862 C CG2 . ILE D 2 150 ? -48.211 16.722  18.716  1.00 113.50 ?  2    ILE L CG2 1 
ATOM   6863 C CD1 . ILE D 2 150 ? -47.786 14.108  15.908  1.00 109.75 ?  2    ILE L CD1 1 
ATOM   6864 N N   . VAL D 2 151 ? -51.077 14.171  16.418  1.00 106.75 ?  3    VAL L N   1 
ATOM   6865 C CA  . VAL D 2 151 ? -51.809 12.940  16.695  1.00 119.19 ?  3    VAL L CA  1 
ATOM   6866 C C   . VAL D 2 151 ? -51.334 11.866  15.725  1.00 117.50 ?  3    VAL L C   1 
ATOM   6867 O O   . VAL D 2 151 ? -50.824 12.157  14.641  1.00 112.32 ?  3    VAL L O   1 
ATOM   6868 C CB  . VAL D 2 151 ? -53.343 13.140  16.592  1.00 116.08 ?  3    VAL L CB  1 
ATOM   6869 C CG1 . VAL D 2 151 ? -53.798 13.125  15.139  1.00 109.26 ?  3    VAL L CG1 1 
ATOM   6870 C CG2 . VAL D 2 151 ? -54.080 12.088  17.413  1.00 111.88 ?  3    VAL L CG2 1 
ATOM   6871 N N   . MET D 2 152 ? -51.489 10.609  16.134  1.00 113.12 ?  4    MET L N   1 
ATOM   6872 C CA  . MET D 2 152 ? -51.122 9.459   15.322  1.00 106.29 ?  4    MET L CA  1 
ATOM   6873 C C   . MET D 2 152 ? -52.382 8.763   14.826  1.00 103.52 ?  4    MET L C   1 
ATOM   6874 O O   . MET D 2 152 ? -53.353 8.610   15.574  1.00 107.98 ?  4    MET L O   1 
ATOM   6875 C CB  . MET D 2 152 ? -50.262 8.473   16.118  1.00 115.60 ?  4    MET L CB  1 
ATOM   6876 C CG  . MET D 2 152 ? -49.075 9.105   16.835  1.00 108.32 ?  4    MET L CG  1 
ATOM   6877 S SD  . MET D 2 152 ? -47.873 9.857   15.720  1.00 120.77 ?  4    MET L SD  1 
ATOM   6878 C CE  . MET D 2 152 ? -47.388 8.445   14.734  1.00 108.54 ?  4    MET L CE  1 
ATOM   6879 N N   . THR D 2 153 ? -52.362 8.338   13.564  1.00 106.35 ?  5    THR L N   1 
ATOM   6880 C CA  . THR D 2 153 ? -53.495 7.669   12.934  1.00 116.50 ?  5    THR L CA  1 
ATOM   6881 C C   . THR D 2 153 ? -53.066 6.280   12.486  1.00 107.76 ?  5    THR L C   1 
ATOM   6882 O O   . THR D 2 153 ? -52.130 6.143   11.691  1.00 109.05 ?  5    THR L O   1 
ATOM   6883 C CB  . THR D 2 153 ? -54.023 8.478   11.747  1.00 117.67 ?  5    THR L CB  1 
ATOM   6884 O OG1 . THR D 2 153 ? -54.559 9.725   12.210  1.00 106.60 ?  5    THR L OG1 1 
ATOM   6885 C CG2 . THR D 2 153 ? -55.106 7.705   11.014  1.00 110.46 ?  5    THR L CG2 1 
ATOM   6886 N N   . GLN D 2 154 ? -53.751 5.259   12.992  1.00 100.48 ?  6    GLN L N   1 
ATOM   6887 C CA  . GLN D 2 154 ? -53.494 3.874   12.623  1.00 112.29 ?  6    GLN L CA  1 
ATOM   6888 C C   . GLN D 2 154 ? -54.566 3.373   11.663  1.00 113.11 ?  6    GLN L C   1 
ATOM   6889 O O   . GLN D 2 154 ? -55.746 3.713   11.795  1.00 110.71 ?  6    GLN L O   1 
ATOM   6890 C CB  . GLN D 2 154 ? -53.448 2.980   13.863  1.00 110.09 ?  6    GLN L CB  1 
ATOM   6891 C CG  . GLN D 2 154 ? -52.121 2.988   14.585  1.00 108.06 ?  6    GLN L CG  1 
ATOM   6892 C CD  . GLN D 2 154 ? -52.204 2.361   15.959  1.00 110.27 ?  6    GLN L CD  1 
ATOM   6893 O OE1 . GLN D 2 154 ? -53.291 2.105   16.477  1.00 121.76 ?  6    GLN L OE1 1 
ATOM   6894 N NE2 . GLN D 2 154 ? -51.052 2.116   16.560  1.00 103.13 ?  6    GLN L NE2 1 
ATOM   6895 N N   . SER D 2 155 ? -54.145 2.569   10.690  1.00 117.47 ?  7    SER L N   1 
ATOM   6896 C CA  . SER D 2 155 ? -55.080 1.973   9.745   1.00 124.11 ?  7    SER L CA  1 
ATOM   6897 C C   . SER D 2 155 ? -55.405 0.559   10.225  1.00 129.91 ?  7    SER L C   1 
ATOM   6898 O O   . SER D 2 155 ? -54.842 0.125   11.239  1.00 130.79 ?  7    SER L O   1 
ATOM   6899 C CB  . SER D 2 155 ? -54.507 2.021   8.325   1.00 121.64 ?  7    SER L CB  1 
ATOM   6900 O OG  . SER D 2 155 ? -53.398 1.154   8.159   1.00 125.89 ?  7    SER L OG  1 
ATOM   6901 N N   . PRO D 2 156 ? -56.187 -0.234  9.461   1.00 133.51 ?  8    PRO L N   1 
ATOM   6902 C CA  . PRO D 2 156 ? -57.298 -0.987  10.066  1.00 137.41 ?  8    PRO L CA  1 
ATOM   6903 C C   . PRO D 2 156 ? -57.320 -1.054  11.587  1.00 129.04 ?  8    PRO L C   1 
ATOM   6904 O O   . PRO D 2 156 ? -56.426 -1.636  12.210  1.00 132.68 ?  8    PRO L O   1 
ATOM   6905 C CB  . PRO D 2 156 ? -57.137 -2.394  9.462   1.00 136.27 ?  8    PRO L CB  1 
ATOM   6906 C CG  . PRO D 2 156 ? -55.788 -2.423  8.825   1.00 130.07 ?  8    PRO L CG  1 
ATOM   6907 C CD  . PRO D 2 156 ? -55.626 -1.010  8.343   1.00 133.75 ?  8    PRO L CD  1 
ATOM   6908 N N   . LEU D 2 157 ? -58.367 -0.477  12.188  1.00 133.14 ?  9    LEU L N   1 
ATOM   6909 C CA  . LEU D 2 157 ? -58.609 -0.683  13.612  1.00 129.24 ?  9    LEU L CA  1 
ATOM   6910 C C   . LEU D 2 157 ? -58.670 -2.166  13.950  1.00 129.92 ?  9    LEU L C   1 
ATOM   6911 O O   . LEU D 2 157 ? -58.379 -2.559  15.085  1.00 133.25 ?  9    LEU L O   1 
ATOM   6912 C CB  . LEU D 2 157 ? -59.907 0.006   14.046  1.00 133.75 ?  9    LEU L CB  1 
ATOM   6913 C CG  . LEU D 2 157 ? -59.932 1.529   14.224  1.00 139.74 ?  9    LEU L CG  1 
ATOM   6914 C CD1 . LEU D 2 157 ? -60.057 2.243   12.886  1.00 131.97 ?  9    LEU L CD1 1 
ATOM   6915 C CD2 . LEU D 2 157 ? -61.057 1.944   15.164  1.00 142.13 ?  9    LEU L CD2 1 
ATOM   6916 N N   . SER D 2 158 ? -59.040 -3.000  12.978  1.00 125.64 ?  10   SER L N   1 
ATOM   6917 C CA  . SER D 2 158 ? -59.069 -4.447  13.133  1.00 127.10 ?  10   SER L CA  1 
ATOM   6918 C C   . SER D 2 158 ? -58.488 -5.088  11.882  1.00 128.23 ?  10   SER L C   1 
ATOM   6919 O O   . SER D 2 158 ? -58.883 -4.740  10.765  1.00 125.75 ?  10   SER L O   1 
ATOM   6920 C CB  . SER D 2 158 ? -60.496 -4.950  13.371  1.00 123.44 ?  10   SER L CB  1 
ATOM   6921 O OG  . SER D 2 158 ? -60.544 -6.365  13.346  1.00 123.52 ?  10   SER L OG  1 
ATOM   6922 N N   . LEU D 2 159 ? -57.555 -6.021  12.071  1.00 130.15 ?  11   LEU L N   1 
ATOM   6923 C CA  . LEU D 2 159 ? -56.903 -6.732  10.970  1.00 131.50 ?  11   LEU L CA  1 
ATOM   6924 C C   . LEU D 2 159 ? -57.002 -8.231  11.221  1.00 123.18 ?  11   LEU L C   1 
ATOM   6925 O O   . LEU D 2 159 ? -56.040 -8.862  11.680  1.00 123.79 ?  11   LEU L O   1 
ATOM   6926 C CB  . LEU D 2 159 ? -55.445 -6.294  10.816  1.00 116.05 ?  11   LEU L CB  1 
ATOM   6927 C CG  . LEU D 2 159 ? -54.705 -6.769  9.563   1.00 112.90 ?  11   LEU L CG  1 
ATOM   6928 C CD1 . LEU D 2 159 ? -55.309 -6.150  8.312   1.00 113.76 ?  11   LEU L CD1 1 
ATOM   6929 C CD2 . LEU D 2 159 ? -53.219 -6.454  9.658   1.00 108.83 ?  11   LEU L CD2 1 
ATOM   6930 N N   . PRO D 2 160 ? -58.153 -8.836  10.932  1.00 129.83 ?  12   PRO L N   1 
ATOM   6931 C CA  . PRO D 2 160 ? -58.277 -10.291 11.075  1.00 133.27 ?  12   PRO L CA  1 
ATOM   6932 C C   . PRO D 2 160 ? -57.680 -11.014 9.878   1.00 136.20 ?  12   PRO L C   1 
ATOM   6933 O O   . PRO D 2 160 ? -57.832 -10.588 8.730   1.00 130.48 ?  12   PRO L O   1 
ATOM   6934 C CB  . PRO D 2 160 ? -59.793 -10.505 11.156  1.00 124.51 ?  12   PRO L CB  1 
ATOM   6935 C CG  . PRO D 2 160 ? -60.357 -9.386  10.343  1.00 124.78 ?  12   PRO L CG  1 
ATOM   6936 C CD  . PRO D 2 160 ? -59.426 -8.208  10.534  1.00 132.42 ?  12   PRO L CD  1 
ATOM   6937 N N   . VAL D 2 161 ? -56.994 -12.122 10.156  1.00 139.11 ?  13   VAL L N   1 
ATOM   6938 C CA  . VAL D 2 161 ? -56.315 -12.885 9.114   1.00 149.93 ?  13   VAL L CA  1 
ATOM   6939 C C   . VAL D 2 161 ? -56.084 -14.301 9.625   1.00 154.68 ?  13   VAL L C   1 
ATOM   6940 O O   . VAL D 2 161 ? -56.148 -14.564 10.827  1.00 146.84 ?  13   VAL L O   1 
ATOM   6941 C CB  . VAL D 2 161 ? -54.985 -12.203 8.699   1.00 145.71 ?  13   VAL L CB  1 
ATOM   6942 C CG1 . VAL D 2 161 ? -53.881 -12.522 9.697   1.00 141.14 ?  13   VAL L CG1 1 
ATOM   6943 C CG2 . VAL D 2 161 ? -54.587 -12.603 7.282   1.00 149.78 ?  13   VAL L CG2 1 
ATOM   6944 N N   . THR D 2 162 ? -55.821 -15.218 8.700   1.00 162.87 ?  14   THR L N   1 
ATOM   6945 C CA  . THR D 2 162 ? -55.528 -16.609 9.014   1.00 176.01 ?  14   THR L CA  1 
ATOM   6946 C C   . THR D 2 162 ? -54.089 -16.730 9.513   1.00 181.56 ?  14   THR L C   1 
ATOM   6947 O O   . THR D 2 162 ? -53.339 -15.753 9.521   1.00 185.18 ?  14   THR L O   1 
ATOM   6948 C CB  . THR D 2 162 ? -55.797 -17.466 7.774   1.00 173.32 ?  14   THR L CB  1 
ATOM   6949 O OG1 . THR D 2 162 ? -54.710 -18.369 7.539   1.00 170.30 ?  14   THR L OG1 1 
ATOM   6950 C CG2 . THR D 2 162 ? -55.993 -16.586 6.546   1.00 171.89 ?  14   THR L CG2 1 
ATOM   6951 N N   . PRO D 2 163 ? -53.679 -17.913 10.002  1.00 165.54 ?  15   PRO L N   1 
ATOM   6952 C CA  . PRO D 2 163 ? -52.265 -18.092 10.370  1.00 158.71 ?  15   PRO L CA  1 
ATOM   6953 C C   . PRO D 2 163 ? -51.379 -18.510 9.203   1.00 151.54 ?  15   PRO L C   1 
ATOM   6954 O O   . PRO D 2 163 ? -51.585 -19.575 8.613   1.00 135.14 ?  15   PRO L O   1 
ATOM   6955 C CB  . PRO D 2 163 ? -52.314 -19.191 11.443  1.00 150.25 ?  15   PRO L CB  1 
ATOM   6956 C CG  . PRO D 2 163 ? -53.760 -19.326 11.825  1.00 147.81 ?  15   PRO L CG  1 
ATOM   6957 C CD  . PRO D 2 163 ? -54.527 -18.955 10.605  1.00 151.24 ?  15   PRO L CD  1 
ATOM   6958 N N   . GLY D 2 164 ? -50.386 -17.685 8.868   1.00 152.41 ?  16   GLY L N   1 
ATOM   6959 C CA  . GLY D 2 164 ? -49.386 -18.062 7.885   1.00 140.81 ?  16   GLY L CA  1 
ATOM   6960 C C   . GLY D 2 164 ? -49.348 -17.209 6.632   1.00 140.38 ?  16   GLY L C   1 
ATOM   6961 O O   . GLY D 2 164 ? -48.972 -17.694 5.561   1.00 133.92 ?  16   GLY L O   1 
ATOM   6962 N N   . GLU D 2 165 ? -49.723 -15.943 6.749   1.00 163.06 ?  17   GLU L N   1 
ATOM   6963 C CA  . GLU D 2 165 ? -49.823 -15.014 5.632   1.00 160.66 ?  17   GLU L CA  1 
ATOM   6964 C C   . GLU D 2 165 ? -49.179 -13.698 6.025   1.00 153.00 ?  17   GLU L C   1 
ATOM   6965 O O   . GLU D 2 165 ? -48.864 -13.473 7.197   1.00 148.05 ?  17   GLU L O   1 
ATOM   6966 C CB  . GLU D 2 165 ? -51.294 -14.786 5.234   1.00 159.14 ?  17   GLU L CB  1 
ATOM   6967 C CG  . GLU D 2 165 ? -52.110 -16.050 5.016   1.00 165.90 ?  17   GLU L CG  1 
ATOM   6968 C CD  . GLU D 2 165 ? -52.512 -16.697 6.320   1.00 176.75 ?  17   GLU L CD  1 
ATOM   6969 O OE1 . GLU D 2 165 ? -52.891 -17.887 6.318   1.00 184.74 ?  17   GLU L OE1 1 
ATOM   6970 O OE2 . GLU D 2 165 ? -52.425 -16.006 7.354   1.00 173.20 -1 17   GLU L OE2 1 
ATOM   6971 N N   . PRO D 2 166 ? -48.946 -12.805 5.064   1.00 140.47 ?  18   PRO L N   1 
ATOM   6972 C CA  . PRO D 2 166 ? -48.451 -11.471 5.414   1.00 138.64 ?  18   PRO L CA  1 
ATOM   6973 C C   . PRO D 2 166 ? -49.543 -10.591 6.001   1.00 134.80 ?  18   PRO L C   1 
ATOM   6974 O O   . PRO D 2 166 ? -50.736 -10.775 5.749   1.00 127.48 ?  18   PRO L O   1 
ATOM   6975 C CB  . PRO D 2 166 ? -47.961 -10.914 4.072   1.00 129.74 ?  18   PRO L CB  1 
ATOM   6976 C CG  . PRO D 2 166 ? -48.764 -11.639 3.055   1.00 136.79 ?  18   PRO L CG  1 
ATOM   6977 C CD  . PRO D 2 166 ? -48.928 -13.025 3.606   1.00 138.86 ?  18   PRO L CD  1 
ATOM   6978 N N   . ALA D 2 167 ? -49.108 -9.621  6.802   1.00 130.79 ?  19   ALA L N   1 
ATOM   6979 C CA  . ALA D 2 167 ? -49.996 -8.627  7.385   1.00 115.68 ?  19   ALA L CA  1 
ATOM   6980 C C   . ALA D 2 167 ? -49.285 -7.283  7.404   1.00 108.88 ?  19   ALA L C   1 
ATOM   6981 O O   . ALA D 2 167 ? -48.059 -7.216  7.519   1.00 111.66 ?  19   ALA L O   1 
ATOM   6982 C CB  . ALA D 2 167 ? -50.437 -9.014  8.803   1.00 116.36 ?  19   ALA L CB  1 
ATOM   6983 N N   . SER D 2 168 ? -50.067 -6.212  7.289   1.00 121.97 ?  20   SER L N   1 
ATOM   6984 C CA  . SER D 2 168 ? -49.520 -4.864  7.233   1.00 108.57 ?  20   SER L CA  1 
ATOM   6985 C C   . SER D 2 168 ? -50.321 -3.941  8.137   1.00 107.63 ?  20   SER L C   1 
ATOM   6986 O O   . SER D 2 168 ? -51.554 -4.003  8.169   1.00 123.00 ?  20   SER L O   1 
ATOM   6987 C CB  . SER D 2 168 ? -49.520 -4.319  5.799   1.00 105.61 ?  20   SER L CB  1 
ATOM   6988 O OG  . SER D 2 168 ? -48.629 -5.051  4.975   1.00 106.68 ?  20   SER L OG  1 
ATOM   6989 N N   . ILE D 2 169 ? -49.609 -3.086  8.867   1.00 102.12 ?  21   ILE L N   1 
ATOM   6990 C CA  . ILE D 2 169 ? -50.206 -2.085  9.741   1.00 102.13 ?  21   ILE L CA  1 
ATOM   6991 C C   . ILE D 2 169 ? -49.547 -0.747  9.441   1.00 107.66 ?  21   ILE L C   1 
ATOM   6992 O O   . ILE D 2 169 ? -48.315 -0.651  9.417   1.00 113.06 ?  21   ILE L O   1 
ATOM   6993 C CB  . ILE D 2 169 ? -50.039 -2.448  11.229  1.00 105.19 ?  21   ILE L CB  1 
ATOM   6994 C CG1 . ILE D 2 169 ? -50.820 -3.720  11.562  1.00 115.12 ?  21   ILE L CG1 1 
ATOM   6995 C CG2 . ILE D 2 169 ? -50.478 -1.293  12.117  1.00 113.80 ?  21   ILE L CG2 1 
ATOM   6996 C CD1 . ILE D 2 169 ? -50.636 -4.189  12.986  1.00 106.98 ?  21   ILE L CD1 1 
ATOM   6997 N N   . SER D 2 170 ? -50.360 0.278   9.209   1.00 113.16 ?  22   SER L N   1 
ATOM   6998 C CA  . SER D 2 170 ? -49.862 1.613   8.922   1.00 113.43 ?  22   SER L CA  1 
ATOM   6999 C C   . SER D 2 170 ? -50.077 2.529   10.119  1.00 108.81 ?  22   SER L C   1 
ATOM   7000 O O   . SER D 2 170 ? -50.985 2.324   10.930  1.00 111.88 ?  22   SER L O   1 
ATOM   7001 C CB  . SER D 2 170 ? -50.543 2.211   7.686   1.00 109.81 ?  22   SER L CB  1 
ATOM   7002 O OG  . SER D 2 170 ? -50.249 1.456   6.524   1.00 114.56 ?  22   SER L OG  1 
ATOM   7003 N N   . CYS D 2 171 ? -49.224 3.545   10.216  1.00 106.78 ?  23   CYS L N   1 
ATOM   7004 C CA  . CYS D 2 171 ? -49.305 4.526   11.291  1.00 112.96 ?  23   CYS L CA  1 
ATOM   7005 C C   . CYS D 2 171 ? -48.822 5.859   10.745  1.00 110.75 ?  23   CYS L C   1 
ATOM   7006 O O   . CYS D 2 171 ? -47.658 5.986   10.353  1.00 109.98 ?  23   CYS L O   1 
ATOM   7007 C CB  . CYS D 2 171 ? -48.474 4.087   12.499  1.00 110.61 ?  23   CYS L CB  1 
ATOM   7008 S SG  . CYS D 2 171 ? -48.535 5.198   13.923  1.00 112.94 ?  23   CYS L SG  1 
ATOM   7009 N N   . ARG D 2 172 ? -49.717 6.843   10.708  1.00 113.77 ?  24   ARG L N   1 
ATOM   7010 C CA  . ARG D 2 172 ? -49.457 8.130   10.083  1.00 114.23 ?  24   ARG L CA  1 
ATOM   7011 C C   . ARG D 2 172 ? -49.524 9.237   11.126  1.00 110.47 ?  24   ARG L C   1 
ATOM   7012 O O   . ARG D 2 172 ? -50.433 9.262   11.961  1.00 113.69 ?  24   ARG L O   1 
ATOM   7013 C CB  . ARG D 2 172 ? -50.463 8.398   8.959   1.00 119.61 ?  24   ARG L CB  1 
ATOM   7014 C CG  . ARG D 2 172 ? -50.556 7.269   7.945   1.00 126.27 ?  24   ARG L CG  1 
ATOM   7015 C CD  . ARG D 2 172 ? -51.705 7.480   6.974   1.00 148.74 ?  24   ARG L CD  1 
ATOM   7016 N NE  . ARG D 2 172 ? -51.260 7.397   5.587   1.00 155.85 ?  24   ARG L NE  1 
ATOM   7017 C CZ  . ARG D 2 172 ? -50.892 8.445   4.860   1.00 153.70 ?  24   ARG L CZ  1 
ATOM   7018 N NH1 . ARG D 2 172 ? -50.923 9.662   5.387   1.00 151.51 1  24   ARG L NH1 1 
ATOM   7019 N NH2 . ARG D 2 172 ? -50.496 8.279   3.605   1.00 152.58 ?  24   ARG L NH2 1 
ATOM   7020 N N   . SER D 2 173 ? -48.558 10.150  11.073  1.00 105.94 ?  25   SER L N   1 
ATOM   7021 C CA  . SER D 2 173 ? -48.434 11.224  12.045  1.00 106.51 ?  25   SER L CA  1 
ATOM   7022 C C   . SER D 2 173 ? -48.883 12.550  11.445  1.00 106.95 ?  25   SER L C   1 
ATOM   7023 O O   . SER D 2 173 ? -48.887 12.740  10.226  1.00 107.12 ?  25   SER L O   1 
ATOM   7024 C CB  . SER D 2 173 ? -46.990 11.347  12.548  1.00 105.08 ?  25   SER L CB  1 
ATOM   7025 O OG  . SER D 2 173 ? -46.126 11.793  11.518  1.00 117.51 ?  25   SER L OG  1 
ATOM   7026 N N   . SER D 2 174 ? -49.263 13.473  12.332  1.00 113.10 ?  26   SER L N   1 
ATOM   7027 C CA  . SER D 2 174 ? -49.658 14.807  11.892  1.00 113.45 ?  26   SER L CA  1 
ATOM   7028 C C   . SER D 2 174 ? -48.456 15.598  11.394  1.00 112.24 ?  26   SER L C   1 
ATOM   7029 O O   . SER D 2 174 ? -48.540 16.293  10.374  1.00 105.32 ?  26   SER L O   1 
ATOM   7030 C CB  . SER D 2 174 ? -50.348 15.551  13.034  1.00 110.04 ?  26   SER L CB  1 
ATOM   7031 O OG  . SER D 2 174 ? -50.956 14.646  13.939  1.00 117.71 ?  26   SER L OG  1 
ATOM   7032 N N   . GLN D 2 175 ? -47.335 15.507  12.101  1.00 112.17 ?  27   GLN L N   1 
ATOM   7033 C CA  . GLN D 2 175 ? -46.102 16.190  11.745  1.00 103.66 ?  27   GLN L CA  1 
ATOM   7034 C C   . GLN D 2 175 ? -44.978 15.171  11.596  1.00 104.10 ?  27   GLN L C   1 
ATOM   7035 O O   . GLN D 2 175 ? -45.122 13.996  11.941  1.00 111.43 ?  27   GLN L O   1 
ATOM   7036 C CB  . GLN D 2 175 ? -45.745 17.253  12.791  1.00 104.03 ?  27   GLN L CB  1 
ATOM   7037 C CG  . GLN D 2 175 ? -45.864 16.775  14.229  1.00 108.88 ?  27   GLN L CG  1 
ATOM   7038 C CD  . GLN D 2 175 ? -45.809 17.914  15.229  1.00 120.35 ?  27   GLN L CD  1 
ATOM   7039 O OE1 . GLN D 2 175 ? -46.022 19.075  14.878  1.00 124.69 ?  27   GLN L OE1 1 
ATOM   7040 N NE2 . GLN D 2 175 ? -45.519 17.587  16.483  1.00 113.55 ?  27   GLN L NE2 1 
ATOM   7041 N N   . SER D 2 176 A -43.848 15.639  11.073  1.00 105.08 ?  27   SER L N   1 
ATOM   7042 C CA  . SER D 2 176 A -42.745 14.742  10.753  1.00 96.28  ?  27   SER L CA  1 
ATOM   7043 C C   . SER D 2 176 A -42.079 14.220  12.021  1.00 98.24  ?  27   SER L C   1 
ATOM   7044 O O   . SER D 2 176 A -41.859 14.964  12.981  1.00 102.76 ?  27   SER L O   1 
ATOM   7045 C CB  . SER D 2 176 A -41.719 15.459  9.876   1.00 95.54  ?  27   SER L CB  1 
ATOM   7046 O OG  . SER D 2 176 A -40.740 14.555  9.395   1.00 106.16 ?  27   SER L OG  1 
ATOM   7047 N N   . LEU D 2 177 B -41.761 12.927  12.018  1.00 96.28  ?  27   LEU L N   1 
ATOM   7048 C CA  . LEU D 2 177 B -41.071 12.280  13.124  1.00 93.66  ?  27   LEU L CA  1 
ATOM   7049 C C   . LEU D 2 177 B -39.586 12.077  12.849  1.00 96.49  ?  27   LEU L C   1 
ATOM   7050 O O   . LEU D 2 177 B -38.900 11.433  13.648  1.00 97.28  ?  27   LEU L O   1 
ATOM   7051 C CB  . LEU D 2 177 B -41.730 10.937  13.447  1.00 91.78  ?  27   LEU L CB  1 
ATOM   7052 C CG  . LEU D 2 177 B -43.164 10.983  13.978  1.00 97.83  ?  27   LEU L CG  1 
ATOM   7053 C CD1 . LEU D 2 177 B -43.665 9.582   14.297  1.00 84.20  ?  27   LEU L CD1 1 
ATOM   7054 C CD2 . LEU D 2 177 B -43.257 11.880  15.202  1.00 94.62  ?  27   LEU L CD2 1 
ATOM   7055 N N   . LEU D 2 178 C -39.078 12.606  11.738  1.00 94.75  ?  27   LEU L N   1 
ATOM   7056 C CA  . LEU D 2 178 C -37.666 12.478  11.394  1.00 91.87  ?  27   LEU L CA  1 
ATOM   7057 C C   . LEU D 2 178 C -36.872 13.482  12.222  1.00 89.16  ?  27   LEU L C   1 
ATOM   7058 O O   . LEU D 2 178 C -37.016 14.696  12.045  1.00 95.53  ?  27   LEU L O   1 
ATOM   7059 C CB  . LEU D 2 178 C -37.464 12.701  9.897   1.00 97.79  ?  27   LEU L CB  1 
ATOM   7060 C CG  . LEU D 2 178 C -36.227 12.106  9.213   1.00 94.95  ?  27   LEU L CG  1 
ATOM   7061 C CD1 . LEU D 2 178 C -34.965 12.899  9.521   1.00 99.79  ?  27   LEU L CD1 1 
ATOM   7062 C CD2 . LEU D 2 178 C -36.049 10.646  9.602   1.00 90.49  ?  27   LEU L CD2 1 
ATOM   7063 N N   . HIS D 2 179 D -36.036 12.980  13.125  1.00 91.70  ?  27   HIS L N   1 
ATOM   7064 C CA  . HIS D 2 179 D -35.259 13.844  13.998  1.00 90.70  ?  27   HIS L CA  1 
ATOM   7065 C C   . HIS D 2 179 D -33.987 14.314  13.297  1.00 80.73  ?  27   HIS L C   1 
ATOM   7066 O O   . HIS D 2 179 D -33.525 13.718  12.321  1.00 80.82  ?  27   HIS L O   1 
ATOM   7067 C CB  . HIS D 2 179 D -34.910 13.118  15.298  1.00 84.38  ?  27   HIS L CB  1 
ATOM   7068 C CG  . HIS D 2 179 D -34.476 14.029  16.404  1.00 83.00  ?  27   HIS L CG  1 
ATOM   7069 N ND1 . HIS D 2 179 D -33.158 14.372  16.614  1.00 78.38  ?  27   HIS L ND1 1 
ATOM   7070 C CD2 . HIS D 2 179 D -35.188 14.669  17.362  1.00 76.55  ?  27   HIS L CD2 1 
ATOM   7071 C CE1 . HIS D 2 179 D -33.076 15.184  17.652  1.00 78.20  ?  27   HIS L CE1 1 
ATOM   7072 N NE2 . HIS D 2 179 D -34.294 15.380  18.125  1.00 80.53  ?  27   HIS L NE2 1 
ATOM   7073 N N   . THR D 2 180 E -33.419 15.407  13.817  1.00 81.33  ?  27   THR L N   1 
ATOM   7074 C CA  . THR D 2 180 E -32.193 15.953  13.243  1.00 82.44  ?  27   THR L CA  1 
ATOM   7075 C C   . THR D 2 180 E -31.040 14.961  13.337  1.00 78.64  ?  27   THR L C   1 
ATOM   7076 O O   . THR D 2 180 E -30.123 14.993  12.508  1.00 81.69  ?  27   THR L O   1 
ATOM   7077 C CB  . THR D 2 180 E -31.824 17.264  13.942  1.00 81.96  ?  27   THR L CB  1 
ATOM   7078 O OG1 . THR D 2 180 E -33.002 18.061  14.119  1.00 88.76  ?  27   THR L OG1 1 
ATOM   7079 C CG2 . THR D 2 180 E -30.817 18.049  13.111  1.00 84.98  ?  27   THR L CG2 1 
ATOM   7080 N N   . TYR D 2 181 ? -31.070 14.070  14.331  1.00 83.10  ?  28   TYR L N   1 
ATOM   7081 C CA  . TYR D 2 181 ? -30.037 13.047  14.446  1.00 81.49  ?  28   TYR L CA  1 
ATOM   7082 C C   . TYR D 2 181 ? -30.121 12.011  13.333  1.00 81.04  ?  28   TYR L C   1 
ATOM   7083 O O   . TYR D 2 181 ? -29.157 11.267  13.123  1.00 88.28  ?  28   TYR L O   1 
ATOM   7084 C CB  . TYR D 2 181 ? -30.129 12.349  15.805  1.00 70.28  ?  28   TYR L CB  1 
ATOM   7085 C CG  . TYR D 2 181 ? -29.851 13.249  16.988  1.00 70.82  ?  28   TYR L CG  1 
ATOM   7086 C CD1 . TYR D 2 181 ? -29.175 14.452  16.830  1.00 79.93  ?  28   TYR L CD1 1 
ATOM   7087 C CD2 . TYR D 2 181 ? -30.263 12.892  18.266  1.00 67.64  ?  28   TYR L CD2 1 
ATOM   7088 C CE1 . TYR D 2 181 ? -28.920 15.276  17.910  1.00 70.34  ?  28   TYR L CE1 1 
ATOM   7089 C CE2 . TYR D 2 181 ? -30.011 13.708  19.352  1.00 76.15  ?  28   TYR L CE2 1 
ATOM   7090 C CZ  . TYR D 2 181 ? -29.340 14.898  19.168  1.00 81.17  ?  28   TYR L CZ  1 
ATOM   7091 O OH  . TYR D 2 181 ? -29.088 15.714  20.248  1.00 85.71  ?  28   TYR L OH  1 
ATOM   7092 N N   . GLY D 2 182 ? -31.242 11.943  12.622  1.00 78.58  ?  29   GLY L N   1 
ATOM   7093 C CA  . GLY D 2 182 ? -31.410 10.996  11.541  1.00 86.22  ?  29   GLY L CA  1 
ATOM   7094 C C   . GLY D 2 182 ? -32.222 9.764   11.870  1.00 83.98  ?  29   GLY L C   1 
ATOM   7095 O O   . GLY D 2 182 ? -32.214 8.813   11.079  1.00 101.01 ?  29   GLY L O   1 
ATOM   7096 N N   . TYR D 2 183 ? -32.919 9.746   13.003  1.00 78.87  ?  30   TYR L N   1 
ATOM   7097 C CA  . TYR D 2 183 ? -33.749 8.621   13.407  1.00 87.54  ?  30   TYR L CA  1 
ATOM   7098 C C   . TYR D 2 183 ? -35.219 9.016   13.371  1.00 90.54  ?  30   TYR L C   1 
ATOM   7099 O O   . TYR D 2 183 ? -35.580 10.138  13.738  1.00 101.53 ?  30   TYR L O   1 
ATOM   7100 C CB  . TYR D 2 183 ? -33.387 8.139   14.816  1.00 79.40  ?  30   TYR L CB  1 
ATOM   7101 C CG  . TYR D 2 183 ? -31.994 7.568   14.952  1.00 87.78  ?  30   TYR L CG  1 
ATOM   7102 C CD1 . TYR D 2 183 ? -31.734 6.240   14.639  1.00 85.97  ?  30   TYR L CD1 1 
ATOM   7103 C CD2 . TYR D 2 183 ? -30.943 8.351   15.409  1.00 80.68  ?  30   TYR L CD2 1 
ATOM   7104 C CE1 . TYR D 2 183 ? -30.464 5.711   14.768  1.00 74.80  ?  30   TYR L CE1 1 
ATOM   7105 C CE2 . TYR D 2 183 ? -29.669 7.831   15.542  1.00 74.86  ?  30   TYR L CE2 1 
ATOM   7106 C CZ  . TYR D 2 183 ? -29.435 6.511   15.220  1.00 75.94  ?  30   TYR L CZ  1 
ATOM   7107 O OH  . TYR D 2 183 ? -28.168 5.992   15.350  1.00 76.80  ?  30   TYR L OH  1 
ATOM   7108 N N   . ASN D 2 184 ? -36.061 8.087   12.923  1.00 82.63  ?  31   ASN L N   1 
ATOM   7109 C CA  . ASN D 2 184 ? -37.507 8.256   13.004  1.00 84.98  ?  31   ASN L CA  1 
ATOM   7110 C C   . ASN D 2 184 ? -37.944 7.899   14.419  1.00 84.45  ?  31   ASN L C   1 
ATOM   7111 O O   . ASN D 2 184 ? -37.847 6.739   14.831  1.00 88.03  ?  31   ASN L O   1 
ATOM   7112 C CB  . ASN D 2 184 ? -38.213 7.382   11.970  1.00 88.70  ?  31   ASN L CB  1 
ATOM   7113 C CG  . ASN D 2 184 ? -37.961 7.841   10.546  1.00 100.26 ?  31   ASN L CG  1 
ATOM   7114 O OD1 . ASN D 2 184 ? -38.635 8.740   10.042  1.00 104.72 ?  31   ASN L OD1 1 
ATOM   7115 N ND2 . ASN D 2 184 ? -36.996 7.213   9.885   1.00 96.02  ?  31   ASN L ND2 1 
ATOM   7116 N N   . CYS D 2 185 ? -38.429 8.889   15.168  1.00 83.55  ?  32   CYS L N   1 
ATOM   7117 C CA  . CYS D 2 185 ? -38.781 8.689   16.573  1.00 80.74  ?  32   CYS L CA  1 
ATOM   7118 C C   . CYS D 2 185 ? -40.162 8.037   16.668  1.00 82.88  ?  32   CYS L C   1 
ATOM   7119 O O   . CYS D 2 185 ? -41.167 8.657   17.019  1.00 82.43  ?  32   CYS L O   1 
ATOM   7120 C CB  . CYS D 2 185 ? -38.723 10.009  17.327  1.00 72.95  ?  32   CYS L CB  1 
ATOM   7121 S SG  . CYS D 2 185 ? -37.081 10.768  17.360  1.00 86.42  ?  32   CYS L SG  1 
ATOM   7122 N N   . LEU D 2 186 ? -40.193 6.745   16.349  1.00 87.01  ?  33   LEU L N   1 
ATOM   7123 C CA  . LEU D 2 186 ? -41.423 5.969   16.413  1.00 82.53  ?  33   LEU L CA  1 
ATOM   7124 C C   . LEU D 2 186 ? -41.098 4.541   16.827  1.00 80.15  ?  33   LEU L C   1 
ATOM   7125 O O   . LEU D 2 186 ? -40.145 3.944   16.318  1.00 81.91  ?  33   LEU L O   1 
ATOM   7126 C CB  . LEU D 2 186 ? -42.157 5.964   15.068  1.00 84.12  ?  33   LEU L CB  1 
ATOM   7127 C CG  . LEU D 2 186 ? -43.460 5.163   15.052  1.00 98.09  ?  33   LEU L CG  1 
ATOM   7128 C CD1 . LEU D 2 186 ? -44.650 6.053   15.381  1.00 101.01 ?  33   LEU L CD1 1 
ATOM   7129 C CD2 . LEU D 2 186 ? -43.651 4.460   13.721  1.00 97.56  ?  33   LEU L CD2 1 
ATOM   7130 N N   . ASP D 2 187 ? -41.893 4.000   17.745  1.00 75.42  ?  34   ASP L N   1 
ATOM   7131 C CA  . ASP D 2 187 ? -41.758 2.623   18.195  1.00 76.59  ?  34   ASP L CA  1 
ATOM   7132 C C   . ASP D 2 187 ? -43.005 1.835   17.816  1.00 81.96  ?  34   ASP L C   1 
ATOM   7133 O O   . ASP D 2 187 ? -44.036 2.397   17.439  1.00 83.58  ?  34   ASP L O   1 
ATOM   7134 C CB  . ASP D 2 187 ? -41.528 2.550   19.710  1.00 78.79  ?  34   ASP L CB  1 
ATOM   7135 C CG  . ASP D 2 187 ? -40.286 3.296   20.148  1.00 83.94  ?  34   ASP L CG  1 
ATOM   7136 O OD1 . ASP D 2 187 ? -39.396 3.517   19.300  1.00 88.23  ?  34   ASP L OD1 1 
ATOM   7137 O OD2 . ASP D 2 187 ? -40.198 3.657   21.340  1.00 94.80  -1 34   ASP L OD2 1 
ATOM   7138 N N   . TRP D 2 188 ? -42.899 0.511   17.919  1.00 92.05  ?  35   TRP L N   1 
ATOM   7139 C CA  . TRP D 2 188 ? -44.018 -0.392  17.682  1.00 87.34  ?  35   TRP L CA  1 
ATOM   7140 C C   . TRP D 2 188 ? -44.139 -1.327  18.873  1.00 86.45  ?  35   TRP L C   1 
ATOM   7141 O O   . TRP D 2 188 ? -43.168 -1.997  19.240  1.00 82.05  ?  35   TRP L O   1 
ATOM   7142 C CB  . TRP D 2 188 ? -43.832 -1.190  16.389  1.00 91.65  ?  35   TRP L CB  1 
ATOM   7143 C CG  . TRP D 2 188 ? -44.144 -0.416  15.147  1.00 85.32  ?  35   TRP L CG  1 
ATOM   7144 C CD1 . TRP D 2 188 ? -43.249 0.144   14.281  1.00 87.53  ?  35   TRP L CD1 1 
ATOM   7145 C CD2 . TRP D 2 188 ? -45.445 -0.118  14.627  1.00 88.97  ?  35   TRP L CD2 1 
ATOM   7146 N NE1 . TRP D 2 188 ? -43.913 0.771   13.255  1.00 93.72  ?  35   TRP L NE1 1 
ATOM   7147 C CE2 . TRP D 2 188 ? -45.262 0.625   13.444  1.00 92.92  ?  35   TRP L CE2 1 
ATOM   7148 C CE3 . TRP D 2 188 ? -46.747 -0.408  15.048  1.00 94.00  ?  35   TRP L CE3 1 
ATOM   7149 C CZ2 . TRP D 2 188 ? -46.333 1.081   12.678  1.00 94.44  ?  35   TRP L CZ2 1 
ATOM   7150 C CZ3 . TRP D 2 188 ? -47.807 0.046   14.286  1.00 88.75  ?  35   TRP L CZ3 1 
ATOM   7151 C CH2 . TRP D 2 188 ? -47.594 0.781   13.114  1.00 96.41  ?  35   TRP L CH2 1 
ATOM   7152 N N   . TYR D 2 189 ? -45.325 -1.373  19.474  1.00 86.08  ?  36   TYR L N   1 
ATOM   7153 C CA  . TYR D 2 189 ? -45.570 -2.196  20.648  1.00 83.93  ?  36   TYR L CA  1 
ATOM   7154 C C   . TYR D 2 189 ? -46.687 -3.195  20.375  1.00 95.80  ?  36   TYR L C   1 
ATOM   7155 O O   . TYR D 2 189 ? -47.543 -2.979  19.512  1.00 106.08 ?  36   TYR L O   1 
ATOM   7156 C CB  . TYR D 2 189 ? -45.927 -1.339  21.867  1.00 81.69  ?  36   TYR L CB  1 
ATOM   7157 C CG  . TYR D 2 189 ? -44.794 -0.460  22.341  1.00 80.73  ?  36   TYR L CG  1 
ATOM   7158 C CD1 . TYR D 2 189 ? -43.821 -0.953  23.199  1.00 80.53  ?  36   TYR L CD1 1 
ATOM   7159 C CD2 . TYR D 2 189 ? -44.697 0.862   21.930  1.00 76.12  ?  36   TYR L CD2 1 
ATOM   7160 C CE1 . TYR D 2 189 ? -42.784 -0.155  23.635  1.00 83.02  ?  36   TYR L CE1 1 
ATOM   7161 C CE2 . TYR D 2 189 ? -43.664 1.669   22.361  1.00 82.23  ?  36   TYR L CE2 1 
ATOM   7162 C CZ  . TYR D 2 189 ? -42.709 1.156   23.212  1.00 82.64  ?  36   TYR L CZ  1 
ATOM   7163 O OH  . TYR D 2 189 ? -41.676 1.956   23.645  1.00 83.41  ?  36   TYR L OH  1 
ATOM   7164 N N   . LEU D 2 190 ? -46.661 -4.295  21.125  1.00 96.22  ?  37   LEU L N   1 
ATOM   7165 C CA  . LEU D 2 190 ? -47.646 -5.361  21.016  1.00 95.76  ?  37   LEU L CA  1 
ATOM   7166 C C   . LEU D 2 190 ? -48.140 -5.716  22.408  1.00 99.41  ?  37   LEU L C   1 
ATOM   7167 O O   . LEU D 2 190 ? -47.336 -5.871  23.332  1.00 103.96 ?  37   LEU L O   1 
ATOM   7168 C CB  . LEU D 2 190 ? -47.050 -6.600  20.336  1.00 97.84  ?  37   LEU L CB  1 
ATOM   7169 C CG  . LEU D 2 190 ? -47.763 -7.941  20.527  1.00 101.20 ?  37   LEU L CG  1 
ATOM   7170 C CD1 . LEU D 2 190 ? -49.134 -7.949  19.859  1.00 100.12 ?  37   LEU L CD1 1 
ATOM   7171 C CD2 . LEU D 2 190 ? -46.898 -9.080  20.005  1.00 110.37 ?  37   LEU L CD2 1 
ATOM   7172 N N   . GLN D 2 191 ? -49.456 -5.846  22.560  1.00 103.93 ?  38   GLN L N   1 
ATOM   7173 C CA  . GLN D 2 191 ? -50.060 -6.207  23.838  1.00 104.92 ?  38   GLN L CA  1 
ATOM   7174 C C   . GLN D 2 191 ? -50.896 -7.465  23.645  1.00 102.89 ?  38   GLN L C   1 
ATOM   7175 O O   . GLN D 2 191 ? -51.941 -7.427  22.987  1.00 104.31 ?  38   GLN L O   1 
ATOM   7176 C CB  . GLN D 2 191 ? -50.906 -5.066  24.398  1.00 97.85  ?  38   GLN L CB  1 
ATOM   7177 C CG  . GLN D 2 191 ? -51.409 -5.323  25.811  1.00 98.29  ?  38   GLN L CG  1 
ATOM   7178 C CD  . GLN D 2 191 ? -52.304 -4.218  26.331  1.00 94.22  ?  38   GLN L CD  1 
ATOM   7179 O OE1 . GLN D 2 191 ? -52.908 -3.475  25.558  1.00 109.34 ?  38   GLN L OE1 1 
ATOM   7180 N NE2 . GLN D 2 191 ? -52.394 -4.104  27.651  1.00 95.44  ?  38   GLN L NE2 1 
ATOM   7181 N N   . ARG D 2 192 ? -50.433 -8.574  24.214  1.00 110.21 ?  39   ARG L N   1 
ATOM   7182 C CA  . ARG D 2 192 ? -51.189 -9.810  24.188  1.00 103.23 ?  39   ARG L CA  1 
ATOM   7183 C C   . ARG D 2 192 ? -52.387 -9.706  25.134  1.00 108.39 ?  39   ARG L C   1 
ATOM   7184 O O   . ARG D 2 192 ? -52.406 -8.853  26.024  1.00 102.82 ?  39   ARG L O   1 
ATOM   7185 C CB  . ARG D 2 192 ? -50.277 -10.980 24.556  1.00 104.40 ?  39   ARG L CB  1 
ATOM   7186 C CG  . ARG D 2 192 ? -49.450 -11.459 23.371  1.00 105.02 ?  39   ARG L CG  1 
ATOM   7187 C CD  . ARG D 2 192 ? -48.114 -12.052 23.778  1.00 104.29 ?  39   ARG L CD  1 
ATOM   7188 N NE  . ARG D 2 192 ? -47.288 -12.325 22.603  1.00 121.80 ?  39   ARG L NE  1 
ATOM   7189 C CZ  . ARG D 2 192 ? -46.038 -12.771 22.649  1.00 134.03 ?  39   ARG L CZ  1 
ATOM   7190 N NH1 . ARG D 2 192 ? -45.454 -13.000 23.817  1.00 138.71 1  39   ARG L NH1 1 
ATOM   7191 N NH2 . ARG D 2 192 ? -45.369 -12.988 21.523  1.00 133.26 ?  39   ARG L NH2 1 
ATOM   7192 N N   . PRO D 2 193 ? -53.413 -10.551 24.940  1.00 122.86 ?  40   PRO L N   1 
ATOM   7193 C CA  . PRO D 2 193 ? -54.675 -10.362 25.688  1.00 116.85 ?  40   PRO L CA  1 
ATOM   7194 C C   . PRO D 2 193 ? -54.519 -10.178 27.191  1.00 119.23 ?  40   PRO L C   1 
ATOM   7195 O O   . PRO D 2 193 ? -55.074 -9.224  27.753  1.00 128.05 ?  40   PRO L O   1 
ATOM   7196 C CB  . PRO D 2 193 ? -55.455 -11.637 25.347  1.00 112.83 ?  40   PRO L CB  1 
ATOM   7197 C CG  . PRO D 2 193 ? -54.988 -11.991 23.985  1.00 113.84 ?  40   PRO L CG  1 
ATOM   7198 C CD  . PRO D 2 193 ? -53.528 -11.633 23.945  1.00 111.10 ?  40   PRO L CD  1 
ATOM   7199 N N   . GLY D 2 194 ? -53.782 -11.058 27.859  1.00 106.91 ?  41   GLY L N   1 
ATOM   7200 C CA  . GLY D 2 194 ? -53.578 -10.960 29.289  1.00 110.36 ?  41   GLY L CA  1 
ATOM   7201 C C   . GLY D 2 194 ? -52.222 -10.449 29.720  1.00 125.51 ?  41   GLY L C   1 
ATOM   7202 O O   . GLY D 2 194 ? -51.922 -10.479 30.919  1.00 113.98 ?  41   GLY L O   1 
ATOM   7203 N N   . GLN D 2 195 ? -51.397 -9.971  28.794  1.00 106.56 ?  42   GLN L N   1 
ATOM   7204 C CA  . GLN D 2 195 ? -50.025 -9.591  29.088  1.00 107.81 ?  42   GLN L CA  1 
ATOM   7205 C C   . GLN D 2 195 ? -49.842 -8.083  28.987  1.00 116.35 ?  42   GLN L C   1 
ATOM   7206 O O   . GLN D 2 195 ? -50.651 -7.369  28.388  1.00 116.67 ?  42   GLN L O   1 
ATOM   7207 C CB  . GLN D 2 195 ? -49.050 -10.291 28.134  1.00 104.29 ?  42   GLN L CB  1 
ATOM   7208 C CG  . GLN D 2 195 ? -49.241 -11.795 28.036  1.00 106.46 ?  42   GLN L CG  1 
ATOM   7209 C CD  . GLN D 2 195 ? -49.005 -12.502 29.356  1.00 119.77 ?  42   GLN L CD  1 
ATOM   7210 O OE1 . GLN D 2 195 ? -49.923 -12.658 30.161  1.00 131.61 ?  42   GLN L OE1 1 
ATOM   7211 N NE2 . GLN D 2 195 ? -47.770 -12.936 29.583  1.00 115.57 ?  42   GLN L NE2 1 
ATOM   7212 N N   . SER D 2 196 ? -48.757 -7.607  29.593  1.00 106.84 ?  43   SER L N   1 
ATOM   7213 C CA  . SER D 2 196 ? -48.351 -6.224  29.443  1.00 99.87  ?  43   SER L CA  1 
ATOM   7214 C C   . SER D 2 196 ? -47.791 -6.002  28.039  1.00 96.33  ?  43   SER L C   1 
ATOM   7215 O O   . SER D 2 196 ? -47.439 -6.959  27.345  1.00 105.43 ?  43   SER L O   1 
ATOM   7216 C CB  . SER D 2 196 ? -47.308 -5.864  30.499  1.00 98.78  ?  43   SER L CB  1 
ATOM   7217 O OG  . SER D 2 196 ? -47.820 -6.049  31.807  1.00 103.04 ?  43   SER L OG  1 
ATOM   7218 N N   . PRO D 2 197 ? -47.716 -4.748  27.588  1.00 103.00 ?  44   PRO L N   1 
ATOM   7219 C CA  . PRO D 2 197 ? -47.129 -4.477  26.271  1.00 102.80 ?  44   PRO L CA  1 
ATOM   7220 C C   . PRO D 2 197 ? -45.686 -4.954  26.182  1.00 84.94  ?  44   PRO L C   1 
ATOM   7221 O O   . PRO D 2 197 ? -44.978 -5.087  27.183  1.00 85.39  ?  44   PRO L O   1 
ATOM   7222 C CB  . PRO D 2 197 ? -47.218 -2.952  26.149  1.00 82.95  ?  44   PRO L CB  1 
ATOM   7223 C CG  . PRO D 2 197 ? -48.361 -2.579  27.018  1.00 87.27  ?  44   PRO L CG  1 
ATOM   7224 C CD  . PRO D 2 197 ? -48.320 -3.538  28.175  1.00 100.37 ?  44   PRO L CD  1 
ATOM   7225 N N   . GLN D 2 198 ? -45.255 -5.219  24.950  1.00 85.88  ?  45   GLN L N   1 
ATOM   7226 C CA  . GLN D 2 198 ? -43.890 -5.636  24.670  1.00 92.98  ?  45   GLN L CA  1 
ATOM   7227 C C   . GLN D 2 198 ? -43.338 -4.811  23.515  1.00 88.05  ?  45   GLN L C   1 
ATOM   7228 O O   . GLN D 2 198 ? -44.085 -4.214  22.736  1.00 91.47  ?  45   GLN L O   1 
ATOM   7229 C CB  . GLN D 2 198 ? -43.807 -7.132  24.335  1.00 93.05  ?  45   GLN L CB  1 
ATOM   7230 C CG  . GLN D 2 198 ? -44.208 -7.480  22.911  1.00 96.99  ?  45   GLN L CG  1 
ATOM   7231 C CD  . GLN D 2 198 ? -44.123 -8.969  22.629  1.00 117.10 ?  45   GLN L CD  1 
ATOM   7232 O OE1 . GLN D 2 198 ? -44.590 -9.790  23.419  1.00 125.33 ?  45   GLN L OE1 1 
ATOM   7233 N NE2 . GLN D 2 198 ? -43.520 -9.324  21.500  1.00 116.49 ?  45   GLN L NE2 1 
ATOM   7234 N N   . LEU D 2 199 ? -42.012 -4.788  23.412  1.00 88.01  ?  46   LEU L N   1 
ATOM   7235 C CA  . LEU D 2 199 ? -41.325 -3.998  22.398  1.00 81.02  ?  46   LEU L CA  1 
ATOM   7236 C C   . LEU D 2 199 ? -41.088 -4.835  21.148  1.00 89.82  ?  46   LEU L C   1 
ATOM   7237 O O   . LEU D 2 199 ? -40.603 -5.968  21.231  1.00 89.81  ?  46   LEU L O   1 
ATOM   7238 C CB  . LEU D 2 199 ? -39.997 -3.470  22.940  1.00 78.07  ?  46   LEU L CB  1 
ATOM   7239 C CG  . LEU D 2 199 ? -39.114 -2.679  21.971  1.00 82.46  ?  46   LEU L CG  1 
ATOM   7240 C CD1 . LEU D 2 199 ? -39.871 -1.496  21.388  1.00 77.44  ?  46   LEU L CD1 1 
ATOM   7241 C CD2 . LEU D 2 199 ? -37.843 -2.216  22.666  1.00 73.62  ?  46   LEU L CD2 1 
ATOM   7242 N N   . LEU D 2 200 ? -41.433 -4.270  19.991  1.00 83.78  ?  47   LEU L N   1 
ATOM   7243 C CA  . LEU D 2 200 ? -41.193 -4.901  18.699  1.00 88.62  ?  47   LEU L CA  1 
ATOM   7244 C C   . LEU D 2 200 ? -40.153 -4.140  17.888  1.00 95.07  ?  47   LEU L C   1 
ATOM   7245 O O   . LEU D 2 200 ? -39.093 -4.683  17.564  1.00 94.23  ?  47   LEU L O   1 
ATOM   7246 C CB  . LEU D 2 200 ? -42.503 -5.003  17.906  1.00 88.27  ?  47   LEU L CB  1 
ATOM   7247 C CG  . LEU D 2 200 ? -43.606 -5.920  18.428  1.00 90.80  ?  47   LEU L CG  1 
ATOM   7248 C CD1 . LEU D 2 200 ? -44.871 -5.698  17.622  1.00 102.18 ?  47   LEU L CD1 1 
ATOM   7249 C CD2 . LEU D 2 200 ? -43.173 -7.375  18.357  1.00 104.84 ?  47   LEU L CD2 1 
ATOM   7250 N N   . ILE D 2 201 ? -40.437 -2.885  17.552  1.00 85.64  ?  48   ILE L N   1 
ATOM   7251 C CA  . ILE D 2 201 ? -39.556 -2.053  16.745  1.00 85.47  ?  48   ILE L CA  1 
ATOM   7252 C C   . ILE D 2 201 ? -39.286 -0.762  17.504  1.00 87.62  ?  48   ILE L C   1 
ATOM   7253 O O   . ILE D 2 201 ? -40.196 -0.188  18.112  1.00 84.82  ?  48   ILE L O   1 
ATOM   7254 C CB  . ILE D 2 201 ? -40.172 -1.750  15.362  1.00 86.01  ?  48   ILE L CB  1 
ATOM   7255 C CG1 . ILE D 2 201 ? -40.436 -3.046  14.591  1.00 88.60  ?  48   ILE L CG1 1 
ATOM   7256 C CG2 . ILE D 2 201 ? -39.268 -0.829  14.560  1.00 86.81  ?  48   ILE L CG2 1 
ATOM   7257 C CD1 . ILE D 2 201 ? -39.185 -3.701  14.049  1.00 93.04  ?  48   ILE L CD1 1 
ATOM   7258 N N   . SER D 2 202 ? -38.036 -0.312  17.476  1.00 84.21  ?  49   SER L N   1 
ATOM   7259 C CA  . SER D 2 202 ? -37.646 0.964   18.054  1.00 72.84  ?  49   SER L CA  1 
ATOM   7260 C C   . SER D 2 202 ? -37.014 1.835   16.978  1.00 89.58  ?  49   SER L C   1 
ATOM   7261 O O   . SER D 2 202 ? -36.251 1.346   16.140  1.00 86.07  ?  49   SER L O   1 
ATOM   7262 C CB  . SER D 2 202 ? -36.669 0.780   19.220  1.00 70.11  ?  49   SER L CB  1 
ATOM   7263 O OG  . SER D 2 202 ? -36.325 -0.583  19.390  1.00 94.62  ?  49   SER L OG  1 
ATOM   7264 N N   . LEU D 2 203 ? -37.349 3.125   17.007  1.00 80.74  ?  50   LEU L N   1 
ATOM   7265 C CA  . LEU D 2 203 ? -36.788 4.116   16.087  1.00 71.41  ?  50   LEU L CA  1 
ATOM   7266 C C   . LEU D 2 203 ? -37.075 3.765   14.628  1.00 78.83  ?  50   LEU L C   1 
ATOM   7267 O O   . LEU D 2 203 ? -36.214 3.901   13.755  1.00 87.12  ?  50   LEU L O   1 
ATOM   7268 C CB  . LEU D 2 203 ? -35.288 4.303   16.319  1.00 80.25  ?  50   LEU L CB  1 
ATOM   7269 C CG  . LEU D 2 203 ? -34.911 4.896   17.678  1.00 71.21  ?  50   LEU L CG  1 
ATOM   7270 C CD1 . LEU D 2 203 ? -33.442 5.283   17.708  1.00 68.41  ?  50   LEU L CD1 1 
ATOM   7271 C CD2 . LEU D 2 203 ? -35.795 6.091   18.010  1.00 77.06  ?  50   LEU L CD2 1 
ATOM   7272 N N   . GLY D 2 204 ? -38.295 3.310   14.358  1.00 80.30  ?  51   GLY L N   1 
ATOM   7273 C CA  . GLY D 2 204 ? -38.742 3.131   12.991  1.00 87.34  ?  51   GLY L CA  1 
ATOM   7274 C C   . GLY D 2 204 ? -38.513 1.757   12.395  1.00 91.80  ?  51   GLY L C   1 
ATOM   7275 O O   . GLY D 2 204 ? -39.460 1.120   11.924  1.00 90.90  ?  51   GLY L O   1 
ATOM   7276 N N   . SER D 2 205 ? -37.264 1.287   12.402  1.00 89.49  ?  52   SER L N   1 
ATOM   7277 C CA  . SER D 2 205 ? -36.927 0.053   11.705  1.00 93.74  ?  52   SER L CA  1 
ATOM   7278 C C   . SER D 2 205 ? -35.996 -0.874  12.475  1.00 89.62  ?  52   SER L C   1 
ATOM   7279 O O   . SER D 2 205 ? -35.694 -1.961  11.972  1.00 90.04  ?  52   SER L O   1 
ATOM   7280 C CB  . SER D 2 205 ? -36.294 0.377   10.341  1.00 100.13 ?  52   SER L CB  1 
ATOM   7281 O OG  . SER D 2 205 ? -35.207 1.274   10.487  1.00 91.08  ?  52   SER L OG  1 
ATOM   7282 N N   . TYR D 2 206 ? -35.533 -0.495  13.663  1.00 91.29  ?  53   TYR L N   1 
ATOM   7283 C CA  . TYR D 2 206 ? -34.579 -1.311  14.406  1.00 87.61  ?  53   TYR L CA  1 
ATOM   7284 C C   . TYR D 2 206 ? -35.333 -2.384  15.181  1.00 85.81  ?  53   TYR L C   1 
ATOM   7285 O O   . TYR D 2 206 ? -35.995 -2.092  16.182  1.00 85.71  ?  53   TYR L O   1 
ATOM   7286 C CB  . TYR D 2 206 ? -33.739 -0.437  15.332  1.00 77.89  ?  53   TYR L CB  1 
ATOM   7287 C CG  . TYR D 2 206 ? -32.922 0.591   14.586  1.00 93.33  ?  53   TYR L CG  1 
ATOM   7288 C CD1 . TYR D 2 206 ? -31.664 0.276   14.088  1.00 76.30  ?  53   TYR L CD1 1 
ATOM   7289 C CD2 . TYR D 2 206 ? -33.413 1.871   14.365  1.00 84.06  ?  53   TYR L CD2 1 
ATOM   7290 C CE1 . TYR D 2 206 ? -30.915 1.208   13.399  1.00 77.64  ?  53   TYR L CE1 1 
ATOM   7291 C CE2 . TYR D 2 206 ? -32.671 2.811   13.677  1.00 75.73  ?  53   TYR L CE2 1 
ATOM   7292 C CZ  . TYR D 2 206 ? -31.423 2.474   13.197  1.00 78.75  ?  53   TYR L CZ  1 
ATOM   7293 O OH  . TYR D 2 206 ? -30.680 3.406   12.511  1.00 86.87  ?  53   TYR L OH  1 
ATOM   7294 N N   . ARG D 2 207 ? -35.229 -3.627  14.716  1.00 93.70  ?  54   ARG L N   1 
ATOM   7295 C CA  . ARG D 2 207 ? -35.918 -4.739  15.355  1.00 89.01  ?  54   ARG L CA  1 
ATOM   7296 C C   . ARG D 2 207 ? -35.349 -4.977  16.748  1.00 89.28  ?  54   ARG L C   1 
ATOM   7297 O O   . ARG D 2 207 ? -34.132 -5.083  16.923  1.00 80.87  ?  54   ARG L O   1 
ATOM   7298 C CB  . ARG D 2 207 ? -35.790 -5.996  14.499  1.00 86.68  ?  54   ARG L CB  1 
ATOM   7299 C CG  . ARG D 2 207 ? -36.754 -7.109  14.871  1.00 90.95  ?  54   ARG L CG  1 
ATOM   7300 C CD  . ARG D 2 207 ? -36.677 -8.273  13.889  1.00 109.30 ?  54   ARG L CD  1 
ATOM   7301 N NE  . ARG D 2 207 ? -36.882 -7.844  12.507  1.00 119.40 ?  54   ARG L NE  1 
ATOM   7302 C CZ  . ARG D 2 207 ? -35.937 -7.858  11.571  1.00 112.77 ?  54   ARG L CZ  1 
ATOM   7303 N NH1 . ARG D 2 207 ? -34.718 -8.291  11.863  1.00 97.34  1  54   ARG L NH1 1 
ATOM   7304 N NH2 . ARG D 2 207 ? -36.214 -7.446  10.341  1.00 99.31  ?  54   ARG L NH2 1 
ATOM   7305 N N   . ALA D 2 208 ? -36.233 -5.056  17.740  1.00 86.24  ?  55   ALA L N   1 
ATOM   7306 C CA  . ALA D 2 208 ? -35.796 -5.247  19.114  1.00 88.97  ?  55   ALA L CA  1 
ATOM   7307 C C   . ALA D 2 208 ? -35.220 -6.647  19.310  1.00 92.11  ?  55   ALA L C   1 
ATOM   7308 O O   . ALA D 2 208 ? -35.529 -7.587  18.572  1.00 94.29  ?  55   ALA L O   1 
ATOM   7309 C CB  . ALA D 2 208 ? -36.959 -5.018  20.081  1.00 82.37  ?  55   ALA L CB  1 
ATOM   7310 N N   . SER D 2 209 ? -34.365 -6.774  20.322  1.00 80.97  ?  56   SER L N   1 
ATOM   7311 C CA  . SER D 2 209 ? -33.760 -8.059  20.641  1.00 84.70  ?  56   SER L CA  1 
ATOM   7312 C C   . SER D 2 209 ? -34.822 -9.048  21.103  1.00 91.99  ?  56   SER L C   1 
ATOM   7313 O O   . SER D 2 209 ? -35.760 -8.689  21.819  1.00 89.77  ?  56   SER L O   1 
ATOM   7314 C CB  . SER D 2 209 ? -32.695 -7.894  21.722  1.00 82.59  ?  56   SER L CB  1 
ATOM   7315 O OG  . SER D 2 209 ? -32.101 -9.139  22.051  1.00 73.72  ?  56   SER L OG  1 
ATOM   7316 N N   . GLY D 2 210 ? -34.667 -10.304 20.690  1.00 83.33  ?  57   GLY L N   1 
ATOM   7317 C CA  . GLY D 2 210 ? -35.640 -11.328 21.004  1.00 74.57  ?  57   GLY L CA  1 
ATOM   7318 C C   . GLY D 2 210 ? -36.872 -11.330 20.128  1.00 100.15 ?  57   GLY L C   1 
ATOM   7319 O O   . GLY D 2 210 ? -37.737 -12.195 20.310  1.00 90.60  ?  57   GLY L O   1 
ATOM   7320 N N   . VAL D 2 211 ? -36.984 -10.394 19.189  1.00 97.38  ?  58   VAL L N   1 
ATOM   7321 C CA  . VAL D 2 211 ? -38.109 -10.340 18.262  1.00 91.23  ?  58   VAL L CA  1 
ATOM   7322 C C   . VAL D 2 211 ? -37.726 -11.093 16.992  1.00 101.38 ?  58   VAL L C   1 
ATOM   7323 O O   . VAL D 2 211 ? -36.677 -10.807 16.397  1.00 96.28  ?  58   VAL L O   1 
ATOM   7324 C CB  . VAL D 2 211 ? -38.513 -8.887  17.962  1.00 94.83  ?  58   VAL L CB  1 
ATOM   7325 C CG1 . VAL D 2 211 ? -39.491 -8.832  16.800  1.00 96.46  ?  58   VAL L CG1 1 
ATOM   7326 C CG2 . VAL D 2 211 ? -39.112 -8.242  19.200  1.00 90.92  ?  58   VAL L CG2 1 
ATOM   7327 N N   . PRO D 2 212 ? -38.534 -12.052 16.539  1.00 105.01 ?  59   PRO L N   1 
ATOM   7328 C CA  . PRO D 2 212 ? -38.159 -12.851 15.366  1.00 108.03 ?  59   PRO L CA  1 
ATOM   7329 C C   . PRO D 2 212 ? -38.129 -12.011 14.098  1.00 112.20 ?  59   PRO L C   1 
ATOM   7330 O O   . PRO D 2 212 ? -38.641 -10.892 14.032  1.00 104.56 ?  59   PRO L O   1 
ATOM   7331 C CB  . PRO D 2 212 ? -39.247 -13.928 15.300  1.00 101.71 ?  59   PRO L CB  1 
ATOM   7332 C CG  . PRO D 2 212 ? -40.405 -13.342 16.028  1.00 103.88 ?  59   PRO L CG  1 
ATOM   7333 C CD  . PRO D 2 212 ? -39.821 -12.485 17.112  1.00 97.86  ?  59   PRO L CD  1 
ATOM   7334 N N   . ASP D 2 213 ? -37.506 -12.590 13.070  1.00 108.53 ?  60   ASP L N   1 
ATOM   7335 C CA  . ASP D 2 213 ? -37.259 -11.900 11.810  1.00 109.29 ?  60   ASP L CA  1 
ATOM   7336 C C   . ASP D 2 213 ? -38.531 -11.603 11.027  1.00 114.36 ?  60   ASP L C   1 
ATOM   7337 O O   . ASP D 2 213 ? -38.472 -10.831 10.064  1.00 124.99 ?  60   ASP L O   1 
ATOM   7338 C CB  . ASP D 2 213 ? -36.320 -12.737 10.940  1.00 114.50 ?  60   ASP L CB  1 
ATOM   7339 C CG  . ASP D 2 213 ? -35.465 -13.686 11.755  1.00 119.80 ?  60   ASP L CG  1 
ATOM   7340 O OD1 . ASP D 2 213 ? -34.368 -13.280 12.193  1.00 121.45 ?  60   ASP L OD1 1 
ATOM   7341 O OD2 . ASP D 2 213 ? -35.905 -14.836 11.974  1.00 121.41 -1 60   ASP L OD2 1 
ATOM   7342 N N   . ARG D 2 214 ? -39.668 -12.196 11.399  1.00 116.31 ?  61   ARG L N   1 
ATOM   7343 C CA  . ARG D 2 214 ? -40.879 -12.002 10.610  1.00 122.77 ?  61   ARG L CA  1 
ATOM   7344 C C   . ARG D 2 214 ? -41.414 -10.583 10.745  1.00 118.04 ?  61   ARG L C   1 
ATOM   7345 O O   . ARG D 2 214 ? -42.046 -10.070 9.814   1.00 121.59 ?  61   ARG L O   1 
ATOM   7346 C CB  . ARG D 2 214 ? -41.942 -13.027 11.013  1.00 119.19 ?  61   ARG L CB  1 
ATOM   7347 C CG  . ARG D 2 214 ? -42.877 -12.596 12.132  1.00 125.41 ?  61   ARG L CG  1 
ATOM   7348 C CD  . ARG D 2 214 ? -43.890 -13.687 12.438  1.00 111.20 ?  61   ARG L CD  1 
ATOM   7349 N NE  . ARG D 2 214 ? -43.268 -14.845 13.073  1.00 99.56  ?  61   ARG L NE  1 
ATOM   7350 C CZ  . ARG D 2 214 ? -43.315 -15.094 14.378  1.00 106.04 ?  61   ARG L CZ  1 
ATOM   7351 N NH1 . ARG D 2 214 ? -43.966 -14.270 15.187  1.00 105.67 1  61   ARG L NH1 1 
ATOM   7352 N NH2 . ARG D 2 214 ? -42.720 -16.170 14.872  1.00 104.35 ?  61   ARG L NH2 1 
ATOM   7353 N N   . PHE D 2 215 ? -41.166 -9.934  11.878  1.00 115.38 ?  62   PHE L N   1 
ATOM   7354 C CA  . PHE D 2 215 ? -41.551 -8.542  12.048  1.00 109.95 ?  62   PHE L CA  1 
ATOM   7355 C C   . PHE D 2 215 ? -40.520 -7.635  11.388  1.00 111.27 ?  62   PHE L C   1 
ATOM   7356 O O   . PHE D 2 215 ? -39.329 -7.954  11.324  1.00 107.68 ?  62   PHE L O   1 
ATOM   7357 C CB  . PHE D 2 215 ? -41.684 -8.193  13.531  1.00 110.67 ?  62   PHE L CB  1 
ATOM   7358 C CG  . PHE D 2 215 ? -42.632 -9.085  14.284  1.00 113.47 ?  62   PHE L CG  1 
ATOM   7359 C CD1 . PHE D 2 215 ? -42.168 -10.212 14.945  1.00 110.15 ?  62   PHE L CD1 1 
ATOM   7360 C CD2 . PHE D 2 215 ? -43.985 -8.794  14.338  1.00 114.42 ?  62   PHE L CD2 1 
ATOM   7361 C CE1 . PHE D 2 215 ? -43.035 -11.033 15.642  1.00 107.63 ?  62   PHE L CE1 1 
ATOM   7362 C CE2 . PHE D 2 215 ? -44.858 -9.612  15.034  1.00 109.54 ?  62   PHE L CE2 1 
ATOM   7363 C CZ  . PHE D 2 215 ? -44.382 -10.732 15.687  1.00 108.97 ?  62   PHE L CZ  1 
ATOM   7364 N N   . SER D 2 216 ? -40.992 -6.496  10.888  1.00 114.77 ?  63   SER L N   1 
ATOM   7365 C CA  . SER D 2 216 ? -40.125 -5.576  10.166  1.00 116.91 ?  63   SER L CA  1 
ATOM   7366 C C   . SER D 2 216 ? -40.745 -4.188  10.172  1.00 102.77 ?  63   SER L C   1 
ATOM   7367 O O   . SER D 2 216 ? -41.948 -4.037  9.948   1.00 98.38  ?  63   SER L O   1 
ATOM   7368 C CB  . SER D 2 216 ? -39.892 -6.047  8.726   1.00 111.56 ?  63   SER L CB  1 
ATOM   7369 O OG  . SER D 2 216 ? -39.250 -5.041  7.965   1.00 120.61 ?  63   SER L OG  1 
ATOM   7370 N N   . GLY D 2 217 ? -39.916 -3.181  10.423  1.00 102.02 ?  64   GLY L N   1 
ATOM   7371 C CA  . GLY D 2 217 ? -40.353 -1.798  10.437  1.00 96.23  ?  64   GLY L CA  1 
ATOM   7372 C C   . GLY D 2 217 ? -39.762 -1.020  9.277   1.00 101.24 ?  64   GLY L C   1 
ATOM   7373 O O   . GLY D 2 217 ? -38.637 -1.282  8.846   1.00 100.77 ?  64   GLY L O   1 
ATOM   7374 N N   . SER D 2 218 ? -40.523 -0.046  8.785   1.00 98.43  ?  65   SER L N   1 
ATOM   7375 C CA  . SER D 2 218 ? -40.093 0.768   7.656   1.00 98.63  ?  65   SER L CA  1 
ATOM   7376 C C   . SER D 2 218 ? -40.882 2.070   7.662   1.00 95.38  ?  65   SER L C   1 
ATOM   7377 O O   . SER D 2 218 ? -41.893 2.205   8.355   1.00 96.63  ?  65   SER L O   1 
ATOM   7378 C CB  . SER D 2 218 ? -40.273 0.020   6.330   1.00 96.61  ?  65   SER L CB  1 
ATOM   7379 O OG  . SER D 2 218 ? -41.612 -0.415  6.161   1.00 109.75 ?  65   SER L OG  1 
ATOM   7380 N N   . GLY D 2 219 ? -40.407 3.026   6.877   1.00 94.59  ?  66   GLY L N   1 
ATOM   7381 C CA  . GLY D 2 219 ? -41.047 4.319   6.753   1.00 104.42 ?  66   GLY L CA  1 
ATOM   7382 C C   . GLY D 2 219 ? -40.095 5.460   7.065   1.00 104.51 ?  66   GLY L C   1 
ATOM   7383 O O   . GLY D 2 219 ? -38.959 5.271   7.497   1.00 102.30 ?  66   GLY L O   1 
ATOM   7384 N N   . SER D 2 220 ? -40.599 6.669   6.826   1.00 101.57 ?  67   SER L N   1 
ATOM   7385 C CA  . SER D 2 220 ? -39.839 7.884   7.081   1.00 103.47 ?  67   SER L CA  1 
ATOM   7386 C C   . SER D 2 220 ? -40.799 9.063   7.114   1.00 115.21 ?  67   SER L C   1 
ATOM   7387 O O   . SER D 2 220 ? -41.869 9.027   6.500   1.00 120.01 ?  67   SER L O   1 
ATOM   7388 C CB  . SER D 2 220 ? -38.753 8.107   6.021   1.00 102.34 ?  67   SER L CB  1 
ATOM   7389 O OG  . SER D 2 220 ? -38.024 9.294   6.281   1.00 111.52 ?  67   SER L OG  1 
ATOM   7390 N N   . GLY D 2 221 ? -40.406 10.102  7.845   1.00 108.98 ?  68   GLY L N   1 
ATOM   7391 C CA  . GLY D 2 221 ? -41.197 11.313  7.931   1.00 110.63 ?  68   GLY L CA  1 
ATOM   7392 C C   . GLY D 2 221 ? -42.485 11.145  8.709   1.00 105.91 ?  68   GLY L C   1 
ATOM   7393 O O   . GLY D 2 221 ? -42.491 11.220  9.942   1.00 106.89 ?  68   GLY L O   1 
ATOM   7394 N N   . THR D 2 222 ? -43.589 10.914  7.995   1.00 105.87 ?  69   THR L N   1 
ATOM   7395 C CA  . THR D 2 222 ? -44.899 10.782  8.613   1.00 113.69 ?  69   THR L CA  1 
ATOM   7396 C C   . THR D 2 222 ? -45.603 9.468   8.313   1.00 111.43 ?  69   THR L C   1 
ATOM   7397 O O   . THR D 2 222 ? -46.554 9.129   9.024   1.00 113.45 ?  69   THR L O   1 
ATOM   7398 C CB  . THR D 2 222 ? -45.824 11.929  8.173   1.00 111.57 ?  69   THR L CB  1 
ATOM   7399 O OG1 . THR D 2 222 ? -45.958 11.916  6.747   1.00 110.49 ?  69   THR L OG1 1 
ATOM   7400 C CG2 . THR D 2 222 ? -45.264 13.270  8.612   1.00 106.32 ?  69   THR L CG2 1 
ATOM   7401 N N   . ASP D 2 223 ? -45.178 8.727   7.296   1.00 109.32 ?  70   ASP L N   1 
ATOM   7402 C CA  . ASP D 2 223 ? -45.868 7.514   6.860   1.00 120.48 ?  70   ASP L CA  1 
ATOM   7403 C C   . ASP D 2 223 ? -45.005 6.311   7.226   1.00 114.77 ?  70   ASP L C   1 
ATOM   7404 O O   . ASP D 2 223 ? -43.994 6.037   6.574   1.00 107.39 ?  70   ASP L O   1 
ATOM   7405 C CB  . ASP D 2 223 ? -46.158 7.576   5.363   1.00 119.76 ?  70   ASP L CB  1 
ATOM   7406 C CG  . ASP D 2 223 ? -47.151 6.522   4.917   1.00 134.58 ?  70   ASP L CG  1 
ATOM   7407 O OD1 . ASP D 2 223 ? -46.718 5.472   4.396   1.00 138.81 ?  70   ASP L OD1 1 
ATOM   7408 O OD2 . ASP D 2 223 ? -48.366 6.737   5.108   1.00 131.75 -1 70   ASP L OD2 1 
ATOM   7409 N N   . PHE D 2 224 ? -45.410 5.593   8.271   1.00 112.48 ?  71   PHE L N   1 
ATOM   7410 C CA  . PHE D 2 224 ? -44.677 4.440   8.766   1.00 115.32 ?  71   PHE L CA  1 
ATOM   7411 C C   . PHE D 2 224 ? -45.523 3.184   8.625   1.00 110.00 ?  71   PHE L C   1 
ATOM   7412 O O   . PHE D 2 224 ? -46.755 3.237   8.585   1.00 109.94 ?  71   PHE L O   1 
ATOM   7413 C CB  . PHE D 2 224 ? -44.255 4.642   10.224  1.00 111.00 ?  71   PHE L CB  1 
ATOM   7414 C CG  . PHE D 2 224 ? -43.365 5.831   10.431  1.00 111.34 ?  71   PHE L CG  1 
ATOM   7415 C CD1 . PHE D 2 224 ? -43.872 7.018   10.934  1.00 107.91 ?  71   PHE L CD1 1 
ATOM   7416 C CD2 . PHE D 2 224 ? -42.022 5.767   10.103  1.00 106.05 ?  71   PHE L CD2 1 
ATOM   7417 C CE1 . PHE D 2 224 ? -43.053 8.113   11.117  1.00 105.93 ?  71   PHE L CE1 1 
ATOM   7418 C CE2 . PHE D 2 224 ? -41.199 6.857   10.282  1.00 104.48 ?  71   PHE L CE2 1 
ATOM   7419 C CZ  . PHE D 2 224 ? -41.714 8.032   10.791  1.00 106.68 ?  71   PHE L CZ  1 
ATOM   7420 N N   . THR D 2 225 ? -44.843 2.042   8.548   1.00 114.70 ?  72   THR L N   1 
ATOM   7421 C CA  . THR D 2 225 ? -45.501 0.785   8.224   1.00 109.86 ?  72   THR L CA  1 
ATOM   7422 C C   . THR D 2 225 ? -44.828 -0.350  8.980   1.00 99.95  ?  72   THR L C   1 
ATOM   7423 O O   . THR D 2 225 ? -43.600 -0.396  9.078   1.00 106.28 ?  72   THR L O   1 
ATOM   7424 C CB  . THR D 2 225 ? -45.446 0.516   6.714   1.00 106.09 ?  72   THR L CB  1 
ATOM   7425 O OG1 . THR D 2 225 ? -45.613 1.746   5.996   1.00 105.11 ?  72   THR L OG1 1 
ATOM   7426 C CG2 . THR D 2 225 ? -46.538 -0.452  6.302   1.00 109.66 ?  72   THR L CG2 1 
ATOM   7427 N N   . LEU D 2 226 ? -45.637 -1.272  9.501   1.00 101.30 ?  73   LEU L N   1 
ATOM   7428 C CA  . LEU D 2 226 ? -45.145 -2.444  10.217  1.00 98.27  ?  73   LEU L CA  1 
ATOM   7429 C C   . LEU D 2 226 ? -45.513 -3.689  9.418   1.00 106.80 ?  73   LEU L C   1 
ATOM   7430 O O   . LEU D 2 226 ? -46.697 -4.007  9.262   1.00 115.52 ?  73   LEU L O   1 
ATOM   7431 C CB  . LEU D 2 226 ? -45.720 -2.504  11.631  1.00 93.73  ?  73   LEU L CB  1 
ATOM   7432 C CG  . LEU D 2 226 ? -45.384 -3.751  12.451  1.00 105.70 ?  73   LEU L CG  1 
ATOM   7433 C CD1 . LEU D 2 226 ? -43.883 -3.944  12.529  1.00 103.17 ?  73   LEU L CD1 1 
ATOM   7434 C CD2 . LEU D 2 226 ? -45.979 -3.659  13.845  1.00 91.37  ?  73   LEU L CD2 1 
ATOM   7435 N N   . LYS D 2 227 ? -44.501 -4.388  8.916   1.00 104.65 ?  74   LYS L N   1 
ATOM   7436 C CA  . LYS D 2 227 ? -44.703 -5.609  8.149   1.00 110.36 ?  74   LYS L CA  1 
ATOM   7437 C C   . LYS D 2 227 ? -44.418 -6.832  9.011   1.00 116.20 ?  74   LYS L C   1 
ATOM   7438 O O   . LYS D 2 227 ? -43.421 -6.877  9.737   1.00 120.95 ?  74   LYS L O   1 
ATOM   7439 C CB  . LYS D 2 227 ? -43.806 -5.643  6.910   1.00 114.09 ?  74   LYS L CB  1 
ATOM   7440 C CG  . LYS D 2 227 ? -44.033 -6.860  6.021   1.00 118.92 ?  74   LYS L CG  1 
ATOM   7441 C CD  . LYS D 2 227 ? -42.801 -7.192  5.193   1.00 124.37 ?  74   LYS L CD  1 
ATOM   7442 C CE  . LYS D 2 227 ? -41.631 -7.588  6.087   1.00 126.13 ?  74   LYS L CE  1 
ATOM   7443 N NZ  . LYS D 2 227 ? -42.004 -8.640  7.082   1.00 124.70 1  74   LYS L NZ  1 
ATOM   7444 N N   . ILE D 2 228 ? -45.298 -7.825  8.919   1.00 121.91 ?  75   ILE L N   1 
ATOM   7445 C CA  . ILE D 2 228 ? -45.125 -9.104  9.597   1.00 122.66 ?  75   ILE L CA  1 
ATOM   7446 C C   . ILE D 2 228 ? -45.437 -10.205 8.594   1.00 123.68 ?  75   ILE L C   1 
ATOM   7447 O O   . ILE D 2 228 ? -46.561 -10.284 8.084   1.00 116.51 ?  75   ILE L O   1 
ATOM   7448 C CB  . ILE D 2 228 ? -46.014 -9.225  10.849  1.00 117.14 ?  75   ILE L CB  1 
ATOM   7449 C CG1 . ILE D 2 228 ? -46.243 -10.696 11.216  1.00 123.16 ?  75   ILE L CG1 1 
ATOM   7450 C CG2 . ILE D 2 228 ? -47.326 -8.484  10.652  1.00 112.30 ?  75   ILE L CG2 1 
ATOM   7451 C CD1 . ILE D 2 228 ? -47.195 -10.888 12.368  1.00 115.72 ?  75   ILE L CD1 1 
ATOM   7452 N N   . SER D 2 229 ? -44.444 -11.038 8.298   1.00 122.38 ?  76   SER L N   1 
ATOM   7453 C CA  . SER D 2 229 ? -44.580 -12.108 7.320   1.00 131.08 ?  76   SER L CA  1 
ATOM   7454 C C   . SER D 2 229 ? -44.875 -13.424 8.026   1.00 128.93 ?  76   SER L C   1 
ATOM   7455 O O   . SER D 2 229 ? -44.324 -13.702 9.095   1.00 129.44 ?  76   SER L O   1 
ATOM   7456 C CB  . SER D 2 229 ? -43.310 -12.240 6.477   1.00 127.03 ?  76   SER L CB  1 
ATOM   7457 O OG  . SER D 2 229 ? -42.194 -12.561 7.289   1.00 116.30 ?  76   SER L OG  1 
ATOM   7458 N N   . ARG D 2 230 ? -45.739 -14.235 7.410   1.00 120.23 ?  77   ARG L N   1 
ATOM   7459 C CA  . ARG D 2 230 ? -46.217 -15.484 7.997   1.00 127.86 ?  77   ARG L CA  1 
ATOM   7460 C C   . ARG D 2 230 ? -46.732 -15.258 9.413   1.00 121.33 ?  77   ARG L C   1 
ATOM   7461 O O   . ARG D 2 230 ? -46.034 -15.556 10.388  1.00 119.51 ?  77   ARG L O   1 
ATOM   7462 C CB  . ARG D 2 230 ? -45.118 -16.553 7.994   1.00 120.57 ?  77   ARG L CB  1 
ATOM   7463 C CG  . ARG D 2 230 ? -45.124 -17.450 6.763   1.00 121.05 ?  77   ARG L CG  1 
ATOM   7464 C CD  . ARG D 2 230 ? -44.092 -18.569 6.867   1.00 123.33 ?  77   ARG L CD  1 
ATOM   7465 N NE  . ARG D 2 230 ? -44.700 -19.871 7.136   1.00 137.32 ?  77   ARG L NE  1 
ATOM   7466 C CZ  . ARG D 2 230 ? -44.048 -21.028 7.073   1.00 129.48 ?  77   ARG L CZ  1 
ATOM   7467 N NH1 . ARG D 2 230 ? -44.681 -22.165 7.333   1.00 123.97 1  77   ARG L NH1 1 
ATOM   7468 N NH2 . ARG D 2 230 ? -42.763 -21.052 6.747   1.00 127.47 ?  77   ARG L NH2 1 
ATOM   7469 N N   . VAL D 2 231 ? -47.949 -14.721 9.532   1.00 122.12 ?  78   VAL L N   1 
ATOM   7470 C CA  . VAL D 2 231 ? -48.531 -14.475 10.846  1.00 122.68 ?  78   VAL L CA  1 
ATOM   7471 C C   . VAL D 2 231 ? -48.703 -15.796 11.580  1.00 122.31 ?  78   VAL L C   1 
ATOM   7472 O O   . VAL D 2 231 ? -49.213 -16.776 11.023  1.00 133.44 ?  78   VAL L O   1 
ATOM   7473 C CB  . VAL D 2 231 ? -49.867 -13.730 10.708  1.00 128.78 ?  78   VAL L CB  1 
ATOM   7474 C CG1 . VAL D 2 231 ? -50.521 -13.554 12.069  1.00 118.90 ?  78   VAL L CG1 1 
ATOM   7475 C CG2 . VAL D 2 231 ? -49.655 -12.380 10.045  1.00 131.16 ?  78   VAL L CG2 1 
ATOM   7476 N N   . GLU D 2 232 ? -48.267 -15.829 12.834  1.00 113.96 ?  79   GLU L N   1 
ATOM   7477 C CA  . GLU D 2 232 ? -48.335 -17.015 13.672  1.00 114.09 ?  79   GLU L CA  1 
ATOM   7478 C C   . GLU D 2 232 ? -49.457 -16.860 14.695  1.00 116.90 ?  79   GLU L C   1 
ATOM   7479 O O   . GLU D 2 232 ? -50.116 -15.820 14.782  1.00 110.71 ?  79   GLU L O   1 
ATOM   7480 C CB  . GLU D 2 232 ? -46.991 -17.261 14.359  1.00 114.49 ?  79   GLU L CB  1 
ATOM   7481 C CG  . GLU D 2 232 ? -45.793 -17.210 13.421  1.00 116.54 ?  79   GLU L CG  1 
ATOM   7482 C CD  . GLU D 2 232 ? -45.169 -18.572 13.189  1.00 123.43 ?  79   GLU L CD  1 
ATOM   7483 O OE1 . GLU D 2 232 ? -44.956 -18.938 12.013  1.00 123.58 ?  79   GLU L OE1 1 
ATOM   7484 O OE2 . GLU D 2 232 ? -44.893 -19.277 14.182  1.00 115.50 -1 79   GLU L OE2 1 
ATOM   7485 N N   . ALA D 2 233 ? -49.669 -17.917 15.481  1.00 124.05 ?  80   ALA L N   1 
ATOM   7486 C CA  . ALA D 2 233 ? -50.726 -17.887 16.486  1.00 118.91 ?  80   ALA L CA  1 
ATOM   7487 C C   . ALA D 2 233 ? -50.360 -16.996 17.665  1.00 118.21 ?  80   ALA L C   1 
ATOM   7488 O O   . ALA D 2 233 ? -51.249 -16.463 18.337  1.00 121.13 ?  80   ALA L O   1 
ATOM   7489 C CB  . ALA D 2 233 ? -51.034 -19.304 16.968  1.00 109.12 ?  80   ALA L CB  1 
ATOM   7490 N N   . GLU D 2 234 ? -49.063 -16.821 17.928  1.00 125.51 ?  81   GLU L N   1 
ATOM   7491 C CA  . GLU D 2 234 ? -48.629 -16.018 19.065  1.00 126.34 ?  81   GLU L CA  1 
ATOM   7492 C C   . GLU D 2 234 ? -48.800 -14.525 18.823  1.00 126.71 ?  81   GLU L C   1 
ATOM   7493 O O   . GLU D 2 234 ? -48.744 -13.745 19.779  1.00 128.41 ?  81   GLU L O   1 
ATOM   7494 C CB  . GLU D 2 234 ? -47.166 -16.326 19.386  1.00 127.24 ?  81   GLU L CB  1 
ATOM   7495 C CG  . GLU D 2 234 ? -46.191 -15.838 18.325  1.00 128.00 ?  81   GLU L CG  1 
ATOM   7496 C CD  . GLU D 2 234 ? -44.806 -16.434 18.479  1.00 135.79 ?  81   GLU L CD  1 
ATOM   7497 O OE1 . GLU D 2 234 ? -44.417 -17.262 17.628  1.00 129.42 ?  81   GLU L OE1 1 
ATOM   7498 O OE2 . GLU D 2 234 ? -44.110 -16.081 19.454  1.00 138.54 -1 81   GLU L OE2 1 
ATOM   7499 N N   . ASP D 2 235 ? -49.015 -14.112 17.575  1.00 119.36 ?  82   ASP L N   1 
ATOM   7500 C CA  . ASP D 2 235 ? -49.076 -12.700 17.220  1.00 112.38 ?  82   ASP L CA  1 
ATOM   7501 C C   . ASP D 2 235 ? -50.391 -12.034 17.605  1.00 117.53 ?  82   ASP L C   1 
ATOM   7502 O O   . ASP D 2 235 ? -50.547 -10.834 17.355  1.00 112.61 ?  82   ASP L O   1 
ATOM   7503 C CB  . ASP D 2 235 ? -48.840 -12.534 15.717  1.00 112.73 ?  82   ASP L CB  1 
ATOM   7504 C CG  . ASP D 2 235 ? -47.543 -13.169 15.258  1.00 123.36 ?  82   ASP L CG  1 
ATOM   7505 O OD1 . ASP D 2 235 ? -46.706 -13.502 16.123  1.00 124.28 ?  82   ASP L OD1 1 
ATOM   7506 O OD2 . ASP D 2 235 ? -47.364 -13.344 14.034  1.00 120.39 -1 82   ASP L OD2 1 
ATOM   7507 N N   . VAL D 2 236 ? -51.332 -12.767 18.202  1.00 121.67 ?  83   VAL L N   1 
ATOM   7508 C CA  . VAL D 2 236 ? -52.624 -12.190 18.552  1.00 121.91 ?  83   VAL L CA  1 
ATOM   7509 C C   . VAL D 2 236 ? -52.443 -11.116 19.616  1.00 111.78 ?  83   VAL L C   1 
ATOM   7510 O O   . VAL D 2 236 ? -51.632 -11.256 20.542  1.00 114.25 ?  83   VAL L O   1 
ATOM   7511 C CB  . VAL D 2 236 ? -53.593 -13.287 19.026  1.00 120.85 ?  83   VAL L CB  1 
ATOM   7512 C CG1 . VAL D 2 236 ? -54.073 -14.116 17.845  1.00 122.43 ?  83   VAL L CG1 1 
ATOM   7513 C CG2 . VAL D 2 236 ? -52.923 -14.175 20.064  1.00 122.93 ?  83   VAL L CG2 1 
ATOM   7514 N N   . GLY D 2 237 ? -53.197 -10.036 19.484  1.00 115.46 ?  84   GLY L N   1 
ATOM   7515 C CA  . GLY D 2 237 ? -53.124 -8.928  20.410  1.00 117.26 ?  84   GLY L CA  1 
ATOM   7516 C C   . GLY D 2 237 ? -53.437 -7.625  19.703  1.00 111.24 ?  84   GLY L C   1 
ATOM   7517 O O   . GLY D 2 237 ? -53.986 -7.616  18.605  1.00 109.56 ?  84   GLY L O   1 
ATOM   7518 N N   . VAL D 2 238 ? -53.075 -6.526  20.358  1.00 104.74 ?  85   VAL L N   1 
ATOM   7519 C CA  . VAL D 2 238 ? -53.294 -5.182  19.837  1.00 109.17 ?  85   VAL L CA  1 
ATOM   7520 C C   . VAL D 2 238 ? -51.937 -4.545  19.571  1.00 107.53 ?  85   VAL L C   1 
ATOM   7521 O O   . VAL D 2 238 ? -51.028 -4.632  20.406  1.00 100.90 ?  85   VAL L O   1 
ATOM   7522 C CB  . VAL D 2 238 ? -54.123 -4.326  20.810  1.00 109.90 ?  85   VAL L CB  1 
ATOM   7523 C CG1 . VAL D 2 238 ? -54.759 -3.154  20.076  1.00 106.47 ?  85   VAL L CG1 1 
ATOM   7524 C CG2 . VAL D 2 238 ? -55.179 -5.172  21.502  1.00 111.65 ?  85   VAL L CG2 1 
ATOM   7525 N N   . TYR D 2 239 ? -51.803 -3.905  18.414  1.00 106.99 ?  86   TYR L N   1 
ATOM   7526 C CA  . TYR D 2 239 ? -50.560 -3.262  18.011  1.00 101.73 ?  86   TYR L CA  1 
ATOM   7527 C C   . TYR D 2 239 ? -50.670 -1.754  18.188  1.00 103.27 ?  86   TYR L C   1 
ATOM   7528 O O   . TYR D 2 239 ? -51.682 -1.148  17.825  1.00 103.65 ?  86   TYR L O   1 
ATOM   7529 C CB  . TYR D 2 239 ? -50.220 -3.597  16.558  1.00 99.58  ?  86   TYR L CB  1 
ATOM   7530 C CG  . TYR D 2 239 ? -49.627 -4.975  16.364  1.00 103.61 ?  86   TYR L CG  1 
ATOM   7531 C CD1 . TYR D 2 239 ? -50.382 -6.120  16.595  1.00 112.55 ?  86   TYR L CD1 1 
ATOM   7532 C CD2 . TYR D 2 239 ? -48.314 -5.130  15.941  1.00 96.28  ?  86   TYR L CD2 1 
ATOM   7533 C CE1 . TYR D 2 239 ? -49.841 -7.381  16.416  1.00 105.49 ?  86   TYR L CE1 1 
ATOM   7534 C CE2 . TYR D 2 239 ? -47.765 -6.384  15.756  1.00 102.25 ?  86   TYR L CE2 1 
ATOM   7535 C CZ  . TYR D 2 239 ? -48.532 -7.506  15.997  1.00 100.35 ?  86   TYR L CZ  1 
ATOM   7536 O OH  . TYR D 2 239 ? -47.984 -8.755  15.814  1.00 99.78  ?  86   TYR L OH  1 
ATOM   7537 N N   . TYR D 2 240 ? -49.619 -1.154  18.744  1.00 100.62 ?  87   TYR L N   1 
ATOM   7538 C CA  . TYR D 2 240 ? -49.581 0.279   19.007  1.00 83.75  ?  87   TYR L CA  1 
ATOM   7539 C C   . TYR D 2 240 ? -48.269 0.857   18.504  1.00 86.17  ?  87   TYR L C   1 
ATOM   7540 O O   . TYR D 2 240 ? -47.193 0.364   18.861  1.00 99.48  ?  87   TYR L O   1 
ATOM   7541 C CB  . TYR D 2 240 ? -49.726 0.580   20.504  1.00 84.72  ?  87   TYR L CB  1 
ATOM   7542 C CG  . TYR D 2 240 ? -50.999 0.075   21.140  1.00 91.75  ?  87   TYR L CG  1 
ATOM   7543 C CD1 . TYR D 2 240 ? -52.097 0.910   21.296  1.00 101.14 ?  87   TYR L CD1 1 
ATOM   7544 C CD2 . TYR D 2 240 ? -51.096 -1.231  21.600  1.00 100.11 ?  87   TYR L CD2 1 
ATOM   7545 C CE1 . TYR D 2 240 ? -53.260 0.456   21.886  1.00 105.04 ?  87   TYR L CE1 1 
ATOM   7546 C CE2 . TYR D 2 240 ? -52.255 -1.695  22.190  1.00 106.64 ?  87   TYR L CE2 1 
ATOM   7547 C CZ  . TYR D 2 240 ? -53.335 -0.847  22.329  1.00 109.74 ?  87   TYR L CZ  1 
ATOM   7548 O OH  . TYR D 2 240 ? -54.493 -1.304  22.915  1.00 105.48 ?  87   TYR L OH  1 
ATOM   7549 N N   . CYS D 2 241 ? -48.358 1.894   17.678  1.00 89.78  ?  88   CYS L N   1 
ATOM   7550 C CA  . CYS D 2 241 ? -47.212 2.736   17.373  1.00 95.46  ?  88   CYS L CA  1 
ATOM   7551 C C   . CYS D 2 241 ? -47.160 3.878   18.377  1.00 85.19  ?  88   CYS L C   1 
ATOM   7552 O O   . CYS D 2 241 ? -48.197 4.397   18.800  1.00 89.07  ?  88   CYS L O   1 
ATOM   7553 C CB  . CYS D 2 241 ? -47.289 3.288   15.948  1.00 96.45  ?  88   CYS L CB  1 
ATOM   7554 S SG  . CYS D 2 241 ? -48.902 3.968   15.499  1.00 118.23 ?  88   CYS L SG  1 
ATOM   7555 N N   . MET D 2 242 ? -45.946 4.260   18.765  1.00 81.10  ?  89   MET L N   1 
ATOM   7556 C CA  . MET D 2 242 ? -45.769 5.302   19.764  1.00 84.96  ?  89   MET L CA  1 
ATOM   7557 C C   . MET D 2 242 ? -44.674 6.261   19.327  1.00 82.75  ?  89   MET L C   1 
ATOM   7558 O O   . MET D 2 242 ? -43.622 5.837   18.840  1.00 71.76  ?  89   MET L O   1 
ATOM   7559 C CB  . MET D 2 242 ? -45.421 4.714   21.136  1.00 73.60  ?  89   MET L CB  1 
ATOM   7560 C CG  . MET D 2 242 ? -45.469 5.731   22.265  1.00 81.51  ?  89   MET L CG  1 
ATOM   7561 S SD  . MET D 2 242 ? -44.527 5.227   23.715  1.00 87.06  ?  89   MET L SD  1 
ATOM   7562 C CE  . MET D 2 242 ? -42.860 5.276   23.062  1.00 76.50  ?  89   MET L CE  1 
ATOM   7563 N N   . GLN D 2 243 ? -44.934 7.553   19.506  1.00 79.68  ?  90   GLN L N   1 
ATOM   7564 C CA  . GLN D 2 243 ? -43.916 8.566   19.274  1.00 78.18  ?  90   GLN L CA  1 
ATOM   7565 C C   . GLN D 2 243 ? -42.846 8.471   20.353  1.00 87.44  ?  90   GLN L C   1 
ATOM   7566 O O   . GLN D 2 243 ? -43.157 8.352   21.542  1.00 81.87  ?  90   GLN L O   1 
ATOM   7567 C CB  . GLN D 2 243 ? -44.551 9.956   19.266  1.00 87.02  ?  90   GLN L CB  1 
ATOM   7568 C CG  . GLN D 2 243 ? -43.586 11.088  18.972  1.00 92.16  ?  90   GLN L CG  1 
ATOM   7569 C CD  . GLN D 2 243 ? -44.274 12.437  18.945  1.00 89.00  ?  90   GLN L CD  1 
ATOM   7570 O OE1 . GLN D 2 243 ? -45.464 12.545  19.241  1.00 85.84  ?  90   GLN L OE1 1 
ATOM   7571 N NE2 . GLN D 2 243 ? -43.528 13.475  18.586  1.00 99.88  ?  90   GLN L NE2 1 
ATOM   7572 N N   . ALA D 2 244 ? -41.583 8.517   19.940  1.00 84.47  ?  91   ALA L N   1 
ATOM   7573 C CA  . ALA D 2 244 ? -40.469 8.302   20.853  1.00 79.43  ?  91   ALA L CA  1 
ATOM   7574 C C   . ALA D 2 244 ? -40.029 9.568   21.578  1.00 79.42  ?  91   ALA L C   1 
ATOM   7575 O O   . ALA D 2 244 ? -39.124 9.498   22.415  1.00 85.86  ?  91   ALA L O   1 
ATOM   7576 C CB  . ALA D 2 244 ? -39.280 7.699   20.100  1.00 82.10  ?  91   ALA L CB  1 
ATOM   7577 N N   . LEU D 2 245 ? -40.637 10.712  21.287  1.00 84.72  ?  92   LEU L N   1 
ATOM   7578 C CA  . LEU D 2 245 ? -40.331 11.962  21.971  1.00 72.94  ?  92   LEU L CA  1 
ATOM   7579 C C   . LEU D 2 245 ? -41.578 12.461  22.701  1.00 74.56  ?  92   LEU L C   1 
ATOM   7580 O O   . LEU D 2 245 ? -42.631 11.821  22.679  1.00 93.87  ?  92   LEU L O   1 
ATOM   7581 C CB  . LEU D 2 245 ? -39.782 12.997  20.986  1.00 82.68  ?  92   LEU L CB  1 
ATOM   7582 C CG  . LEU D 2 245 ? -38.427 12.607  20.383  1.00 65.11  ?  92   LEU L CG  1 
ATOM   7583 C CD1 . LEU D 2 245 ? -37.858 13.724  19.520  1.00 72.00  ?  92   LEU L CD1 1 
ATOM   7584 C CD2 . LEU D 2 245 ? -37.435 12.208  21.471  1.00 70.44  ?  92   LEU L CD2 1 
ATOM   7585 N N   . HIS D 2 246 ? -41.452 13.632  23.334  1.00 82.91  ?  93   HIS L N   1 
ATOM   7586 C CA  . HIS D 2 246 ? -42.330 14.071  24.420  1.00 86.42  ?  93   HIS L CA  1 
ATOM   7587 C C   . HIS D 2 246 ? -43.834 13.950  24.173  1.00 101.39 ?  93   HIS L C   1 
ATOM   7588 O O   . HIS D 2 246 ? -44.526 13.323  24.985  1.00 111.02 ?  93   HIS L O   1 
ATOM   7589 C CB  . HIS D 2 246 ? -42.035 15.520  24.805  1.00 85.85  ?  93   HIS L CB  1 
ATOM   7590 C CG  . HIS D 2 246 ? -42.991 16.063  25.820  1.00 91.43  ?  93   HIS L CG  1 
ATOM   7591 N ND1 . HIS D 2 246 ? -44.115 16.783  25.475  1.00 88.83  ?  93   HIS L ND1 1 
ATOM   7592 C CD2 . HIS D 2 246 ? -43.013 15.955  27.170  1.00 85.93  ?  93   HIS L CD2 1 
ATOM   7593 C CE1 . HIS D 2 246 ? -44.778 17.111  26.569  1.00 93.94  ?  93   HIS L CE1 1 
ATOM   7594 N NE2 . HIS D 2 246 ? -44.129 16.623  27.612  1.00 91.05  ?  93   HIS L NE2 1 
ATOM   7595 N N   . PRO D 2 247 ? -44.396 14.549  23.105  1.00 91.63  ?  94   PRO L N   1 
ATOM   7596 C CA  . PRO D 2 247 ? -45.865 14.622  23.085  1.00 90.45  ?  94   PRO L CA  1 
ATOM   7597 C C   . PRO D 2 247 ? -46.552 13.269  22.929  1.00 104.74 ?  94   PRO L C   1 
ATOM   7598 O O   . PRO D 2 247 ? -47.023 12.732  23.933  1.00 91.71  ?  94   PRO L O   1 
ATOM   7599 C CB  . PRO D 2 247 ? -46.150 15.509  21.873  1.00 92.18  ?  94   PRO L CB  1 
ATOM   7600 C CG  . PRO D 2 247 ? -45.007 15.263  20.967  1.00 104.98 ?  94   PRO L CG  1 
ATOM   7601 C CD  . PRO D 2 247 ? -43.809 15.080  21.861  1.00 90.17  ?  94   PRO L CD  1 
ATOM   7602 N N   . PHE D 2 248 ? -44.670 10.934  22.671  1.00 94.50  ?  95   PHE L N   1 
ATOM   7603 C CA  . PHE D 2 248 ? -45.180 9.859   23.513  1.00 90.27  ?  95   PHE L CA  1 
ATOM   7604 C C   . PHE D 2 248 ? -46.671 9.657   23.282  1.00 90.86  ?  95   PHE L C   1 
ATOM   7605 O O   . PHE D 2 248 ? -47.353 9.011   24.079  1.00 92.95  ?  95   PHE L O   1 
ATOM   7606 C CB  . PHE D 2 248 ? -44.893 10.150  24.987  1.00 81.20  ?  95   PHE L CB  1 
ATOM   7607 C CG  . PHE D 2 248 ? -43.425 10.242  25.310  1.00 82.60  ?  95   PHE L CG  1 
ATOM   7608 C CD1 . PHE D 2 248 ? -42.970 11.097  26.299  1.00 80.51  ?  95   PHE L CD1 1 
ATOM   7609 C CD2 . PHE D 2 248 ? -42.502 9.469   24.625  1.00 81.00  ?  95   PHE L CD2 1 
ATOM   7610 C CE1 . PHE D 2 248 ? -41.624 11.187  26.598  1.00 69.75  ?  95   PHE L CE1 1 
ATOM   7611 C CE2 . PHE D 2 248 ? -41.153 9.553   24.919  1.00 86.17  ?  95   PHE L CE2 1 
ATOM   7612 C CZ  . PHE D 2 248 ? -40.715 10.413  25.908  1.00 73.06  ?  95   PHE L CZ  1 
ATOM   7613 N N   . THR D 2 249 ? -47.177 10.215  22.185  1.00 90.35  ?  96   THR L N   1 
ATOM   7614 C CA  . THR D 2 249 ? -48.545 9.936   21.777  1.00 96.91  ?  96   THR L CA  1 
ATOM   7615 C C   . THR D 2 249 ? -48.637 8.535   21.188  1.00 89.73  ?  96   THR L C   1 
ATOM   7616 O O   . THR D 2 249 ? -47.736 8.083   20.477  1.00 86.10  ?  96   THR L O   1 
ATOM   7617 C CB  . THR D 2 249 ? -49.028 10.965  20.754  1.00 91.89  ?  96   THR L CB  1 
ATOM   7618 O OG1 . THR D 2 249 ? -47.981 11.240  19.815  1.00 101.28 ?  96   THR L OG1 1 
ATOM   7619 C CG2 . THR D 2 249 ? -49.446 12.253  21.444  1.00 82.88  ?  96   THR L CG2 1 
ATOM   7620 N N   . PHE D 2 250 ? -49.729 7.845   21.491  1.00 92.24  ?  97   PHE L N   1 
ATOM   7621 C CA  . PHE D 2 250 ? -49.949 6.492   21.004  1.00 87.64  ?  97   PHE L CA  1 
ATOM   7622 C C   . PHE D 2 250 ? -50.855 6.502   19.776  1.00 88.64  ?  97   PHE L C   1 
ATOM   7623 O O   . PHE D 2 250 ? -51.591 7.458   19.518  1.00 103.44 ?  97   PHE L O   1 
ATOM   7624 C CB  . PHE D 2 250 ? -50.546 5.612   22.104  1.00 94.48  ?  97   PHE L CB  1 
ATOM   7625 C CG  . PHE D 2 250 ? -49.514 4.987   23.001  1.00 84.73  ?  97   PHE L CG  1 
ATOM   7626 C CD1 . PHE D 2 250 ? -49.187 5.560   24.220  1.00 82.62  ?  97   PHE L CD1 1 
ATOM   7627 C CD2 . PHE D 2 250 ? -48.862 3.827   22.616  1.00 86.35  ?  97   PHE L CD2 1 
ATOM   7628 C CE1 . PHE D 2 250 ? -48.232 4.980   25.042  1.00 78.91  ?  97   PHE L CE1 1 
ATOM   7629 C CE2 . PHE D 2 250 ? -47.909 3.244   23.430  1.00 76.39  ?  97   PHE L CE2 1 
ATOM   7630 C CZ  . PHE D 2 250 ? -47.593 3.820   24.645  1.00 76.39  ?  97   PHE L CZ  1 
ATOM   7631 N N   . GLY D 2 251 ? -50.780 5.415   19.011  1.00 98.53  ?  98   GLY L N   1 
ATOM   7632 C CA  . GLY D 2 251 ? -51.543 5.277   17.789  1.00 106.51 ?  98   GLY L CA  1 
ATOM   7633 C C   . GLY D 2 251 ? -53.032 5.083   17.988  1.00 115.52 ?  98   GLY L C   1 
ATOM   7634 O O   . GLY D 2 251 ? -53.837 5.632   17.227  1.00 123.25 ?  98   GLY L O   1 
ATOM   7635 N N   . GLY D 2 252 ? -53.425 4.313   19.000  1.00 110.09 ?  99   GLY L N   1 
ATOM   7636 C CA  . GLY D 2 252 ? -54.827 4.006   19.252  1.00 114.86 ?  99   GLY L CA  1 
ATOM   7637 C C   . GLY D 2 252 ? -55.173 2.531   19.229  1.00 105.88 ?  99   GLY L C   1 
ATOM   7638 O O   . GLY D 2 252 ? -56.241 2.160   19.735  1.00 98.75  ?  99   GLY L O   1 
ATOM   7639 N N   . GLY D 2 253 ? -54.336 1.677   18.664  1.00 98.21  ?  100  GLY L N   1 
ATOM   7640 C CA  . GLY D 2 253 ? -54.585 0.248   18.710  1.00 110.47 ?  100  GLY L CA  1 
ATOM   7641 C C   . GLY D 2 253 ? -55.009 -0.309  17.364  1.00 112.46 ?  100  GLY L C   1 
ATOM   7642 O O   . GLY D 2 253 ? -55.820 0.288   16.647  1.00 114.37 ?  100  GLY L O   1 
ATOM   7643 N N   . THR D 2 254 ? -54.438 -1.457  17.008  1.00 119.56 ?  101  THR L N   1 
ATOM   7644 C CA  . THR D 2 254 ? -54.843 -2.218  15.831  1.00 117.24 ?  101  THR L CA  1 
ATOM   7645 C C   . THR D 2 254 ? -54.971 -3.675  16.246  1.00 109.29 ?  101  THR L C   1 
ATOM   7646 O O   . THR D 2 254 ? -53.982 -4.294  16.654  1.00 106.97 ?  101  THR L O   1 
ATOM   7647 C CB  . THR D 2 254 ? -53.838 -2.071  14.684  1.00 114.28 ?  101  THR L CB  1 
ATOM   7648 O OG1 . THR D 2 254 ? -53.970 -0.775  14.088  1.00 118.21 ?  101  THR L OG1 1 
ATOM   7649 C CG2 . THR D 2 254 ? -54.074 -3.142  13.627  1.00 101.47 ?  101  THR L CG2 1 
ATOM   7650 N N   . LYS D 2 255 ? -56.183 -4.214  16.160  1.00 112.23 ?  102  LYS L N   1 
ATOM   7651 C CA  . LYS D 2 255 ? -56.455 -5.565  16.626  1.00 110.86 ?  102  LYS L CA  1 
ATOM   7652 C C   . LYS D 2 255 ? -56.175 -6.579  15.526  1.00 122.76 ?  102  LYS L C   1 
ATOM   7653 O O   . LYS D 2 255 ? -56.555 -6.381  14.368  1.00 133.86 ?  102  LYS L O   1 
ATOM   7654 C CB  . LYS D 2 255 ? -57.905 -5.692  17.096  1.00 112.25 ?  102  LYS L CB  1 
ATOM   7655 C CG  . LYS D 2 255 ? -58.173 -6.939  17.916  1.00 119.87 ?  102  LYS L CG  1 
ATOM   7656 C CD  . LYS D 2 255 ? -57.284 -6.971  19.149  1.00 119.80 ?  102  LYS L CD  1 
ATOM   7657 C CE  . LYS D 2 255 ? -57.421 -8.283  19.902  1.00 121.56 ?  102  LYS L CE  1 
ATOM   7658 N NZ  . LYS D 2 255 ? -57.021 -9.443  19.059  1.00 125.54 1  102  LYS L NZ  1 
ATOM   7659 N N   . VAL D 2 256 ? -55.502 -7.666  15.895  1.00 126.96 ?  103  VAL L N   1 
ATOM   7660 C CA  . VAL D 2 256 ? -55.220 -8.773  14.990  1.00 118.88 ?  103  VAL L CA  1 
ATOM   7661 C C   . VAL D 2 256 ? -55.805 -10.043 15.592  1.00 125.93 ?  103  VAL L C   1 
ATOM   7662 O O   . VAL D 2 256 ? -55.823 -10.211 16.817  1.00 114.82 ?  103  VAL L O   1 
ATOM   7663 C CB  . VAL D 2 256 ? -53.707 -8.930  14.724  1.00 116.32 ?  103  VAL L CB  1 
ATOM   7664 C CG1 . VAL D 2 256 ? -53.151 -7.670  14.077  1.00 110.18 ?  103  VAL L CG1 1 
ATOM   7665 C CG2 . VAL D 2 256 ? -52.962 -9.241  16.011  1.00 120.94 ?  103  VAL L CG2 1 
ATOM   7666 N N   . GLU D 2 257 ? -56.293 -10.929 14.730  1.00 138.36 ?  104  GLU L N   1 
ATOM   7667 C CA  . GLU D 2 257 ? -56.973 -12.136 15.182  1.00 123.42 ?  104  GLU L CA  1 
ATOM   7668 C C   . GLU D 2 257 ? -57.084 -13.171 14.068  1.00 118.37 ?  104  GLU L C   1 
ATOM   7669 O O   . GLU D 2 257 ? -57.326 -12.827 12.912  1.00 123.79 ?  104  GLU L O   1 
ATOM   7670 C CB  . GLU D 2 257 ? -58.362 -11.786 15.720  1.00 115.35 ?  104  GLU L CB  1 
ATOM   7671 C CG  . GLU D 2 257 ? -59.111 -10.765 14.875  1.00 122.13 ?  104  GLU L CG  1 
ATOM   7672 C CD  . GLU D 2 257 ? -60.253 -10.110 15.627  1.00 135.87 ?  104  GLU L CD  1 
ATOM   7673 O OE1 . GLU D 2 257 ? -60.750 -10.714 16.601  1.00 136.89 ?  104  GLU L OE1 1 
ATOM   7674 O OE2 . GLU D 2 257 ? -60.647 -8.986  15.248  1.00 134.74 -1 104  GLU L OE2 1 
HETATM 7675 C C1  . NAG E 3 .   ? -16.684 -4.334  45.164  1.00 48.33  ?  1    NAG C C1  1 
HETATM 7676 C C2  . NAG E 3 .   ? -15.669 -3.205  45.322  1.00 58.00  ?  1    NAG C C2  1 
HETATM 7677 C C3  . NAG E 3 .   ? -16.086 -2.269  46.456  1.00 55.79  ?  1    NAG C C3  1 
HETATM 7678 C C4  . NAG E 3 .   ? -17.529 -1.804  46.286  1.00 51.37  ?  1    NAG C C4  1 
HETATM 7679 C C5  . NAG E 3 .   ? -18.452 -2.999  46.059  1.00 63.98  ?  1    NAG C C5  1 
HETATM 7680 C C6  . NAG E 3 .   ? -19.872 -2.599  45.733  1.00 59.54  ?  1    NAG C C6  1 
HETATM 7681 C C7  . NAG E 3 .   ? -13.461 -3.996  44.591  1.00 51.38  ?  1    NAG C C7  1 
HETATM 7682 C C8  . NAG E 3 .   ? -12.131 -4.526  45.031  1.00 53.53  ?  1    NAG C C8  1 
HETATM 7683 N N2  . NAG E 3 .   ? -14.336 -3.730  45.566  1.00 50.85  ?  1    NAG C N2  1 
HETATM 7684 O O3  . NAG E 3 .   ? -15.198 -1.156  46.466  1.00 51.36  ?  1    NAG C O3  1 
HETATM 7685 O O4  . NAG E 3 .   ? -17.975 -1.141  47.465  1.00 61.13  ?  1    NAG C O4  1 
HETATM 7686 O O5  . NAG E 3 .   ? -17.980 -3.786  44.957  1.00 51.66  ?  1    NAG C O5  1 
HETATM 7687 O O6  . NAG E 3 .   ? -19.973 -2.052  44.425  1.00 73.43  ?  1    NAG C O6  1 
HETATM 7688 O O7  . NAG E 3 .   ? -13.732 -3.819  43.408  1.00 67.76  ?  1    NAG C O7  1 
HETATM 7689 C C1  . NAG E 3 .   ? -17.675 0.269   47.446  1.00 61.29  ?  2    NAG C C1  1 
HETATM 7690 C C2  . NAG E 3 .   ? -18.777 1.026   48.180  1.00 67.30  ?  2    NAG C C2  1 
HETATM 7691 C C3  . NAG E 3 .   ? -18.440 2.515   48.252  1.00 67.81  ?  2    NAG C C3  1 
HETATM 7692 C C4  . NAG E 3 .   ? -17.039 2.739   48.809  1.00 62.78  ?  2    NAG C C4  1 
HETATM 7693 C C5  . NAG E 3 .   ? -16.020 1.876   48.065  1.00 66.74  ?  2    NAG C C5  1 
HETATM 7694 C C6  . NAG E 3 .   ? -14.638 1.919   48.676  1.00 55.97  ?  2    NAG C C6  1 
HETATM 7695 C C7  . NAG E 3 .   ? -21.012 0.011   47.998  1.00 77.19  ?  2    NAG C C7  1 
HETATM 7696 C C8  . NAG E 3 .   ? -20.690 -0.714  49.271  1.00 57.83  ?  2    NAG C C8  1 
HETATM 7697 N N2  . NAG E 3 .   ? -20.062 0.827   47.528  1.00 62.95  ?  2    NAG C N2  1 
HETATM 7698 O O3  . NAG E 3 .   ? -19.398 3.175   49.072  1.00 81.97  ?  2    NAG C O3  1 
HETATM 7699 O O4  . NAG E 3 .   ? -16.696 4.108   48.626  1.00 84.20  ?  2    NAG C O4  1 
HETATM 7700 O O5  . NAG E 3 .   ? -16.430 0.502   48.085  1.00 61.33  ?  2    NAG C O5  1 
HETATM 7701 O O6  . NAG E 3 .   ? -13.852 0.809   48.264  1.00 72.26  ?  2    NAG C O6  1 
HETATM 7702 O O7  . NAG E 3 .   ? -22.085 -0.134  47.421  1.00 84.81  ?  2    NAG C O7  1 
HETATM 7703 C C1  . BMA E 3 .   ? -16.231 4.737   49.841  1.00 76.72  ?  3    BMA C C1  1 
HETATM 7704 C C2  . BMA E 3 .   ? -15.246 5.820   49.380  1.00 89.87  ?  3    BMA C C2  1 
HETATM 7705 C C3  . BMA E 3 .   ? -14.783 6.667   50.553  1.00 99.70  ?  3    BMA C C3  1 
HETATM 7706 C C4  . BMA E 3 .   ? -15.963 7.136   51.423  1.00 96.34  ?  3    BMA C C4  1 
HETATM 7707 C C5  . BMA E 3 .   ? -16.912 5.973   51.780  1.00 93.65  ?  3    BMA C C5  1 
HETATM 7708 C C6  . BMA E 3 .   ? -18.184 6.476   52.417  1.00 108.19 ?  3    BMA C C6  1 
HETATM 7709 O O2  . BMA E 3 .   ? -15.883 6.710   48.472  1.00 102.93 ?  3    BMA C O2  1 
HETATM 7710 O O3  . BMA E 3 .   ? -14.071 7.802   50.078  1.00 108.04 ?  3    BMA C O3  1 
HETATM 7711 O O4  . BMA E 3 .   ? -15.476 7.732   52.618  1.00 115.05 ?  3    BMA C O4  1 
HETATM 7712 O O5  . BMA E 3 .   ? -17.300 5.297   50.573  1.00 82.15  ?  3    BMA C O5  1 
HETATM 7713 O O6  . BMA E 3 .   ? -18.776 7.354   51.463  1.00 115.33 ?  3    BMA C O6  1 
HETATM 7714 C C1  . MAN E 3 .   ? -12.704 7.757   50.538  1.00 111.89 ?  4    MAN C C1  1 
HETATM 7715 C C2  . MAN E 3 .   ? -12.144 9.207   50.411  1.00 118.91 ?  4    MAN C C2  1 
HETATM 7716 C C3  . MAN E 3 .   ? -11.795 9.545   48.954  1.00 110.95 ?  4    MAN C C3  1 
HETATM 7717 C C4  . MAN E 3 .   ? -10.968 8.429   48.310  1.00 97.10  ?  4    MAN C C4  1 
HETATM 7718 C C5  . MAN E 3 .   ? -11.747 7.120   48.398  1.00 106.30 ?  4    MAN C C5  1 
HETATM 7719 C C6  . MAN E 3 .   ? -11.015 5.952   47.772  1.00 76.04  ?  4    MAN C C6  1 
HETATM 7720 O O2  . MAN E 3 .   ? -10.941 9.390   51.173  1.00 121.82 ?  4    MAN C O2  1 
HETATM 7721 O O3  . MAN E 3 .   ? -11.112 10.791  48.848  1.00 104.19 ?  4    MAN C O3  1 
HETATM 7722 O O4  . MAN E 3 .   ? -10.713 8.739   46.949  1.00 84.64  ?  4    MAN C O4  1 
HETATM 7723 O O5  . MAN E 3 .   ? -11.948 6.807   49.792  1.00 108.94 ?  4    MAN C O5  1 
HETATM 7724 O O6  . MAN E 3 .   ? -11.954 4.902   47.560  1.00 74.85  ?  4    MAN C O6  1 
HETATM 7725 C C1  . MAN E 3 .   ? -11.279 9.874   52.495  1.00 130.73 ?  5    MAN C C1  1 
HETATM 7726 C C2  . MAN E 3 .   ? -12.132 11.163  52.346  1.00 129.17 ?  5    MAN C C2  1 
HETATM 7727 C C3  . MAN E 3 .   ? -11.575 12.262  53.235  1.00 127.97 ?  5    MAN C C3  1 
HETATM 7728 C C4  . MAN E 3 .   ? -11.325 11.728  54.645  1.00 132.01 ?  5    MAN C C4  1 
HETATM 7729 C C5  . MAN E 3 .   ? -10.272 10.602  54.600  1.00 124.70 ?  5    MAN C C5  1 
HETATM 7730 C C6  . MAN E 3 .   ? -10.622 9.413   55.473  1.00 121.92 ?  5    MAN C C6  1 
HETATM 7731 O O2  . MAN E 3 .   ? -13.470 10.946  52.802  1.00 122.77 ?  5    MAN C O2  1 
HETATM 7732 O O3  . MAN E 3 .   ? -12.443 13.389  53.283  1.00 126.26 ?  5    MAN C O3  1 
HETATM 7733 O O4  . MAN E 3 .   ? -10.851 12.777  55.476  1.00 134.95 ?  5    MAN C O4  1 
HETATM 7734 O O5  . MAN E 3 .   ? -10.095 10.117  53.239  1.00 126.40 ?  5    MAN C O5  1 
HETATM 7735 O O6  . MAN E 3 .   ? -11.545 9.848   56.465  1.00 125.82 ?  5    MAN C O6  1 
HETATM 7736 C C1  . MAN E 3 .   ? -19.695 8.280   52.083  1.00 122.25 ?  6    MAN C C1  1 
HETATM 7737 C C2  . MAN E 3 .   ? -20.213 9.203   50.945  1.00 121.17 ?  6    MAN C C2  1 
HETATM 7738 C C3  . MAN E 3 .   ? -19.122 10.190  50.528  1.00 122.23 ?  6    MAN C C3  1 
HETATM 7739 C C4  . MAN E 3 .   ? -18.591 10.957  51.745  1.00 126.30 ?  6    MAN C C4  1 
HETATM 7740 C C5  . MAN E 3 .   ? -18.041 9.965   52.775  1.00 124.97 ?  6    MAN C C5  1 
HETATM 7741 C C6  . MAN E 3 .   ? -17.566 10.635  54.050  1.00 115.07 ?  6    MAN C C6  1 
HETATM 7742 O O2  . MAN E 3 .   ? -21.315 9.999   51.380  1.00 121.46 ?  6    MAN C O2  1 
HETATM 7743 O O3  . MAN E 3 .   ? -19.579 11.100  49.530  1.00 107.93 ?  6    MAN C O3  1 
HETATM 7744 O O4  . MAN E 3 .   ? -17.553 11.833  51.345  1.00 120.55 ?  6    MAN C O4  1 
HETATM 7745 O O5  . MAN E 3 .   ? -19.082 9.021   53.146  1.00 129.49 ?  6    MAN C O5  1 
HETATM 7746 O O6  . MAN E 3 .   ? -17.293 9.617   55.014  1.00 102.35 ?  6    MAN C O6  1 
HETATM 7747 C C1  . NAG F 4 .   ? -5.728  -4.534  20.916  1.00 73.75  ?  1    NAG D C1  1 
HETATM 7748 C C2  . NAG F 4 .   ? -6.262  -3.314  20.173  1.00 76.66  ?  1    NAG D C2  1 
HETATM 7749 C C3  . NAG F 4 .   ? -5.530  -3.141  18.844  1.00 83.24  ?  1    NAG D C3  1 
HETATM 7750 C C4  . NAG F 4 .   ? -4.017  -3.146  19.041  1.00 75.11  ?  1    NAG D C4  1 
HETATM 7751 C C5  . NAG F 4 .   ? -3.580  -4.338  19.893  1.00 81.18  ?  1    NAG D C5  1 
HETATM 7752 C C6  . NAG F 4 .   ? -2.120  -4.296  20.282  1.00 71.75  ?  1    NAG D C6  1 
HETATM 7753 C C7  . NAG F 4 .   ? -8.527  -2.378  20.028  1.00 93.60  ?  1    NAG D C7  1 
HETATM 7754 C C8  . NAG F 4 .   ? -9.975  -2.672  19.773  1.00 81.00  ?  1    NAG D C8  1 
HETATM 7755 N N2  . NAG F 4 .   ? -7.696  -3.423  19.955  1.00 77.55  ?  1    NAG D N2  1 
HETATM 7756 O O3  . NAG F 4 .   ? -5.932  -1.915  18.243  1.00 89.35  ?  1    NAG D O3  1 
HETATM 7757 O O4  . NAG F 4 .   ? -3.398  -3.257  17.764  1.00 89.83  ?  1    NAG D O4  1 
HETATM 7758 O O5  . NAG F 4 .   ? -4.329  -4.390  21.117  1.00 81.13  ?  1    NAG D O5  1 
HETATM 7759 O O6  . NAG F 4 .   ? -1.777  -3.056  20.885  1.00 93.47  ?  1    NAG D O6  1 
HETATM 7760 O O7  . NAG F 4 .   ? -8.129  -1.247  20.290  1.00 77.54  ?  1    NAG D O7  1 
HETATM 7761 C C1  . NAG F 4 .   ? -2.435  -2.216  17.507  1.00 97.66  ?  2    NAG D C1  1 
HETATM 7762 C C2  . NAG F 4 .   ? -1.395  -2.783  16.547  1.00 100.20 ?  2    NAG D C2  1 
HETATM 7763 C C3  . NAG F 4 .   ? -0.347  -1.725  16.219  1.00 103.10 ?  2    NAG D C3  1 
HETATM 7764 C C4  . NAG F 4 .   ? -1.018  -0.461  15.698  1.00 110.01 ?  2    NAG D C4  1 
HETATM 7765 C C5  . NAG F 4 .   ? -2.090  0.015   16.677  1.00 105.32 ?  2    NAG D C5  1 
HETATM 7766 C C6  . NAG F 4 .   ? -2.891  1.184   16.151  1.00 102.37 ?  2    NAG D C6  1 
HETATM 7767 C C7  . NAG F 4 .   ? -1.121  -5.214  16.729  1.00 95.44  ?  2    NAG D C7  1 
HETATM 7768 C C8  . NAG F 4 .   ? -0.370  -6.331  17.389  1.00 98.14  ?  2    NAG D C8  1 
HETATM 7769 N N2  . NAG F 4 .   ? -0.767  -3.976  17.090  1.00 92.48  ?  2    NAG D N2  1 
HETATM 7770 O O3  . NAG F 4 .   ? 0.555   -2.237  15.244  1.00 115.01 ?  2    NAG D O3  1 
HETATM 7771 O O4  . NAG F 4 .   ? -0.049  0.566   15.525  1.00 115.59 ?  2    NAG D O4  1 
HETATM 7772 O O5  . NAG F 4 .   ? -3.026  -1.042  16.942  1.00 102.75 ?  2    NAG D O5  1 
HETATM 7773 O O6  . NAG F 4 .   ? -4.065  0.748   15.480  1.00 96.08  ?  2    NAG D O6  1 
HETATM 7774 O O7  . NAG F 4 .   ? -2.009  -5.423  15.908  1.00 84.62  ?  2    NAG D O7  1 
HETATM 7775 C C1  . NAG G 4 .   ? 24.829  16.604  59.698  1.00 96.24  ?  1    NAG E C1  1 
HETATM 7776 C C2  . NAG G 4 .   ? 25.015  18.061  59.276  1.00 97.30  ?  1    NAG E C2  1 
HETATM 7777 C C3  . NAG G 4 .   ? 25.658  18.138  57.891  1.00 107.21 ?  1    NAG E C3  1 
HETATM 7778 C C4  . NAG G 4 .   ? 26.927  17.296  57.823  1.00 111.20 ?  1    NAG E C4  1 
HETATM 7779 C C5  . NAG G 4 .   ? 26.646  15.878  58.324  1.00 109.66 ?  1    NAG E C5  1 
HETATM 7780 C C6  . NAG G 4 .   ? 27.881  15.012  58.429  1.00 111.32 ?  1    NAG E C6  1 
HETATM 7781 C C7  . NAG G 4 .   ? 23.629  20.064  59.594  1.00 90.47  ?  1    NAG E C7  1 
HETATM 7782 C C8  . NAG G 4 .   ? 22.242  20.628  59.549  1.00 81.07  ?  1    NAG E C8  1 
HETATM 7783 N N2  . NAG G 4 .   ? 23.744  18.768  59.285  1.00 91.74  ?  1    NAG E N2  1 
HETATM 7784 O O3  . NAG G 4 .   ? 25.960  19.495  57.584  1.00 108.78 ?  1    NAG E O3  1 
HETATM 7785 O O4  . NAG G 4 .   ? 27.359  17.251  56.466  1.00 119.39 ?  1    NAG E O4  1 
HETATM 7786 O O5  . NAG G 4 .   ? 26.076  15.928  59.639  1.00 103.55 ?  1    NAG E O5  1 
HETATM 7787 O O6  . NAG G 4 .   ? 27.611  13.807  59.132  1.00 113.20 ?  1    NAG E O6  1 
HETATM 7788 O O7  . NAG G 4 .   ? 24.600  20.748  59.898  1.00 107.68 ?  1    NAG E O7  1 
HETATM 7789 C C1  . NAG G 4 .   ? 28.779  17.469  56.288  1.00 125.12 ?  2    NAG E C1  1 
HETATM 7790 C C2  . NAG G 4 .   ? 29.085  17.193  54.817  1.00 126.71 ?  2    NAG E C2  1 
HETATM 7791 C C3  . NAG G 4 .   ? 30.575  17.373  54.541  1.00 128.96 ?  2    NAG E C3  1 
HETATM 7792 C C4  . NAG G 4 .   ? 31.037  18.746  55.012  1.00 126.30 ?  2    NAG E C4  1 
HETATM 7793 C C5  . NAG G 4 .   ? 30.641  18.975  56.471  1.00 128.33 ?  2    NAG E C5  1 
HETATM 7794 C C6  . NAG G 4 .   ? 30.960  20.369  56.958  1.00 117.89 ?  2    NAG E C6  1 
HETATM 7795 C C7  . NAG G 4 .   ? 29.057  14.722  54.940  1.00 116.37 ?  2    NAG E C7  1 
HETATM 7796 C C8  . NAG G 4 .   ? 28.454  13.474  54.369  1.00 104.55 ?  2    NAG E C8  1 
HETATM 7797 N N2  . NAG G 4 .   ? 28.631  15.873  54.404  1.00 120.09 ?  2    NAG E N2  1 
HETATM 7798 O O3  . NAG G 4 .   ? 30.822  17.225  53.147  1.00 127.54 ?  2    NAG E O3  1 
HETATM 7799 O O4  . NAG G 4 .   ? 32.451  18.852  54.887  1.00 121.97 ?  2    NAG E O4  1 
HETATM 7800 O O5  . NAG G 4 .   ? 29.225  18.789  56.638  1.00 126.53 ?  2    NAG E O5  1 
HETATM 7801 O O6  . NAG G 4 .   ? 31.018  21.295  55.882  1.00 118.59 ?  2    NAG E O6  1 
HETATM 7802 O O7  . NAG G 4 .   ? 29.890  14.684  55.842  1.00 115.21 ?  2    NAG E O7  1 
HETATM 7803 C C1  . GOL H 5 .   ? -2.586  -2.875  43.435  1.00 91.84  ?  1001 GOL A C1  1 
HETATM 7804 O O1  . GOL H 5 .   ? -2.343  -3.243  42.114  1.00 79.70  ?  1001 GOL A O1  1 
HETATM 7805 C C2  . GOL H 5 .   ? -1.490  -3.545  44.294  1.00 70.69  ?  1001 GOL A C2  1 
HETATM 7806 O O2  . GOL H 5 .   ? -0.216  -3.150  43.913  1.00 68.67  ?  1001 GOL A O2  1 
HETATM 7807 C C3  . GOL H 5 .   ? -1.822  -3.139  45.746  1.00 67.72  ?  1001 GOL A C3  1 
HETATM 7808 O O3  . GOL H 5 .   ? -0.840  -3.707  46.552  1.00 59.84  ?  1001 GOL A O3  1 
HETATM 7809 O O   . HOH I 6 .   ? -4.033  -23.388 52.336  1.00 59.10  ?  1101 HOH A O   1 
HETATM 7810 O O   . HOH I 6 .   ? -6.053  -21.920 50.609  1.00 62.57  ?  1102 HOH A O   1 
HETATM 7811 O O   . HOH I 6 .   ? -11.017 -25.462 32.564  1.00 59.54  ?  1103 HOH A O   1 
HETATM 7812 O O   . HOH I 6 .   ? -1.936  -25.083 40.057  1.00 58.13  ?  1104 HOH A O   1 
HETATM 7813 O O   . HOH I 6 .   ? -23.838 -11.590 45.108  1.00 57.50  ?  1105 HOH A O   1 
HETATM 7814 O O   . HOH I 6 .   ? -4.121  -0.773  38.686  1.00 57.97  ?  1106 HOH A O   1 
HETATM 7815 O O   . HOH I 6 .   ? -30.985 -7.388  18.450  1.00 70.88  ?  1107 HOH A O   1 
HETATM 7816 O O   . HOH I 6 .   ? -8.740  -8.499  31.560  1.00 58.64  ?  1108 HOH A O   1 
HETATM 7817 O O   . HOH I 6 .   ? -8.648  -4.956  41.066  1.00 57.56  ?  1109 HOH A O   1 
HETATM 7818 O O   . HOH I 6 .   ? 20.007  -22.778 45.511  1.00 72.64  ?  1110 HOH A O   1 
HETATM 7819 O O   . HOH I 6 .   ? -7.111  3.728   22.420  1.00 63.29  ?  1111 HOH A O   1 
HETATM 7820 O O   . HOH J 6 .   ? 35.276  28.116  81.567  1.00 73.15  ?  1201 HOH B O   1 
HETATM 7821 O O   . HOH J 6 .   ? -1.339  13.375  59.380  1.00 69.62  ?  1202 HOH B O   1 
HETATM 7822 O O   . HOH J 6 .   ? -12.064 6.639   34.326  1.00 59.49  ?  1203 HOH B O   1 
HETATM 7823 O O   . HOH J 6 .   ? -12.242 6.650   24.973  1.00 58.32  ?  1204 HOH B O   1 
HETATM 7824 O O   . HOH J 6 .   ? -3.240  16.132  30.531  1.00 53.16  ?  1205 HOH B O   1 
HETATM 7825 O O   . HOH J 6 .   ? 43.389  19.029  86.644  1.00 77.03  ?  1206 HOH B O   1 
HETATM 7826 O O   . HOH J 6 .   ? -1.186  15.959  56.464  1.00 63.41  ?  1207 HOH B O   1 
HETATM 7827 O O   . HOH J 6 .   ? -1.349  17.781  59.889  1.00 70.03  ?  1208 HOH B O   1 
HETATM 7828 O O   . HOH J 6 .   ? -9.545  11.839  46.389  1.00 64.51  ?  1209 HOH B O   1 
HETATM 7829 O O   . HOH J 6 .   ? 33.264  30.485  82.838  1.00 73.21  ?  1210 HOH B O   1 
HETATM 7830 O O   . HOH J 6 .   ? -11.362 18.612  20.651  1.00 65.06  ?  1211 HOH B O   1 
HETATM 7831 O O   . HOH J 6 .   ? -12.377 -1.069  45.067  1.00 53.52  ?  1212 HOH B O   1 
HETATM 7832 O O   . HOH J 6 .   ? -3.715  13.095  57.971  1.00 58.90  ?  1213 HOH B O   1 
HETATM 7833 O O   . HOH K 6 .   ? -26.216 -2.167  37.184  1.00 83.26  ?  301  HOH H O   1 
HETATM 7834 O O   . HOH L 6 .   ? -37.551 3.378   5.443   1.00 72.94  ?  201  HOH L O   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   . ASN A 9   ? 1.4295 1.5755 1.0581 0.3652  0.2099  0.1623  26   ASN A N   
2    C CA  . ASN A 9   ? 1.5838 1.7324 1.2752 0.3293  0.2117  0.1753  26   ASN A CA  
3    C C   . ASN A 9   ? 1.5520 1.6785 1.2569 0.3054  0.1970  0.1522  26   ASN A C   
4    O O   . ASN A 9   ? 1.3634 1.4644 1.0328 0.3069  0.1795  0.1213  26   ASN A O   
5    C CB  . ASN A 9   ? 1.5338 1.6729 1.2404 0.3092  0.2028  0.1735  26   ASN A CB  
6    C CG  . ASN A 9   ? 1.5287 1.6739 1.3002 0.2779  0.2062  0.1909  26   ASN A CG  
7    O OD1 . ASN A 9   ? 1.5125 1.6760 1.3219 0.2747  0.2189  0.2123  26   ASN A OD1 
8    N ND2 . ASN A 9   ? 1.4584 1.5881 1.2438 0.2556  0.1938  0.1815  26   ASN A ND2 
9    N N   . LEU A 10  ? 1.5668 1.7034 1.3249 0.2839  0.2032  0.1678  27   LEU A N   
10   C CA  . LEU A 10  ? 1.4601 1.5797 1.2342 0.2623  0.1912  0.1495  27   LEU A CA  
11   C C   . LEU A 10  ? 1.4433 1.5571 1.2681 0.2278  0.1837  0.1518  27   LEU A C   
12   O O   . LEU A 10  ? 1.3452 1.4733 1.2035 0.2213  0.1916  0.1739  27   LEU A O   
13   C CB  . LEU A 10  ? 1.4543 1.5922 1.2389 0.2750  0.2046  0.1635  27   LEU A CB  
14   C CG  . LEU A 10  ? 1.4579 1.6236 1.3033 0.2653  0.2203  0.1970  27   LEU A CG  
15   C CD1 . LEU A 10  ? 1.3112 1.4897 1.1629 0.2757  0.2291  0.2038  27   LEU A CD1 
16   C CD2 . LEU A 10  ? 1.4291 1.6239 1.2886 0.2813  0.2397  0.2315  27   LEU A CD2 
17   N N   . ASN A 11  ? 1.2469 1.3392 1.0769 0.2071  0.1677  0.1286  28   ASN A N   
18   C CA  . ASN A 11  ? 1.2020 1.2853 1.0722 0.1768  0.1574  0.1248  28   ASN A CA  
19   C C   . ASN A 11  ? 1.2005 1.2797 1.0910 0.1641  0.1522  0.1174  28   ASN A C   
20   O O   . ASN A 11  ? 1.2490 1.3161 1.1108 0.1699  0.1462  0.0994  28   ASN A O   
21   C CB  . ASN A 11  ? 1.2604 1.3189 1.1098 0.1644  0.1401  0.1005  28   ASN A CB  
22   C CG  . ASN A 11  ? 1.3085 1.3635 1.1136 0.1844  0.1401  0.0952  28   ASN A CG  
23   O OD1 . ASN A 11  ? 1.1508 1.1969 0.9165 0.2005  0.1358  0.0804  28   ASN A OD1 
24   N ND2 . ASN A 11  ? 1.3667 1.4278 1.1782 0.1843  0.1436  0.1065  28   ASN A ND2 
25   N N   . GLU A 12  ? 1.0993 1.1878 1.0401 0.1472  0.1530  0.1307  29   GLU A N   
26   C CA  . GLU A 12  ? 1.0698 1.1574 1.0337 0.1362  0.1481  0.1261  29   GLU A CA  
27   C C   . GLU A 12  ? 0.9927 1.0563 0.9549 0.1153  0.1287  0.1001  29   GLU A C   
28   O O   . GLU A 12  ? 1.0444 1.1024 1.0299 0.0994  0.1206  0.0986  29   GLU A O   
29   C CB  . GLU A 12  ? 1.1292 1.2384 1.1509 0.1289  0.1556  0.1524  29   GLU A CB  
30   C CG  . GLU A 12  ? 1.1975 1.3072 1.2447 0.1185  0.1494  0.1479  29   GLU A CG  
31   C CD  . GLU A 12  ? 1.3265 1.4464 1.4360 0.1018  0.1454  0.1637  29   GLU A CD  
32   O OE1 . GLU A 12  ? 1.3673 1.4854 1.4982 0.0930  0.1421  0.1701  29   GLU A OE1 
33   O OE2 . GLU A 12  ? 1.2596 1.3886 1.3981 0.0978  0.1444  0.1692  29   GLU A OE2 
34   N N   . LEU A 13  ? 1.0901 1.1401 1.0255 0.1166  0.1215  0.0806  30   LEU A N   
35   C CA  . LEU A 13  ? 0.9372 0.9687 0.8733 0.0991  0.1053  0.0595  30   LEU A CA  
36   C C   . LEU A 13  ? 0.8841 0.9228 0.8524 0.0907  0.1034  0.0631  30   LEU A C   
37   O O   . LEU A 13  ? 1.0046 1.0490 0.9668 0.1000  0.1087  0.0651  30   LEU A O   
38   C CB  . LEU A 13  ? 0.8210 0.8341 0.7147 0.1047  0.0977  0.0386  30   LEU A CB  
39   C CG  . LEU A 13  ? 0.8214 0.8192 0.7150 0.0906  0.0840  0.0204  30   LEU A CG  
40   C CD1 . LEU A 13  ? 1.0255 1.0175 0.9363 0.0737  0.0747  0.0153  30   LEU A CD1 
41   C CD2 . LEU A 13  ? 0.9618 0.9423 0.8186 0.0971  0.0769  0.0036  30   LEU A CD2 
42   N N   . LYS A 14  ? 0.8899 0.9279 0.8920 0.0743  0.0948  0.0630  31   LYS A N   
43   C CA  . LYS A 14  ? 0.8888 0.9339 0.9258 0.0661  0.0903  0.0664  31   LYS A CA  
44   C C   . LYS A 14  ? 0.8901 0.9196 0.9139 0.0575  0.0764  0.0442  31   LYS A C   
45   O O   . LYS A 14  ? 0.9581 0.9742 0.9723 0.0492  0.0661  0.0303  31   LYS A O   
46   C CB  . LYS A 14  ? 0.7744 0.8270 0.8588 0.0551  0.0862  0.0787  31   LYS A CB  
47   C CG  . LYS A 14  ? 1.0265 1.0941 1.1553 0.0515  0.0858  0.0917  31   LYS A CG  
48   C CD  . LYS A 14  ? 1.0428 1.1143 1.2225 0.0395  0.0777  0.1021  31   LYS A CD  
49   C CE  . LYS A 14  ? 1.1158 1.2043 1.3451 0.0366  0.0771  0.1183  31   LYS A CE  
50   N NZ  . LYS A 14  ? 1.0683 1.1504 1.3426 0.0215  0.0574  0.1135  31   LYS A NZ  
51   N N   . MET A 15  ? 0.7143 0.7475 0.7380 0.0609  0.0769  0.0425  32   MET A N   
52   C CA  . MET A 15  ? 0.8951 0.9170 0.9092 0.0545  0.0652  0.0250  32   MET A CA  
53   C C   . MET A 15  ? 0.7476 0.7769 0.8010 0.0452  0.0564  0.0273  32   MET A C   
54   O O   . MET A 15  ? 0.7997 0.8420 0.8744 0.0483  0.0603  0.0375  32   MET A O   
55   C CB  . MET A 15  ? 0.7979 0.8175 0.7859 0.0649  0.0701  0.0208  32   MET A CB  
56   C CG  . MET A 15  ? 0.7868 0.7966 0.7365 0.0755  0.0754  0.0163  32   MET A CG  
57   S SD  . MET A 15  ? 0.8931 0.8817 0.8172 0.0671  0.0631  -0.0029 32   MET A SD  
58   C CE  . MET A 15  ? 0.9132 0.8930 0.8270 0.0661  0.0560  -0.0146 32   MET A CE  
59   N N   . GLU A 16  ? 0.7230 0.7441 0.7861 0.0352  0.0434  0.0173  33   GLU A N   
60   C CA  . GLU A 16  ? 0.7935 0.8185 0.8935 0.0273  0.0308  0.0162  33   GLU A CA  
61   C C   . GLU A 16  ? 0.7977 0.8192 0.8865 0.0276  0.0222  0.0027  33   GLU A C   
62   O O   . GLU A 16  ? 0.7843 0.7945 0.8505 0.0262  0.0139  -0.0129 33   GLU A O   
63   C CB  . GLU A 16  ? 0.8851 0.9013 0.9965 0.0195  0.0193  0.0093  33   GLU A CB  
64   C CG  . GLU A 16  ? 0.9387 0.9576 1.0580 0.0197  0.0282  0.0227  33   GLU A CG  
65   C CD  . GLU A 16  ? 0.9978 1.0072 1.1311 0.0124  0.0162  0.0161  33   GLU A CD  
66   O OE1 . GLU A 16  ? 1.0540 1.0558 1.1945 0.0082  -0.0001 0.0014  33   GLU A OE1 
67   O OE2 . GLU A 16  ? 1.1328 1.1423 1.2685 0.0125  0.0226  0.0253  33   GLU A OE2 
68   N N   . CYS A 17  ? 0.6897 0.7226 0.7951 0.0307  0.0250  0.0105  34   CYS A N   
69   C CA  . CYS A 17  ? 0.8057 0.8391 0.9037 0.0331  0.0199  0.0024  34   CYS A CA  
70   C C   . CYS A 17  ? 0.7926 0.8280 0.9203 0.0271  0.0021  -0.0045 34   CYS A C   
71   O O   . CYS A 17  ? 0.8209 0.8620 0.9874 0.0215  -0.0044 0.0028  34   CYS A O   
72   C CB  . CYS A 17  ? 0.7826 0.8288 0.8852 0.0410  0.0327  0.0160  34   CYS A CB  
73   S SG  . CYS A 17  ? 1.0022 1.0447 1.0658 0.0526  0.0510  0.0211  34   CYS A SG  
74   N N   . PRO A 18  ? 0.8464 0.8772 0.9578 0.0290  -0.0072 -0.0183 35   PRO A N   
75   C CA  . PRO A 18  ? 0.8009 0.8346 0.9380 0.0266  -0.0254 -0.0259 35   PRO A CA  
76   C C   . PRO A 18  ? 0.8742 0.9231 1.0446 0.0271  -0.0242 -0.0134 35   PRO A C   
77   O O   . PRO A 18  ? 0.9467 1.0034 1.1099 0.0320  -0.0088 -0.0020 35   PRO A O   
78   C CB  . PRO A 18  ? 0.8704 0.8970 0.9732 0.0319  -0.0318 -0.0419 35   PRO A CB  
79   C CG  . PRO A 18  ? 0.7607 0.7853 0.8318 0.0364  -0.0151 -0.0370 35   PRO A CG  
80   C CD  . PRO A 18  ? 0.8830 0.9057 0.9529 0.0343  -0.0025 -0.0271 35   PRO A CD  
81   N N   . HIS A 19  ? 0.8679 0.9208 1.0762 0.0227  -0.0418 -0.0160 36   HIS A N   
82   C CA  . HIS A 19  ? 0.8227 0.8917 1.0691 0.0223  -0.0429 -0.0033 36   HIS A CA  
83   C C   . HIS A 19  ? 0.8690 0.9416 1.0949 0.0294  -0.0429 -0.0095 36   HIS A C   
84   O O   . HIS A 19  ? 0.8563 0.9429 1.0983 0.0322  -0.0343 0.0040  36   HIS A O   
85   C CB  . HIS A 19  ? 0.8690 0.9399 1.1662 0.0150  -0.0652 -0.0051 36   HIS A CB  
86   C CG  . HIS A 19  ? 0.9911 1.0683 1.3311 0.0076  -0.0609 0.0137  36   HIS A CG  
87   N ND1 . HIS A 19  ? 0.9282 1.0252 1.3117 0.0060  -0.0515 0.0384  36   HIS A ND1 
88   C CD2 . HIS A 19  ? 0.9140 0.9818 1.2614 0.0024  -0.0639 0.0134  36   HIS A CD2 
89   C CE1 . HIS A 19  ? 0.8639 0.9641 1.2809 0.0000  -0.0484 0.0538  36   HIS A CE1 
90   N NE2 . HIS A 19  ? 0.8232 0.9049 1.2188 -0.0026 -0.0563 0.0384  36   HIS A NE2 
91   N N   . THR A 20  ? 0.8498 0.9114 1.0407 0.0335  -0.0514 -0.0280 37   THR A N   
92   C CA  . THR A 20  ? 0.8486 0.9132 1.0185 0.0409  -0.0513 -0.0331 37   THR A CA  
93   C C   . THR A 20  ? 0.9584 1.0176 1.0878 0.0458  -0.0317 -0.0297 37   THR A C   
94   O O   . THR A 20  ? 0.9649 1.0124 1.0617 0.0471  -0.0304 -0.0387 37   THR A O   
95   C CB  . THR A 20  ? 0.8564 0.9145 1.0119 0.0451  -0.0708 -0.0526 37   THR A CB  
96   O OG1 . THR A 20  ? 1.1033 1.1491 1.2211 0.0473  -0.0676 -0.0620 37   THR A OG1 
97   C CG2 . THR A 20  ? 0.8476 0.9062 1.0419 0.0407  -0.0938 -0.0595 37   THR A CG2 
98   N N   . ILE A 21  ? 0.8698 0.9375 1.0028 0.0494  -0.0173 -0.0163 38   ILE A N   
99   C CA  . ILE A 21  ? 0.9126 0.9731 1.0093 0.0554  -0.0015 -0.0144 38   ILE A CA  
100  C C   . ILE A 21  ? 0.9771 1.0370 1.0552 0.0621  -0.0026 -0.0193 38   ILE A C   
101  O O   . ILE A 21  ? 0.9553 1.0038 1.0013 0.0648  -0.0008 -0.0265 38   ILE A O   
102  C CB  . ILE A 21  ? 1.0409 1.1095 1.1467 0.0589  0.0154  0.0021  38   ILE A CB  
103  C CG1 . ILE A 21  ? 0.8882 0.9599 1.0163 0.0528  0.0171  0.0101  38   ILE A CG1 
104  C CG2 . ILE A 21  ? 1.0061 1.0638 1.0727 0.0666  0.0284  0.0008  38   ILE A CG2 
105  C CD1 . ILE A 21  ? 0.8995 0.9565 0.9988 0.0511  0.0209  0.0036  38   ILE A CD1 
106  N N   . GLY A 22  ? 0.9916 1.0645 1.0925 0.0649  -0.0057 -0.0139 39   GLY A N   
107  C CA  . GLY A 22  ? 0.8404 0.9141 0.9264 0.0719  -0.0071 -0.0173 39   GLY A CA  
108  C C   . GLY A 22  ? 0.9080 0.9756 0.9765 0.0728  -0.0205 -0.0312 39   GLY A C   
109  O O   . GLY A 22  ? 0.8516 0.9143 0.8946 0.0786  -0.0176 -0.0337 39   GLY A O   
110  N N   . LEU A 23  ? 0.9217 0.9899 1.0039 0.0685  -0.0354 -0.0396 40   LEU A N   
111  C CA  . LEU A 23  ? 0.8826 0.9460 0.9450 0.0725  -0.0481 -0.0532 40   LEU A CA  
112  C C   . LEU A 23  ? 0.8986 0.9504 0.9413 0.0694  -0.0462 -0.0589 40   LEU A C   
113  O O   . LEU A 23  ? 1.0105 1.0598 1.0406 0.0733  -0.0575 -0.0701 40   LEU A O   
114  C CB  . LEU A 23  ? 0.7268 0.7977 0.8146 0.0734  -0.0694 -0.0619 40   LEU A CB  
115  C CG  . LEU A 23  ? 0.7892 0.8733 0.8987 0.0769  -0.0742 -0.0571 40   LEU A CG  
116  C CD1 . LEU A 23  ? 0.7344 0.8239 0.8699 0.0779  -0.0992 -0.0680 40   LEU A CD1 
117  C CD2 . LEU A 23  ? 0.7240 0.8090 0.8038 0.0863  -0.0669 -0.0560 40   LEU A CD2 
118  N N   . GLY A 24  ? 0.8584 0.9039 0.8970 0.0642  -0.0324 -0.0515 41   GLY A N   
119  C CA  . GLY A 24  ? 0.9040 0.9392 0.9254 0.0611  -0.0302 -0.0558 41   GLY A CA  
120  C C   . GLY A 24  ? 0.8634 0.8911 0.8518 0.0651  -0.0222 -0.0562 41   GLY A C   
121  O O   . GLY A 24  ? 0.8696 0.8978 0.8487 0.0695  -0.0160 -0.0514 41   GLY A O   
122  N N   . GLN A 25  ? 0.7731 0.7940 0.7468 0.0636  -0.0230 -0.0608 42   GLN A N   
123  C CA  . GLN A 25  ? 0.8369 0.8521 0.7850 0.0665  -0.0168 -0.0594 42   GLN A CA  
124  C C   . GLN A 25  ? 0.7168 0.7232 0.6573 0.0609  -0.0120 -0.0593 42   GLN A C   
125  O O   . GLN A 25  ? 0.9369 0.9425 0.8872 0.0569  -0.0165 -0.0633 42   GLN A O   
126  C CB  . GLN A 25  ? 0.8073 0.8288 0.7428 0.0752  -0.0249 -0.0647 42   GLN A CB  
127  C CG  . GLN A 25  ? 0.8365 0.8617 0.7787 0.0777  -0.0390 -0.0758 42   GLN A CG  
128  C CD  . GLN A 25  ? 1.0340 1.0682 0.9644 0.0906  -0.0489 -0.0820 42   GLN A CD  
129  O OE1 . GLN A 25  ? 0.9525 0.9910 0.8658 0.0977  -0.0428 -0.0760 42   GLN A OE1 
130  N NE2 . GLN A 25  ? 0.9395 0.9766 0.8800 0.0948  -0.0652 -0.0938 42   GLN A NE2 
131  N N   . GLY A 26  ? 0.7022 0.7013 0.6273 0.0605  -0.0041 -0.0545 43   GLY A N   
132  C CA  . GLY A 26  ? 0.8474 0.8383 0.7649 0.0556  -0.0003 -0.0542 43   GLY A CA  
133  C C   . GLY A 26  ? 0.7622 0.7453 0.6818 0.0517  0.0068  -0.0507 43   GLY A C   
134  O O   . GLY A 26  ? 0.7631 0.7447 0.6836 0.0545  0.0113  -0.0471 43   GLY A O   
135  N N   . LEU A 27  ? 0.8482 0.8269 0.7671 0.0473  0.0080  -0.0517 44   LEU A N   
136  C CA  . LEU A 27  ? 0.7648 0.7370 0.6817 0.0462  0.0147  -0.0484 44   LEU A CA  
137  C C   . LEU A 27  ? 0.7767 0.7536 0.7083 0.0430  0.0150  -0.0473 44   LEU A C   
138  O O   . LEU A 27  ? 0.8193 0.8015 0.7630 0.0405  0.0081  -0.0506 44   LEU A O   
139  C CB  . LEU A 27  ? 0.7202 0.6812 0.6213 0.0445  0.0160  -0.0490 44   LEU A CB  
140  C CG  . LEU A 27  ? 0.8273 0.7819 0.7191 0.0464  0.0148  -0.0479 44   LEU A CG  
141  C CD1 . LEU A 27  ? 0.7101 0.6542 0.5933 0.0433  0.0137  -0.0479 44   LEU A CD1 
142  C CD2 . LEU A 27  ? 0.7581 0.7090 0.6485 0.0518  0.0177  -0.0462 44   LEU A CD2 
143  N N   . VAL A 28  ? 0.7648 0.7397 0.6954 0.0445  0.0223  -0.0422 45   VAL A N   
144  C CA  . VAL A 28  ? 0.7933 0.7727 0.7375 0.0421  0.0249  -0.0375 45   VAL A CA  
145  C C   . VAL A 28  ? 0.7006 0.6713 0.6274 0.0429  0.0292  -0.0373 45   VAL A C   
146  O O   . VAL A 28  ? 0.8325 0.7958 0.7414 0.0483  0.0328  -0.0380 45   VAL A O   
147  C CB  . VAL A 28  ? 0.8920 0.8824 0.8553 0.0459  0.0312  -0.0276 45   VAL A CB  
148  C CG1 . VAL A 28  ? 0.7482 0.7362 0.6950 0.0551  0.0397  -0.0242 45   VAL A CG1 
149  C CG2 . VAL A 28  ? 0.6949 0.6912 0.6754 0.0438  0.0350  -0.0191 45   VAL A CG2 
150  N N   . ILE A 29  ? 0.8134 0.7840 0.7457 0.0383  0.0274  -0.0374 46   ILE A N   
151  C CA  . ILE A 29  ? 0.7713 0.7341 0.6876 0.0385  0.0296  -0.0381 46   ILE A CA  
152  C C   . ILE A 29  ? 0.7775 0.7459 0.7068 0.0379  0.0338  -0.0306 46   ILE A C   
153  O O   . ILE A 29  ? 0.7830 0.7584 0.7362 0.0337  0.0311  -0.0275 46   ILE A O   
154  C CB  . ILE A 29  ? 0.7334 0.6896 0.6402 0.0337  0.0226  -0.0456 46   ILE A CB  
155  C CG1 . ILE A 29  ? 0.7321 0.6801 0.6234 0.0340  0.0236  -0.0463 46   ILE A CG1 
156  C CG2 . ILE A 29  ? 0.6885 0.6498 0.6102 0.0291  0.0167  -0.0481 46   ILE A CG2 
157  C CD1 . ILE A 29  ? 0.8893 0.8335 0.7750 0.0294  0.0179  -0.0507 46   ILE A CD1 
158  N N   . GLY A 30  ? 0.8137 0.7787 0.7280 0.0430  0.0395  -0.0275 47   GLY A N   
159  C CA  . GLY A 30  ? 0.7083 0.6787 0.6318 0.0437  0.0445  -0.0188 47   GLY A CA  
160  C C   . GLY A 30  ? 0.8414 0.8035 0.7411 0.0474  0.0452  -0.0217 47   GLY A C   
161  O O   . GLY A 30  ? 0.7937 0.7461 0.6713 0.0511  0.0423  -0.0293 47   GLY A O   
162  N N   . SER A 31  ? 0.7341 0.6994 0.6405 0.0464  0.0476  -0.0157 48   SER A N   
163  C CA  . SER A 31  ? 0.7249 0.6837 0.6103 0.0503  0.0475  -0.0179 48   SER A CA  
164  C C   . SER A 31  ? 0.7736 0.7419 0.6674 0.0555  0.0560  -0.0045 48   SER A C   
165  O O   . SER A 31  ? 0.8254 0.8034 0.7473 0.0516  0.0594  0.0058  48   SER A O   
166  C CB  . SER A 31  ? 0.7172 0.6676 0.5994 0.0413  0.0382  -0.0273 48   SER A CB  
167  O OG  . SER A 31  ? 0.7739 0.7288 0.6781 0.0339  0.0362  -0.0248 48   SER A OG  
168  N N   . ILE A 32  ? 0.8172 0.7826 0.6878 0.0649  0.0585  -0.0041 49   ILE A N   
169  C CA  . ILE A 32  ? 0.7892 0.7652 0.6640 0.0727  0.0679  0.0105  49   ILE A CA  
170  C C   . ILE A 32  ? 0.9347 0.9032 0.7841 0.0779  0.0644  0.0050  49   ILE A C   
171  O O   . ILE A 32  ? 0.8849 0.8419 0.7088 0.0821  0.0570  -0.0077 49   ILE A O   
172  C CB  . ILE A 32  ? 0.8276 0.8168 0.7009 0.0876  0.0805  0.0237  49   ILE A CB  
173  C CG1 . ILE A 32  ? 0.8667 0.8708 0.7501 0.0960  0.0922  0.0435  49   ILE A CG1 
174  C CG2 . ILE A 32  ? 0.8018 0.7828 0.6386 0.1018  0.0790  0.0134  49   ILE A CG2 
175  C CD1 . ILE A 32  ? 1.0198 1.0433 0.9197 0.1068  0.1065  0.0635  49   ILE A CD1 
176  N N   . GLU A 33  ? 0.8809 0.8557 0.7402 0.0776  0.0683  0.0151  50   GLU A N   
177  C CA  . GLU A 33  ? 0.8898 0.8601 0.7271 0.0838  0.0657  0.0123  50   GLU A CA  
178  C C   . GLU A 33  ? 0.8854 0.8655 0.7033 0.1042  0.0760  0.0232  50   GLU A C   
179  O O   . GLU A 33  ? 0.8214 0.8173 0.6560 0.1106  0.0889  0.0416  50   GLU A O   
180  C CB  . GLU A 33  ? 0.9106 0.8826 0.7675 0.0741  0.0644  0.0177  50   GLU A CB  
181  C CG  . GLU A 33  ? 1.0730 1.0393 0.9526 0.0574  0.0564  0.0102  50   GLU A CG  
182  C CD  . GLU A 33  ? 1.1958 1.1497 1.0595 0.0512  0.0449  -0.0068 50   GLU A CD  
183  O OE1 . GLU A 33  ? 1.1692 1.1173 1.0088 0.0573  0.0410  -0.0126 50   GLU A OE1 
184  O OE2 . GLU A 33  ? 1.0404 0.9910 0.9168 0.0411  0.0391  -0.0135 50   GLU A OE2 
185  N N   . LEU A 34  ? 0.9323 0.9036 0.7161 0.1157  0.0698  0.0124  51   LEU A N   
186  C CA  . LEU A 34  ? 1.0123 0.9915 0.7692 0.1394  0.0774  0.0191  51   LEU A CA  
187  C C   . LEU A 34  ? 0.9862 0.9679 0.7312 0.1461  0.0770  0.0235  51   LEU A C   
188  O O   . LEU A 34  ? 0.9484 0.9213 0.6998 0.1326  0.0674  0.0160  51   LEU A O   
189  C CB  . LEU A 34  ? 1.0340 0.9996 0.7573 0.1516  0.0679  0.0015  51   LEU A CB  
190  C CG  . LEU A 34  ? 1.0034 0.9706 0.7313 0.1540  0.0724  0.0013  51   LEU A CG  
191  C CD1 . LEU A 34  ? 0.9572 0.9097 0.6503 0.1693  0.0623  -0.0161 51   LEU A CD1 
192  C CD2 . LEU A 34  ? 0.9663 0.9567 0.7080 0.1653  0.0920  0.0245  51   LEU A CD2 
193  N N   . PRO A 35  ? 0.9560 0.9514 0.6837 0.1683  0.0882  0.0368  52   PRO A N   
194  C CA  . PRO A 35  ? 0.9338 0.9328 0.6476 0.1771  0.0880  0.0417  52   PRO A CA  
195  C C   . PRO A 35  ? 1.0617 1.0413 0.7462 0.1781  0.0686  0.0181  52   PRO A C   
196  O O   . PRO A 35  ? 1.1311 1.0963 0.7976 0.1807  0.0571  -0.0001 52   PRO A O   
197  C CB  . PRO A 35  ? 1.0615 1.0796 0.7555 0.2058  0.1038  0.0591  52   PRO A CB  
198  C CG  . PRO A 35  ? 1.0554 1.0861 0.7740 0.2042  0.1170  0.0730  52   PRO A CG  
199  C CD  . PRO A 35  ? 1.0054 1.0174 0.7292 0.1869  0.1037  0.0519  52   PRO A CD  
200  N N   . PRO A 36  ? 1.0536 1.0321 0.7355 0.1759  0.0634  0.0182  53   PRO A N   
201  C CA  . PRO A 36  ? 1.0289 0.9896 0.6888 0.1752  0.0432  -0.0032 53   PRO A CA  
202  C C   . PRO A 36  ? 1.1137 1.0705 0.7302 0.2027  0.0365  -0.0131 53   PRO A C   
203  O O   . PRO A 36  ? 1.2204 1.1921 0.8180 0.2257  0.0486  0.0001  53   PRO A O   
204  C CB  . PRO A 36  ? 1.0638 1.0287 0.7355 0.1674  0.0425  0.0038  53   PRO A CB  
205  C CG  . PRO A 36  ? 1.1540 1.1396 0.8371 0.1765  0.0628  0.0292  53   PRO A CG  
206  C CD  . PRO A 36  ? 1.0706 1.0635 0.7732 0.1732  0.0749  0.0386  53   PRO A CD  
207  N N   . VAL A 37  ? 1.0838 1.0204 0.6851 0.2014  0.0164  -0.0361 54   VAL A N   
208  C CA  . VAL A 37  ? 1.1972 1.1243 0.7567 0.2273  0.0038  -0.0512 54   VAL A CA  
209  C C   . VAL A 37  ? 1.1258 1.0389 0.6768 0.2238  -0.0185 -0.0667 54   VAL A C   
210  O O   . VAL A 37  ? 0.9881 0.8938 0.5668 0.1988  -0.0271 -0.0705 54   VAL A O   
211  C CB  . VAL A 37  ? 1.1532 1.0662 0.7034 0.2312  -0.0038 -0.0658 54   VAL A CB  
212  C CG1 . VAL A 37  ? 1.0200 0.9458 0.5940 0.2230  0.0161  -0.0504 54   VAL A CG1 
213  C CG2 . VAL A 37  ? 1.0934 0.9829 0.6557 0.2121  -0.0275 -0.0861 54   VAL A CG2 
214  N N   . PRO A 38  ? 1.2704 1.1809 0.7844 0.2492  -0.0284 -0.0751 55   PRO A N   
215  C CA  . PRO A 38  ? 1.1215 1.0190 0.6301 0.2458  -0.0516 -0.0900 55   PRO A CA  
216  C C   . PRO A 38  ? 1.2122 1.0850 0.7318 0.2311  -0.0764 -0.1119 55   PRO A C   
217  O O   . PRO A 38  ? 1.1874 1.0503 0.7065 0.2314  -0.0787 -0.1196 55   PRO A O   
218  C CB  . PRO A 38  ? 1.1642 1.0641 0.6256 0.2815  -0.0573 -0.0958 55   PRO A CB  
219  C CG  . PRO A 38  ? 1.3875 1.2946 0.8262 0.3042  -0.0429 -0.0912 55   PRO A CG  
220  C CD  . PRO A 38  ? 1.2727 1.1945 0.7482 0.2840  -0.0183 -0.0699 55   PRO A CD  
221  N N   . LEU A 39  ? 1.2356 1.0995 0.7682 0.2182  -0.0952 -0.1202 56   LEU A N   
222  C CA  . LEU A 39  ? 1.2616 1.1057 0.8169 0.1995  -0.1173 -0.1352 56   LEU A CA  
223  C C   . LEU A 39  ? 1.2776 1.0995 0.8073 0.2176  -0.1406 -0.1581 56   LEU A C   
224  O O   . LEU A 39  ? 1.2296 1.0351 0.7784 0.2045  -0.1540 -0.1680 56   LEU A O   
225  C CB  . LEU A 39  ? 1.0417 0.8844 0.6181 0.1840  -0.1316 -0.1362 56   LEU A CB  
226  C CG  . LEU A 39  ? 1.0547 0.8979 0.6766 0.1526  -0.1308 -0.1295 56   LEU A CG  
227  C CD1 . LEU A 39  ? 1.0397 0.8999 0.6779 0.1414  -0.1023 -0.1107 56   LEU A CD1 
228  C CD2 . LEU A 39  ? 1.1689 1.0145 0.8091 0.1415  -0.1430 -0.1283 56   LEU A CD2 
229  N N   . ILE A 40  ? 1.2800 1.1007 0.7664 0.2489  -0.1464 -0.1668 57   ILE A N   
230  C CA  . ILE A 40  ? 1.3429 1.1399 0.8020 0.2692  -0.1724 -0.1919 57   ILE A CA  
231  C C   . ILE A 40  ? 1.3901 1.1819 0.8436 0.2748  -0.1631 -0.1937 57   ILE A C   
232  O O   . ILE A 40  ? 1.5467 1.3146 0.9984 0.2774  -0.1854 -0.2133 57   ILE A O   
233  C CB  . ILE A 40  ? 1.3677 1.1664 0.7768 0.3057  -0.1805 -0.2011 57   ILE A CB  
234  C CG1 . ILE A 40  ? 1.5264 1.3426 0.9394 0.3021  -0.1739 -0.1878 57   ILE A CG1 
235  C CG2 . ILE A 40  ? 1.3637 1.1325 0.7535 0.3207  -0.2195 -0.2321 57   ILE A CG2 
236  C CD1 . ILE A 40  ? 1.4325 1.2772 0.8255 0.3192  -0.1415 -0.1644 57   ILE A CD1 
237  N N   . GLN A 41  ? 1.3561 1.1698 0.8097 0.2763  -0.1315 -0.1732 58   GLN A N   
238  C CA  . GLN A 41  ? 1.3139 1.1269 0.7599 0.2848  -0.1200 -0.1725 58   GLN A CA  
239  C C   . GLN A 41  ? 1.3721 1.1794 0.8602 0.2539  -0.1170 -0.1686 58   GLN A C   
240  O O   . GLN A 41  ? 1.4774 1.2850 0.9639 0.2580  -0.1068 -0.1667 58   GLN A O   
241  C CB  . GLN A 41  ? 1.3335 1.1749 0.7646 0.3012  -0.0875 -0.1498 58   GLN A CB  
242  C CG  . GLN A 41  ? 1.3502 1.2035 0.7414 0.3326  -0.0850 -0.1473 58   GLN A CG  
243  C CD  . GLN A 41  ? 1.2881 1.1727 0.6740 0.3459  -0.0509 -0.1193 58   GLN A CD  
244  O OE1 . GLN A 41  ? 1.3464 1.2433 0.7621 0.3292  -0.0305 -0.1021 58   GLN A OE1 
245  N NE2 . GLN A 41  ? 1.2256 1.1242 0.5755 0.3768  -0.0452 -0.1134 58   GLN A NE2 
246  N N   . VAL A 42  ? 1.3238 1.1274 0.8487 0.2250  -0.1254 -0.1667 59   VAL A N   
247  C CA  . VAL A 42  ? 1.3249 1.1280 0.8890 0.1973  -0.1192 -0.1594 59   VAL A CA  
248  C C   . VAL A 42  ? 1.3050 1.0839 0.8723 0.1971  -0.1390 -0.1763 59   VAL A C   
249  O O   . VAL A 42  ? 1.3565 1.1361 0.9345 0.1912  -0.1285 -0.1718 59   VAL A O   
250  C CB  . VAL A 42  ? 1.3864 1.1948 0.9866 0.1701  -0.1216 -0.1511 59   VAL A CB  
251  C CG1 . VAL A 42  ? 1.1114 0.9186 0.7488 0.1450  -0.1179 -0.1451 59   VAL A CG1 
252  C CG2 . VAL A 42  ? 1.1400 0.9718 0.7405 0.1691  -0.1003 -0.1332 59   VAL A CG2 
253  N N   . GLU A 43  ? 1.3560 1.1126 0.9160 0.2036  -0.1690 -0.1959 60   GLU A N   
254  C CA  . GLU A 43  ? 1.4505 1.1813 1.0209 0.2010  -0.1917 -0.2119 60   GLU A CA  
255  C C   . GLU A 43  ? 1.4172 1.1400 0.9574 0.2243  -0.1879 -0.2207 60   GLU A C   
256  O O   . GLU A 43  ? 1.4081 1.1151 0.9638 0.2174  -0.1967 -0.2270 60   GLU A O   
257  C CB  . GLU A 43  ? 1.4889 1.1969 1.0578 0.2058  -0.2273 -0.2318 60   GLU A CB  
258  C CG  . GLU A 43  ? 1.6435 1.3615 1.2388 0.1867  -0.2312 -0.2229 60   GLU A CG  
259  C CD  . GLU A 43  ? 1.8062 1.5132 1.3787 0.2041  -0.2565 -0.2394 60   GLU A CD  
260  O OE1 . GLU A 43  ? 1.6573 1.3409 1.2054 0.2252  -0.2812 -0.2621 60   GLU A OE1 
261  O OE2 . GLU A 43  ? 1.6024 1.3239 1.1807 0.1978  -0.2524 -0.2305 60   GLU A OE2 
262  N N   . SER A 44  ? 1.3460 1.0808 0.8448 0.2524  -0.1741 -0.2197 61   SER A N   
263  C CA  . SER A 44  ? 1.3177 1.0484 0.7848 0.2785  -0.1685 -0.2265 61   SER A CA  
264  C C   . SER A 44  ? 1.3322 1.0879 0.8077 0.2737  -0.1341 -0.2040 61   SER A C   
265  O O   . SER A 44  ? 1.4780 1.2376 0.9268 0.2973  -0.1237 -0.2045 61   SER A O   
266  C CB  . SER A 44  ? 1.3707 1.1007 0.7849 0.3172  -0.1747 -0.2384 61   SER A CB  
267  O OG  . SER A 44  ? 1.5425 1.2976 0.9492 0.3199  -0.1571 -0.2219 61   SER A OG  
268  N N   . LEU A 45  ? 1.3346 1.1075 0.8467 0.2452  -0.1173 -0.1846 62   LEU A N   
269  C CA  . LEU A 45  ? 1.3128 1.1080 0.8381 0.2387  -0.0882 -0.1643 62   LEU A CA  
270  C C   . LEU A 45  ? 1.3457 1.1292 0.8847 0.2319  -0.0906 -0.1689 62   LEU A C   
271  O O   . LEU A 45  ? 1.3774 1.1437 0.9412 0.2129  -0.1074 -0.1767 62   LEU A O   
272  C CB  . LEU A 45  ? 1.2314 1.0447 0.7917 0.2112  -0.0740 -0.1457 62   LEU A CB  
273  C CG  . LEU A 45  ? 1.1516 0.9835 0.7033 0.2169  -0.0627 -0.1337 62   LEU A CG  
274  C CD1 . LEU A 45  ? 1.0431 0.8852 0.6318 0.1880  -0.0561 -0.1209 62   LEU A CD1 
275  C CD2 . LEU A 45  ? 1.1148 0.9689 0.6491 0.2371  -0.0379 -0.1179 62   LEU A CD2 
276  N N   . LYS A 46  ? 1.3420 1.1364 0.8666 0.2479  -0.0733 -0.1622 63   LYS A N   
277  C CA  . LYS A 46  ? 1.3028 1.0898 0.8396 0.2431  -0.0720 -0.1640 63   LYS A CA  
278  C C   . LYS A 46  ? 1.2527 1.0670 0.8040 0.2383  -0.0428 -0.1417 63   LYS A C   
279  O O   . LYS A 46  ? 1.2875 1.1222 0.8219 0.2562  -0.0249 -0.1297 63   LYS A O   
280  C CB  . LYS A 46  ? 1.3956 1.1635 0.8975 0.2726  -0.0853 -0.1827 63   LYS A CB  
281  C CG  . LYS A 46  ? 1.5726 1.3078 1.0655 0.2765  -0.1194 -0.2079 63   LYS A CG  
282  C CD  . LYS A 46  ? 1.6374 1.3512 1.1032 0.3022  -0.1327 -0.2267 63   LYS A CD  
283  C CE  . LYS A 46  ? 1.6827 1.3640 1.1302 0.3156  -0.1686 -0.2542 63   LYS A CE  
284  N NZ  . LYS A 46  ? 1.7042 1.3631 1.1219 0.3442  -0.1826 -0.2742 63   LYS A NZ  
285  N N   . LEU A 47  ? 1.1566 0.9722 0.7408 0.2151  -0.0387 -0.1353 64   LEU A N   
286  C CA  . LEU A 47  ? 1.1533 0.9921 0.7554 0.2091  -0.0150 -0.1163 64   LEU A CA  
287  C C   . LEU A 47  ? 1.1704 1.0067 0.7581 0.2273  -0.0109 -0.1194 64   LEU A C   
288  O O   . LEU A 47  ? 1.1620 0.9802 0.7559 0.2221  -0.0231 -0.1303 64   LEU A O   
289  C CB  . LEU A 47  ? 1.0218 0.8640 0.6631 0.1781  -0.0136 -0.1090 64   LEU A CB  
290  C CG  . LEU A 47  ? 1.1859 1.0514 0.8500 0.1693  0.0074  -0.0905 64   LEU A CG  
291  C CD1 . LEU A 47  ? 1.1687 1.0562 0.8302 0.1771  0.0238  -0.0752 64   LEU A CD1 
292  C CD2 . LEU A 47  ? 1.0637 0.9302 0.7609 0.1420  0.0054  -0.0867 64   LEU A CD2 
293  N N   . GLU A 48  ? 1.2032 1.0585 0.7731 0.2496  0.0068  -0.1085 65   GLU A N   
294  C CA  . GLU A 48  ? 1.2208 1.0780 0.7756 0.2705  0.0136  -0.1090 65   GLU A CA  
295  C C   . GLU A 48  ? 1.2604 1.1395 0.8475 0.2568  0.0331  -0.0894 65   GLU A C   
296  O O   . GLU A 48  ? 1.1527 1.0535 0.7631 0.2441  0.0475  -0.0712 65   GLU A O   
297  C CB  . GLU A 48  ? 1.2986 1.1668 0.8143 0.3066  0.0224  -0.1067 65   GLU A CB  
298  C CG  . GLU A 48  ? 1.3872 1.2369 0.8686 0.3228  0.0032  -0.1254 65   GLU A CG  
299  C CD  . GLU A 48  ? 1.5687 1.3855 1.0249 0.3377  -0.0220 -0.1530 65   GLU A CD  
300  O OE1 . GLU A 48  ? 1.5258 1.3273 1.0019 0.3225  -0.0306 -0.1598 65   GLU A OE1 
301  O OE2 . GLU A 48  ? 1.6589 1.4648 1.0754 0.3657  -0.0342 -0.1680 65   GLU A OE2 
302  N N   . SER A 49  ? 1.3032 1.1757 0.8927 0.2599  0.0321  -0.0937 66   SER A N   
303  C CA  . SER A 49  ? 1.2399 1.1300 0.8618 0.2453  0.0464  -0.0779 66   SER A CA  
304  C C   . SER A 49  ? 1.2289 1.1445 0.8458 0.2669  0.0676  -0.0609 66   SER A C   
305  O O   . SER A 49  ? 1.3198 1.2615 0.9547 0.2640  0.0845  -0.0403 66   SER A O   
306  C CB  . SER A 49  ? 1.4273 1.2982 1.0597 0.2342  0.0340  -0.0895 66   SER A CB  
307  O OG  . SER A 49  ? 1.3365 1.2248 0.9970 0.2235  0.0469  -0.0754 66   SER A OG  
308  N N   . SER A 50  ? 1.1243 1.0331 0.7198 0.2889  0.0668  -0.0683 67   SER A N   
309  C CA  . SER A 50  ? 1.2835 1.2172 0.8769 0.3101  0.0871  -0.0515 67   SER A CA  
310  C C   . SER A 50  ? 1.2782 1.2345 0.9167 0.2891  0.1009  -0.0313 67   SER A C   
311  O O   . SER A 50  ? 1.2539 1.2388 0.9041 0.3004  0.1206  -0.0097 67   SER A O   
312  C CB  . SER A 50  ? 1.2150 1.1700 0.7864 0.3362  0.1020  -0.0381 67   SER A CB  
313  O OG  . SER A 50  ? 1.2066 1.1858 0.8101 0.3193  0.1156  -0.0159 67   SER A OG  
314  N N   . CYS A 51  ? 1.3000 1.2449 0.9653 0.2597  0.0903  -0.0372 68   CYS A N   
315  C CA  . CYS A 51  ? 1.1386 1.1017 0.8448 0.2401  0.0992  -0.0219 68   CYS A CA  
316  C C   . CYS A 51  ? 1.1392 1.0972 0.8488 0.2432  0.0974  -0.0262 68   CYS A C   
317  O O   . CYS A 51  ? 1.3466 1.2835 1.0292 0.2572  0.0875  -0.0424 68   CYS A O   
318  C CB  . CYS A 51  ? 1.2436 1.2000 0.9753 0.2093  0.0895  -0.0250 68   CYS A CB  
319  S SG  . CYS A 51  ? 1.3942 1.3621 1.1343 0.2011  0.0943  -0.0149 68   CYS A SG  
320  N N   . ASN A 52  ? 1.1757 1.1522 0.9204 0.2300  0.1056  -0.0120 69   ASN A N   
321  C CA  . ASN A 52  ? 1.0523 1.0272 0.8055 0.2305  0.1045  -0.0138 69   ASN A CA  
322  C C   . ASN A 52  ? 1.0606 1.0233 0.8352 0.2035  0.0917  -0.0216 69   ASN A C   
323  O O   . ASN A 52  ? 1.0856 1.0622 0.8899 0.1911  0.0949  -0.0125 69   ASN A O   
324  C CB  . ASN A 52  ? 1.0517 1.0582 0.8289 0.2384  0.1226  0.0087  69   ASN A CB  
325  C CG  . ASN A 52  ? 1.2057 1.2120 0.9886 0.2430  0.1226  0.0075  69   ASN A CG  
326  O OD1 . ASN A 52  ? 1.5659 1.5484 1.3255 0.2494  0.1118  -0.0097 69   ASN A OD1 
327  N ND2 . ASN A 52  ? 1.3489 1.3818 1.1657 0.2394  0.1337  0.0263  69   ASN A ND2 
328  N N   . PHE A 53  ? 1.0785 1.0163 0.8384 0.1954  0.0765  -0.0380 70   PHE A N   
329  C CA  . PHE A 53  ? 1.0939 1.0193 0.8692 0.1745  0.0646  -0.0451 70   PHE A CA  
330  C C   . PHE A 53  ? 1.1198 1.0152 0.8733 0.1775  0.0486  -0.0628 70   PHE A C   
331  O O   . PHE A 53  ? 1.0315 0.9144 0.7575 0.1966  0.0453  -0.0717 70   PHE A O   
332  C CB  . PHE A 53  ? 1.0543 0.9887 0.8526 0.1527  0.0636  -0.0398 70   PHE A CB  
333  C CG  . PHE A 53  ? 1.0242 0.9560 0.8115 0.1522  0.0627  -0.0414 70   PHE A CG  
334  C CD1 . PHE A 53  ? 0.9812 0.9325 0.7854 0.1471  0.0720  -0.0286 70   PHE A CD1 
335  C CD2 . PHE A 53  ? 0.9945 0.9041 0.7581 0.1562  0.0512  -0.0552 70   PHE A CD2 
336  C CE1 . PHE A 53  ? 0.8487 0.7982 0.6436 0.1468  0.0715  -0.0290 70   PHE A CE1 
337  C CE2 . PHE A 53  ? 1.0718 0.9800 0.8257 0.1561  0.0499  -0.0565 70   PHE A CE2 
338  C CZ  . PHE A 53  ? 0.9890 0.9175 0.7575 0.1516  0.0608  -0.0431 70   PHE A CZ  
339  N N   . ASP A 54  ? 1.0472 0.9314 0.8143 0.1595  0.0379  -0.0674 71   ASP A N   
340  C CA  . ASP A 54  ? 0.9501 0.8068 0.7076 0.1588  0.0216  -0.0809 71   ASP A CA  
341  C C   . ASP A 54  ? 0.8930 0.7416 0.6524 0.1454  0.0125  -0.0851 71   ASP A C   
342  O O   . ASP A 54  ? 0.9592 0.8118 0.7383 0.1271  0.0101  -0.0807 71   ASP A O   
343  C CB  . ASP A 54  ? 0.9426 0.7954 0.7173 0.1499  0.0176  -0.0791 71   ASP A CB  
344  C CG  . ASP A 54  ? 1.1043 0.9292 0.8698 0.1565  0.0028  -0.0908 71   ASP A CG  
345  O OD1 . ASP A 54  ? 1.1529 0.9595 0.8994 0.1664  -0.0072 -0.1025 71   ASP A OD1 
346  O OD2 . ASP A 54  ? 1.1723 0.9933 0.9508 0.1524  0.0000  -0.0884 71   ASP A OD2 
347  N N   . LEU A 55  ? 0.9021 0.7401 0.6398 0.1565  0.0072  -0.0935 72   LEU A N   
348  C CA  . LEU A 55  ? 0.8967 0.7291 0.6354 0.1457  -0.0006 -0.0968 72   LEU A CA  
349  C C   . LEU A 55  ? 1.0157 0.8244 0.7614 0.1366  -0.0194 -0.1060 72   LEU A C   
350  O O   . LEU A 55  ? 1.1919 0.9795 0.9271 0.1476  -0.0312 -0.1168 72   LEU A O   
351  C CB  . LEU A 55  ? 0.9230 0.7541 0.6354 0.1627  0.0001  -0.1020 72   LEU A CB  
352  C CG  . LEU A 55  ? 0.9297 0.7594 0.6425 0.1530  -0.0056 -0.1036 72   LEU A CG  
353  C CD1 . LEU A 55  ? 0.9890 0.8443 0.7152 0.1443  0.0103  -0.0889 72   LEU A CD1 
354  C CD2 . LEU A 55  ? 1.0651 0.8803 0.7474 0.1720  -0.0152 -0.1161 72   LEU A CD2 
355  N N   . HIS A 56  ? 0.9988 0.8112 0.7641 0.1174  -0.0224 -0.1009 73   HIS A N   
356  C CA  . HIS A 56  ? 0.9216 0.7154 0.6995 0.1074  -0.0392 -0.1055 73   HIS A CA  
357  C C   . HIS A 56  ? 0.9227 0.7021 0.6869 0.1123  -0.0521 -0.1162 73   HIS A C   
358  O O   . HIS A 56  ? 1.2211 1.0117 0.9806 0.1095  -0.0467 -0.1135 73   HIS A O   
359  C CB  . HIS A 56  ? 0.9408 0.7483 0.7448 0.0877  -0.0355 -0.0935 73   HIS A CB  
360  C CG  . HIS A 56  ? 0.9466 0.7403 0.7709 0.0777  -0.0492 -0.0920 73   HIS A CG  
361  N ND1 . HIS A 56  ? 0.8757 0.6740 0.7192 0.0709  -0.0469 -0.0825 73   HIS A ND1 
362  C CD2 . HIS A 56  ? 0.9426 0.7194 0.7742 0.0736  -0.0655 -0.0970 73   HIS A CD2 
363  C CE1 . HIS A 56  ? 0.8704 0.6562 0.7335 0.0630  -0.0599 -0.0798 73   HIS A CE1 
364  N NE2 . HIS A 56  ? 0.8839 0.6560 0.7419 0.0638  -0.0721 -0.0887 73   HIS A NE2 
365  N N   . THR A 57  ? 0.9586 0.7120 0.7170 0.1200  -0.0706 -0.1288 74   THR A N   
366  C CA  . THR A 57  ? 1.0066 0.7435 0.7463 0.1304  -0.0856 -0.1428 74   THR A CA  
367  C C   . THR A 57  ? 1.0832 0.8103 0.8445 0.1145  -0.1018 -0.1433 74   THR A C   
368  O O   . THR A 57  ? 1.0025 0.7160 0.7508 0.1217  -0.1165 -0.1552 74   THR A O   
369  C CB  . THR A 57  ? 1.0508 0.7625 0.7700 0.1513  -0.1000 -0.1595 74   THR A CB  
370  O OG1 . THR A 57  ? 1.0324 0.7282 0.7752 0.1432  -0.1113 -0.1592 74   THR A OG1 
371  C CG2 . THR A 57  ? 1.1502 0.8740 0.8424 0.1719  -0.0831 -0.1590 74   THR A CG2 
372  N N   . SER A 58  ? 1.0244 0.7597 0.8181 0.0946  -0.0996 -0.1300 75   SER A N   
373  C CA  . SER A 58  ? 0.9702 0.6986 0.7890 0.0800  -0.1143 -0.1272 75   SER A CA  
374  C C   . SER A 58  ? 1.1231 0.8598 0.9319 0.0787  -0.1135 -0.1290 75   SER A C   
375  O O   . SER A 58  ? 1.0019 0.7240 0.8154 0.0776  -0.1322 -0.1367 75   SER A O   
376  C CB  . SER A 58  ? 0.9157 0.6591 0.7680 0.0619  -0.1064 -0.1087 75   SER A CB  
377  O OG  . SER A 58  ? 1.0498 0.7813 0.9175 0.0617  -0.1124 -0.1064 75   SER A OG  
378  N N   . THR A 59  ? 1.0426 0.8023 0.8396 0.0790  -0.0934 -0.1218 76   THR A N   
379  C CA  . THR A 59  ? 0.9757 0.7444 0.7643 0.0778  -0.0912 -0.1218 76   THR A CA  
380  C C   . THR A 59  ? 1.0499 0.8048 0.8081 0.0962  -0.1015 -0.1372 76   THR A C   
381  O O   . THR A 59  ? 1.0482 0.8065 0.8000 0.0961  -0.1043 -0.1387 76   THR A O   
382  C CB  . THR A 59  ? 0.9442 0.7388 0.7296 0.0748  -0.0684 -0.1104 76   THR A CB  
383  O OG1 . THR A 59  ? 1.1184 0.9174 0.8849 0.0887  -0.0569 -0.1119 76   THR A OG1 
384  C CG2 . THR A 59  ? 0.8747 0.6835 0.6872 0.0584  -0.0604 -0.0968 76   THR A CG2 
385  N N   . SER A 60  ? 1.1291 0.8688 0.8669 0.1138  -0.1074 -0.1488 77   SER A N   
386  C CA  . SER A 60  ? 1.1703 0.8976 0.8738 0.1361  -0.1170 -0.1644 77   SER A CA  
387  C C   . SER A 60  ? 1.0701 0.7685 0.7766 0.1388  -0.1474 -0.1810 77   SER A C   
388  O O   . SER A 60  ? 1.1817 0.8644 0.8575 0.1609  -0.1602 -0.1979 77   SER A O   
389  C CB  . SER A 60  ? 1.0335 0.7609 0.7102 0.1579  -0.1075 -0.1689 77   SER A CB  
390  O OG  . SER A 60  ? 1.2471 0.9589 0.9358 0.1566  -0.1156 -0.1727 77   SER A OG  
391  N N   . SER A 61  ? 1.1468 0.8383 0.8903 0.1183  -0.1598 -0.1759 78   SER A N   
392  C CA  . SER A 61  ? 1.1824 0.8469 0.9385 0.1176  -0.1907 -0.1893 78   SER A CA  
393  C C   . SER A 61  ? 1.1923 0.8626 0.9557 0.1093  -0.1981 -0.1879 78   SER A C   
394  O O   . SER A 61  ? 1.0997 0.7947 0.8641 0.1009  -0.1788 -0.1746 78   SER A O   
395  C CB  . SER A 61  ? 1.0603 0.7142 0.8586 0.1005  -0.2011 -0.1817 78   SER A CB  
396  O OG  . SER A 61  ? 1.2183 0.8926 1.0514 0.0774  -0.1908 -0.1612 78   SER A OG  
397  N N   . GLN A 62  ? 1.2331 0.8792 1.0032 0.1121  -0.2281 -0.2025 79   GLN A N   
398  C CA  . GLN A 62  ? 1.1632 0.8125 0.9405 0.1060  -0.2389 -0.2031 79   GLN A CA  
399  C C   . GLN A 62  ? 1.1767 0.8356 1.0057 0.0786  -0.2405 -0.1845 79   GLN A C   
400  O O   . GLN A 62  ? 1.1182 0.7670 0.9819 0.0673  -0.2501 -0.1788 79   GLN A O   
401  C CB  . GLN A 62  ? 1.2157 0.8351 0.9782 0.1223  -0.2729 -0.2278 79   GLN A CB  
402  C CG  . GLN A 62  ? 1.3286 0.9416 1.0344 0.1539  -0.2713 -0.2461 79   GLN A CG  
403  C CD  . GLN A 62  ? 1.5468 1.1349 1.2325 0.1720  -0.3043 -0.2707 79   GLN A CD  
404  O OE1 . GLN A 62  ? 1.4386 1.0074 1.1569 0.1608  -0.3335 -0.2773 79   GLN A OE1 
405  N NE2 . GLN A 62  ? 1.7173 1.3068 1.3504 0.2013  -0.3002 -0.2836 79   GLN A NE2 
406  N N   . GLN A 63  ? 1.2153 0.8949 1.0500 0.0693  -0.2303 -0.1737 80   GLN A N   
407  C CA  . GLN A 63  ? 1.1687 0.8611 1.0494 0.0464  -0.2304 -0.1551 80   GLN A CA  
408  C C   . GLN A 63  ? 1.1807 0.8752 1.0645 0.0446  -0.2432 -0.1583 80   GLN A C   
409  O O   . GLN A 63  ? 1.1718 0.8722 1.0201 0.0572  -0.2366 -0.1660 80   GLN A O   
410  C CB  . GLN A 63  ? 1.1311 0.8533 1.0189 0.0355  -0.1988 -0.1339 80   GLN A CB  
411  C CG  . GLN A 63  ? 1.1790 0.9071 1.1085 0.0195  -0.1958 -0.1162 80   GLN A CG  
412  C CD  . GLN A 63  ? 1.0999 0.8274 1.0752 0.0045  -0.2129 -0.1056 80   GLN A CD  
413  O OE1 . GLN A 63  ? 1.0671 0.7995 1.0452 0.0021  -0.2195 -0.1063 80   GLN A OE1 
414  N NE2 . GLN A 63  ? 1.1490 0.8718 1.1630 -0.0055 -0.2200 -0.0939 80   GLN A NE2 
415  N N   . ALA A 64  ? 1.1469 0.8378 1.0754 0.0292  -0.2612 -0.1505 81   ALA A N   
416  C CA  . ALA A 64  ? 1.1190 0.8111 1.0569 0.0263  -0.2766 -0.1530 81   ALA A CA  
417  C C   . ALA A 64  ? 1.1265 0.8507 1.0705 0.0158  -0.2515 -0.1333 81   ALA A C   
418  O O   . ALA A 64  ? 1.1000 0.8423 1.0745 0.0012  -0.2364 -0.1123 81   ALA A O   
419  C CB  . ALA A 64  ? 1.0222 0.6984 1.0113 0.0137  -0.3072 -0.1508 81   ALA A CB  
420  N N   . PHE A 65  ? 1.1123 0.8434 1.0263 0.0250  -0.2473 -0.1401 82   PHE A N   
421  C CA  . PHE A 65  ? 1.0636 0.8220 0.9810 0.0174  -0.2269 -0.1245 82   PHE A CA  
422  C C   . PHE A 65  ? 1.0238 0.7814 0.9534 0.0152  -0.2458 -0.1273 82   PHE A C   
423  O O   . PHE A 65  ? 0.9844 0.7224 0.8963 0.0274  -0.2690 -0.1465 82   PHE A O   
424  C CB  . PHE A 65  ? 1.0630 0.8330 0.9363 0.0299  -0.2024 -0.1271 82   PHE A CB  
425  C CG  . PHE A 65  ? 1.0669 0.8492 0.9382 0.0266  -0.1775 -0.1166 82   PHE A CG  
426  C CD1 . PHE A 65  ? 0.9342 0.7405 0.8101 0.0192  -0.1541 -0.1013 82   PHE A CD1 
427  C CD2 . PHE A 65  ? 1.3107 1.0796 1.1754 0.0318  -0.1790 -0.1229 82   PHE A CD2 
428  C CE1 . PHE A 65  ? 1.0564 0.8732 0.9307 0.0170  -0.1340 -0.0933 82   PHE A CE1 
429  C CE2 . PHE A 65  ? 1.2312 1.0120 1.0949 0.0290  -0.1573 -0.1134 82   PHE A CE2 
430  C CZ  . PHE A 65  ? 0.9996 0.8042 0.8682 0.0216  -0.1355 -0.0989 82   PHE A CZ  
431  N N   . THR A 66  ? 1.1063 0.8857 1.0650 0.0014  -0.2364 -0.1085 83   THR A N   
432  C CA  . THR A 66  ? 1.1498 0.9333 1.1212 -0.0013 -0.2509 -0.1083 83   THR A CA  
433  C C   . THR A 66  ? 1.0665 0.8628 0.9987 0.0093  -0.2333 -0.1111 83   THR A C   
434  O O   . THR A 66  ? 1.1253 0.9443 1.0621 0.0031  -0.2112 -0.0957 83   THR A O   
435  C CB  . THR A 66  ? 1.0837 0.8859 1.1080 -0.0198 -0.2493 -0.0850 83   THR A CB  
436  O OG1 . THR A 66  ? 1.1302 0.9209 1.1943 -0.0293 -0.2651 -0.0798 83   THR A OG1 
437  C CG2 . THR A 66  ? 1.1663 0.9735 1.2059 -0.0224 -0.2650 -0.0843 83   THR A CG2 
438  N N   . LYS A 67  ? 1.0424 0.8239 0.9349 0.0271  -0.2433 -0.1305 84   LYS A N   
439  C CA  . LYS A 67  ? 1.0912 0.8841 0.9484 0.0387  -0.2290 -0.1320 84   LYS A CA  
440  C C   . LYS A 67  ? 1.0891 0.8950 0.9668 0.0310  -0.2346 -0.1236 84   LYS A C   
441  O O   . LYS A 67  ? 1.1308 0.9259 1.0249 0.0300  -0.2618 -0.1311 84   LYS A O   
442  C CB  . LYS A 67  ? 1.0621 0.8374 0.8745 0.0619  -0.2413 -0.1533 84   LYS A CB  
443  C CG  . LYS A 67  ? 1.0839 0.8705 0.8620 0.0761  -0.2310 -0.1541 84   LYS A CG  
444  C CD  . LYS A 67  ? 1.0686 0.8418 0.7983 0.1025  -0.2362 -0.1717 84   LYS A CD  
445  C CE  . LYS A 67  ? 1.1833 0.9605 0.8838 0.1193  -0.2420 -0.1775 84   LYS A CE  
446  N NZ  . LYS A 67  ? 1.1367 0.9042 0.7871 0.1488  -0.2449 -0.1927 84   LYS A NZ  
447  N N   . TRP A 68  ? 0.9933 0.8217 0.8715 0.0259  -0.2100 -0.1085 85   TRP A N   
448  C CA  . TRP A 68  ? 0.9752 0.8198 0.8761 0.0173  -0.2102 -0.0968 85   TRP A CA  
449  C C   . TRP A 68  ? 0.9939 0.8490 0.8623 0.0283  -0.1948 -0.0966 85   TRP A C   
450  O O   . TRP A 68  ? 0.8995 0.7665 0.7569 0.0284  -0.1698 -0.0882 85   TRP A O   
451  C CB  . TRP A 68  ? 0.8651 0.7281 0.8032 0.0008  -0.1951 -0.0763 85   TRP A CB  
452  C CG  . TRP A 68  ? 0.8504 0.7325 0.8122 -0.0065 -0.1925 -0.0625 85   TRP A CG  
453  C CD1 . TRP A 68  ? 0.8646 0.7461 0.8359 -0.0059 -0.2112 -0.0653 85   TRP A CD1 
454  C CD2 . TRP A 68  ? 0.8522 0.7573 0.8301 -0.0139 -0.1704 -0.0441 85   TRP A CD2 
455  N NE1 . TRP A 68  ? 0.8869 0.7906 0.8809 -0.0131 -0.2009 -0.0485 85   TRP A NE1 
456  C CE2 . TRP A 68  ? 0.9181 0.8362 0.9152 -0.0172 -0.1758 -0.0357 85   TRP A CE2 
457  C CE3 . TRP A 68  ? 0.8474 0.7632 0.8242 -0.0164 -0.1476 -0.0349 85   TRP A CE3 
458  C CZ2 . TRP A 68  ? 0.9461 0.8876 0.9600 -0.0219 -0.1582 -0.0183 85   TRP A CZ2 
459  C CZ3 . TRP A 68  ? 0.8752 0.8131 0.8673 -0.0204 -0.1317 -0.0191 85   TRP A CZ3 
460  C CH2 . TRP A 68  ? 0.9156 0.8662 0.9254 -0.0226 -0.1365 -0.0108 85   TRP A CH2 
461  N N   . THR A 69  ? 0.9894 0.8400 0.8444 0.0377  -0.2108 -0.1054 86   THR A N   
462  C CA  . THR A 69  ? 1.0052 0.8647 0.8285 0.0504  -0.1980 -0.1049 86   THR A CA  
463  C C   . THR A 69  ? 1.1072 0.9787 0.9476 0.0457  -0.2044 -0.0977 86   THR A C   
464  O O   . THR A 69  ? 1.2379 1.1086 1.1117 0.0352  -0.2229 -0.0960 86   THR A O   
465  C CB  . THR A 69  ? 1.0681 0.9129 0.8484 0.0726  -0.2085 -0.1223 86   THR A CB  
466  O OG1 . THR A 69  ? 1.2042 1.0332 0.9895 0.0767  -0.2414 -0.1371 86   THR A OG1 
467  C CG2 . THR A 69  ? 1.0646 0.8999 0.8263 0.0792  -0.1997 -0.1281 86   THR A CG2 
468  N N   . TRP A 70  ? 0.9260 0.8093 0.7458 0.0536  -0.1884 -0.0920 87   TRP A N   
469  C CA  . TRP A 70  ? 0.9392 0.8337 0.7677 0.0531  -0.1932 -0.0862 87   TRP A CA  
470  C C   . TRP A 70  ? 1.0185 0.9110 0.8066 0.0734  -0.1940 -0.0935 87   TRP A C   
471  O O   . TRP A 70  ? 0.9745 0.8645 0.7316 0.0859  -0.1803 -0.0958 87   TRP A O   
472  C CB  . TRP A 70  ? 0.8869 0.8012 0.7356 0.0420  -0.1706 -0.0680 87   TRP A CB  
473  C CG  . TRP A 70  ? 0.8951 0.8157 0.7192 0.0495  -0.1454 -0.0626 87   TRP A CG  
474  C CD1 . TRP A 70  ? 1.0178 0.9389 0.8385 0.0468  -0.1270 -0.0591 87   TRP A CD1 
475  C CD2 . TRP A 70  ? 0.9178 0.8455 0.7214 0.0607  -0.1370 -0.0588 87   TRP A CD2 
476  N NE1 . TRP A 70  ? 0.8425 0.7699 0.6448 0.0548  -0.1088 -0.0533 87   TRP A NE1 
477  C CE2 . TRP A 70  ? 1.0475 0.9793 0.8394 0.0634  -0.1138 -0.0522 87   TRP A CE2 
478  C CE3 . TRP A 70  ? 1.0632 0.9946 0.8591 0.0689  -0.1474 -0.0595 87   TRP A CE3 
479  C CZ2 . TRP A 70  ? 0.9927 0.9318 0.7684 0.0734  -0.1005 -0.0448 87   TRP A CZ2 
480  C CZ3 . TRP A 70  ? 1.0306 0.9697 0.8066 0.0798  -0.1331 -0.0526 87   TRP A CZ3 
481  C CH2 . TRP A 70  ? 0.9598 0.9028 0.7274 0.0816  -0.1097 -0.0446 87   TRP A CH2 
482  N N   . GLU A 71  ? 1.0311 0.9265 0.8209 0.0776  -0.2096 -0.0955 88   GLU A N   
483  C CA  . GLU A 71  ? 1.1089 1.0056 0.8608 0.0983  -0.2097 -0.1000 88   GLU A CA  
484  C C   . GLU A 71  ? 1.1110 1.0179 0.8761 0.0968  -0.2197 -0.0951 88   GLU A C   
485  O O   . GLU A 71  ? 1.0415 0.9497 0.8424 0.0829  -0.2357 -0.0937 88   GLU A O   
486  C CB  . GLU A 71  ? 1.1844 1.0629 0.9025 0.1179  -0.2300 -0.1202 88   GLU A CB  
487  C CG  . GLU A 71  ? 1.2538 1.1174 0.9889 0.1154  -0.2664 -0.1355 88   GLU A CG  
488  C CD  . GLU A 71  ? 1.4863 1.3310 1.1816 0.1396  -0.2884 -0.1580 88   GLU A CD  
489  O OE1 . GLU A 71  ? 1.4449 1.2922 1.0969 0.1606  -0.2734 -0.1592 88   GLU A OE1 
490  O OE2 . GLU A 71  ? 1.6156 1.4431 1.3239 0.1388  -0.3212 -0.1740 88   GLU A OE2 
491  N N   . VAL A 72  ? 1.0760 0.9915 0.8136 0.1119  -0.2096 -0.0907 89   VAL A N   
492  C CA  . VAL A 72  ? 1.1514 1.0766 0.8963 0.1138  -0.2191 -0.0866 89   VAL A CA  
493  C C   . VAL A 72  ? 1.1022 1.0149 0.8450 0.1209  -0.2552 -0.1043 89   VAL A C   
494  O O   . VAL A 72  ? 1.1837 1.0798 0.9018 0.1340  -0.2705 -0.1214 89   VAL A O   
495  C CB  . VAL A 72  ? 1.0126 0.9486 0.7261 0.1308  -0.2011 -0.0779 89   VAL A CB  
496  C CG1 . VAL A 72  ? 1.0320 0.9594 0.6987 0.1571  -0.2091 -0.0905 89   VAL A CG1 
497  C CG2 . VAL A 72  ? 0.9893 0.9381 0.7160 0.1296  -0.2055 -0.0696 89   VAL A CG2 
498  N N   . LYS A 73  ? 1.0179 0.9380 0.7885 0.1129  -0.2702 -0.1007 90   LYS A N   
499  C CA  . LYS A 73  ? 1.0696 0.9781 0.8439 0.1186  -0.3075 -0.1172 90   LYS A CA  
500  C C   . LYS A 73  ? 1.2544 1.1577 0.9769 0.1476  -0.3172 -0.1304 90   LYS A C   
501  O O   . LYS A 73  ? 1.2120 1.1291 0.9121 0.1589  -0.2993 -0.1201 90   LYS A O   
502  C CB  . LYS A 73  ? 1.0517 0.9732 0.8698 0.1039  -0.3192 -0.1072 90   LYS A CB  
503  C CG  . LYS A 73  ? 1.0102 0.9352 0.8829 0.0785  -0.3201 -0.0970 90   LYS A CG  
504  C CD  . LYS A 73  ? 0.9990 0.9402 0.9158 0.0662  -0.3304 -0.0845 90   LYS A CD  
505  C CE  . LYS A 73  ? 0.9781 0.9234 0.9515 0.0436  -0.3353 -0.0738 90   LYS A CE  
506  N NZ  . LYS A 73  ? 1.1645 1.1311 1.1836 0.0320  -0.3390 -0.0564 90   LYS A NZ  
507  N N   . SER A 74  ? 1.2561 1.1391 0.9593 0.1612  -0.3459 -0.1531 91   SER A N   
508  C CA  . SER A 74  ? 1.3024 1.1800 0.9514 0.1930  -0.3567 -0.1675 91   SER A CA  
509  C C   . SER A 74  ? 1.3413 1.2292 0.9892 0.2010  -0.3715 -0.1664 91   SER A C   
510  O O   . SER A 74  ? 1.4496 1.3452 1.0544 0.2256  -0.3644 -0.1658 91   SER A O   
511  C CB  . SER A 74  ? 1.2394 1.0910 0.8701 0.2066  -0.3888 -0.1947 91   SER A CB  
512  O OG  . SER A 74  ? 1.4137 1.2553 1.0528 0.1963  -0.3776 -0.1953 91   SER A OG  
513  N N   . ASP A 75  ? 1.4062 1.2963 1.1024 0.1812  -0.3913 -0.1643 92   ASP A N   
514  C CA  . ASP A 75  ? 1.4193 1.3194 1.1210 0.1866  -0.4083 -0.1633 92   ASP A CA  
515  C C   . ASP A 75  ? 1.4912 1.4163 1.2168 0.1722  -0.3788 -0.1366 92   ASP A C   
516  O O   . ASP A 75  ? 1.6291 1.5645 1.3958 0.1574  -0.3892 -0.1284 92   ASP A O   
517  C CB  . ASP A 75  ? 1.4474 1.3353 1.1906 0.1751  -0.4507 -0.1768 92   ASP A CB  
518  C CG  . ASP A 75  ? 1.4529 1.3444 1.2597 0.1422  -0.4460 -0.1628 92   ASP A CG  
519  O OD1 . ASP A 75  ? 1.4420 1.3403 1.2978 0.1266  -0.4653 -0.1570 92   ASP A OD1 
520  O OD2 . ASP A 75  ? 1.4558 1.3452 1.2643 0.1328  -0.4223 -0.1561 92   ASP A OD2 
521  N N   . LEU A 76  ? 1.3921 1.3274 1.0936 0.1773  -0.3421 -0.1223 93   LEU A N   
522  C CA  . LEU A 76  ? 1.2376 1.1937 0.9585 0.1659  -0.3134 -0.0984 93   LEU A CA  
523  C C   . LEU A 76  ? 1.2006 1.1684 0.8920 0.1864  -0.3113 -0.0936 93   LEU A C   
524  O O   . LEU A 76  ? 1.3573 1.3240 1.0019 0.2102  -0.3028 -0.0964 93   LEU A O   
525  C CB  . LEU A 76  ? 1.1740 1.1333 0.8899 0.1594  -0.2772 -0.0855 93   LEU A CB  
526  C CG  . LEU A 76  ? 1.1147 1.0911 0.8614 0.1424  -0.2508 -0.0634 93   LEU A CG  
527  C CD1 . LEU A 76  ? 0.9984 0.9773 0.7965 0.1178  -0.2592 -0.0597 93   LEU A CD1 
528  C CD2 . LEU A 76  ? 1.0730 1.0515 0.8063 0.1423  -0.2176 -0.0527 93   LEU A CD2 
529  N N   . ALA A 77  ? 1.1689 1.1495 0.8884 0.1783  -0.3183 -0.0848 94   ALA A N   
530  C CA  . ALA A 77  ? 1.2224 1.2154 0.9180 0.1967  -0.3167 -0.0787 94   ALA A CA  
531  C C   . ALA A 77  ? 1.2158 1.2200 0.8912 0.2033  -0.2782 -0.0596 94   ALA A C   
532  O O   . ALA A 77  ? 1.2241 1.2294 0.9158 0.1884  -0.2532 -0.0487 94   ALA A O   
533  C CB  . ALA A 77  ? 1.1781 1.1840 0.9139 0.1841  -0.3294 -0.0708 94   ALA A CB  
534  N N   . GLU A 78  ? 1.2161 1.2286 0.8568 0.2268  -0.2747 -0.0552 95   GLU A N   
535  C CA  . GLU A 78  ? 1.3367 1.3603 0.9613 0.2347  -0.2402 -0.0349 95   GLU A CA  
536  C C   . GLU A 78  ? 1.2347 1.2697 0.8998 0.2136  -0.2206 -0.0157 95   GLU A C   
537  O O   . GLU A 78  ? 1.2098 1.2515 0.9030 0.2037  -0.2334 -0.0141 95   GLU A O   
538  C CB  . GLU A 78  ? 1.3430 1.3756 0.9260 0.2649  -0.2421 -0.0316 95   GLU A CB  
539  C CG  . GLU A 78  ? 1.4788 1.5017 1.0142 0.2919  -0.2601 -0.0505 95   GLU A CG  
540  C CD  . GLU A 78  ? 1.8677 1.8936 1.3785 0.3144  -0.2885 -0.0616 95   GLU A CD  
541  O OE1 . GLU A 78  ? 1.7716 1.7982 1.3132 0.3010  -0.3104 -0.0669 95   GLU A OE1 
542  O OE2 . GLU A 78  ? 1.8869 1.9161 1.3481 0.3465  -0.2888 -0.0643 95   GLU A OE2 
543  N N   . ASN A 79  ? 1.2484 1.2856 0.9172 0.2078  -0.1902 -0.0013 96   ASN A N   
544  C CA  . ASN A 79  ? 1.2637 1.3093 0.9664 0.1910  -0.1700 0.0157  96   ASN A CA  
545  C C   . ASN A 79  ? 1.2128 1.2569 0.9569 0.1668  -0.1786 0.0113  96   ASN A C   
546  O O   . ASN A 79  ? 1.2466 1.3001 1.0192 0.1561  -0.1704 0.0227  96   ASN A O   
547  C CB  . ASN A 79  ? 1.2110 1.2702 0.9128 0.2010  -0.1663 0.0294  96   ASN A CB  
548  C CG  . ASN A 79  ? 1.2928 1.3568 0.9559 0.2264  -0.1557 0.0379  96   ASN A CG  
549  O OD1 . ASN A 79  ? 1.3997 1.4601 1.0460 0.2326  -0.1393 0.0421  96   ASN A OD1 
550  N ND2 . ASN A 79  ? 1.3391 1.4130 0.9889 0.2420  -0.1646 0.0422  96   ASN A ND2 
551  N N   . THR A 80  ? 1.0508 1.0839 0.7994 0.1594  -0.1948 -0.0038 97   THR A N   
552  C CA  . THR A 80  ? 1.0268 1.0603 0.8167 0.1371  -0.2005 -0.0046 97   THR A CA  
553  C C   . THR A 80  ? 1.0610 1.0954 0.8658 0.1245  -0.1732 0.0059  97   THR A C   
554  O O   . THR A 80  ? 1.1182 1.1442 0.9049 0.1273  -0.1599 0.0041  97   THR A O   
555  C CB  . THR A 80  ? 1.0597 1.0801 0.8522 0.1329  -0.2247 -0.0223 97   THR A CB  
556  O OG1 . THR A 80  ? 1.2745 1.2920 1.0524 0.1463  -0.2536 -0.0346 97   THR A OG1 
557  C CG2 . THR A 80  ? 0.9563 0.9801 0.7958 0.1103  -0.2297 -0.0190 97   THR A CG2 
558  N N   . GLN A 81  ? 0.9858 1.0309 0.8233 0.1121  -0.1655 0.0167  98   GLN A N   
559  C CA  . GLN A 81  ? 0.9425 0.9885 0.7935 0.1023  -0.1420 0.0252  98   GLN A CA  
560  C C   . GLN A 81  ? 0.9717 1.0113 0.8382 0.0888  -0.1448 0.0184  98   GLN A C   
561  O O   . GLN A 81  ? 1.0088 1.0498 0.8956 0.0810  -0.1632 0.0138  98   GLN A O   
562  C CB  . GLN A 81  ? 0.9011 0.9610 0.7780 0.0976  -0.1333 0.0382  98   GLN A CB  
563  C CG  . GLN A 81  ? 0.9371 1.0030 0.8007 0.1107  -0.1285 0.0466  98   GLN A CG  
564  C CD  . GLN A 81  ? 0.9465 1.0251 0.8352 0.1073  -0.1201 0.0586  98   GLN A CD  
565  O OE1 . GLN A 81  ? 1.0168 1.1070 0.9252 0.1047  -0.1329 0.0611  98   GLN A OE1 
566  N NE2 . GLN A 81  ? 0.9062 0.9826 0.7956 0.1081  -0.0995 0.0662  98   GLN A NE2 
567  N N   . ALA A 82  ? 0.9011 0.9338 0.7604 0.0861  -0.1270 0.0190  99   ALA A N   
568  C CA  . ALA A 82  ? 0.8465 0.8725 0.7163 0.0751  -0.1280 0.0128  99   ALA A CA  
569  C C   . ALA A 82  ? 0.8870 0.9243 0.7936 0.0620  -0.1283 0.0199  99   ALA A C   
570  O O   . ALA A 82  ? 0.9847 1.0330 0.9045 0.0614  -0.1165 0.0303  99   ALA A O   
571  C CB  . ALA A 82  ? 0.8707 0.8888 0.7266 0.0757  -0.1081 0.0133  99   ALA A CB  
572  N N   . SER A 83  ? 0.9091 0.9441 0.8327 0.0530  -0.1419 0.0150  100  SER A N   
573  C CA  . SER A 83  ? 0.8093 0.8575 0.7705 0.0414  -0.1422 0.0245  100  SER A CA  
574  C C   . SER A 83  ? 0.9313 0.9717 0.9024 0.0324  -0.1470 0.0194  100  SER A C   
575  O O   . SER A 83  ? 0.9795 1.0038 0.9269 0.0353  -0.1488 0.0080  100  SER A O   
576  C CB  . SER A 83  ? 0.8690 0.9294 0.8554 0.0397  -0.1606 0.0297  100  SER A CB  
577  O OG  . SER A 83  ? 0.9226 0.9720 0.9059 0.0402  -0.1862 0.0178  100  SER A OG  
578  N N   . SER A 84  ? 0.9150 0.9681 0.9224 0.0223  -0.1485 0.0296  101  SER A N   
579  C CA  . SER A 84  ? 0.7974 0.8447 0.8198 0.0132  -0.1541 0.0276  101  SER A CA  
580  C C   . SER A 84  ? 0.8562 0.8907 0.8847 0.0106  -0.1823 0.0168  101  SER A C   
581  O O   . SER A 84  ? 0.8629 0.8867 0.8971 0.0049  -0.1890 0.0113  101  SER A O   
582  C CB  . SER A 84  ? 0.7722 0.8400 0.8340 0.0050  -0.1464 0.0452  101  SER A CB  
583  O OG  . SER A 84  ? 0.7975 0.8807 0.8927 0.0016  -0.1602 0.0557  101  SER A OG  
584  N N   . THR A 85  ? 0.8296 0.8640 0.8564 0.0156  -0.2001 0.0125  102  THR A N   
585  C CA  . THR A 85  ? 0.8950 0.9163 0.9286 0.0149  -0.2311 0.0002  102  THR A CA  
586  C C   . THR A 85  ? 0.9439 0.9487 0.9318 0.0305  -0.2411 -0.0178 102  THR A C   
587  O O   . THR A 85  ? 0.9965 0.9892 0.9837 0.0341  -0.2693 -0.0309 102  THR A O   
588  C CB  . THR A 85  ? 0.8982 0.9345 0.9757 0.0080  -0.2499 0.0105  102  THR A CB  
589  O OG1 . THR A 85  ? 1.1240 1.1677 1.1860 0.0179  -0.2508 0.0107  102  THR A OG1 
590  C CG2 . THR A 85  ? 0.8982 0.9574 1.0185 -0.0034 -0.2344 0.0331  102  THR A CG2 
591  N N   . SER A 86  ? 1.0405 1.0449 0.9917 0.0411  -0.2195 -0.0180 103  SER A N   
592  C CA  . SER A 86  ? 0.9875 0.9796 0.8944 0.0583  -0.2252 -0.0315 103  SER A CA  
593  C C   . SER A 86  ? 0.9704 0.9437 0.8510 0.0635  -0.2269 -0.0455 103  SER A C   
594  O O   . SER A 86  ? 1.0485 1.0128 0.8894 0.0803  -0.2288 -0.0556 103  SER A O   
595  C CB  . SER A 86  ? 0.9490 0.9500 0.8324 0.0678  -0.2011 -0.0226 103  SER A CB  
596  O OG  . SER A 86  ? 1.0449 1.0438 0.9183 0.0656  -0.1762 -0.0184 103  SER A OG  
597  N N   . PHE A 87  ? 0.9159 0.8845 0.8174 0.0510  -0.2255 -0.0450 104  PHE A N   
598  C CA  . PHE A 87  ? 1.0733 1.0243 0.9532 0.0551  -0.2269 -0.0576 104  PHE A CA  
599  C C   . PHE A 87  ? 0.9806 0.9253 0.8965 0.0406  -0.2424 -0.0592 104  PHE A C   
600  O O   . PHE A 87  ? 0.9454 0.9031 0.9034 0.0265  -0.2437 -0.0460 104  PHE A O   
601  C CB  . PHE A 87  ? 0.9900 0.9433 0.8505 0.0567  -0.1964 -0.0514 104  PHE A CB  
602  C CG  . PHE A 87  ? 0.9153 0.8805 0.8064 0.0414  -0.1785 -0.0371 104  PHE A CG  
603  C CD1 . PHE A 87  ? 0.8553 0.8378 0.7632 0.0375  -0.1665 -0.0231 104  PHE A CD1 
604  C CD2 . PHE A 87  ? 0.9558 0.9152 0.8569 0.0330  -0.1739 -0.0379 104  PHE A CD2 
605  C CE1 . PHE A 87  ? 0.8175 0.8114 0.7494 0.0272  -0.1506 -0.0111 104  PHE A CE1 
606  C CE2 . PHE A 87  ? 0.8871 0.8587 0.8129 0.0220  -0.1577 -0.0250 104  PHE A CE2 
607  C CZ  . PHE A 87  ? 0.8913 0.8802 0.8314 0.0199  -0.1462 -0.0119 104  PHE A CZ  
608  N N   . GLN A 88  ? 0.9303 0.8557 0.8304 0.0452  -0.2538 -0.0741 105  GLN A N   
609  C CA  . GLN A 88  ? 1.0753 0.9914 1.0091 0.0327  -0.2710 -0.0766 105  GLN A CA  
610  C C   . GLN A 88  ? 0.9244 0.8309 0.8446 0.0318  -0.2566 -0.0797 105  GLN A C   
611  O O   . GLN A 88  ? 0.9613 0.8652 0.8430 0.0431  -0.2386 -0.0836 105  GLN A O   
612  C CB  . GLN A 88  ? 1.0134 0.9112 0.9488 0.0389  -0.3091 -0.0948 105  GLN A CB  
613  C CG  . GLN A 88  ? 1.1127 1.0203 1.0838 0.0324  -0.3298 -0.0891 105  GLN A CG  
614  C CD  . GLN A 88  ? 1.1844 1.0723 1.1491 0.0426  -0.3693 -0.1105 105  GLN A CD  
615  O OE1 . GLN A 88  ? 1.3722 1.2420 1.2916 0.0610  -0.3775 -0.1305 105  GLN A OE1 
616  N NE2 . GLN A 88  ? 1.3034 1.1955 1.3143 0.0321  -0.3948 -0.1064 105  GLN A NE2 
617  N N   . THR A 89  ? 0.9947 0.8972 0.9503 0.0182  -0.2645 -0.0760 106  THR A N   
618  C CA  . THR A 89  ? 1.0125 0.9049 0.9609 0.0163  -0.2551 -0.0791 106  THR A CA  
619  C C   . THR A 89  ? 1.0606 0.9317 1.0259 0.0140  -0.2854 -0.0921 106  THR A C   
620  O O   . THR A 89  ? 1.0427 0.9116 1.0422 0.0072  -0.3109 -0.0920 106  THR A O   
621  C CB  . THR A 89  ? 0.9954 0.9053 0.9712 0.0023  -0.2308 -0.0591 106  THR A CB  
622  O OG1 . THR A 89  ? 1.1237 1.0239 1.0873 0.0024  -0.2206 -0.0631 106  THR A OG1 
623  C CG2 . THR A 89  ? 0.9987 0.9187 1.0300 -0.0132 -0.2433 -0.0448 106  THR A CG2 
624  N N   . LYS A 90  ? 1.0868 0.9416 1.0297 0.0200  -0.2834 -0.1032 107  LYS A N   
625  C CA  . LYS A 90  ? 1.0685 0.8992 1.0225 0.0203  -0.3123 -0.1180 107  LYS A CA  
626  C C   . LYS A 90  ? 1.1587 0.9821 1.1074 0.0181  -0.2983 -0.1178 107  LYS A C   
627  O O   . LYS A 90  ? 1.1134 0.9470 1.0382 0.0211  -0.2691 -0.1114 107  LYS A O   
628  C CB  . LYS A 90  ? 1.0191 0.8296 0.9336 0.0413  -0.3366 -0.1431 107  LYS A CB  
629  C CG  . LYS A 90  ? 1.2353 1.0495 1.0917 0.0612  -0.3148 -0.1488 107  LYS A CG  
630  C CD  . LYS A 90  ? 1.0676 0.8671 0.8840 0.0849  -0.3377 -0.1706 107  LYS A CD  
631  C CE  . LYS A 90  ? 1.1039 0.8762 0.8990 0.0985  -0.3581 -0.1928 107  LYS A CE  
632  N NZ  . LYS A 90  ? 1.3946 1.1560 1.1369 0.1282  -0.3728 -0.2135 107  LYS A NZ  
633  N N   . SER A 91  ? 1.0018 0.8068 0.9755 0.0126  -0.3210 -0.1245 108  SER A N   
634  C CA  . SER A 91  ? 1.1493 0.9462 1.1225 0.0100  -0.3109 -0.1240 108  SER A CA  
635  C C   . SER A 91  ? 1.2458 1.0119 1.2203 0.0163  -0.3435 -0.1447 108  SER A C   
636  O O   . SER A 91  ? 1.2576 1.0115 1.2585 0.0136  -0.3758 -0.1521 108  SER A O   
637  C CB  . SER A 91  ? 1.1063 0.9216 1.1275 -0.0102 -0.2957 -0.0989 108  SER A CB  
638  O OG  . SER A 91  ? 1.1765 0.9937 1.2518 -0.0237 -0.3183 -0.0894 108  SER A OG  
639  N N   . SER A 92  ? 1.2339 0.9869 1.1802 0.0255  -0.3357 -0.1544 109  SER A N   
640  C CA  . SER A 92  ? 1.1690 0.8911 1.1140 0.0331  -0.3647 -0.1745 109  SER A CA  
641  C C   . SER A 92  ? 1.1709 0.8884 1.1015 0.0353  -0.3463 -0.1738 109  SER A C   
642  O O   . SER A 92  ? 1.2632 0.9971 1.1666 0.0389  -0.3142 -0.1655 109  SER A O   
643  C CB  . SER A 92  ? 1.1430 0.8459 1.0416 0.0580  -0.3871 -0.2019 109  SER A CB  
644  O OG  . SER A 92  ? 1.2785 0.9848 1.1196 0.0777  -0.3638 -0.2086 109  SER A OG  
645  N N   . GLU A 93  ? 1.1494 0.8436 1.1006 0.0331  -0.3680 -0.1824 110  GLU A N   
646  C CA  . GLU A 93  ? 1.0947 0.7835 1.0364 0.0346  -0.3529 -0.1813 110  GLU A CA  
647  C C   . GLU A 93  ? 1.1499 0.8223 1.0313 0.0611  -0.3531 -0.2046 110  GLU A C   
648  O O   . GLU A 93  ? 1.2398 0.8920 1.0972 0.0786  -0.3796 -0.2274 110  GLU A O   
649  C CB  . GLU A 93  ? 1.1468 0.8179 1.1383 0.0214  -0.3751 -0.1787 110  GLU A CB  
650  C CG  . GLU A 93  ? 1.0630 0.7573 1.1104 -0.0032 -0.3601 -0.1478 110  GLU A CG  
651  C CD  . GLU A 93  ? 1.2109 0.9241 1.2896 -0.0147 -0.3640 -0.1338 110  GLU A CD  
652  O OE1 . GLU A 93  ? 1.3485 1.0476 1.4307 -0.0101 -0.3935 -0.1483 110  GLU A OE1 
653  O OE2 . GLU A 93  ? 1.2924 1.0348 1.3912 -0.0271 -0.3382 -0.1089 110  GLU A OE2 
654  N N   . VAL A 94  ? 1.0908 0.7733 0.9480 0.0654  -0.3237 -0.1984 111  VAL A N   
655  C CA  . VAL A 94  ? 1.1371 0.8104 0.9390 0.0909  -0.3176 -0.2152 111  VAL A CA  
656  C C   . VAL A 94  ? 1.1289 0.8049 0.9301 0.0880  -0.2964 -0.2074 111  VAL A C   
657  O O   . VAL A 94  ? 1.1912 0.8866 1.0192 0.0697  -0.2746 -0.1864 111  VAL A O   
658  C CB  . VAL A 94  ? 1.3321 1.0249 1.0936 0.1043  -0.2974 -0.2130 111  VAL A CB  
659  C CG1 . VAL A 94  ? 1.0932 0.8162 0.8694 0.0877  -0.2631 -0.1879 111  VAL A CG1 
660  C CG2 . VAL A 94  ? 1.3631 1.0489 1.0692 0.1331  -0.2911 -0.2277 111  VAL A CG2 
661  N N   . ASN A 95  ? 1.3356 0.9925 1.1054 0.1078  -0.3035 -0.2248 112  ASN A N   
662  C CA  . ASN A 95  ? 1.2580 0.9154 1.0262 0.1072  -0.2863 -0.2194 112  ASN A CA  
663  C C   . ASN A 95  ? 1.2692 0.9492 1.0006 0.1181  -0.2523 -0.2114 112  ASN A C   
664  O O   . ASN A 95  ? 1.3390 1.0179 1.0266 0.1419  -0.2507 -0.2227 112  ASN A O   
665  C CB  . ASN A 95  ? 1.2624 0.8878 1.0172 0.1236  -0.3110 -0.2416 112  ASN A CB  
666  C CG  . ASN A 95  ? 1.3696 0.9725 1.1731 0.1083  -0.3428 -0.2451 112  ASN A CG  
667  O OD1 . ASN A 95  ? 1.3412 0.9531 1.1869 0.0873  -0.3482 -0.2314 112  ASN A OD1 
668  N ND2 . ASN A 95  ? 1.4606 1.0344 1.2606 0.1194  -0.3642 -0.2623 112  ASN A ND2 
669  N N   . LEU A 96  ? 1.2498 0.9508 1.0004 0.1019  -0.2259 -0.1912 113  LEU A N   
670  C CA  . LEU A 96  ? 1.1949 0.9170 0.9206 0.1089  -0.1948 -0.1815 113  LEU A CA  
671  C C   . LEU A 96  ? 1.1453 0.8643 0.8705 0.1107  -0.1846 -0.1799 113  LEU A C   
672  O O   . LEU A 96  ? 1.2065 0.9175 0.9626 0.0968  -0.1918 -0.1762 113  LEU A O   
673  C CB  . LEU A 96  ? 1.1437 0.8923 0.8901 0.0908  -0.1738 -0.1612 113  LEU A CB  
674  C CG  . LEU A 96  ? 1.0858 0.8403 0.8340 0.0885  -0.1812 -0.1605 113  LEU A CG  
675  C CD1 . LEU A 96  ? 1.1130 0.8928 0.8799 0.0727  -0.1597 -0.1411 113  LEU A CD1 
676  C CD2 . LEU A 96  ? 1.2092 0.9609 0.9139 0.1128  -0.1837 -0.1725 113  LEU A CD2 
677  N N   . ARG A 97  ? 1.1435 0.8702 0.8353 0.1284  -0.1673 -0.1809 114  ARG A N   
678  C CA  . ARG A 97  ? 1.1698 0.8935 0.8562 0.1343  -0.1582 -0.1809 114  ARG A CA  
679  C C   . ARG A 97  ? 1.1332 0.8835 0.8133 0.1338  -0.1269 -0.1647 114  ARG A C   
680  O O   . ARG A 97  ? 1.1988 0.9631 0.8574 0.1448  -0.1147 -0.1609 114  ARG A O   
681  C CB  . ARG A 97  ? 1.2312 0.9340 0.8816 0.1619  -0.1728 -0.2011 114  ARG A CB  
682  C CG  . ARG A 97  ? 1.3753 1.0720 1.0212 0.1692  -0.1666 -0.2028 114  ARG A CG  
683  C CD  . ARG A 97  ? 1.4330 1.1149 1.0353 0.2019  -0.1754 -0.2212 114  ARG A CD  
684  N NE  . ARG A 97  ? 1.5434 1.1931 1.1413 0.2108  -0.2104 -0.2440 114  ARG A NE  
685  C CZ  . ARG A 97  ? 1.5402 1.1642 1.1495 0.2115  -0.2297 -0.2558 114  ARG A CZ  
686  N NH1 . ARG A 97  ? 1.4337 1.0618 1.0576 0.2041  -0.2158 -0.2462 114  ARG A NH1 
687  N NH2 . ARG A 97  ? 1.4939 1.0872 1.1016 0.2198  -0.2643 -0.2774 114  ARG A NH2 
688  N N   . GLY A 98  ? 1.0970 0.8543 0.7981 0.1213  -0.1151 -0.1545 115  GLY A N   
689  C CA  . GLY A 98  ? 1.1188 0.8988 0.8182 0.1207  -0.0889 -0.1406 115  GLY A CA  
690  C C   . GLY A 98  ? 0.9611 0.7605 0.6872 0.0999  -0.0758 -0.1249 115  GLY A C   
691  O O   . GLY A 98  ? 1.0549 0.8716 0.7842 0.0979  -0.0567 -0.1141 115  GLY A O   
692  N N   . LEU A 99  ? 1.0657 0.8629 0.8120 0.0855  -0.0862 -0.1233 116  LEU A N   
693  C CA  . LEU A 99  ? 0.9677 0.7832 0.7359 0.0689  -0.0743 -0.1095 116  LEU A CA  
694  C C   . LEU A 99  ? 0.9731 0.7950 0.7628 0.0577  -0.0665 -0.1009 116  LEU A C   
695  O O   . LEU A 99  ? 1.1104 0.9207 0.9048 0.0587  -0.0736 -0.1046 116  LEU A O   
696  C CB  . LEU A 99  ? 0.8986 0.7116 0.6828 0.0586  -0.0873 -0.1090 116  LEU A CB  
697  C CG  . LEU A 99  ? 0.9133 0.7262 0.6787 0.0676  -0.0918 -0.1143 116  LEU A CG  
698  C CD1 . LEU A 99  ? 1.0624 0.8675 0.8447 0.0592  -0.1107 -0.1170 116  LEU A CD1 
699  C CD2 . LEU A 99  ? 1.0444 0.8778 0.8066 0.0662  -0.0723 -0.1034 116  LEU A CD2 
700  N N   . CYS A 100 ? 1.0064 0.8468 0.8086 0.0481  -0.0527 -0.0897 117  CYS A N   
701  C CA  . CYS A 100 ? 0.9944 0.8434 0.8140 0.0396  -0.0449 -0.0816 117  CYS A CA  
702  C C   . CYS A 100 ? 1.0654 0.9101 0.9085 0.0290  -0.0553 -0.0774 117  CYS A C   
703  O O   . CYS A 100 ? 1.0827 0.9386 0.9416 0.0199  -0.0533 -0.0690 117  CYS A O   
704  C CB  . CYS A 100 ? 0.9557 0.8240 0.7807 0.0348  -0.0302 -0.0731 117  CYS A CB  
705  S SG  . CYS A 100 ? 1.2088 1.0852 1.0179 0.0453  -0.0162 -0.0726 117  CYS A SG  
706  N N   . LEU A 101 ? 1.0174 0.8463 0.8644 0.0311  -0.0665 -0.0821 118  LEU A N   
707  C CA  . LEU A 101 ? 0.9940 0.8181 0.8685 0.0214  -0.0772 -0.0756 118  LEU A CA  
708  C C   . LEU A 101 ? 1.0291 0.8498 0.9102 0.0224  -0.0747 -0.0728 118  LEU A C   
709  O O   . LEU A 101 ? 1.0151 0.8168 0.8980 0.0263  -0.0875 -0.0795 118  LEU A O   
710  C CB  . LEU A 101 ? 1.0124 0.8168 0.8917 0.0222  -0.0987 -0.0843 118  LEU A CB  
711  C CG  . LEU A 101 ? 1.0747 0.8869 0.9650 0.0150  -0.1027 -0.0797 118  LEU A CG  
712  C CD1 . LEU A 101 ? 1.0627 0.8549 0.9602 0.0158  -0.1269 -0.0892 118  LEU A CD1 
713  C CD2 . LEU A 101 ? 1.1833 1.0141 1.1029 0.0027  -0.0946 -0.0615 118  LEU A CD2 
714  N N   . VAL A 102 ? 0.9555 0.7940 0.8400 0.0196  -0.0594 -0.0633 119  VAL A N   
715  C CA  . VAL A 102 ? 0.7930 0.6312 0.6806 0.0220  -0.0549 -0.0604 119  VAL A CA  
716  C C   . VAL A 102 ? 0.9537 0.7918 0.8703 0.0139  -0.0611 -0.0483 119  VAL A C   
717  O O   . VAL A 102 ? 0.8521 0.7045 0.7858 0.0066  -0.0581 -0.0364 119  VAL A O   
718  C CB  . VAL A 102 ? 0.7737 0.6311 0.6537 0.0235  -0.0382 -0.0561 119  VAL A CB  
719  C CG1 . VAL A 102 ? 0.7751 0.6319 0.6559 0.0274  -0.0343 -0.0545 119  VAL A CG1 
720  C CG2 . VAL A 102 ? 0.8451 0.7054 0.7043 0.0296  -0.0318 -0.0637 119  VAL A CG2 
721  N N   . PRO A 103 ? 0.8071 0.6306 0.7316 0.0160  -0.0692 -0.0495 120  PRO A N   
722  C CA  . PRO A 103 ? 0.8064 0.6320 0.7624 0.0087  -0.0732 -0.0342 120  PRO A CA  
723  C C   . PRO A 103 ? 0.7864 0.6357 0.7460 0.0082  -0.0565 -0.0204 120  PRO A C   
724  O O   . PRO A 103 ? 0.8145 0.6727 0.7530 0.0139  -0.0450 -0.0258 120  PRO A O   
725  C CB  . PRO A 103 ? 0.8294 0.6309 0.7881 0.0135  -0.0858 -0.0418 120  PRO A CB  
726  C CG  . PRO A 103 ? 0.9847 0.7691 0.9137 0.0236  -0.0927 -0.0626 120  PRO A CG  
727  C CD  . PRO A 103 ? 0.8286 0.6316 0.7342 0.0266  -0.0763 -0.0645 120  PRO A CD  
728  N N   . PRO A 104 ? 0.7812 0.6423 0.7683 0.0026  -0.0551 -0.0018 121  PRO A N   
729  C CA  . PRO A 104 ? 0.7660 0.6509 0.7533 0.0053  -0.0398 0.0111  121  PRO A CA  
730  C C   . PRO A 104 ? 0.7844 0.6656 0.7613 0.0119  -0.0357 0.0076  121  PRO A C   
731  O O   . PRO A 104 ? 0.9101 0.7708 0.8885 0.0134  -0.0450 0.0006  121  PRO A O   
732  C CB  . PRO A 104 ? 0.7718 0.6681 0.7934 -0.0001 -0.0408 0.0339  121  PRO A CB  
733  C CG  . PRO A 104 ? 0.7834 0.6566 0.8280 -0.0068 -0.0591 0.0324  121  PRO A CG  
734  C CD  . PRO A 104 ? 0.7899 0.6455 0.8105 -0.0056 -0.0674 0.0097  121  PRO A CD  
735  N N   . LEU A 105 ? 0.8220 0.7230 0.7877 0.0169  -0.0228 0.0113  122  LEU A N   
736  C CA  . LEU A 105 ? 0.8310 0.7342 0.7884 0.0236  -0.0175 0.0103  122  LEU A CA  
737  C C   . LEU A 105 ? 0.8072 0.6971 0.7430 0.0280  -0.0187 -0.0078 122  LEU A C   
738  O O   . LEU A 105 ? 0.8525 0.7462 0.7803 0.0338  -0.0136 -0.0098 122  LEU A O   
739  C CB  . LEU A 105 ? 0.8150 0.7116 0.7946 0.0230  -0.0221 0.0230  122  LEU A CB  
740  C CG  . LEU A 105 ? 0.7816 0.6959 0.7867 0.0207  -0.0184 0.0465  122  LEU A CG  
741  C CD1 . LEU A 105 ? 0.8112 0.7157 0.8428 0.0192  -0.0245 0.0598  122  LEU A CD1 
742  C CD2 . LEU A 105 ? 0.8483 0.7901 0.8412 0.0287  -0.0046 0.0539  122  LEU A CD2 
743  N N   . VAL A 106 ? 0.8094 0.6856 0.7359 0.0266  -0.0248 -0.0197 123  VAL A N   
744  C CA  . VAL A 106 ? 0.7732 0.6394 0.6792 0.0333  -0.0244 -0.0342 123  VAL A CA  
745  C C   . VAL A 106 ? 0.8324 0.7158 0.7257 0.0361  -0.0131 -0.0367 123  VAL A C   
746  O O   . VAL A 106 ? 0.8994 0.7856 0.7854 0.0420  -0.0083 -0.0398 123  VAL A O   
747  C CB  . VAL A 106 ? 0.8284 0.6770 0.7262 0.0338  -0.0341 -0.0453 123  VAL A CB  
748  C CG1 . VAL A 106 ? 0.8100 0.6541 0.6842 0.0435  -0.0302 -0.0574 123  VAL A CG1 
749  C CG2 . VAL A 106 ? 0.9170 0.7443 0.8288 0.0325  -0.0491 -0.0459 123  VAL A CG2 
750  N N   . ILE A 107 ? 0.8942 0.7894 0.7873 0.0320  -0.0098 -0.0350 124  ILE A N   
751  C CA  . ILE A 107 ? 0.8300 0.7395 0.7151 0.0341  -0.0020 -0.0380 124  ILE A CA  
752  C C   . ILE A 107 ? 0.7748 0.6993 0.6649 0.0366  0.0025  -0.0317 124  ILE A C   
753  O O   . ILE A 107 ? 0.8744 0.8064 0.7605 0.0403  0.0063  -0.0353 124  ILE A O   
754  C CB  . ILE A 107 ? 0.9096 0.8250 0.7932 0.0300  -0.0013 -0.0390 124  ILE A CB  
755  C CG1 . ILE A 107 ? 0.8378 0.7389 0.7146 0.0290  -0.0063 -0.0455 124  ILE A CG1 
756  C CG2 . ILE A 107 ? 0.7663 0.6939 0.6457 0.0318  0.0044  -0.0424 124  ILE A CG2 
757  C CD1 . ILE A 107 ? 0.7413 0.6476 0.6171 0.0252  -0.0059 -0.0459 124  ILE A CD1 
758  N N   . GLU A 108 ? 0.8395 0.7697 0.7398 0.0355  0.0019  -0.0211 125  GLU A N   
759  C CA  . GLU A 108 ? 0.7236 0.6698 0.6257 0.0408  0.0061  -0.0144 125  GLU A CA  
760  C C   . GLU A 108 ? 0.8246 0.7674 0.7252 0.0454  0.0067  -0.0161 125  GLU A C   
761  O O   . GLU A 108 ? 0.8940 0.8482 0.7904 0.0505  0.0094  -0.0183 125  GLU A O   
762  C CB  . GLU A 108 ? 0.8041 0.7587 0.7187 0.0406  0.0068  0.0009  125  GLU A CB  
763  C CG  . GLU A 108 ? 0.7208 0.6833 0.6385 0.0378  0.0075  0.0053  125  GLU A CG  
764  C CD  . GLU A 108 ? 0.7855 0.7329 0.7135 0.0294  0.0012  0.0059  125  GLU A CD  
765  O OE1 . GLU A 108 ? 0.8777 0.8092 0.7980 0.0266  -0.0032 -0.0064 125  GLU A OE1 
766  O OE2 . GLU A 108 ? 0.8493 0.8019 0.7941 0.0266  0.0004  0.0197  125  GLU A OE2 
767  N N   . THR A 109 ? 0.7718 0.6985 0.6765 0.0446  0.0030  -0.0159 126  THR A N   
768  C CA  . THR A 109 ? 0.7465 0.6689 0.6506 0.0499  0.0035  -0.0165 126  THR A CA  
769  C C   . THR A 109 ? 0.7591 0.6728 0.6524 0.0531  0.0040  -0.0280 126  THR A C   
770  O O   . THR A 109 ? 0.8214 0.7286 0.7136 0.0585  0.0039  -0.0293 126  THR A O   
771  C CB  . THR A 109 ? 0.7926 0.7020 0.7091 0.0490  -0.0017 -0.0086 126  THR A CB  
772  O OG1 . THR A 109 ? 0.8031 0.6920 0.7195 0.0457  -0.0095 -0.0157 126  THR A OG1 
773  C CG2 . THR A 109 ? 0.7545 0.6761 0.6859 0.0467  -0.0004 0.0074  126  THR A CG2 
774  N N   . ALA A 110 ? 0.8146 0.7294 0.7008 0.0512  0.0053  -0.0349 127  ALA A N   
775  C CA  . ALA A 110 ? 0.7473 0.6572 0.6245 0.0560  0.0077  -0.0424 127  ALA A CA  
776  C C   . ALA A 110 ? 0.7674 0.6894 0.6471 0.0610  0.0128  -0.0415 127  ALA A C   
777  O O   . ALA A 110 ? 0.8852 0.8036 0.7606 0.0676  0.0155  -0.0440 127  ALA A O   
778  C CB  . ALA A 110 ? 0.7965 0.7085 0.6686 0.0531  0.0092  -0.0467 127  ALA A CB  
779  N N   . ALA A 111 ? 0.8213 0.7584 0.7078 0.0594  0.0135  -0.0380 128  ALA A N   
780  C CA  . ALA A 111 ? 0.7907 0.7396 0.6824 0.0639  0.0157  -0.0375 128  ALA A CA  
781  C C   . ALA A 111 ? 0.9134 0.8574 0.8054 0.0697  0.0160  -0.0341 128  ALA A C   
782  O O   . ALA A 111 ? 0.8685 0.8162 0.7627 0.0750  0.0188  -0.0346 128  ALA A O   
783  C CB  . ALA A 111 ? 0.8082 0.7724 0.7047 0.0629  0.0134  -0.0367 128  ALA A CB  
784  N N   . ARG A 112 ? 0.8864 0.8228 0.7790 0.0689  0.0132  -0.0293 129  ARG A N   
785  C CA  . ARG A 112 ? 0.9384 0.8684 0.8335 0.0744  0.0126  -0.0253 129  ARG A CA  
786  C C   . ARG A 112 ? 0.9601 0.8698 0.8493 0.0778  0.0105  -0.0305 129  ARG A C   
787  O O   . ARG A 112 ? 1.0319 0.9382 0.9191 0.0855  0.0121  -0.0319 129  ARG A O   
788  C CB  . ARG A 112 ? 1.0736 1.0053 0.9762 0.0729  0.0105  -0.0151 129  ARG A CB  
789  C CG  . ARG A 112 ? 1.1500 1.0755 1.0581 0.0783  0.0096  -0.0089 129  ARG A CG  
790  C CD  . ARG A 112 ? 1.2623 1.1939 1.1810 0.0776  0.0092  0.0052  129  ARG A CD  
791  N NE  . ARG A 112 ? 1.5415 1.4659 1.4684 0.0824  0.0080  0.0126  129  ARG A NE  
792  C CZ  . ARG A 112 ? 1.5953 1.5249 1.5347 0.0835  0.0084  0.0281  129  ARG A CZ  
793  N NH1 . ARG A 112 ? 1.5575 1.5013 1.5015 0.0813  0.0109  0.0384  129  ARG A NH1 
794  N NH2 . ARG A 112 ? 1.3212 1.2428 1.2694 0.0880  0.0070  0.0347  129  ARG A NH2 
795  N N   . THR A 113 ? 0.9468 0.8429 0.8326 0.0738  0.0060  -0.0342 130  THR A N   
796  C CA  . THR A 113 ? 0.8330 0.7080 0.7101 0.0795  0.0012  -0.0419 130  THR A CA  
797  C C   . THR A 113 ? 0.8980 0.7757 0.7617 0.0873  0.0069  -0.0489 130  THR A C   
798  O O   . THR A 113 ? 0.9322 0.7949 0.7846 0.0970  0.0042  -0.0557 130  THR A O   
799  C CB  . THR A 113 ? 0.8628 0.7230 0.7413 0.0733  -0.0074 -0.0443 130  THR A CB  
800  O OG1 . THR A 113 ? 0.9208 0.7901 0.7944 0.0683  -0.0043 -0.0466 130  THR A OG1 
801  C CG2 . THR A 113 ? 0.7982 0.6585 0.6950 0.0660  -0.0118 -0.0333 130  THR A CG2 
802  N N   . ARG A 114 ? 0.9400 0.8366 0.8060 0.0847  0.0141  -0.0468 131  ARG A N   
803  C CA  . ARG A 114 ? 0.8881 0.7920 0.7477 0.0917  0.0212  -0.0488 131  ARG A CA  
804  C C   . ARG A 114 ? 0.9328 0.8239 0.7772 0.0961  0.0193  -0.0554 131  ARG A C   
805  O O   . ARG A 114 ? 0.9229 0.8141 0.7562 0.1078  0.0243  -0.0573 131  ARG A O   
806  C CB  . ARG A 114 ? 0.9952 0.9021 0.8540 0.1030  0.0258  -0.0471 131  ARG A CB  
807  C CG  . ARG A 114 ? 0.9485 0.8668 0.8211 0.1004  0.0262  -0.0411 131  ARG A CG  
808  C CD  . ARG A 114 ? 1.1045 1.0451 0.9908 0.0953  0.0302  -0.0367 131  ARG A CD  
809  N NE  . ARG A 114 ? 1.2325 1.1859 1.1261 0.1032  0.0367  -0.0326 131  ARG A NE  
810  C CZ  . ARG A 114 ? 1.3248 1.2973 1.2361 0.1001  0.0380  -0.0280 131  ARG A CZ  
811  N NH1 . ARG A 114 ? 1.2600 1.2393 1.1796 0.0908  0.0324  -0.0291 131  ARG A NH1 
812  N NH2 . ARG A 114 ? 1.0758 1.0606 0.9974 0.1073  0.0439  -0.0223 131  ARG A NH2 
813  N N   . LYS A 115 ? 0.9163 0.7978 0.7597 0.0882  0.0122  -0.0583 132  LYS A N   
814  C CA  . LYS A 115 ? 0.9584 0.8275 0.7874 0.0922  0.0082  -0.0654 132  LYS A CA  
815  C C   . LYS A 115 ? 0.9320 0.8142 0.7619 0.0868  0.0137  -0.0630 132  LYS A C   
816  O O   . LYS A 115 ? 0.9028 0.7990 0.7462 0.0771  0.0167  -0.0575 132  LYS A O   
817  C CB  . LYS A 115 ? 0.9486 0.7979 0.7792 0.0869  -0.0050 -0.0698 132  LYS A CB  
818  C CG  . LYS A 115 ? 0.9692 0.7974 0.7937 0.0966  -0.0139 -0.0764 132  LYS A CG  
819  C CD  . LYS A 115 ? 1.1452 0.9508 0.9616 0.0989  -0.0282 -0.0866 132  LYS A CD  
820  C CE  . LYS A 115 ? 1.1159 0.8982 0.9211 0.1132  -0.0385 -0.0970 132  LYS A CE  
821  N NZ  . LYS A 115 ? 1.1206 0.9074 0.9022 0.1319  -0.0296 -0.1021 132  LYS A NZ  
822  N N   . THR A 116 ? 0.9236 0.8006 0.7380 0.0949  0.0143  -0.0675 133  THR A N   
823  C CA  . THR A 116 ? 0.8798 0.7680 0.6942 0.0919  0.0199  -0.0643 133  THR A CA  
824  C C   . THR A 116 ? 0.9590 0.8333 0.7629 0.0902  0.0109  -0.0712 133  THR A C   
825  O O   . THR A 116 ? 0.8797 0.7369 0.6676 0.1000  0.0030  -0.0798 133  THR A O   
826  C CB  . THR A 116 ? 0.8919 0.7917 0.6991 0.1052  0.0311  -0.0598 133  THR A CB  
827  O OG1 . THR A 116 ? 0.9293 0.8437 0.7514 0.1056  0.0386  -0.0522 133  THR A OG1 
828  C CG2 . THR A 116 ? 0.9346 0.8457 0.7447 0.1023  0.0368  -0.0544 133  THR A CG2 
829  N N   . ILE A 117 ? 0.9492 0.8302 0.7622 0.0787  0.0107  -0.0682 134  ILE A N   
830  C CA  . ILE A 117 ? 0.8343 0.7051 0.6411 0.0754  0.0023  -0.0731 134  ILE A CA  
831  C C   . ILE A 117 ? 0.9020 0.7816 0.7004 0.0800  0.0092  -0.0710 134  ILE A C   
832  O O   . ILE A 117 ? 1.0116 0.9075 0.8214 0.0755  0.0183  -0.0632 134  ILE A O   
833  C CB  . ILE A 117 ? 0.8142 0.6872 0.6377 0.0605  -0.0025 -0.0697 134  ILE A CB  
834  C CG1 . ILE A 117 ? 0.8041 0.6693 0.6376 0.0571  -0.0091 -0.0689 134  ILE A CG1 
835  C CG2 . ILE A 117 ? 0.8706 0.7367 0.6908 0.0567  -0.0100 -0.0730 134  ILE A CG2 
836  C CD1 . ILE A 117 ? 0.7821 0.6605 0.6264 0.0549  -0.0019 -0.0623 134  ILE A CD1 
837  N N   . ALA A 118 ? 0.8886 0.7571 0.6680 0.0898  0.0037  -0.0779 135  ALA A N   
838  C CA  . ALA A 118 ? 0.8633 0.7396 0.6327 0.0957  0.0097  -0.0750 135  ALA A CA  
839  C C   . ALA A 118 ? 0.9540 0.8165 0.7129 0.0953  -0.0030 -0.0834 135  ALA A C   
840  O O   . ALA A 118 ? 1.0389 0.8833 0.7851 0.1027  -0.0155 -0.0941 135  ALA A O   
841  C CB  . ALA A 118 ? 0.8573 0.7391 0.6092 0.1154  0.0188  -0.0729 135  ALA A CB  
842  N N   . CYS A 119 ? 0.9238 0.7940 0.6896 0.0870  -0.0012 -0.0791 136  CYS A N   
843  C CA  . CYS A 119 ? 0.9248 0.7840 0.6841 0.0851  -0.0134 -0.0858 136  CYS A CA  
844  C C   . CYS A 119 ? 1.0353 0.9070 0.7947 0.0837  -0.0061 -0.0791 136  CYS A C   
845  O O   . CYS A 119 ? 1.0412 0.9281 0.8050 0.0858  0.0075  -0.0696 136  CYS A O   
846  C CB  . CYS A 119 ? 0.8253 0.6771 0.6038 0.0699  -0.0243 -0.0872 136  CYS A CB  
847  S SG  . CYS A 119 ? 1.1403 1.0099 0.9445 0.0534  -0.0147 -0.0758 136  CYS A SG  
848  N N   . PHE A 120 ? 0.9456 0.8110 0.7029 0.0800  -0.0159 -0.0832 137  PHE A N   
849  C CA  . PHE A 120 ? 0.9042 0.7804 0.6624 0.0783  -0.0099 -0.0769 137  PHE A CA  
850  C C   . PHE A 120 ? 0.9086 0.7800 0.6768 0.0668  -0.0209 -0.0794 137  PHE A C   
851  O O   . PHE A 120 ? 0.8885 0.7466 0.6585 0.0641  -0.0351 -0.0868 137  PHE A O   
852  C CB  . PHE A 120 ? 0.8723 0.7497 0.6054 0.0968  -0.0067 -0.0775 137  PHE A CB  
853  C CG  . PHE A 120 ? 0.8696 0.7297 0.5811 0.1076  -0.0233 -0.0912 137  PHE A CG  
854  C CD1 . PHE A 120 ? 0.8897 0.7455 0.5988 0.1050  -0.0334 -0.0949 137  PHE A CD1 
855  C CD2 . PHE A 120 ? 0.9776 0.8249 0.6715 0.1215  -0.0301 -0.1012 137  PHE A CD2 
856  C CE1 . PHE A 120 ? 0.9483 0.7872 0.6394 0.1152  -0.0517 -0.1088 137  PHE A CE1 
857  C CE2 . PHE A 120 ? 0.9877 0.8164 0.6619 0.1327  -0.0486 -0.1161 137  PHE A CE2 
858  C CZ  . PHE A 120 ? 0.9545 0.7789 0.6280 0.1293  -0.0602 -0.1202 137  PHE A CZ  
859  N N   . ASP A 121 ? 0.9028 0.7856 0.6804 0.0602  -0.0145 -0.0721 138  ASP A N   
860  C CA  . ASP A 121 ? 0.8544 0.7362 0.6402 0.0517  -0.0225 -0.0724 138  ASP A CA  
861  C C   . ASP A 121 ? 0.8998 0.7850 0.6724 0.0595  -0.0209 -0.0710 138  ASP A C   
862  O O   . ASP A 121 ? 0.9036 0.7951 0.6646 0.0703  -0.0110 -0.0668 138  ASP A O   
863  C CB  . ASP A 121 ? 0.8892 0.7816 0.6974 0.0383  -0.0171 -0.0653 138  ASP A CB  
864  C CG  . ASP A 121 ? 0.9434 0.8346 0.7635 0.0296  -0.0265 -0.0650 138  ASP A CG  
865  O OD1 . ASP A 121 ? 0.9230 0.8047 0.7373 0.0320  -0.0384 -0.0703 138  ASP A OD1 
866  O OD2 . ASP A 121 ? 0.9550 0.8555 0.7908 0.0214  -0.0226 -0.0593 138  ASP A OD2 
867  N N   . LEU A 122 ? 0.8563 0.7392 0.6327 0.0547  -0.0301 -0.0727 139  LEU A N   
868  C CA  . LEU A 122 ? 0.8996 0.7845 0.6623 0.0629  -0.0311 -0.0723 139  LEU A CA  
869  C C   . LEU A 122 ? 0.8699 0.7652 0.6486 0.0530  -0.0268 -0.0645 139  LEU A C   
870  O O   . LEU A 122 ? 0.8912 0.7871 0.6875 0.0414  -0.0319 -0.0639 139  LEU A O   
871  C CB  . LEU A 122 ? 0.8887 0.7595 0.6380 0.0696  -0.0497 -0.0837 139  LEU A CB  
872  C CG  . LEU A 122 ? 0.8751 0.7329 0.6030 0.0840  -0.0566 -0.0942 139  LEU A CG  
873  C CD1 . LEU A 122 ? 0.8908 0.7322 0.6080 0.0904  -0.0791 -0.1078 139  LEU A CD1 
874  C CD2 . LEU A 122 ? 1.0345 0.9009 0.7399 0.1012  -0.0422 -0.0897 139  LEU A CD2 
875  N N   . SER A 123 ? 0.9066 0.8106 0.6799 0.0589  -0.0170 -0.0573 140  SER A N   
876  C CA  . SER A 123 ? 0.8032 0.7151 0.5884 0.0525  -0.0142 -0.0508 140  SER A CA  
877  C C   . SER A 123 ? 0.8445 0.7570 0.6121 0.0640  -0.0164 -0.0500 140  SER A C   
878  O O   . SER A 123 ? 0.8634 0.7809 0.6183 0.0760  -0.0073 -0.0444 140  SER A O   
879  C CB  . SER A 123 ? 0.7644 0.6862 0.5653 0.0479  -0.0007 -0.0416 140  SER A CB  
880  O OG  . SER A 123 ? 1.0014 0.9228 0.8155 0.0396  0.0002  -0.0436 140  SER A OG  
881  N N   . CYS A 124 ? 0.8706 0.7798 0.6381 0.0616  -0.0281 -0.0541 141  CYS A N   
882  C CA  . CYS A 124 ? 0.8829 0.7902 0.6296 0.0746  -0.0347 -0.0568 141  CYS A CA  
883  C C   . CYS A 124 ? 0.8975 0.8115 0.6529 0.0703  -0.0358 -0.0513 141  CYS A C   
884  O O   . CYS A 124 ? 1.0286 0.9456 0.8054 0.0571  -0.0369 -0.0490 141  CYS A O   
885  C CB  . CYS A 124 ? 1.0058 0.8988 0.7399 0.0796  -0.0539 -0.0709 141  CYS A CB  
886  S SG  . CYS A 124 ? 1.0006 0.8826 0.7326 0.0799  -0.0567 -0.0790 141  CYS A SG  
887  N N   . ASN A 125 ? 0.9346 0.8519 0.6718 0.0836  -0.0351 -0.0487 142  ASN A N   
888  C CA  . ASN A 125 ? 0.9660 0.8874 0.7058 0.0830  -0.0404 -0.0461 142  ASN A CA  
889  C C   . ASN A 125 ? 0.9223 0.8345 0.6428 0.0930  -0.0599 -0.0582 142  ASN A C   
890  O O   . ASN A 125 ? 1.1138 1.0142 0.8299 0.0933  -0.0724 -0.0699 142  ASN A O   
891  C CB  . ASN A 125 ? 0.9665 0.8995 0.7044 0.0900  -0.0250 -0.0321 142  ASN A CB  
892  C CG  . ASN A 125 ? 1.1123 1.0485 0.8223 0.1110  -0.0197 -0.0288 142  ASN A CG  
893  O OD1 . ASN A 125 ? 1.0735 1.0021 0.7607 0.1226  -0.0288 -0.0394 142  ASN A OD1 
894  N ND2 . ASN A 125 ? 0.9530 0.9011 0.6655 0.1172  -0.0047 -0.0130 142  ASN A ND2 
895  N N   . GLN A 126 ? 0.9979 0.9144 0.7077 0.1016  -0.0639 -0.0561 143  GLN A N   
896  C CA  . GLN A 126 ? 1.0459 0.9532 0.7415 0.1096  -0.0862 -0.0691 143  GLN A CA  
897  C C   . GLN A 126 ? 1.0978 0.9968 0.7585 0.1312  -0.0924 -0.0794 143  GLN A C   
898  O O   . GLN A 126 ? 1.0731 0.9580 0.7248 0.1360  -0.1144 -0.0953 143  GLN A O   
899  C CB  . GLN A 126 ? 0.9566 0.8718 0.6510 0.1131  -0.0895 -0.0639 143  GLN A CB  
900  C CG  . GLN A 126 ? 0.9358 0.8429 0.6333 0.1119  -0.1153 -0.0759 143  GLN A CG  
901  C CD  . GLN A 126 ? 1.1317 1.0483 0.8307 0.1145  -0.1178 -0.0696 143  GLN A CD  
902  O OE1 . GLN A 126 ? 1.1307 1.0585 0.8214 0.1215  -0.1011 -0.0575 143  GLN A OE1 
903  N NE2 . GLN A 126 ? 1.0361 0.9486 0.7487 0.1086  -0.1391 -0.0768 143  GLN A NE2 
904  N N   . THR A 127 ? 1.0846 0.9924 0.7267 0.1455  -0.0742 -0.0703 144  THR A N   
905  C CA  . THR A 127 ? 1.0143 0.9183 0.6187 0.1712  -0.0778 -0.0778 144  THR A CA  
906  C C   . THR A 127 ? 1.0421 0.9449 0.6401 0.1763  -0.0661 -0.0769 144  THR A C   
907  O O   . THR A 127 ? 1.0847 0.9824 0.6506 0.1985  -0.0711 -0.0857 144  THR A O   
908  C CB  . THR A 127 ? 1.0683 0.9872 0.6500 0.1915  -0.0665 -0.0656 144  THR A CB  
909  O OG1 . THR A 127 ? 1.1932 1.1280 0.7910 0.1868  -0.0402 -0.0441 144  THR A OG1 
910  C CG2 . THR A 127 ? 1.1371 1.0577 0.7235 0.1882  -0.0782 -0.0663 144  THR A CG2 
911  N N   . THR A 128 ? 1.2025 1.1101 0.8284 0.1582  -0.0516 -0.0673 145  THR A N   
912  C CA  . THR A 128 ? 1.2483 1.1573 0.8702 0.1632  -0.0394 -0.0645 145  THR A CA  
913  C C   . THR A 128 ? 1.1623 1.0667 0.8156 0.1397  -0.0378 -0.0651 145  THR A C   
914  O O   . THR A 128 ? 1.1194 1.0244 0.7984 0.1207  -0.0404 -0.0630 145  THR A O   
915  C CB  . THR A 128 ? 1.1432 1.0713 0.7625 0.1740  -0.0152 -0.0439 145  THR A CB  
916  O OG1 . THR A 128 ? 1.3920 1.3223 1.0066 0.1812  -0.0048 -0.0413 145  THR A OG1 
917  C CG2 . THR A 128 ? 1.0853 1.0232 0.7399 0.1539  -0.0030 -0.0290 145  THR A CG2 
918  N N   . CYS A 129 ? 1.0688 0.9701 0.7183 0.1432  -0.0328 -0.0673 146  CYS A N   
919  C CA  . CYS A 129 ? 1.0776 0.9765 0.7531 0.1246  -0.0292 -0.0667 146  CYS A CA  
920  C C   . CYS A 129 ? 1.0226 0.9334 0.7022 0.1287  -0.0091 -0.0540 146  CYS A C   
921  O O   . CYS A 129 ? 1.0223 0.9371 0.6795 0.1484  -0.0027 -0.0518 146  CYS A O   
922  C CB  . CYS A 129 ? 1.0164 0.8975 0.6883 0.1229  -0.0464 -0.0832 146  CYS A CB  
923  S SG  . CYS A 129 ? 1.4184 1.2869 1.1079 0.1073  -0.0697 -0.0937 146  CYS A SG  
924  N N   . GLN A 130 ? 0.9881 0.9055 0.6970 0.1114  0.0002  -0.0454 147  GLN A N   
925  C CA  . GLN A 130 ? 0.9898 0.9172 0.7102 0.1117  0.0161  -0.0342 147  GLN A CA  
926  C C   . GLN A 130 ? 0.8882 0.8074 0.6178 0.1022  0.0119  -0.0424 147  GLN A C   
927  O O   . GLN A 130 ? 0.9563 0.8700 0.7029 0.0860  0.0045  -0.0476 147  GLN A O   
928  C CB  . GLN A 130 ? 0.9020 0.8410 0.6499 0.1004  0.0271  -0.0199 147  GLN A CB  
929  C CG  . GLN A 130 ? 1.1139 1.0611 0.8838 0.0950  0.0389  -0.0102 147  GLN A CG  
930  C CD  . GLN A 130 ? 1.2521 1.2079 1.0510 0.0848  0.0460  0.0021  147  GLN A CD  
931  O OE1 . GLN A 130 ? 1.1593 1.1209 0.9584 0.0892  0.0496  0.0110  147  GLN A OE1 
932  N NE2 . GLN A 130 ? 1.1073 1.0632 0.9306 0.0720  0.0468  0.0021  147  GLN A NE2 
933  N N   . PRO A 131 ? 0.9186 0.8378 0.6372 0.1131  0.0165  -0.0431 148  PRO A N   
934  C CA  . PRO A 131 ? 0.9256 0.8371 0.6530 0.1048  0.0126  -0.0503 148  PRO A CA  
935  C C   . PRO A 131 ? 1.0290 0.9518 0.7823 0.0947  0.0251  -0.0394 148  PRO A C   
936  O O   . PRO A 131 ? 1.0801 1.0165 0.8407 0.1002  0.0384  -0.0257 148  PRO A O   
937  C CB  . PRO A 131 ? 0.8656 0.7710 0.5656 0.1246  0.0106  -0.0571 148  PRO A CB  
938  C CG  . PRO A 131 ? 0.8893 0.8025 0.5654 0.1450  0.0159  -0.0516 148  PRO A CG  
939  C CD  . PRO A 131 ? 1.0725 0.9989 0.7671 0.1361  0.0249  -0.0375 148  PRO A CD  
940  N N   . THR A 132 ? 0.9321 0.8496 0.7014 0.0803  0.0197  -0.0448 149  THR A N   
941  C CA  . THR A 132 ? 0.8971 0.8224 0.6892 0.0713  0.0273  -0.0385 149  THR A CA  
942  C C   . THR A 132 ? 0.9677 0.8870 0.7550 0.0737  0.0250  -0.0447 149  THR A C   
943  O O   . THR A 132 ? 0.9316 0.8400 0.7175 0.0677  0.0146  -0.0541 149  THR A O   
944  C CB  . THR A 132 ? 0.8997 0.8255 0.7118 0.0554  0.0233  -0.0394 149  THR A CB  
945  O OG1 . THR A 132 ? 1.0089 0.9384 0.8236 0.0543  0.0241  -0.0349 149  THR A OG1 
946  C CG2 . THR A 132 ? 0.8407 0.7743 0.6750 0.0486  0.0291  -0.0343 149  THR A CG2 
947  N N   . VAL A 133 ? 0.8411 0.7683 0.6279 0.0829  0.0349  -0.0378 150  VAL A N   
948  C CA  . VAL A 133 ? 0.8660 0.7884 0.6470 0.0877  0.0340  -0.0427 150  VAL A CA  
949  C C   . VAL A 133 ? 0.9011 0.8287 0.7068 0.0748  0.0360  -0.0401 150  VAL A C   
950  O O   . VAL A 133 ? 0.8112 0.7513 0.6371 0.0706  0.0438  -0.0301 150  VAL A O   
951  C CB  . VAL A 133 ? 0.9075 0.8380 0.6744 0.1067  0.0445  -0.0358 150  VAL A CB  
952  C CG1 . VAL A 133 ? 0.8284 0.7549 0.5918 0.1117  0.0444  -0.0401 150  VAL A CG1 
953  C CG2 . VAL A 133 ? 0.8493 0.7737 0.5861 0.1232  0.0406  -0.0409 150  VAL A CG2 
954  N N   . PHE A 134 ? 0.8643 0.7821 0.6696 0.0692  0.0278  -0.0488 151  PHE A N   
955  C CA  . PHE A 134 ? 0.7886 0.7106 0.6121 0.0602  0.0284  -0.0477 151  PHE A CA  
956  C C   . PHE A 134 ? 0.8143 0.7340 0.6316 0.0683  0.0302  -0.0493 151  PHE A C   
957  O O   . PHE A 134 ? 0.7942 0.7020 0.5931 0.0768  0.0248  -0.0564 151  PHE A O   
958  C CB  . PHE A 134 ? 0.7439 0.6595 0.5732 0.0490  0.0190  -0.0535 151  PHE A CB  
959  C CG  . PHE A 134 ? 0.7676 0.6860 0.6030 0.0418  0.0171  -0.0522 151  PHE A CG  
960  C CD1 . PHE A 134 ? 0.8122 0.7401 0.6646 0.0352  0.0199  -0.0485 151  PHE A CD1 
961  C CD2 . PHE A 134 ? 0.7938 0.7047 0.6186 0.0425  0.0110  -0.0557 151  PHE A CD2 
962  C CE1 . PHE A 134 ? 0.7708 0.7005 0.6278 0.0302  0.0179  -0.0479 151  PHE A CE1 
963  C CE2 . PHE A 134 ? 0.9663 0.8807 0.7972 0.0366  0.0096  -0.0539 151  PHE A CE2 
964  C CZ  . PHE A 134 ? 0.7867 0.7105 0.6331 0.0308  0.0137  -0.0499 151  PHE A CZ  
965  N N   . LEU A 135 ? 0.7851 0.7155 0.6190 0.0661  0.0363  -0.0432 152  LEU A N   
966  C CA  . LEU A 135 ? 0.7681 0.6989 0.5998 0.0732  0.0390  -0.0432 152  LEU A CA  
967  C C   . LEU A 135 ? 0.8377 0.7747 0.6896 0.0635  0.0377  -0.0420 152  LEU A C   
968  O O   . LEU A 135 ? 0.8570 0.8055 0.7285 0.0579  0.0406  -0.0360 152  LEU A O   
969  C CB  . LEU A 135 ? 0.7733 0.7157 0.6035 0.0863  0.0506  -0.0335 152  LEU A CB  
970  C CG  . LEU A 135 ? 0.7747 0.7213 0.6059 0.0946  0.0554  -0.0311 152  LEU A CG  
971  C CD1 . LEU A 135 ? 0.8361 0.7659 0.6412 0.1052  0.0491  -0.0422 152  LEU A CD1 
972  C CD2 . LEU A 135 ? 0.8627 0.8277 0.7026 0.1054  0.0691  -0.0162 152  LEU A CD2 
973  N N   . MET A 136 ? 0.8707 0.7999 0.7188 0.0625  0.0323  -0.0476 153  MET A N   
974  C CA  . MET A 136 ? 0.8388 0.7743 0.7024 0.0559  0.0306  -0.0467 153  MET A CA  
975  C C   . MET A 136 ? 0.9405 0.8720 0.7995 0.0621  0.0306  -0.0481 153  MET A C   
976  O O   . MET A 136 ? 0.8562 0.7744 0.6999 0.0678  0.0270  -0.0530 153  MET A O   
977  C CB  . MET A 136 ? 0.7220 0.6545 0.5886 0.0465  0.0234  -0.0503 153  MET A CB  
978  C CG  . MET A 136 ? 0.8106 0.7293 0.6655 0.0461  0.0169  -0.0546 153  MET A CG  
979  S SD  . MET A 136 ? 0.8951 0.8156 0.7568 0.0365  0.0113  -0.0542 153  MET A SD  
980  C CE  . MET A 136 ? 0.7296 0.6391 0.5812 0.0360  0.0068  -0.0571 153  MET A CE  
981  N N   . GLY A 137 ? 0.8632 0.8053 0.7364 0.0614  0.0330  -0.0443 154  GLY A N   
982  C CA  . GLY A 137 ? 0.7471 0.6875 0.6180 0.0676  0.0337  -0.0444 154  GLY A CA  
983  C C   . GLY A 137 ? 0.8278 0.7796 0.7159 0.0639  0.0328  -0.0417 154  GLY A C   
984  O O   . GLY A 137 ? 0.8054 0.7654 0.7063 0.0569  0.0299  -0.0414 154  GLY A O   
985  N N   . PRO A 138 ? 0.9051 0.8570 0.7928 0.0697  0.0339  -0.0408 155  PRO A N   
986  C CA  . PRO A 138 ? 0.9182 0.8817 0.8216 0.0677  0.0321  -0.0385 155  PRO A CA  
987  C C   . PRO A 138 ? 0.8766 0.8559 0.8009 0.0668  0.0353  -0.0327 155  PRO A C   
988  O O   . PRO A 138 ? 0.8261 0.8095 0.7532 0.0705  0.0423  -0.0271 155  PRO A O   
989  C CB  . PRO A 138 ? 0.7971 0.7562 0.6943 0.0758  0.0338  -0.0378 155  PRO A CB  
990  C CG  . PRO A 138 ? 0.7482 0.6891 0.6258 0.0800  0.0326  -0.0424 155  PRO A CG  
991  C CD  . PRO A 138 ? 0.8330 0.7728 0.7050 0.0794  0.0350  -0.0431 155  PRO A CD  
992  N N   . ILE A 139 ? 0.9361 0.9248 0.8765 0.0625  0.0292  -0.0333 156  ILE A N   
993  C CA  . ILE A 139 ? 0.8368 0.8397 0.8040 0.0603  0.0286  -0.0280 156  ILE A CA  
994  C C   . ILE A 139 ? 0.9537 0.9659 0.9309 0.0679  0.0374  -0.0182 156  ILE A C   
995  O O   . ILE A 139 ? 0.8285 0.8514 0.8248 0.0683  0.0427  -0.0087 156  ILE A O   
996  C CB  . ILE A 139 ? 0.7653 0.7745 0.7458 0.0567  0.0171  -0.0332 156  ILE A CB  
997  C CG1 . ILE A 139 ? 0.8844 0.8871 0.8549 0.0520  0.0096  -0.0417 156  ILE A CG1 
998  C CG2 . ILE A 139 ? 0.8773 0.9000 0.8910 0.0542  0.0132  -0.0280 156  ILE A CG2 
999  C CD1 . ILE A 139 ? 0.8632 0.8654 0.8443 0.0465  0.0087  -0.0412 156  ILE A CD1 
1000 N N   . GLN A 140 ? 0.9526 0.9618 0.9180 0.0749  0.0398  -0.0189 157  GLN A N   
1001 C CA  . GLN A 140 ? 0.8456 0.8647 0.8193 0.0843  0.0484  -0.0097 157  GLN A CA  
1002 C C   . GLN A 140 ? 0.8689 0.8883 0.8333 0.0927  0.0598  -0.0030 157  GLN A C   
1003 O O   . GLN A 140 ? 0.8207 0.8548 0.7991 0.1006  0.0689  0.0089  157  GLN A O   
1004 C CB  . GLN A 140 ? 0.9637 0.9763 0.9232 0.0911  0.0478  -0.0132 157  GLN A CB  
1005 C CG  . GLN A 140 ? 1.0677 1.0914 1.0354 0.1022  0.0562  -0.0042 157  GLN A CG  
1006 C CD  . GLN A 140 ? 1.1900 1.2344 1.1922 0.0987  0.0539  0.0039  157  GLN A CD  
1007 O OE1 . GLN A 140 ? 1.1612 1.2092 1.1792 0.0886  0.0435  0.0002  157  GLN A OE1 
1008 N NE2 . GLN A 140 ? 1.2643 1.3222 1.2787 0.1083  0.0624  0.0148  157  GLN A NE2 
1009 N N   . THR A 141 ? 0.8699 0.8750 0.8116 0.0926  0.0597  -0.0092 158  THR A N   
1010 C CA  . THR A 141 ? 0.8577 0.8635 0.7875 0.1028  0.0696  -0.0036 158  THR A CA  
1011 C C   . THR A 141 ? 0.9326 0.9565 0.8886 0.1003  0.0759  0.0100  158  THR A C   
1012 O O   . THR A 141 ? 0.8968 0.9280 0.8477 0.1115  0.0869  0.0196  158  THR A O   
1013 C CB  . THR A 141 ? 0.7824 0.7688 0.6842 0.1024  0.0653  -0.0142 158  THR A CB  
1014 O OG1 . THR A 141 ? 1.1237 1.1057 1.0030 0.1186  0.0725  -0.0134 158  THR A OG1 
1015 C CG2 . THR A 141 ? 0.8219 0.8102 0.7326 0.0917  0.0629  -0.0134 158  THR A CG2 
1016 N N   . CYS A 142 ? 0.9625 0.9939 0.9471 0.0872  0.0686  0.0114  159  CYS A N   
1017 C CA  . CYS A 142 ? 0.9567 1.0056 0.9754 0.0837  0.0725  0.0260  159  CYS A CA  
1018 C C   . CYS A 142 ? 0.9051 0.9744 0.9470 0.0926  0.0823  0.0426  159  CYS A C   
1019 O O   . CYS A 142 ? 0.9693 1.0559 1.0431 0.0918  0.0881  0.0594  159  CYS A O   
1020 C CB  . CYS A 142 ? 0.8870 0.9360 0.9315 0.0688  0.0585  0.0206  159  CYS A CB  
1021 S SG  . CYS A 142 ? 1.0658 1.0971 1.0914 0.0595  0.0497  0.0068  159  CYS A SG  
1022 N N   . ILE A 143 ? 0.9980 1.0666 1.0273 0.1013  0.0845  0.0398  160  ILE A N   
1023 C CA  . ILE A 143 ? 0.9281 1.0168 0.9770 0.1117  0.0946  0.0556  160  ILE A CA  
1024 C C   . ILE A 143 ? 0.9208 1.0068 0.9362 0.1319  0.1072  0.0570  160  ILE A C   
1025 O O   . ILE A 143 ? 0.9564 1.0611 0.9808 0.1456  0.1215  0.0744  160  ILE A O   
1026 C CB  . ILE A 143 ? 0.8575 0.9510 0.9265 0.1059  0.0850  0.0523  160  ILE A CB  
1027 C CG1 . ILE A 143 ? 0.8323 0.9310 0.9381 0.0894  0.0713  0.0518  160  ILE A CG1 
1028 C CG2 . ILE A 143 ? 0.8011 0.9147 0.8867 0.1184  0.0960  0.0680  160  ILE A CG2 
1029 C CD1 . ILE A 143 ? 0.9662 1.0689 1.0894 0.0847  0.0591  0.0463  160  ILE A CD1 
1030 N N   . THR A 144 ? 0.9013 0.9642 0.8789 0.1353  0.1016  0.0394  161  THR A N   
1031 C CA  . THR A 144 ? 0.9319 0.9877 0.8762 0.1555  0.1095  0.0367  161  THR A CA  
1032 C C   . THR A 144 ? 0.8539 0.9085 0.7764 0.1675  0.1179  0.0399  161  THR A C   
1033 O O   . THR A 144 ? 1.0949 1.1531 0.9965 0.1892  0.1280  0.0440  161  THR A O   
1034 C CB  . THR A 144 ? 0.9188 0.9485 0.8351 0.1541  0.0982  0.0172  161  THR A CB  
1035 O OG1 . THR A 144 ? 1.0506 1.0614 0.9491 0.1454  0.0897  0.0051  161  THR A OG1 
1036 C CG2 . THR A 144 ? 0.8396 0.8709 0.7759 0.1418  0.0893  0.0143  161  THR A CG2 
1037 N N   . THR A 145 ? 0.9983 1.0484 0.9237 0.1558  0.1138  0.0379  162  THR A N   
1038 C CA  . THR A 145 ? 1.0075 1.0565 0.9118 0.1666  0.1205  0.0406  162  THR A CA  
1039 C C   . THR A 145 ? 1.1246 1.1993 1.0595 0.1669  0.1325  0.0634  162  THR A C   
1040 O O   . THR A 145 ? 1.1300 1.2191 1.0558 0.1865  0.1469  0.0771  162  THR A O   
1041 C CB  . THR A 145 ? 1.0492 1.0748 0.9341 0.1549  0.1079  0.0235  162  THR A CB  
1042 O OG1 . THR A 145 ? 1.0733 1.0773 0.9408 0.1511  0.0959  0.0058  162  THR A OG1 
1043 C CG2 . THR A 145 ? 1.0780 1.0982 0.9324 0.1699  0.1125  0.0220  162  THR A CG2 
1044 N N   . LYS A 146 ? 1.0926 1.1735 1.0642 0.1466  0.1263  0.0682  163  LYS A N   
1045 C CA  . LYS A 146 ? 1.1388 1.2435 1.1503 0.1433  0.1348  0.0911  163  LYS A CA  
1046 C C   . LYS A 146 ? 1.0930 1.2003 1.0900 0.1519  0.1436  0.0990  163  LYS A C   
1047 O O   . LYS A 146 ? 0.9673 1.0743 0.9835 0.1386  0.1393  0.1022  163  LYS A O   
1048 C CB  . LYS A 146 ? 1.1488 1.2802 1.1868 0.1550  0.1478  0.1127  163  LYS A CB  
1049 C CG  . LYS A 146 ? 1.2507 1.4059 1.3479 0.1438  0.1500  0.1355  163  LYS A CG  
1050 C CD  . LYS A 146 ? 1.3072 1.4582 1.4360 0.1241  0.1330  0.1265  163  LYS A CD  
1051 C CE  . LYS A 146 ? 1.3779 1.5524 1.5705 0.1143  0.1327  0.1493  163  LYS A CE  
1052 N NZ  . LYS A 146 ? 1.3189 1.4913 1.5414 0.0994  0.1152  0.1403  163  LYS A NZ  
1053 N N   . SER A 147 ? 1.2119 1.3217 1.1743 0.1756  0.1552  0.1018  164  SER A N   
1054 C CA  . SER A 147 ? 1.1880 1.3029 1.1328 0.1883  0.1646  0.1105  164  SER A CA  
1055 C C   . SER A 147 ? 1.3145 1.4091 1.2019 0.2066  0.1619  0.0912  164  SER A C   
1056 O O   . SER A 147 ? 1.2671 1.3566 1.1322 0.2211  0.1626  0.0835  164  SER A O   
1057 C CB  . SER A 147 ? 1.1263 1.2753 1.0954 0.2050  0.1855  0.1427  164  SER A CB  
1058 O OG  . SER A 147 ? 1.1735 1.3277 1.1115 0.2264  0.1967  0.1497  164  SER A OG  
1059 N N   . CYS A 148 ? 1.3886 1.4707 1.2535 0.2063  0.1572  0.0829  165  CYS A N   
1060 C CA  . CYS A 148 ? 1.3550 1.4172 1.1678 0.2241  0.1518  0.0641  165  CYS A CA  
1061 C C   . CYS A 148 ? 1.3383 1.4015 1.1344 0.2312  0.1545  0.0677  165  CYS A C   
1062 O O   . CYS A 148 ? 1.3393 1.4183 1.1648 0.2218  0.1615  0.0853  165  CYS A O   
1063 C CB  . CYS A 148 ? 1.3311 1.3621 1.1283 0.2096  0.1317  0.0366  165  CYS A CB  
1064 S SG  . CYS A 148 ? 1.9499 1.9537 1.6909 0.2284  0.1204  0.0131  165  CYS A SG  
1065 N N   . LEU A 149 ? 1.2095 1.2541 0.9592 0.2477  0.1471  0.0497  166  LEU A N   
1066 C CA  . LEU A 149 ? 1.2167 1.2607 0.9436 0.2580  0.1479  0.0503  166  LEU A CA  
1067 C C   . LEU A 149 ? 1.2328 1.2440 0.9239 0.2569  0.1271  0.0208  166  LEU A C   
1068 O O   . LEU A 149 ? 1.2822 1.2795 0.9376 0.2772  0.1209  0.0057  166  LEU A O   
1069 C CB  . LEU A 149 ? 1.0614 1.1277 0.7660 0.2926  0.1660  0.0674  166  LEU A CB  
1070 C CG  . LEU A 149 ? 1.0844 1.1645 0.7813 0.3032  0.1749  0.0817  166  LEU A CG  
1071 C CD1 . LEU A 149 ? 1.0530 1.1591 0.8036 0.2861  0.1884  0.1111  166  LEU A CD1 
1072 C CD2 . LEU A 149 ? 1.0724 1.1667 0.7282 0.3442  0.1877  0.0892  166  LEU A CD2 
1073 N N   . LEU A 150 ? 1.1879 1.1867 0.8904 0.2341  0.1157  0.0129  167  LEU A N   
1074 C CA  . LEU A 150 ? 1.0924 1.0632 0.7681 0.2312  0.0961  -0.0113 167  LEU A CA  
1075 C C   . LEU A 150 ? 1.1528 1.1252 0.7988 0.2500  0.0968  -0.0112 167  LEU A C   
1076 O O   . LEU A 150 ? 1.2318 1.2277 0.8835 0.2600  0.1131  0.0095  167  LEU A O   
1077 C CB  . LEU A 150 ? 1.0628 1.0227 0.7652 0.1996  0.0846  -0.0178 167  LEU A CB  
1078 C CG  . LEU A 150 ? 1.0982 1.0543 0.8275 0.1801  0.0807  -0.0205 167  LEU A CG  
1079 C CD1 . LEU A 150 ? 0.9961 0.9462 0.7485 0.1537  0.0719  -0.0239 167  LEU A CD1 
1080 C CD2 . LEU A 150 ? 1.1699 1.1056 0.8790 0.1870  0.0691  -0.0380 167  LEU A CD2 
1081 N N   . GLY A 151 ? 1.0515 0.9989 0.6680 0.2547  0.0780  -0.0339 168  GLY A N   
1082 C CA  . GLY A 151 ? 1.0076 0.9537 0.5933 0.2729  0.0749  -0.0374 168  GLY A CA  
1083 C C   . GLY A 151 ? 1.1747 1.0966 0.7544 0.2588  0.0528  -0.0569 168  GLY A C   
1084 O O   . GLY A 151 ? 1.0052 0.9039 0.5861 0.2480  0.0352  -0.0752 168  GLY A O   
1085 N N   . LEU A 152 ? 1.1708 1.0990 0.7467 0.2589  0.0537  -0.0516 169  LEU A N   
1086 C CA  . LEU A 152 ? 1.0629 0.9709 0.6336 0.2475  0.0332  -0.0683 169  LEU A CA  
1087 C C   . LEU A 152 ? 1.1708 1.0859 0.7145 0.2673  0.0345  -0.0654 169  LEU A C   
1088 O O   . LEU A 152 ? 1.2656 1.2029 0.8222 0.2663  0.0513  -0.0446 169  LEU A O   
1089 C CB  . LEU A 152 ? 1.0838 0.9921 0.6944 0.2135  0.0319  -0.0633 169  LEU A CB  
1090 C CG  . LEU A 152 ? 1.0244 0.9128 0.6362 0.1990  0.0108  -0.0791 169  LEU A CG  
1091 C CD1 . LEU A 152 ? 1.0204 0.8835 0.6224 0.1999  -0.0095 -0.1001 169  LEU A CD1 
1092 C CD2 . LEU A 152 ? 1.0004 0.8942 0.6493 0.1698  0.0133  -0.0710 169  LEU A CD2 
1093 N N   . GLY A 153 ? 1.2719 1.1680 0.7797 0.2859  0.0157  -0.0862 170  GLY A N   
1094 C CA  . GLY A 153 ? 1.2653 1.1673 0.7427 0.3080  0.0146  -0.0857 170  GLY A CA  
1095 C C   . GLY A 153 ? 1.3027 1.2325 0.7622 0.3367  0.0391  -0.0648 170  GLY A C   
1096 O O   . GLY A 153 ? 1.3898 1.3230 0.8316 0.3577  0.0457  -0.0652 170  GLY A O   
1097 N N   . ASP A 154 ? 1.3484 1.2997 0.8144 0.3383  0.0536  -0.0446 171  ASP A N   
1098 C CA  . ASP A 154 ? 1.3749 1.3574 0.8321 0.3636  0.0795  -0.0182 171  ASP A CA  
1099 C C   . ASP A 154 ? 1.3875 1.3931 0.8936 0.3435  0.1023  0.0099  171  ASP A C   
1100 O O   . ASP A 154 ? 1.3656 1.4003 0.8788 0.3576  0.1249  0.0380  171  ASP A O   
1101 C CB  . ASP A 154 ? 1.4219 1.4158 0.8583 0.3801  0.0822  -0.0101 171  ASP A CB  
1102 C CG  . ASP A 154 ? 1.4957 1.4895 0.9677 0.3487  0.0801  -0.0030 171  ASP A CG  
1103 O OD1 . ASP A 154 ? 1.5480 1.5665 1.0413 0.3472  0.1000  0.0247  171  ASP A OD1 
1104 O OD2 . ASP A 154 ? 1.5782 1.5477 1.0589 0.3259  0.0588  -0.0239 171  ASP A OD2 
1105 N N   . GLN A 155 ? 1.3619 1.3557 0.9030 0.3119  0.0959  0.0038  172  GLN A N   
1106 C CA  . GLN A 155 ? 1.2185 1.2303 0.8083 0.2905  0.1123  0.0264  172  GLN A CA  
1107 C C   . GLN A 155 ? 1.1773 1.1877 0.7774 0.2882  0.1152  0.0240  172  GLN A C   
1108 O O   . GLN A 155 ? 1.3098 1.2970 0.8941 0.2861  0.0987  0.0003  172  GLN A O   
1109 C CB  . GLN A 155 ? 1.1242 1.1259 0.7485 0.2555  0.1029  0.0227  172  GLN A CB  
1110 C CG  . GLN A 155 ? 1.1163 1.1207 0.7366 0.2551  0.1012  0.0273  172  GLN A CG  
1111 C CD  . GLN A 155 ? 1.2474 1.2812 0.8865 0.2634  0.1236  0.0591  172  GLN A CD  
1112 O OE1 . GLN A 155 ? 1.3761 1.4261 1.0510 0.2550  0.1377  0.0786  172  GLN A OE1 
1113 N NE2 . GLN A 155 ? 1.2989 1.3400 0.9164 0.2802  0.1262  0.0654  172  GLN A NE2 
1114 N N   . ARG A 156 ? 1.1430 1.1790 0.7725 0.2886  0.1356  0.0498  173  ARG A N   
1115 C CA  . ARG A 156 ? 1.1286 1.1674 0.7776 0.2825  0.1399  0.0518  173  ARG A CA  
1116 C C   . ARG A 156 ? 1.2164 1.2603 0.9190 0.2495  0.1418  0.0624  173  ARG A C   
1117 O O   . ARG A 156 ? 1.3148 1.3693 1.0429 0.2382  0.1471  0.0774  173  ARG A O   
1118 C CB  . ARG A 156 ? 1.1699 1.2357 0.8120 0.3115  0.1613  0.0737  173  ARG A CB  
1119 C CG  . ARG A 156 ? 1.2593 1.3197 0.8442 0.3488  0.1589  0.0610  173  ARG A CG  
1120 C CD  . ARG A 156 ? 1.4187 1.5090 0.9989 0.3785  0.1821  0.0847  173  ARG A CD  
1121 N NE  . ARG A 156 ? 1.7676 1.8550 1.2890 0.4194  0.1808  0.0735  173  ARG A NE  
1122 C CZ  . ARG A 156 ? 1.8134 1.9270 1.3180 0.4539  0.2007  0.0923  173  ARG A CZ  
1123 N NH1 . ARG A 156 ? 1.7223 1.8680 1.2691 0.4503  0.2238  0.1252  173  ARG A NH1 
1124 N NH2 . ARG A 156 ? 1.8327 1.9410 1.2789 0.4933  0.1969  0.0783  173  ARG A NH2 
1125 N N   . ILE A 157 ? 1.0659 1.1016 0.7849 0.2354  0.1362  0.0539  174  ILE A N   
1126 C CA  . ILE A 157 ? 1.0414 1.0774 0.8058 0.2054  0.1332  0.0578  174  ILE A CA  
1127 C C   . ILE A 157 ? 1.1062 1.1567 0.8948 0.2060  0.1428  0.0697  174  ILE A C   
1128 O O   . ILE A 157 ? 1.0921 1.1316 0.8663 0.2097  0.1370  0.0559  174  ILE A O   
1129 C CB  . ILE A 157 ? 0.9241 0.9328 0.6842 0.1846  0.1128  0.0324  174  ILE A CB  
1130 C CG1 . ILE A 157 ? 1.0318 1.0287 0.7747 0.1820  0.1033  0.0231  174  ILE A CG1 
1131 C CG2 . ILE A 157 ? 0.9798 0.9901 0.7817 0.1586  0.1098  0.0352  174  ILE A CG2 
1132 C CD1 . ILE A 157 ? 1.0469 1.0189 0.7835 0.1654  0.0838  0.0000  174  ILE A CD1 
1133 N N   . GLN A 158 ? 0.9898 1.0649 0.8182 0.2024  0.1567  0.0959  175  GLN A N   
1134 C CA  . GLN A 158 ? 0.9810 1.0722 0.8408 0.2006  0.1649  0.1095  175  GLN A CA  
1135 C C   . GLN A 158 ? 1.0963 1.1739 0.9845 0.1724  0.1504  0.0966  175  GLN A C   
1136 O O   . GLN A 158 ? 1.1135 1.1900 1.0316 0.1529  0.1448  0.0995  175  GLN A O   
1137 C CB  . GLN A 158 ? 0.9922 1.1151 0.8901 0.2062  0.1834  0.1441  175  GLN A CB  
1138 C CG  . GLN A 158 ? 1.0849 1.2250 1.0315 0.1964  0.1885  0.1604  175  GLN A CG  
1139 C CD  . GLN A 158 ? 1.1940 1.3429 1.1243 0.2156  0.1968  0.1619  175  GLN A CD  
1140 O OE1 . GLN A 158 ? 1.2649 1.4085 1.1469 0.2394  0.2002  0.1525  175  GLN A OE1 
1141 N NE2 . GLN A 158 ? 1.1796 1.3413 1.1505 0.2064  0.1989  0.1729  175  GLN A NE2 
1142 N N   . VAL A 159 ? 1.0480 1.1151 0.9255 0.1719  0.1439  0.0822  176  VAL A N   
1143 C CA  . VAL A 159 ? 1.0474 1.1022 0.9453 0.1492  0.1303  0.0690  176  VAL A CA  
1144 C C   . VAL A 159 ? 0.9797 1.0541 0.9189 0.1448  0.1368  0.0856  176  VAL A C   
1145 O O   . VAL A 159 ? 1.0756 1.1611 1.0102 0.1599  0.1460  0.0930  176  VAL A O   
1146 C CB  . VAL A 159 ? 1.0345 1.0660 0.8988 0.1506  0.1184  0.0446  176  VAL A CB  
1147 C CG1 . VAL A 159 ? 0.9934 1.0160 0.8788 0.1296  0.1064  0.0342  176  VAL A CG1 
1148 C CG2 . VAL A 159 ? 0.8877 0.8999 0.7167 0.1539  0.1097  0.0289  176  VAL A CG2 
1149 N N   . ASN A 160 ? 0.8803 0.9585 0.8604 0.1250  0.1307  0.0907  177  ASN A N   
1150 C CA  . ASN A 160 ? 1.0012 1.0963 1.0274 0.1177  0.1323  0.1051  177  ASN A CA  
1151 C C   . ASN A 160 ? 0.8808 0.9612 0.9192 0.0986  0.1146  0.0869  177  ASN A C   
1152 O O   . ASN A 160 ? 0.8295 0.8951 0.8655 0.0857  0.1028  0.0738  177  ASN A O   
1153 C CB  . ASN A 160 ? 1.0118 1.1262 1.0829 0.1131  0.1392  0.1301  177  ASN A CB  
1154 C CG  . ASN A 160 ? 1.1210 1.2561 1.1848 0.1346  0.1595  0.1537  177  ASN A CG  
1155 O OD1 . ASN A 160 ? 1.2349 1.3787 1.2752 0.1542  0.1707  0.1579  177  ASN A OD1 
1156 N ND2 . ASN A 160 ? 1.1272 1.2709 1.2103 0.1327  0.1646  0.1699  177  ASN A ND2 
1157 N N   . TYR A 161 ? 0.8449 0.9309 0.8954 0.0986  0.1131  0.0866  178  TYR A N   
1158 C CA  . TYR A 161 ? 0.8238 0.9003 0.8884 0.0834  0.0971  0.0721  178  TYR A CA  
1159 C C   . TYR A 161 ? 0.8722 0.9659 0.9922 0.0744  0.0940  0.0874  178  TYR A C   
1160 O O   . TYR A 161 ? 0.9102 1.0234 1.0528 0.0818  0.1036  0.1049  178  TYR A O   
1161 C CB  . TYR A 161 ? 0.9861 1.0557 1.0265 0.0897  0.0954  0.0602  178  TYR A CB  
1162 C CG  . TYR A 161 ? 0.9059 0.9555 0.8973 0.0968  0.0943  0.0437  178  TYR A CG  
1163 C CD1 . TYR A 161 ? 0.8874 0.9379 0.8503 0.1150  0.1057  0.0477  178  TYR A CD1 
1164 C CD2 . TYR A 161 ? 0.8747 0.9052 0.8498 0.0866  0.0811  0.0246  178  TYR A CD2 
1165 C CE1 . TYR A 161 ? 0.9919 1.0221 0.9137 0.1213  0.1011  0.0312  178  TYR A CE1 
1166 C CE2 . TYR A 161 ? 0.7697 0.7823 0.7072 0.0919  0.0785  0.0113  178  TYR A CE2 
1167 C CZ  . TYR A 161 ? 0.9652 0.9765 0.8772 0.1084  0.0872  0.0137  178  TYR A CZ  
1168 O OH  . TYR A 161 ? 0.9003 0.8917 0.7782 0.1134  0.0813  -0.0008 178  TYR A OH  
1169 N N   . GLU A 162 ? 0.9217 1.0082 1.0649 0.0593  0.0798  0.0809  179  GLU A N   
1170 C CA  . GLU A 162 ? 0.8964 0.9957 1.0960 0.0496  0.0724  0.0933  179  GLU A CA  
1171 C C   . GLU A 162 ? 0.8460 0.9315 1.0539 0.0371  0.0503  0.0727  179  GLU A C   
1172 O O   . GLU A 162 ? 0.8521 0.9196 1.0342 0.0326  0.0413  0.0544  179  GLU A O   
1173 C CB  . GLU A 162 ? 0.8915 0.9975 1.1198 0.0460  0.0764  0.1103  179  GLU A CB  
1174 C CG  . GLU A 162 ? 1.1274 1.2535 1.3566 0.0605  0.0990  0.1364  179  GLU A CG  
1175 C CD  . GLU A 162 ? 1.2203 1.3582 1.4919 0.0562  0.1029  0.1590  179  GLU A CD  
1176 O OE1 . GLU A 162 ? 1.2041 1.3493 1.4588 0.0675  0.1187  0.1726  179  GLU A OE1 
1177 O OE2 . GLU A 162 ? 1.2211 1.3605 1.5434 0.0423  0.0891  0.1631  179  GLU A OE2 
1178 N N   . LYS A 163 ? 0.7418 0.8369 0.9856 0.0331  0.0416  0.0762  180  LYS A N   
1179 C CA  . LYS A 163 ? 0.7920 0.8760 1.0459 0.0239  0.0190  0.0570  180  LYS A CA  
1180 C C   . LYS A 163 ? 0.8971 0.9727 1.1764 0.0141  0.0053  0.0536  180  LYS A C   
1181 O O   . LYS A 163 ? 0.8231 0.9091 1.1451 0.0102  0.0077  0.0727  180  LYS A O   
1182 C CB  . LYS A 163 ? 0.7471 0.8447 1.0383 0.0226  0.0114  0.0629  180  LYS A CB  
1183 C CG  . LYS A 163 ? 0.7917 0.8948 1.0561 0.0323  0.0210  0.0618  180  LYS A CG  
1184 C CD  . LYS A 163 ? 0.9156 1.0304 1.2161 0.0301  0.0097  0.0641  180  LYS A CD  
1185 C CE  . LYS A 163 ? 1.0443 1.1635 1.3173 0.0402  0.0189  0.0624  180  LYS A CE  
1186 N NZ  . LYS A 163 ? 1.0472 1.1783 1.3548 0.0385  0.0071  0.0643  180  LYS A NZ  
1187 N N   . THR A 164 ? 0.8694 0.9266 1.1235 0.0111  -0.0089 0.0305  181  THR A N   
1188 C CA  . THR A 164 ? 0.6860 0.7319 0.9546 0.0042  -0.0218 0.0237  181  THR A CA  
1189 C C   . THR A 164 ? 0.9107 0.9442 1.1776 0.0021  -0.0459 0.0001  181  THR A C   
1190 O O   . THR A 164 ? 0.8606 0.8906 1.0951 0.0073  -0.0483 -0.0139 181  THR A O   
1191 C CB  . THR A 164 ? 0.8342 0.8701 1.0636 0.0067  -0.0108 0.0205  181  THR A CB  
1192 O OG1 . THR A 164 ? 0.9120 0.9597 1.1380 0.0119  0.0108  0.0411  181  THR A OG1 
1193 C CG2 . THR A 164 ? 0.7456 0.7705 0.9914 0.0003  -0.0229 0.0153  181  THR A CG2 
1194 N N   . TYR A 165 ? 0.9734 1.0005 1.2762 -0.0042 -0.0642 -0.0038 182  TYR A N   
1195 C CA  . TYR A 165 ? 0.8647 0.8791 1.1656 -0.0033 -0.0896 -0.0279 182  TYR A CA  
1196 C C   . TYR A 165 ? 0.9082 0.9073 1.1630 0.0014  -0.0911 -0.0460 182  TYR A C   
1197 O O   . TYR A 165 ? 0.9375 0.9324 1.1825 -0.0004 -0.0805 -0.0400 182  TYR A O   
1198 C CB  . TYR A 165 ? 0.9937 1.0047 1.3529 -0.0106 -0.1118 -0.0267 182  TYR A CB  
1199 C CG  . TYR A 165 ? 1.0896 1.1177 1.5044 -0.0163 -0.1119 -0.0059 182  TYR A CG  
1200 C CD1 . TYR A 165 ? 1.0702 1.1072 1.4896 -0.0134 -0.1178 -0.0093 182  TYR A CD1 
1201 C CD2 . TYR A 165 ? 1.0771 1.1140 1.5422 -0.0240 -0.1059 0.0189  182  TYR A CD2 
1202 C CE1 . TYR A 165 ? 1.0437 1.0982 1.5166 -0.0184 -0.1179 0.0111  182  TYR A CE1 
1203 C CE2 . TYR A 165 ? 1.1436 1.1991 1.6639 -0.0286 -0.1051 0.0412  182  TYR A CE2 
1204 C CZ  . TYR A 165 ? 1.2318 1.2961 1.7560 -0.0260 -0.1112 0.0369  182  TYR A CZ  
1205 O OH  . TYR A 165 ? 1.1488 1.2336 1.7305 -0.0304 -0.1101 0.0606  182  TYR A OH  
1206 N N   . CYS A 166 ? 0.8678 0.8603 1.0951 0.0087  -0.1040 -0.0669 183  CYS A N   
1207 C CA  . CYS A 166 ? 1.0233 1.0039 1.2104 0.0152  -0.1077 -0.0840 183  CYS A CA  
1208 C C   . CYS A 166 ? 0.9309 0.9122 1.0817 0.0156  -0.0844 -0.0759 183  CYS A C   
1209 O O   . CYS A 166 ? 1.0206 0.9943 1.1612 0.0148  -0.0817 -0.0772 183  CYS A O   
1210 C CB  . CYS A 166 ? 0.9338 0.9015 1.1428 0.0136  -0.1265 -0.0938 183  CYS A CB  
1211 S SG  . CYS A 166 ? 1.0971 1.0520 1.2684 0.0277  -0.1456 -0.1228 183  CYS A SG  
1212 N N   . VAL A 167 ? 0.8644 0.8541 0.9963 0.0175  -0.0690 -0.0679 184  VAL A N   
1213 C CA  . VAL A 167 ? 0.8741 0.8632 0.9733 0.0184  -0.0497 -0.0614 184  VAL A CA  
1214 C C   . VAL A 167 ? 0.7930 0.7753 0.8527 0.0246  -0.0509 -0.0745 184  VAL A C   
1215 O O   . VAL A 167 ? 0.7967 0.7758 0.8338 0.0243  -0.0393 -0.0711 184  VAL A O   
1216 C CB  . VAL A 167 ? 0.9508 0.9491 1.0437 0.0198  -0.0348 -0.0498 184  VAL A CB  
1217 C CG1 . VAL A 167 ? 0.8951 0.9031 1.0236 0.0156  -0.0277 -0.0317 184  VAL A CG1 
1218 C CG2 . VAL A 167 ? 0.8290 0.8312 0.9167 0.0246  -0.0423 -0.0575 184  VAL A CG2 
1219 N N   . SER A 168 ? 0.8888 0.8701 0.9404 0.0313  -0.0648 -0.0885 185  SER A N   
1220 C CA  . SER A 168 ? 0.8458 0.8250 0.8611 0.0395  -0.0641 -0.0976 185  SER A CA  
1221 C C   . SER A 168 ? 0.8964 0.8691 0.9073 0.0459  -0.0789 -0.1119 185  SER A C   
1222 O O   . SER A 168 ? 0.8069 0.7798 0.7886 0.0538  -0.0763 -0.1169 185  SER A O   
1223 C CB  . SER A 168 ? 0.7773 0.7636 0.7781 0.0469  -0.0652 -0.1006 185  SER A CB  
1224 O OG  . SER A 168 ? 0.8711 0.8623 0.8762 0.0425  -0.0529 -0.0886 185  SER A OG  
1225 N N   . GLY A 169 ? 0.8900 0.8572 0.9303 0.0435  -0.0945 -0.1180 186  GLY A N   
1226 C CA  . GLY A 169 ? 1.0142 0.9728 1.0512 0.0515  -0.1114 -0.1340 186  GLY A CA  
1227 C C   . GLY A 169 ? 0.9116 0.8610 0.9757 0.0432  -0.1153 -0.1310 186  GLY A C   
1228 O O   . GLY A 169 ? 0.8936 0.8439 0.9610 0.0345  -0.0996 -0.1168 186  GLY A O   
1229 N N   . GLN A 170 ? 0.7521 0.7349 0.9566 0.0424  0.0950  0.0308  187  GLN A N   
1230 C CA  . GLN A 170 ? 0.8207 0.8112 1.0394 0.0239  0.1185  0.0181  187  GLN A CA  
1231 C C   . GLN A 170 ? 0.7848 0.8035 1.0478 0.0153  0.0942  0.0015  187  GLN A C   
1232 O O   . GLN A 170 ? 0.8571 0.8770 1.1084 0.0204  0.0585  -0.0006 187  GLN A O   
1233 C CB  . GLN A 170 ? 0.8220 0.7771 0.9668 0.0140  0.1333  0.0206  187  GLN A CB  
1234 C CG  . GLN A 170 ? 0.8081 0.7674 0.9653 -0.0049 0.1576  0.0087  187  GLN A CG  
1235 C CD  . GLN A 170 ? 0.7612 0.6920 0.8534 -0.0151 0.1562  0.0049  187  GLN A CD  
1236 O OE1 . GLN A 170 ? 0.8651 0.7652 0.8942 -0.0110 0.1643  0.0153  187  GLN A OE1 
1237 N NE2 . GLN A 170 ? 0.8115 0.7530 0.9204 -0.0286 0.1455  -0.0109 187  GLN A NE2 
1238 N N   . LEU A 171 ? 0.7456 0.7876 1.0602 0.0021  0.1136  -0.0098 188  LEU A N   
1239 C CA  . LEU A 171 ? 0.7594 0.8285 1.1205 -0.0084 0.0938  -0.0264 188  LEU A CA  
1240 C C   . LEU A 171 ? 0.7320 0.7812 1.0491 -0.0235 0.0911  -0.0350 188  LEU A C   
1241 O O   . LEU A 171 ? 0.7456 0.7793 1.0423 -0.0352 0.1205  -0.0349 188  LEU A O   
1242 C CB  . LEU A 171 ? 0.6803 0.7847 1.1190 -0.0167 0.1157  -0.0339 188  LEU A CB  
1243 C CG  . LEU A 171 ? 0.7378 0.8755 1.2411 -0.0033 0.1078  -0.0333 188  LEU A CG  
1244 C CD1 . LEU A 171 ? 0.7328 0.9056 1.3075 -0.0138 0.1338  -0.0410 188  LEU A CD1 
1245 C CD2 . LEU A 171 ? 0.7023 0.8560 1.2268 0.0041  0.0636  -0.0405 188  LEU A CD2 
1246 N N   . ILE A 172 ? 0.7676 0.8173 1.0699 -0.0229 0.0552  -0.0431 189  ILE A N   
1247 C CA  . ILE A 172 ? 0.7863 0.8224 1.0548 -0.0367 0.0470  -0.0553 189  ILE A CA  
1248 C C   . ILE A 172 ? 0.7891 0.8582 1.1226 -0.0465 0.0275  -0.0737 189  ILE A C   
1249 O O   . ILE A 172 ? 0.8114 0.8996 1.1686 -0.0382 -0.0062 -0.0784 189  ILE A O   
1250 C CB  . ILE A 172 ? 0.8286 0.8388 1.0222 -0.0287 0.0212  -0.0512 189  ILE A CB  
1251 C CG1 . ILE A 172 ? 0.8261 0.8055 0.9606 -0.0185 0.0401  -0.0315 189  ILE A CG1 
1252 C CG2 . ILE A 172 ? 0.8810 0.8783 1.0402 -0.0430 0.0148  -0.0662 189  ILE A CG2 
1253 C CD1 . ILE A 172 ? 0.9188 0.8734 0.9784 -0.0106 0.0167  -0.0246 189  ILE A CD1 
1254 N N   . GLU A 173 ? 0.7786 0.8546 1.1430 -0.0640 0.0486  -0.0835 190  GLU A N   
1255 C CA  . GLU A 173 ? 0.7676 0.8733 1.1957 -0.0764 0.0339  -0.1014 190  GLU A CA  
1256 C C   . GLU A 173 ? 0.7621 0.9062 1.2608 -0.0676 0.0180  -0.1027 190  GLU A C   
1257 O O   . GLU A 173 ? 0.7797 0.9471 1.3169 -0.0697 -0.0118 -0.1164 190  GLU A O   
1258 C CB  . GLU A 173 ? 0.8054 0.9016 1.2014 -0.0816 0.0023  -0.1164 190  GLU A CB  
1259 C CG  . GLU A 173 ? 0.8958 0.9590 1.2343 -0.0929 0.0183  -0.1198 190  GLU A CG  
1260 C CD  . GLU A 173 ? 1.0560 1.1240 1.4354 -0.1118 0.0469  -0.1262 190  GLU A CD  
1261 O OE1 . GLU A 173 ? 0.8599 0.9540 1.3015 -0.1227 0.0363  -0.1400 190  GLU A OE1 
1262 O OE2 . GLU A 173 ? 1.0007 1.0466 1.3511 -0.1159 0.0796  -0.1167 190  GLU A OE2 
1263 N N   . GLY A 174 ? 0.7378 0.8895 1.2550 -0.0573 0.0377  -0.0894 191  GLY A N   
1264 C CA  . GLY A 174 ? 0.7282 0.9175 1.3161 -0.0487 0.0278  -0.0908 191  GLY A CA  
1265 C C   . GLY A 174 ? 0.7529 0.9423 1.3273 -0.0274 -0.0027 -0.0837 191  GLY A C   
1266 O O   . GLY A 174 ? 0.7441 0.9636 1.3769 -0.0179 -0.0101 -0.0841 191  GLY A O   
1267 N N   . ILE A 175 ? 0.7845 0.9421 1.2852 -0.0197 -0.0206 -0.0770 192  ILE A N   
1268 C CA  . ILE A 175 ? 0.8130 0.9675 1.2949 0.0000  -0.0514 -0.0680 192  ILE A CA  
1269 C C   . ILE A 175 ? 0.8309 0.9534 1.2557 0.0114  -0.0323 -0.0478 192  ILE A C   
1270 O O   . ILE A 175 ? 0.8075 0.8991 1.1726 0.0044  -0.0124 -0.0428 192  ILE A O   
1271 C CB  . ILE A 175 ? 0.9045 1.0509 1.3476 0.0004  -0.0914 -0.0755 192  ILE A CB  
1272 C CG1 . ILE A 175 ? 0.8648 1.0477 1.3746 -0.0069 -0.1164 -0.0955 192  ILE A CG1 
1273 C CG2 . ILE A 175 ? 0.8913 1.0242 1.2941 0.0203  -0.1188 -0.0608 192  ILE A CG2 
1274 C CD1 . ILE A 175 ? 0.8526 1.0394 1.3784 -0.0289 -0.1024 -0.1120 192  ILE A CD1 
1275 N N   . CYS A 176 ? 0.8075 0.9376 1.2530 0.0288  -0.0385 -0.0370 193  CYS A N   
1276 C CA  . CYS A 176 ? 0.8044 0.9056 1.2026 0.0405  -0.0221 -0.0179 193  CYS A CA  
1277 C C   . CYS A 176 ? 0.8471 0.9157 1.1664 0.0478  -0.0466 -0.0070 193  CYS A C   
1278 O O   . CYS A 176 ? 0.8820 0.9578 1.1995 0.0545  -0.0849 -0.0090 193  CYS A O   
1279 C CB  . CYS A 176 ? 0.8589 0.9792 1.3086 0.0572  -0.0229 -0.0110 193  CYS A CB  
1280 S SG  . CYS A 176 ? 0.9697 1.0568 1.3728 0.0713  0.0000  0.0110  193  CYS A SG  
1281 N N   . PHE A 177 ? 0.8452 0.8788 1.0988 0.0463  -0.0239 0.0048  194  PHE A N   
1282 C CA  . PHE A 177 ? 0.8838 0.8850 1.0579 0.0525  -0.0410 0.0174  194  PHE A CA  
1283 C C   . PHE A 177 ? 0.8753 0.8522 1.0201 0.0641  -0.0216 0.0377  194  PHE A C   
1284 O O   . PHE A 177 ? 0.9018 0.8688 1.0429 0.0586  0.0154  0.0398  194  PHE A O   
1285 C CB  . PHE A 177 ? 0.8942 0.8749 1.0103 0.0370  -0.0332 0.0098  194  PHE A CB  
1286 C CG  . PHE A 177 ? 0.9284 0.9241 1.0495 0.0294  -0.0643 -0.0072 194  PHE A CG  
1287 C CD1 . PHE A 177 ? 0.9713 0.9531 1.0342 0.0338  -0.0951 -0.0040 194  PHE A CD1 
1288 C CD2 . PHE A 177 ? 0.9424 0.9667 1.1261 0.0174  -0.0626 -0.0265 194  PHE A CD2 
1289 C CE1 . PHE A 177 ? 0.9949 0.9915 1.0617 0.0272  -0.1243 -0.0212 194  PHE A CE1 
1290 C CE2 . PHE A 177 ? 0.9899 1.0279 1.1800 0.0103  -0.0918 -0.0434 194  PHE A CE2 
1291 C CZ  . PHE A 177 ? 0.9743 0.9986 1.1057 0.0155  -0.1230 -0.0415 194  PHE A CZ  
1292 N N   . ASN A 178 ? 0.9059 0.8731 1.0311 0.0801  -0.0471 0.0527  195  ASN A N   
1293 C CA  . ASN A 178 ? 0.9160 0.8583 1.0128 0.0917  -0.0326 0.0727  195  ASN A CA  
1294 C C   . ASN A 178 ? 0.9355 0.8404 0.9417 0.0904  -0.0356 0.0863  195  ASN A C   
1295 O O   . ASN A 178 ? 0.9705 0.8721 0.9390 0.0859  -0.0603 0.0826  195  ASN A O   
1296 C CB  . ASN A 178 ? 0.9163 0.8700 1.0524 0.1108  -0.0576 0.0828  195  ASN A CB  
1297 C CG  . ASN A 178 ? 0.8976 0.8839 1.1202 0.1148  -0.0440 0.0730  195  ASN A CG  
1298 O OD1 . ASN A 178 ? 0.9003 0.8941 1.1448 0.1052  -0.0090 0.0645  195  ASN A OD1 
1299 N ND2 . ASN A 178 ? 0.9761 0.9829 1.2483 0.1291  -0.0718 0.0741  195  ASN A ND2 
1300 N N   . PRO A 179 ? 0.9719 0.8497 0.9422 0.0938  -0.0103 0.1012  196  PRO A N   
1301 C CA  . PRO A 179 ? 0.9997 0.8426 0.8845 0.0929  -0.0123 0.1154  196  PRO A CA  
1302 C C   . PRO A 179 ? 1.0521 0.8898 0.9109 0.1045  -0.0534 0.1291  196  PRO A C   
1303 O O   . PRO A 179 ? 1.0278 0.8786 0.9300 0.1182  -0.0743 0.1356  196  PRO A O   
1304 C CB  . PRO A 179 ? 0.9332 0.7536 0.8040 0.0977  0.0201  0.1295  196  PRO A CB  
1305 C CG  . PRO A 179 ? 0.8830 0.7253 0.8188 0.0938  0.0483  0.1162  196  PRO A CG  
1306 C CD  . PRO A 179 ? 0.9075 0.7864 0.9127 0.0970  0.0239  0.1037  196  PRO A CD  
1307 N N   . VAL A 180 ? 1.1305 0.9497 0.9173 0.0988  -0.0652 0.1332  197  VAL A N   
1308 C CA  . VAL A 180 ? 1.2203 1.0338 0.9727 0.1083  -0.1043 0.1473  197  VAL A CA  
1309 C C   . VAL A 180 ? 1.1792 0.9734 0.9245 0.1235  -0.1064 0.1732  197  VAL A C   
1310 O O   . VAL A 180 ? 1.1347 0.9056 0.8561 0.1232  -0.0768 0.1840  197  VAL A O   
1311 C CB  . VAL A 180 ? 1.1771 0.9737 0.8479 0.0983  -0.1104 0.1468  197  VAL A CB  
1312 C CG1 . VAL A 180 ? 1.3441 1.1254 0.9622 0.1084  -0.1415 0.1694  197  VAL A CG1 
1313 C CG2 . VAL A 180 ? 1.1374 0.9575 0.8225 0.0870  -0.1241 0.1213  197  VAL A CG2 
1314 N N   . HIS A 181 ? 1.3666 1.1704 1.1350 0.1372  -0.1422 0.1830  198  HIS A N   
1315 C CA  . HIS A 181 ? 1.5473 1.3340 1.3174 0.1529  -0.1495 0.2076  198  HIS A CA  
1316 C C   . HIS A 181 ? 1.5696 1.3290 1.2586 0.1549  -0.1689 0.2305  198  HIS A C   
1317 O O   . HIS A 181 ? 1.5849 1.3522 1.2555 0.1577  -0.2056 0.2333  198  HIS A O   
1318 C CB  . HIS A 181 ? 1.5337 1.3459 1.3779 0.1674  -0.1779 0.2061  198  HIS A CB  
1319 C CG  . HIS A 181 ? 1.6833 1.4780 1.5285 0.1846  -0.1939 0.2317  198  HIS A CG  
1320 N ND1 . HIS A 181 ? 1.7373 1.5248 1.5535 0.1937  -0.2342 0.2495  198  HIS A ND1 
1321 C CD2 . HIS A 181 ? 1.7523 1.5349 1.6248 0.1943  -0.1756 0.2426  198  HIS A CD2 
1322 C CE1 . HIS A 181 ? 1.7544 1.5249 1.5811 0.2082  -0.2402 0.2713  198  HIS A CE1 
1323 N NE2 . HIS A 181 ? 1.8568 1.6240 1.7184 0.2090  -0.2052 0.2667  198  HIS A NE2 
1324 N N   . THR A 182 ? 1.6247 1.3530 1.2650 0.1532  -0.1442 0.2467  199  THR A N   
1325 C CA  . THR A 182 ? 1.7957 1.4969 1.3613 0.1555  -0.1593 0.2720  199  THR A CA  
1326 C C   . THR A 182 ? 1.6817 1.3520 1.2278 0.1596  -0.1335 0.2928  199  THR A C   
1327 O O   . THR A 182 ? 1.5841 1.2373 1.0894 0.1491  -0.1012 0.2914  199  THR A O   
1328 C CB  . THR A 182 ? 1.8277 1.5233 1.3197 0.1407  -0.1575 0.2649  199  THR A CB  
1329 O OG1 . THR A 182 ? 1.6427 1.3674 1.1560 0.1358  -0.1792 0.2423  199  THR A OG1 
1330 C CG2 . THR A 182 ? 1.7430 1.4157 1.1604 0.1438  -0.1779 0.2918  199  THR A CG2 
1331 N N   . GLN A 187 ? 2.0105 1.6952 1.3257 0.1107  -0.1634 0.2497  204  GLN A N   
1332 C CA  . GLN A 187 ? 2.0103 1.7016 1.3061 0.0952  -0.1444 0.2236  204  GLN A CA  
1333 C C   . GLN A 187 ? 2.2125 1.9047 1.4361 0.0892  -0.1662 0.2218  204  GLN A C   
1334 O O   . GLN A 187 ? 2.2674 1.9413 1.4247 0.0814  -0.1488 0.2267  204  GLN A O   
1335 C CB  . GLN A 187 ? 1.8836 1.5533 1.1617 0.0875  -0.0988 0.2238  204  GLN A CB  
1336 C CG  . GLN A 187 ? 1.9499 1.6285 1.2350 0.0731  -0.0749 0.1946  204  GLN A CG  
1337 C CD  . GLN A 187 ? 1.7581 1.4618 1.1273 0.0730  -0.0730 0.1744  204  GLN A CD  
1338 O OE1 . GLN A 187 ? 1.6544 1.3652 1.0801 0.0834  -0.0763 0.1823  204  GLN A OE1 
1339 N NE2 . GLN A 187 ? 1.8657 1.5838 1.2449 0.0611  -0.0677 0.1480  204  GLN A NE2 
1340 N N   . PRO A 188 ? 2.2419 1.9568 1.4785 0.0928  -0.2045 0.2141  205  PRO A N   
1341 C CA  . PRO A 188 ? 2.2868 2.0049 1.4539 0.0886  -0.2291 0.2133  205  PRO A CA  
1342 C C   . PRO A 188 ? 2.3262 2.0551 1.4745 0.0739  -0.2179 0.1819  205  PRO A C   
1343 O O   . PRO A 188 ? 2.3167 2.0383 1.3931 0.0667  -0.2172 0.1808  205  PRO A O   
1344 C CB  . PRO A 188 ? 2.1628 1.9025 1.3605 0.0996  -0.2752 0.2165  205  PRO A CB  
1345 C CG  . PRO A 188 ? 2.1343 1.8926 1.4258 0.1030  -0.2709 0.2005  205  PRO A CG  
1346 C CD  . PRO A 188 ? 2.1408 1.8806 1.4558 0.1019  -0.2284 0.2066  205  PRO A CD  
1347 N N   . SER A 189 ? 2.2303 1.9770 1.4437 0.0690  -0.2095 0.1560  206  SER A N   
1348 C CA  . SER A 189 ? 2.1843 1.9431 1.3896 0.0555  -0.2037 0.1246  206  SER A CA  
1349 C C   . SER A 189 ? 2.2854 2.0239 1.4613 0.0446  -0.1608 0.1189  206  SER A C   
1350 O O   . SER A 189 ? 2.2376 1.9520 1.3777 0.0468  -0.1400 0.1406  206  SER A O   
1351 C CB  . SER A 189 ? 2.1733 1.9588 1.4617 0.0538  -0.2116 0.1004  206  SER A CB  
1352 O OG  . SER A 189 ? 1.9114 1.7175 1.2283 0.0639  -0.2527 0.1036  206  SER A OG  
1353 N N   . HIS A 190 ? 2.3142 2.0620 1.5062 0.0327  -0.1478 0.0896  207  HIS A N   
1354 C CA  . HIS A 190 ? 2.2796 2.0096 1.4466 0.0219  -0.1086 0.0813  207  HIS A CA  
1355 C C   . HIS A 190 ? 2.2157 1.9481 1.4515 0.0173  -0.0800 0.0696  207  HIS A C   
1356 O O   . HIS A 190 ? 2.1108 1.8317 1.3713 0.0225  -0.0585 0.0861  207  HIS A O   
1357 C CB  . HIS A 190 ? 2.3549 2.0900 1.4763 0.0109  -0.1134 0.0569  207  HIS A CB  
1358 C CG  . HIS A 190 ? 2.5384 2.2508 1.5891 0.0048  -0.0873 0.0614  207  HIS A CG  
1359 N ND1 . HIS A 190 ? 2.6371 2.3513 1.6444 -0.0054 -0.0848 0.0387  207  HIS A ND1 
1360 C CD2 . HIS A 190 ? 2.6163 2.3044 1.6337 0.0075  -0.0628 0.0851  207  HIS A CD2 
1361 C CE1 . HIS A 190 ? 2.7268 2.4273 1.6920 -0.0084 -0.0586 0.0478  207  HIS A CE1 
1362 N NE2 . HIS A 190 ? 2.7458 2.4379 1.7314 -0.0011 -0.0443 0.0752  207  HIS A NE2 
1363 N N   . THR A 191 ? 2.2211 1.9688 1.4884 0.0072  -0.0795 0.0411  208  THR A N   
1364 C CA  . THR A 191 ? 2.0440 1.7949 1.3734 0.0006  -0.0519 0.0288  208  THR A CA  
1365 C C   . THR A 191 ? 1.8432 1.6232 1.2417 -0.0016 -0.0732 0.0094  208  THR A C   
1366 O O   . THR A 191 ? 1.6991 1.4921 1.0894 -0.0078 -0.0941 -0.0115 208  THR A O   
1367 C CB  . THR A 191 ? 1.9225 1.6587 1.2228 -0.0122 -0.0216 0.0135  208  THR A CB  
1368 O OG1 . THR A 191 ? 1.7672 1.5131 1.1321 -0.0204 -0.0046 -0.0035 208  THR A OG1 
1369 C CG2 . THR A 191 ? 1.7664 1.5052 1.0121 -0.0188 -0.0393 -0.0045 208  THR A CG2 
1370 N N   . TYR A 192 ? 1.7665 1.5575 1.2342 0.0031  -0.0672 0.0151  209  TYR A N   
1371 C CA  . TYR A 192 ? 1.6559 1.4761 1.1966 0.0007  -0.0844 -0.0022 209  TYR A CA  
1372 C C   . TYR A 192 ? 1.5096 1.3371 1.1216 -0.0015 -0.0572 -0.0027 209  TYR A C   
1373 O O   . TYR A 192 ? 1.5577 1.3696 1.1636 -0.0082 -0.0218 -0.0021 209  TYR A O   
1374 C CB  . TYR A 192 ? 1.5999 1.4376 1.1541 0.0130  -0.1249 0.0059  209  TYR A CB  
1375 C CG  . TYR A 192 ? 1.7112 1.5577 1.2251 0.0110  -0.1592 -0.0071 209  TYR A CG  
1376 C CD1 . TYR A 192 ? 1.7996 1.6701 1.3535 0.0033  -0.1778 -0.0336 209  TYR A CD1 
1377 C CD2 . TYR A 192 ? 1.8105 1.6422 1.2466 0.0164  -0.1730 0.0068  209  TYR A CD2 
1378 C CE1 . TYR A 192 ? 1.8456 1.7255 1.3631 0.0017  -0.2099 -0.0475 209  TYR A CE1 
1379 C CE2 . TYR A 192 ? 1.9051 1.7469 1.3022 0.0146  -0.2043 -0.0058 209  TYR A CE2 
1380 C CZ  . TYR A 192 ? 1.9023 1.7685 1.3405 0.0076  -0.2230 -0.0338 209  TYR A CZ  
1381 O OH  . TYR A 192 ? 1.7665 1.6441 1.1664 0.0061  -0.2548 -0.0481 209  TYR A OH  
1382 N N   . ASP A 193 ? 1.1994 1.0523 0.8795 0.0039  -0.0736 -0.0041 210  ASP A N   
1383 C CA  . ASP A 193 ? 1.0495 0.9163 0.8033 0.0007  -0.0506 -0.0077 210  ASP A CA  
1384 C C   . ASP A 193 ? 1.0648 0.9135 0.8130 0.0067  -0.0179 0.0122  210  ASP A C   
1385 O O   . ASP A 193 ? 1.2537 1.0979 0.9969 0.0205  -0.0259 0.0313  210  ASP A O   
1386 C CB  . ASP A 193 ? 1.0331 0.9319 0.8572 0.0074  -0.0772 -0.0116 210  ASP A CB  
1387 C CG  . ASP A 193 ? 1.2287 1.1488 1.0715 -0.0003 -0.1065 -0.0345 210  ASP A CG  
1388 O OD1 . ASP A 193 ? 1.2014 1.1195 1.0414 -0.0147 -0.0949 -0.0526 210  ASP A OD1 
1389 O OD2 . ASP A 193 ? 1.2586 1.1971 1.1196 0.0083  -0.1420 -0.0349 210  ASP A OD2 
1390 N N   . ILE A 194 ? 0.9680 0.8062 0.7186 -0.0034 0.0181  0.0074  211  ILE A N   
1391 C CA  . ILE A 194 ? 0.9536 0.7733 0.6938 0.0006  0.0516  0.0237  211  ILE A CA  
1392 C C   . ILE A 194 ? 0.8940 0.7339 0.7103 -0.0003 0.0711  0.0213  211  ILE A C   
1393 O O   . ILE A 194 ? 0.9822 0.8383 0.8409 -0.0121 0.0783  0.0049  211  ILE A O   
1394 C CB  . ILE A 194 ? 0.9334 0.7264 0.6178 -0.0094 0.0789  0.0210  211  ILE A CB  
1395 C CG1 . ILE A 194 ? 1.0211 0.7916 0.6247 -0.0051 0.0657  0.0302  211  ILE A CG1 
1396 C CG2 . ILE A 194 ? 0.8917 0.6730 0.5871 -0.0091 0.1179  0.0311  211  ILE A CG2 
1397 C CD1 . ILE A 194 ? 1.1645 0.9090 0.7117 -0.0136 0.0928  0.0283  211  ILE A CD1 
1398 N N   . VAL A 195 ? 0.8794 0.7189 0.7138 0.0119  0.0795  0.0375  212  VAL A N   
1399 C CA  . VAL A 195 ? 0.8361 0.6934 0.7358 0.0121  0.1027  0.0367  212  VAL A CA  
1400 C C   . VAL A 195 ? 0.8102 0.6443 0.6823 0.0125  0.1398  0.0479  212  VAL A C   
1401 O O   . VAL A 195 ? 0.8573 0.6635 0.6677 0.0170  0.1433  0.0602  212  VAL A O   
1402 C CB  . VAL A 195 ? 0.8371 0.7170 0.7899 0.0265  0.0833  0.0432  212  VAL A CB  
1403 C CG1 . VAL A 195 ? 0.8692 0.7690 0.8398 0.0279  0.0427  0.0338  212  VAL A CG1 
1404 C CG2 . VAL A 195 ? 0.8489 0.7081 0.7686 0.0420  0.0826  0.0644  212  VAL A CG2 
1405 N N   . THR A 196 ? 0.7692 0.6162 0.6881 0.0074  0.1681  0.0436  213  THR A N   
1406 C CA  . THR A 196 ? 0.8030 0.6326 0.7050 0.0077  0.2044  0.0524  213  THR A CA  
1407 C C   . THR A 196 ? 0.7734 0.6232 0.7335 0.0175  0.2153  0.0578  213  THR A C   
1408 O O   . THR A 196 ? 0.7240 0.6021 0.7452 0.0121  0.2233  0.0481  213  THR A O   
1409 C CB  . THR A 196 ? 0.8518 0.6767 0.7498 -0.0088 0.2313  0.0418  213  THR A CB  
1410 O OG1 . THR A 196 ? 0.9597 0.7697 0.8111 -0.0177 0.2178  0.0333  213  THR A OG1 
1411 C CG2 . THR A 196 ? 0.8292 0.6330 0.6999 -0.0078 0.2666  0.0515  213  THR A CG2 
1412 N N   . VAL A 197 ? 0.8270 0.6630 0.7690 0.0317  0.2157  0.0730  214  VAL A N   
1413 C CA  . VAL A 197 ? 0.7559 0.6101 0.7511 0.0437  0.2221  0.0776  214  VAL A CA  
1414 C C   . VAL A 197 ? 0.8122 0.6487 0.7886 0.0466  0.2564  0.0863  214  VAL A C   
1415 O O   . VAL A 197 ? 0.8501 0.6554 0.7650 0.0446  0.2668  0.0940  214  VAL A O   
1416 C CB  . VAL A 197 ? 0.7719 0.6283 0.7738 0.0600  0.1888  0.0872  214  VAL A CB  
1417 C CG1 . VAL A 197 ? 0.7575 0.6401 0.7957 0.0582  0.1562  0.0763  214  VAL A CG1 
1418 C CG2 . VAL A 197 ? 0.7609 0.5814 0.6880 0.0650  0.1781  0.1023  214  VAL A CG2 
1419 N N   . MET A 198 ? 0.6763 0.5347 0.7076 0.0513  0.2741  0.0840  215  MET A N   
1420 C CA  . MET A 198 ? 0.7678 0.6149 0.7912 0.0557  0.3056  0.0906  215  MET A CA  
1421 C C   . MET A 198 ? 0.7808 0.6143 0.7952 0.0736  0.2943  0.1041  215  MET A C   
1422 O O   . MET A 198 ? 0.7625 0.6121 0.8137 0.0847  0.2696  0.1052  215  MET A O   
1423 C CB  . MET A 198 ? 0.6903 0.5700 0.7774 0.0528  0.3295  0.0810  215  MET A CB  
1424 C CG  . MET A 198 ? 0.8021 0.6742 0.8864 0.0577  0.3491  0.0834  215  MET A CG  
1425 S SD  . MET A 198 ? 0.9849 0.8961 1.1399 0.0555  0.3471  0.0699  215  MET A SD  
1426 C CE  . MET A 198 ? 1.0071 0.8936 1.1245 0.0533  0.3280  0.0667  215  MET A CE  
1427 N N   . VAL A 199 ? 0.6438 0.6315 0.5174 0.0194  -0.0099 -0.0516 216  VAL A N   
1428 C CA  . VAL A 199 ? 0.7608 0.7393 0.6374 0.0243  -0.0008 -0.0518 216  VAL A CA  
1429 C C   . VAL A 199 ? 0.7197 0.6993 0.6034 0.0147  0.0027  -0.0567 216  VAL A C   
1430 O O   . VAL A 199 ? 0.7301 0.7130 0.6154 0.0055  0.0002  -0.0567 216  VAL A O   
1431 C CB  . VAL A 199 ? 0.7297 0.6939 0.6008 0.0316  0.0041  -0.0448 216  VAL A CB  
1432 C CG1 . VAL A 199 ? 0.7694 0.7310 0.6290 0.0423  0.0000  -0.0410 216  VAL A CG1 
1433 C CG2 . VAL A 199 ? 0.7421 0.7050 0.6143 0.0259  0.0051  -0.0421 216  VAL A CG2 
1434 N N   . ARG A 200 ? 0.8056 0.7812 0.6926 0.0175  0.0074  -0.0615 217  ARG A N   
1435 C CA  . ARG A 200 ? 0.7021 0.6737 0.5923 0.0099  0.0098  -0.0679 217  ARG A CA  
1436 C C   . ARG A 200 ? 0.7278 0.6790 0.6210 0.0143  0.0146  -0.0664 217  ARG A C   
1437 O O   . ARG A 200 ? 0.8064 0.7507 0.6998 0.0240  0.0171  -0.0682 217  ARG A O   
1438 C CB  . ARG A 200 ? 0.6546 0.6393 0.5439 0.0094  0.0100  -0.0771 217  ARG A CB  
1439 C CG  . ARG A 200 ? 0.6756 0.6795 0.5635 -0.0010 0.0051  -0.0775 217  ARG A CG  
1440 C CD  . ARG A 200 ? 0.5991 0.6228 0.4867 0.0006  0.0066  -0.0829 217  ARG A CD  
1441 N NE  . ARG A 200 ? 0.7048 0.7399 0.5969 0.0087  0.0052  -0.0781 217  ARG A NE  
1442 C CZ  . ARG A 200 ? 0.6646 0.7235 0.5608 0.0093  0.0052  -0.0782 217  ARG A CZ  
1443 N NH1 . ARG A 200 ? 0.6674 0.7418 0.5613 0.0032  0.0080  -0.0830 217  ARG A NH1 
1444 N NH2 . ARG A 200 ? 0.5946 0.6636 0.4973 0.0159  0.0021  -0.0725 217  ARG A NH2 
1445 N N   . CYS A 201 ? 0.7590 0.7014 0.6566 0.0071  0.0151  -0.0617 218  CYS A N   
1446 C CA  . CYS A 201 ? 0.8409 0.7645 0.7440 0.0085  0.0185  -0.0566 218  CYS A CA  
1447 C C   . CYS A 201 ? 0.7712 0.6832 0.6782 -0.0002 0.0163  -0.0646 218  CYS A C   
1448 O O   . CYS A 201 ? 0.7806 0.7004 0.6858 -0.0095 0.0124  -0.0714 218  CYS A O   
1449 C CB  . CYS A 201 ? 0.8701 0.7939 0.7780 0.0064  0.0210  -0.0436 218  CYS A CB  
1450 S SG  . CYS A 201 ? 1.3097 1.2269 1.2136 0.0197  0.0268  -0.0305 218  CYS A SG  
1451 N N   . PHE A 202 ? 0.9433 0.8347 0.8545 0.0028  0.0174  -0.0634 219  PHE A N   
1452 C CA  . PHE A 202 ? 0.7912 0.6649 0.7044 -0.0044 0.0132  -0.0721 219  PHE A CA  
1453 C C   . PHE A 202 ? 0.7052 0.5598 0.6305 -0.0095 0.0125  -0.0604 219  PHE A C   
1454 O O   . PHE A 202 ? 0.8265 0.6729 0.7549 -0.0013 0.0163  -0.0504 219  PHE A O   
1455 C CB  . PHE A 202 ? 0.7078 0.5717 0.6131 0.0060  0.0135  -0.0859 219  PHE A CB  
1456 C CG  . PHE A 202 ? 0.8297 0.7165 0.7259 0.0108  0.0152  -0.0954 219  PHE A CG  
1457 C CD1 . PHE A 202 ? 0.6993 0.5923 0.5873 0.0043  0.0127  -0.1080 219  PHE A CD1 
1458 C CD2 . PHE A 202 ? 0.7567 0.6597 0.6524 0.0208  0.0187  -0.0905 219  PHE A CD2 
1459 C CE1 . PHE A 202 ? 0.7516 0.6687 0.6324 0.0078  0.0151  -0.1140 219  PHE A CE1 
1460 C CE2 . PHE A 202 ? 0.6837 0.6097 0.5743 0.0234  0.0195  -0.0967 219  PHE A CE2 
1461 C CZ  . PHE A 202 ? 0.7821 0.7163 0.6660 0.0168  0.0184  -0.1076 219  PHE A CZ  
1462 N N   . LEU A 203 ? 0.7114 0.5602 0.6442 -0.0237 0.0069  -0.0601 220  LEU A N   
1463 C CA  . LEU A 203 ? 0.7254 0.5593 0.6738 -0.0317 0.0051  -0.0466 220  LEU A CA  
1464 C C   . LEU A 203 ? 0.8225 0.6249 0.7712 -0.0290 0.0008  -0.0519 220  LEU A C   
1465 O O   . LEU A 203 ? 0.7898 0.5784 0.7282 -0.0278 -0.0047 -0.0698 220  LEU A O   
1466 C CB  . LEU A 203 ? 0.7234 0.5623 0.6824 -0.0488 -0.0016 -0.0443 220  LEU A CB  
1467 C CG  . LEU A 203 ? 0.8724 0.7018 0.8527 -0.0598 -0.0040 -0.0272 220  LEU A CG  
1468 C CD1 . LEU A 203 ? 0.7223 0.5683 0.7117 -0.0535 0.0070  -0.0068 220  LEU A CD1 
1469 C CD2 . LEU A 203 ? 0.7449 0.5796 0.7367 -0.0773 -0.0132 -0.0267 220  LEU A CD2 
1470 N N   . ILE A 204 ? 0.7762 0.5667 0.7358 -0.0273 0.0031  -0.0359 221  ILE A N   
1471 C CA  . ILE A 204 ? 0.8788 0.6365 0.8412 -0.0245 -0.0019 -0.0373 221  ILE A CA  
1472 C C   . ILE A 204 ? 0.8167 0.5609 0.7993 -0.0396 -0.0070 -0.0199 221  ILE A C   
1473 O O   . ILE A 204 ? 0.8159 0.5789 0.8105 -0.0439 -0.0006 0.0001  221  ILE A O   
1474 C CB  . ILE A 204 ? 0.8632 0.6180 0.8203 -0.0071 0.0047  -0.0318 221  ILE A CB  
1475 C CG1 . ILE A 204 ? 0.7826 0.5581 0.7241 0.0062  0.0098  -0.0448 221  ILE A CG1 
1476 C CG2 . ILE A 204 ? 0.8390 0.5576 0.7982 -0.0024 -0.0018 -0.0357 221  ILE A CG2 
1477 C CD1 . ILE A 204 ? 0.7948 0.5632 0.7256 0.0095  0.0055  -0.0681 221  ILE A CD1 
1478 N N   . VAL A 205 ? 0.8491 0.5611 0.8356 -0.0473 -0.0187 -0.0274 222  VAL A N   
1479 C CA  . VAL A 205 ? 0.9617 0.6571 0.9698 -0.0638 -0.0265 -0.0107 222  VAL A CA  
1480 C C   . VAL A 205 ? 0.8971 0.5653 0.9108 -0.0570 -0.0272 0.0003  222  VAL A C   
1481 O O   . VAL A 205 ? 1.0503 0.6905 1.0525 -0.0464 -0.0324 -0.0154 222  VAL A O   
1482 C CB  . VAL A 205 ? 0.8955 0.5691 0.9048 -0.0789 -0.0425 -0.0253 222  VAL A CB  
1483 C CG1 . VAL A 205 ? 0.9170 0.5737 0.9523 -0.0980 -0.0527 -0.0060 222  VAL A CG1 
1484 C CG2 . VAL A 205 ? 0.9046 0.6059 0.9071 -0.0851 -0.0424 -0.0352 222  VAL A CG2 
1485 N N   . LYS A 206 ? 0.9717 0.6490 1.0029 -0.0622 -0.0218 0.0278  223  LYS A N   
1486 C CA  . LYS A 206 ? 1.0425 0.6964 1.0798 -0.0568 -0.0222 0.0429  223  LYS A CA  
1487 C C   . LYS A 206 ? 0.9577 0.6186 1.0209 -0.0730 -0.0214 0.0739  223  LYS A C   
1488 O O   . LYS A 206 ? 0.9486 0.6448 1.0166 -0.0723 -0.0084 0.0913  223  LYS A O   
1489 C CB  . LYS A 206 ? 0.9740 0.6421 0.9956 -0.0357 -0.0099 0.0447  223  LYS A CB  
1490 C CG  . LYS A 206 ? 1.0226 0.6602 1.0441 -0.0256 -0.0133 0.0514  223  LYS A CG  
1491 C CD  . LYS A 206 ? 1.1198 0.7614 1.1562 -0.0311 -0.0084 0.0846  223  LYS A CD  
1492 C CE  . LYS A 206 ? 0.9877 0.5973 1.0241 -0.0214 -0.0133 0.0926  223  LYS A CE  
1493 N NZ  . LYS A 206 ? 1.1928 0.7563 1.2377 -0.0284 -0.0302 0.0816  223  LYS A NZ  
1494 N N   . LYS A 207 ? 1.0082 0.6355 1.0881 -0.0870 -0.0354 0.0809  224  LYS A N   
1495 C CA  . LYS A 207 ? 1.0657 0.6985 1.1748 -0.1055 -0.0369 0.1118  224  LYS A CA  
1496 C C   . LYS A 207 ? 1.0025 0.6197 1.1179 -0.1006 -0.0341 0.1353  224  LYS A C   
1497 O O   . LYS A 207 ? 1.0619 0.6466 1.1646 -0.0883 -0.0395 0.1248  224  LYS A O   
1498 C CB  . LYS A 207 ? 1.0165 0.6218 1.1430 -0.1277 -0.0570 0.1074  224  LYS A CB  
1499 C CG  . LYS A 207 ? 1.2387 0.8514 1.3543 -0.1318 -0.0633 0.0807  224  LYS A CG  
1500 C CD  . LYS A 207 ? 1.1624 0.7344 1.2838 -0.1485 -0.0870 0.0673  224  LYS A CD  
1501 C CE  . LYS A 207 ? 1.3444 0.9247 1.5004 -0.1754 -0.0966 0.0914  224  LYS A CE  
1502 N NZ  . LYS A 207 ? 1.3489 0.9059 1.5295 -0.1861 -0.1031 0.1186  224  LYS A NZ  
1503 N N   . VAL A 208 ? 1.1231 0.7655 1.2585 -0.1094 -0.0249 0.1682  225  VAL A N   
1504 C CA  . VAL A 208 ? 1.0809 0.7109 1.2257 -0.1091 -0.0229 0.1964  225  VAL A CA  
1505 C C   . VAL A 208 ? 1.2381 0.8676 1.4189 -0.1347 -0.0301 0.2257  225  VAL A C   
1506 O O   . VAL A 208 ? 1.1382 0.7881 1.3363 -0.1501 -0.0323 0.2274  225  VAL A O   
1507 C CB  . VAL A 208 ? 1.0001 0.6652 1.1305 -0.0919 -0.0020 0.2123  225  VAL A CB  
1508 C CG1 . VAL A 208 ? 0.9854 0.6464 1.0834 -0.0680 0.0017  0.1860  225  VAL A CG1 
1509 C CG2 . VAL A 208 ? 1.0882 0.8035 1.2261 -0.0960 0.0130  0.2244  225  VAL A CG2 
1510 N N   . THR A 209 ? 1.0770 0.6841 1.2706 -0.1396 -0.0346 0.2507  226  THR A N   
1511 C CA  . THR A 209 ? 1.1075 0.7017 1.3373 -0.1662 -0.0473 0.2769  226  THR A CA  
1512 C C   . THR A 209 ? 1.1987 0.8450 1.4535 -0.1777 -0.0316 0.3123  226  THR A C   
1513 O O   . THR A 209 ? 1.1139 0.7657 1.4014 -0.2016 -0.0408 0.3276  226  THR A O   
1514 C CB  . THR A 209 ? 1.1544 0.7033 1.3902 -0.1680 -0.0592 0.2924  226  THR A CB  
1515 O OG1 . THR A 209 ? 1.3655 0.8724 1.5745 -0.1501 -0.0688 0.2595  226  THR A OG1 
1516 C CG2 . THR A 209 ? 1.1935 0.7138 1.4652 -0.1973 -0.0804 0.3102  226  THR A CG2 
1517 N N   . THR A 210 ? 1.0670 0.7524 1.3074 -0.1610 -0.0085 0.3258  227  THR A N   
1518 C CA  . THR A 210 ? 1.1153 0.8473 1.3793 -0.1700 0.0076  0.3637  227  THR A CA  
1519 C C   . THR A 210 ? 1.1499 0.9355 1.3980 -0.1538 0.0308  0.3595  227  THR A C   
1520 O O   . THR A 210 ? 1.4212 1.2451 1.6919 -0.1637 0.0382  0.3721  227  THR A O   
1521 C CB  . THR A 210 ? 1.1773 0.9030 1.4445 -0.1687 0.0131  0.3978  227  THR A CB  
1522 O OG1 . THR A 210 ? 1.3748 1.0465 1.6578 -0.1837 -0.0103 0.4019  227  THR A OG1 
1523 C CG2 . THR A 210 ? 1.1007 0.8758 1.3950 -0.1796 0.0299  0.4399  227  THR A CG2 
1524 N N   . GLY A 211 ? 1.1481 0.9362 1.3586 -0.1288 0.0414  0.3424  228  GLY A N   
1525 C CA  . GLY A 211 ? 1.3275 1.1627 1.5206 -0.1121 0.0635  0.3433  228  GLY A CA  
1526 C C   . GLY A 211 ? 1.3134 1.1686 1.5043 -0.1107 0.0642  0.3177  228  GLY A C   
1527 O O   . GLY A 211 ? 1.2376 1.0713 1.4366 -0.1216 0.0477  0.2965  228  GLY A O   
1528 N N   . ASP A 212 ? 1.3528 1.2498 1.5311 -0.0962 0.0834  0.3205  229  ASP A N   
1529 C CA  . ASP A 212 ? 1.2753 1.1930 1.4458 -0.0899 0.0862  0.2966  229  ASP A CA  
1530 C C   . ASP A 212 ? 1.2089 1.1161 1.3386 -0.0683 0.0875  0.2665  229  ASP A C   
1531 O O   . ASP A 212 ? 1.2147 1.1413 1.3330 -0.0597 0.0921  0.2489  229  ASP A O   
1532 C CB  . ASP A 212 ? 1.2452 1.2142 1.4279 -0.0861 0.1056  0.3166  229  ASP A CB  
1533 C CG  . ASP A 212 ? 1.2994 1.2866 1.5278 -0.1092 0.1015  0.3372  229  ASP A CG  
1534 O OD1 . ASP A 212 ? 1.4796 1.4368 1.7288 -0.1296 0.0821  0.3361  229  ASP A OD1 
1535 O OD2 . ASP A 212 ? 1.3396 1.3713 1.5832 -0.1065 0.1172  0.3543  229  ASP A OD2 
1536 N N   . SER A 213 ? 1.2060 1.0833 1.3156 -0.0597 0.0825  0.2614  230  SER A N   
1537 C CA  . SER A 213 ? 1.1776 1.0498 1.2507 -0.0387 0.0847  0.2382  230  SER A CA  
1538 C C   . SER A 213 ? 0.9242 0.7835 0.9893 -0.0386 0.0733  0.2040  230  SER A C   
1539 O O   . SER A 213 ? 1.0794 0.9456 1.1188 -0.0233 0.0766  0.1853  230  SER A O   
1540 C CB  . SER A 213 ? 1.0957 0.9399 1.1541 -0.0305 0.0807  0.2434  230  SER A CB  
1541 O OG  . SER A 213 ? 0.9159 0.7227 0.9918 -0.0440 0.0643  0.2415  230  SER A OG  
1542 N N   . MET A 214 ? 1.0643 0.9051 1.1498 -0.0557 0.0594  0.1960  231  MET A N   
1543 C CA  . MET A 214 ? 0.8879 0.7163 0.9643 -0.0562 0.0485  0.1646  231  MET A CA  
1544 C C   . MET A 214 ? 0.8580 0.7126 0.9461 -0.0646 0.0494  0.1593  231  MET A C   
1545 O O   . MET A 214 ? 0.8013 0.6499 0.8811 -0.0656 0.0411  0.1349  231  MET A O   
1546 C CB  . MET A 214 ? 0.9938 0.7813 1.0789 -0.0674 0.0309  0.1547  231  MET A CB  
1547 C CG  . MET A 214 ? 1.1020 0.8593 1.1754 -0.0573 0.0277  0.1559  231  MET A CG  
1548 S SD  . MET A 214 ? 1.0783 0.8398 1.1164 -0.0317 0.0338  0.1347  231  MET A SD  
1549 C CE  . MET A 214 ? 1.0732 0.8528 1.1031 -0.0201 0.0483  0.1636  231  MET A CE  
1550 N N   . LYS A 215 ? 0.8087 0.6936 0.9163 -0.0700 0.0595  0.1824  232  LYS A N   
1551 C CA  . LYS A 215 ? 0.8555 0.7682 0.9768 -0.0762 0.0609  0.1798  232  LYS A CA  
1552 C C   . LYS A 215 ? 0.9004 0.8336 0.9958 -0.0571 0.0711  0.1657  232  LYS A C   
1553 O O   . LYS A 215 ? 0.8150 0.7769 0.9083 -0.0466 0.0860  0.1788  232  LYS A O   
1554 C CB  . LYS A 215 ? 0.8257 0.7659 0.9799 -0.0873 0.0688  0.2108  232  LYS A CB  
1555 C CG  . LYS A 215 ? 0.8307 0.7517 1.0162 -0.1110 0.0547  0.2245  232  LYS A CG  
1556 C CD  . LYS A 215 ? 1.1518 1.1030 1.3704 -0.1204 0.0649  0.2610  232  LYS A CD  
1557 C CE  . LYS A 215 ? 1.0627 1.0015 1.3190 -0.1479 0.0479  0.2737  232  LYS A CE  
1558 N NZ  . LYS A 215 ? 1.1367 1.0247 1.3871 -0.1563 0.0304  0.2657  232  LYS A NZ  
1559 N N   . ILE A 216 ? 0.9410 0.8584 1.0158 -0.0522 0.0625  0.1383  233  ILE A N   
1560 C CA  . ILE A 216 ? 1.0114 0.9429 1.0613 -0.0356 0.0687  0.1239  233  ILE A CA  
1561 C C   . ILE A 216 ? 0.8431 0.8044 0.9041 -0.0367 0.0734  0.1261  233  ILE A C   
1562 O O   . ILE A 216 ? 0.8124 0.7912 0.8578 -0.0217 0.0827  0.1239  233  ILE A O   
1563 C CB  . ILE A 216 ? 0.7448 0.6551 0.7746 -0.0325 0.0578  0.0966  233  ILE A CB  
1564 C CG1 . ILE A 216 ? 0.7382 0.6619 0.7438 -0.0168 0.0626  0.0838  233  ILE A CG1 
1565 C CG2 . ILE A 216 ? 0.7861 0.6885 0.8287 -0.0485 0.0447  0.0840  233  ILE A CG2 
1566 C CD1 . ILE A 216 ? 0.7192 0.6287 0.7080 -0.0143 0.0531  0.0598  233  ILE A CD1 
1567 N N   . GLU A 217 ? 0.8368 0.8034 0.9249 -0.0540 0.0660  0.1304  234  GLU A N   
1568 C CA  . GLU A 217 ? 0.8487 0.8447 0.9511 -0.0550 0.0695  0.1339  234  GLU A CA  
1569 C C   . GLU A 217 ? 0.8409 0.8671 0.9526 -0.0449 0.0874  0.1569  234  GLU A C   
1570 O O   . GLU A 217 ? 0.8606 0.9114 0.9734 -0.0359 0.0944  0.1566  234  GLU A O   
1571 C CB  . GLU A 217 ? 0.7974 0.7931 0.9290 -0.0768 0.0563  0.1361  234  GLU A CB  
1572 C CG  . GLU A 217 ? 0.8515 0.8748 0.9976 -0.0784 0.0560  0.1361  234  GLU A CG  
1573 C CD  . GLU A 217 ? 0.9258 0.9513 1.0444 -0.0635 0.0572  0.1160  234  GLU A CD  
1574 O OE1 . GLU A 217 ? 0.7854 0.8352 0.9047 -0.0510 0.0673  0.1211  234  GLU A OE1 
1575 O OE2 . GLU A 217 ? 0.9423 0.9453 1.0390 -0.0638 0.0477  0.0955  234  GLU A OE2 
1576 N N   . LYS A 218 ? 0.7971 0.8220 0.9147 -0.0453 0.0951  0.1771  235  LYS A N   
1577 C CA  . LYS A 218 ? 0.8673 0.9223 0.9882 -0.0331 0.1143  0.1990  235  LYS A CA  
1578 C C   . LYS A 218 ? 0.8559 0.9129 0.9385 -0.0087 0.1241  0.1873  235  LYS A C   
1579 O O   . LYS A 218 ? 0.8981 0.9821 0.9768 0.0057  0.1392  0.1966  235  LYS A O   
1580 C CB  . LYS A 218 ? 0.8058 0.8584 0.9412 -0.0406 0.1196  0.2254  235  LYS A CB  
1581 C CG  . LYS A 218 ? 0.8871 0.9385 1.0633 -0.0660 0.1091  0.2407  235  LYS A CG  
1582 C CD  . LYS A 218 ? 0.8718 0.9207 1.0632 -0.0739 0.1139  0.2695  235  LYS A CD  
1583 C CE  . LYS A 218 ? 0.9471 1.0410 1.1608 -0.0706 0.1335  0.3007  235  LYS A CE  
1584 N NZ  . LYS A 218 ? 0.9011 1.0172 1.1610 -0.0907 0.1280  0.3159  235  LYS A NZ  
1585 N N   . SER A 219 ? 0.7655 0.7946 0.8198 -0.0033 0.1154  0.1670  236  SER A N   
1586 C CA  . SER A 219 ? 0.8660 0.8950 0.8847 0.0178  0.1209  0.1545  236  SER A CA  
1587 C C   . SER A 219 ? 0.9204 0.9606 0.9342 0.0238  0.1184  0.1380  236  SER A C   
1588 O O   . SER A 219 ? 0.9312 0.9833 0.9254 0.0416  0.1271  0.1353  236  SER A O   
1589 C CB  . SER A 219 ? 0.8346 0.8335 0.8293 0.0206  0.1112  0.1395  236  SER A CB  
1590 O OG  . SER A 219 ? 1.0971 1.0866 1.0893 0.0214  0.1156  0.1559  236  SER A OG  
1591 N N   . PHE A 220 ? 0.8870 0.9219 0.9168 0.0095  0.1056  0.1267  237  PHE A N   
1592 C CA  . PHE A 220 ? 0.7873 0.8330 0.8158 0.0134  0.1020  0.1137  237  PHE A CA  
1593 C C   . PHE A 220 ? 0.8833 0.9605 0.9315 0.0190  0.1141  0.1293  237  PHE A C   
1594 O O   . PHE A 220 ? 0.9050 0.9930 0.9406 0.0345  0.1188  0.1227  237  PHE A O   
1595 C CB  . PHE A 220 ? 0.7235 0.7580 0.7647 -0.0042 0.0857  0.1007  237  PHE A CB  
1596 C CG  . PHE A 220 ? 0.7130 0.7211 0.7326 -0.0059 0.0749  0.0819  237  PHE A CG  
1597 C CD1 . PHE A 220 ? 0.7792 0.7815 0.7711 0.0073  0.0735  0.0671  237  PHE A CD1 
1598 C CD2 . PHE A 220 ? 0.7320 0.7213 0.7597 -0.0204 0.0656  0.0789  237  PHE A CD2 
1599 C CE1 . PHE A 220 ? 0.6704 0.6533 0.6460 0.0059  0.0645  0.0517  237  PHE A CE1 
1600 C CE2 . PHE A 220 ? 0.7511 0.7191 0.7599 -0.0197 0.0574  0.0616  237  PHE A CE2 
1601 C CZ  . PHE A 220 ? 0.7316 0.6988 0.7158 -0.0067 0.0575  0.0489  237  PHE A CZ  
1602 N N   . GLU A 221 ? 0.7840 0.8763 0.8643 0.0068  0.1186  0.1504  238  GLU A N   
1603 C CA  . GLU A 221 ? 0.8157 0.9432 0.9195 0.0123  0.1315  0.1681  238  GLU A CA  
1604 C C   . GLU A 221 ? 0.8748 1.0171 0.9568 0.0360  0.1507  0.1762  238  GLU A C   
1605 O O   . GLU A 221 ? 0.9193 1.0872 1.0057 0.0502  0.1617  0.1804  238  GLU A O   
1606 C CB  . GLU A 221 ? 0.7932 0.9343 0.9378 -0.0076 0.1314  0.1916  238  GLU A CB  
1607 C CG  . GLU A 221 ? 0.8643 0.9922 1.0302 -0.0307 0.1115  0.1835  238  GLU A CG  
1608 C CD  . GLU A 221 ? 0.9884 1.1205 1.1906 -0.0524 0.1074  0.2051  238  GLU A CD  
1609 O OE1 . GLU A 221 ? 0.9369 1.0598 1.1581 -0.0719 0.0905  0.2002  238  GLU A OE1 
1610 O OE2 . GLU A 221 ? 0.9868 1.1307 1.1978 -0.0505 0.1202  0.2275  238  GLU A OE2 
1611 N N   . THR A 222 ? 0.8229 0.9491 0.8801 0.0416  0.1545  0.1781  239  THR A N   
1612 C CA  . THR A 222 ? 0.8302 0.9668 0.8589 0.0650  0.1709  0.1830  239  THR A CA  
1613 C C   . THR A 222 ? 0.8964 1.0227 0.8913 0.0834  0.1671  0.1585  239  THR A C   
1614 O O   . THR A 222 ? 1.0023 1.1455 0.9833 0.1038  0.1796  0.1593  239  THR A O   
1615 C CB  . THR A 222 ? 0.9450 1.0648 0.9551 0.0650  0.1731  0.1915  239  THR A CB  
1616 O OG1 . THR A 222 ? 0.9175 1.0478 0.9599 0.0488  0.1775  0.2176  239  THR A OG1 
1617 C CG2 . THR A 222 ? 0.8496 0.9773 0.8235 0.0897  0.1879  0.1942  239  THR A CG2 
1618 N N   . LEU A 223 ? 0.9286 1.0274 0.9105 0.0767  0.1495  0.1367  240  LEU A N   
1619 C CA  . LEU A 223 ? 0.9062 0.9926 0.8578 0.0912  0.1430  0.1145  240  LEU A CA  
1620 C C   . LEU A 223 ? 0.8972 0.9993 0.8616 0.0967  0.1431  0.1093  240  LEU A C   
1621 O O   . LEU A 223 ? 0.9751 1.0753 0.9156 0.1155  0.1447  0.0980  240  LEU A O   
1622 C CB  . LEU A 223 ? 0.7817 0.8395 0.7221 0.0803  0.1246  0.0959  240  LEU A CB  
1623 C CG  . LEU A 223 ? 0.8619 0.9001 0.7701 0.0884  0.1226  0.0904  240  LEU A CG  
1624 C CD1 . LEU A 223 ? 0.8101 0.8260 0.7139 0.0774  0.1056  0.0735  240  LEU A CD1 
1625 C CD2 . LEU A 223 ? 0.7824 0.8210 0.6568 0.1112  0.1275  0.0832  240  LEU A CD2 
1626 N N   . VAL A 224 ? 0.8957 1.0116 0.8973 0.0808  0.1397  0.1169  241  VAL A N   
1627 C CA  . VAL A 224 ? 0.8283 0.9628 0.8474 0.0862  0.1404  0.1158  241  VAL A CA  
1628 C C   . VAL A 224 ? 0.9567 1.1265 0.9963 0.0970  0.1601  0.1370  241  VAL A C   
1629 O O   . VAL A 224 ? 0.8241 1.0138 0.8839 0.1023  0.1621  0.1389  241  VAL A O   
1630 C CB  . VAL A 224 ? 0.7962 0.9287 0.8442 0.0638  0.1246  0.1124  241  VAL A CB  
1631 C CG1 . VAL A 224 ? 0.6914 0.7931 0.7183 0.0551  0.1069  0.0916  241  VAL A CG1 
1632 C CG2 . VAL A 224 ? 0.9002 1.0438 0.9817 0.0439  0.1260  0.1314  241  VAL A CG2 
1633 N N   . GLN A 225 ? 0.8878 1.0676 0.9237 0.1009  0.1749  0.1542  242  GLN A N   
1634 C CA  . GLN A 225 ? 0.8764 1.0935 0.9286 0.1134  0.1966  0.1764  242  GLN A CA  
1635 C C   . GLN A 225 ? 0.8391 1.0858 0.9436 0.0981  0.1971  0.1939  242  GLN A C   
1636 O O   . GLN A 225 ? 0.8373 1.1166 0.9601 0.1112  0.2099  0.2037  242  GLN A O   
1637 C CB  . GLN A 225 ? 0.9038 1.1281 0.9274 0.1440  0.2075  0.1658  242  GLN A CB  
1638 C CG  . GLN A 225 ? 0.9841 1.1831 0.9556 0.1602  0.2084  0.1522  242  GLN A CG  
1639 C CD  . GLN A 225 ? 1.0474 1.2361 0.9866 0.1851  0.2068  0.1306  242  GLN A CD  
1640 O OE1 . GLN A 225 ? 1.0521 1.2366 1.0028 0.1844  0.1960  0.1181  242  GLN A OE1 
1641 N NE2 . GLN A 225 ? 1.1900 1.3726 1.0872 0.2070  0.2163  0.1262  242  GLN A NE2 
1642 N N   . LYS A 226 ? 0.8707 1.1064 0.9995 0.0709  0.1827  0.1980  243  LYS A N   
1643 C CA  . LYS A 226 ? 0.7674 1.0272 0.9460 0.0520  0.1792  0.2152  243  LYS A CA  
1644 C C   . LYS A 226 ? 0.8802 1.1554 1.0826 0.0391  0.1885  0.2434  243  LYS A C   
1645 O O   . LYS A 226 ? 0.8330 1.0818 1.0268 0.0250  0.1803  0.2432  243  LYS A O   
1646 C CB  . LYS A 226 ? 0.8343 1.0697 1.0224 0.0296  0.1547  0.1999  243  LYS A CB  
1647 C CG  . LYS A 226 ? 0.8160 1.0728 1.0537 0.0079  0.1472  0.2167  243  LYS A CG  
1648 C CD  . LYS A 226 ? 0.7442 1.0406 1.0091 0.0205  0.1571  0.2271  243  LYS A CD  
1649 C CE  . LYS A 226 ? 0.7362 1.0559 1.0533 -0.0023 0.1477  0.2451  243  LYS A CE  
1650 N NZ  . LYS A 226 ? 0.9900 1.3466 1.3350 0.0098  0.1537  0.2525  243  LYS A NZ  
1651 N N   . THR A 227 ? 0.8399 1.1580 1.0734 0.0443  0.2054  0.2683  244  THR A N   
1652 C CA  . THR A 227 ? 0.8557 1.1948 1.1157 0.0326  0.2161  0.2997  244  THR A CA  
1653 C C   . THR A 227 ? 0.9234 1.2800 1.2388 0.0054  0.2048  0.3175  244  THR A C   
1654 O O   . THR A 227 ? 0.9715 1.3432 1.3104 0.0034  0.1977  0.3129  244  THR A O   
1655 C CB  . THR A 227 ? 0.8580 1.2382 1.1161 0.0569  0.2448  0.3194  244  THR A CB  
1656 O OG1 . THR A 227 ? 0.7523 1.1702 1.0391 0.0672  0.2522  0.3240  244  THR A OG1 
1657 C CG2 . THR A 227 ? 0.8158 1.1768 1.0156 0.0843  0.2541  0.3006  244  THR A CG2 
1658 N N   . GLY A 228 ? 0.8209 1.1736 1.1570 -0.0162 0.2014  0.3383  245  GLY A N   
1659 C CA  . GLY A 228 ? 0.7611 1.1335 1.1521 -0.0428 0.1918  0.3607  245  GLY A CA  
1660 C C   . GLY A 228 ? 0.9440 1.2784 1.3432 -0.0702 0.1623  0.3462  245  GLY A C   
1661 O O   . GLY A 228 ? 0.8773 1.2244 1.3212 -0.0941 0.1509  0.3636  245  GLY A O   
1662 N N   . CYS A 229 ? 0.9302 1.2196 1.2882 -0.0676 0.1493  0.3153  246  CYS A N   
1663 C CA  . CYS A 229 ? 0.9056 1.1588 1.2668 -0.0913 0.1226  0.2997  246  CYS A CA  
1664 C C   . CYS A 229 ? 0.9111 1.1391 1.2791 -0.1105 0.1149  0.3122  246  CYS A C   
1665 O O   . CYS A 229 ? 0.8498 1.0690 1.1971 -0.1011 0.1267  0.3189  246  CYS A O   
1666 C CB  . CYS A 229 ? 1.0028 1.2202 1.3188 -0.0811 0.1128  0.2637  246  CYS A CB  
1667 S SG  . CYS A 229 ? 1.0107 1.2463 1.3155 -0.0611 0.1157  0.2453  246  CYS A SG  
1668 N N   . THR A 230 ? 0.9629 1.1776 1.3593 -0.1376 0.0934  0.3152  247  THR A N   
1669 C CA  . THR A 230 ? 0.8763 1.0600 1.2802 -0.1578 0.0812  0.3242  247  THR A CA  
1670 C C   . THR A 230 ? 0.8847 1.0205 1.2725 -0.1725 0.0547  0.2966  247  THR A C   
1671 O O   . THR A 230 ? 0.8153 0.9195 1.2086 -0.1895 0.0411  0.3004  247  THR A O   
1672 C CB  . THR A 230 ? 0.7530 0.9656 1.2120 -0.1796 0.0795  0.3604  247  THR A CB  
1673 O OG1 . THR A 230 ? 0.8231 1.0434 1.3124 -0.1980 0.0605  0.3575  247  THR A OG1 
1674 C CG2 . THR A 230 ? 0.7502 1.0171 1.2277 -0.1640 0.1077  0.3892  247  THR A CG2 
1675 N N   . ASP A 231 ? 1.0173 1.1463 1.3848 -0.1661 0.0470  0.2694  248  ASP A N   
1676 C CA  . ASP A 231 ? 1.0168 1.1042 1.3657 -0.1781 0.0236  0.2422  248  ASP A CA  
1677 C C   . ASP A 231 ? 0.8557 0.9113 1.1554 -0.1606 0.0268  0.2156  248  ASP A C   
1678 O O   . ASP A 231 ? 0.8066 0.8484 1.0816 -0.1561 0.0186  0.1894  248  ASP A O   
1679 C CB  . ASP A 231 ? 0.8169 0.9184 1.1764 -0.1847 0.0113  0.2315  248  ASP A CB  
1680 C CG  . ASP A 231 ? 0.9561 1.0844 1.3669 -0.2061 0.0023  0.2564  248  ASP A CG  
1681 O OD1 . ASP A 231 ? 0.9754 1.1435 1.4164 -0.2020 0.0188  0.2843  248  ASP A OD1 
1682 O OD2 . ASP A 231 ? 0.9564 1.0670 1.3768 -0.2268 -0.0215 0.2484  248  ASP A OD2 
1683 N N   . ASN A 232 ? 0.8988 0.9442 1.1852 -0.1509 0.0386  0.2237  249  ASN A N   
1684 C CA  . ASN A 232 ? 0.9522 0.9719 1.1955 -0.1333 0.0430  0.2026  249  ASN A CA  
1685 C C   . ASN A 232 ? 0.9132 0.8955 1.1505 -0.1401 0.0356  0.2043  249  ASN A C   
1686 O O   . ASN A 232 ? 0.9241 0.8970 1.1399 -0.1258 0.0460  0.2056  249  ASN A O   
1687 C CB  . ASN A 232 ? 0.8885 0.9338 1.1151 -0.1091 0.0657  0.2089  249  ASN A CB  
1688 C CG  . ASN A 232 ? 0.9089 0.9862 1.1625 -0.1091 0.0816  0.2426  249  ASN A CG  
1689 O OD1 . ASN A 232 ? 0.9750 1.0456 1.2520 -0.1248 0.0774  0.2626  249  ASN A OD1 
1690 N ND2 . ASN A 232 ? 1.0129 1.1252 1.2634 -0.0910 0.0999  0.2495  249  ASN A ND2 
1691 N N   . GLY A 233 ? 0.8748 0.8334 1.1302 -0.1619 0.0161  0.2037  250  GLY A N   
1692 C CA  . GLY A 233 ? 1.0301 0.9503 1.2839 -0.1697 0.0068  0.2066  250  GLY A CA  
1693 C C   . GLY A 233 ? 0.9567 0.8360 1.1740 -0.1607 -0.0019 0.1762  250  GLY A C   
1694 O O   . GLY A 233 ? 1.0559 0.9012 1.2696 -0.1634 -0.0089 0.1771  250  GLY A O   
1695 N N   . PHE A 234 ? 0.9002 0.7828 1.0922 -0.1497 -0.0017 0.1505  251  PHE A N   
1696 C CA  . PHE A 234 ? 0.8463 0.6959 1.0053 -0.1402 -0.0084 0.1223  251  PHE A CA  
1697 C C   . PHE A 234 ? 0.8643 0.7038 1.0050 -0.1227 0.0033  0.1258  251  PHE A C   
1698 O O   . PHE A 234 ? 0.8712 0.7365 1.0098 -0.1106 0.0199  0.1403  251  PHE A O   
1699 C CB  . PHE A 234 ? 0.9318 0.7947 1.0694 -0.1315 -0.0077 0.0991  251  PHE A CB  
1700 C CG  . PHE A 234 ? 0.8115 0.6497 0.9156 -0.1189 -0.0104 0.0727  251  PHE A CG  
1701 C CD1 . PHE A 234 ? 0.9235 0.7308 1.0181 -0.1266 -0.0264 0.0525  251  PHE A CD1 
1702 C CD2 . PHE A 234 ? 0.7887 0.6359 0.8709 -0.0988 0.0028  0.0679  251  PHE A CD2 
1703 C CE1 . PHE A 234 ? 0.8044 0.5934 0.8699 -0.1134 -0.0270 0.0291  251  PHE A CE1 
1704 C CE2 . PHE A 234 ? 0.7663 0.5952 0.8219 -0.0875 0.0006  0.0457  251  PHE A CE2 
1705 C CZ  . PHE A 234 ? 0.8036 0.6051 0.8518 -0.0942 -0.0133 0.0267  251  PHE A CZ  
1706 N N   . GLN A 235 ? 0.9371 0.7382 1.0635 -0.1205 -0.0061 0.1121  252  GLN A N   
1707 C CA  . GLN A 235 ? 0.9078 0.6952 1.0179 -0.1045 0.0017  0.1146  252  GLN A CA  
1708 C C   . GLN A 235 ? 0.8646 0.6363 0.9439 -0.0896 -0.0007 0.0850  252  GLN A C   
1709 O O   . GLN A 235 ? 0.8529 0.5965 0.9260 -0.0942 -0.0142 0.0654  252  GLN A O   
1710 C CB  . GLN A 235 ? 0.9319 0.6874 1.0574 -0.1142 -0.0071 0.1297  252  GLN A CB  
1711 C CG  . GLN A 235 ? 0.9487 0.7245 1.1039 -0.1255 -0.0003 0.1652  252  GLN A CG  
1712 C CD  . GLN A 235 ? 0.9346 0.6773 1.1051 -0.1355 -0.0099 0.1822  252  GLN A CD  
1713 O OE1 . GLN A 235 ? 1.1319 0.8363 1.3064 -0.1464 -0.0286 0.1701  252  GLN A OE1 
1714 N NE2 . GLN A 235 ? 1.0324 0.7881 1.2100 -0.1314 0.0024  0.2104  252  GLN A NE2 
1715 N N   . GLY A 236 ? 0.8698 0.6604 0.9301 -0.0717 0.0120  0.0820  253  GLY A N   
1716 C CA  . GLY A 236 ? 0.8844 0.6665 0.9189 -0.0576 0.0109  0.0572  253  GLY A CA  
1717 C C   . GLY A 236 ? 0.8811 0.6890 0.8992 -0.0410 0.0240  0.0587  253  GLY A C   
1718 O O   . GLY A 236 ? 0.8704 0.6981 0.8934 -0.0381 0.0343  0.0782  253  GLY A O   
1719 N N   . TYR A 237 ? 0.7812 0.5886 0.7792 -0.0300 0.0230  0.0379  254  TYR A N   
1720 C CA  . TYR A 237 ? 0.7758 0.6037 0.7569 -0.0150 0.0318  0.0366  254  TYR A CA  
1721 C C   . TYR A 237 ? 0.8490 0.6816 0.8155 -0.0107 0.0278  0.0133  254  TYR A C   
1722 O O   . TYR A 237 ? 0.7942 0.6159 0.7619 -0.0182 0.0198  -0.0012 254  TYR A O   
1723 C CB  . TYR A 237 ? 0.7657 0.5838 0.7385 -0.0016 0.0361  0.0461  254  TYR A CB  
1724 C CG  . TYR A 237 ? 0.8886 0.6792 0.8569 0.0041  0.0288  0.0339  254  TYR A CG  
1725 C CD1 . TYR A 237 ? 0.8285 0.5907 0.8095 -0.0026 0.0223  0.0400  254  TYR A CD1 
1726 C CD2 . TYR A 237 ? 0.9420 0.7356 0.8949 0.0167  0.0279  0.0170  254  TYR A CD2 
1727 C CE1 . TYR A 237 ? 0.9490 0.6840 0.9254 0.0050  0.0154  0.0278  254  TYR A CE1 
1728 C CE2 . TYR A 237 ? 0.8459 0.6171 0.7961 0.0243  0.0224  0.0060  254  TYR A CE2 
1729 C CZ  . TYR A 237 ? 0.8690 0.6100 0.8301 0.0195  0.0164  0.0105  254  TYR A CZ  
1730 O OH  . TYR A 237 ? 0.9236 0.6403 0.8816 0.0293  0.0108  -0.0017 254  TYR A OH  
1731 N N   . TYR A 238 ? 0.7197 0.5691 0.6716 0.0013  0.0329  0.0104  255  TYR A N   
1732 C CA  . TYR A 238 ? 0.7987 0.6570 0.7381 0.0054  0.0298  -0.0079 255  TYR A CA  
1733 C C   . TYR A 238 ? 0.7697 0.6247 0.6969 0.0204  0.0307  -0.0122 255  TYR A C   
1734 O O   . TYR A 238 ? 0.7405 0.5954 0.6637 0.0293  0.0349  -0.0001 255  TYR A O   
1735 C CB  . TYR A 238 ? 0.7343 0.6169 0.6699 0.0041  0.0321  -0.0075 255  TYR A CB  
1736 C CG  . TYR A 238 ? 0.6831 0.5726 0.6297 -0.0102 0.0285  -0.0091 255  TYR A CG  
1737 C CD1 . TYR A 238 ? 0.6735 0.5707 0.6345 -0.0168 0.0320  0.0060  255  TYR A CD1 
1738 C CD2 . TYR A 238 ? 0.6687 0.5594 0.6116 -0.0168 0.0216  -0.0246 255  TYR A CD2 
1739 C CE1 . TYR A 238 ? 0.6671 0.5723 0.6406 -0.0299 0.0274  0.0055  255  TYR A CE1 
1740 C CE2 . TYR A 238 ? 0.6638 0.5609 0.6158 -0.0301 0.0167  -0.0254 255  TYR A CE2 
1741 C CZ  . TYR A 238 ? 0.7636 0.6675 0.7319 -0.0368 0.0190  -0.0104 255  TYR A CZ  
1742 O OH  . TYR A 238 ? 0.7460 0.6578 0.7258 -0.0500 0.0129  -0.0101 255  TYR A OH  
1743 N N   . VAL A 239 ? 0.7571 0.6114 0.6786 0.0235  0.0268  -0.0288 256  VAL A N   
1744 C CA  . VAL A 239 ? 0.7811 0.6385 0.6941 0.0375  0.0270  -0.0337 256  VAL A CA  
1745 C C   . VAL A 239 ? 0.7978 0.6784 0.7033 0.0376  0.0259  -0.0428 256  VAL A C   
1746 O O   . VAL A 239 ? 0.8905 0.7766 0.7960 0.0311  0.0235  -0.0547 256  VAL A O   
1747 C CB  . VAL A 239 ? 0.7514 0.5898 0.6665 0.0434  0.0243  -0.0441 256  VAL A CB  
1748 C CG1 . VAL A 239 ? 0.8825 0.7294 0.7925 0.0584  0.0248  -0.0478 256  VAL A CG1 
1749 C CG2 . VAL A 239 ? 0.8048 0.6164 0.7283 0.0420  0.0233  -0.0339 256  VAL A CG2 
1750 N N   . CYS A 240 ? 0.8924 0.7859 0.7908 0.0444  0.0266  -0.0366 257  CYS A N   
1751 C CA  . CYS A 240 ? 0.8007 0.7145 0.6932 0.0435  0.0235  -0.0425 257  CYS A CA  
1752 C C   . CYS A 240 ? 0.7180 0.6398 0.6079 0.0536  0.0209  -0.0472 257  CYS A C   
1753 O O   . CYS A 240 ? 0.8806 0.7938 0.7707 0.0639  0.0215  -0.0428 257  CYS A O   
1754 C CB  . CYS A 240 ? 0.7300 0.6512 0.6155 0.0438  0.0238  -0.0335 257  CYS A CB  
1755 S SG  . CYS A 240 ? 1.1157 1.0466 1.0041 0.0313  0.0230  -0.0344 257  CYS A SG  
1756 N N   . LEU A 241 ? 0.7885 0.7286 0.6778 0.0501  0.0176  -0.0545 258  LEU A N   
1757 C CA  . LEU A 241 ? 0.6935 0.6482 0.5835 0.0577  0.0144  -0.0567 258  LEU A CA  
1758 C C   . LEU A 241 ? 0.7769 0.7481 0.6626 0.0524  0.0080  -0.0546 258  LEU A C   
1759 O O   . LEU A 241 ? 0.8509 0.8288 0.7363 0.0418  0.0067  -0.0576 258  LEU A O   
1760 C CB  . LEU A 241 ? 0.6953 0.6580 0.5917 0.0590  0.0167  -0.0675 258  LEU A CB  
1761 C CG  . LEU A 241 ? 0.8218 0.7691 0.7227 0.0704  0.0204  -0.0706 258  LEU A CG  
1762 C CD1 . LEU A 241 ? 0.8319 0.7837 0.7352 0.0715  0.0240  -0.0841 258  LEU A CD1 
1763 C CD2 . LEU A 241 ? 0.7388 0.6917 0.6430 0.0834  0.0180  -0.0641 258  LEU A CD2 
1764 N N   . ILE A 242 ? 0.8346 0.8105 0.7165 0.0596  0.0026  -0.0493 259  ILE A N   
1765 C CA  . ILE A 242 ? 0.7031 0.6889 0.5793 0.0552  -0.0061 -0.0471 259  ILE A CA  
1766 C C   . ILE A 242 ? 0.7972 0.8057 0.6829 0.0516  -0.0115 -0.0500 259  ILE A C   
1767 O O   . ILE A 242 ? 0.8144 0.8323 0.7084 0.0589  -0.0108 -0.0501 259  ILE A O   
1768 C CB  . ILE A 242 ? 0.7055 0.6824 0.5697 0.0643  -0.0111 -0.0400 259  ILE A CB  
1769 C CG1 . ILE A 242 ? 0.7709 0.7298 0.6257 0.0675  -0.0041 -0.0350 259  ILE A CG1 
1770 C CG2 . ILE A 242 ? 0.7668 0.7507 0.6240 0.0605  -0.0230 -0.0396 259  ILE A CG2 
1771 C CD1 . ILE A 242 ? 0.7994 0.7499 0.6377 0.0773  -0.0077 -0.0279 259  ILE A CD1 
1772 N N   . GLY A 243 ? 0.7189 0.7374 0.6048 0.0405  -0.0168 -0.0510 260  GLY A N   
1773 C CA  . GLY A 243 ? 0.5993 0.6422 0.4956 0.0348  -0.0219 -0.0509 260  GLY A CA  
1774 C C   . GLY A 243 ? 0.7293 0.7855 0.6351 0.0357  -0.0124 -0.0565 260  GLY A C   
1775 O O   . GLY A 243 ? 0.8511 0.8978 0.7539 0.0338  -0.0046 -0.0624 260  GLY A O   
1776 N N   . SER A 244 ? 0.6835 0.7627 0.6011 0.0393  -0.0134 -0.0548 261  SER A N   
1777 C CA  . SER A 244 ? 0.8248 0.9187 0.7506 0.0444  -0.0032 -0.0609 261  SER A CA  
1778 C C   . SER A 244 ? 0.7985 0.8864 0.7295 0.0610  0.0016  -0.0624 261  SER A C   
1779 O O   . SER A 244 ? 0.7102 0.8031 0.6455 0.0687  0.0109  -0.0698 261  SER A O   
1780 C CB  . SER A 244 ? 0.6079 0.7374 0.5462 0.0380  -0.0051 -0.0569 261  SER A CB  
1781 O OG  . SER A 244 ? 0.7518 0.8968 0.7023 0.0422  -0.0131 -0.0484 261  SER A OG  
1782 N N   . SER A 245 ? 0.7180 0.7941 0.6473 0.0675  -0.0049 -0.0559 262  SER A N   
1783 C CA  . SER A 245 ? 0.7321 0.8020 0.6670 0.0833  -0.0022 -0.0551 262  SER A CA  
1784 C C   . SER A 245 ? 0.8282 0.8740 0.7518 0.0872  -0.0080 -0.0485 262  SER A C   
1785 O O   . SER A 245 ? 0.8397 0.8880 0.7579 0.0830  -0.0183 -0.0421 262  SER A O   
1786 C CB  . SER A 245 ? 0.7472 0.8480 0.7001 0.0896  -0.0055 -0.0505 262  SER A CB  
1787 O OG  . SER A 245 ? 0.7672 0.8611 0.7260 0.1053  -0.0056 -0.0476 262  SER A OG  
1788 N N   . SER A 246 ? 0.7355 0.7574 0.6545 0.0952  -0.0019 -0.0497 263  SER A N   
1789 C CA  . SER A 246 ? 0.7897 0.7901 0.6975 0.1002  -0.0052 -0.0416 263  SER A CA  
1790 C C   . SER A 246 ? 0.7510 0.7292 0.6603 0.1090  0.0022  -0.0424 263  SER A C   
1791 O O   . SER A 246 ? 0.7480 0.7244 0.6649 0.1109  0.0088  -0.0511 263  SER A O   
1792 C CB  . SER A 246 ? 0.7038 0.6930 0.5963 0.0901  -0.0069 -0.0395 263  SER A CB  
1793 O OG  . SER A 246 ? 0.7333 0.7103 0.6245 0.0835  0.0013  -0.0445 263  SER A OG  
1794 N N   . GLU A 247 ? 0.7683 0.7283 0.6689 0.1146  0.0003  -0.0329 264  GLU A N   
1795 C CA  . GLU A 247 ? 0.7623 0.6973 0.6636 0.1198  0.0060  -0.0306 264  GLU A CA  
1796 C C   . GLU A 247 ? 0.8531 0.7737 0.7482 0.1082  0.0116  -0.0321 264  GLU A C   
1797 O O   . GLU A 247 ? 0.8023 0.7282 0.6882 0.0997  0.0106  -0.0300 264  GLU A O   
1798 C CB  . GLU A 247 ? 0.7199 0.6429 0.6144 0.1292  0.0020  -0.0172 264  GLU A CB  
1799 C CG  . GLU A 247 ? 0.7833 0.7167 0.6874 0.1424  -0.0041 -0.0142 264  GLU A CG  
1800 C CD  . GLU A 247 ? 0.9370 0.8583 0.8316 0.1510  -0.0095 0.0003  264  GLU A CD  
1801 O OE1 . GLU A 247 ? 1.0761 0.9823 0.9555 0.1469  -0.0071 0.0083  264  GLU A OE1 
1802 O OE2 . GLU A 247 ? 1.1727 1.1015 1.0753 0.1621  -0.0159 0.0048  264  GLU A OE2 
1803 N N   . PRO A 248 ? 0.7665 0.6684 0.6673 0.1078  0.0164  -0.0358 265  PRO A N   
1804 C CA  . PRO A 248 ? 0.7553 0.6448 0.6535 0.0955  0.0202  -0.0359 265  PRO A CA  
1805 C C   . PRO A 248 ? 0.7412 0.6236 0.6308 0.0932  0.0212  -0.0212 265  PRO A C   
1806 O O   . PRO A 248 ? 0.8344 0.7093 0.7200 0.1019  0.0201  -0.0101 265  PRO A O   
1807 C CB  . PRO A 248 ? 0.8402 0.7067 0.7465 0.0977  0.0221  -0.0411 265  PRO A CB  
1808 C CG  . PRO A 248 ? 0.7387 0.6125 0.6514 0.1105  0.0212  -0.0501 265  PRO A CG  
1809 C CD  . PRO A 248 ? 0.7958 0.6869 0.7068 0.1186  0.0174  -0.0412 265  PRO A CD  
1810 N N   . LEU A 249 ? 0.8190 0.7053 0.7053 0.0821  0.0236  -0.0206 266  LEU A N   
1811 C CA  . LEU A 249 ? 0.7053 0.5899 0.5830 0.0807  0.0266  -0.0076 266  LEU A CA  
1812 C C   . LEU A 249 ? 0.8048 0.6768 0.6911 0.0712  0.0317  -0.0018 266  LEU A C   
1813 O O   . LEU A 249 ? 0.8503 0.7237 0.7441 0.0608  0.0316  -0.0102 266  LEU A O   
1814 C CB  . LEU A 249 ? 0.7221 0.6238 0.5900 0.0775  0.0246  -0.0105 266  LEU A CB  
1815 C CG  . LEU A 249 ? 0.8375 0.7396 0.6936 0.0789  0.0286  0.0007  266  LEU A CG  
1816 C CD1 . LEU A 249 ? 0.9053 0.8013 0.7491 0.0908  0.0284  0.0121  266  LEU A CD1 
1817 C CD2 . LEU A 249 ? 0.8469 0.7621 0.6938 0.0766  0.0249  -0.0053 266  LEU A CD2 
1818 N N   . TYR A 250 ? 0.8150 0.6759 0.7007 0.0741  0.0353  0.0137  267  TYR A N   
1819 C CA  . TYR A 250 ? 0.7501 0.6004 0.6470 0.0642  0.0395  0.0233  267  TYR A CA  
1820 C C   . TYR A 250 ? 0.7931 0.6589 0.6863 0.0596  0.0455  0.0315  267  TYR A C   
1821 O O   . TYR A 250 ? 1.0056 0.8800 0.8845 0.0680  0.0489  0.0400  267  TYR A O   
1822 C CB  . TYR A 250 ? 0.9637 0.7957 0.8640 0.0688  0.0405  0.0388  267  TYR A CB  
1823 C CG  . TYR A 250 ? 0.8678 0.6862 0.7841 0.0569  0.0425  0.0499  267  TYR A CG  
1824 C CD1 . TYR A 250 ? 0.9314 0.7255 0.8606 0.0525  0.0366  0.0450  267  TYR A CD1 
1825 C CD2 . TYR A 250 ? 0.8847 0.7144 0.8040 0.0504  0.0498  0.0656  267  TYR A CD2 
1826 C CE1 . TYR A 250 ? 0.8278 0.6074 0.7729 0.0397  0.0358  0.0559  267  TYR A CE1 
1827 C CE2 . TYR A 250 ? 0.8894 0.7096 0.8270 0.0379  0.0508  0.0781  267  TYR A CE2 
1828 C CZ  . TYR A 250 ? 0.8352 0.6293 0.7860 0.0315  0.0427  0.0734  267  TYR A CZ  
1829 O OH  . TYR A 250 ? 0.8630 0.6455 0.8333 0.0172  0.0411  0.0865  267  TYR A OH  
1830 N N   . ILE A 251 ? 0.8328 0.7021 0.7381 0.0472  0.0463  0.0286  268  ILE A N   
1831 C CA  . ILE A 251 ? 0.8319 0.7170 0.7384 0.0430  0.0522  0.0364  268  ILE A CA  
1832 C C   . ILE A 251 ? 0.8647 0.7442 0.7901 0.0323  0.0561  0.0510  268  ILE A C   
1833 O O   . ILE A 251 ? 0.9562 0.8248 0.8962 0.0209  0.0506  0.0454  268  ILE A O   
1834 C CB  . ILE A 251 ? 0.8220 0.7199 0.7292 0.0368  0.0485  0.0222  268  ILE A CB  
1835 C CG1 . ILE A 251 ? 0.7990 0.7013 0.6916 0.0445  0.0427  0.0086  268  ILE A CG1 
1836 C CG2 . ILE A 251 ? 0.8014 0.7157 0.7092 0.0362  0.0545  0.0302  268  ILE A CG2 
1837 C CD1 . ILE A 251 ? 0.8325 0.7399 0.7068 0.0575  0.0442  0.0139  268  ILE A CD1 
1838 N N   . PRO A 252 ? 0.9108 0.7983 0.8366 0.0352  0.0650  0.0704  269  PRO A N   
1839 C CA  . PRO A 252 ? 0.9165 0.8159 0.8213 0.0496  0.0717  0.0769  269  PRO A CA  
1840 C C   . PRO A 252 ? 0.8769 0.7649 0.7702 0.0593  0.0729  0.0883  269  PRO A C   
1841 O O   . PRO A 252 ? 0.9839 0.8595 0.8902 0.0539  0.0736  0.1019  269  PRO A O   
1842 C CB  . PRO A 252 ? 0.8496 0.7676 0.7628 0.0469  0.0823  0.0920  269  PRO A CB  
1843 C CG  . PRO A 252 ? 0.7443 0.6549 0.6846 0.0319  0.0820  0.1043  269  PRO A CG  
1844 C CD  . PRO A 252 ? 0.8583 0.7484 0.8061 0.0232  0.0694  0.0872  269  PRO A CD  
1845 N N   . THR A 253 ? 0.9734 0.8648 0.8430 0.0728  0.0715  0.0834  270  THR A N   
1846 C CA  . THR A 253 ? 0.9268 0.8115 0.7809 0.0838  0.0727  0.0959  270  THR A CA  
1847 C C   . THR A 253 ? 1.1364 1.0370 0.9685 0.0942  0.0817  0.1052  270  THR A C   
1848 O O   . THR A 253 ? 1.1967 1.1065 1.0133 0.1003  0.0798  0.0925  270  THR A O   
1849 C CB  . THR A 253 ? 1.0876 0.9628 0.9311 0.0917  0.0620  0.0830  270  THR A CB  
1850 O OG1 . THR A 253 ? 0.9378 0.7979 0.8006 0.0848  0.0556  0.0755  270  THR A OG1 
1851 C CG2 . THR A 253 ? 0.9252 0.7956 0.7504 0.1039  0.0620  0.0965  270  THR A CG2 
1852 N N   . LEU A 254 ? 1.2152 1.1183 1.0451 0.0966  0.0910  0.1274  271  LEU A N   
1853 C CA  . LEU A 254 ? 1.2781 1.1998 1.0903 0.1059  0.1032  0.1384  271  LEU A CA  
1854 C C   . LEU A 254 ? 1.2587 1.1804 1.0336 0.1229  0.1005  0.1335  271  LEU A C   
1855 O O   . LEU A 254 ? 1.2136 1.1492 0.9677 0.1332  0.1091  0.1362  271  LEU A O   
1856 C CB  . LEU A 254 ? 1.1973 1.1246 1.0206 0.1019  0.1150  0.1665  271  LEU A CB  
1857 C CG  . LEU A 254 ? 1.1636 1.0861 1.0251 0.0832  0.1145  0.1742  271  LEU A CG  
1858 C CD1 . LEU A 254 ? 1.2806 1.1778 1.1526 0.0775  0.1055  0.1808  271  LEU A CD1 
1859 C CD2 . LEU A 254 ? 1.3420 1.2864 1.2185 0.0782  0.1295  0.1976  271  LEU A CD2 
1860 N N   . ASP A 255 ? 1.2593 1.1663 1.0250 0.1268  0.0881  0.1261  272  ASP A N   
1861 C CA  . ASP A 255 ? 1.3272 1.2330 1.0584 0.1414  0.0821  0.1213  272  ASP A CA  
1862 C C   . ASP A 255 ? 1.3615 1.2629 1.0886 0.1420  0.0675  0.0977  272  ASP A C   
1863 O O   . ASP A 255 ? 1.4650 1.3642 1.1652 0.1524  0.0591  0.0918  272  ASP A O   
1864 C CB  . ASP A 255 ? 1.4678 1.3631 1.1900 0.1468  0.0791  0.1372  272  ASP A CB  
1865 C CG  . ASP A 255 ? 1.6523 1.5318 1.3993 0.1394  0.0689  0.1338  272  ASP A CG  
1866 O OD1 . ASP A 255 ? 1.6922 1.5643 1.4303 0.1459  0.0567  0.1268  272  ASP A OD1 
1867 O OD2 . ASP A 255 ? 1.6993 1.5740 1.4751 0.1275  0.0725  0.1376  272  ASP A OD2 
1868 N N   . ASP A 256 ? 1.2275 1.1281 0.9800 0.1305  0.0635  0.0851  273  ASP A N   
1869 C CA  . ASP A 256 ? 1.1428 1.0426 0.8950 0.1291  0.0506  0.0650  273  ASP A CA  
1870 C C   . ASP A 256 ? 1.1338 1.0428 0.8791 0.1287  0.0519  0.0541  273  ASP A C   
1871 O O   . ASP A 256 ? 1.1325 1.0481 0.8950 0.1208  0.0597  0.0548  273  ASP A O   
1872 C CB  . ASP A 256 ? 1.0688 0.9636 0.8499 0.1180  0.0461  0.0576  273  ASP A CB  
1873 C CG  . ASP A 256 ? 1.0521 0.9478 0.8331 0.1186  0.0328  0.0421  273  ASP A CG  
1874 O OD1 . ASP A 256 ? 1.0847 0.9746 0.8721 0.1214  0.0269  0.0428  273  ASP A OD1 
1875 O OD2 . ASP A 256 ? 1.0317 0.9347 0.8076 0.1165  0.0281  0.0302  273  ASP A OD2 
1876 N N   . TYR A 257 ? 1.0844 0.9926 0.8051 0.1372  0.0429  0.0444  274  TYR A N   
1877 C CA  . TYR A 257 ? 1.0769 0.9899 0.7899 0.1381  0.0419  0.0331  274  TYR A CA  
1878 C C   . TYR A 257 ? 1.0142 0.9303 0.7525 0.1246  0.0363  0.0213  274  TYR A C   
1879 O O   . TYR A 257 ? 1.0344 0.9560 0.7783 0.1214  0.0397  0.0166  274  TYR A O   
1880 C CB  . TYR A 257 ? 1.0646 0.9711 0.7451 0.1493  0.0299  0.0242  274  TYR A CB  
1881 C CG  . TYR A 257 ? 1.0044 0.9067 0.6897 0.1439  0.0118  0.0130  274  TYR A CG  
1882 C CD1 . TYR A 257 ? 0.9960 0.8990 0.6871 0.1373  0.0017  -0.0008 274  TYR A CD1 
1883 C CD2 . TYR A 257 ? 1.1019 1.0013 0.7878 0.1455  0.0048  0.0180  274  TYR A CD2 
1884 C CE1 . TYR A 257 ? 0.9931 0.8962 0.6913 0.1314  -0.0142 -0.0084 274  TYR A CE1 
1885 C CE2 . TYR A 257 ? 1.1636 1.0638 0.8574 0.1409  -0.0109 0.0095  274  TYR A CE2 
1886 C CZ  . TYR A 257 ? 0.9444 0.8476 0.6446 0.1334  -0.0199 -0.0031 274  TYR A CZ  
1887 O OH  . TYR A 257 ? 1.0569 0.9646 0.7675 0.1278  -0.0349 -0.0091 274  TYR A OH  
1888 N N   . ARG A 258 ? 0.9113 0.8251 0.6647 0.1174  0.0281  0.0168  275  ARG A N   
1889 C CA  . ARG A 258 ? 0.8894 0.8079 0.6653 0.1047  0.0242  0.0068  275  ARG A CA  
1890 C C   . ARG A 258 ? 0.9579 0.8794 0.7551 0.0957  0.0353  0.0120  275  ARG A C   
1891 O O   . ARG A 258 ? 0.9437 0.8709 0.7526 0.0871  0.0347  0.0055  275  ARG A O   
1892 C CB  . ARG A 258 ? 0.7422 0.6602 0.5289 0.1015  0.0155  0.0021  275  ARG A CB  
1893 C CG  . ARG A 258 ? 0.8405 0.7576 0.6109 0.1090  0.0029  -0.0009 275  ARG A CG  
1894 C CD  . ARG A 258 ? 0.8475 0.7668 0.6321 0.1085  -0.0023 -0.0012 275  ARG A CD  
1895 N NE  . ARG A 258 ? 1.0891 1.0005 0.8787 0.1130  0.0058  0.0095  275  ARG A NE  
1896 C CZ  . ARG A 258 ? 1.0881 0.9982 0.8931 0.1139  0.0044  0.0100  275  ARG A CZ  
1897 N NH1 . ARG A 258 ? 1.0163 0.9364 0.8336 0.1112  -0.0029 0.0008  275  ARG A NH1 
1898 N NH2 . ARG A 258 ? 1.0604 0.9596 0.8692 0.1180  0.0105  0.0205  275  ARG A NH2 
1899 N N   . SER A 259 ? 0.9583 0.8756 0.7611 0.0967  0.0439  0.0249  276  SER A N   
1900 C CA  . SER A 259 ? 0.8423 0.7613 0.6668 0.0867  0.0525  0.0316  276  SER A CA  
1901 C C   . SER A 259 ? 0.8104 0.7405 0.6343 0.0871  0.0603  0.0356  276  SER A C   
1902 O O   . SER A 259 ? 0.7905 0.7264 0.6327 0.0768  0.0614  0.0329  276  SER A O   
1903 C CB  . SER A 259 ? 0.9780 0.8885 0.8085 0.0875  0.0585  0.0468  276  SER A CB  
1904 O OG  . SER A 259 ? 0.9459 0.8589 0.7962 0.0778  0.0664  0.0565  276  SER A OG  
1905 N N   . ALA A 260 ? 0.7524 0.6862 0.5549 0.1000  0.0658  0.0418  277  ALA A N   
1906 C CA  . ALA A 260 ? 0.8465 0.7925 0.6478 0.1039  0.0748  0.0455  277  ALA A CA  
1907 C C   . ALA A 260 ? 0.8937 0.8423 0.6959 0.1014  0.0668  0.0301  277  ALA A C   
1908 O O   . ALA A 260 ? 0.9188 0.8777 0.7350 0.0978  0.0719  0.0317  277  ALA A O   
1909 C CB  . ALA A 260 ? 0.8953 0.8437 0.6678 0.1210  0.0822  0.0532  277  ALA A CB  
1910 N N   . GLU A 261 ? 0.8551 0.7954 0.6446 0.1026  0.0534  0.0167  278  GLU A N   
1911 C CA  . GLU A 261 ? 0.9334 0.8747 0.7243 0.0988  0.0440  0.0037  278  GLU A CA  
1912 C C   . GLU A 261 ? 0.8490 0.7945 0.6667 0.0821  0.0407  -0.0001 278  GLU A C   
1913 O O   . GLU A 261 ? 0.8030 0.7543 0.6302 0.0771  0.0390  -0.0039 278  GLU A O   
1914 C CB  . GLU A 261 ? 0.8816 0.8134 0.6523 0.1036  0.0296  -0.0072 278  GLU A CB  
1915 C CG  . GLU A 261 ? 0.9891 0.9195 0.7596 0.0997  0.0179  -0.0190 278  GLU A CG  
1916 C CD  . GLU A 261 ? 1.1068 1.0382 0.8698 0.1084  0.0227  -0.0199 278  GLU A CD  
1917 O OE1 . GLU A 261 ? 0.9031 0.8369 0.6781 0.1018  0.0176  -0.0252 278  GLU A OE1 
1918 O OE2 . GLU A 261 ? 1.1972 1.1279 0.9420 0.1228  0.0317  -0.0149 278  GLU A OE2 
1919 N N   . VAL A 262 ? 0.7328 0.6749 0.5615 0.0744  0.0393  0.0006  279  VAL A N   
1920 C CA  . VAL A 262 ? 0.7229 0.6678 0.5732 0.0597  0.0368  -0.0036 279  VAL A CA  
1921 C C   . VAL A 262 ? 0.8125 0.7636 0.6806 0.0533  0.0454  0.0054  279  VAL A C   
1922 O O   . VAL A 262 ? 0.7633 0.7203 0.6450 0.0434  0.0424  0.0017  279  VAL A O   
1923 C CB  . VAL A 262 ? 0.7422 0.6802 0.5981 0.0560  0.0342  -0.0058 279  VAL A CB  
1924 C CG1 . VAL A 262 ? 0.6383 0.5768 0.5134 0.0423  0.0334  -0.0098 279  VAL A CG1 
1925 C CG2 . VAL A 262 ? 0.8738 0.8114 0.7186 0.0599  0.0243  -0.0147 279  VAL A CG2 
1926 N N   . LEU A 263 ? 0.7493 0.7006 0.6184 0.0584  0.0557  0.0188  280  LEU A N   
1927 C CA  . LEU A 263 ? 0.7708 0.7312 0.6599 0.0519  0.0640  0.0303  280  LEU A CA  
1928 C C   . LEU A 263 ? 0.7942 0.7680 0.6843 0.0560  0.0666  0.0300  280  LEU A C   
1929 O O   . LEU A 263 ? 0.7588 0.7419 0.6699 0.0464  0.0669  0.0329  280  LEU A O   
1930 C CB  . LEU A 263 ? 0.7498 0.7101 0.6392 0.0571  0.0749  0.0475  280  LEU A CB  
1931 C CG  . LEU A 263 ? 0.8584 0.8265 0.7742 0.0466  0.0821  0.0630  280  LEU A CG  
1932 C CD1 . LEU A 263 ? 0.7007 0.6559 0.6343 0.0306  0.0736  0.0586  280  LEU A CD1 
1933 C CD2 . LEU A 263 ? 0.9342 0.9060 0.8469 0.0539  0.0940  0.0826  280  LEU A CD2 
1934 N N   . SER A 264 ? 0.7081 0.6819 0.5754 0.0709  0.0672  0.0262  281  SER A N   
1935 C CA  . SER A 264 ? 0.7512 0.7348 0.6175 0.0779  0.0691  0.0243  281  SER A CA  
1936 C C   . SER A 264 ? 0.7597 0.7425 0.6358 0.0676  0.0569  0.0127  281  SER A C   
1937 O O   . SER A 264 ? 0.6959 0.6896 0.5877 0.0650  0.0582  0.0152  281  SER A O   
1938 C CB  . SER A 264 ? 0.7710 0.7491 0.6061 0.0969  0.0700  0.0197  281  SER A CB  
1939 O OG  . SER A 264 ? 0.9079 0.8917 0.7402 0.1058  0.0707  0.0156  281  SER A OG  
1940 N N   . ARG A 265 ? 0.7490 0.7212 0.6173 0.0618  0.0450  0.0016  282  ARG A N   
1941 C CA  . ARG A 265 ? 0.6250 0.5980 0.5018 0.0508  0.0336  -0.0074 282  ARG A CA  
1942 C C   . ARG A 265 ? 0.6774 0.6579 0.5791 0.0353  0.0342  -0.0034 282  ARG A C   
1943 O O   . ARG A 265 ? 0.8209 0.8072 0.7333 0.0278  0.0282  -0.0059 282  ARG A O   
1944 C CB  . ARG A 265 ? 0.7683 0.7325 0.6334 0.0475  0.0225  -0.0174 282  ARG A CB  
1945 C CG  . ARG A 265 ? 0.7938 0.7496 0.6353 0.0601  0.0166  -0.0228 282  ARG A CG  
1946 C CD  . ARG A 265 ? 0.8126 0.7666 0.6515 0.0603  0.0067  -0.0291 282  ARG A CD  
1947 N NE  . ARG A 265 ? 0.9590 0.9026 0.7745 0.0758  0.0034  -0.0331 282  ARG A NE  
1948 C CZ  . ARG A 265 ? 1.0681 1.0032 0.8756 0.0783  -0.0086 -0.0404 282  ARG A CZ  
1949 N NH1 . ARG A 265 ? 0.9543 0.8924 0.7768 0.0655  -0.0178 -0.0424 282  ARG A NH1 
1950 N NH2 . ARG A 265 ? 1.0694 0.9916 0.8526 0.0936  -0.0123 -0.0455 282  ARG A NH2 
1951 N N   . MET A 266 ? 0.7849 0.7635 0.6955 0.0299  0.0400  0.0028  283  MET A N   
1952 C CA  . MET A 266 ? 0.7139 0.6968 0.6469 0.0149  0.0390  0.0064  283  MET A CA  
1953 C C   . MET A 266 ? 0.7240 0.7215 0.6751 0.0148  0.0452  0.0179  283  MET A C   
1954 O O   . MET A 266 ? 0.7555 0.7601 0.7238 0.0033  0.0398  0.0183  283  MET A O   
1955 C CB  . MET A 266 ? 0.7828 0.7560 0.7203 0.0101  0.0422  0.0103  283  MET A CB  
1956 C CG  . MET A 266 ? 0.6407 0.6019 0.5671 0.0083  0.0356  -0.0014 283  MET A CG  
1957 S SD  . MET A 266 ? 0.8062 0.7523 0.7396 0.0044  0.0385  0.0031  283  MET A SD  
1958 C CE  . MET A 266 ? 0.7156 0.6529 0.6377 0.0039  0.0305  -0.0137 283  MET A CE  
1959 N N   . ALA A 267 ? 0.7872 0.7912 0.7347 0.0279  0.0567  0.0280  284  ALA A N   
1960 C CA  . ALA A 267 ? 0.7832 0.8056 0.7508 0.0294  0.0651  0.0411  284  ALA A CA  
1961 C C   . ALA A 267 ? 0.6991 0.7302 0.6713 0.0319  0.0597  0.0359  284  ALA A C   
1962 O O   . ALA A 267 ? 0.7539 0.8006 0.7508 0.0259  0.0608  0.0443  284  ALA A O   
1963 C CB  . ALA A 267 ? 0.8299 0.8594 0.7882 0.0456  0.0801  0.0526  284  ALA A CB  
1964 N N   . PHE A 268 ? 0.7873 0.8085 0.7379 0.0402  0.0526  0.0231  285  PHE A N   
1965 C CA  . PHE A 268 ? 0.7939 0.8192 0.7470 0.0438  0.0459  0.0180  285  PHE A CA  
1966 C C   . PHE A 268 ? 0.7069 0.7255 0.6626 0.0287  0.0302  0.0086  285  PHE A C   
1967 O O   . PHE A 268 ? 0.7919 0.8129 0.7518 0.0290  0.0224  0.0056  285  PHE A O   
1968 C CB  . PHE A 268 ? 0.8638 0.8807 0.7909 0.0638  0.0471  0.0110  285  PHE A CB  
1969 C CG  . PHE A 268 ? 1.0052 1.0312 0.9263 0.0811  0.0636  0.0203  285  PHE A CG  
1970 C CD1 . PHE A 268 ? 0.9445 0.9923 0.8896 0.0835  0.0752  0.0339  285  PHE A CD1 
1971 C CD2 . PHE A 268 ? 1.0173 1.0321 0.9093 0.0946  0.0676  0.0166  285  PHE A CD2 
1972 C CE1 . PHE A 268 ? 0.9169 0.9772 0.8568 0.0997  0.0922  0.0442  285  PHE A CE1 
1973 C CE2 . PHE A 268 ? 1.1241 1.1488 1.0076 0.1110  0.0836  0.0259  285  PHE A CE2 
1974 C CZ  . PHE A 268 ? 0.9853 1.0336 0.8927 0.1138  0.0968  0.0400  285  PHE A CZ  
1975 N N   . ALA A 269 ? 0.6518 0.6626 0.6046 0.0164  0.0256  0.0042  286  ALA A N   
1976 C CA  . ALA A 269 ? 0.6762 0.6844 0.6317 0.0012  0.0129  -0.0032 286  ALA A CA  
1977 C C   . ALA A 269 ? 0.7329 0.7390 0.6966 -0.0121 0.0135  -0.0024 286  ALA A C   
1978 O O   . ALA A 269 ? 0.7085 0.7052 0.6603 -0.0150 0.0111  -0.0100 286  ALA A O   
1979 C CB  . ALA A 269 ? 0.5883 0.5861 0.5229 0.0038  0.0045  -0.0139 286  ALA A CB  
1980 N N   . PRO A 270 ? 0.6859 0.7005 0.6711 -0.0200 0.0161  0.0067  287  PRO A N   
1981 C CA  . PRO A 270 ? 0.5832 0.5912 0.5755 -0.0317 0.0159  0.0076  287  PRO A CA  
1982 C C   . PRO A 270 ? 0.7373 0.7372 0.7215 -0.0438 0.0051  -0.0046 287  PRO A C   
1983 O O   . PRO A 270 ? 0.7568 0.7450 0.7362 -0.0477 0.0053  -0.0093 287  PRO A O   
1984 C CB  . PRO A 270 ? 0.6131 0.6339 0.6328 -0.0394 0.0173  0.0208  287  PRO A CB  
1985 C CG  . PRO A 270 ? 0.7016 0.7373 0.7269 -0.0258 0.0247  0.0289  287  PRO A CG  
1986 C CD  . PRO A 270 ? 0.6533 0.6837 0.6586 -0.0181 0.0187  0.0173  287  PRO A CD  
1987 N N   . HIS A 271 ? 0.6855 0.6914 0.6674 -0.0490 -0.0040 -0.0094 288  HIS A N   
1988 C CA  . HIS A 271 ? 0.6098 0.6115 0.5820 -0.0600 -0.0130 -0.0198 288  HIS A CA  
1989 C C   . HIS A 271 ? 0.6158 0.6139 0.5680 -0.0537 -0.0136 -0.0288 288  HIS A C   
1990 O O   . HIS A 271 ? 0.7644 0.7623 0.7072 -0.0610 -0.0190 -0.0370 288  HIS A O   
1991 C CB  . HIS A 271 ? 0.5732 0.5851 0.5540 -0.0712 -0.0235 -0.0180 288  HIS A CB  
1992 C CG  . HIS A 271 ? 0.7234 0.7394 0.7246 -0.0816 -0.0265 -0.0105 288  HIS A CG  
1993 N ND1 . HIS A 271 ? 0.7470 0.7558 0.7475 -0.0950 -0.0332 -0.0158 288  HIS A ND1 
1994 C CD2 . HIS A 271 ? 0.6552 0.6826 0.6791 -0.0807 -0.0243 0.0021  288  HIS A CD2 
1995 C CE1 . HIS A 271 ? 0.7611 0.7754 0.7836 -0.1036 -0.0368 -0.0062 288  HIS A CE1 
1996 N NE2 . HIS A 271 ? 0.7683 0.7961 0.8071 -0.0952 -0.0308 0.0057  288  HIS A NE2 
1997 N N   . GLY A 272 ? 0.6339 0.6303 0.5792 -0.0404 -0.0083 -0.0271 289  GLY A N   
1998 C CA  . GLY A 272 ? 0.8016 0.7952 0.7308 -0.0348 -0.0100 -0.0339 289  GLY A CA  
1999 C C   . GLY A 272 ? 0.8084 0.8092 0.7331 -0.0426 -0.0203 -0.0374 289  GLY A C   
2000 O O   . GLY A 272 ? 0.8283 0.8349 0.7606 -0.0488 -0.0267 -0.0337 289  GLY A O   
2001 N N   . GLU A 273 ? 1.0451 0.9241 1.0853 0.0378  0.1622  -0.1134 290  GLU A N   
2002 C CA  . GLU A 273 ? 1.0627 0.9424 1.1407 0.0102  0.1399  -0.0774 290  GLU A CA  
2003 C C   . GLU A 273 ? 1.0221 0.9418 1.1174 0.0118  0.1684  -0.0522 290  GLU A C   
2004 O O   . GLU A 273 ? 0.9761 0.9399 1.0625 0.0282  0.2062  -0.0530 290  GLU A O   
2005 C CB  . GLU A 273 ? 1.0695 0.9764 1.1760 -0.0169 0.1215  -0.0493 290  GLU A CB  
2006 C CG  . GLU A 273 ? 1.1242 0.9810 1.2257 -0.0282 0.0801  -0.0643 290  GLU A CG  
2007 C CD  . GLU A 273 ? 1.1732 0.9664 1.2740 -0.0328 0.0486  -0.0737 290  GLU A CD  
2008 O OE1 . GLU A 273 ? 1.2089 0.9488 1.2818 -0.0212 0.0306  -0.1085 290  GLU A OE1 
2009 O OE2 . GLU A 273 ? 1.3634 1.1599 1.4915 -0.0476 0.0421  -0.0465 290  GLU A OE2 
2010 N N   . ASP A 274 ? 1.0515 0.9548 1.1717 -0.0052 0.1495  -0.0300 291  ASP A N   
2011 C CA  . ASP A 274 ? 1.0186 0.9575 1.1595 -0.0075 0.1715  -0.0021 291  ASP A CA  
2012 C C   . ASP A 274 ? 0.9974 0.9924 1.1766 -0.0324 0.1735  0.0422  291  ASP A C   
2013 O O   . ASP A 274 ? 1.0173 1.0147 1.2117 -0.0520 0.1504  0.0539  291  ASP A O   
2014 C CB  . ASP A 274 ? 1.0516 0.9448 1.2002 -0.0130 0.1507  0.0001  291  ASP A CB  
2015 C CG  . ASP A 274 ? 1.2733 1.1262 1.4408 -0.0387 0.1045  0.0098  291  ASP A CG  
2016 O OD1 . ASP A 274 ? 1.3384 1.1494 1.4865 -0.0358 0.0818  -0.0173 291  ASP A OD1 
2017 O OD2 . ASP A 274 ? 1.3052 1.1689 1.5075 -0.0617 0.0910  0.0447  291  ASP A OD2 
2018 N N   . HIS A 275 ? 0.9478 0.9886 1.1428 -0.0312 0.2016  0.0670  292  HIS A N   
2019 C CA  . HIS A 275 ? 0.9259 1.0210 1.1587 -0.0541 0.2055  0.1114  292  HIS A CA  
2020 C C   . HIS A 275 ? 1.0145 1.1005 1.2771 -0.0719 0.1904  0.1407  292  HIS A C   
2021 O O   . HIS A 275 ? 1.1561 1.2869 1.4398 -0.0763 0.2114  0.1705  292  HIS A O   
2022 C CB  . HIS A 275 ? 0.8648 1.0248 1.0948 -0.0403 0.2498  0.1203  292  HIS A CB  
2023 C CG  . HIS A 275 ? 0.8464 1.0186 1.0479 -0.0226 0.2666  0.0928  292  HIS A CG  
2024 N ND1 . HIS A 275 ? 0.8314 1.0433 1.0436 -0.0336 0.2691  0.1067  292  HIS A ND1 
2025 C CD2 . HIS A 275 ? 0.8410 0.9908 1.0038 0.0054  0.2816  0.0523  292  HIS A CD2 
2026 C CE1 . HIS A 275 ? 0.8173 1.0309 0.9985 -0.0131 0.2851  0.0759  292  HIS A CE1 
2027 N NE2 . HIS A 275 ? 0.8228 0.9991 0.9738 0.0108  0.2930  0.0427  292  HIS A NE2 
2028 N N   . ASP A 276 ? 1.2028 1.2307 1.4673 -0.0820 0.1538  0.1323  293  ASP A N   
2029 C CA  . ASP A 276 ? 1.2405 1.2507 1.5290 -0.0961 0.1380  0.1546  293  ASP A CA  
2030 C C   . ASP A 276 ? 1.3200 1.3663 1.6526 -0.1269 0.1255  0.2014  293  ASP A C   
2031 O O   . ASP A 276 ? 1.0998 1.1601 1.4451 -0.1428 0.1111  0.2120  293  ASP A O   
2032 C CB  . ASP A 276 ? 1.4497 1.3858 1.7267 -0.0981 0.1012  0.1308  293  ASP A CB  
2033 C CG  . ASP A 276 ? 1.5857 1.4998 1.8864 -0.1122 0.0838  0.1520  293  ASP A CG  
2034 O OD1 . ASP A 276 ? 1.3360 1.2868 1.6532 -0.1126 0.1060  0.1770  293  ASP A OD1 
2035 O OD2 . ASP A 276 ? 1.8215 1.6815 2.1243 -0.1228 0.0475  0.1438  293  ASP A OD2 
2036 N N   . ILE A 277 ? 1.7324 1.7938 2.0885 -0.1349 0.1313  0.2295  294  ILE A N   
2037 C CA  . ILE A 277 ? 1.8073 1.8930 2.2068 -0.1649 0.1149  0.2743  294  ILE A CA  
2038 C C   . ILE A 277 ? 1.8497 1.8755 2.2595 -0.1794 0.0748  0.2734  294  ILE A C   
2039 O O   . ILE A 277 ? 1.8306 1.8380 2.2451 -0.1774 0.0742  0.2783  294  ILE A O   
2040 C CB  . ILE A 277 ? 1.7688 1.9088 2.1885 -0.1651 0.1453  0.3068  294  ILE A CB  
2041 C CG1 . ILE A 277 ? 1.7259 1.8516 2.1218 -0.1397 0.1687  0.2865  294  ILE A CG1 
2042 C CG2 . ILE A 277 ? 1.5029 1.7090 1.9268 -0.1631 0.1748  0.3213  294  ILE A CG2 
2043 C CD1 . ILE A 277 ? 1.5891 1.7651 2.0031 -0.1385 0.1985  0.3168  294  ILE A CD1 
2044 N N   . GLU A 278 ? 1.6138 1.6082 2.0270 -0.1940 0.0405  0.2668  295  GLU A N   
2045 C CA  . GLU A 278 ? 1.6651 1.5970 2.0836 -0.2061 0.0003  0.2601  295  GLU A CA  
2046 C C   . GLU A 278 ? 1.9464 1.8845 2.4066 -0.2319 -0.0172 0.3012  295  GLU A C   
2047 O O   . GLU A 278 ? 1.9333 1.8226 2.4030 -0.2461 -0.0539 0.3000  295  GLU A O   
2048 C CB  . GLU A 278 ? 1.6911 1.5912 2.1032 -0.2153 -0.0314 0.2433  295  GLU A CB  
2049 C CG  . GLU A 278 ? 1.5550 1.4162 1.9219 -0.1896 -0.0287 0.1939  295  GLU A CG  
2050 C CD  . GLU A 278 ? 1.6214 1.5125 1.9737 -0.1827 -0.0150 0.1824  295  GLU A CD  
2051 O OE1 . GLU A 278 ? 1.5779 1.4533 1.8925 -0.1577 -0.0007 0.1449  295  GLU A OE1 
2052 O OE2 . GLU A 278 ? 1.4622 1.3926 1.8411 -0.2023 -0.0186 0.2111  295  GLU A OE2 
2053 N N   . LYS A 279 ? 1.9173 1.9109 2.4026 -0.2388 0.0059  0.3371  296  LYS A N   
2054 C CA  . LYS A 279 ? 2.0663 2.0612 2.5873 -0.2594 -0.0081 0.3728  296  LYS A CA  
2055 C C   . LYS A 279 ? 2.2532 2.2021 2.7597 -0.2467 -0.0114 0.3552  296  LYS A C   
2056 O O   . LYS A 279 ? 2.2754 2.2127 2.7479 -0.2198 0.0106  0.3239  296  LYS A O   
2057 C CB  . LYS A 279 ? 2.0139 2.0790 2.5605 -0.2654 0.0217  0.4121  296  LYS A CB  
2058 C CG  . LYS A 279 ? 2.0191 2.1052 2.6126 -0.2977 0.0007  0.4582  296  LYS A CG  
2059 C CD  . LYS A 279 ? 1.9989 2.0520 2.6113 -0.3087 -0.0195 0.4728  296  LYS A CD  
2060 C CE  . LYS A 279 ? 1.8466 1.9454 2.4795 -0.3093 0.0072  0.5060  296  LYS A CE  
2061 N NZ  . LYS A 279 ? 1.5847 1.7285 2.2609 -0.3365 0.0012  0.5534  296  LYS A NZ  
2062 N N   . ASN A 280 ? 2.4485 2.3701 2.9811 -0.2664 -0.0401 0.3752  297  ASN A N   
2063 C CA  . ASN A 280 ? 2.5002 2.3719 3.0232 -0.2589 -0.0508 0.3609  297  ASN A CA  
2064 C C   . ASN A 280 ? 2.5307 2.3368 3.0212 -0.2473 -0.0735 0.3166  297  ASN A C   
2065 O O   . ASN A 280 ? 2.4995 2.2532 2.9936 -0.2550 -0.1037 0.3107  297  ASN A O   
2066 C CB  . ASN A 280 ? 2.4625 2.3573 2.9711 -0.2364 -0.0122 0.3574  297  ASN A CB  
2067 C CG  . ASN A 280 ? 2.4393 2.3978 2.9791 -0.2467 0.0107  0.4009  297  ASN A CG  
2068 O OD1 . ASN A 280 ? 2.3972 2.4080 2.9440 -0.2489 0.0298  0.4154  297  ASN A OD1 
2069 N ND2 . ASN A 280 ? 2.4097 2.3642 2.9679 -0.2528 0.0092  0.4218  297  ASN A ND2 
2070 N N   . ALA A 281 ? 2.1286 1.9371 2.5872 -0.2286 -0.0591 0.2855  298  ALA A N   
2071 C CA  . ALA A 281 ? 1.9660 1.7163 2.3916 -0.2162 -0.0786 0.2424  298  ALA A CA  
2072 C C   . ALA A 281 ? 1.8595 1.5596 2.2628 -0.1991 -0.0805 0.2165  298  ALA A C   
2073 O O   . ALA A 281 ? 1.9585 1.5990 2.3483 -0.1989 -0.1102 0.1923  298  ALA A O   
2074 C CB  . ALA A 281 ? 2.0555 1.7734 2.4976 -0.2401 -0.1225 0.2470  298  ALA A CB  
2075 N N   . ILE A 282 ? 1.6803 1.4039 2.0794 -0.1845 -0.0492 0.2214  299  ILE A N   
2076 C CA  . ILE A 282 ? 1.5298 1.2114 1.9064 -0.1659 -0.0457 0.1968  299  ILE A CA  
2077 C C   . ILE A 282 ? 1.3596 1.0514 1.6969 -0.1340 -0.0110 0.1630  299  ILE A C   
2078 O O   . ILE A 282 ? 1.4237 1.1626 1.7599 -0.1220 0.0256  0.1725  299  ILE A O   
2079 C CB  . ILE A 282 ? 1.5839 1.2803 1.9852 -0.1731 -0.0379 0.2269  299  ILE A CB  
2080 C CG1 . ILE A 282 ? 1.2701 0.9333 1.6444 -0.1491 -0.0249 0.2000  299  ILE A CG1 
2081 C CG2 . ILE A 282 ? 1.7022 1.4726 2.1259 -0.1780 -0.0066 0.2622  299  ILE A CG2 
2082 C CD1 . ILE A 282 ? 1.2562 0.9349 1.6521 -0.1536 -0.0144 0.2276  299  ILE A CD1 
2083 N N   . SER A 283 ? 1.2902 0.9382 1.5951 -0.1200 -0.0223 0.1232  300  SER A N   
2084 C CA  . SER A 283 ? 1.2446 0.8980 1.5108 -0.0896 0.0080  0.0884  300  SER A CA  
2085 C C   . SER A 283 ? 1.2514 0.8650 1.4941 -0.0686 0.0149  0.0631  300  SER A C   
2086 O O   . SER A 283 ? 1.2895 0.8448 1.5096 -0.0605 -0.0059 0.0317  300  SER A O   
2087 C CB  . SER A 283 ? 1.2655 0.8961 1.5092 -0.0850 -0.0064 0.0596  300  SER A CB  
2088 O OG  . SER A 283 ? 1.4127 1.0874 1.6753 -0.1008 -0.0060 0.0817  300  SER A OG  
2089 N N   . ALA A 284 ? 0.9317 0.9450 0.6927 0.0415  0.0269  -0.0125 301  ALA A N   
2090 C CA  . ALA A 284 ? 1.0205 1.0250 0.7815 0.0496  0.0158  -0.0200 301  ALA A CA  
2091 C C   . ALA A 284 ? 1.0627 1.0737 0.8427 0.0575  0.0063  -0.0336 301  ALA A C   
2092 O O   . ALA A 284 ? 1.1530 1.1679 0.9249 0.0630  0.0064  -0.0392 301  ALA A O   
2093 C CB  . ALA A 284 ? 0.9612 0.9533 0.6876 0.0555  0.0128  -0.0179 301  ALA A CB  
2094 N N   . MET A 285 ? 0.8424 0.8543 0.6473 0.0582  -0.0020 -0.0385 302  MET A N   
2095 C CA  . MET A 285 ? 0.8879 0.9035 0.7140 0.0628  -0.0140 -0.0507 302  MET A CA  
2096 C C   . MET A 285 ? 0.9018 0.9183 0.7453 0.0658  -0.0260 -0.0543 302  MET A C   
2097 O O   . MET A 285 ? 0.8660 0.8821 0.7081 0.0652  -0.0225 -0.0471 302  MET A O   
2098 C CB  . MET A 285 ? 0.9377 0.9602 0.7915 0.0556  -0.0097 -0.0504 302  MET A CB  
2099 C CG  . MET A 285 ? 0.9960 1.0240 0.8769 0.0469  -0.0045 -0.0422 302  MET A CG  
2100 S SD  . MET A 285 ? 1.0426 1.0752 0.9442 0.0383  0.0045  -0.0378 302  MET A SD  
2101 C CE  . MET A 285 ? 0.9608 0.9928 0.8343 0.0350  0.0186  -0.0278 302  MET A CE  
2102 N N   . ARG A 286 ? 0.9106 0.9283 0.7708 0.0696  -0.0412 -0.0657 303  ARG A N   
2103 C CA  . ARG A 286 ? 0.8177 0.8409 0.7001 0.0721  -0.0554 -0.0698 303  ARG A CA  
2104 C C   . ARG A 286 ? 0.8214 0.8554 0.7489 0.0630  -0.0594 -0.0703 303  ARG A C   
2105 O O   . ARG A 286 ? 0.8152 0.8441 0.7501 0.0606  -0.0653 -0.0774 303  ARG A O   
2106 C CB  . ARG A 286 ? 0.8156 0.8296 0.6788 0.0834  -0.0738 -0.0824 303  ARG A CB  
2107 C CG  . ARG A 286 ? 0.8976 0.9027 0.7231 0.0931  -0.0734 -0.0799 303  ARG A CG  
2108 C CD  . ARG A 286 ? 0.7922 0.7885 0.5802 0.0931  -0.0569 -0.0727 303  ARG A CD  
2109 N NE  . ARG A 286 ? 0.9503 0.9404 0.7180 0.0990  -0.0588 -0.0809 303  ARG A NE  
2110 C CZ  . ARG A 286 ? 0.9906 0.9799 0.7346 0.0983  -0.0439 -0.0749 303  ARG A CZ  
2111 N NH1 . ARG A 286 ? 0.9721 0.9645 0.7111 0.0896  -0.0282 -0.0609 303  ARG A NH1 
2112 N NH2 . ARG A 286 ? 1.1704 1.1561 0.8961 0.1070  -0.0453 -0.0829 303  ARG A NH2 
2113 N N   . ILE A 287 ? 0.7756 0.8237 0.7318 0.0586  -0.0558 -0.0621 304  ILE A N   
2114 C CA  . ILE A 287 ? 0.7455 0.8068 0.7472 0.0487  -0.0577 -0.0591 304  ILE A CA  
2115 C C   . ILE A 287 ? 0.7282 0.7970 0.7559 0.0499  -0.0797 -0.0676 304  ILE A C   
2116 O O   . ILE A 287 ? 0.8074 0.8887 0.8450 0.0552  -0.0848 -0.0656 304  ILE A O   
2117 C CB  . ILE A 287 ? 0.7381 0.8132 0.7575 0.0448  -0.0413 -0.0448 304  ILE A CB  
2118 C CG1 . ILE A 287 ? 0.6555 0.7201 0.6471 0.0430  -0.0229 -0.0373 304  ILE A CG1 
2119 C CG2 . ILE A 287 ? 0.6697 0.7603 0.7366 0.0343  -0.0418 -0.0395 304  ILE A CG2 
2120 C CD1 . ILE A 287 ? 0.5791 0.6370 0.5730 0.0355  -0.0191 -0.0384 304  ILE A CD1 
2121 N N   . VAL A 288 ? 0.8762 0.9365 0.9149 0.0456  -0.0943 -0.0773 305  VAL A N   
2122 C CA  . VAL A 288 ? 0.7652 0.8294 0.8284 0.0451  -0.1192 -0.0863 305  VAL A CA  
2123 C C   . VAL A 288 ? 0.7364 0.8264 0.8555 0.0334  -0.1197 -0.0759 305  VAL A C   
2124 O O   . VAL A 288 ? 0.7336 0.8403 0.8778 0.0346  -0.1336 -0.0767 305  VAL A O   
2125 C CB  . VAL A 288 ? 0.7906 0.8320 0.8435 0.0447  -0.1364 -0.1007 305  VAL A CB  
2126 C CG1 . VAL A 288 ? 0.7834 0.8255 0.8621 0.0424  -0.1657 -0.1106 305  VAL A CG1 
2127 C CG2 . VAL A 288 ? 0.7338 0.7546 0.7309 0.0590  -0.1336 -0.1096 305  VAL A CG2 
2128 N N   . GLY A 289 ? 0.6881 0.7834 0.8280 0.0224  -0.1042 -0.0649 306  GLY A N   
2129 C CA  . GLY A 289 ? 0.7122 0.8345 0.9035 0.0118  -0.0999 -0.0518 306  GLY A CA  
2130 C C   . GLY A 289 ? 0.6519 0.7714 0.8721 -0.0039 -0.0972 -0.0455 306  GLY A C   
2131 O O   . GLY A 289 ? 0.7329 0.8271 0.9338 -0.0060 -0.1014 -0.0532 306  GLY A O   
2132 N N   . LYS A 290 ? 0.6347 0.7804 0.9007 -0.0139 -0.0896 -0.0306 307  LYS A N   
2133 C CA  . LYS A 290 ? 0.6698 0.8135 0.9657 -0.0300 -0.0863 -0.0216 307  LYS A CA  
2134 C C   . LYS A 290 ? 0.6465 0.7802 0.9689 -0.0417 -0.1150 -0.0308 307  LYS A C   
2135 O O   . LYS A 290 ? 0.7172 0.8667 1.0658 -0.0432 -0.1337 -0.0346 307  LYS A O   
2136 C CB  . LYS A 290 ? 0.6037 0.7806 0.9391 -0.0362 -0.0675 -0.0008 307  LYS A CB  
2137 C CG  . LYS A 290 ? 0.8585 1.0308 1.2119 -0.0501 -0.0552 0.0124  307  LYS A CG  
2138 C CD  . LYS A 290 ? 0.8314 1.0263 1.1911 -0.0466 -0.0265 0.0313  307  LYS A CD  
2139 C CE  . LYS A 290 ? 0.9612 1.1469 1.3293 -0.0582 -0.0129 0.0445  307  LYS A CE  
2140 N NZ  . LYS A 290 ? 0.6888 0.8894 1.0496 -0.0511 0.0156  0.0609  307  LYS A NZ  
2141 N N   . VAL A 291 ? 0.7643 0.8696 1.0784 -0.0492 -0.1203 -0.0351 308  VAL A N   
2142 C CA  . VAL A 291 ? 0.7546 0.8394 1.0840 -0.0590 -0.1496 -0.0462 308  VAL A CA  
2143 C C   . VAL A 291 ? 0.7550 0.8287 1.1101 -0.0764 -0.1470 -0.0354 308  VAL A C   
2144 O O   . VAL A 291 ? 0.7656 0.8370 1.1096 -0.0762 -0.1237 -0.0246 308  VAL A O   
2145 C CB  . VAL A 291 ? 0.6780 0.7266 0.9556 -0.0448 -0.1651 -0.0685 308  VAL A CB  
2146 C CG1 . VAL A 291 ? 0.6769 0.7343 0.9286 -0.0286 -0.1693 -0.0781 308  VAL A CG1 
2147 C CG2 . VAL A 291 ? 0.6921 0.7196 0.9304 -0.0373 -0.1462 -0.0689 308  VAL A CG2 
2148 N N   . THR A 292 ? 0.8114 0.8762 1.2002 -0.0918 -0.1727 -0.0380 309  THR A N   
2149 C CA  . THR A 292 ? 0.8179 0.8631 1.2279 -0.1094 -0.1765 -0.0298 309  THR A CA  
2150 C C   . THR A 292 ? 0.8931 0.8937 1.2851 -0.1104 -0.2094 -0.0501 309  THR A C   
2151 O O   . THR A 292 ? 0.9058 0.8988 1.2844 -0.1022 -0.2322 -0.0675 309  THR A O   
2152 C CB  . THR A 292 ? 0.7549 0.8329 1.2317 -0.1319 -0.1755 -0.0083 309  THR A CB  
2153 O OG1 . THR A 292 ? 0.8723 0.9636 1.3821 -0.1394 -0.2039 -0.0149 309  THR A OG1 
2154 C CG2 . THR A 292 ? 0.7561 0.8771 1.2466 -0.1275 -0.1420 0.0115  309  THR A CG2 
2155 N N   . GLY A 293 ? 0.9195 0.8877 1.3082 -0.1189 -0.2123 -0.0481 310  GLY A N   
2156 C CA  . GLY A 293 ? 0.8789 0.7983 1.2437 -0.1170 -0.2426 -0.0680 310  GLY A CA  
2157 C C   . GLY A 293 ? 0.9570 0.8491 1.3467 -0.1374 -0.2529 -0.0589 310  GLY A C   
2158 O O   . GLY A 293 ? 0.8779 0.7882 1.2990 -0.1519 -0.2331 -0.0362 310  GLY A O   
2159 N N   . LYS A 294 ? 1.0759 0.9206 1.4477 -0.1373 -0.2849 -0.0771 311  LYS A N   
2160 C CA  . LYS A 294 ? 0.9221 0.7293 1.3109 -0.1559 -0.3014 -0.0719 311  LYS A CA  
2161 C C   . LYS A 294 ? 0.9913 0.7548 1.3266 -0.1380 -0.2948 -0.0820 311  LYS A C   
2162 O O   . LYS A 294 ? 1.0059 0.7377 1.2924 -0.1164 -0.3089 -0.1058 311  LYS A O   
2163 C CB  . LYS A 294 ? 1.0214 0.8001 1.4264 -0.1686 -0.3455 -0.0856 311  LYS A CB  
2164 C CG  . LYS A 294 ? 1.0291 0.8524 1.4948 -0.1888 -0.3558 -0.0743 311  LYS A CG  
2165 C CD  . LYS A 294 ? 1.0092 0.8014 1.4819 -0.1973 -0.4032 -0.0924 311  LYS A CD  
2166 C CE  . LYS A 294 ? 0.9983 0.8378 1.5392 -0.2199 -0.4157 -0.0793 311  LYS A CE  
2167 N NZ  . LYS A 294 ? 1.1568 0.9668 1.7022 -0.2269 -0.4647 -0.0987 311  LYS A NZ  
2168 N N   . ALA A 295 ? 1.0133 0.7763 1.3573 -0.1455 -0.2732 -0.0635 312  ALA A N   
2169 C CA  . ALA A 295 ? 1.0588 0.7832 1.3580 -0.1297 -0.2665 -0.0701 312  ALA A CA  
2170 C C   . ALA A 295 ? 1.1184 0.8143 1.4417 -0.1508 -0.2719 -0.0542 312  ALA A C   
2171 O O   . ALA A 295 ? 0.9581 0.6818 1.3127 -0.1653 -0.2481 -0.0289 312  ALA A O   
2172 C CB  . ALA A 295 ? 0.9917 0.7459 1.2659 -0.1115 -0.2298 -0.0638 312  ALA A CB  
2173 N N   . PRO A 296 ? 1.2191 0.8574 1.5265 -0.1527 -0.3027 -0.0674 313  PRO A N   
2174 C CA  . PRO A 296 ? 1.2338 0.8328 1.4990 -0.1335 -0.3319 -0.0978 313  PRO A CA  
2175 C C   . PRO A 296 ? 1.1920 0.8019 1.4816 -0.1442 -0.3589 -0.1070 313  PRO A C   
2176 O O   . PRO A 296 ? 1.1094 0.7522 1.4556 -0.1706 -0.3597 -0.0889 313  PRO A O   
2177 C CB  . PRO A 296 ? 1.1838 0.7162 1.4322 -0.1370 -0.3556 -0.1034 313  PRO A CB  
2178 C CG  . PRO A 296 ? 1.1322 0.6720 1.4352 -0.1709 -0.3522 -0.0751 313  PRO A CG  
2179 C CD  . PRO A 296 ? 1.0656 0.6690 1.3927 -0.1734 -0.3108 -0.0523 313  PRO A CD  
2180 N N   . SER A 297 ? 1.2041 0.7880 1.4506 -0.1226 -0.3804 -0.1345 314  SER A N   
2181 C CA  . SER A 297 ? 1.2968 0.8894 1.5592 -0.1288 -0.4075 -0.1458 314  SER A CA  
2182 C C   . SER A 297 ? 1.2892 0.8504 1.5903 -0.1582 -0.4461 -0.1438 314  SER A C   
2183 O O   . SER A 297 ? 1.3050 0.8830 1.6360 -0.1707 -0.4684 -0.1470 314  SER A O   
2184 C CB  . SER A 297 ? 1.3396 0.9064 1.5389 -0.0962 -0.4211 -0.1759 314  SER A CB  
2185 O OG  . SER A 297 ? 1.4267 0.9294 1.5796 -0.0811 -0.4393 -0.1932 314  SER A OG  
2186 N N   . THR A 298 ? 1.3149 0.8307 1.6167 -0.1698 -0.4559 -0.1383 315  THR A N   
2187 C CA  . THR A 298 ? 1.4663 0.9523 1.8098 -0.2023 -0.4915 -0.1322 315  THR A CA  
2188 C C   . THR A 298 ? 1.3751 0.9116 1.7948 -0.2376 -0.4744 -0.0976 315  THR A C   
2189 O O   . THR A 298 ? 1.4235 0.9438 1.8879 -0.2692 -0.5009 -0.0873 315  THR A O   
2190 C CB  . THR A 298 ? 1.3941 0.8037 1.7031 -0.1999 -0.5114 -0.1407 315  THR A CB  
2191 O OG1 . THR A 298 ? 1.3158 0.7320 1.6214 -0.1975 -0.4765 -0.1219 315  THR A OG1 
2192 C CG2 . THR A 298 ? 1.3666 0.7251 1.5996 -0.1630 -0.5302 -0.1756 315  THR A CG2 
2193 N N   . GLU A 299 ? 1.2885 0.8845 1.7230 -0.2328 -0.4313 -0.0793 316  GLU A N   
2194 C CA  . GLU A 299 ? 1.2659 0.9144 1.7685 -0.2616 -0.4111 -0.0464 316  GLU A CA  
2195 C C   . GLU A 299 ? 1.2309 0.9213 1.7864 -0.2789 -0.4293 -0.0436 316  GLU A C   
2196 O O   . GLU A 299 ? 1.2328 0.9269 1.7674 -0.2627 -0.4455 -0.0655 316  GLU A O   
2197 C CB  . GLU A 299 ? 1.1979 0.8950 1.6934 -0.2470 -0.3619 -0.0309 316  GLU A CB  
2198 C CG  . GLU A 299 ? 1.2208 0.9544 1.7693 -0.2716 -0.3354 0.0046  316  GLU A CG  
2199 C CD  . GLU A 299 ? 1.3773 1.0715 1.9044 -0.2730 -0.3233 0.0153  316  GLU A CD  
2200 O OE1 . GLU A 299 ? 1.4917 1.1283 1.9676 -0.2567 -0.3393 -0.0051 316  GLU A OE1 
2201 O OE2 . GLU A 299 ? 1.4835 1.2043 2.0430 -0.2885 -0.2975 0.0443  316  GLU A OE2 
2202 N N   . SER A 300 ? 1.1064 0.8306 1.7319 -0.3119 -0.4260 -0.0151 317  SER A N   
2203 C CA  . SER A 300 ? 1.2378 1.0091 1.9240 -0.3309 -0.4420 -0.0082 317  SER A CA  
2204 C C   . SER A 300 ? 1.1088 0.9576 1.8187 -0.3211 -0.4050 0.0058  317  SER A C   
2205 O O   . SER A 300 ? 1.0916 0.9847 1.8466 -0.3302 -0.4161 0.0091  317  SER A O   
2206 C CB  . SER A 300 ? 1.1282 0.9006 1.8841 -0.3730 -0.4589 0.0170  317  SER A CB  
2207 O OG  . SER A 300 ? 1.2547 1.0520 2.0353 -0.3847 -0.4210 0.0486  317  SER A OG  
2208 N N   . SER A 301 ? 1.0306 0.8954 1.7103 -0.3020 -0.3633 0.0136  318  SER A N   
2209 C CA  . SER A 301 ? 1.0963 1.0279 1.7918 -0.2909 -0.3279 0.0264  318  SER A CA  
2210 C C   . SER A 301 ? 1.0714 0.9941 1.6995 -0.2575 -0.3003 0.0137  318  SER A C   
2211 O O   . SER A 301 ? 1.1456 1.0184 1.7239 -0.2458 -0.3021 0.0015  318  SER A O   
2212 C CB  . SER A 301 ? 0.9448 0.9219 1.6984 -0.3129 -0.2993 0.0630  318  SER A CB  
2213 O OG  . SER A 301 ? 1.1865 1.1767 2.0083 -0.3462 -0.3239 0.0777  318  SER A OG  
2214 N N   . ASP A 302 ? 0.9462 0.9184 1.5741 -0.2421 -0.2754 0.0172  319  ASP A N   
2215 C CA  . ASP A 302 ? 0.9973 0.9665 1.5667 -0.2132 -0.2486 0.0079  319  ASP A CA  
2216 C C   . ASP A 302 ? 0.9784 0.9442 1.5391 -0.2144 -0.2169 0.0268  319  ASP A C   
2217 O O   . ASP A 302 ? 0.8928 0.8890 1.4975 -0.2314 -0.1991 0.0532  319  ASP A O   
2218 C CB  . ASP A 302 ? 0.8737 0.8937 1.4465 -0.1983 -0.2318 0.0085  319  ASP A CB  
2219 C CG  . ASP A 302 ? 0.9208 0.9333 1.4742 -0.1857 -0.2595 -0.0165 319  ASP A CG  
2220 O OD1 . ASP A 302 ? 0.9538 0.9192 1.4826 -0.1849 -0.2897 -0.0362 319  ASP A OD1 
2221 O OD2 . ASP A 302 ? 1.0136 1.0647 1.5731 -0.1752 -0.2515 -0.0165 319  ASP A OD2 
2222 N N   . THR A 303 ? 0.8293 0.7590 1.3324 -0.1953 -0.2097 0.0137  320  THR A N   
2223 C CA  . THR A 303 ? 0.8139 0.7339 1.3016 -0.1939 -0.1834 0.0285  320  THR A CA  
2224 C C   . THR A 303 ? 0.9256 0.8580 1.3682 -0.1688 -0.1549 0.0245  320  THR A C   
2225 O O   . THR A 303 ? 0.9151 0.8502 1.3498 -0.1675 -0.1300 0.0397  320  THR A O   
2226 C CB  . THR A 303 ? 0.9252 0.7850 1.3889 -0.1969 -0.2023 0.0201  320  THR A CB  
2227 O OG1 . THR A 303 ? 0.8739 0.7002 1.2910 -0.1769 -0.2232 -0.0095 320  THR A OG1 
2228 C CG2 . THR A 303 ? 0.9459 0.7902 1.4575 -0.2269 -0.2265 0.0312  320  THR A CG2 
2229 N N   . VAL A 304 ? 0.7626 0.7014 1.1752 -0.1495 -0.1587 0.0053  321  VAL A N   
2230 C CA  . VAL A 304 ? 0.8299 0.7783 1.1997 -0.1274 -0.1346 0.0011  321  VAL A CA  
2231 C C   . VAL A 304 ? 0.7771 0.7604 1.1477 -0.1177 -0.1313 -0.0044 321  VAL A C   
2232 O O   . VAL A 304 ? 0.7340 0.7190 1.1173 -0.1199 -0.1546 -0.0157 321  VAL A O   
2233 C CB  . VAL A 304 ? 0.7514 0.6589 1.0686 -0.1096 -0.1429 -0.0190 321  VAL A CB  
2234 C CG1 . VAL A 304 ? 0.7783 0.6649 1.0805 -0.1026 -0.1729 -0.0427 321  VAL A CG1 
2235 C CG2 . VAL A 304 ? 0.7788 0.6993 1.0573 -0.0900 -0.1176 -0.0202 321  VAL A CG2 
2236 N N   . GLN A 305 ? 0.7288 0.7375 1.0846 -0.1068 -0.1039 0.0039  322  GLN A N   
2237 C CA  . GLN A 305 ? 0.7926 0.8300 1.1420 -0.0952 -0.0987 -0.0007 322  GLN A CA  
2238 C C   . GLN A 305 ? 0.7307 0.7610 1.0281 -0.0754 -0.0830 -0.0087 322  GLN A C   
2239 O O   . GLN A 305 ? 0.7701 0.7793 1.0417 -0.0711 -0.0747 -0.0090 322  GLN A O   
2240 C CB  . GLN A 305 ? 0.6332 0.7134 1.0219 -0.1024 -0.0810 0.0198  322  GLN A CB  
2241 C CG  . GLN A 305 ? 0.6137 0.7037 0.9893 -0.0978 -0.0497 0.0361  322  GLN A CG  
2242 C CD  . GLN A 305 ? 0.6369 0.7684 1.0486 -0.1018 -0.0318 0.0561  322  GLN A CD  
2243 O OE1 . GLN A 305 ? 0.7768 0.9298 1.2375 -0.1159 -0.0405 0.0650  322  GLN A OE1 
2244 N NE2 . GLN A 305 ? 0.7049 0.8481 1.0925 -0.0890 -0.0071 0.0634  322  GLN A NE2 
2245 N N   . GLY A 306 ? 0.7696 0.8180 1.0529 -0.0638 -0.0799 -0.0144 323  GLY A N   
2246 C CA  . GLY A 306 ? 0.6268 0.6702 0.8635 -0.0473 -0.0662 -0.0205 323  GLY A CA  
2247 C C   . GLY A 306 ? 0.6849 0.7456 0.9101 -0.0367 -0.0672 -0.0263 323  GLY A C   
2248 O O   . GLY A 306 ? 0.7338 0.8154 0.9893 -0.0409 -0.0749 -0.0235 323  GLY A O   
2249 N N   . ILE A 307 ? 0.6722 0.7248 0.8541 -0.0230 -0.0597 -0.0337 324  ILE A N   
2250 C CA  . ILE A 307 ? 0.7356 0.7985 0.8978 -0.0117 -0.0600 -0.0391 324  ILE A CA  
2251 C C   . ILE A 307 ? 0.7231 0.7652 0.8503 -0.0012 -0.0745 -0.0570 324  ILE A C   
2252 O O   . ILE A 307 ? 0.6931 0.7198 0.7908 0.0046  -0.0683 -0.0610 324  ILE A O   
2253 C CB  . ILE A 307 ? 0.5770 0.6486 0.7165 -0.0054 -0.0368 -0.0293 324  ILE A CB  
2254 C CG1 . ILE A 307 ? 0.5599 0.6509 0.7292 -0.0125 -0.0216 -0.0119 324  ILE A CG1 
2255 C CG2 . ILE A 307 ? 0.5743 0.6503 0.6890 0.0063  -0.0388 -0.0351 324  ILE A CG2 
2256 C CD1 . ILE A 307 ? 0.5595 0.6752 0.7651 -0.0148 -0.0281 -0.0076 324  ILE A CD1 
2257 N N   . ALA A 308 ? 0.6736 0.7165 0.8041 0.0025  -0.0937 -0.0673 325  ALA A N   
2258 C CA  . ALA A 308 ? 0.6958 0.7194 0.7882 0.0153  -0.1069 -0.0840 325  ALA A CA  
2259 C C   . ALA A 308 ? 0.8895 0.9186 0.9455 0.0274  -0.0937 -0.0828 325  ALA A C   
2260 O O   . ALA A 308 ? 0.7501 0.7966 0.8140 0.0278  -0.0872 -0.0749 325  ALA A O   
2261 C CB  . ALA A 308 ? 0.7212 0.7406 0.8282 0.0150  -0.1349 -0.0958 325  ALA A CB  
2262 N N   . PHE A 309 ? 0.8604 0.8746 0.8764 0.0375  -0.0895 -0.0898 326  PHE A N   
2263 C CA  . PHE A 309 ? 0.7243 0.7419 0.7051 0.0465  -0.0761 -0.0866 326  PHE A CA  
2264 C C   . PHE A 309 ? 0.8702 0.8722 0.8113 0.0605  -0.0848 -0.0998 326  PHE A C   
2265 O O   . PHE A 309 ? 0.7818 0.7684 0.7189 0.0648  -0.0991 -0.1120 326  PHE A O   
2266 C CB  . PHE A 309 ? 0.6917 0.7140 0.6653 0.0425  -0.0534 -0.0745 326  PHE A CB  
2267 C CG  . PHE A 309 ? 0.7453 0.7568 0.7044 0.0456  -0.0500 -0.0789 326  PHE A CG  
2268 C CD1 . PHE A 309 ? 0.7847 0.7898 0.7668 0.0391  -0.0536 -0.0794 326  PHE A CD1 
2269 C CD2 . PHE A 309 ? 0.7486 0.7572 0.6714 0.0556  -0.0427 -0.0813 326  PHE A CD2 
2270 C CE1 . PHE A 309 ? 0.6767 0.6713 0.6444 0.0446  -0.0510 -0.0837 326  PHE A CE1 
2271 C CE2 . PHE A 309 ? 0.8122 0.8151 0.7237 0.0608  -0.0387 -0.0849 326  PHE A CE2 
2272 C CZ  . PHE A 309 ? 0.6476 0.6426 0.5806 0.0563  -0.0433 -0.0868 326  PHE A CZ  
2273 N N   . SER A 310 ? 0.8384 0.8426 0.7476 0.0683  -0.0758 -0.0968 327  SER A N   
2274 C CA  . SER A 310 ? 0.7892 0.7815 0.6562 0.0824  -0.0786 -0.1057 327  SER A CA  
2275 C C   . SER A 310 ? 0.9276 0.9264 0.7688 0.0834  -0.0569 -0.0945 327  SER A C   
2276 O O   . SER A 310 ? 0.9046 0.9103 0.7442 0.0790  -0.0485 -0.0841 327  SER A O   
2277 C CB  . SER A 310 ? 0.7852 0.7713 0.6373 0.0915  -0.0958 -0.1141 327  SER A CB  
2278 O OG  . SER A 310 ? 1.1452 1.1196 0.9518 0.1063  -0.0958 -0.1208 327  SER A OG  
2279 N N   . GLY A 311 ? 0.8954 0.8920 0.7170 0.0895  -0.0488 -0.0962 328  GLY A N   
2280 C CA  . GLY A 311 ? 0.8710 0.8771 0.6729 0.0884  -0.0290 -0.0843 328  GLY A CA  
2281 C C   . GLY A 311 ? 0.8091 0.8186 0.6040 0.0939  -0.0206 -0.0859 328  GLY A C   
2282 O O   . GLY A 311 ? 1.0593 1.0588 0.8532 0.1030  -0.0310 -0.0985 328  GLY A O   
2283 N N   . ASN A 312 ? 0.9565 0.9797 0.7465 0.0888  -0.0029 -0.0731 329  ASN A N   
2284 C CA  . ASN A 312 ? 0.8575 0.8897 0.6448 0.0944  0.0065  -0.0726 329  ASN A CA  
2285 C C   . ASN A 312 ? 0.9252 0.9559 0.7437 0.0878  0.0040  -0.0738 329  ASN A C   
2286 O O   . ASN A 312 ? 0.8361 0.8652 0.6785 0.0750  0.0020  -0.0687 329  ASN A O   
2287 C CB  . ASN A 312 ? 0.9455 0.9960 0.7229 0.0888  0.0246  -0.0569 329  ASN A CB  
2288 C CG  . ASN A 312 ? 0.9746 1.0276 0.7175 0.0977  0.0297  -0.0547 329  ASN A CG  
2289 O OD1 . ASN A 312 ? 1.1866 1.2262 0.9096 0.1097  0.0193  -0.0655 329  ASN A OD1 
2290 N ND2 . ASN A 312 ? 0.9613 1.0310 0.6967 0.0914  0.0449  -0.0397 329  ASN A ND2 
2291 N N   . PRO A 313 ? 0.8803 0.9106 0.6973 0.0977  0.0045  -0.0800 330  PRO A N   
2292 C CA  . PRO A 313 ? 0.8670 0.8934 0.7108 0.0919  0.0024  -0.0799 330  PRO A CA  
2293 C C   . PRO A 313 ? 0.8114 0.8534 0.6712 0.0779  0.0161  -0.0639 330  PRO A C   
2294 O O   . PRO A 313 ? 0.8045 0.8638 0.6543 0.0780  0.0288  -0.0548 330  PRO A O   
2295 C CB  . PRO A 313 ? 0.7351 0.7587 0.5654 0.1093  0.0020  -0.0891 330  PRO A CB  
2296 C CG  . PRO A 313 ? 0.7954 0.8132 0.5932 0.1252  -0.0026 -0.0992 330  PRO A CG  
2297 C CD  . PRO A 313 ? 0.9526 0.9830 0.7409 0.1172  0.0057  -0.0885 330  PRO A CD  
2298 N N   . LEU A 314 ? 0.8140 0.8498 0.6989 0.0658  0.0128  -0.0600 331  LEU A N   
2299 C CA  . LEU A 314 ? 0.6999 0.7455 0.5966 0.0533  0.0237  -0.0457 331  LEU A CA  
2300 C C   . LEU A 314 ? 0.8015 0.8420 0.7187 0.0500  0.0231  -0.0439 331  LEU A C   
2301 O O   . LEU A 314 ? 0.7750 0.8247 0.6915 0.0522  0.0301  -0.0392 331  LEU A O   
2302 C CB  . LEU A 314 ? 0.7043 0.7475 0.6053 0.0431  0.0234  -0.0397 331  LEU A CB  
2303 C CG  . LEU A 314 ? 0.8052 0.8549 0.7070 0.0324  0.0340  -0.0257 331  LEU A CG  
2304 C CD1 . LEU A 314 ? 0.8691 0.9315 0.7533 0.0330  0.0426  -0.0195 331  LEU A CD1 
2305 C CD2 . LEU A 314 ? 0.7323 0.7769 0.6321 0.0270  0.0331  -0.0219 331  LEU A CD2 
2306 N N   . TYR A 315 ? 0.7802 0.8074 0.7165 0.0446  0.0147  -0.0464 332  TYR A N   
2307 C CA  . TYR A 315 ? 0.6224 0.6423 0.5773 0.0399  0.0147  -0.0423 332  TYR A CA  
2308 C C   . TYR A 315 ? 0.7807 0.7839 0.7382 0.0486  0.0028  -0.0541 332  TYR A C   
2309 O O   . TYR A 315 ? 0.7675 0.7628 0.7136 0.0576  -0.0072 -0.0664 332  TYR A O   
2310 C CB  . TYR A 315 ? 0.6322 0.6489 0.6079 0.0272  0.0151  -0.0342 332  TYR A CB  
2311 C CG  . TYR A 315 ? 0.6896 0.7171 0.6596 0.0205  0.0265  -0.0226 332  TYR A CG  
2312 C CD1 . TYR A 315 ? 0.6649 0.6967 0.6290 0.0192  0.0263  -0.0224 332  TYR A CD1 
2313 C CD2 . TYR A 315 ? 0.6472 0.6779 0.6153 0.0167  0.0356  -0.0125 332  TYR A CD2 
2314 C CE1 . TYR A 315 ? 0.7532 0.7894 0.7080 0.0145  0.0352  -0.0127 332  TYR A CE1 
2315 C CE2 . TYR A 315 ? 0.8762 0.9114 0.8351 0.0111  0.0436  -0.0031 332  TYR A CE2 
2316 C CZ  . TYR A 315 ? 0.7330 0.7697 0.6845 0.0102  0.0434  -0.0034 332  TYR A CZ  
2317 O OH  . TYR A 315 ? 0.8500 0.8861 0.7885 0.0061  0.0498  0.0052  332  TYR A OH  
2318 N N   . THR A 316 ? 0.8067 0.8011 0.7762 0.0465  0.0029  -0.0502 333  THR A N   
2319 C CA  . THR A 316 ? 0.7036 0.6762 0.6745 0.0541  -0.0095 -0.0605 333  THR A CA  
2320 C C   . THR A 316 ? 0.7730 0.7285 0.7572 0.0477  -0.0250 -0.0675 333  THR A C   
2321 O O   . THR A 316 ? 0.7424 0.7036 0.7459 0.0342  -0.0240 -0.0597 333  THR A O   
2322 C CB  . THR A 316 ? 0.6343 0.5985 0.6162 0.0511  -0.0065 -0.0524 333  THR A CB  
2323 O OG1 . THR A 316 ? 1.0466 0.9831 1.0317 0.0557  -0.0209 -0.0614 333  THR A OG1 
2324 C CG2 . THR A 316 ? 0.8211 0.7894 0.8226 0.0343  0.0006  -0.0377 333  THR A CG2 
2325 N N   . SER A 317 ? 0.7921 0.7270 0.7657 0.0584  -0.0402 -0.0823 334  SER A N   
2326 C CA  . SER A 317 ? 0.7437 0.6603 0.7284 0.0529  -0.0592 -0.0910 334  SER A CA  
2327 C C   . SER A 317 ? 0.8240 0.7103 0.8212 0.0492  -0.0737 -0.0943 334  SER A C   
2328 O O   . SER A 317 ? 0.7921 0.6571 0.7949 0.0465  -0.0938 -0.1042 334  SER A O   
2329 C CB  . SER A 317 ? 0.7511 0.6626 0.7090 0.0678  -0.0694 -0.1071 334  SER A CB  
2330 O OG  . SER A 317 ? 0.8561 0.7930 0.8012 0.0702  -0.0564 -0.1028 334  SER A OG  
2331 N N   . THR A 318 ? 0.7207 0.6024 0.7216 0.0487  -0.0654 -0.0858 335  THR A N   
2332 C CA  . THR A 318 ? 0.8583 0.7074 0.8670 0.0463  -0.0786 -0.0877 335  THR A CA  
2333 C C   . THR A 318 ? 0.8263 0.6792 0.8618 0.0288  -0.0690 -0.0687 335  THR A C   
2334 O O   . THR A 318 ? 0.9176 0.7945 0.9545 0.0263  -0.0503 -0.0563 335  THR A O   
2335 C CB  . THR A 318 ? 0.8216 0.6547 0.8026 0.0679  -0.0800 -0.0973 335  THR A CB  
2336 O OG1 . THR A 318 ? 0.9030 0.7614 0.8795 0.0727  -0.0597 -0.0866 335  THR A OG1 
2337 C CG2 . THR A 318 ? 0.8310 0.6594 0.7820 0.0878  -0.0884 -0.1159 335  THR A CG2 
2338 N N   . GLY A 319 ? 0.8954 0.7226 0.9505 0.0165  -0.0825 -0.0661 336  GLY A N   
2339 C CA  . GLY A 319 ? 0.8417 0.6702 0.9214 -0.0001 -0.0732 -0.0468 336  GLY A CA  
2340 C C   . GLY A 319 ? 0.7798 0.5744 0.8781 -0.0127 -0.0913 -0.0453 336  GLY A C   
2341 O O   . GLY A 319 ? 0.8262 0.5935 0.9175 -0.0087 -0.1131 -0.0606 336  GLY A O   
2342 N N   . VAL A 320 ? 0.7922 0.5868 0.9127 -0.0283 -0.0825 -0.0261 337  VAL A N   
2343 C CA  . VAL A 320 ? 0.8213 0.5865 0.9649 -0.0450 -0.0970 -0.0191 337  VAL A CA  
2344 C C   . VAL A 320 ? 0.7879 0.5792 0.9709 -0.0673 -0.0874 0.0003  337  VAL A C   
2345 O O   . VAL A 320 ? 0.7774 0.6013 0.9637 -0.0677 -0.0654 0.0124  337  VAL A O   
2346 C CB  . VAL A 320 ? 0.8571 0.5914 0.9884 -0.0415 -0.0958 -0.0119 337  VAL A CB  
2347 C CG1 . VAL A 320 ? 0.8472 0.5639 0.9400 -0.0157 -0.1013 -0.0297 337  VAL A CG1 
2348 C CG2 . VAL A 320 ? 0.8550 0.6113 0.9924 -0.0468 -0.0710 0.0096  337  VAL A CG2 
2349 N N   . LEU A 321 ? 0.8156 0.5925 1.0284 -0.0855 -0.1048 0.0032  338  LEU A N   
2350 C CA  . LEU A 321 ? 0.8189 0.6217 1.0741 -0.1074 -0.0952 0.0246  338  LEU A CA  
2351 C C   . LEU A 321 ? 0.9244 0.7233 1.1837 -0.1143 -0.0768 0.0471  338  LEU A C   
2352 O O   . LEU A 321 ? 1.0144 0.7758 1.2601 -0.1133 -0.0840 0.0481  338  LEU A O   
2353 C CB  . LEU A 321 ? 0.8662 0.6544 1.1561 -0.1274 -0.1202 0.0240  338  LEU A CB  
2354 C CG  . LEU A 321 ? 0.9477 0.7563 1.2528 -0.1291 -0.1347 0.0112  338  LEU A CG  
2355 C CD1 . LEU A 321 ? 1.1019 0.8734 1.3776 -0.1164 -0.1625 -0.0156 338  LEU A CD1 
2356 C CD2 . LEU A 321 ? 0.8756 0.7010 1.2359 -0.1558 -0.1426 0.0271  338  LEU A CD2 
2357 N N   . THR A 322 ? 0.8470 0.6828 1.1217 -0.1194 -0.0530 0.0650  339  THR A N   
2358 C CA  . THR A 322 ? 0.8619 0.6963 1.1401 -0.1258 -0.0342 0.0882  339  THR A CA  
2359 C C   . THR A 322 ? 0.8627 0.6868 1.1803 -0.1504 -0.0402 0.1070  339  THR A C   
2360 O O   . THR A 322 ? 0.9465 0.7652 1.2670 -0.1571 -0.0254 0.1281  339  THR A O   
2361 C CB  . THR A 322 ? 0.7767 0.6517 1.0535 -0.1206 -0.0068 0.1003  339  THR A CB  
2362 O OG1 . THR A 322 ? 0.8040 0.7122 1.1208 -0.1342 -0.0028 0.1106  339  THR A OG1 
2363 C CG2 . THR A 322 ? 0.7120 0.5994 0.9554 -0.1002 -0.0034 0.0823  339  THR A CG2 
2364 N N   . ALA A 323 ? 0.8981 0.7187 1.2455 -0.1645 -0.0622 0.1007  340  ALA A N   
2365 C CA  . ALA A 323 ? 0.9313 0.7490 1.3241 -0.1915 -0.0688 0.1204  340  ALA A CA  
2366 C C   . ALA A 323 ? 0.9917 0.7532 1.3772 -0.2003 -0.0891 0.1203  340  ALA A C   
2367 O O   . ALA A 323 ? 1.0879 0.8401 1.4968 -0.2194 -0.0843 0.1439  340  ALA A O   
2368 C CB  . ALA A 323 ? 0.8390 0.6810 1.2714 -0.2043 -0.0854 0.1146  340  ALA A CB  
2369 N N   . LYS A 324 ? 0.9600 0.6829 1.3122 -0.1860 -0.1115 0.0950  341  LYS A N   
2370 C CA  . LYS A 324 ? 1.1529 0.8168 1.4943 -0.1917 -0.1352 0.0912  341  LYS A CA  
2371 C C   . LYS A 324 ? 1.2019 0.8364 1.4954 -0.1694 -0.1271 0.0863  341  LYS A C   
2372 O O   . LYS A 324 ? 1.1917 0.8389 1.4521 -0.1448 -0.1189 0.0703  341  LYS A O   
2373 C CB  . LYS A 324 ? 1.2152 0.8509 1.5515 -0.1897 -0.1698 0.0649  341  LYS A CB  
2374 C CG  . LYS A 324 ? 1.1928 0.8561 1.5761 -0.2106 -0.1829 0.0669  341  LYS A CG  
2375 C CD  . LYS A 324 ? 1.2001 0.8567 1.6322 -0.2443 -0.1893 0.0926  341  LYS A CD  
2376 C CE  . LYS A 324 ? 1.2444 0.9247 1.7254 -0.2654 -0.2089 0.0922  341  LYS A CE  
2377 N NZ  . LYS A 324 ? 1.1527 0.7924 1.6139 -0.2591 -0.2473 0.0622  341  LYS A NZ  
2378 N N   . ASP A 325 ? 1.1457 0.7415 1.4367 -0.1786 -0.1301 0.1012  342  ASP A N   
2379 C CA  . ASP A 325 ? 1.1765 0.7392 1.4227 -0.1570 -0.1271 0.0958  342  ASP A CA  
2380 C C   . ASP A 325 ? 1.2284 0.7452 1.4422 -0.1394 -0.1554 0.0674  342  ASP A C   
2381 O O   . ASP A 325 ? 1.3504 0.8579 1.5247 -0.1124 -0.1517 0.0540  342  ASP A O   
2382 C CB  . ASP A 325 ? 1.2955 0.8301 1.5465 -0.1710 -0.1205 0.1220  342  ASP A CB  
2383 C CG  . ASP A 325 ? 1.3098 0.8104 1.5930 -0.2000 -0.1427 0.1326  342  ASP A CG  
2384 O OD1 . ASP A 325 ? 1.4640 0.9465 1.7547 -0.2044 -0.1702 0.1140  342  ASP A OD1 
2385 O OD2 . ASP A 325 ? 1.4567 0.9483 1.7574 -0.2190 -0.1331 0.1604  342  ASP A OD2 
2386 N N   . ASP A 326 ? 1.3476 0.8358 1.5770 -0.1532 -0.1839 0.0582  343  ASP A N   
2387 C CA  . ASP A 326 ? 1.3576 0.8095 1.5539 -0.1331 -0.2101 0.0276  343  ASP A CA  
2388 C C   . ASP A 326 ? 1.4878 0.9854 1.6742 -0.1149 -0.2008 0.0098  343  ASP A C   
2389 O O   . ASP A 326 ? 1.5835 1.1156 1.8007 -0.1290 -0.2009 0.0113  343  ASP A O   
2390 C CB  . ASP A 326 ? 1.6999 1.1089 1.9143 -0.1534 -0.2452 0.0216  343  ASP A CB  
2391 C CG  . ASP A 326 ? 1.6000 1.0492 1.8670 -0.1814 -0.2467 0.0322  343  ASP A CG  
2392 O OD1 . ASP A 326 ? 1.4652 0.9275 1.7330 -0.1762 -0.2607 0.0126  343  ASP A OD1 
2393 O OD2 . ASP A 326 ? 1.6012 1.0704 1.9082 -0.2073 -0.2333 0.0606  343  ASP A OD2 
2394 N N   . PRO A 327 ? 1.5677 1.0689 1.7137 -0.0844 -0.1922 -0.0055 344  PRO A N   
2395 C CA  . PRO A 327 ? 1.1029 0.6543 1.2420 -0.0698 -0.1765 -0.0157 344  PRO A CA  
2396 C C   . PRO A 327 ? 1.0819 0.6334 1.2230 -0.0691 -0.1971 -0.0360 344  PRO A C   
2397 O O   . PRO A 327 ? 1.1107 0.6202 1.2265 -0.0566 -0.2219 -0.0565 344  PRO A O   
2398 C CB  . PRO A 327 ? 1.0793 0.6256 1.1753 -0.0384 -0.1676 -0.0271 344  PRO A CB  
2399 C CG  . PRO A 327 ? 1.2672 0.7517 1.3414 -0.0309 -0.1893 -0.0344 344  PRO A CG  
2400 C CD  . PRO A 327 ? 1.3802 0.8404 1.4862 -0.0614 -0.1970 -0.0137 344  PRO A CD  
2401 N N   . VAL A 328 ? 1.1588 0.7562 1.3279 -0.0810 -0.1875 -0.0303 345  VAL A N   
2402 C CA  . VAL A 328 ? 1.1117 0.7170 1.2833 -0.0796 -0.2046 -0.0480 345  VAL A CA  
2403 C C   . VAL A 328 ? 1.0240 0.6659 1.1692 -0.0562 -0.1865 -0.0588 345  VAL A C   
2404 O O   . VAL A 328 ? 0.9986 0.6867 1.1596 -0.0609 -0.1641 -0.0469 345  VAL A O   
2405 C CB  . VAL A 328 ? 1.0748 0.7063 1.2973 -0.1084 -0.2084 -0.0341 345  VAL A CB  
2406 C CG1 . VAL A 328 ? 1.1094 0.7372 1.3327 -0.1073 -0.2339 -0.0542 345  VAL A CG1 
2407 C CG2 . VAL A 328 ? 1.0081 0.6130 1.2624 -0.1349 -0.2177 -0.0151 345  VAL A CG2 
2408 N N   . TYR A 329 ? 1.0010 0.6210 1.1045 -0.0305 -0.1960 -0.0809 346  TYR A N   
2409 C CA  . TYR A 329 ? 0.9518 0.6042 1.0286 -0.0081 -0.1791 -0.0901 346  TYR A CA  
2410 C C   . TYR A 329 ? 1.0207 0.6933 1.1012 -0.0087 -0.1872 -0.1012 346  TYR A C   
2411 O O   . TYR A 329 ? 1.0088 0.6526 1.0853 -0.0095 -0.2141 -0.1160 346  TYR A O   
2412 C CB  . TYR A 329 ? 0.9989 0.6237 1.0307 0.0213  -0.1837 -0.1072 346  TYR A CB  
2413 C CG  . TYR A 329 ? 1.0899 0.7002 1.1155 0.0259  -0.1737 -0.0963 346  TYR A CG  
2414 C CD1 . TYR A 329 ? 1.0839 0.7304 1.1085 0.0312  -0.1466 -0.0837 346  TYR A CD1 
2415 C CD2 . TYR A 329 ? 1.0483 0.6062 1.0676 0.0247  -0.1930 -0.0986 346  TYR A CD2 
2416 C CE1 . TYR A 329 ? 1.0662 0.6996 1.0843 0.0361  -0.1390 -0.0738 346  TYR A CE1 
2417 C CE2 . TYR A 329 ? 1.1487 0.6917 1.1604 0.0301  -0.1845 -0.0882 346  TYR A CE2 
2418 C CZ  . TYR A 329 ? 1.0333 0.6155 1.0448 0.0362  -0.1574 -0.0759 346  TYR A CZ  
2419 O OH  . TYR A 329 ? 1.1891 0.7564 1.1921 0.0424  -0.1505 -0.0658 346  TYR A OH  
2420 N N   . VAL A 330 ? 0.8798 0.5990 0.9659 -0.0080 -0.1656 -0.0941 347  VAL A N   
2421 C CA  . VAL A 330 ? 0.9116 0.6535 1.0014 -0.0083 -0.1705 -0.1019 347  VAL A CA  
2422 C C   . VAL A 330 ? 0.9941 0.7568 1.0479 0.0151  -0.1556 -0.1111 347  VAL A C   
2423 O O   . VAL A 330 ? 0.8153 0.6029 0.8644 0.0194  -0.1315 -0.1004 347  VAL A O   
2424 C CB  . VAL A 330 ? 0.9016 0.6806 1.0341 -0.0305 -0.1592 -0.0832 347  VAL A CB  
2425 C CG1 . VAL A 330 ? 0.8675 0.6630 1.0065 -0.0316 -0.1710 -0.0925 347  VAL A CG1 
2426 C CG2 . VAL A 330 ? 0.8447 0.6098 1.0153 -0.0544 -0.1666 -0.0681 347  VAL A CG2 
2427 N N   . TRP A 331 ? 1.0510 0.8027 1.0792 0.0297  -0.1706 -0.1303 348  TRP A N   
2428 C CA  . TRP A 331 ? 0.8567 0.6296 0.8520 0.0504  -0.1577 -0.1383 348  TRP A CA  
2429 C C   . TRP A 331 ? 0.9426 0.7356 0.9462 0.0445  -0.1630 -0.1408 348  TRP A C   
2430 O O   . TRP A 331 ? 0.9541 0.7257 0.9517 0.0463  -0.1874 -0.1552 348  TRP A O   
2431 C CB  . TRP A 331 ? 0.9031 0.6455 0.8549 0.0767  -0.1690 -0.1583 348  TRP A CB  
2432 C CG  . TRP A 331 ? 0.8936 0.6569 0.8113 0.0980  -0.1574 -0.1663 348  TRP A CG  
2433 C CD1 . TRP A 331 ? 0.9305 0.7345 0.8477 0.0991  -0.1319 -0.1548 348  TRP A CD1 
2434 C CD2 . TRP A 331 ? 1.0872 0.8297 0.9643 0.1213  -0.1712 -0.1869 348  TRP A CD2 
2435 N NE1 . TRP A 331 ? 0.9343 0.7461 0.8158 0.1200  -0.1280 -0.1654 348  TRP A NE1 
2436 C CE2 . TRP A 331 ? 0.9605 0.7359 0.8159 0.1351  -0.1508 -0.1851 348  TRP A CE2 
2437 C CE3 . TRP A 331 ? 1.0192 0.7161 0.8740 0.1322  -0.1994 -0.2065 348  TRP A CE3 
2438 C CZ2 . TRP A 331 ? 0.9622 0.7293 0.7746 0.1600  -0.1554 -0.2009 348  TRP A CZ2 
2439 C CZ3 . TRP A 331 ? 1.1359 0.8221 0.9452 0.1586  -0.2053 -0.2242 348  TRP A CZ3 
2440 C CH2 . TRP A 331 ? 1.2035 0.9261 0.9921 0.1726  -0.1822 -0.2207 348  TRP A CH2 
2441 N N   . ALA A 332 ? 0.8805 0.7122 0.8963 0.0382  -0.1417 -0.1273 349  ALA A N   
2442 C CA  . ALA A 332 ? 0.8169 0.6700 0.8444 0.0317  -0.1447 -0.1265 349  ALA A CA  
2443 C C   . ALA A 332 ? 0.8324 0.7069 0.8282 0.0474  -0.1290 -0.1289 349  ALA A C   
2444 O O   . ALA A 332 ? 0.8919 0.7949 0.8948 0.0425  -0.1081 -0.1151 349  ALA A O   
2445 C CB  . ALA A 332 ? 0.8347 0.7125 0.9062 0.0098  -0.1350 -0.1073 349  ALA A CB  
2446 N N   . PRO A 333 ? 0.9211 0.7810 0.8799 0.0666  -0.1386 -0.1456 350  PRO A N   
2447 C CA  . PRO A 333 ? 0.8576 0.7380 0.7866 0.0802  -0.1240 -0.1461 350  PRO A CA  
2448 C C   . PRO A 333 ? 0.8024 0.7008 0.7429 0.0720  -0.1264 -0.1424 350  PRO A C   
2449 O O   . PRO A 333 ? 0.9026 0.7900 0.8550 0.0672  -0.1482 -0.1502 350  PRO A O   
2450 C CB  . PRO A 333 ? 0.9765 0.8322 0.8632 0.1035  -0.1364 -0.1653 350  PRO A CB  
2451 C CG  . PRO A 333 ? 0.8956 0.7165 0.7923 0.0990  -0.1655 -0.1777 350  PRO A CG  
2452 C CD  . PRO A 333 ? 0.8793 0.7006 0.8183 0.0778  -0.1634 -0.1643 350  PRO A CD  
2453 N N   . GLY A 334 ? 0.9182 0.8436 0.8552 0.0707  -0.1053 -0.1303 351  GLY A N   
2454 C CA  . GLY A 334 ? 0.7807 0.7227 0.7262 0.0649  -0.1056 -0.1255 351  GLY A CA  
2455 C C   . GLY A 334 ? 0.8087 0.7650 0.7985 0.0459  -0.1044 -0.1129 351  GLY A C   
2456 O O   . GLY A 334 ? 0.8327 0.8031 0.8330 0.0424  -0.1068 -0.1096 351  GLY A O   
2457 N N   . ILE A 335 ? 0.7768 0.7302 0.7917 0.0351  -0.1001 -0.1051 352  ILE A N   
2458 C CA  . ILE A 335 ? 0.7786 0.7470 0.8352 0.0178  -0.0958 -0.0909 352  ILE A CA  
2459 C C   . ILE A 335 ? 0.8167 0.7913 0.8775 0.0129  -0.0747 -0.0770 352  ILE A C   
2460 O O   . ILE A 335 ? 0.8739 0.8322 0.9263 0.0157  -0.0745 -0.0795 352  ILE A O   
2461 C CB  . ILE A 335 ? 0.7037 0.6588 0.7931 0.0061  -0.1177 -0.0945 352  ILE A CB  
2462 C CG1 . ILE A 335 ? 0.7257 0.6710 0.8083 0.0117  -0.1429 -0.1103 352  ILE A CG1 
2463 C CG2 . ILE A 335 ? 0.6696 0.6466 0.8044 -0.0113 -0.1103 -0.0771 352  ILE A CG2 
2464 C CD1 . ILE A 335 ? 0.8584 0.7860 0.9709 -0.0005 -0.1689 -0.1156 352  ILE A CD1 
2465 N N   . MET A 336 ? 0.8198 0.8157 0.8909 0.0072  -0.0580 -0.0629 353  MET A N   
2466 C CA  . MET A 336 ? 0.7234 0.7243 0.8005 0.0015  -0.0398 -0.0488 353  MET A CA  
2467 C C   . MET A 336 ? 0.6865 0.6876 0.8024 -0.0128 -0.0426 -0.0392 353  MET A C   
2468 O O   . MET A 336 ? 0.7745 0.7929 0.9165 -0.0202 -0.0413 -0.0312 353  MET A O   
2469 C CB  . MET A 336 ? 0.6499 0.6689 0.7161 0.0030  -0.0221 -0.0387 353  MET A CB  
2470 C CG  . MET A 336 ? 0.8316 0.8507 0.8607 0.0142  -0.0176 -0.0446 353  MET A CG  
2471 S SD  . MET A 336 ? 0.7369 0.7699 0.7519 0.0138  0.0002  -0.0322 353  MET A SD  
2472 C CE  . MET A 336 ? 0.6259 0.6705 0.6623 0.0119  -0.0060 -0.0307 353  MET A CE  
2473 N N   . MET A 337 ? 0.6806 0.6631 0.8005 -0.0162 -0.0460 -0.0389 354  MET A N   
2474 C CA  . MET A 337 ? 0.8308 0.8096 0.9869 -0.0312 -0.0504 -0.0291 354  MET A CA  
2475 C C   . MET A 337 ? 0.6391 0.6366 0.8103 -0.0385 -0.0291 -0.0093 354  MET A C   
2476 O O   . MET A 337 ? 0.7086 0.7115 0.8575 -0.0318 -0.0127 -0.0042 354  MET A O   
2477 C CB  . MET A 337 ? 0.8285 0.7772 0.9796 -0.0317 -0.0600 -0.0338 354  MET A CB  
2478 C CG  . MET A 337 ? 0.9007 0.8258 1.0383 -0.0244 -0.0838 -0.0536 354  MET A CG  
2479 S SD  . MET A 337 ? 0.8678 0.7522 1.0009 -0.0247 -0.0978 -0.0589 354  MET A SD  
2480 C CE  . MET A 337 ? 0.7019 0.5890 0.8051 -0.0112 -0.0756 -0.0538 354  MET A CE  
2481 N N   . GLU A 338 ? 0.6369 0.6446 0.8464 -0.0521 -0.0303 0.0023  355  GLU A N   
2482 C CA  . GLU A 338 ? 0.5937 0.6208 0.8186 -0.0576 -0.0095 0.0219  355  GLU A CA  
2483 C C   . GLU A 338 ? 0.6794 0.6904 0.8896 -0.0577 0.0025  0.0308  355  GLU A C   
2484 O O   . GLU A 338 ? 0.7045 0.6949 0.9241 -0.0650 -0.0057 0.0322  355  GLU A O   
2485 C CB  . GLU A 338 ? 0.5994 0.6428 0.8722 -0.0726 -0.0136 0.0337  355  GLU A CB  
2486 C CG  . GLU A 338 ? 0.8030 0.8681 1.0925 -0.0768 0.0094  0.0555  355  GLU A CG  
2487 C CD  . GLU A 338 ? 0.8314 0.9187 1.1043 -0.0641 0.0246  0.0571  355  GLU A CD  
2488 O OE1 . GLU A 338 ? 0.8628 0.9701 1.1506 -0.0619 0.0182  0.0530  355  GLU A OE1 
2489 O OE2 . GLU A 338 ? 0.8148 0.8973 1.0581 -0.0560 0.0412  0.0622  355  GLU A OE2 
2490 N N   . GLY A 339 ? 0.6734 0.6916 0.8592 -0.0495 0.0203  0.0366  356  GLY A N   
2491 C CA  . GLY A 339 ? 0.5853 0.5896 0.7546 -0.0481 0.0310  0.0448  356  GLY A CA  
2492 C C   . GLY A 339 ? 0.6306 0.6480 0.8004 -0.0489 0.0515  0.0627  356  GLY A C   
2493 O O   . GLY A 339 ? 0.7530 0.7587 0.9086 -0.0477 0.0606  0.0713  356  GLY A O   
2494 N N   . ASN A 340 ? 0.6361 0.6768 0.8199 -0.0489 0.0585  0.0681  357  ASN A N   
2495 C CA  . ASN A 340 ? 0.7124 0.7658 0.8939 -0.0464 0.0788  0.0846  357  ASN A CA  
2496 C C   . ASN A 340 ? 0.6509 0.7023 0.8571 -0.0571 0.0860  0.1020  357  ASN A C   
2497 O O   . ASN A 340 ? 0.7558 0.8162 1.0003 -0.0689 0.0792  0.1068  357  ASN A O   
2498 C CB  . ASN A 340 ? 0.5902 0.6700 0.7843 -0.0421 0.0834  0.0860  357  ASN A CB  
2499 C CG  . ASN A 340 ? 0.6532 0.7438 0.8352 -0.0341 0.1048  0.1003  357  ASN A CG  
2500 O OD1 . ASN A 340 ? 0.6788 0.7668 0.8638 -0.0369 0.1175  0.1153  357  ASN A OD1 
2501 N ND2 . ASN A 340 ? 0.6818 0.7819 0.8467 -0.0228 0.1084  0.0957  357  ASN A ND2 
2502 N N   . HIS A 341 ? 0.6888 0.7277 0.8727 -0.0536 0.0988  0.1122  358  HIS A N   
2503 C CA  . HIS A 341 ? 0.7176 0.7503 0.9186 -0.0629 0.1067  0.1301  358  HIS A CA  
2504 C C   . HIS A 341 ? 0.7141 0.7740 0.9410 -0.0660 0.1240  0.1491  358  HIS A C   
2505 O O   . HIS A 341 ? 0.8152 0.8752 1.0653 -0.0767 0.1305  0.1663  358  HIS A O   
2506 C CB  . HIS A 341 ? 0.6940 0.7037 0.8591 -0.0562 0.1143  0.1348  358  HIS A CB  
2507 C CG  . HIS A 341 ? 0.7117 0.6986 0.8553 -0.0525 0.0989  0.1188  358  HIS A CG  
2508 N ND1 . HIS A 341 ? 0.7424 0.7110 0.8997 -0.0598 0.0837  0.1135  358  HIS A ND1 
2509 C CD2 . HIS A 341 ? 0.7453 0.7256 0.8553 -0.0415 0.0964  0.1075  358  HIS A CD2 
2510 C CE1 . HIS A 341 ? 0.7100 0.6638 0.8424 -0.0513 0.0740  0.0994  358  HIS A CE1 
2511 N NE2 . HIS A 341 ? 0.7422 0.7051 0.8481 -0.0412 0.0818  0.0963  358  HIS A NE2 
2512 N N   . SER A 342 ? 0.7788 0.8617 1.0024 -0.0562 0.1320  0.1475  359  SER A N   
2513 C CA  . SER A 342 ? 0.7326 0.8453 0.9806 -0.0555 0.1501  0.1657  359  SER A CA  
2514 C C   . SER A 342 ? 0.6459 0.7837 0.9502 -0.0704 0.1419  0.1708  359  SER A C   
2515 O O   . SER A 342 ? 0.8528 1.0175 1.1880 -0.0745 0.1569  0.1903  359  SER A O   
2516 C CB  . SER A 342 ? 0.6543 0.7808 0.8777 -0.0376 0.1602  0.1615  359  SER A CB  
2517 O OG  . SER A 342 ? 0.8021 0.9071 0.9766 -0.0252 0.1702  0.1621  359  SER A OG  
2518 N N   . VAL A 343 ? 0.6059 0.7367 0.9242 -0.0782 0.1182  0.1542  360  VAL A N   
2519 C CA  . VAL A 343 ? 0.7034 0.8525 1.0751 -0.0948 0.1058  0.1584  360  VAL A CA  
2520 C C   . VAL A 343 ? 0.7511 0.8803 1.1416 -0.1127 0.1013  0.1699  360  VAL A C   
2521 O O   . VAL A 343 ? 0.8615 0.9593 1.2207 -0.1105 0.1035  0.1697  360  VAL A O   
2522 C CB  . VAL A 343 ? 0.7172 0.8628 1.0926 -0.0949 0.0803  0.1356  360  VAL A CB  
2523 C CG1 . VAL A 343 ? 0.5706 0.7258 0.9154 -0.0760 0.0844  0.1234  360  VAL A CG1 
2524 C CG2 . VAL A 343 ? 0.7649 0.8710 1.1193 -0.0990 0.0612  0.1202  360  VAL A CG2 
2525 N N   . CYS A 344 ? 0.7442 0.8915 1.1874 -0.1309 0.0942  0.1810  361  CYS A N   
2526 C CA  . CYS A 344 ? 0.8171 0.9429 1.2817 -0.1507 0.0868  0.1926  361  CYS A CA  
2527 C C   . CYS A 344 ? 0.8238 0.9253 1.3026 -0.1633 0.0540  0.1752  361  CYS A C   
2528 O O   . CYS A 344 ? 0.9882 1.0511 1.4557 -0.1708 0.0425  0.1730  361  CYS A O   
2529 C CB  . CYS A 344 ? 0.7365 0.8964 1.2521 -0.1661 0.1023  0.2218  361  CYS A CB  
2530 S SG  . CYS A 344 ? 1.0834 1.2619 1.5803 -0.1536 0.1426  0.2482  361  CYS A SG  
2531 N N   . ASP A 345 ? 0.7335 0.8542 1.2336 -0.1639 0.0376  0.1622  362  ASP A N   
2532 C CA  . ASP A 345 ? 0.7347 0.8345 1.2521 -0.1765 0.0048  0.1470  362  ASP A CA  
2533 C C   . ASP A 345 ? 0.6968 0.7727 1.1700 -0.1594 -0.0114 0.1175  362  ASP A C   
2534 O O   . ASP A 345 ? 0.7740 0.8659 1.2221 -0.1416 -0.0013 0.1090  362  ASP A O   
2535 C CB  . ASP A 345 ? 0.7486 0.8867 1.3243 -0.1907 -0.0058 0.1536  362  ASP A CB  
2536 C CG  . ASP A 345 ? 1.0141 1.1735 1.6422 -0.2130 0.0045  0.1834  362  ASP A CG  
2537 O OD1 . ASP A 345 ? 0.7872 0.9499 1.4621 -0.2350 -0.0174 0.1871  362  ASP A OD1 
2538 O OD2 . ASP A 345 ? 1.2155 1.3872 1.8370 -0.2090 0.0340  0.2037  362  ASP A OD2 
2539 N N   . LYS A 346 ? 0.7040 0.7398 1.1663 -0.1643 -0.0362 0.1026  363  LYS A N   
2540 C CA  . LYS A 346 ? 0.6870 0.7011 1.1153 -0.1504 -0.0562 0.0748  363  LYS A CA  
2541 C C   . LYS A 346 ? 0.6688 0.6740 1.0433 -0.1281 -0.0410 0.0649  363  LYS A C   
2542 O O   . LYS A 346 ? 0.6939 0.7020 1.0436 -0.1137 -0.0465 0.0475  363  LYS A O   
2543 C CB  . LYS A 346 ? 0.7423 0.7838 1.1917 -0.1495 -0.0696 0.0651  363  LYS A CB  
2544 C CG  . LYS A 346 ? 0.6946 0.7506 1.2024 -0.1725 -0.0871 0.0747  363  LYS A CG  
2545 C CD  . LYS A 346 ? 0.7556 0.8398 1.2822 -0.1692 -0.1015 0.0643  363  LYS A CD  
2546 C CE  . LYS A 346 ? 0.7023 0.8060 1.2927 -0.1934 -0.1200 0.0754  363  LYS A CE  
2547 N NZ  . LYS A 346 ? 0.7618 0.9050 1.3977 -0.2066 -0.0952 0.1059  363  LYS A NZ  
2548 N N   . LYS A 347 ? 0.6688 0.6627 1.0248 -0.1255 -0.0231 0.0763  364  LYS A N   
2549 C CA  . LYS A 347 ? 0.6975 0.6834 1.0063 -0.1067 -0.0102 0.0688  364  LYS A CA  
2550 C C   . LYS A 347 ? 0.6746 0.6204 0.9542 -0.1006 -0.0238 0.0554  364  LYS A C   
2551 O O   . LYS A 347 ? 0.7872 0.7063 1.0797 -0.1112 -0.0383 0.0566  364  LYS A O   
2552 C CB  . LYS A 347 ? 0.6447 0.6439 0.9480 -0.1049 0.0171  0.0890  364  LYS A CB  
2553 C CG  . LYS A 347 ? 0.9074 0.9084 1.2454 -0.1224 0.0236  0.1118  364  LYS A CG  
2554 C CD  . LYS A 347 ? 0.6899 0.7125 1.0248 -0.1188 0.0523  0.1325  364  LYS A CD  
2555 C CE  . LYS A 347 ? 0.7185 0.7173 1.0108 -0.1077 0.0630  0.1338  364  LYS A CE  
2556 N NZ  . LYS A 347 ? 0.7521 0.7642 1.0416 -0.1062 0.0887  0.1563  364  LYS A NZ  
2557 N N   . THR A 348 ? 0.8404 0.7821 1.0805 -0.0829 -0.0193 0.0429  365  THR A N   
2558 C CA  . THR A 348 ? 0.7203 0.6302 0.9308 -0.0725 -0.0303 0.0290  365  THR A CA  
2559 C C   . THR A 348 ? 0.7158 0.6258 0.8957 -0.0604 -0.0130 0.0333  365  THR A C   
2560 O O   . THR A 348 ? 0.7666 0.6996 0.9408 -0.0578 0.0049  0.0421  365  THR A O   
2561 C CB  . THR A 348 ? 0.7245 0.6297 0.9169 -0.0608 -0.0467 0.0060  365  THR A CB  
2562 O OG1 . THR A 348 ? 0.8023 0.7306 0.9723 -0.0484 -0.0335 0.0020  365  THR A OG1 
2563 C CG2 . THR A 348 ? 0.7981 0.7074 1.0193 -0.0716 -0.0648 0.0009  365  THR A CG2 
2564 N N   . LEU A 349 ? 0.6997 0.5823 0.8590 -0.0523 -0.0201 0.0264  366  LEU A N   
2565 C CA  . LEU A 349 ? 0.7209 0.6024 0.8517 -0.0397 -0.0084 0.0280  366  LEU A CA  
2566 C C   . LEU A 349 ? 0.7848 0.6604 0.8891 -0.0225 -0.0175 0.0086  366  LEU A C   
2567 O O   . LEU A 349 ? 0.8279 0.6811 0.9301 -0.0189 -0.0351 -0.0044 366  LEU A O   
2568 C CB  . LEU A 349 ? 0.7451 0.6015 0.8757 -0.0432 -0.0070 0.0400  366  LEU A CB  
2569 C CG  . LEU A 349 ? 0.8083 0.6753 0.9401 -0.0484 0.0128  0.0608  366  LEU A CG  
2570 C CD1 . LEU A 349 ? 0.6873 0.5835 0.8399 -0.0580 0.0243  0.0705  366  LEU A CD1 
2571 C CD2 . LEU A 349 ? 0.7216 0.5606 0.8612 -0.0568 0.0109  0.0746  366  LEU A CD2 
2572 N N   . PRO A 350 ? 0.7232 0.6179 0.8066 -0.0116 -0.0065 0.0064  367  PRO A N   
2573 C CA  . PRO A 350 ? 0.7650 0.6601 0.8256 0.0047  -0.0127 -0.0101 367  PRO A CA  
2574 C C   . PRO A 350 ? 0.7615 0.6343 0.8078 0.0166  -0.0187 -0.0146 367  PRO A C   
2575 O O   . PRO A 350 ? 0.7938 0.6554 0.8419 0.0140  -0.0145 -0.0035 367  PRO A O   
2576 C CB  . PRO A 350 ? 0.6345 0.5583 0.6818 0.0088  0.0022  -0.0064 367  PRO A CB  
2577 C CG  . PRO A 350 ? 0.6381 0.5656 0.6916 0.0001  0.0149  0.0111  367  PRO A CG  
2578 C CD  . PRO A 350 ? 0.6360 0.5522 0.7148 -0.0137 0.0117  0.0192  367  PRO A CD  
2579 N N   . LEU A 351 ? 0.7879 0.6540 0.8176 0.0319  -0.0286 -0.0313 368  LEU A N   
2580 C CA  . LEU A 351 ? 0.7598 0.6068 0.7730 0.0480  -0.0343 -0.0376 368  LEU A CA  
2581 C C   . LEU A 351 ? 0.7803 0.6512 0.7816 0.0583  -0.0203 -0.0318 368  LEU A C   
2582 O O   . LEU A 351 ? 0.8464 0.7059 0.8426 0.0653  -0.0203 -0.0275 368  LEU A O   
2583 C CB  . LEU A 351 ? 0.7529 0.5854 0.7494 0.0638  -0.0486 -0.0575 368  LEU A CB  
2584 C CG  . LEU A 351 ? 0.8308 0.6196 0.8286 0.0629  -0.0695 -0.0660 368  LEU A CG  
2585 C CD1 . LEU A 351 ? 0.7933 0.5736 0.8203 0.0377  -0.0744 -0.0555 368  LEU A CD1 
2586 C CD2 . LEU A 351 ? 0.9462 0.7224 0.9235 0.0787  -0.0838 -0.0870 368  LEU A CD2 
2587 N N   . THR A 352 ? 0.8870 0.7899 0.8839 0.0588  -0.0099 -0.0314 369  THR A N   
2588 C CA  . THR A 352 ? 0.8167 0.7452 0.8061 0.0644  0.0021  -0.0244 369  THR A CA  
2589 C C   . THR A 352 ? 0.6933 0.6423 0.6888 0.0496  0.0133  -0.0131 369  THR A C   
2590 O O   . THR A 352 ? 0.6662 0.6182 0.6678 0.0405  0.0132  -0.0143 369  THR A O   
2591 C CB  . THR A 352 ? 0.8656 0.8135 0.8399 0.0821  0.0034  -0.0350 369  THR A CB  
2592 O OG1 . THR A 352 ? 0.8393 0.7960 0.8097 0.0801  0.0028  -0.0425 369  THR A OG1 
2593 C CG2 . THR A 352 ? 0.8192 0.7463 0.7831 0.1013  -0.0067 -0.0464 369  THR A CG2 
2594 N N   . TRP A 353 ? 0.7228 0.6845 0.7152 0.0484  0.0216  -0.0024 370  TRP A N   
2595 C CA  . TRP A 353 ? 0.6485 0.6234 0.6418 0.0360  0.0310  0.0084  370  TRP A CA  
2596 C C   . TRP A 353 ? 0.6851 0.6810 0.6689 0.0396  0.0364  0.0134  370  TRP A C   
2597 O O   . TRP A 353 ? 0.7587 0.7525 0.7407 0.0459  0.0350  0.0172  370  TRP A O   
2598 C CB  . TRP A 353 ? 0.6633 0.6208 0.6645 0.0256  0.0336  0.0201  370  TRP A CB  
2599 C CG  . TRP A 353 ? 0.6781 0.6453 0.6777 0.0153  0.0431  0.0298  370  TRP A CG  
2600 C CD1 . TRP A 353 ? 0.5832 0.5530 0.5911 0.0072  0.0459  0.0307  370  TRP A CD1 
2601 C CD2 . TRP A 353 ? 0.6964 0.6702 0.6834 0.0138  0.0497  0.0393  370  TRP A CD2 
2602 N NE1 . TRP A 353 ? 0.7227 0.6994 0.7221 0.0024  0.0550  0.0400  370  TRP A NE1 
2603 C CE2 . TRP A 353 ? 0.7062 0.6835 0.6913 0.0059  0.0568  0.0450  370  TRP A CE2 
2604 C CE3 . TRP A 353 ? 0.5874 0.5642 0.5642 0.0192  0.0489  0.0433  370  TRP A CE3 
2605 C CZ2 . TRP A 353 ? 0.6141 0.5931 0.5835 0.0037  0.0626  0.0536  370  TRP A CZ2 
2606 C CZ3 . TRP A 353 ? 0.6150 0.5951 0.5788 0.0150  0.0535  0.0522  370  TRP A CZ3 
2607 C CH2 . TRP A 353 ? 0.7456 0.7246 0.7038 0.0076  0.0601  0.0568  370  TRP A CH2 
2608 N N   . THR A 354 ? 0.8539 0.8694 0.8323 0.0352  0.0413  0.0139  371  THR A N   
2609 C CA  . THR A 354 ? 0.6968 0.7332 0.6685 0.0349  0.0450  0.0198  371  THR A CA  
2610 C C   . THR A 354 ? 0.7092 0.7440 0.6743 0.0223  0.0495  0.0291  371  THR A C   
2611 O O   . THR A 354 ? 0.8822 0.9141 0.8454 0.0163  0.0519  0.0277  371  THR A O   
2612 C CB  . THR A 354 ? 0.7090 0.7689 0.6775 0.0409  0.0463  0.0134  371  THR A CB  
2613 O OG1 . THR A 354 ? 0.9473 1.0104 0.9181 0.0566  0.0430  0.0056  371  THR A OG1 
2614 C CG2 . THR A 354 ? 0.6933 0.7758 0.6581 0.0350  0.0499  0.0221  371  THR A CG2 
2615 N N   . GLY A 355 ? 0.7230 0.7582 0.6826 0.0198  0.0496  0.0379  372  GLY A N   
2616 C CA  . GLY A 355 ? 0.7094 0.7386 0.6571 0.0102  0.0524  0.0459  372  GLY A CA  
2617 C C   . GLY A 355 ? 0.6550 0.6929 0.5947 0.0080  0.0489  0.0527  372  GLY A C   
2618 O O   . GLY A 355 ? 0.6757 0.7272 0.6227 0.0142  0.0449  0.0524  372  GLY A O   
2619 N N   . PHE A 356 ? 0.8106 0.8402 0.7348 0.0000  0.0492  0.0586  373  PHE A N   
2620 C CA  . PHE A 356 ? 0.7324 0.7646 0.6461 -0.0043 0.0430  0.0652  373  PHE A CA  
2621 C C   . PHE A 356 ? 0.7638 0.7701 0.6602 -0.0041 0.0430  0.0717  373  PHE A C   
2622 O O   . PHE A 356 ? 0.8564 0.8462 0.7414 -0.0057 0.0489  0.0729  373  PHE A O   
2623 C CB  . PHE A 356 ? 0.5765 0.6173 0.4817 -0.0140 0.0408  0.0664  373  PHE A CB  
2624 C CG  . PHE A 356 ? 0.5698 0.6367 0.4892 -0.0139 0.0426  0.0620  373  PHE A CG  
2625 C CD1 . PHE A 356 ? 0.6549 0.7210 0.5737 -0.0138 0.0482  0.0563  373  PHE A CD1 
2626 C CD2 . PHE A 356 ? 0.6401 0.7338 0.5733 -0.0125 0.0391  0.0640  373  PHE A CD2 
2627 C CE1 . PHE A 356 ? 0.7070 0.7953 0.6344 -0.0120 0.0504  0.0525  373  PHE A CE1 
2628 C CE2 . PHE A 356 ? 0.6360 0.7554 0.5804 -0.0104 0.0431  0.0611  373  PHE A CE2 
2629 C CZ  . PHE A 356 ? 0.6141 0.7292 0.5536 -0.0100 0.0488  0.0552  373  PHE A CZ  
2630 N N   . ILE A 357 ? 0.6864 0.6901 0.5800 -0.0006 0.0367  0.0763  374  ILE A N   
2631 C CA  . ILE A 357 ? 0.7418 0.7201 0.6184 0.0029  0.0374  0.0828  374  ILE A CA  
2632 C C   . ILE A 357 ? 0.7653 0.7359 0.6201 -0.0010 0.0275  0.0879  374  ILE A C   
2633 O O   . ILE A 357 ? 0.8508 0.8385 0.7134 -0.0029 0.0172  0.0883  374  ILE A O   
2634 C CB  . ILE A 357 ? 0.7512 0.7261 0.6384 0.0119  0.0366  0.0842  374  ILE A CB  
2635 C CG1 . ILE A 357 ? 0.8209 0.8011 0.7292 0.0151  0.0426  0.0777  374  ILE A CG1 
2636 C CG2 . ILE A 357 ? 0.7271 0.6742 0.5947 0.0154  0.0393  0.0926  374  ILE A CG2 
2637 C CD1 . ILE A 357 ? 0.8662 0.8347 0.7741 0.0110  0.0522  0.0778  374  ILE A CD1 
2638 N N   . PRO A 358 ? 0.8048 0.7501 0.6320 -0.0017 0.0294  0.0918  375  PRO A N   
2639 C CA  . PRO A 358 ? 0.8174 0.7480 0.6186 -0.0035 0.0173  0.0959  375  PRO A CA  
2640 C C   . PRO A 358 ? 0.9234 0.8385 0.7130 0.0053  0.0143  0.1017  375  PRO A C   
2641 O O   . PRO A 358 ? 0.9474 0.8436 0.7259 0.0123  0.0249  0.1058  375  PRO A O   
2642 C CB  . PRO A 358 ? 0.6838 0.5907 0.4560 -0.0049 0.0216  0.0962  375  PRO A CB  
2643 C CG  . PRO A 358 ? 0.8319 0.7445 0.6189 -0.0028 0.0375  0.0935  375  PRO A CG  
2644 C CD  . PRO A 358 ? 0.8266 0.7566 0.6444 0.0002  0.0421  0.0923  375  PRO A CD  
2645 N N   . LEU A 359 ? 0.8760 0.8002 0.6690 0.0052  -0.0001 0.1032  376  LEU A N   
2646 C CA  . LEU A 359 ? 0.8846 0.7947 0.6665 0.0147  -0.0052 0.1086  376  LEU A CA  
2647 C C   . LEU A 359 ? 0.9860 0.8875 0.7465 0.0124  -0.0242 0.1112  376  LEU A C   
2648 O O   . LEU A 359 ? 0.9105 0.8295 0.6803 0.0021  -0.0358 0.1089  376  LEU A O   
2649 C CB  . LEU A 359 ? 0.8674 0.7993 0.6802 0.0209  -0.0056 0.1074  376  LEU A CB  
2650 C CG  . LEU A 359 ? 0.8110 0.7461 0.6435 0.0242  0.0095  0.1044  376  LEU A CG  
2651 C CD1 . LEU A 359 ? 0.9136 0.8669 0.7717 0.0321  0.0059  0.1016  376  LEU A CD1 
2652 C CD2 . LEU A 359 ? 0.8224 0.7271 0.6360 0.0286  0.0208  0.1108  376  LEU A CD2 
2653 N N   . PRO A 360 ? 0.9213 0.7948 0.6521 0.0213  -0.0284 0.1166  377  PRO A N   
2654 C CA  . PRO A 360 ? 0.9671 0.8316 0.6778 0.0203  -0.0500 0.1185  377  PRO A CA  
2655 C C   . PRO A 360 ? 1.0216 0.9212 0.7668 0.0185  -0.0637 0.1180  377  PRO A C   
2656 O O   . PRO A 360 ? 1.0200 0.9361 0.7897 0.0263  -0.0575 0.1183  377  PRO A O   
2657 C CB  . PRO A 360 ? 1.0387 0.8673 0.7126 0.0339  -0.0482 0.1249  377  PRO A CB  
2658 C CG  . PRO A 360 ? 1.1041 0.9191 0.7716 0.0382  -0.0243 0.1270  377  PRO A CG  
2659 C CD  . PRO A 360 ? 0.9802 0.8273 0.6919 0.0319  -0.0137 0.1222  377  PRO A CD  
2660 N N   . GLY A 361 ? 1.0165 0.9274 0.7637 0.0082  -0.0831 0.1176  378  GLY A N   
2661 C CA  . GLY A 361 ? 0.9134 0.8658 0.6988 0.0051  -0.0952 0.1183  378  GLY A CA  
2662 C C   . GLY A 361 ? 0.8871 0.8374 0.6635 0.0059  -0.1203 0.1222  378  GLY A C   
2663 O O   . GLY A 361 ? 1.0584 0.9722 0.7945 0.0055  -0.1321 0.1232  378  GLY A O   
2664 N N   . GLU A 362 ? 0.9419 0.9317 0.7550 0.0084  -0.1291 0.1241  379  GLU A N   
2665 C CA  . GLU A 362 ? 0.9648 0.9624 0.7788 0.0084  -0.1550 0.1280  379  GLU A CA  
2666 C C   . GLU A 362 ? 0.9197 0.9772 0.7873 0.0023  -0.1617 0.1302  379  GLU A C   
2667 O O   . GLU A 362 ? 0.9758 1.0645 0.8751 0.0066  -0.1445 0.1284  379  GLU A O   
2668 C CB  . GLU A 362 ? 1.0029 0.9771 0.7959 0.0281  -0.1589 0.1305  379  GLU A CB  
2669 C CG  . GLU A 362 ? 1.1517 1.1401 0.9668 0.0438  -0.1413 0.1298  379  GLU A CG  
2670 C CD  . GLU A 362 ? 1.3347 1.2926 1.1237 0.0624  -0.1450 0.1335  379  GLU A CD  
2671 O OE1 . GLU A 362 ? 1.2079 1.1725 1.0123 0.0759  -0.1347 0.1335  379  GLU A OE1 
2672 O OE2 . GLU A 362 ? 1.4005 1.3249 1.1509 0.0640  -0.1590 0.1365  379  GLU A OE2 
2673 N N   . ILE A 363 ? 0.9569 1.0306 0.8340 -0.0075 -0.1872 0.1345  380  ILE A N   
2674 C CA  . ILE A 363 ? 1.0507 1.1862 0.9815 -0.0156 -0.1944 0.1391  380  ILE A CA  
2675 C C   . ILE A 363 ? 0.9813 1.1494 0.9411 0.0057  -0.1900 0.1400  380  ILE A C   
2676 O O   . ILE A 363 ? 0.9984 1.1409 0.9362 0.0229  -0.1956 0.1394  380  ILE A O   
2677 C CB  . ILE A 363 ? 1.0974 1.2400 1.0316 -0.0331 -0.2256 0.1445  380  ILE A CB  
2678 C CG1 . ILE A 363 ? 1.0604 1.2738 1.0560 -0.0423 -0.2326 0.1519  380  ILE A CG1 
2679 C CG2 . ILE A 363 ? 1.0250 1.1343 0.9265 -0.0212 -0.2473 0.1446  380  ILE A CG2 
2680 C CD1 . ILE A 363 ? 1.0275 1.2527 1.0337 -0.0625 -0.2653 0.1587  380  ILE A CD1 
2681 N N   . GLU A 364 ? 0.9296 1.1525 0.9363 0.0062  -0.1792 0.1415  381  GLU A N   
2682 C CA  . GLU A 364 ? 0.9867 1.2452 1.0233 0.0281  -0.1755 0.1420  381  GLU A CA  
2683 C C   . GLU A 364 ? 1.0011 1.2731 1.0461 0.0346  -0.2020 0.1474  381  GLU A C   
2684 O O   . GLU A 364 ? 1.0166 1.3415 1.1029 0.0272  -0.2151 0.1541  381  GLU A O   
2685 C CB  . GLU A 364 ? 0.9577 1.2781 1.0433 0.0264  -0.1618 0.1441  381  GLU A CB  
2686 C CG  . GLU A 364 ? 1.0627 1.3741 1.1431 0.0321  -0.1341 0.1368  381  GLU A CG  
2687 C CD  . GLU A 364 ? 1.1089 1.4807 1.2333 0.0385  -0.1204 0.1384  381  GLU A CD  
2688 O OE1 . GLU A 364 ? 1.0885 1.5105 1.2483 0.0262  -0.1284 0.1472  381  GLU A OE1 
2689 O OE2 . GLU A 364 ? 1.0122 1.3811 1.1354 0.0560  -0.1021 0.1312  381  GLU A OE2 
2690 N N   . GLU B 409 ? 1.4923 1.5345 1.5322 0.0500  0.2665  0.1614  659  GLU B N   
2691 C CA  . GLU B 409 ? 1.6609 1.7122 1.6590 0.0720  0.2757  0.1870  659  GLU B CA  
2692 C C   . GLU B 409 ? 1.6897 1.7844 1.6645 0.0675  0.2445  0.1674  659  GLU B C   
2693 O O   . GLU B 409 ? 1.6537 1.7545 1.6496 0.0434  0.2335  0.1365  659  GLU B O   
2694 C CB  . GLU B 409 ? 1.6207 1.6319 1.6252 0.0675  0.3207  0.1990  659  GLU B CB  
2695 C CG  . GLU B 409 ? 1.6785 1.6945 1.6348 0.0884  0.3347  0.2255  659  GLU B CG  
2696 C CD  . GLU B 409 ? 1.7763 1.8075 1.6889 0.1258  0.3260  0.2622  659  GLU B CD  
2697 O OE1 . GLU B 409 ? 1.7142 1.7947 1.6000 0.1356  0.2887  0.2554  659  GLU B OE1 
2698 O OE2 . GLU B 409 ? 1.7378 1.7331 1.6453 0.1461  0.3570  0.2969  659  GLU B OE2 
2699 N N   . THR B 410 ? 1.6968 1.8232 1.6294 0.0917  0.2304  0.1846  660  THR B N   
2700 C CA  . THR B 410 ? 1.6342 1.8033 1.5448 0.0875  0.2041  0.1645  660  THR B CA  
2701 C C   . THR B 410 ? 1.6283 1.7885 1.5244 0.0815  0.2261  0.1644  660  THR B C   
2702 O O   . THR B 410 ? 1.7038 1.8299 1.5930 0.0885  0.2620  0.1881  660  THR B O   
2703 C CB  . THR B 410 ? 1.6114 1.8250 1.4838 0.1143  0.1811  0.1777  660  THR B CB  
2704 O OG1 . THR B 410 ? 1.5731 1.8301 1.4357 0.1040  0.1530  0.1481  660  THR B OG1 
2705 C CG2 . THR B 410 ? 1.5872 1.7969 1.4145 0.1433  0.2031  0.2159  660  THR B CG2 
2706 N N   . GLN B 411 ? 1.4534 1.6421 1.3472 0.0675  0.2071  0.1362  661  GLN B N   
2707 C CA  . GLN B 411 ? 1.4738 1.6594 1.3581 0.0594  0.2257  0.1299  661  GLN B CA  
2708 C C   . GLN B 411 ? 1.4418 1.6746 1.2923 0.0644  0.2030  0.1168  661  GLN B C   
2709 O O   . GLN B 411 ? 1.2668 1.5247 1.1335 0.0514  0.1753  0.0872  661  GLN B O   
2710 C CB  . GLN B 411 ? 1.4130 1.5799 1.3461 0.0309  0.2313  0.1006  661  GLN B CB  
2711 C CG  . GLN B 411 ? 1.3804 1.5041 1.3489 0.0228  0.2586  0.1080  661  GLN B CG  
2712 C CD  . GLN B 411 ? 1.4023 1.5184 1.4207 -0.0040 0.2582  0.0751  661  GLN B CD  
2713 O OE1 . GLN B 411 ? 1.5492 1.6893 1.5777 -0.0145 0.2322  0.0489  661  GLN B OE1 
2714 N NE2 . GLN B 411 ? 1.2618 1.3452 1.3131 -0.0143 0.2879  0.0755  661  GLN B NE2 
2715 N N   . ASN B 412 ? 1.4812 1.7251 1.2840 0.0830  0.2168  0.1381  662  ASN B N   
2716 C CA  . ASN B 412 ? 1.4205 1.7145 1.1857 0.0897  0.1969  0.1258  662  ASN B CA  
2717 C C   . ASN B 412 ? 1.3669 1.6635 1.1433 0.0677  0.2052  0.0971  662  ASN B C   
2718 O O   . ASN B 412 ? 1.3298 1.6142 1.0839 0.0692  0.2332  0.1069  662  ASN B O   
2719 C CB  . ASN B 412 ? 1.4493 1.7570 1.1537 0.1208  0.2072  0.1614  662  ASN B CB  
2720 C CG  . ASN B 412 ? 1.4499 1.7603 1.1460 0.1465  0.1965  0.1897  662  ASN B CG  
2721 O OD1 . ASN B 412 ? 1.4131 1.7052 1.1510 0.1388  0.1892  0.1851  662  ASN B OD1 
2722 N ND2 . ASN B 412 ? 1.4277 1.7627 1.0692 0.1784  0.1954  0.2188  662  ASN B ND2 
2723 N N   . LEU B 413 ? 1.3804 1.6914 1.1921 0.0479  0.1824  0.0616  663  LEU B N   
2724 C CA  . LEU B 413 ? 1.3479 1.6645 1.1756 0.0289  0.1873  0.0322  663  LEU B CA  
2725 C C   . LEU B 413 ? 1.3204 1.6803 1.1048 0.0353  0.1820  0.0224  663  LEU B C   
2726 O O   . LEU B 413 ? 1.3993 1.7948 1.1495 0.0511  0.1639  0.0287  663  LEU B O   
2727 C CB  . LEU B 413 ? 1.2130 1.5295 1.0885 0.0097  0.1648  0.0007  663  LEU B CB  
2728 C CG  . LEU B 413 ? 1.1712 1.4540 1.0865 0.0028  0.1627  0.0052  663  LEU B CG  
2729 C CD1 . LEU B 413 ? 1.1678 1.4565 1.1141 -0.0106 0.1360  -0.0219 663  LEU B CD1 
2730 C CD2 . LEU B 413 ? 1.1571 1.4066 1.1003 -0.0069 0.1908  0.0076  663  LEU B CD2 
2731 N N   . ASN B 414 ? 1.2617 1.6220 1.0501 0.0223  0.1982  0.0040  664  ASN B N   
2732 C CA  . ASN B 414 ? 1.3550 1.7563 1.1072 0.0234  0.1958  -0.0126 664  ASN B CA  
2733 C C   . ASN B 414 ? 1.3376 1.7446 1.1295 0.0004  0.1931  -0.0532 664  ASN B C   
2734 O O   . ASN B 414 ? 1.1984 1.5747 1.0384 -0.0133 0.2011  -0.0623 664  ASN B O   
2735 C CB  . ASN B 414 ? 1.3846 1.7808 1.0865 0.0352  0.2270  0.0110  664  ASN B CB  
2736 C CG  . ASN B 414 ? 1.4044 1.8169 1.0476 0.0644  0.2225  0.0469  664  ASN B CG  
2737 O OD1 . ASN B 414 ? 1.3712 1.8338 0.9757 0.0754  0.2024  0.0394  664  ASN B OD1 
2738 N ND2 . ASN B 414 ? 1.5181 1.8899 1.1564 0.0780  0.2416  0.0847  664  ASN B ND2 
2739 N N   . SER B 415 ? 1.3582 1.8074 1.1311 -0.0028 0.1818  -0.0787 665  SER B N   
2740 C CA  . SER B 415 ? 1.3266 1.7816 1.1378 -0.0229 0.1801  -0.1179 665  SER B CA  
2741 C C   . SER B 415 ? 1.3531 1.7932 1.1706 -0.0320 0.2111  -0.1248 665  SER B C   
2742 O O   . SER B 415 ? 1.4290 1.8696 1.2040 -0.0237 0.2337  -0.1062 665  SER B O   
2743 C CB  . SER B 415 ? 1.4428 1.9476 1.2348 -0.0256 0.1629  -0.1469 665  SER B CB  
2744 O OG  . SER B 415 ? 1.4860 2.0215 1.2286 -0.0208 0.1774  -0.1492 665  SER B OG  
2745 N N   . GLY B 416 ? 1.3333 1.7596 1.2044 -0.0482 0.2133  -0.1513 666  GLY B N   
2746 C CA  . GLY B 416 ? 1.1514 1.5656 1.0424 -0.0586 0.2418  -0.1639 666  GLY B CA  
2747 C C   . GLY B 416 ? 1.1002 1.4825 1.0577 -0.0674 0.2421  -0.1710 666  GLY B C   
2748 O O   . GLY B 416 ? 1.2205 1.5829 1.1978 -0.0636 0.2277  -0.1561 666  GLY B O   
2749 N N   . TRP B 417 ? 1.1123 1.4929 1.1061 -0.0789 0.2585  -0.1959 667  TRP B N   
2750 C CA  . TRP B 417 ? 1.0229 1.3817 1.0831 -0.0854 0.2582  -0.2065 667  TRP B CA  
2751 C C   . TRP B 417 ? 1.1360 1.4757 1.2096 -0.0884 0.2889  -0.1957 667  TRP B C   
2752 O O   . TRP B 417 ? 1.1848 1.5281 1.2280 -0.0904 0.3183  -0.1931 667  TRP B O   
2753 C CB  . TRP B 417 ? 1.1191 1.4883 1.2212 -0.0942 0.2572  -0.2420 667  TRP B CB  
2754 C CG  . TRP B 417 ? 1.0688 1.4221 1.2392 -0.0976 0.2585  -0.2536 667  TRP B CG  
2755 C CD1 . TRP B 417 ? 1.1060 1.4582 1.3121 -0.1046 0.2847  -0.2679 667  TRP B CD1 
2756 C CD2 . TRP B 417 ? 1.1159 1.4561 1.3270 -0.0933 0.2319  -0.2529 667  TRP B CD2 
2757 N NE1 . TRP B 417 ? 1.0461 1.3899 1.3164 -0.1038 0.2736  -0.2775 667  TRP B NE1 
2758 C CE2 . TRP B 417 ? 1.0731 1.4092 1.3442 -0.0961 0.2407  -0.2674 667  TRP B CE2 
2759 C CE3 . TRP B 417 ? 0.9482 1.2810 1.1500 -0.0871 0.2023  -0.2421 667  TRP B CE3 
2760 C CZ2 . TRP B 417 ? 1.0731 1.4013 1.3912 -0.0907 0.2178  -0.2703 667  TRP B CZ2 
2761 C CZ3 . TRP B 417 ? 0.8652 1.1846 1.1102 -0.0832 0.1827  -0.2438 667  TRP B CZ3 
2762 C CH2 . TRP B 417 ? 0.9298 1.2484 1.2305 -0.0840 0.1891  -0.2572 667  TRP B CH2 
2763 N N   . THR B 418 ? 1.1975 1.5174 1.3161 -0.0895 0.2836  -0.1912 668  THR B N   
2764 C CA  . THR B 418 ? 1.1010 1.4030 1.2456 -0.0952 0.3132  -0.1866 668  THR B CA  
2765 C C   . THR B 418 ? 1.0891 1.3931 1.3106 -0.1029 0.3081  -0.2140 668  THR B C   
2766 O O   . THR B 418 ? 1.1274 1.4327 1.3782 -0.0993 0.2768  -0.2195 668  THR B O   
2767 C CB  . THR B 418 ? 1.1167 1.3963 1.2450 -0.0893 0.3144  -0.1562 668  THR B CB  
2768 O OG1 . THR B 418 ? 1.2131 1.4900 1.2718 -0.0795 0.3279  -0.1284 668  THR B OG1 
2769 C CG2 . THR B 418 ? 1.1909 1.4518 1.3658 -0.0986 0.3419  -0.1597 668  THR B CG2 
2770 N N   . ASP B 419 ? 1.1193 1.4250 1.3725 -0.1123 0.3390  -0.2313 669  ASP B N   
2771 C CA  . ASP B 419 ? 1.1495 1.4634 1.4809 -0.1178 0.3351  -0.2593 669  ASP B CA  
2772 C C   . ASP B 419 ? 1.1150 1.4193 1.4826 -0.1180 0.3250  -0.2533 669  ASP B C   
2773 O O   . ASP B 419 ? 1.1457 1.4335 1.5049 -0.1231 0.3502  -0.2394 669  ASP B O   
2774 C CB  . ASP B 419 ? 1.1952 1.5142 1.5542 -0.1291 0.3749  -0.2800 669  ASP B CB  
2775 C CG  . ASP B 419 ? 1.1523 1.4874 1.4999 -0.1305 0.3800  -0.2989 669  ASP B CG  
2776 O OD1 . ASP B 419 ? 1.1746 1.5198 1.5264 -0.1238 0.3496  -0.3070 669  ASP B OD1 
2777 O OD2 . ASP B 419 ? 1.2049 1.5408 1.5395 -0.1393 0.4171  -0.3066 669  ASP B OD2 
2778 N N   . THR B 420 ? 1.1019 1.4156 1.5084 -0.1123 0.2898  -0.2642 670  THR B N   
2779 C CA  . THR B 420 ? 0.9877 1.2994 1.4309 -0.1126 0.2754  -0.2642 670  THR B CA  
2780 C C   . THR B 420 ? 1.0329 1.3677 1.5524 -0.1123 0.2635  -0.2952 670  THR B C   
2781 O O   . THR B 420 ? 1.1553 1.5031 1.6936 -0.1063 0.2530  -0.3106 670  THR B O   
2782 C CB  . THR B 420 ? 1.0747 1.3774 1.4852 -0.1031 0.2396  -0.2446 670  THR B CB  
2783 O OG1 . THR B 420 ? 0.9516 1.2642 1.3722 -0.0939 0.2088  -0.2548 670  THR B OG1 
2784 C CG2 . THR B 420 ? 1.0227 1.3095 1.3610 -0.1002 0.2471  -0.2160 670  THR B CG2 
2785 N N   . ALA B 421 ? 1.0540 1.3960 1.6201 -0.1181 0.2658  -0.3057 671  ALA B N   
2786 C CA  . ALA B 421 ? 0.8951 1.2665 1.5357 -0.1149 0.2484  -0.3354 671  ALA B CA  
2787 C C   . ALA B 421 ? 0.9918 1.3687 1.6294 -0.0991 0.2003  -0.3297 671  ALA B C   
2788 O O   . ALA B 421 ? 1.0309 1.3874 1.6126 -0.0938 0.1836  -0.3049 671  ALA B O   
2789 C CB  . ALA B 421 ? 0.7463 1.1294 1.4402 -0.1283 0.2688  -0.3537 671  ALA B CB  
2790 N N   . HIS B 422 ? 0.8983 1.3037 1.5968 -0.0905 0.1784  -0.3528 672  HIS B N   
2791 C CA  . HIS B 422 ? 0.8537 1.2637 1.5489 -0.0733 0.1339  -0.3465 672  HIS B CA  
2792 C C   . HIS B 422 ? 1.0022 1.4032 1.6715 -0.0774 0.1205  -0.3325 672  HIS B C   
2793 O O   . HIS B 422 ? 1.0306 1.4362 1.7180 -0.0920 0.1403  -0.3400 672  HIS B O   
2794 C CB  . HIS B 422 ? 0.9190 1.3663 1.6869 -0.0606 0.1134  -0.3737 672  HIS B CB  
2795 C CG  . HIS B 422 ? 0.9175 1.3668 1.7003 -0.0458 0.1077  -0.3793 672  HIS B CG  
2796 N ND1 . HIS B 422 ? 0.9192 1.3749 1.7300 -0.0530 0.1389  -0.3966 672  HIS B ND1 
2797 C CD2 . HIS B 422 ? 0.8261 1.2690 1.6006 -0.0243 0.0774  -0.3704 672  HIS B CD2 
2798 C CE1 . HIS B 422 ? 0.8734 1.3282 1.6958 -0.0371 0.1277  -0.3997 672  HIS B CE1 
2799 N NE2 . HIS B 422 ? 0.9796 1.4249 1.7805 -0.0189 0.0912  -0.3829 672  HIS B NE2 
2800 N N   . GLY B 423 ? 0.9483 1.3341 1.5762 -0.0657 0.0903  -0.3131 673  GLY B N   
2801 C CA  . GLY B 423 ? 1.0118 1.3895 1.6153 -0.0684 0.0747  -0.3012 673  GLY B CA  
2802 C C   . GLY B 423 ? 1.0187 1.3648 1.5551 -0.0625 0.0610  -0.2728 673  GLY B C   
2803 O O   . GLY B 423 ? 0.8947 1.2243 1.3991 -0.0604 0.0697  -0.2619 673  GLY B O   
2804 N N   . SER B 424 ? 1.0447 1.3848 1.5615 -0.0610 0.0401  -0.2639 674  SER B N   
2805 C CA  . SER B 424 ? 0.9529 1.2639 1.4100 -0.0579 0.0286  -0.2392 674  SER B CA  
2806 C C   . SER B 424 ? 0.9183 1.2231 1.3613 -0.0674 0.0278  -0.2330 674  SER B C   
2807 O O   . SER B 424 ? 0.9557 1.2796 1.4267 -0.0677 0.0129  -0.2472 674  SER B O   
2808 C CB  . SER B 424 ? 1.0420 1.3476 1.4878 -0.0403 -0.0025 -0.2346 674  SER B CB  
2809 O OG  . SER B 424 ? 1.0893 1.4156 1.5625 -0.0319 -0.0278 -0.2457 674  SER B OG  
2810 N N   . GLY B 425 ? 1.0002 1.2813 1.4015 -0.0746 0.0436  -0.2136 675  GLY B N   
2811 C CA  . GLY B 425 ? 0.6768 0.9488 1.0683 -0.0845 0.0496  -0.2077 675  GLY B CA  
2812 C C   . GLY B 425 ? 0.6503 0.9193 1.0257 -0.0797 0.0195  -0.2057 675  GLY B C   
2813 O O   . GLY B 425 ? 0.7873 1.0420 1.1286 -0.0702 0.0015  -0.1932 675  GLY B O   
2814 N N   . VAL B 426 ? 0.6774 0.9598 1.0772 -0.0875 0.0162  -0.2196 676  VAL B N   
2815 C CA  . VAL B 426 ? 0.8257 1.1073 1.2079 -0.0852 -0.0098 -0.2198 676  VAL B CA  
2816 C C   . VAL B 426 ? 0.8013 1.0667 1.1697 -0.0995 0.0073  -0.2140 676  VAL B C   
2817 O O   . VAL B 426 ? 0.7963 1.0683 1.1967 -0.1126 0.0321  -0.2256 676  VAL B O   
2818 C CB  . VAL B 426 ? 0.6140 0.9325 1.0369 -0.0808 -0.0323 -0.2456 676  VAL B CB  
2819 C CG1 . VAL B 426 ? 0.7166 1.0344 1.1120 -0.0774 -0.0594 -0.2444 676  VAL B CG1 
2820 C CG2 . VAL B 426 ? 0.5999 0.9340 1.0424 -0.0639 -0.0470 -0.2505 676  VAL B CG2 
2821 N N   . ILE B 427 ? 0.7625 1.0049 1.0863 -0.0975 -0.0029 -0.1970 677  ILE B N   
2822 C CA  . ILE B 427 ? 0.7366 0.9610 1.0466 -0.1093 0.0136  -0.1898 677  ILE B CA  
2823 C C   . ILE B 427 ? 0.7749 1.0025 1.0738 -0.1127 -0.0071 -0.1988 677  ILE B C   
2824 O O   . ILE B 427 ? 0.7941 1.0092 1.0553 -0.1043 -0.0281 -0.1879 677  ILE B O   
2825 C CB  . ILE B 427 ? 0.7768 0.9733 1.0459 -0.1054 0.0242  -0.1632 677  ILE B CB  
2826 C CG1 . ILE B 427 ? 0.6898 0.8862 0.9658 -0.1028 0.0471  -0.1551 677  ILE B CG1 
2827 C CG2 . ILE B 427 ? 0.7428 0.9209 0.9987 -0.1143 0.0377  -0.1552 677  ILE B CG2 
2828 C CD1 . ILE B 427 ? 0.6972 0.8748 0.9354 -0.0979 0.0577  -0.1311 677  ILE B CD1 
2829 N N   . PRO B 428 ? 0.7615 1.0052 1.0914 -0.1259 0.0001  -0.2200 678  PRO B N   
2830 C CA  . PRO B 428 ? 0.6984 0.9457 1.0130 -0.1314 -0.0167 -0.2300 678  PRO B CA  
2831 C C   . PRO B 428 ? 0.7377 0.9508 1.0183 -0.1380 -0.0022 -0.2119 678  PRO B C   
2832 O O   . PRO B 428 ? 0.8127 1.0117 1.1075 -0.1476 0.0281  -0.2076 678  PRO B O   
2833 C CB  . PRO B 428 ? 0.7298 1.0085 1.0964 -0.1465 -0.0072 -0.2630 678  PRO B CB  
2834 C CG  . PRO B 428 ? 0.6017 0.8737 1.0027 -0.1536 0.0289  -0.2619 678  PRO B CG  
2835 C CD  . PRO B 428 ? 0.7603 1.0212 1.1425 -0.1378 0.0256  -0.2395 678  PRO B CD  
2836 N N   . MET B 429 ? 0.7552 0.9538 0.9918 -0.1319 -0.0224 -0.2008 679  MET B N   
2837 C CA  . MET B 429 ? 0.8679 1.0353 1.0720 -0.1360 -0.0107 -0.1834 679  MET B CA  
2838 C C   . MET B 429 ? 0.8491 1.0157 1.0604 -0.1524 -0.0008 -0.1987 679  MET B C   
2839 O O   . MET B 429 ? 0.9355 1.0964 1.1177 -0.1554 -0.0144 -0.2021 679  MET B O   
2840 C CB  . MET B 429 ? 0.8671 1.0171 1.0244 -0.1250 -0.0313 -0.1679 679  MET B CB  
2841 C CG  . MET B 429 ? 0.7975 0.9449 0.9490 -0.1108 -0.0365 -0.1545 679  MET B CG  
2842 S SD  . MET B 429 ? 0.8170 0.9544 0.9751 -0.1109 -0.0088 -0.1380 679  MET B SD  
2843 C CE  . MET B 429 ? 0.7485 0.8592 0.8686 -0.1135 -0.0052 -0.1233 679  MET B CE  
2844 N N   . ARG B 430 ? 0.8393 1.0098 1.0903 -0.1640 0.0268  -0.2089 680  ARG B N   
2845 C CA  . ARG B 430 ? 0.8919 1.0557 1.1546 -0.1811 0.0448  -0.2227 680  ARG B CA  
2846 C C   . ARG B 430 ? 0.9030 1.0321 1.1460 -0.1808 0.0653  -0.1995 680  ARG B C   
2847 O O   . ARG B 430 ? 0.9269 1.0447 1.1624 -0.1914 0.0722  -0.2061 680  ARG B O   
2848 C CB  . ARG B 430 ? 0.7303 0.9094 1.0485 -0.1950 0.0706  -0.2456 680  ARG B CB  
2849 C CG  . ARG B 430 ? 0.7883 1.0104 1.1349 -0.1987 0.0503  -0.2774 680  ARG B CG  
2850 C CD  . ARG B 430 ? 0.6817 0.9196 1.0895 -0.2151 0.0803  -0.3039 680  ARG B CD  
2851 N NE  . ARG B 430 ? 0.8236 1.1031 1.2638 -0.2116 0.0628  -0.3260 680  ARG B NE  
2852 C CZ  . ARG B 430 ? 0.7783 1.1014 1.2312 -0.2144 0.0344  -0.3573 680  ARG B CZ  
2853 N NH1 . ARG B 430 ? 0.6595 0.9885 1.0908 -0.2224 0.0215  -0.3703 680  ARG B NH1 
2854 N NH2 . ARG B 430 ? 0.9566 1.3198 1.4438 -0.2083 0.0187  -0.3763 680  ARG B NH2 
2855 N N   . THR B 431 ? 0.8964 1.0116 1.1317 -0.1682 0.0748  -0.1740 681  THR B N   
2856 C CA  . THR B 431 ? 0.8336 0.9232 1.0511 -0.1630 0.0900  -0.1507 681  THR B CA  
2857 C C   . THR B 431 ? 0.8479 0.9357 1.0323 -0.1470 0.0726  -0.1303 681  THR B C   
2858 O O   . THR B 431 ? 0.9184 1.0199 1.0957 -0.1404 0.0529  -0.1330 681  THR B O   
2859 C CB  . THR B 431 ? 0.8996 0.9758 1.1455 -0.1629 0.1263  -0.1402 681  THR B CB  
2860 O OG1 . THR B 431 ? 1.0297 1.0950 1.2542 -0.1462 0.1307  -0.1109 681  THR B OG1 
2861 C CG2 . THR B 431 ? 0.7661 0.8571 1.0464 -0.1669 0.1375  -0.1528 681  THR B CG2 
2862 N N   . ASP B 432 ? 0.8583 0.9307 1.0258 -0.1408 0.0807  -0.1119 682  ASP B N   
2863 C CA  . ASP B 432 ? 0.6505 0.7252 0.7920 -0.1273 0.0681  -0.0961 682  ASP B CA  
2864 C C   . ASP B 432 ? 0.7220 0.8078 0.8730 -0.1171 0.0748  -0.0867 682  ASP B C   
2865 O O   . ASP B 432 ? 0.9020 0.9837 1.0709 -0.1150 0.0986  -0.0780 682  ASP B O   
2866 C CB  . ASP B 432 ? 0.6983 0.7616 0.8273 -0.1225 0.0765  -0.0818 682  ASP B CB  
2867 C CG  . ASP B 432 ? 0.7940 0.8459 0.9074 -0.1323 0.0685  -0.0913 682  ASP B CG  
2868 O OD1 . ASP B 432 ? 0.8931 0.9454 0.9908 -0.1383 0.0505  -0.1036 682  ASP B OD1 
2869 O OD2 . ASP B 432 ? 0.8775 0.9193 0.9932 -0.1329 0.0812  -0.0857 682  ASP B OD2 
2870 N N   . LEU B 433 ? 0.8342 0.9315 0.9724 -0.1109 0.0565  -0.0883 683  LEU B N   
2871 C CA  . LEU B 433 ? 0.7478 0.8568 0.8907 -0.1018 0.0626  -0.0810 683  LEU B CA  
2872 C C   . LEU B 433 ? 0.7260 0.8358 0.8496 -0.0904 0.0695  -0.0618 683  LEU B C   
2873 O O   . LEU B 433 ? 0.7209 0.8335 0.8233 -0.0869 0.0555  -0.0606 683  LEU B O   
2874 C CB  . LEU B 433 ? 0.7470 0.8679 0.8856 -0.0990 0.0422  -0.0910 683  LEU B CB  
2875 C CG  . LEU B 433 ? 0.5979 0.7319 0.7395 -0.0909 0.0479  -0.0868 683  LEU B CG  
2876 C CD1 . LEU B 433 ? 0.6393 0.7758 0.8066 -0.0932 0.0719  -0.0858 683  LEU B CD1 
2877 C CD2 . LEU B 433 ? 0.7227 0.8658 0.8665 -0.0884 0.0292  -0.0990 683  LEU B CD2 
2878 N N   . GLU B 434 ? 0.7218 0.8297 0.8527 -0.0840 0.0919  -0.0476 684  GLU B N   
2879 C CA  . GLU B 434 ? 0.8251 0.9381 0.9369 -0.0694 0.0981  -0.0274 684  GLU B CA  
2880 C C   . GLU B 434 ? 0.8038 0.9306 0.9068 -0.0595 0.1050  -0.0192 684  GLU B C   
2881 O O   . GLU B 434 ? 0.8339 0.9552 0.9528 -0.0625 0.1222  -0.0196 684  GLU B O   
2882 C CB  . GLU B 434 ? 0.8074 0.9035 0.9286 -0.0654 0.1205  -0.0121 684  GLU B CB  
2883 C CG  . GLU B 434 ? 0.9269 1.0315 1.0291 -0.0452 0.1267  0.0120  684  GLU B CG  
2884 C CD  . GLU B 434 ? 1.2098 1.3014 1.3189 -0.0398 0.1368  0.0234  684  GLU B CD  
2885 O OE1 . GLU B 434 ? 1.2895 1.3617 1.4190 -0.0540 0.1441  0.0122  684  GLU B OE1 
2886 O OE2 . GLU B 434 ? 1.2457 1.3492 1.3408 -0.0207 0.1370  0.0420  684  GLU B OE2 
2887 N N   . LEU B 435 ? 0.7004 0.8468 0.7794 -0.0491 0.0931  -0.0143 685  LEU B N   
2888 C CA  . LEU B 435 ? 0.7997 0.9632 0.8636 -0.0393 0.0987  -0.0075 685  LEU B CA  
2889 C C   . LEU B 435 ? 0.8581 1.0367 0.8973 -0.0212 0.1008  0.0123  685  LEU B C   
2890 O O   . LEU B 435 ? 0.9693 1.1624 0.9998 -0.0181 0.0845  0.0086  685  LEU B O   
2891 C CB  . LEU B 435 ? 0.7015 0.8821 0.7605 -0.0444 0.0804  -0.0267 685  LEU B CB  
2892 C CG  . LEU B 435 ? 0.6923 0.8631 0.7744 -0.0575 0.0733  -0.0458 685  LEU B CG  
2893 C CD1 . LEU B 435 ? 0.7978 0.9823 0.8740 -0.0588 0.0578  -0.0612 685  LEU B CD1 
2894 C CD2 . LEU B 435 ? 0.7223 0.8860 0.8263 -0.0611 0.0928  -0.0458 685  LEU B CD2 
2895 N N   . ASP B 436 ? 1.0139 1.1899 1.0422 -0.0085 0.1218  0.0332  686  ASP B N   
2896 C CA  . ASP B 436 ? 1.0939 1.2885 1.0937 0.0138  0.1230  0.0552  686  ASP B CA  
2897 C C   . ASP B 436 ? 1.0572 1.2664 1.0317 0.0226  0.1326  0.0627  686  ASP B C   
2898 O O   . ASP B 436 ? 1.1382 1.3251 1.1161 0.0218  0.1583  0.0731  686  ASP B O   
2899 C CB  . ASP B 436 ? 1.2552 1.4258 1.2605 0.0261  0.1433  0.0812  686  ASP B CB  
2900 C CG  . ASP B 436 ? 1.2198 1.4146 1.2025 0.0507  0.1346  0.1004  686  ASP B CG  
2901 O OD1 . ASP B 436 ? 1.1150 1.3307 1.1025 0.0488  0.1120  0.0868  686  ASP B OD1 
2902 O OD2 . ASP B 436 ? 1.4161 1.6098 1.3764 0.0727  0.1509  0.1289  686  ASP B OD2 
2903 N N   . PHE B 437 ? 1.1407 1.3877 1.0909 0.0294  0.1142  0.0547  687  PHE B N   
2904 C CA  . PHE B 437 ? 1.1117 1.3772 1.0358 0.0348  0.1213  0.0556  687  PHE B CA  
2905 C C   . PHE B 437 ? 1.1115 1.4246 1.0044 0.0491  0.1015  0.0529  687  PHE B C   
2906 O O   . PHE B 437 ? 1.1094 1.4427 1.0108 0.0471  0.0798  0.0389  687  PHE B O   
2907 C CB  . PHE B 437 ? 1.0371 1.2988 0.9806 0.0140  0.1200  0.0282  687  PHE B CB  
2908 C CG  . PHE B 437 ? 1.0413 1.3177 0.9997 0.0012  0.0942  0.0000  687  PHE B CG  
2909 C CD1 . PHE B 437 ? 1.0366 1.2904 1.0235 -0.0113 0.0861  -0.0096 687  PHE B CD1 
2910 C CD2 . PHE B 437 ? 1.0896 1.4010 1.0320 0.0012  0.0807  -0.0177 687  PHE B CD2 
2911 C CE1 . PHE B 437 ? 1.0268 1.2877 1.0230 -0.0219 0.0663  -0.0322 687  PHE B CE1 
2912 C CE2 . PHE B 437 ? 1.0291 1.3478 0.9866 -0.0112 0.0624  -0.0433 687  PHE B CE2 
2913 C CZ  . PHE B 437 ? 0.9499 1.2408 0.9328 -0.0219 0.0560  -0.0485 687  PHE B CZ  
2914 N N   . SER B 438 ? 1.1658 1.4983 1.0228 0.0626  0.1105  0.0643  688  SER B N   
2915 C CA  . SER B 438 ? 1.1667 1.5528 0.9916 0.0752  0.0919  0.0569  688  SER B CA  
2916 C C   . SER B 438 ? 1.2183 1.6214 1.0292 0.0644  0.0961  0.0363  688  SER B C   
2917 O O   . SER B 438 ? 1.3702 1.7516 1.1694 0.0643  0.1203  0.0484  688  SER B O   
2918 C CB  . SER B 438 ? 1.3014 1.7029 1.0868 0.1072  0.0968  0.0925  688  SER B CB  
2919 O OG  . SER B 438 ? 1.3806 1.7635 1.1353 0.1161  0.1238  0.1152  688  SER B OG  
2920 N N   . LEU B 439 ? 1.1409 1.5812 0.9559 0.0541  0.0758  0.0035  689  LEU B N   
2921 C CA  . LEU B 439 ? 1.2621 1.7206 1.0681 0.0425  0.0801  -0.0207 689  LEU B CA  
2922 C C   . LEU B 439 ? 1.3031 1.8238 1.0761 0.0522  0.0641  -0.0354 689  LEU B C   
2923 O O   . LEU B 439 ? 1.3081 1.8601 1.0822 0.0601  0.0435  -0.0402 689  LEU B O   
2924 C CB  . LEU B 439 ? 1.2897 1.7312 1.1385 0.0169  0.0751  -0.0533 689  LEU B CB  
2925 C CG  . LEU B 439 ? 1.1449 1.6142 1.0096 0.0065  0.0535  -0.0852 689  LEU B CG  
2926 C CD1 . LEU B 439 ? 1.0895 1.5346 0.9896 -0.0153 0.0555  -0.1117 689  LEU B CD1 
2927 C CD2 . LEU B 439 ? 1.2501 1.7175 1.1260 0.0123  0.0391  -0.0763 689  LEU B CD2 
2928 N N   . PRO B 440 ? 1.3347 1.8777 1.0793 0.0514  0.0735  -0.0451 690  PRO B N   
2929 C CA  . PRO B 440 ? 1.2237 1.8324 0.9368 0.0585  0.0577  -0.0651 690  PRO B CA  
2930 C C   . PRO B 440 ? 1.3038 1.9370 1.0523 0.0367  0.0413  -0.1111 690  PRO B C   
2931 O O   . PRO B 440 ? 1.3179 1.9153 1.1073 0.0156  0.0464  -0.1283 690  PRO B O   
2932 C CB  . PRO B 440 ? 1.2480 1.8640 0.9246 0.0585  0.0778  -0.0655 690  PRO B CB  
2933 C CG  . PRO B 440 ? 1.3117 1.8653 0.9964 0.0573  0.1056  -0.0368 690  PRO B CG  
2934 C CD  . PRO B 440 ? 1.2622 1.7743 1.0021 0.0439  0.1006  -0.0396 690  PRO B CD  
2935 N N   . SER B 441 ? 1.2861 1.9822 1.0189 0.0430  0.0220  -0.1315 691  SER B N   
2936 C CA  . SER B 441 ? 1.2103 1.9338 0.9744 0.0206  0.0121  -0.1800 691  SER B CA  
2937 C C   . SER B 441 ? 1.3164 2.0419 1.0793 0.0025  0.0279  -0.2083 691  SER B C   
2938 O O   . SER B 441 ? 1.3833 2.1003 1.1157 0.0087  0.0441  -0.1923 691  SER B O   
2939 C CB  . SER B 441 ? 1.2692 2.0669 1.0206 0.0307  -0.0111 -0.2000 691  SER B CB  
2940 O OG  . SER B 441 ? 1.2739 2.1263 0.9766 0.0432  -0.0128 -0.2043 691  SER B OG  
2941 N N   . SER B 442 ? 1.2260 1.9603 1.0245 -0.0206 0.0264  -0.2516 692  SER B N   
2942 C CA  . SER B 442 ? 1.2949 2.0233 1.1061 -0.0406 0.0435  -0.2827 692  SER B CA  
2943 C C   . SER B 442 ? 1.2160 1.8796 1.0433 -0.0449 0.0629  -0.2615 692  SER B C   
2944 O O   . SER B 442 ? 1.2551 1.9125 1.0875 -0.0561 0.0800  -0.2789 692  SER B O   
2945 C CB  . SER B 442 ? 1.2483 2.0356 1.0160 -0.0366 0.0466  -0.2998 692  SER B CB  
2946 O OG  . SER B 442 ? 1.1850 1.9665 0.9049 -0.0154 0.0539  -0.2593 692  SER B OG  
2947 N N   . ALA B 443 ? 1.2970 1.9152 1.1355 -0.0365 0.0609  -0.2270 693  ALA B N   
2948 C CA  . ALA B 443 ? 1.2139 1.7760 1.0725 -0.0401 0.0769  -0.2088 693  ALA B CA  
2949 C C   . ALA B 443 ? 1.0800 1.5999 0.9806 -0.0478 0.0691  -0.2072 693  ALA B C   
2950 O O   . ALA B 443 ? 1.1213 1.6333 1.0208 -0.0394 0.0573  -0.1877 693  ALA B O   
2951 C CB  . ALA B 443 ? 1.2598 1.8069 1.0873 -0.0221 0.0866  -0.1673 693  ALA B CB  
2952 N N   . SER B 444 ? 0.9863 1.4793 0.9225 -0.0625 0.0761  -0.2272 694  SER B N   
2953 C CA  . SER B 444 ? 1.0612 1.5122 1.0319 -0.0682 0.0695  -0.2244 694  SER B CA  
2954 C C   . SER B 444 ? 1.1446 1.5560 1.1258 -0.0623 0.0745  -0.1958 694  SER B C   
2955 O O   . SER B 444 ? 1.1384 1.5445 1.1193 -0.0611 0.0890  -0.1907 694  SER B O   
2956 C CB  . SER B 444 ? 1.0443 1.4822 1.0475 -0.0829 0.0752  -0.2556 694  SER B CB  
2957 O OG  . SER B 444 ? 1.0426 1.4912 1.0478 -0.0872 0.0911  -0.2711 694  SER B OG  
2958 N N   . TYR B 445 ? 1.0659 1.4509 1.0580 -0.0602 0.0640  -0.1802 695  TYR B N   
2959 C CA  . TYR B 445 ? 0.9349 1.2869 0.9384 -0.0559 0.0675  -0.1562 695  TYR B CA  
2960 C C   . TYR B 445 ? 0.9271 1.2453 0.9651 -0.0632 0.0623  -0.1642 695  TYR B C   
2961 O O   . TYR B 445 ? 0.9264 1.2357 0.9717 -0.0680 0.0523  -0.1746 695  TYR B O   
2962 C CB  . TYR B 445 ? 0.8901 1.2391 0.8778 -0.0468 0.0607  -0.1315 695  TYR B CB  
2963 C CG  . TYR B 445 ? 0.9000 1.2184 0.8989 -0.0436 0.0685  -0.1090 695  TYR B CG  
2964 C CD1 . TYR B 445 ? 1.0129 1.3254 1.0150 -0.0426 0.0865  -0.1026 695  TYR B CD1 
2965 C CD2 . TYR B 445 ? 0.8868 1.1835 0.8949 -0.0434 0.0604  -0.0971 695  TYR B CD2 
2966 C CE1 . TYR B 445 ? 1.0863 1.3728 1.1040 -0.0422 0.0966  -0.0868 695  TYR B CE1 
2967 C CE2 . TYR B 445 ? 0.9570 1.2286 0.9784 -0.0427 0.0693  -0.0814 695  TYR B CE2 
2968 C CZ  . TYR B 445 ? 0.9960 1.2633 1.0239 -0.0425 0.0876  -0.0771 695  TYR B CZ  
2969 O OH  . TYR B 445 ? 0.9785 1.2227 1.0249 -0.0443 0.0993  -0.0659 695  TYR B OH  
2970 N N   . THR B 446 ? 0.8701 1.1707 0.9291 -0.0631 0.0701  -0.1597 696  THR B N   
2971 C CA  . THR B 446 ? 0.8503 1.1238 0.9414 -0.0658 0.0630  -0.1651 696  THR B CA  
2972 C C   . THR B 446 ? 0.9181 1.1756 1.0219 -0.0632 0.0639  -0.1484 696  THR B C   
2973 O O   . THR B 446 ? 0.9267 1.1880 1.0422 -0.0630 0.0778  -0.1469 696  THR B O   
2974 C CB  . THR B 446 ? 0.9253 1.2007 1.0410 -0.0685 0.0710  -0.1853 696  THR B CB  
2975 O OG1 . THR B 446 ? 0.9541 1.2467 1.0587 -0.0732 0.0745  -0.2043 696  THR B OG1 
2976 C CG2 . THR B 446 ? 0.8438 1.0931 0.9903 -0.0666 0.0604  -0.1890 696  THR B CG2 
2977 N N   . TYR B 447 ? 0.8721 1.1123 0.9748 -0.0628 0.0515  -0.1384 697  TYR B N   
2978 C CA  . TYR B 447 ? 0.7396 0.9661 0.8564 -0.0626 0.0518  -0.1269 697  TYR B CA  
2979 C C   . TYR B 447 ? 0.7041 0.9135 0.8426 -0.0632 0.0364  -0.1341 697  TYR B C   
2980 O O   . TYR B 447 ? 0.7425 0.9387 0.8694 -0.0634 0.0236  -0.1337 697  TYR B O   
2981 C CB  . TYR B 447 ? 0.6927 0.9149 0.7883 -0.0611 0.0518  -0.1093 697  TYR B CB  
2982 C CG  . TYR B 447 ? 0.7193 0.9266 0.8311 -0.0632 0.0557  -0.1005 697  TYR B CG  
2983 C CD1 . TYR B 447 ? 0.6881 0.8796 0.8064 -0.0665 0.0417  -0.1015 697  TYR B CD1 
2984 C CD2 . TYR B 447 ? 0.7187 0.9272 0.8391 -0.0631 0.0759  -0.0929 697  TYR B CD2 
2985 C CE1 . TYR B 447 ? 0.7139 0.8959 0.8487 -0.0705 0.0459  -0.0982 697  TYR B CE1 
2986 C CE2 . TYR B 447 ? 0.6904 0.8859 0.8308 -0.0676 0.0830  -0.0893 697  TYR B CE2 
2987 C CZ  . TYR B 447 ? 0.7756 0.9603 0.9243 -0.0717 0.0669  -0.0936 697  TYR B CZ  
2988 O OH  . TYR B 447 ? 0.7320 0.9076 0.9021 -0.0782 0.0746  -0.0946 697  TYR B OH  
2989 N N   . ARG B 448 ? 0.5869 0.7979 0.7565 -0.0627 0.0382  -0.1410 698  ARG B N   
2990 C CA  . ARG B 448 ? 0.6741 0.8757 0.8651 -0.0592 0.0214  -0.1482 698  ARG B CA  
2991 C C   . ARG B 448 ? 0.6813 0.8860 0.8952 -0.0614 0.0198  -0.1483 698  ARG B C   
2992 O O   . ARG B 448 ? 0.6202 0.8373 0.8562 -0.0650 0.0354  -0.1530 698  ARG B O   
2993 C CB  . ARG B 448 ? 0.5890 0.7973 0.8049 -0.0541 0.0218  -0.1630 698  ARG B CB  
2994 C CG  . ARG B 448 ? 0.8058 1.0088 1.0049 -0.0534 0.0236  -0.1681 698  ARG B CG  
2995 C CD  . ARG B 448 ? 0.7791 0.9885 1.0075 -0.0491 0.0293  -0.1840 698  ARG B CD  
2996 N NE  . ARG B 448 ? 0.8032 1.0115 1.0661 -0.0400 0.0172  -0.1877 698  ARG B NE  
2997 C CZ  . ARG B 448 ? 0.7825 0.9728 1.0475 -0.0297 -0.0001 -0.1844 698  ARG B CZ  
2998 N NH1 . ARG B 448 ? 0.7015 0.8681 0.9370 -0.0296 -0.0035 -0.1777 698  ARG B NH1 
2999 N NH2 . ARG B 448 ? 0.7266 0.9234 1.0229 -0.0186 -0.0134 -0.1881 698  ARG B NH2 
3000 N N   . ARG B 449 ? 0.6520 0.8455 0.8606 -0.0605 0.0029  -0.1453 699  ARG B N   
3001 C CA  . ARG B 449 ? 0.7367 0.9372 0.9686 -0.0637 -0.0014 -0.1508 699  ARG B CA  
3002 C C   . ARG B 449 ? 0.6023 0.7973 0.8323 -0.0565 -0.0269 -0.1539 699  ARG B C   
3003 O O   . ARG B 449 ? 0.6738 0.8500 0.8761 -0.0510 -0.0371 -0.1463 699  ARG B O   
3004 C CB  . ARG B 449 ? 0.5746 0.7678 0.7937 -0.0729 0.0104  -0.1412 699  ARG B CB  
3005 C CG  . ARG B 449 ? 0.7373 0.9342 0.9582 -0.0771 0.0374  -0.1347 699  ARG B CG  
3006 C CD  . ARG B 449 ? 0.6303 0.8431 0.8917 -0.0807 0.0517  -0.1486 699  ARG B CD  
3007 N NE  . ARG B 449 ? 0.7953 1.0043 1.0541 -0.0852 0.0820  -0.1392 699  ARG B NE  
3008 C CZ  . ARG B 449 ? 0.7711 0.9814 1.0101 -0.0812 0.0962  -0.1305 699  ARG B CZ  
3009 N NH1 . ARG B 449 ? 0.7191 0.9363 0.9444 -0.0752 0.0839  -0.1340 699  ARG B NH1 
3010 N NH2 . ARG B 449 ? 0.7885 0.9925 1.0201 -0.0829 0.1245  -0.1186 699  ARG B NH2 
3011 N N   . GLN B 450 ? 0.7227 0.9349 0.9820 -0.0562 -0.0359 -0.1661 700  GLN B N   
3012 C CA  . GLN B 450 ? 0.7533 0.9652 1.0063 -0.0483 -0.0616 -0.1684 700  GLN B CA  
3013 C C   . GLN B 450 ? 0.6921 0.9021 0.9339 -0.0597 -0.0617 -0.1686 700  GLN B C   
3014 O O   . GLN B 450 ? 0.8118 1.0404 1.0838 -0.0697 -0.0515 -0.1815 700  GLN B O   
3015 C CB  . GLN B 450 ? 0.6835 0.9246 0.9787 -0.0380 -0.0760 -0.1854 700  GLN B CB  
3016 C CG  . GLN B 450 ? 0.8024 1.0417 1.1083 -0.0233 -0.0795 -0.1849 700  GLN B CG  
3017 C CD  . GLN B 450 ? 0.9423 1.1873 1.2526 -0.0029 -0.1077 -0.1860 700  GLN B CD  
3018 O OE1 . GLN B 450 ? 0.7835 1.0022 1.0541 0.0059  -0.1205 -0.1708 700  GLN B OE1 
3019 N NE2 . GLN B 450 ? 1.0091 1.2889 1.3681 0.0058  -0.1167 -0.2036 700  GLN B NE2 
3020 N N   . LEU B 451 ? 0.7347 0.9207 0.9354 -0.0596 -0.0699 -0.1563 701  LEU B N   
3021 C CA  . LEU B 451 ? 0.8061 0.9867 0.9930 -0.0711 -0.0682 -0.1568 701  LEU B CA  
3022 C C   . LEU B 451 ? 0.7319 0.9279 0.9208 -0.0666 -0.0919 -0.1686 701  LEU B C   
3023 O O   . LEU B 451 ? 0.7523 0.9382 0.9153 -0.0532 -0.1118 -0.1615 701  LEU B O   
3024 C CB  . LEU B 451 ? 0.8209 0.9703 0.9646 -0.0743 -0.0635 -0.1402 701  LEU B CB  
3025 C CG  . LEU B 451 ? 0.6168 0.7571 0.7542 -0.0753 -0.0456 -0.1297 701  LEU B CG  
3026 C CD1 . LEU B 451 ? 0.7181 0.8348 0.8201 -0.0795 -0.0417 -0.1182 701  LEU B CD1 
3027 C CD2 . LEU B 451 ? 0.7009 0.8556 0.8647 -0.0822 -0.0245 -0.1318 701  LEU B CD2 
3028 N N   . GLN B 452 ? 0.6850 0.9058 0.9039 -0.0774 -0.0886 -0.1870 702  GLN B N   
3029 C CA  . GLN B 452 ? 0.7691 1.0177 0.9977 -0.0737 -0.1121 -0.2048 702  GLN B CA  
3030 C C   . GLN B 452 ? 0.8588 1.1017 1.0662 -0.0879 -0.1106 -0.2103 702  GLN B C   
3031 O O   . GLN B 452 ? 0.8465 1.0796 1.0632 -0.1047 -0.0856 -0.2119 702  GLN B O   
3032 C CB  . GLN B 452 ? 0.8076 1.0985 1.0967 -0.0768 -0.1097 -0.2307 702  GLN B CB  
3033 C CG  . GLN B 452 ? 0.7959 1.1277 1.1019 -0.0708 -0.1379 -0.2538 702  GLN B CG  
3034 C CD  . GLN B 452 ? 0.8676 1.2453 1.2417 -0.0769 -0.1322 -0.2845 702  GLN B CD  
3035 O OE1 . GLN B 452 ? 0.8289 1.2062 1.2349 -0.0960 -0.1014 -0.2949 702  GLN B OE1 
3036 N NE2 . GLN B 452 ? 0.9554 1.3723 1.3536 -0.0598 -0.1604 -0.2991 702  GLN B NE2 
3037 N N   . ASN B 453 ? 0.8698 1.1178 1.0478 -0.0799 -0.1361 -0.2124 703  ASN B N   
3038 C CA  . ASN B 453 ? 0.9210 1.1660 1.0757 -0.0936 -0.1361 -0.2206 703  ASN B CA  
3039 C C   . ASN B 453 ? 0.9455 1.2335 1.1478 -0.1079 -0.1335 -0.2542 703  ASN B C   
3040 O O   . ASN B 453 ? 1.0576 1.3868 1.2887 -0.0987 -0.1538 -0.2727 703  ASN B O   
3041 C CB  . ASN B 453 ? 0.9820 1.2180 1.0835 -0.0792 -0.1634 -0.2111 703  ASN B CB  
3042 C CG  . ASN B 453 ? 1.0857 1.3135 1.1543 -0.0940 -0.1613 -0.2180 703  ASN B CG  
3043 O OD1 . ASN B 453 ? 1.1314 1.3524 1.2151 -0.1148 -0.1370 -0.2263 703  ASN B OD1 
3044 N ND2 . ASN B 453 ? 1.0218 1.2485 1.0436 -0.0821 -0.1854 -0.2137 703  ASN B ND2 
3045 N N   . PRO B 454 ? 0.9483 1.2294 1.1649 -0.1302 -0.1074 -0.2646 704  PRO B N   
3046 C CA  . PRO B 454 ? 0.9091 1.2297 1.1753 -0.1469 -0.1003 -0.3009 704  PRO B CA  
3047 C C   . PRO B 454 ? 1.0740 1.4373 1.3336 -0.1426 -0.1334 -0.3256 704  PRO B C   
3048 O O   . PRO B 454 ? 1.1501 1.5626 1.4581 -0.1441 -0.1424 -0.3558 704  PRO B O   
3049 C CB  . PRO B 454 ? 0.8483 1.1412 1.1140 -0.1689 -0.0674 -0.3014 704  PRO B CB  
3050 C CG  . PRO B 454 ? 0.8239 1.0717 1.0642 -0.1620 -0.0512 -0.2661 704  PRO B CG  
3051 C CD  . PRO B 454 ? 0.8684 1.1068 1.0654 -0.1404 -0.0798 -0.2450 704  PRO B CD  
3052 N N   . ALA B 455 ? 1.0821 1.4299 1.2827 -0.1372 -0.1512 -0.3146 705  ALA B N   
3053 C CA  . ALA B 455 ? 0.9442 1.3308 1.1241 -0.1254 -0.1881 -0.3303 705  ALA B CA  
3054 C C   . ALA B 455 ? 1.1116 1.4976 1.2700 -0.0935 -0.2169 -0.3071 705  ALA B C   
3055 O O   . ALA B 455 ? 1.2838 1.6238 1.4134 -0.0830 -0.2094 -0.2740 705  ALA B O   
3056 C CB  . ALA B 455 ? 0.8970 1.2642 1.0173 -0.1330 -0.1920 -0.3275 705  ALA B CB  
3057 N N   . ASN B 456 ? 1.1167 1.5560 1.2926 -0.0777 -0.2491 -0.3264 706  ASN B N   
3058 C CA  . ASN B 456 ? 1.2561 1.7004 1.4245 -0.0450 -0.2756 -0.3074 706  ASN B CA  
3059 C C   . ASN B 456 ? 1.1094 1.5358 1.3199 -0.0438 -0.2539 -0.2962 706  ASN B C   
3060 O O   . ASN B 456 ? 1.0703 1.4455 1.2498 -0.0371 -0.2418 -0.2641 706  ASN B O   
3061 C CB  . ASN B 456 ? 1.2711 1.6693 1.3584 -0.0248 -0.2899 -0.2707 706  ASN B CB  
3062 C CG  . ASN B 456 ? 1.2956 1.7004 1.3724 0.0122  -0.3192 -0.2522 706  ASN B CG  
3063 O OD1 . ASN B 456 ? 1.2738 1.7069 1.4055 0.0227  -0.3238 -0.2608 706  ASN B OD1 
3064 N ND2 . ASN B 456 ? 1.3811 1.7568 1.3872 0.0327  -0.3365 -0.2258 706  ASN B ND2 
3065 N N   . GLU B 457 ? 1.0874 1.5574 1.3692 -0.0515 -0.2474 -0.3250 707  GLU B N   
3066 C CA  . GLU B 457 ? 1.0475 1.5036 1.3704 -0.0535 -0.2230 -0.3182 707  GLU B CA  
3067 C C   . GLU B 457 ? 1.0509 1.4957 1.3645 -0.0241 -0.2397 -0.2949 707  GLU B C   
3068 O O   . GLU B 457 ? 1.0035 1.4300 1.3399 -0.0248 -0.2190 -0.2856 707  GLU B O   
3069 C CB  . GLU B 457 ? 1.0255 1.5322 1.4274 -0.0689 -0.2109 -0.3575 707  GLU B CB  
3070 C CG  . GLU B 457 ? 1.1165 1.6351 1.5363 -0.0993 -0.1904 -0.3851 707  GLU B CG  
3071 C CD  . GLU B 457 ? 1.3588 1.9332 1.8595 -0.1144 -0.1804 -0.4298 707  GLU B CD  
3072 O OE1 . GLU B 457 ? 1.3671 1.9500 1.9136 -0.1108 -0.1684 -0.4331 707  GLU B OE1 
3073 O OE2 . GLU B 457 ? 1.2977 1.9084 1.8180 -0.1312 -0.1827 -0.4644 707  GLU B OE2 
3074 N N   . GLN B 458 ? 1.0625 1.5166 1.3423 0.0024  -0.2746 -0.2851 708  GLN B N   
3075 C CA  . GLN B 458 ? 1.0982 1.5355 1.3671 0.0325  -0.2885 -0.2608 708  GLN B CA  
3076 C C   . GLN B 458 ? 1.1518 1.5189 1.3570 0.0366  -0.2757 -0.2225 708  GLN B C   
3077 O O   . GLN B 458 ? 1.2023 1.5463 1.3923 0.0607  -0.2835 -0.2006 708  GLN B O   
3078 C CB  . GLN B 458 ? 1.1349 1.6140 1.3983 0.0633  -0.3311 -0.2658 708  GLN B CB  
3079 C CG  . GLN B 458 ? 1.1519 1.7052 1.4933 0.0672  -0.3458 -0.3035 708  GLN B CG  
3080 C CD  . GLN B 458 ? 1.2568 1.8665 1.5912 0.0917  -0.3905 -0.3173 708  GLN B CD  
3081 O OE1 . GLN B 458 ? 1.1983 1.8157 1.4897 0.0852  -0.4030 -0.3223 708  GLN B OE1 
3082 N NE2 . GLN B 458 ? 1.2466 1.8983 1.6229 0.1210  -0.4152 -0.3242 708  GLN B NE2 
3083 N N   . GLU B 459 ? 1.1323 1.4660 1.3045 0.0134  -0.2545 -0.2160 709  GLU B N   
3084 C CA  . GLU B 459 ? 1.0225 1.2941 1.1442 0.0120  -0.2374 -0.1855 709  GLU B CA  
3085 C C   . GLU B 459 ? 0.9858 1.2419 1.1378 -0.0053 -0.2051 -0.1850 709  GLU B C   
3086 O O   . GLU B 459 ? 0.8901 1.1416 1.0476 -0.0285 -0.1839 -0.1918 709  GLU B O   
3087 C CB  . GLU B 459 ? 1.1248 1.3722 1.1923 -0.0010 -0.2347 -0.1796 709  GLU B CB  
3088 C CG  . GLU B 459 ? 1.2020 1.4365 1.2110 0.0204  -0.2602 -0.1639 709  GLU B CG  
3089 C CD  . GLU B 459 ? 1.3258 1.5339 1.2805 0.0046  -0.2529 -0.1596 709  GLU B CD  
3090 O OE1 . GLU B 459 ? 1.1975 1.4101 1.1696 -0.0224 -0.2331 -0.1750 709  GLU B OE1 
3091 O OE2 . GLU B 459 ? 1.3382 1.5188 1.2328 0.0196  -0.2646 -0.1402 709  GLU B OE2 
3092 N N   . LYS B 460 ? 0.9362 1.1845 1.1071 0.0074  -0.2008 -0.1767 710  LYS B N   
3093 C CA  . LYS B 460 ? 0.8605 1.0960 1.0539 -0.0056 -0.1721 -0.1751 710  LYS B CA  
3094 C C   . LYS B 460 ? 0.8859 1.0756 1.0434 0.0015  -0.1630 -0.1517 710  LYS B C   
3095 O O   . LYS B 460 ? 0.8623 1.0397 1.0092 0.0225  -0.1759 -0.1413 710  LYS B O   
3096 C CB  . LYS B 460 ? 0.8383 1.1101 1.0929 -0.0017 -0.1695 -0.1929 710  LYS B CB  
3097 C CG  . LYS B 460 ? 0.8223 1.1371 1.1217 -0.0166 -0.1667 -0.2206 710  LYS B CG  
3098 C CD  . LYS B 460 ? 0.9243 1.2652 1.2834 -0.0203 -0.1509 -0.2375 710  LYS B CD  
3099 C CE  . LYS B 460 ? 1.0464 1.4218 1.4423 0.0021  -0.1744 -0.2495 710  LYS B CE  
3100 N NZ  . LYS B 460 ? 0.9388 1.3456 1.3998 -0.0052 -0.1570 -0.2724 710  LYS B NZ  
3101 N N   . ILE B 461 ? 0.8809 1.0468 1.0224 -0.0154 -0.1399 -0.1445 711  ILE B N   
3102 C CA  . ILE B 461 ? 0.8473 0.9743 0.9582 -0.0132 -0.1286 -0.1278 711  ILE B CA  
3103 C C   . ILE B 461 ? 0.7998 0.9323 0.9371 -0.0201 -0.1078 -0.1317 711  ILE B C   
3104 O O   . ILE B 461 ? 0.8466 0.9991 1.0070 -0.0328 -0.0952 -0.1403 711  ILE B O   
3105 C CB  . ILE B 461 ? 0.7893 0.8870 0.8559 -0.0255 -0.1213 -0.1178 711  ILE B CB  
3106 C CG1 . ILE B 461 ? 0.9245 0.9854 0.9477 -0.0129 -0.1293 -0.1024 711  ILE B CG1 
3107 C CG2 . ILE B 461 ? 0.8498 0.9373 0.9161 -0.0403 -0.0975 -0.1154 711  ILE B CG2 
3108 C CD1 . ILE B 461 ? 1.1381 1.2084 1.1585 0.0091  -0.1544 -0.1002 711  ILE B CD1 
3109 N N   . PRO B 462 ? 0.7806 0.8956 0.9150 -0.0119 -0.1020 -0.1263 712  PRO B N   
3110 C CA  . PRO B 462 ? 0.7312 0.8533 0.8842 -0.0196 -0.0819 -0.1317 712  PRO B CA  
3111 C C   . PRO B 462 ? 0.6914 0.7990 0.8173 -0.0343 -0.0662 -0.1257 712  PRO B C   
3112 O O   . PRO B 462 ? 0.7238 0.8046 0.8171 -0.0360 -0.0668 -0.1172 712  PRO B O   
3113 C CB  . PRO B 462 ? 0.6660 0.7740 0.8257 -0.0057 -0.0817 -0.1310 712  PRO B CB  
3114 C CG  . PRO B 462 ? 0.7103 0.7864 0.8364 0.0056  -0.0942 -0.1177 712  PRO B CG  
3115 C CD  . PRO B 462 ? 0.8970 0.9868 1.0146 0.0065  -0.1126 -0.1166 712  PRO B CD  
3116 N N   . PHE B 463 ? 0.7138 0.8402 0.8537 -0.0439 -0.0512 -0.1300 713  PHE B N   
3117 C CA  . PHE B 463 ? 0.6385 0.7597 0.7574 -0.0541 -0.0374 -0.1249 713  PHE B CA  
3118 C C   . PHE B 463 ? 0.7611 0.8975 0.8914 -0.0549 -0.0233 -0.1309 713  PHE B C   
3119 O O   . PHE B 463 ? 0.7667 0.9234 0.9191 -0.0555 -0.0154 -0.1354 713  PHE B O   
3120 C CB  . PHE B 463 ? 0.6790 0.8078 0.7960 -0.0630 -0.0321 -0.1206 713  PHE B CB  
3121 C CG  . PHE B 463 ? 0.6953 0.8243 0.7951 -0.0692 -0.0191 -0.1141 713  PHE B CG  
3122 C CD1 . PHE B 463 ? 0.6540 0.7669 0.7288 -0.0719 -0.0203 -0.1111 713  PHE B CD1 
3123 C CD2 . PHE B 463 ? 0.6610 0.8071 0.7701 -0.0713 -0.0047 -0.1111 713  PHE B CD2 
3124 C CE1 . PHE B 463 ? 0.5859 0.7065 0.6495 -0.0759 -0.0108 -0.1077 713  PHE B CE1 
3125 C CE2 . PHE B 463 ? 0.7305 0.8810 0.8226 -0.0727 0.0045  -0.1034 713  PHE B CE2 
3126 C CZ  . PHE B 463 ? 0.7382 0.8793 0.8096 -0.0747 -0.0002 -0.1029 713  PHE B CZ  
3127 N N   . HIS B 464 ? 0.8000 0.9269 0.9151 -0.0560 -0.0182 -0.1332 714  HIS B N   
3128 C CA  . HIS B 464 ? 0.7474 0.8913 0.8685 -0.0581 -0.0051 -0.1423 714  HIS B CA  
3129 C C   . HIS B 464 ? 0.7487 0.8981 0.8462 -0.0654 0.0016  -0.1413 714  HIS B C   
3130 O O   . HIS B 464 ? 0.7762 0.9085 0.8595 -0.0686 0.0001  -0.1433 714  HIS B O   
3131 C CB  . HIS B 464 ? 0.7688 0.9019 0.9022 -0.0527 -0.0040 -0.1528 714  HIS B CB  
3132 C CG  . HIS B 464 ? 0.8514 1.0038 0.9926 -0.0565 0.0107  -0.1667 714  HIS B CG  
3133 N ND1 . HIS B 464 ? 0.8911 1.0530 1.0596 -0.0520 0.0165  -0.1773 714  HIS B ND1 
3134 C CD2 . HIS B 464 ? 0.8797 1.0469 1.0053 -0.0645 0.0204  -0.1742 714  HIS B CD2 
3135 C CE1 . HIS B 464 ? 0.8904 1.0699 1.0570 -0.0583 0.0306  -0.1905 714  HIS B CE1 
3136 N NE2 . HIS B 464 ? 0.7867 0.9718 0.9265 -0.0655 0.0321  -0.1892 714  HIS B NE2 
3137 N N   . LEU B 465 ? 0.7495 0.9230 0.8434 -0.0671 0.0098  -0.1382 715  LEU B N   
3138 C CA  . LEU B 465 ? 0.6788 0.8675 0.7528 -0.0703 0.0141  -0.1377 715  LEU B CA  
3139 C C   . LEU B 465 ? 0.7625 0.9770 0.8358 -0.0708 0.0230  -0.1511 715  LEU B C   
3140 O O   . LEU B 465 ? 0.8940 1.1250 0.9713 -0.0678 0.0311  -0.1494 715  LEU B O   
3141 C CB  . LEU B 465 ? 0.6391 0.8362 0.7050 -0.0682 0.0168  -0.1215 715  LEU B CB  
3142 C CG  . LEU B 465 ? 0.6910 0.9098 0.7381 -0.0668 0.0192  -0.1188 715  LEU B CG  
3143 C CD1 . LEU B 465 ? 0.7314 0.9415 0.7720 -0.0726 0.0125  -0.1268 715  LEU B CD1 
3144 C CD2 . LEU B 465 ? 0.6503 0.8723 0.6920 -0.0611 0.0245  -0.0993 715  LEU B CD2 
3145 N N   . GLN B 466 ? 0.7668 0.9850 0.8355 -0.0760 0.0240  -0.1665 716  GLN B N   
3146 C CA  . GLN B 466 ? 0.7808 1.0270 0.8487 -0.0789 0.0326  -0.1851 716  GLN B CA  
3147 C C   . GLN B 466 ? 0.8130 1.0891 0.8629 -0.0813 0.0310  -0.1907 716  GLN B C   
3148 O O   . GLN B 466 ? 0.8307 1.0986 0.8802 -0.0872 0.0280  -0.1979 716  GLN B O   
3149 C CB  . GLN B 466 ? 0.7679 0.9968 0.8529 -0.0841 0.0380  -0.2048 716  GLN B CB  
3150 C CG  . GLN B 466 ? 0.8190 1.0766 0.9081 -0.0891 0.0497  -0.2285 716  GLN B CG  
3151 C CD  . GLN B 466 ? 0.9233 1.1935 1.0202 -0.0844 0.0564  -0.2267 716  GLN B CD  
3152 O OE1 . GLN B 466 ? 0.9056 1.1563 1.0173 -0.0783 0.0538  -0.2141 716  GLN B OE1 
3153 N NE2 . GLN B 466 ? 0.8606 1.1662 0.9479 -0.0877 0.0656  -0.2416 716  GLN B NE2 
3154 N N   . ILE B 467 ? 0.8542 1.1658 0.8890 -0.0758 0.0336  -0.1874 717  ILE B N   
3155 C CA  . ILE B 467 ? 0.8606 1.2104 0.8776 -0.0735 0.0291  -0.1917 717  ILE B CA  
3156 C C   . ILE B 467 ? 0.9620 1.3503 0.9739 -0.0776 0.0349  -0.2173 717  ILE B C   
3157 O O   . ILE B 467 ? 1.0544 1.4579 1.0559 -0.0729 0.0419  -0.2144 717  ILE B O   
3158 C CB  . ILE B 467 ? 0.8513 1.2124 0.8495 -0.0599 0.0268  -0.1639 717  ILE B CB  
3159 C CG1 . ILE B 467 ? 0.8050 1.1304 0.8114 -0.0589 0.0226  -0.1443 717  ILE B CG1 
3160 C CG2 . ILE B 467 ? 0.8857 1.2945 0.8645 -0.0527 0.0204  -0.1682 717  ILE B CG2 
3161 C CD1 . ILE B 467 ? 0.9842 1.3115 0.9782 -0.0463 0.0252  -0.1166 717  ILE B CD1 
3162 N N   . SER B 468 ? 0.9933 1.3976 1.0134 -0.0879 0.0342  -0.2449 718  SER B N   
3163 C CA  . SER B 468 ? 0.8576 1.3007 0.8769 -0.0952 0.0409  -0.2762 718  SER B CA  
3164 C C   . SER B 468 ? 0.8894 1.3910 0.8798 -0.0848 0.0333  -0.2748 718  SER B C   
3165 O O   . SER B 468 ? 0.8698 1.3787 0.8430 -0.0708 0.0238  -0.2482 718  SER B O   
3166 C CB  . SER B 468 ? 0.9206 1.3625 0.9619 -0.1114 0.0459  -0.3095 718  SER B CB  
3167 O OG  . SER B 468 ? 1.1720 1.5572 1.2351 -0.1177 0.0546  -0.3079 718  SER B OG  
3168 N N   . LYS B 469 ? 1.0374 1.5815 1.0219 -0.0909 0.0383  -0.3042 719  LYS B N   
3169 C CA  . LYS B 469 ? 0.9272 1.5320 0.8783 -0.0791 0.0302  -0.3044 719  LYS B CA  
3170 C C   . LYS B 469 ? 0.9546 1.5967 0.9039 -0.0736 0.0136  -0.3086 719  LYS B C   
3171 O O   . LYS B 469 ? 0.9410 1.5727 0.9184 -0.0861 0.0125  -0.3273 719  LYS B O   
3172 C CB  . LYS B 469 ? 0.8810 1.5269 0.8274 -0.0896 0.0392  -0.3416 719  LYS B CB  
3173 C CG  . LYS B 469 ? 1.0339 1.6582 0.9730 -0.0899 0.0554  -0.3345 719  LYS B CG  
3174 C CD  . LYS B 469 ? 1.0154 1.6786 0.9538 -0.1033 0.0669  -0.3763 719  LYS B CD  
3175 C CE  . LYS B 469 ? 1.0977 1.7417 1.0295 -0.1034 0.0849  -0.3699 719  LYS B CE  
3176 N NZ  . LYS B 469 ? 1.0988 1.7738 1.0366 -0.1195 0.0997  -0.4142 719  LYS B NZ  
3177 N N   . GLN B 470 ? 1.1662 1.2902 1.1091 0.0287  -0.1293 -0.1011 720  GLN B N   
3178 C CA  . GLN B 470 ? 1.1277 1.2677 1.0612 0.0170  -0.1149 -0.1008 720  GLN B CA  
3179 C C   . GLN B 470 ? 1.2221 1.3431 1.1333 0.0111  -0.1135 -0.0847 720  GLN B C   
3180 O O   . GLN B 470 ? 1.1733 1.2802 1.0996 0.0199  -0.1091 -0.0809 720  GLN B O   
3181 C CB  . GLN B 470 ? 1.0454 1.2052 1.0176 0.0233  -0.0970 -0.1150 720  GLN B CB  
3182 C CG  . GLN B 470 ? 1.0794 1.2555 1.0478 0.0131  -0.0828 -0.1170 720  GLN B CG  
3183 C CD  . GLN B 470 ? 1.1604 1.3348 1.1571 0.0197  -0.0683 -0.1180 720  GLN B CD  
3184 O OE1 . GLN B 470 ? 1.2049 1.3590 1.2016 0.0250  -0.0682 -0.1075 720  GLN B OE1 
3185 N NE2 . GLN B 470 ? 1.0190 1.2152 1.0405 0.0191  -0.0571 -0.1311 720  GLN B NE2 
3186 N N   . VAL B 471 ? 1.2067 1.3289 1.0822 -0.0046 -0.1171 -0.0756 721  VAL B N   
3187 C CA  . VAL B 471 ? 1.1169 1.2258 0.9717 -0.0126 -0.1135 -0.0618 721  VAL B CA  
3188 C C   . VAL B 471 ? 1.0556 1.1888 0.9177 -0.0199 -0.0943 -0.0697 721  VAL B C   
3189 O O   . VAL B 471 ? 1.0562 1.2164 0.9226 -0.0256 -0.0890 -0.0825 721  VAL B O   
3190 C CB  . VAL B 471 ? 1.0858 1.1792 0.8967 -0.0267 -0.1304 -0.0454 721  VAL B CB  
3191 C CG1 . VAL B 471 ? 1.1298 1.2001 0.9370 -0.0187 -0.1523 -0.0400 721  VAL B CG1 
3192 C CG2 . VAL B 471 ? 1.1648 1.2838 0.9521 -0.0441 -0.1288 -0.0489 721  VAL B CG2 
3193 N N   . ILE B 472 ? 1.0427 1.1672 0.9086 -0.0190 -0.0846 -0.0638 722  ILE B N   
3194 C CA  . ILE B 472 ? 1.1341 1.2786 1.0115 -0.0238 -0.0674 -0.0716 722  ILE B CA  
3195 C C   . ILE B 472 ? 1.0353 1.1737 0.8813 -0.0377 -0.0661 -0.0594 722  ILE B C   
3196 O O   . ILE B 472 ? 1.0467 1.1596 0.8801 -0.0361 -0.0716 -0.0451 722  ILE B O   
3197 C CB  . ILE B 472 ? 1.0813 1.2234 0.9958 -0.0102 -0.0560 -0.0769 722  ILE B CB  
3198 C CG1 . ILE B 472 ? 0.9862 1.1355 0.9039 -0.0155 -0.0425 -0.0771 722  ILE B CG1 
3199 C CG2 . ILE B 472 ? 0.9500 1.0654 0.8685 0.0010  -0.0631 -0.0670 722  ILE B CG2 
3200 C CD1 . ILE B 472 ? 1.0380 1.1842 0.9895 -0.0040 -0.0326 -0.0802 722  ILE B CD1 
3201 N N   . HIS B 473 ? 1.0591 1.2224 0.8937 -0.0516 -0.0591 -0.0663 723  HIS B N   
3202 C CA  . HIS B 473 ? 1.0539 1.2172 0.8594 -0.0672 -0.0563 -0.0569 723  HIS B CA  
3203 C C   . HIS B 473 ? 1.0186 1.1965 0.8460 -0.0660 -0.0395 -0.0664 723  HIS B C   
3204 O O   . HIS B 473 ? 1.0686 1.2718 0.9227 -0.0628 -0.0305 -0.0845 723  HIS B O   
3205 C CB  . HIS B 473 ? 1.0908 1.2752 0.8655 -0.0863 -0.0607 -0.0583 723  HIS B CB  
3206 C CG  . HIS B 473 ? 1.1847 1.3604 0.9427 -0.0870 -0.0777 -0.0527 723  HIS B CG  
3207 N ND1 . HIS B 473 ? 1.3260 1.4774 1.0478 -0.0963 -0.0943 -0.0327 723  HIS B ND1 
3208 C CD2 . HIS B 473 ? 1.1056 1.2928 0.8791 -0.0795 -0.0821 -0.0644 723  HIS B CD2 
3209 C CE1 . HIS B 473 ? 1.3230 1.4708 1.0383 -0.0944 -0.1087 -0.0322 723  HIS B CE1 
3210 N NE2 . HIS B 473 ? 1.1830 1.3531 0.9291 -0.0841 -0.1010 -0.0516 723  HIS B NE2 
3211 N N   . ALA B 474 ? 1.0403 1.2016 0.8576 -0.0682 -0.0366 -0.0548 724  ALA B N   
3212 C CA  . ALA B 474 ? 1.0236 1.1943 0.8606 -0.0663 -0.0225 -0.0619 724  ALA B CA  
3213 C C   . ALA B 474 ? 1.0039 1.1761 0.8125 -0.0823 -0.0197 -0.0542 724  ALA B C   
3214 O O   . ALA B 474 ? 1.0821 1.2290 0.8681 -0.0851 -0.0268 -0.0368 724  ALA B O   
3215 C CB  . ALA B 474 ? 0.8062 0.9546 0.6664 -0.0500 -0.0203 -0.0565 724  ALA B CB  
3216 N N   . GLU B 475 ? 0.9947 1.1976 0.8062 -0.0928 -0.0099 -0.0682 725  GLU B N   
3217 C CA  . GLU B 475 ? 1.0205 1.2288 0.8116 -0.1074 -0.0044 -0.0640 725  GLU B CA  
3218 C C   . GLU B 475 ? 0.9695 1.1598 0.7775 -0.0970 0.0016  -0.0593 725  GLU B C   
3219 O O   . GLU B 475 ? 1.0010 1.1980 0.8435 -0.0850 0.0089  -0.0710 725  GLU B O   
3220 C CB  . GLU B 475 ? 1.0658 1.3157 0.8625 -0.1195 0.0056  -0.0845 725  GLU B CB  
3221 C CG  . GLU B 475 ? 1.2931 1.5559 1.0538 -0.1424 0.0071  -0.0793 725  GLU B CG  
3222 C CD  . GLU B 475 ? 1.4566 1.7627 1.2299 -0.1526 0.0196  -0.1029 725  GLU B CD  
3223 O OE1 . GLU B 475 ? 1.4658 1.7772 1.2390 -0.1588 0.0274  -0.1046 725  GLU B OE1 
3224 O OE2 . GLU B 475 ? 1.4999 1.8360 1.2854 -0.1540 0.0214  -0.1213 725  GLU B OE2 
3225 N N   . ILE B 476 ? 1.0404 1.2072 0.8244 -0.1019 -0.0026 -0.0418 726  ILE B N   
3226 C CA  . ILE B 476 ? 1.0369 1.1829 0.8340 -0.0910 0.0008  -0.0351 726  ILE B CA  
3227 C C   . ILE B 476 ? 0.9395 1.0870 0.7195 -0.1034 0.0058  -0.0305 726  ILE B C   
3228 O O   . ILE B 476 ? 0.9478 1.1033 0.6987 -0.1213 0.0034  -0.0260 726  ILE B O   
3229 C CB  . ILE B 476 ? 1.0254 1.1374 0.8168 -0.0800 -0.0104 -0.0192 726  ILE B CB  
3230 C CG1 . ILE B 476 ? 1.0148 1.1106 0.7684 -0.0926 -0.0234 -0.0031 726  ILE B CG1 
3231 C CG2 . ILE B 476 ? 0.9160 1.0275 0.7296 -0.0662 -0.0138 -0.0254 726  ILE B CG2 
3232 C CD1 . ILE B 476 ? 1.0058 1.0679 0.7553 -0.0821 -0.0361 0.0110  726  ILE B CD1 
3233 N N   . GLN B 477 ? 0.9289 1.0693 0.7274 -0.0946 0.0126  -0.0316 727  GLN B N   
3234 C CA  . GLN B 477 ? 0.9416 1.0765 0.7268 -0.1025 0.0163  -0.0253 727  GLN B CA  
3235 C C   . GLN B 477 ? 0.9377 1.0390 0.7200 -0.0919 0.0104  -0.0095 727  GLN B C   
3236 O O   . GLN B 477 ? 1.0069 1.0990 0.8128 -0.0759 0.0117  -0.0110 727  GLN B O   
3237 C CB  . GLN B 477 ? 1.0176 1.1738 0.8279 -0.1012 0.0284  -0.0413 727  GLN B CB  
3238 C CG  . GLN B 477 ? 1.0716 1.2649 0.8835 -0.1146 0.0351  -0.0593 727  GLN B CG  
3239 C CD  . GLN B 477 ? 1.1595 1.3712 0.9959 -0.1136 0.0450  -0.0750 727  GLN B CD  
3240 O OE1 . GLN B 477 ? 1.2401 1.4358 1.0805 -0.1084 0.0468  -0.0685 727  GLN B OE1 
3241 N NE2 . GLN B 477 ? 1.1895 1.4356 1.0437 -0.1180 0.0507  -0.0969 727  GLN B NE2 
3242 N N   . HIS B 478 ? 0.9832 1.0675 0.7372 -0.1014 0.0034  0.0050  728  HIS B N   
3243 C CA  . HIS B 478 ? 0.8737 0.9280 0.6253 -0.0921 -0.0028 0.0180  728  HIS B CA  
3244 C C   . HIS B 478 ? 0.8589 0.9151 0.6247 -0.0878 0.0073  0.0142  728  HIS B C   
3245 O O   . HIS B 478 ? 0.8877 0.9528 0.6427 -0.1000 0.0121  0.0133  728  HIS B O   
3246 C CB  . HIS B 478 ? 0.9340 0.9688 0.6527 -0.1041 -0.0156 0.0343  728  HIS B CB  
3247 C CG  . HIS B 478 ? 0.9757 1.0041 0.6798 -0.1074 -0.0286 0.0401  728  HIS B CG  
3248 N ND1 . HIS B 478 ? 1.1545 1.1556 0.8561 -0.0978 -0.0432 0.0502  728  HIS B ND1 
3249 C CD2 . HIS B 478 ? 1.0263 1.0732 0.7183 -0.1192 -0.0299 0.0363  728  HIS B CD2 
3250 C CE1 . HIS B 478 ? 1.0623 1.0632 0.7508 -0.1032 -0.0538 0.0532  728  HIS B CE1 
3251 N NE2 . HIS B 478 ? 1.1253 1.1538 0.8065 -0.1165 -0.0458 0.0454  728  HIS B NE2 
3252 N N   . LEU B 479 ? 0.8943 0.9431 0.6841 -0.0713 0.0103  0.0119  729  LEU B N   
3253 C CA  . LEU B 479 ? 0.9100 0.9596 0.7145 -0.0662 0.0185  0.0088  729  LEU B CA  
3254 C C   . LEU B 479 ? 0.9008 0.9266 0.6943 -0.0627 0.0138  0.0209  729  LEU B C   
3255 O O   . LEU B 479 ? 0.8994 0.9249 0.7005 -0.0601 0.0197  0.0197  729  LEU B O   
3256 C CB  . LEU B 479 ? 0.8213 0.8769 0.6571 -0.0521 0.0239  0.0006  729  LEU B CB  
3257 C CG  . LEU B 479 ? 0.8872 0.9672 0.7415 -0.0535 0.0289  -0.0140 729  LEU B CG  
3258 C CD1 . LEU B 479 ? 0.7876 0.8684 0.6726 -0.0400 0.0318  -0.0189 729  LEU B CD1 
3259 C CD2 . LEU B 479 ? 0.9113 1.0124 0.7666 -0.0645 0.0358  -0.0248 729  LEU B CD2 
3260 N N   . GLY B 480 ? 0.8474 0.8536 0.6248 -0.0621 0.0022  0.0316  730  GLY B N   
3261 C CA  . GLY B 480 ? 0.8665 0.8506 0.6364 -0.0578 -0.0040 0.0413  730  GLY B CA  
3262 C C   . GLY B 480 ? 0.9004 0.8731 0.6863 -0.0410 -0.0073 0.0416  730  GLY B C   
3263 O O   . GLY B 480 ? 0.9397 0.9173 0.7378 -0.0340 -0.0080 0.0372  730  GLY B O   
3264 N N   . HIS B 481 ? 0.8397 0.7992 0.6261 -0.0350 -0.0090 0.0458  731  HIS B N   
3265 C CA  . HIS B 481 ? 0.8266 0.7778 0.6270 -0.0203 -0.0118 0.0451  731  HIS B CA  
3266 C C   . HIS B 481 ? 0.7598 0.7216 0.5787 -0.0129 0.0003  0.0400  731  HIS B C   
3267 O O   . HIS B 481 ? 0.7685 0.7326 0.5851 -0.0168 0.0061  0.0404  731  HIS B O   
3268 C CB  . HIS B 481 ? 0.7974 0.7276 0.5871 -0.0181 -0.0237 0.0518  731  HIS B CB  
3269 C CG  . HIS B 481 ? 0.9367 0.8522 0.7095 -0.0245 -0.0392 0.0585  731  HIS B CG  
3270 N ND1 . HIS B 481 ? 0.9604 0.8654 0.7385 -0.0157 -0.0514 0.0580  731  HIS B ND1 
3271 C CD2 . HIS B 481 ? 0.8772 0.7871 0.6278 -0.0396 -0.0455 0.0662  731  HIS B CD2 
3272 C CE1 . HIS B 481 ? 1.0590 0.9501 0.8190 -0.0246 -0.0659 0.0659  731  HIS B CE1 
3273 N NE2 . HIS B 481 ? 1.1779 1.0718 0.9196 -0.0400 -0.0624 0.0718  731  HIS B NE2 
3274 N N   . TRP B 482 ? 0.8025 0.7707 0.6394 -0.0032 0.0033  0.0357  732  TRP B N   
3275 C CA  . TRP B 482 ? 0.7284 0.7038 0.5812 0.0035  0.0122  0.0334  732  TRP B CA  
3276 C C   . TRP B 482 ? 0.7983 0.7632 0.6479 0.0100  0.0086  0.0362  732  TRP B C   
3277 O O   . TRP B 482 ? 0.8233 0.7780 0.6684 0.0140  -0.0010 0.0369  732  TRP B O   
3278 C CB  . TRP B 482 ? 0.7544 0.7406 0.6267 0.0098  0.0162  0.0289  732  TRP B CB  
3279 C CG  . TRP B 482 ? 0.6892 0.6848 0.5773 0.0123  0.0254  0.0279  732  TRP B CG  
3280 C CD1 . TRP B 482 ? 0.8156 0.8125 0.7031 0.0092  0.0302  0.0294  732  TRP B CD1 
3281 C CD2 . TRP B 482 ? 0.7082 0.7127 0.6150 0.0177  0.0296  0.0262  732  TRP B CD2 
3282 N NE1 . TRP B 482 ? 0.6986 0.7030 0.6026 0.0124  0.0359  0.0294  732  TRP B NE1 
3283 C CE2 . TRP B 482 ? 0.7196 0.7289 0.6352 0.0168  0.0359  0.0281  732  TRP B CE2 
3284 C CE3 . TRP B 482 ? 0.6651 0.6740 0.5824 0.0224  0.0280  0.0232  732  TRP B CE3 
3285 C CZ2 . TRP B 482 ? 0.6604 0.6778 0.5933 0.0193  0.0402  0.0290  732  TRP B CZ2 
3286 C CZ3 . TRP B 482 ? 0.7814 0.8002 0.7167 0.0249  0.0337  0.0229  732  TRP B CZ3 
3287 C CH2 . TRP B 482 ? 0.7217 0.7441 0.6638 0.0227  0.0395  0.0267  732  TRP B CH2 
3288 N N   . MET B 483 ? 0.7933 0.7614 0.6465 0.0112  0.0153  0.0369  733  MET B N   
3289 C CA  . MET B 483 ? 0.7966 0.7566 0.6453 0.0161  0.0123  0.0385  733  MET B CA  
3290 C C   . MET B 483 ? 0.7541 0.7242 0.6158 0.0225  0.0198  0.0369  733  MET B C   
3291 O O   . MET B 483 ? 0.7839 0.7626 0.6530 0.0201  0.0275  0.0377  733  MET B O   
3292 C CB  . MET B 483 ? 0.8819 0.8343 0.7170 0.0092  0.0114  0.0420  733  MET B CB  
3293 C CG  . MET B 483 ? 0.8441 0.7878 0.6635 -0.0004 0.0043  0.0452  733  MET B CG  
3294 S SD  . MET B 483 ? 0.8892 0.8122 0.6968 0.0018  -0.0120 0.0491  733  MET B SD  
3295 C CE  . MET B 483 ? 0.7727 0.6883 0.5760 0.0029  -0.0120 0.0506  733  MET B CE  
3296 N N   . ASP B 484 ? 0.7124 0.6824 0.5776 0.0301  0.0166  0.0343  734  ASP B N   
3297 C CA  . ASP B 484 ? 0.6856 0.6668 0.5594 0.0346  0.0232  0.0330  734  ASP B CA  
3298 C C   . ASP B 484 ? 0.7798 0.7564 0.6451 0.0348  0.0231  0.0345  734  ASP B C   
3299 O O   . ASP B 484 ? 0.8213 0.7851 0.6763 0.0339  0.0159  0.0349  734  ASP B O   
3300 C CB  . ASP B 484 ? 0.7146 0.7026 0.5973 0.0421  0.0204  0.0266  734  ASP B CB  
3301 C CG  . ASP B 484 ? 0.8268 0.8309 0.7175 0.0446  0.0283  0.0250  734  ASP B CG  
3302 O OD1 . ASP B 484 ? 0.7661 0.7753 0.6572 0.0401  0.0356  0.0308  734  ASP B OD1 
3303 O OD2 . ASP B 484 ? 0.8838 0.8963 0.7807 0.0505  0.0266  0.0177  734  ASP B OD2 
3304 N N   . GLY B 485 ? 0.8247 0.8113 0.6943 0.0352  0.0304  0.0361  735  GLY B N   
3305 C CA  . GLY B 485 ? 0.6842 0.6679 0.5463 0.0355  0.0307  0.0372  735  GLY B CA  
3306 C C   . GLY B 485 ? 0.7702 0.7678 0.6368 0.0387  0.0358  0.0363  735  GLY B C   
3307 O O   . GLY B 485 ? 0.7668 0.7770 0.6422 0.0391  0.0403  0.0361  735  GLY B O   
3308 N N   . THR B 486 ? 0.7705 0.7668 0.6304 0.0402  0.0351  0.0358  736  THR B N   
3309 C CA  . THR B 486 ? 0.6844 0.6952 0.5454 0.0421  0.0396  0.0348  736  THR B CA  
3310 C C   . THR B 486 ? 0.7645 0.7737 0.6205 0.0380  0.0427  0.0414  736  THR B C   
3311 O O   . THR B 486 ? 0.8709 0.8688 0.7203 0.0375  0.0395  0.0415  736  THR B O   
3312 C CB  . THR B 486 ? 0.7313 0.7449 0.5906 0.0489  0.0348  0.0255  736  THR B CB  
3313 O OG1 . THR B 486 ? 0.8436 0.8581 0.7101 0.0535  0.0300  0.0181  736  THR B OG1 
3314 C CG2 . THR B 486 ? 0.7088 0.7419 0.5682 0.0498  0.0404  0.0233  736  THR B CG2 
3315 N N   . PHE B 487 ? 0.7221 0.7424 0.5817 0.0345  0.0481  0.0471  737  PHE B N   
3316 C CA  . PHE B 487 ? 0.7437 0.7625 0.6004 0.0307  0.0492  0.0539  737  PHE B CA  
3317 C C   . PHE B 487 ? 0.6864 0.7113 0.5343 0.0335  0.0489  0.0513  737  PHE B C   
3318 O O   . PHE B 487 ? 0.7267 0.7676 0.5735 0.0342  0.0518  0.0495  737  PHE B O   
3319 C CB  . PHE B 487 ? 0.7988 0.8258 0.6629 0.0253  0.0526  0.0622  737  PHE B CB  
3320 C CG  . PHE B 487 ? 0.7041 0.7250 0.5695 0.0212  0.0508  0.0697  737  PHE B CG  
3321 C CD1 . PHE B 487 ? 0.7773 0.8026 0.6351 0.0199  0.0503  0.0740  737  PHE B CD1 
3322 C CD2 . PHE B 487 ? 0.8147 0.8268 0.6903 0.0186  0.0488  0.0714  737  PHE B CD2 
3323 C CE1 . PHE B 487 ? 0.8037 0.8223 0.6641 0.0166  0.0467  0.0807  737  PHE B CE1 
3324 C CE2 . PHE B 487 ? 0.7916 0.7985 0.6720 0.0156  0.0454  0.0763  737  PHE B CE2 
3325 C CZ  . PHE B 487 ? 0.7612 0.7702 0.6341 0.0147  0.0438  0.0814  737  PHE B CZ  
3326 N N   . ASN B 488 ? 0.6877 0.7019 0.5298 0.0347  0.0455  0.0500  738  ASN B N   
3327 C CA  . ASN B 488 ? 0.6932 0.7121 0.5277 0.0377  0.0444  0.0465  738  ASN B CA  
3328 C C   . ASN B 488 ? 0.7141 0.7280 0.5454 0.0345  0.0436  0.0525  738  ASN B C   
3329 O O   . ASN B 488 ? 0.7696 0.7707 0.6029 0.0327  0.0415  0.0534  738  ASN B O   
3330 C CB  . ASN B 488 ? 0.7776 0.7877 0.6094 0.0431  0.0391  0.0376  738  ASN B CB  
3331 C CG  . ASN B 488 ? 0.7309 0.7490 0.5669 0.0483  0.0376  0.0291  738  ASN B CG  
3332 O OD1 . ASN B 488 ? 0.8378 0.8735 0.6771 0.0484  0.0420  0.0277  738  ASN B OD1 
3333 N ND2 . ASN B 488 ? 0.9395 0.9452 0.7763 0.0519  0.0306  0.0232  738  ASN B ND2 
3334 N N   . LEU B 489 ? 0.6993 0.7248 0.5258 0.0334  0.0450  0.0560  739  LEU B N   
3335 C CA  . LEU B 489 ? 0.7799 0.8015 0.6035 0.0306  0.0427  0.0622  739  LEU B CA  
3336 C C   . LEU B 489 ? 0.7233 0.7469 0.5385 0.0348  0.0406  0.0560  739  LEU B C   
3337 O O   . LEU B 489 ? 0.8192 0.8570 0.6292 0.0375  0.0422  0.0507  739  LEU B O   
3338 C CB  . LEU B 489 ? 0.7082 0.7402 0.5312 0.0246  0.0440  0.0728  739  LEU B CB  
3339 C CG  . LEU B 489 ? 0.7431 0.7682 0.5667 0.0206  0.0391  0.0819  739  LEU B CG  
3340 C CD1 . LEU B 489 ? 0.9232 0.9332 0.7599 0.0196  0.0359  0.0826  739  LEU B CD1 
3341 C CD2 . LEU B 489 ? 0.7235 0.7600 0.5434 0.0134  0.0392  0.0937  739  LEU B CD2 
3342 N N   . LYS B 490 ? 0.7063 0.7175 0.5214 0.0353  0.0369  0.0551  740  LYS B N   
3343 C CA  . LYS B 490 ? 0.8048 0.8163 0.6135 0.0394  0.0342  0.0488  740  LYS B CA  
3344 C C   . LYS B 490 ? 0.7130 0.7189 0.5211 0.0373  0.0308  0.0531  740  LYS B C   
3345 O O   . LYS B 490 ? 0.7692 0.7650 0.5849 0.0343  0.0292  0.0562  740  LYS B O   
3346 C CB  . LYS B 490 ? 0.7910 0.7913 0.6011 0.0429  0.0319  0.0400  740  LYS B CB  
3347 C CG  . LYS B 490 ? 0.9219 0.9281 0.7324 0.0474  0.0318  0.0327  740  LYS B CG  
3348 C CD  . LYS B 490 ? 0.9169 0.9112 0.7276 0.0510  0.0261  0.0247  740  LYS B CD  
3349 C CE  . LYS B 490 ? 0.9585 0.9578 0.7725 0.0567  0.0232  0.0159  740  LYS B CE  
3350 N NZ  . LYS B 490 ? 1.2377 1.2355 1.0561 0.0552  0.0246  0.0183  740  LYS B NZ  
3351 N N   . THR B 491 ? 0.7202 0.7340 0.5206 0.0393  0.0290  0.0518  741  THR B N   
3352 C CA  . THR B 491 ? 0.8270 0.8359 0.6263 0.0385  0.0243  0.0546  741  THR B CA  
3353 C C   . THR B 491 ? 0.7261 0.7337 0.5216 0.0437  0.0220  0.0448  741  THR B C   
3354 O O   . THR B 491 ? 0.8832 0.9021 0.6726 0.0474  0.0231  0.0386  741  THR B O   
3355 C CB  . THR B 491 ? 0.7775 0.7975 0.5698 0.0346  0.0227  0.0646  741  THR B CB  
3356 O OG1 . THR B 491 ? 0.8716 0.8915 0.6688 0.0290  0.0239  0.0744  741  THR B OG1 
3357 C CG2 . THR B 491 ? 0.7404 0.7534 0.5325 0.0341  0.0156  0.0677  741  THR B CG2 
3358 N N   . ALA B 492 ? 0.7234 0.7187 0.5241 0.0437  0.0186  0.0419  742  ALA B N   
3359 C CA  . ALA B 492 ? 0.7252 0.7174 0.5242 0.0478  0.0159  0.0327  742  ALA B CA  
3360 C C   . ALA B 492 ? 0.7561 0.7451 0.5566 0.0474  0.0111  0.0338  742  ALA B C   
3361 O O   . ALA B 492 ? 0.7950 0.7747 0.6048 0.0445  0.0094  0.0341  742  ALA B O   
3362 C CB  . ALA B 492 ? 0.7198 0.6999 0.5242 0.0471  0.0165  0.0265  742  ALA B CB  
3363 N N   . PHE B 493 ? 0.7369 0.7350 0.5293 0.0502  0.0083  0.0331  743  PHE B N   
3364 C CA  . PHE B 493 ? 0.7496 0.7450 0.5428 0.0506  0.0021  0.0337  743  PHE B CA  
3365 C C   . PHE B 493 ? 0.8163 0.8072 0.6119 0.0547  0.0002  0.0221  743  PHE B C   
3366 O O   . PHE B 493 ? 0.9243 0.9228 0.7137 0.0590  0.0005  0.0155  743  PHE B O   
3367 C CB  . PHE B 493 ? 0.7543 0.7626 0.5356 0.0501  -0.0008 0.0407  743  PHE B CB  
3368 C CG  . PHE B 493 ? 0.8292 0.8347 0.6099 0.0512  -0.0089 0.0411  743  PHE B CG  
3369 C CD1 . PHE B 493 ? 0.9381 0.9536 0.7093 0.0550  -0.0111 0.0353  743  PHE B CD1 
3370 C CD2 . PHE B 493 ? 0.8823 0.8758 0.6736 0.0488  -0.0151 0.0456  743  PHE B CD2 
3371 C CE1 . PHE B 493 ? 0.8754 0.8880 0.6460 0.0563  -0.0194 0.0355  743  PHE B CE1 
3372 C CE2 . PHE B 493 ? 0.8320 0.8222 0.6244 0.0504  -0.0240 0.0450  743  PHE B CE2 
3373 C CZ  . PHE B 493 ? 0.7781 0.7774 0.5593 0.0540  -0.0261 0.0406  743  PHE B CZ  
3374 N N   . HIS B 494 ? 0.7515 0.7314 0.5573 0.0531  -0.0020 0.0185  744  HIS B N   
3375 C CA  . HIS B 494 ? 0.7827 0.7582 0.5918 0.0555  -0.0041 0.0080  744  HIS B CA  
3376 C C   . HIS B 494 ? 0.7755 0.7561 0.5810 0.0593  -0.0103 0.0064  744  HIS B C   
3377 O O   . HIS B 494 ? 0.8602 0.8406 0.6675 0.0582  -0.0151 0.0123  744  HIS B O   
3378 C CB  . HIS B 494 ? 0.7384 0.7040 0.5600 0.0507  -0.0034 0.0038  744  HIS B CB  
3379 C CG  . HIS B 494 ? 0.8898 0.8507 0.7131 0.0461  0.0022  0.0043  744  HIS B CG  
3380 N ND1 . HIS B 494 ? 0.9122 0.8746 0.7351 0.0438  0.0055  0.0118  744  HIS B ND1 
3381 C CD2 . HIS B 494 ? 0.8190 0.7735 0.6437 0.0425  0.0041  -0.0010 744  HIS B CD2 
3382 C CE1 . HIS B 494 ? 0.9287 0.8862 0.7525 0.0397  0.0093  0.0104  744  HIS B CE1 
3383 N NE2 . HIS B 494 ? 0.9416 0.8940 0.7658 0.0383  0.0082  0.0035  744  HIS B NE2 
3384 N N   . CYS B 495 ? 0.8159 0.8009 0.6171 0.0640  -0.0116 -0.0018 745  CYS B N   
3385 C CA  . CYS B 495 ? 0.8373 0.8282 0.6346 0.0679  -0.0177 -0.0047 745  CYS B CA  
3386 C C   . CYS B 495 ? 0.7553 0.7371 0.5640 0.0672  -0.0226 -0.0090 745  CYS B C   
3387 O O   . CYS B 495 ? 0.8477 0.8323 0.6546 0.0696  -0.0294 -0.0088 745  CYS B O   
3388 C CB  . CYS B 495 ? 0.7936 0.7924 0.5863 0.0736  -0.0182 -0.0149 745  CYS B CB  
3389 S SG  . CYS B 495 ? 0.9313 0.9468 0.7135 0.0759  -0.0137 -0.0146 745  CYS B SG  
3390 N N   . TYR B 496 ? 0.7470 0.7193 0.5672 0.0633  -0.0196 -0.0135 746  TYR B N   
3391 C CA  . TYR B 496 ? 0.7449 0.7117 0.5785 0.0616  -0.0233 -0.0197 746  TYR B CA  
3392 C C   . TYR B 496 ? 0.7360 0.6970 0.5799 0.0546  -0.0177 -0.0217 746  TYR B C   
3393 O O   . TYR B 496 ? 0.7325 0.6917 0.5718 0.0516  -0.0118 -0.0189 746  TYR B O   
3394 C CB  . TYR B 496 ? 0.7497 0.7165 0.5860 0.0649  -0.0266 -0.0308 746  TYR B CB  
3395 C CG  . TYR B 496 ? 0.9125 0.8750 0.7500 0.0626  -0.0221 -0.0374 746  TYR B CG  
3396 C CD1 . TYR B 496 ? 0.7968 0.7534 0.6452 0.0557  -0.0194 -0.0434 746  TYR B CD1 
3397 C CD2 . TYR B 496 ? 0.8361 0.8013 0.6647 0.0665  -0.0216 -0.0381 746  TYR B CD2 
3398 C CE1 . TYR B 496 ? 0.9158 0.8669 0.7640 0.0516  -0.0170 -0.0471 746  TYR B CE1 
3399 C CE2 . TYR B 496 ? 0.8727 0.8312 0.7040 0.0642  -0.0204 -0.0433 746  TYR B CE2 
3400 C CZ  . TYR B 496 ? 0.8370 0.7872 0.6770 0.0562  -0.0184 -0.0464 746  TYR B CZ  
3401 O OH  . TYR B 496 ? 0.9622 0.9043 0.8037 0.0521  -0.0186 -0.0493 746  TYR B OH  
3402 N N   . GLY B 497 ? 0.7541 0.7137 0.6125 0.0520  -0.0202 -0.0276 747  GLY B N   
3403 C CA  . GLY B 497 ? 0.7258 0.6843 0.5950 0.0444  -0.0147 -0.0325 747  GLY B CA  
3404 C C   . GLY B 497 ? 0.7377 0.6963 0.6074 0.0413  -0.0112 -0.0245 747  GLY B C   
3405 O O   . GLY B 497 ? 0.7274 0.6862 0.5919 0.0446  -0.0140 -0.0148 747  GLY B O   
3406 N N   . SER B 498 ? 0.8050 0.7643 0.6808 0.0337  -0.0051 -0.0289 748  SER B N   
3407 C CA  . SER B 498 ? 0.7619 0.7226 0.6407 0.0300  -0.0015 -0.0239 748  SER B CA  
3408 C C   . SER B 498 ? 0.8385 0.7960 0.7018 0.0294  0.0035  -0.0147 748  SER B C   
3409 O O   . SER B 498 ? 0.8999 0.8543 0.7522 0.0314  0.0038  -0.0135 748  SER B O   
3410 C CB  . SER B 498 ? 0.8669 0.8332 0.7593 0.0214  0.0029  -0.0345 748  SER B CB  
3411 O OG  . SER B 498 ? 1.0043 0.9699 0.8894 0.0142  0.0084  -0.0379 748  SER B OG  
3412 N N   . CYS B 499 ? 0.8657 0.8242 0.7305 0.0270  0.0063  -0.0092 749  CYS B N   
3413 C CA  . CYS B 499 ? 0.9225 0.8788 0.7755 0.0264  0.0105  -0.0014 749  CYS B CA  
3414 C C   . CYS B 499 ? 0.8780 0.8326 0.7296 0.0180  0.0155  -0.0052 749  CYS B C   
3415 O O   . CYS B 499 ? 0.8998 0.8589 0.7605 0.0115  0.0185  -0.0095 749  CYS B O   
3416 C CB  . CYS B 499 ? 0.8907 0.8492 0.7462 0.0276  0.0108  0.0065  749  CYS B CB  
3417 S SG  . CYS B 499 ? 1.5667 1.5277 1.4409 0.0283  0.0046  0.0041  749  CYS B SG  
3418 N N   . GLU B 500 ? 0.8557 0.8044 0.6964 0.0177  0.0156  -0.0038 750  GLU B N   
3419 C CA  . GLU B 500 ? 0.7803 0.7252 0.6175 0.0082  0.0182  -0.0054 750  GLU B CA  
3420 C C   . GLU B 500 ? 0.7604 0.7051 0.5940 0.0043  0.0215  0.0004  750  GLU B C   
3421 O O   . GLU B 500 ? 0.8155 0.7599 0.6459 0.0104  0.0212  0.0066  750  GLU B O   
3422 C CB  . GLU B 500 ? 0.9278 0.8638 0.7563 0.0094  0.0144  -0.0050 750  GLU B CB  
3423 C CG  . GLU B 500 ? 0.7668 0.7031 0.5989 0.0133  0.0108  -0.0115 750  GLU B CG  
3424 C CD  . GLU B 500 ? 0.9952 0.9353 0.8355 0.0044  0.0128  -0.0195 750  GLU B CD  
3425 O OE1 . GLU B 500 ? 1.1483 1.0900 0.9941 0.0076  0.0101  -0.0261 750  GLU B OE1 
3426 O OE2 . GLU B 500 ? 1.1510 1.0941 0.9925 -0.0061 0.0172  -0.0201 750  GLU B OE2 
3427 N N   . LYS B 501 ? 0.7581 0.7046 0.5920 -0.0068 0.0248  -0.0021 751  LYS B N   
3428 C CA  . LYS B 501 ? 0.7475 0.6952 0.5781 -0.0120 0.0278  0.0023  751  LYS B CA  
3429 C C   . LYS B 501 ? 0.7653 0.7027 0.5828 -0.0186 0.0255  0.0075  751  LYS B C   
3430 O O   . LYS B 501 ? 0.8039 0.7382 0.6177 -0.0272 0.0244  0.0054  751  LYS B O   
3431 C CB  . LYS B 501 ? 0.7070 0.6672 0.5477 -0.0207 0.0328  -0.0051 751  LYS B CB  
3432 C CG  . LYS B 501 ? 0.8042 0.7728 0.6614 -0.0142 0.0325  -0.0107 751  LYS B CG  
3433 C CD  . LYS B 501 ? 0.8288 0.7937 0.6858 -0.0043 0.0303  -0.0023 751  LYS B CD  
3434 C CE  . LYS B 501 ? 0.9059 0.8773 0.7800 0.0003  0.0280  -0.0060 751  LYS B CE  
3435 N NZ  . LYS B 501 ? 0.9630 0.9356 0.8451 0.0030  0.0241  -0.0128 751  LYS B NZ  
3436 N N   . TYR B 502 ? 0.7882 0.7200 0.5995 -0.0151 0.0237  0.0145  752  TYR B N   
3437 C CA  . TYR B 502 ? 0.7526 0.6725 0.5528 -0.0201 0.0187  0.0203  752  TYR B CA  
3438 C C   . TYR B 502 ? 0.8073 0.7162 0.6043 -0.0179 0.0119  0.0198  752  TYR B C   
3439 O O   . TYR B 502 ? 0.8592 0.7590 0.6497 -0.0277 0.0076  0.0221  752  TYR B O   
3440 C CB  . TYR B 502 ? 0.7892 0.7114 0.5837 -0.0357 0.0213  0.0214  752  TYR B CB  
3441 C CG  . TYR B 502 ? 0.7565 0.6891 0.5543 -0.0374 0.0267  0.0213  752  TYR B CG  
3442 C CD1 . TYR B 502 ? 0.8642 0.7913 0.6571 -0.0342 0.0242  0.0277  752  TYR B CD1 
3443 C CD2 . TYR B 502 ? 0.8366 0.7850 0.6447 -0.0417 0.0335  0.0133  752  TYR B CD2 
3444 C CE1 . TYR B 502 ? 0.9007 0.8376 0.6978 -0.0355 0.0288  0.0270  752  TYR B CE1 
3445 C CE2 . TYR B 502 ? 0.7272 0.6855 0.5407 -0.0428 0.0375  0.0118  752  TYR B CE2 
3446 C CZ  . TYR B 502 ? 0.8016 0.7538 0.6089 -0.0398 0.0354  0.0192  752  TYR B CZ  
3447 O OH  . TYR B 502 ? 0.9795 0.9417 0.7933 -0.0407 0.0391  0.0172  752  TYR B OH  
3448 N N   . ALA B 503 ? 0.7641 0.6745 0.5658 -0.0055 0.0102  0.0167  753  ALA B N   
3449 C CA  . ALA B 503 ? 0.7492 0.6514 0.5504 -0.0011 0.0033  0.0141  753  ALA B CA  
3450 C C   . ALA B 503 ? 0.7831 0.6827 0.5846 0.0111  -0.0020 0.0140  753  ALA B C   
3451 O O   . ALA B 503 ? 0.9389 0.8330 0.7421 0.0163  -0.0087 0.0100  753  ALA B O   
3452 C CB  . ALA B 503 ? 0.7792 0.6886 0.5868 0.0019  0.0056  0.0073  753  ALA B CB  
3453 N N   . TYR B 504 ? 0.7824 0.6874 0.5838 0.0156  0.0007  0.0169  754  TYR B N   
3454 C CA  . TYR B 504 ? 0.7587 0.6666 0.5619 0.0268  -0.0027 0.0148  754  TYR B CA  
3455 C C   . TYR B 504 ? 0.7472 0.6505 0.5487 0.0257  -0.0049 0.0191  754  TYR B C   
3456 O O   . TYR B 504 ? 0.8031 0.7049 0.6014 0.0175  -0.0014 0.0243  754  TYR B O   
3457 C CB  . TYR B 504 ? 0.7576 0.6813 0.5634 0.0340  0.0036  0.0134  754  TYR B CB  
3458 C CG  . TYR B 504 ? 0.8078 0.7360 0.6153 0.0337  0.0059  0.0107  754  TYR B CG  
3459 C CD1 . TYR B 504 ? 0.7366 0.6623 0.5450 0.0370  0.0011  0.0047  754  TYR B CD1 
3460 C CD2 . TYR B 504 ? 0.7669 0.7019 0.5771 0.0305  0.0116  0.0133  754  TYR B CD2 
3461 C CE1 . TYR B 504 ? 0.7635 0.6934 0.5740 0.0371  0.0024  0.0017  754  TYR B CE1 
3462 C CE2 . TYR B 504 ? 0.7218 0.6602 0.5353 0.0308  0.0119  0.0100  754  TYR B CE2 
3463 C CZ  . TYR B 504 ? 0.8386 0.7747 0.6517 0.0340  0.0076  0.0044  754  TYR B CZ  
3464 O OH  . TYR B 504 ? 0.8618 0.8013 0.6787 0.0347  0.0072  0.0006  754  TYR B OH  
3465 N N   . PRO B 505 ? 0.7984 0.7006 0.6030 0.0341  -0.0113 0.0154  755  PRO B N   
3466 C CA  . PRO B 505 ? 0.7668 0.6629 0.5711 0.0337  -0.0156 0.0184  755  PRO B CA  
3467 C C   . PRO B 505 ? 0.7789 0.6859 0.5830 0.0331  -0.0069 0.0222  755  PRO B C   
3468 O O   . PRO B 505 ? 0.7484 0.6493 0.5501 0.0282  -0.0085 0.0269  755  PRO B O   
3469 C CB  . PRO B 505 ? 0.8082 0.7054 0.6202 0.0449  -0.0241 0.0097  755  PRO B CB  
3470 C CG  . PRO B 505 ? 0.7658 0.6622 0.5802 0.0480  -0.0275 0.0036  755  PRO B CG  
3471 C CD  . PRO B 505 ? 0.7556 0.6612 0.5655 0.0440  -0.0168 0.0065  755  PRO B CD  
3472 N N   . TRP B 506 ? 0.8295 0.7520 0.6361 0.0375  0.0013  0.0210  756  TRP B N   
3473 C CA  . TRP B 506 ? 0.8010 0.7328 0.6091 0.0366  0.0083  0.0251  756  TRP B CA  
3474 C C   . TRP B 506 ? 0.7218 0.6505 0.5280 0.0269  0.0128  0.0304  756  TRP B C   
3475 O O   . TRP B 506 ? 0.7718 0.7051 0.5803 0.0251  0.0167  0.0335  756  TRP B O   
3476 C CB  . TRP B 506 ? 0.8681 0.8162 0.6787 0.0419  0.0143  0.0241  756  TRP B CB  
3477 C CG  . TRP B 506 ? 0.8749 0.8256 0.6842 0.0412  0.0161  0.0237  756  TRP B CG  
3478 C CD1 . TRP B 506 ? 0.7162 0.6674 0.5268 0.0361  0.0202  0.0274  756  TRP B CD1 
3479 C CD2 . TRP B 506 ? 0.7679 0.7215 0.5761 0.0465  0.0129  0.0178  756  TRP B CD2 
3480 N NE1 . TRP B 506 ? 0.7128 0.6661 0.5228 0.0378  0.0193  0.0250  756  TRP B NE1 
3481 C CE2 . TRP B 506 ? 0.7187 0.6737 0.5263 0.0440  0.0153  0.0194  756  TRP B CE2 
3482 C CE3 . TRP B 506 ? 0.7891 0.7452 0.5986 0.0535  0.0076  0.0099  756  TRP B CE3 
3483 C CZ2 . TRP B 506 ? 0.7673 0.7256 0.5737 0.0479  0.0128  0.0146  756  TRP B CZ2 
3484 C CZ3 . TRP B 506 ? 0.7831 0.7435 0.5919 0.0575  0.0055  0.0043  756  TRP B CZ3 
3485 C CH2 . TRP B 506 ? 0.8230 0.7842 0.6293 0.0545  0.0083  0.0072  756  TRP B CH2 
3486 N N   . GLN B 507 ? 0.7246 0.6476 0.5282 0.0205  0.0124  0.0302  757  GLN B N   
3487 C CA  . GLN B 507 ? 0.7220 0.6454 0.5251 0.0104  0.0166  0.0323  757  GLN B CA  
3488 C C   . GLN B 507 ? 0.7788 0.6924 0.5750 0.0020  0.0125  0.0357  757  GLN B C   
3489 O O   . GLN B 507 ? 0.7955 0.7113 0.5895 -0.0082 0.0158  0.0364  757  GLN B O   
3490 C CB  . GLN B 507 ? 0.7215 0.6461 0.5259 0.0062  0.0184  0.0289  757  GLN B CB  
3491 C CG  . GLN B 507 ? 0.8052 0.7398 0.6168 0.0125  0.0220  0.0267  757  GLN B CG  
3492 C CD  . GLN B 507 ? 0.7601 0.6942 0.5731 0.0118  0.0210  0.0221  757  GLN B CD  
3493 O OE1 . GLN B 507 ? 0.7512 0.6775 0.5598 0.0094  0.0170  0.0203  757  GLN B OE1 
3494 N NE2 . GLN B 507 ? 0.7076 0.6494 0.5280 0.0137  0.0234  0.0202  757  GLN B NE2 
3495 N N   . THR B 508 ? 0.7408 0.6448 0.5340 0.0058  0.0046  0.0371  758  THR B N   
3496 C CA  . THR B 508 ? 0.7519 0.6456 0.5383 -0.0014 -0.0014 0.0419  758  THR B CA  
3497 C C   . THR B 508 ? 0.7458 0.6455 0.5351 0.0015  0.0012  0.0434  758  THR B C   
3498 O O   . THR B 508 ? 0.7552 0.6470 0.5389 -0.0035 -0.0043 0.0473  758  THR B O   
3499 C CB  . THR B 508 ? 0.8096 0.6874 0.5938 0.0016  -0.0143 0.0424  758  THR B CB  
3500 O OG1 . THR B 508 ? 0.7632 0.6451 0.5558 0.0150  -0.0170 0.0373  758  THR B OG1 
3501 C CG2 . THR B 508 ? 0.8391 0.7109 0.6223 -0.0005 -0.0175 0.0403  758  THR B CG2 
3502 N N   . ALA B 509 ? 0.7319 0.6448 0.5295 0.0087  0.0086  0.0408  759  ALA B N   
3503 C CA  . ALA B 509 ? 0.7259 0.6452 0.5280 0.0118  0.0110  0.0417  759  ALA B CA  
3504 C C   . ALA B 509 ? 0.8033 0.7235 0.6022 0.0019  0.0135  0.0446  759  ALA B C   
3505 O O   . ALA B 509 ? 0.7269 0.6487 0.5226 -0.0071 0.0166  0.0444  759  ALA B O   
3506 C CB  . ALA B 509 ? 0.7129 0.6464 0.5238 0.0182  0.0187  0.0401  759  ALA B CB  
3507 N N   . GLY B 510 ? 0.8397 0.7606 0.6403 0.0035  0.0120  0.0458  760  GLY B N   
3508 C CA  . GLY B 510 ? 0.7878 0.7117 0.5856 -0.0054 0.0141  0.0475  760  GLY B CA  
3509 C C   . GLY B 510 ? 0.8239 0.7610 0.6287 -0.0096 0.0234  0.0444  760  GLY B C   
3510 O O   . GLY B 510 ? 0.7648 0.7055 0.5654 -0.0200 0.0255  0.0431  760  GLY B O   
3511 N N   . CYS B 511 ? 0.8025 0.7478 0.6187 -0.0022 0.0283  0.0425  761  CYS B N   
3512 C CA  . CYS B 511 ? 0.9316 0.8875 0.7579 -0.0046 0.0345  0.0390  761  CYS B CA  
3513 C C   . CYS B 511 ? 0.8130 0.7723 0.6472 0.0034  0.0362  0.0397  761  CYS B C   
3514 O O   . CYS B 511 ? 0.7103 0.6692 0.5445 0.0103  0.0352  0.0424  761  CYS B O   
3515 C CB  . CYS B 511 ? 0.8341 0.7989 0.6690 -0.0073 0.0375  0.0370  761  CYS B CB  
3516 S SG  . CYS B 511 ? 1.3863 1.3559 1.2146 -0.0207 0.0384  0.0328  761  CYS B SG  
3517 N N   . PHE B 512 ? 0.8106 0.7744 0.6516 0.0016  0.0384  0.0367  762  PHE B N   
3518 C CA  . PHE B 512 ? 0.7083 0.6740 0.5546 0.0076  0.0385  0.0384  762  PHE B CA  
3519 C C   . PHE B 512 ? 0.7086 0.6797 0.5671 0.0049  0.0393  0.0340  762  PHE B C   
3520 O O   . PHE B 512 ? 0.7270 0.7016 0.5889 -0.0015 0.0406  0.0276  762  PHE B O   
3521 C CB  . PHE B 512 ? 0.7220 0.6816 0.5580 0.0110  0.0358  0.0390  762  PHE B CB  
3522 C CG  . PHE B 512 ? 0.6897 0.6450 0.5210 0.0055  0.0347  0.0350  762  PHE B CG  
3523 C CD1 . PHE B 512 ? 0.7576 0.7061 0.5792 -0.0004 0.0326  0.0348  762  PHE B CD1 
3524 C CD2 . PHE B 512 ? 0.6876 0.6455 0.5242 0.0055  0.0350  0.0317  762  PHE B CD2 
3525 C CE1 . PHE B 512 ? 0.8404 0.7861 0.6574 -0.0074 0.0319  0.0318  762  PHE B CE1 
3526 C CE2 . PHE B 512 ? 0.6916 0.6474 0.5251 -0.0002 0.0346  0.0270  762  PHE B CE2 
3527 C CZ  . PHE B 512 ? 0.7509 0.7010 0.5742 -0.0072 0.0335  0.0272  762  PHE B CZ  
3528 N N   . VAL B 513 ? 0.6722 0.6448 0.5377 0.0095  0.0379  0.0371  763  VAL B N   
3529 C CA  . VAL B 513 ? 0.6757 0.6513 0.5547 0.0086  0.0358  0.0331  763  VAL B CA  
3530 C C   . VAL B 513 ? 0.6738 0.6463 0.5486 0.0131  0.0327  0.0371  763  VAL B C   
3531 O O   . VAL B 513 ? 0.6793 0.6517 0.5479 0.0168  0.0323  0.0447  763  VAL B O   
3532 C CB  . VAL B 513 ? 0.7396 0.7197 0.6361 0.0087  0.0343  0.0338  763  VAL B CB  
3533 C CG1 . VAL B 513 ? 0.6639 0.6458 0.5774 0.0086  0.0294  0.0284  763  VAL B CG1 
3534 C CG2 . VAL B 513 ? 0.8754 0.8604 0.7761 0.0046  0.0375  0.0288  763  VAL B CG2 
3535 N N   . GLU B 514 ? 0.6747 0.6466 0.5529 0.0122  0.0306  0.0312  764  GLU B N   
3536 C CA  . GLU B 514 ? 0.7474 0.7167 0.6216 0.0162  0.0268  0.0339  764  GLU B CA  
3537 C C   . GLU B 514 ? 0.7165 0.6866 0.6072 0.0166  0.0211  0.0309  764  GLU B C   
3538 O O   . GLU B 514 ? 0.7303 0.7041 0.6358 0.0135  0.0206  0.0219  764  GLU B O   
3539 C CB  . GLU B 514 ? 0.6828 0.6489 0.5458 0.0159  0.0278  0.0293  764  GLU B CB  
3540 C CG  . GLU B 514 ? 0.7638 0.7267 0.6129 0.0157  0.0306  0.0313  764  GLU B CG  
3541 C CD  . GLU B 514 ? 0.8036 0.7615 0.6438 0.0150  0.0295  0.0272  764  GLU B CD  
3542 O OE1 . GLU B 514 ? 0.6951 0.6504 0.5264 0.0198  0.0278  0.0293  764  GLU B OE1 
3543 O OE2 . GLU B 514 ? 0.7649 0.7229 0.6085 0.0092  0.0301  0.0209  764  GLU B OE2 
3544 N N   . LYS B 515 ? 0.6854 0.6530 0.5740 0.0202  0.0158  0.0376  765  LYS B N   
3545 C CA  . LYS B 515 ? 0.6885 0.6543 0.5919 0.0212  0.0075  0.0357  765  LYS B CA  
3546 C C   . LYS B 515 ? 0.7501 0.7135 0.6444 0.0242  0.0042  0.0354  765  LYS B C   
3547 O O   . LYS B 515 ? 0.7659 0.7295 0.6435 0.0263  0.0057  0.0425  765  LYS B O   
3548 C CB  . LYS B 515 ? 0.8288 0.7922 0.7396 0.0214  0.0010  0.0467  765  LYS B CB  
3549 C CG  . LYS B 515 ? 0.7006 0.6591 0.6268 0.0227  -0.0109 0.0464  765  LYS B CG  
3550 C CD  . LYS B 515 ? 0.8889 0.8438 0.8309 0.0211  -0.0188 0.0539  765  LYS B CD  
3551 C CE  . LYS B 515 ? 0.7125 0.6607 0.6745 0.0228  -0.0334 0.0513  765  LYS B CE  
3552 N NZ  . LYS B 515 ? 1.0881 1.0314 1.0713 0.0212  -0.0431 0.0560  765  LYS B NZ  
3553 N N   . ASP B 516 ? 0.7013 0.6644 0.6081 0.0245  -0.0003 0.0255  766  ASP B N   
3554 C CA  . ASP B 516 ? 0.7873 0.7484 0.6881 0.0274  -0.0038 0.0229  766  ASP B CA  
3555 C C   . ASP B 516 ? 0.7085 0.6653 0.6182 0.0302  -0.0157 0.0281  766  ASP B C   
3556 O O   . ASP B 516 ? 0.7955 0.7512 0.7267 0.0301  -0.0229 0.0221  766  ASP B O   
3557 C CB  . ASP B 516 ? 0.6999 0.6644 0.6085 0.0252  -0.0011 0.0078  766  ASP B CB  
3558 C CG  . ASP B 516 ? 0.8301 0.7974 0.7288 0.0204  0.0088  0.0046  766  ASP B CG  
3559 O OD1 . ASP B 516 ? 0.7750 0.7401 0.6587 0.0211  0.0127  0.0133  766  ASP B OD1 
3560 O OD2 . ASP B 516 ? 0.9981 0.9705 0.9041 0.0154  0.0121  -0.0069 766  ASP B OD2 
3561 N N   . TYR B 517 ? 0.7181 0.6733 0.6120 0.0323  -0.0188 0.0385  767  TYR B N   
3562 C CA  . TYR B 517 ? 0.7307 0.6808 0.6281 0.0336  -0.0313 0.0464  767  TYR B CA  
3563 C C   . TYR B 517 ? 0.7993 0.7484 0.6950 0.0373  -0.0363 0.0395  767  TYR B C   
3564 O O   . TYR B 517 ? 0.8675 0.8206 0.7482 0.0389  -0.0298 0.0364  767  TYR B O   
3565 C CB  . TYR B 517 ? 0.7412 0.6931 0.6207 0.0316  -0.0317 0.0635  767  TYR B CB  
3566 C CG  . TYR B 517 ? 0.7542 0.7050 0.6398 0.0275  -0.0315 0.0726  767  TYR B CG  
3567 C CD1 . TYR B 517 ? 0.7320 0.6887 0.6114 0.0259  -0.0201 0.0726  767  TYR B CD1 
3568 C CD2 . TYR B 517 ? 0.8090 0.7523 0.7080 0.0252  -0.0442 0.0811  767  TYR B CD2 
3569 C CE1 . TYR B 517 ? 0.8943 0.8507 0.7803 0.0222  -0.0199 0.0803  767  TYR B CE1 
3570 C CE2 . TYR B 517 ? 0.7519 0.6939 0.6581 0.0210  -0.0447 0.0895  767  TYR B CE2 
3571 C CZ  . TYR B 517 ? 0.7467 0.6959 0.6462 0.0196  -0.0319 0.0887  767  TYR B CZ  
3572 O OH  . TYR B 517 ? 0.9234 0.8719 0.8310 0.0156  -0.0323 0.0963  767  TYR B OH  
3573 N N   . GLU B 518 ? 0.7465 0.6901 0.6594 0.0389  -0.0489 0.0364  768  GLU B N   
3574 C CA  . GLU B 518 ? 0.7476 0.6897 0.6598 0.0427  -0.0556 0.0306  768  GLU B CA  
3575 C C   . GLU B 518 ? 0.7820 0.7241 0.6715 0.0432  -0.0597 0.0448  768  GLU B C   
3576 O O   . GLU B 518 ? 0.9687 0.9106 0.8477 0.0397  -0.0613 0.0601  768  GLU B O   
3577 C CB  . GLU B 518 ? 0.7520 0.6881 0.6907 0.0449  -0.0702 0.0230  768  GLU B CB  
3578 C CG  . GLU B 518 ? 0.7826 0.7231 0.7467 0.0440  -0.0669 0.0060  768  GLU B CG  
3579 C CD  . GLU B 518 ? 0.9473 0.8842 0.9408 0.0473  -0.0824 -0.0052 768  GLU B CD  
3580 O OE1 . GLU B 518 ? 0.9582 0.8878 0.9507 0.0508  -0.0955 -0.0006 768  GLU B OE1 
3581 O OE2 . GLU B 518 ? 0.8827 0.8251 0.9012 0.0466  -0.0823 -0.0196 768  GLU B OE2 
3582 N N   . TYR B 519 ? 0.7655 0.7096 0.6473 0.0468  -0.0611 0.0390  769  TYR B N   
3583 C CA  . TYR B 519 ? 0.7808 0.7273 0.6422 0.0473  -0.0663 0.0500  769  TYR B CA  
3584 C C   . TYR B 519 ? 0.8919 0.8292 0.7617 0.0472  -0.0845 0.0576  769  TYR B C   
3585 O O   . TYR B 519 ? 1.0972 1.0287 0.9856 0.0510  -0.0935 0.0468  769  TYR B O   
3586 C CB  . TYR B 519 ? 0.8015 0.7540 0.6528 0.0516  -0.0617 0.0398  769  TYR B CB  
3587 C CG  . TYR B 519 ? 0.8602 0.8180 0.6912 0.0523  -0.0674 0.0487  769  TYR B CG  
3588 C CD1 . TYR B 519 ? 0.7999 0.7686 0.6094 0.0495  -0.0603 0.0579  769  TYR B CD1 
3589 C CD2 . TYR B 519 ? 0.8504 0.8043 0.6841 0.0554  -0.0801 0.0468  769  TYR B CD2 
3590 C CE1 . TYR B 519 ? 0.8159 0.7936 0.6061 0.0489  -0.0648 0.0647  769  TYR B CE1 
3591 C CE2 . TYR B 519 ? 0.9574 0.9178 0.7707 0.0551  -0.0855 0.0550  769  TYR B CE2 
3592 C CZ  . TYR B 519 ? 0.8914 0.8648 0.6826 0.0515  -0.0774 0.0639  769  TYR B CZ  
3593 O OH  . TYR B 519 ? 1.0036 0.9875 0.7738 0.0501  -0.0821 0.0707  769  TYR B OH  
3594 N N   . GLU B 520 ? 0.8947 0.8308 0.7518 0.0422  -0.0907 0.0761  770  GLU B N   
3595 C CA  . GLU B 520 ? 1.0146 0.9397 0.8770 0.0403  -0.1103 0.0873  770  GLU B CA  
3596 C C   . GLU B 520 ? 1.0066 0.9376 0.8431 0.0388  -0.1152 0.0973  770  GLU B C   
3597 O O   . GLU B 520 ? 1.0043 0.9459 0.8171 0.0330  -0.1085 0.1097  770  GLU B O   
3598 C CB  . GLU B 520 ? 0.9734 0.8914 0.8417 0.0336  -0.1163 0.1026  770  GLU B CB  
3599 C CG  . GLU B 520 ? 0.9844 0.9133 0.8312 0.0270  -0.1031 0.1148  770  GLU B CG  
3600 C CD  . GLU B 520 ? 1.2883 1.2094 1.1400 0.0191  -0.1117 0.1323  770  GLU B CD  
3601 O OE1 . GLU B 520 ? 1.3199 1.2448 1.1749 0.0165  -0.1011 0.1330  770  GLU B OE1 
3602 O OE2 . GLU B 520 ? 1.4220 1.3323 1.2747 0.0151  -0.1300 0.1456  770  GLU B OE2 
3603 N N   . SER B 521 ? 1.0922 1.0186 0.9336 0.0437  -0.1264 0.0906  771  SER B N   
3604 C CA  . SER B 521 ? 1.1081 1.0395 0.9260 0.0420  -0.1340 0.1002  771  SER B CA  
3605 C C   . SER B 521 ? 1.1897 1.1140 0.9977 0.0327  -0.1488 0.1241  771  SER B C   
3606 O O   . SER B 521 ? 1.2382 1.1473 1.0657 0.0307  -0.1609 0.1302  771  SER B O   
3607 C CB  . SER B 521 ? 1.1565 1.0825 0.9853 0.0496  -0.1450 0.0875  771  SER B CB  
3608 O OG  . SER B 521 ? 1.0424 0.9723 0.8858 0.0565  -0.1331 0.0657  771  SER B OG  
3609 N N   . GLY B 522 ? 1.2284 1.1650 1.0061 0.0263  -0.1482 0.1373  772  GLY B N   
3610 C CA  . GLY B 522 ? 1.2804 1.2132 1.0436 0.0145  -0.1608 0.1622  772  GLY B CA  
3611 C C   . GLY B 522 ? 1.1818 1.1222 0.9367 0.0053  -0.1493 0.1740  772  GLY B C   
3612 O O   . GLY B 522 ? 1.2790 1.2183 1.0195 -0.0067 -0.1584 0.1960  772  GLY B O   
3613 N N   . TRP B 523 ? 1.1650 1.1128 0.9284 0.0099  -0.1305 0.1605  773  TRP B N   
3614 C CA  . TRP B 523 ? 1.2223 1.1800 0.9771 0.0019  -0.1185 0.1698  773  TRP B CA  
3615 C C   . TRP B 523 ? 1.1821 1.1646 0.9045 -0.0055 -0.1087 0.1767  773  TRP B C   
3616 O O   . TRP B 523 ? 1.2966 1.2882 1.0061 -0.0168 -0.1054 0.1918  773  TRP B O   
3617 C CB  . TRP B 523 ? 1.2083 1.1675 0.9802 0.0091  -0.1022 0.1527  773  TRP B CB  
3618 C CG  . TRP B 523 ? 1.2287 1.1971 0.9954 0.0023  -0.0902 0.1600  773  TRP B CG  
3619 C CD1 . TRP B 523 ? 1.2307 1.1977 0.9916 -0.0092 -0.0959 0.1798  773  TRP B CD1 
3620 C CD2 . TRP B 523 ? 1.0929 1.0729 0.8601 0.0062  -0.0714 0.1475  773  TRP B CD2 
3621 N NE1 . TRP B 523 ? 1.1962 1.1746 0.9548 -0.0123 -0.0808 0.1793  773  TRP B NE1 
3622 C CE2 . TRP B 523 ? 1.0190 1.0051 0.7814 -0.0025 -0.0662 0.1595  773  TRP B CE2 
3623 C CE3 . TRP B 523 ? 0.9966 0.9814 0.7682 0.0155  -0.0598 0.1280  773  TRP B CE3 
3624 C CZ2 . TRP B 523 ? 1.0648 1.0621 0.8275 -0.0010 -0.0500 0.1514  773  TRP B CZ2 
3625 C CZ3 . TRP B 523 ? 0.9612 0.9554 0.7323 0.0164  -0.0449 0.1215  773  TRP B CZ3 
3626 C CH2 . TRP B 523 ? 1.0742 1.0748 0.8412 0.0087  -0.0402 0.1326  773  TRP B CH2 
3627 N N   . GLY B 524 ? 1.0956 1.0911 0.8060 0.0004  -0.1041 0.1648  774  GLY B N   
3628 C CA  . GLY B 524 ? 1.1330 1.1553 0.8148 -0.0055 -0.0957 0.1675  774  GLY B CA  
3629 C C   . GLY B 524 ? 1.2238 1.2663 0.9030 -0.0013 -0.0750 0.1523  774  GLY B C   
3630 O O   . GLY B 524 ? 1.3603 1.4269 1.0210 -0.0020 -0.0676 0.1462  774  GLY B O   
3631 N N   . CYS B 525 ? 1.2032 1.2370 0.9012 0.0030  -0.0664 0.1452  775  CYS B N   
3632 C CA  . CYS B 525 ? 1.1425 1.1926 0.8400 0.0069  -0.0489 0.1316  775  CYS B CA  
3633 C C   . CYS B 525 ? 1.1058 1.1539 0.8124 0.0197  -0.0449 0.1105  775  CYS B C   
3634 O O   . CYS B 525 ? 1.2795 1.3123 1.0055 0.0264  -0.0427 0.1010  775  CYS B O   
3635 C CB  . CYS B 525 ? 1.0695 1.1107 0.7820 0.0053  -0.0429 0.1342  775  CYS B CB  
3636 S SG  . CYS B 525 ? 1.2562 1.3222 0.9607 0.0030  -0.0249 0.1281  775  CYS B SG  
3637 N N   . ASN B 526 ? 0.9488 1.0137 0.6412 0.0221  -0.0440 0.1030  776  ASN B N   
3638 C CA  . ASN B 526 ? 1.0997 1.1639 0.8000 0.0335  -0.0413 0.0833  776  ASN B CA  
3639 C C   . ASN B 526 ? 0.9944 1.0828 0.6865 0.0363  -0.0296 0.0702  776  ASN B C   
3640 O O   . ASN B 526 ? 0.9457 1.0577 0.6196 0.0322  -0.0289 0.0711  776  ASN B O   
3641 C CB  . ASN B 526 ? 1.0757 1.1365 0.7710 0.0360  -0.0532 0.0826  776  ASN B CB  
3642 C CG  . ASN B 526 ? 1.0680 1.1058 0.7732 0.0335  -0.0674 0.0948  776  ASN B CG  
3643 O OD1 . ASN B 526 ? 1.1901 1.2094 0.9162 0.0395  -0.0701 0.0871  776  ASN B OD1 
3644 N ND2 . ASN B 526 ? 1.2181 1.2577 0.9089 0.0239  -0.0773 0.1132  776  ASN B ND2 
3645 N N   . PRO B 527 ? 0.9648 1.0495 0.6701 0.0428  -0.0212 0.0574  777  PRO B N   
3646 C CA  . PRO B 527 ? 0.8804 0.9871 0.5818 0.0464  -0.0122 0.0433  777  PRO B CA  
3647 C C   . PRO B 527 ? 0.9587 1.0761 0.6568 0.0535  -0.0152 0.0288  777  PRO B C   
3648 O O   . PRO B 527 ? 1.0450 1.1470 0.7501 0.0585  -0.0219 0.0249  777  PRO B O   
3649 C CB  . PRO B 527 ? 0.9403 1.0329 0.6591 0.0516  -0.0064 0.0352  777  PRO B CB  
3650 C CG  . PRO B 527 ? 0.8995 0.9653 0.6310 0.0533  -0.0123 0.0384  777  PRO B CG  
3651 C CD  . PRO B 527 ? 0.9968 1.0579 0.7219 0.0465  -0.0204 0.0546  777  PRO B CD  
3652 N N   . ALA B 528 ? 0.8666 1.0125 0.5552 0.0538  -0.0101 0.0191  778  ALA B N   
3653 C CA  . ALA B 528 ? 0.9470 1.1083 0.6320 0.0602  -0.0128 0.0038  778  ALA B CA  
3654 C C   . ALA B 528 ? 1.0036 1.1623 0.7058 0.0714  -0.0103 -0.0171 778  ALA B C   
3655 O O   . ALA B 528 ? 1.0486 1.2198 0.7515 0.0778  -0.0129 -0.0323 778  ALA B O   
3656 C CB  . ALA B 528 ? 0.9720 1.1702 0.6377 0.0538  -0.0094 0.0027  778  ALA B CB  
3657 N N   . ASP B 529 ? 0.9525 1.0949 0.6687 0.0734  -0.0065 -0.0181 779  ASP B N   
3658 C CA  . ASP B 529 ? 0.8657 1.0030 0.5981 0.0825  -0.0061 -0.0357 779  ASP B CA  
3659 C C   . ASP B 529 ? 0.9141 1.0203 0.6599 0.0859  -0.0106 -0.0356 779  ASP B C   
3660 O O   . ASP B 529 ? 1.0959 1.1933 0.8549 0.0916  -0.0116 -0.0472 779  ASP B O   
3661 C CB  . ASP B 529 ? 0.8377 0.9815 0.5763 0.0823  0.0003  -0.0390 779  ASP B CB  
3662 C CG  . ASP B 529 ? 0.9943 1.1235 0.7316 0.0747  0.0040  -0.0214 779  ASP B CG  
3663 O OD1 . ASP B 529 ? 0.9665 1.0824 0.6985 0.0695  0.0013  -0.0068 779  ASP B OD1 
3664 O OD2 . ASP B 529 ? 0.9697 1.1008 0.7130 0.0745  0.0088  -0.0231 779  ASP B OD2 
3665 N N   . CYS B 530 ? 0.9378 1.0280 0.6814 0.0818  -0.0140 -0.0233 780  CYS B N   
3666 C CA  . CYS B 530 ? 1.0540 1.1209 0.8103 0.0846  -0.0182 -0.0266 780  CYS B CA  
3667 C C   . CYS B 530 ? 0.9021 0.9744 0.6597 0.0909  -0.0240 -0.0394 780  CYS B C   
3668 O O   . CYS B 530 ? 1.0079 1.0992 0.7539 0.0916  -0.0262 -0.0409 780  CYS B O   
3669 C CB  . CYS B 530 ? 0.8485 0.8990 0.6057 0.0790  -0.0207 -0.0128 780  CYS B CB  
3670 S SG  . CYS B 530 ? 1.0887 1.1236 0.8537 0.0731  -0.0153 -0.0024 780  CYS B SG  
3671 N N   . PRO B 531 ? 0.8776 0.9343 0.6487 0.0947  -0.0267 -0.0486 781  PRO B N   
3672 C CA  . PRO B 531 ? 0.9034 0.9635 0.6778 0.1005  -0.0329 -0.0607 781  PRO B CA  
3673 C C   . PRO B 531 ? 0.9274 0.9827 0.6977 0.0985  -0.0380 -0.0540 781  PRO B C   
3674 O O   . PRO B 531 ? 1.0146 1.0544 0.7958 0.0990  -0.0414 -0.0572 781  PRO B O   
3675 C CB  . PRO B 531 ? 0.8855 0.9275 0.6763 0.1026  -0.0343 -0.0696 781  PRO B CB  
3676 C CG  . PRO B 531 ? 0.9399 0.9650 0.7342 0.0957  -0.0298 -0.0583 781  PRO B CG  
3677 C CD  . PRO B 531 ? 1.0255 1.0621 0.8091 0.0928  -0.0246 -0.0485 781  PRO B CD  
3678 N N   . GLY B 532 ? 0.9607 1.0298 0.7157 0.0956  -0.0393 -0.0447 782  GLY B N   
3679 C CA  . GLY B 532 ? 0.9365 0.9995 0.6873 0.0931  -0.0464 -0.0358 782  GLY B CA  
3680 C C   . GLY B 532 ? 0.9776 1.0360 0.7215 0.0852  -0.0458 -0.0174 782  GLY B C   
3681 O O   . GLY B 532 ? 1.1153 1.1842 0.8506 0.0813  -0.0398 -0.0109 782  GLY B O   
3682 N N   . VAL B 533 ? 1.0225 1.0655 0.7724 0.0832  -0.0528 -0.0103 783  VAL B N   
3683 C CA  . VAL B 533 ? 0.8250 0.8605 0.5724 0.0763  -0.0552 0.0065  783  VAL B CA  
3684 C C   . VAL B 533 ? 0.8393 0.8588 0.6033 0.0747  -0.0496 0.0063  783  VAL B C   
3685 O O   . VAL B 533 ? 1.0021 1.0085 0.7820 0.0767  -0.0517 -0.0012 783  VAL B O   
3686 C CB  . VAL B 533 ? 0.8430 0.8710 0.5900 0.0753  -0.0684 0.0135  783  VAL B CB  
3687 C CG1 . VAL B 533 ? 0.9352 0.9538 0.6823 0.0681  -0.0729 0.0310  783  VAL B CG1 
3688 C CG2 . VAL B 533 ? 0.9133 0.9584 0.6418 0.0761  -0.0742 0.0138  783  VAL B CG2 
3689 N N   . GLY B 534 ? 0.8340 0.8563 0.5942 0.0704  -0.0424 0.0138  784  GLY B N   
3690 C CA  . GLY B 534 ? 0.8336 0.8427 0.6078 0.0682  -0.0372 0.0141  784  GLY B CA  
3691 C C   . GLY B 534 ? 0.8938 0.8895 0.6786 0.0649  -0.0442 0.0219  784  GLY B C   
3692 O O   . GLY B 534 ? 0.8665 0.8631 0.6446 0.0611  -0.0508 0.0348  784  GLY B O   
3693 N N   . THR B 535 ? 0.8209 0.8049 0.6234 0.0656  -0.0437 0.0136  785  THR B N   
3694 C CA  . THR B 535 ? 0.7799 0.7531 0.5979 0.0634  -0.0508 0.0162  785  THR B CA  
3695 C C   . THR B 535 ? 0.8182 0.7850 0.6513 0.0604  -0.0439 0.0114  785  THR B C   
3696 O O   . THR B 535 ? 0.7626 0.7226 0.6131 0.0593  -0.0489 0.0082  785  THR B O   
3697 C CB  . THR B 535 ? 0.7843 0.7533 0.6121 0.0674  -0.0603 0.0071  785  THR B CB  
3698 O OG1 . THR B 535 ? 1.1164 1.0867 0.9491 0.0701  -0.0545 -0.0075 785  THR B OG1 
3699 C CG2 . THR B 535 ? 0.8091 0.7836 0.6221 0.0694  -0.0700 0.0140  785  THR B CG2 
3700 N N   . GLY B 536 ? 0.8034 0.7730 0.6311 0.0589  -0.0334 0.0101  786  GLY B N   
3701 C CA  . GLY B 536 ? 0.7450 0.7097 0.5842 0.0551  -0.0267 0.0056  786  GLY B CA  
3702 C C   . GLY B 536 ? 0.8414 0.8049 0.6829 0.0513  -0.0250 0.0155  786  GLY B C   
3703 O O   . GLY B 536 ? 0.7896 0.7540 0.6267 0.0508  -0.0304 0.0265  786  GLY B O   
3704 N N   . CYS B 537 ? 0.7586 0.7201 0.6069 0.0476  -0.0179 0.0118  787  CYS B N   
3705 C CA  . CYS B 537 ? 0.7464 0.7070 0.5998 0.0440  -0.0158 0.0187  787  CYS B CA  
3706 C C   . CYS B 537 ? 0.8890 0.8541 0.7274 0.0438  -0.0105 0.0284  787  CYS B C   
3707 O O   . CYS B 537 ? 0.9621 0.9311 0.7890 0.0459  -0.0063 0.0261  787  CYS B O   
3708 C CB  . CYS B 537 ? 0.7504 0.7095 0.6159 0.0396  -0.0100 0.0100  787  CYS B CB  
3709 S SG  . CYS B 537 ? 0.9720 0.9319 0.8376 0.0355  -0.0036 0.0170  787  CYS B SG  
3710 N N   . THR B 538 ? 0.8545 0.8197 0.6952 0.0411  -0.0116 0.0380  788  THR B N   
3711 C CA  . THR B 538 ? 0.7701 0.7411 0.5998 0.0397  -0.0060 0.0464  788  THR B CA  
3712 C C   . THR B 538 ? 0.7563 0.7246 0.5949 0.0366  -0.0003 0.0448  788  THR B C   
3713 O O   . THR B 538 ? 0.8633 0.8280 0.7151 0.0340  -0.0033 0.0469  788  THR B O   
3714 C CB  . THR B 538 ? 0.7566 0.7309 0.5810 0.0374  -0.0115 0.0599  788  THR B CB  
3715 O OG1 . THR B 538 ? 0.7643 0.7416 0.5794 0.0394  -0.0179 0.0614  788  THR B OG1 
3716 C CG2 . THR B 538 ? 0.7446 0.7285 0.5576 0.0352  -0.0047 0.0668  788  THR B CG2 
3717 N N   . ALA B 539 ? 0.7981 0.7679 0.6304 0.0370  0.0067  0.0405  789  ALA B N   
3718 C CA  . ALA B 539 ? 0.8318 0.7990 0.6700 0.0337  0.0119  0.0385  789  ALA B CA  
3719 C C   . ALA B 539 ? 0.8396 0.8119 0.6724 0.0332  0.0154  0.0466  789  ALA B C   
3720 O O   . ALA B 539 ? 0.9519 0.9289 0.7746 0.0355  0.0185  0.0462  789  ALA B O   
3721 C CB  . ALA B 539 ? 0.7381 0.7019 0.5727 0.0333  0.0153  0.0302  789  ALA B CB  
3722 N N   . CYS B 540 ? 0.7773 0.7493 0.6191 0.0303  0.0141  0.0526  790  CYS B N   
3723 C CA  . CYS B 540 ? 0.8056 0.7825 0.6449 0.0287  0.0175  0.0600  790  CYS B CA  
3724 C C   . CYS B 540 ? 0.7501 0.7243 0.5968 0.0266  0.0218  0.0560  790  CYS B C   
3725 O O   . CYS B 540 ? 0.8648 0.8349 0.7234 0.0245  0.0205  0.0509  790  CYS B O   
3726 C CB  . CYS B 540 ? 0.7592 0.7368 0.6040 0.0257  0.0121  0.0707  790  CYS B CB  
3727 S SG  . CYS B 540 ? 0.8582 0.8395 0.6915 0.0260  0.0056  0.0780  790  CYS B SG  
3728 N N   . GLY B 541 ? 0.6968 0.6750 0.5372 0.0272  0.0265  0.0571  791  GLY B N   
3729 C CA  . GLY B 541 ? 0.6901 0.6656 0.5350 0.0253  0.0299  0.0535  791  GLY B CA  
3730 C C   . GLY B 541 ? 0.6895 0.6707 0.5322 0.0257  0.0333  0.0575  791  GLY B C   
3731 O O   . GLY B 541 ? 0.6942 0.6829 0.5292 0.0279  0.0344  0.0602  791  GLY B O   
3732 N N   . VAL B 542 ? 0.7064 0.6860 0.5567 0.0232  0.0350  0.0567  792  VAL B N   
3733 C CA  . VAL B 542 ? 0.6824 0.6663 0.5321 0.0236  0.0381  0.0583  792  VAL B CA  
3734 C C   . VAL B 542 ? 0.6812 0.6593 0.5268 0.0237  0.0385  0.0521  792  VAL B C   
3735 O O   . VAL B 542 ? 0.6914 0.6646 0.5402 0.0200  0.0381  0.0486  792  VAL B O   
3736 C CB  . VAL B 542 ? 0.7785 0.7648 0.6407 0.0204  0.0385  0.0627  792  VAL B CB  
3737 C CG1 . VAL B 542 ? 0.7557 0.7459 0.6182 0.0209  0.0417  0.0624  792  VAL B CG1 
3738 C CG2 . VAL B 542 ? 0.8201 0.8104 0.6853 0.0189  0.0362  0.0714  792  VAL B CG2 
3739 N N   . TYR B 543 ? 0.7394 0.7191 0.5784 0.0272  0.0386  0.0504  793  TYR B N   
3740 C CA  . TYR B 543 ? 0.7285 0.7002 0.5625 0.0273  0.0361  0.0459  793  TYR B CA  
3741 C C   . TYR B 543 ? 0.7304 0.7047 0.5666 0.0290  0.0364  0.0456  793  TYR B C   
3742 O O   . TYR B 543 ? 0.7475 0.7308 0.5848 0.0332  0.0375  0.0450  793  TYR B O   
3743 C CB  . TYR B 543 ? 0.7103 0.6782 0.5365 0.0312  0.0325  0.0419  793  TYR B CB  
3744 C CG  . TYR B 543 ? 0.6941 0.6603 0.5186 0.0301  0.0321  0.0416  793  TYR B CG  
3745 C CD1 . TYR B 543 ? 0.6944 0.6688 0.5188 0.0327  0.0332  0.0436  793  TYR B CD1 
3746 C CD2 . TYR B 543 ? 0.6958 0.6531 0.5182 0.0256  0.0303  0.0393  793  TYR B CD2 
3747 C CE1 . TYR B 543 ? 0.6957 0.6681 0.5191 0.0322  0.0317  0.0429  793  TYR B CE1 
3748 C CE2 . TYR B 543 ? 0.7077 0.6644 0.5304 0.0249  0.0298  0.0376  793  TYR B CE2 
3749 C CZ  . TYR B 543 ? 0.6958 0.6593 0.5194 0.0289  0.0301  0.0392  793  TYR B CZ  
3750 O OH  . TYR B 543 ? 0.6969 0.6593 0.5212 0.0287  0.0285  0.0372  793  TYR B OH  
3751 N N   . LEU B 544 ? 0.6944 0.6631 0.5317 0.0253  0.0354  0.0452  794  LEU B N   
3752 C CA  . LEU B 544 ? 0.7496 0.7193 0.5893 0.0268  0.0344  0.0444  794  LEU B CA  
3753 C C   . LEU B 544 ? 0.7523 0.7127 0.5849 0.0295  0.0273  0.0410  794  LEU B C   
3754 O O   . LEU B 544 ? 0.8342 0.7836 0.6602 0.0246  0.0231  0.0416  794  LEU B O   
3755 C CB  . LEU B 544 ? 0.6832 0.6524 0.5277 0.0212  0.0359  0.0454  794  LEU B CB  
3756 C CG  . LEU B 544 ? 0.7587 0.7355 0.6142 0.0187  0.0405  0.0475  794  LEU B CG  
3757 C CD1 . LEU B 544 ? 0.6701 0.6484 0.5323 0.0142  0.0413  0.0457  794  LEU B CD1 
3758 C CD2 . LEU B 544 ? 0.6770 0.6628 0.5387 0.0223  0.0431  0.0510  794  LEU B CD2 
3759 N N   . ASP B 545 ? 0.8314 0.7969 0.6663 0.0364  0.0253  0.0371  795  ASP B N   
3760 C CA  . ASP B 545 ? 0.7081 0.6647 0.5402 0.0406  0.0163  0.0321  795  ASP B CA  
3761 C C   . ASP B 545 ? 0.7194 0.6766 0.5573 0.0440  0.0120  0.0289  795  ASP B C   
3762 O O   . ASP B 545 ? 0.8009 0.7694 0.6456 0.0445  0.0176  0.0292  795  ASP B O   
3763 C CB  . ASP B 545 ? 0.7104 0.6740 0.5436 0.0472  0.0153  0.0262  795  ASP B CB  
3764 C CG  . ASP B 545 ? 0.7436 0.7068 0.5714 0.0445  0.0187  0.0289  795  ASP B CG  
3765 O OD1 . ASP B 545 ? 0.9153 0.8673 0.7378 0.0384  0.0177  0.0329  795  ASP B OD1 
3766 O OD2 . ASP B 545 ? 0.7632 0.7387 0.5919 0.0479  0.0223  0.0266  795  ASP B OD2 
3767 N N   . LYS B 546 ? 0.8322 0.7763 0.6682 0.0463  0.0008  0.0259  796  LYS B N   
3768 C CA  . LYS B 546 ? 0.7275 0.6695 0.5701 0.0507  -0.0067 0.0214  796  LYS B CA  
3769 C C   . LYS B 546 ? 0.7231 0.6656 0.5654 0.0455  -0.0032 0.0266  796  LYS B C   
3770 O O   . LYS B 546 ? 0.7203 0.6746 0.5719 0.0487  0.0006  0.0234  796  LYS B O   
3771 C CB  . LYS B 546 ? 0.7241 0.6835 0.5789 0.0600  -0.0050 0.0110  796  LYS B CB  
3772 C CG  . LYS B 546 ? 0.7273 0.6915 0.5837 0.0653  -0.0070 0.0038  796  LYS B CG  
3773 C CD  . LYS B 546 ? 0.7635 0.7460 0.6335 0.0744  -0.0082 -0.0100 796  LYS B CD  
3774 C CE  . LYS B 546 ? 1.1266 1.1222 0.9979 0.0786  -0.0059 -0.0179 796  LYS B CE  
3775 N NZ  . LYS B 546 ? 1.2515 1.2620 1.1156 0.0732  0.0081  -0.0108 796  LYS B NZ  
3776 N N   . LEU B 547 ? 0.8036 0.7348 0.6357 0.0366  -0.0045 0.0337  797  LEU B N   
3777 C CA  . LEU B 547 ? 0.7366 0.6689 0.5678 0.0309  -0.0021 0.0374  797  LEU B CA  
3778 C C   . LEU B 547 ? 0.8403 0.7625 0.6712 0.0328  -0.0140 0.0362  797  LEU B C   
3779 O O   . LEU B 547 ? 0.8451 0.7508 0.6678 0.0306  -0.0259 0.0385  797  LEU B O   
3780 C CB  . LEU B 547 ? 0.7322 0.6601 0.5528 0.0200  0.0010  0.0432  797  LEU B CB  
3781 C CG  . LEU B 547 ? 0.7150 0.6514 0.5373 0.0179  0.0109  0.0436  797  LEU B CG  
3782 C CD1 . LEU B 547 ? 0.7181 0.6515 0.5316 0.0070  0.0126  0.0465  797  LEU B CD1 
3783 C CD2 . LEU B 547 ? 0.7759 0.7274 0.6105 0.0209  0.0201  0.0424  797  LEU B CD2 
3784 N N   . LYS B 548 ? 0.8394 0.7706 0.6798 0.0364  -0.0120 0.0331  798  LYS B N   
3785 C CA  . LYS B 548 ? 0.8099 0.7327 0.6521 0.0389  -0.0237 0.0311  798  LYS B CA  
3786 C C   . LYS B 548 ? 0.7997 0.7262 0.6403 0.0330  -0.0204 0.0344  798  LYS B C   
3787 O O   . LYS B 548 ? 0.8031 0.7440 0.6505 0.0317  -0.0084 0.0339  798  LYS B O   
3788 C CB  . LYS B 548 ? 0.8140 0.7463 0.6725 0.0504  -0.0261 0.0207  798  LYS B CB  
3789 C CG  . LYS B 548 ? 0.9472 0.8867 0.8114 0.0569  -0.0239 0.0144  798  LYS B CG  
3790 C CD  . LYS B 548 ? 1.0851 1.0325 0.9652 0.0677  -0.0307 0.0015  798  LYS B CD  
3791 C CE  . LYS B 548 ? 1.0841 1.0456 0.9754 0.0697  -0.0255 -0.0025 798  LYS B CE  
3792 N NZ  . LYS B 548 ? 1.2709 1.2523 1.1651 0.0663  -0.0083 0.0000  798  LYS B NZ  
3793 N N   . SER B 549 ? 0.8297 0.7430 0.6618 0.0290  -0.0322 0.0376  799  SER B N   
3794 C CA  . SER B 549 ? 0.7526 0.6705 0.5835 0.0241  -0.0308 0.0391  799  SER B CA  
3795 C C   . SER B 549 ? 0.8606 0.7889 0.7090 0.0336  -0.0299 0.0314  799  SER B C   
3796 O O   . SER B 549 ? 0.7621 0.6859 0.6184 0.0421  -0.0394 0.0257  799  SER B O   
3797 C CB  . SER B 549 ? 0.8079 0.7088 0.6225 0.0161  -0.0450 0.0458  799  SER B CB  
3798 O OG  . SER B 549 ? 0.8418 0.7482 0.6558 0.0126  -0.0452 0.0457  799  SER B OG  
3799 N N   . VAL B 550 ? 0.7306 0.6737 0.5870 0.0320  -0.0190 0.0300  800  VAL B N   
3800 C CA  . VAL B 550 ? 0.7750 0.7297 0.6485 0.0392  -0.0168 0.0230  800  VAL B CA  
3801 C C   . VAL B 550 ? 0.8112 0.7667 0.6846 0.0358  -0.0202 0.0230  800  VAL B C   
3802 O O   . VAL B 550 ? 0.8813 0.8464 0.7695 0.0412  -0.0189 0.0169  800  VAL B O   
3803 C CB  . VAL B 550 ? 0.7747 0.7472 0.6615 0.0409  -0.0021 0.0210  800  VAL B CB  
3804 C CG1 . VAL B 550 ? 0.7413 0.7160 0.6295 0.0456  0.0001  0.0193  800  VAL B CG1 
3805 C CG2 . VAL B 550 ? 0.6958 0.6729 0.5794 0.0327  0.0069  0.0259  800  VAL B CG2 
3806 N N   . GLY B 551 ? 0.8729 0.8206 0.7301 0.0264  -0.0242 0.0288  801  GLY B N   
3807 C CA  . GLY B 551 ? 0.8885 0.8378 0.7433 0.0225  -0.0284 0.0284  801  GLY B CA  
3808 C C   . GLY B 551 ? 0.8186 0.7715 0.6595 0.0099  -0.0240 0.0327  801  GLY B C   
3809 O O   . GLY B 551 ? 0.8489 0.8051 0.6859 0.0050  -0.0160 0.0347  801  GLY B O   
3810 N N   . LYS B 552 ? 0.8772 0.8311 0.7113 0.0045  -0.0297 0.0328  802  LYS B N   
3811 C CA  . LYS B 552 ? 0.8837 0.8455 0.7047 -0.0084 -0.0259 0.0344  802  LYS B CA  
3812 C C   . LYS B 552 ? 0.8911 0.8737 0.7297 -0.0076 -0.0145 0.0259  802  LYS B C   
3813 O O   . LYS B 552 ? 0.9037 0.8918 0.7601 0.0010  -0.0137 0.0206  802  LYS B O   
3814 C CB  . LYS B 552 ? 0.8829 0.8352 0.6836 -0.0169 -0.0397 0.0399  802  LYS B CB  
3815 C CG  . LYS B 552 ? 0.9355 0.8637 0.7216 -0.0169 -0.0555 0.0487  802  LYS B CG  
3816 C CD  . LYS B 552 ? 0.9885 0.9073 0.7501 -0.0299 -0.0691 0.0572  802  LYS B CD  
3817 C CE  . LYS B 552 ? 1.2439 1.1355 0.9949 -0.0286 -0.0890 0.0660  802  LYS B CE  
3818 N NZ  . LYS B 552 ? 1.2366 1.1203 1.0046 -0.0138 -0.1000 0.0603  802  LYS B NZ  
3819 N N   . ALA B 553 ? 0.7953 0.7904 0.6307 -0.0168 -0.0064 0.0236  803  ALA B N   
3820 C CA  . ALA B 553 ? 0.8288 0.8438 0.6826 -0.0168 0.0029  0.0141  803  ALA B CA  
3821 C C   . ALA B 553 ? 0.9018 0.9296 0.7437 -0.0291 0.0024  0.0101  803  ALA B C   
3822 O O   . ALA B 553 ? 0.8691 0.8951 0.6898 -0.0405 0.0007  0.0145  803  ALA B O   
3823 C CB  . ALA B 553 ? 0.7540 0.7762 0.6222 -0.0151 0.0136  0.0113  803  ALA B CB  
3824 N N   . PHE B 554 ? 0.8408 0.8831 0.6963 -0.0276 0.0039  0.0014  804  PHE B N   
3825 C CA  . PHE B 554 ? 0.8630 0.9224 0.7098 -0.0389 0.0040  -0.0052 804  PHE B CA  
3826 C C   . PHE B 554 ? 0.7845 0.8662 0.6589 -0.0361 0.0128  -0.0196 804  PHE B C   
3827 O O   . PHE B 554 ? 0.8502 0.9318 0.7482 -0.0253 0.0142  -0.0230 804  PHE B O   
3828 C CB  . PHE B 554 ? 0.8311 0.8854 0.6641 -0.0407 -0.0072 -0.0020 804  PHE B CB  
3829 C CG  . PHE B 554 ? 0.9474 0.9766 0.7584 -0.0411 -0.0194 0.0117  804  PHE B CG  
3830 C CD1 . PHE B 554 ? 1.0334 1.0560 0.8155 -0.0550 -0.0250 0.0206  804  PHE B CD1 
3831 C CD2 . PHE B 554 ? 0.9236 0.9367 0.7444 -0.0281 -0.0261 0.0148  804  PHE B CD2 
3832 C CE1 . PHE B 554 ? 0.9570 0.9545 0.7214 -0.0553 -0.0386 0.0334  804  PHE B CE1 
3833 C CE2 . PHE B 554 ? 0.9408 0.9311 0.7453 -0.0274 -0.0393 0.0252  804  PHE B CE2 
3834 C CZ  . PHE B 554 ? 0.9171 0.8980 0.6938 -0.0407 -0.0463 0.0350  804  PHE B CZ  
3835 N N   . LYS B 555 ? 0.8397 0.9414 0.7124 -0.0465 0.0181  -0.0288 805  LYS B N   
3836 C CA  . LYS B 555 ? 0.8732 0.9979 0.7739 -0.0446 0.0246  -0.0451 805  LYS B CA  
3837 C C   . LYS B 555 ? 0.9074 1.0509 0.8044 -0.0509 0.0219  -0.0547 805  LYS B C   
3838 O O   . LYS B 555 ? 0.9816 1.1317 0.8518 -0.0639 0.0195  -0.0529 805  LYS B O   
3839 C CB  . LYS B 555 ? 0.8788 1.0170 0.7858 -0.0506 0.0321  -0.0531 805  LYS B CB  
3840 C CG  . LYS B 555 ? 1.0578 1.2200 0.9973 -0.0483 0.0368  -0.0722 805  LYS B CG  
3841 C CD  . LYS B 555 ? 1.2009 1.3664 1.1570 -0.0471 0.0419  -0.0774 805  LYS B CD  
3842 C CE  . LYS B 555 ? 1.1606 1.3013 1.1236 -0.0363 0.0410  -0.0639 805  LYS B CE  
3843 N NZ  . LYS B 555 ? 1.0925 1.2334 1.0669 -0.0358 0.0445  -0.0665 805  LYS B NZ  
3844 N N   . ILE B 556 ? 0.9907 1.1434 0.9142 -0.0426 0.0221  -0.0647 806  ILE B N   
3845 C CA  . ILE B 556 ? 0.9163 1.0869 0.8389 -0.0467 0.0190  -0.0747 806  ILE B CA  
3846 C C   . ILE B 556 ? 0.8926 1.0947 0.8243 -0.0558 0.0252  -0.0931 806  ILE B C   
3847 O O   . ILE B 556 ? 0.9539 1.1671 0.9169 -0.0504 0.0302  -0.1055 806  ILE B O   
3848 C CB  . ILE B 556 ? 0.9322 1.1008 0.8816 -0.0341 0.0164  -0.0791 806  ILE B CB  
3849 C CG1 . ILE B 556 ? 0.8725 1.0145 0.8116 -0.0263 0.0097  -0.0636 806  ILE B CG1 
3850 C CG2 . ILE B 556 ? 0.8527 1.0437 0.8059 -0.0378 0.0139  -0.0928 806  ILE B CG2 
3851 C CD1 . ILE B 556 ? 0.7002 0.8410 0.6650 -0.0148 0.0076  -0.0677 806  ILE B CD1 
3852 N N   . VAL B 557 ? 0.9120 1.1294 0.8171 -0.0703 0.0241  -0.0954 807  VAL B N   
3853 C CA  . VAL B 557 ? 0.9629 1.2156 0.8759 -0.0804 0.0305  -0.1156 807  VAL B CA  
3854 C C   . VAL B 557 ? 0.9551 1.2309 0.8877 -0.0776 0.0290  -0.1329 807  VAL B C   
3855 O O   . VAL B 557 ? 0.9272 1.2263 0.8925 -0.0742 0.0334  -0.1536 807  VAL B O   
3856 C CB  . VAL B 557 ? 1.0189 1.2815 0.8932 -0.1000 0.0313  -0.1106 807  VAL B CB  
3857 C CG1 . VAL B 557 ? 0.9185 1.2231 0.8015 -0.1116 0.0389  -0.1342 807  VAL B CG1 
3858 C CG2 . VAL B 557 ? 0.9529 1.1925 0.8114 -0.1021 0.0326  -0.0946 807  VAL B CG2 
3859 N N   . SER B 558 ? 0.9206 1.1896 0.8350 -0.0785 0.0215  -0.1253 808  SER B N   
3860 C CA  . SER B 558 ? 0.8682 1.1572 0.7993 -0.0754 0.0189  -0.1406 808  SER B CA  
3861 C C   . SER B 558 ? 0.9071 1.1722 0.8271 -0.0682 0.0091  -0.1262 808  SER B C   
3862 O O   . SER B 558 ? 0.9431 1.1795 0.8399 -0.0678 0.0038  -0.1060 808  SER B O   
3863 C CB  . SER B 558 ? 0.9020 1.2276 0.8167 -0.0922 0.0212  -0.1553 808  SER B CB  
3864 O OG  . SER B 558 ? 1.1453 1.4628 1.0137 -0.1069 0.0159  -0.1385 808  SER B OG  
3865 N N   . LEU B 559 ? 0.9385 1.2164 0.8775 -0.0622 0.0060  -0.1384 809  LEU B N   
3866 C CA  . LEU B 559 ? 0.9925 1.2509 0.9280 -0.0537 -0.0033 -0.1288 809  LEU B CA  
3867 C C   . LEU B 559 ? 1.0870 1.3682 1.0170 -0.0589 -0.0085 -0.1406 809  LEU B C   
3868 O O   . LEU B 559 ? 0.8708 1.1838 0.8201 -0.0615 -0.0035 -0.1618 809  LEU B O   
3869 C CB  . LEU B 559 ? 0.9920 1.2367 0.9655 -0.0363 -0.0020 -0.1301 809  LEU B CB  
3870 C CG  . LEU B 559 ? 1.0120 1.2286 0.9863 -0.0298 0.0002  -0.1142 809  LEU B CG  
3871 C CD1 . LEU B 559 ? 0.9199 1.1343 0.9353 -0.0174 0.0047  -0.1200 809  LEU B CD1 
3872 C CD2 . LEU B 559 ? 0.8993 1.0885 0.8505 -0.0266 -0.0087 -0.0962 809  LEU B CD2 
3873 N N   . ARG B 560 ? 1.0295 1.2945 0.9344 -0.0600 -0.0195 -0.1278 810  ARG B N   
3874 C CA  . ARG B 560 ? 1.0257 1.3084 0.9211 -0.0648 -0.0267 -0.1359 810  ARG B CA  
3875 C C   . ARG B 560 ? 1.0409 1.2968 0.9327 -0.0546 -0.0392 -0.1240 810  ARG B C   
3876 O O   . ARG B 560 ? 1.1600 1.3853 1.0355 -0.0521 -0.0453 -0.1053 810  ARG B O   
3877 C CB  . ARG B 560 ? 1.1219 1.4204 0.9751 -0.0860 -0.0290 -0.1322 810  ARG B CB  
3878 C CG  . ARG B 560 ? 1.2008 1.5109 1.0334 -0.0931 -0.0398 -0.1340 810  ARG B CG  
3879 C CD  . ARG B 560 ? 1.1860 1.5186 0.9786 -0.1170 -0.0398 -0.1324 810  ARG B CD  
3880 N NE  . ARG B 560 ? 1.2400 1.5544 1.0059 -0.1273 -0.0384 -0.1141 810  ARG B NE  
3881 C CZ  . ARG B 560 ? 1.3615 1.6454 1.0918 -0.1341 -0.0512 -0.0895 810  ARG B CZ  
3882 N NH1 . ARG B 560 ? 1.2614 1.5291 0.9781 -0.1314 -0.0669 -0.0803 810  ARG B NH1 
3883 N NH2 . ARG B 560 ? 1.2512 1.5203 0.9610 -0.1433 -0.0493 -0.0747 810  ARG B NH2 
3884 N N   . TYR B 561 ? 1.0828 1.3513 0.9919 -0.0482 -0.0435 -0.1365 811  TYR B N   
3885 C CA  . TYR B 561 ? 1.0839 1.3307 0.9984 -0.0363 -0.0546 -0.1298 811  TYR B CA  
3886 C C   . TYR B 561 ? 1.0541 1.3125 0.9480 -0.0430 -0.0662 -0.1331 811  TYR B C   
3887 O O   . TYR B 561 ? 1.0478 1.3375 0.9522 -0.0467 -0.0628 -0.1513 811  TYR B O   
3888 C CB  . TYR B 561 ? 1.0012 1.2493 0.9629 -0.0197 -0.0488 -0.1415 811  TYR B CB  
3889 C CG  . TYR B 561 ? 1.0322 1.2738 1.0152 -0.0150 -0.0373 -0.1398 811  TYR B CG  
3890 C CD1 . TYR B 561 ? 0.8502 1.1150 0.8540 -0.0179 -0.0268 -0.1545 811  TYR B CD1 
3891 C CD2 . TYR B 561 ? 1.0833 1.2961 1.0657 -0.0078 -0.0378 -0.1243 811  TYR B CD2 
3892 C CE1 . TYR B 561 ? 0.9664 1.2237 0.9889 -0.0139 -0.0181 -0.1521 811  TYR B CE1 
3893 C CE2 . TYR B 561 ? 1.0380 1.2453 1.0375 -0.0044 -0.0278 -0.1220 811  TYR B CE2 
3894 C CZ  . TYR B 561 ? 0.9740 1.2023 0.9928 -0.0075 -0.0185 -0.1350 811  TYR B CZ  
3895 O OH  . TYR B 561 ? 0.9229 1.1442 0.9585 -0.0043 -0.0105 -0.1319 811  TYR B OH  
3896 N N   . THR B 562 ? 0.9511 1.2545 0.8962 -0.1217 -0.0980 -0.1976 812  THR B N   
3897 C CA  . THR B 562 ? 0.9953 1.2972 0.9702 -0.1208 -0.0835 -0.1954 812  THR B CA  
3898 C C   . THR B 562 ? 1.0490 1.3094 1.0110 -0.1267 -0.0644 -0.1987 812  THR B C   
3899 O O   . THR B 562 ? 1.0152 1.2518 0.9511 -0.1382 -0.0607 -0.2059 812  THR B O   
3900 C CB  . THR B 562 ? 0.9083 1.2370 0.9131 -0.1340 -0.0836 -0.2006 812  THR B CB  
3901 O OG1 . THR B 562 ? 0.9257 1.2338 0.9206 -0.1533 -0.0740 -0.2103 812  THR B OG1 
3902 C CG2 . THR B 562 ? 1.0680 1.4381 1.0810 -0.1339 -0.1028 -0.2020 812  THR B CG2 
3903 N N   . ARG B 563 ? 0.9063 1.1593 0.8875 -0.1190 -0.0523 -0.1939 813  ARG B N   
3904 C CA  . ARG B 563 ? 1.0015 1.2206 0.9788 -0.1236 -0.0338 -0.1974 813  ARG B CA  
3905 C C   . ARG B 563 ? 0.9191 1.1467 0.9308 -0.1242 -0.0248 -0.1955 813  ARG B C   
3906 O O   . ARG B 563 ? 0.9845 1.2344 1.0179 -0.1138 -0.0287 -0.1879 813  ARG B O   
3907 C CB  . ARG B 563 ? 0.9956 1.1899 0.9532 -0.1113 -0.0273 -0.1935 813  ARG B CB  
3908 C CG  . ARG B 563 ? 1.0814 1.2609 0.9997 -0.1108 -0.0352 -0.1947 813  ARG B CG  
3909 C CD  . ARG B 563 ? 1.0554 1.1982 0.9488 -0.1065 -0.0222 -0.1953 813  ARG B CD  
3910 N NE  . ARG B 563 ? 1.1793 1.2958 1.0718 -0.1190 -0.0049 -0.2047 813  ARG B NE  
3911 C CZ  . ARG B 563 ? 1.2196 1.3018 1.0839 -0.1233 0.0064  -0.2105 813  ARG B CZ  
3912 N NH1 . ARG B 563 ? 1.2497 1.3170 1.0810 -0.1166 0.0022  -0.2072 813  ARG B NH1 
3913 N NH2 . ARG B 563 ? 1.2958 1.3573 1.1640 -0.1342 0.0223  -0.2199 813  ARG B NH2 
3914 N N   . LYS B 564 ? 0.9717 1.1805 0.9875 -0.1363 -0.0126 -0.2022 814  LYS B N   
3915 C CA  . LYS B 564 ? 0.8959 1.1087 0.9413 -0.1375 -0.0041 -0.2003 814  LYS B CA  
3916 C C   . LYS B 564 ? 0.8780 1.0778 0.9316 -0.1246 0.0062  -0.1950 814  LYS B C   
3917 O O   . LYS B 564 ? 0.8763 1.0485 0.9155 -0.1243 0.0167  -0.1992 814  LYS B O   
3918 C CB  . LYS B 564 ? 0.9086 1.1028 0.9538 -0.1538 0.0055  -0.2093 814  LYS B CB  
3919 C CG  . LYS B 564 ? 0.9084 1.1058 0.9815 -0.1563 0.0125  -0.2070 814  LYS B CG  
3920 C CD  . LYS B 564 ? 1.0176 1.1867 1.0875 -0.1687 0.0254  -0.2156 814  LYS B CD  
3921 C CE  . LYS B 564 ? 1.3225 1.4870 1.3711 -0.1849 0.0222  -0.2255 814  LYS B CE  
3922 N NZ  . LYS B 564 ? 1.1979 1.3285 1.2369 -0.1952 0.0367  -0.2351 814  LYS B NZ  
3923 N N   . ALA B 565 ? 0.7586 0.9791 0.8352 -0.1150 0.0037  -0.1867 815  ALA B N   
3924 C CA  . ALA B 565 ? 0.7277 0.9408 0.8144 -0.1032 0.0125  -0.1816 815  ALA B CA  
3925 C C   . ALA B 565 ? 0.7910 1.0025 0.9025 -0.1063 0.0207  -0.1806 815  ALA B C   
3926 O O   . ALA B 565 ? 0.8725 1.1041 1.0021 -0.1094 0.0157  -0.1769 815  ALA B O   
3927 C CB  . ALA B 565 ? 0.8867 1.1225 0.9799 -0.0898 0.0045  -0.1729 815  ALA B CB  
3928 N N   . CYS B 566 ? 0.7470 0.9342 0.8587 -0.1055 0.0334  -0.1842 816  CYS B N   
3929 C CA  . CYS B 566 ? 0.7559 0.9385 0.8898 -0.1057 0.0412  -0.1826 816  CYS B CA  
3930 C C   . CYS B 566 ? 0.8284 1.0094 0.9721 -0.0929 0.0477  -0.1784 816  CYS B C   
3931 O O   . CYS B 566 ? 0.8203 0.9876 0.9501 -0.0885 0.0534  -0.1822 816  CYS B O   
3932 C CB  . CYS B 566 ? 0.7185 0.8749 0.8478 -0.1158 0.0506  -0.1916 816  CYS B CB  
3933 S SG  . CYS B 566 ? 0.9378 1.0956 1.0611 -0.1333 0.0456  -0.1969 816  CYS B SG  
3934 N N   . ILE B 567 ? 0.7259 0.9205 0.8919 -0.0881 0.0471  -0.1712 817  ILE B N   
3935 C CA  . ILE B 567 ? 0.7505 0.9497 0.9276 -0.0765 0.0516  -0.1665 817  ILE B CA  
3936 C C   . ILE B 567 ? 0.7261 0.9206 0.9239 -0.0754 0.0572  -0.1644 817  ILE B C   
3937 O O   . ILE B 567 ? 0.7937 0.9938 1.0019 -0.0808 0.0535  -0.1606 817  ILE B O   
3938 C CB  . ILE B 567 ? 0.7399 0.9652 0.9224 -0.0698 0.0433  -0.1581 817  ILE B CB  
3939 C CG1 . ILE B 567 ? 0.7159 0.9450 0.8776 -0.0686 0.0368  -0.1596 817  ILE B CG1 
3940 C CG2 . ILE B 567 ? 0.6036 0.8335 0.7973 -0.0593 0.0488  -0.1539 817  ILE B CG2 
3941 C CD1 . ILE B 567 ? 0.6183 0.8744 0.7865 -0.0630 0.0274  -0.1522 817  ILE B CD1 
3942 N N   . GLN B 568 ? 0.7464 0.9303 0.9494 -0.0686 0.0661  -0.1671 818  GLN B N   
3943 C CA  . GLN B 568 ? 0.7037 0.8857 0.9274 -0.0641 0.0703  -0.1643 818  GLN B CA  
3944 C C   . GLN B 568 ? 0.7645 0.9618 0.9980 -0.0538 0.0710  -0.1592 818  GLN B C   
3945 O O   . GLN B 568 ? 0.8678 1.0592 1.0968 -0.0489 0.0781  -0.1646 818  GLN B O   
3946 C CB  . GLN B 568 ? 0.7047 0.8625 0.9293 -0.0651 0.0804  -0.1736 818  GLN B CB  
3947 C CG  . GLN B 568 ? 0.6938 0.8497 0.9406 -0.0582 0.0840  -0.1709 818  GLN B CG  
3948 C CD  . GLN B 568 ? 0.7915 0.9450 1.0473 -0.0624 0.0795  -0.1646 818  GLN B CD  
3949 O OE1 . GLN B 568 ? 0.8547 0.9974 1.1010 -0.0724 0.0787  -0.1675 818  GLN B OE1 
3950 N NE2 . GLN B 568 ? 0.7551 0.9175 1.0277 -0.0556 0.0768  -0.1562 818  GLN B NE2 
3951 N N   . LEU B 569 ? 0.6641 0.8806 0.9098 -0.0516 0.0646  -0.1496 819  LEU B N   
3952 C CA  . LEU B 569 ? 0.6783 0.9111 0.9333 -0.0432 0.0650  -0.1444 819  LEU B CA  
3953 C C   . LEU B 569 ? 0.6989 0.9346 0.9733 -0.0399 0.0651  -0.1390 819  LEU B C   
3954 O O   . LEU B 569 ? 0.7514 0.9949 1.0325 -0.0433 0.0591  -0.1315 819  LEU B O   
3955 C CB  . LEU B 569 ? 0.7397 0.9935 0.9915 -0.0432 0.0576  -0.1379 819  LEU B CB  
3956 C CG  . LEU B 569 ? 0.5374 0.8081 0.7977 -0.0356 0.0587  -0.1328 819  LEU B CG  
3957 C CD1 . LEU B 569 ? 0.6047 0.8681 0.8550 -0.0300 0.0665  -0.1390 819  LEU B CD1 
3958 C CD2 . LEU B 569 ? 0.5929 0.8849 0.8541 -0.0365 0.0513  -0.1260 819  LEU B CD2 
3959 N N   . GLY B 570 ? 0.7104 0.9399 0.9932 -0.0334 0.0719  -0.1432 820  GLY B N   
3960 C CA  . GLY B 570 ? 0.7723 1.0041 1.0731 -0.0288 0.0710  -0.1381 820  GLY B CA  
3961 C C   . GLY B 570 ? 0.7898 1.0047 1.0929 -0.0334 0.0694  -0.1372 820  GLY B C   
3962 O O   . GLY B 570 ? 0.8468 1.0426 1.1441 -0.0366 0.0744  -0.1454 820  GLY B O   
3963 N N   . THR B 571 ? 0.7668 0.9870 1.0769 -0.0345 0.0632  -0.1273 821  THR B N   
3964 C CA  . THR B 571 ? 0.6995 0.9023 1.0098 -0.0398 0.0618  -0.1250 821  THR B CA  
3965 C C   . THR B 571 ? 0.8106 1.0136 1.1083 -0.0519 0.0581  -0.1243 821  THR B C   
3966 O O   . THR B 571 ? 0.8158 1.0049 1.1117 -0.0585 0.0573  -0.1223 821  THR B O   
3967 C CB  . THR B 571 ? 0.7456 0.9505 1.0675 -0.0352 0.0575  -0.1146 821  THR B CB  
3968 O OG1 . THR B 571 ? 1.2000 1.3882 1.5175 -0.0426 0.0557  -0.1107 821  THR B OG1 
3969 C CG2 . THR B 571 ? 0.9878 1.2178 1.3117 -0.0348 0.0521  -0.1063 821  THR B CG2 
3970 N N   . GLU B 572 ? 0.8714 1.0896 1.1605 -0.0548 0.0559  -0.1261 822  GLU B N   
3971 C CA  . GLU B 572 ? 0.7261 0.9498 1.0052 -0.0655 0.0513  -0.1263 822  GLU B CA  
3972 C C   . GLU B 572 ? 0.7030 0.9161 0.9679 -0.0700 0.0538  -0.1364 822  GLU B C   
3973 O O   . GLU B 572 ? 0.7486 0.9561 1.0091 -0.0644 0.0586  -0.1423 822  GLU B O   
3974 C CB  . GLU B 572 ? 0.7018 0.9523 0.9822 -0.0651 0.0454  -0.1207 822  GLU B CB  
3975 C CG  . GLU B 572 ? 0.7644 1.0262 1.0564 -0.0632 0.0428  -0.1108 822  GLU B CG  
3976 C CD  . GLU B 572 ? 0.8382 1.1260 1.1316 -0.0648 0.0380  -0.1065 822  GLU B CD  
3977 O OE1 . GLU B 572 ? 0.8726 1.1705 1.1734 -0.0657 0.0360  -0.0989 822  GLU B OE1 
3978 O OE2 . GLU B 572 ? 0.8523 1.1500 1.1390 -0.0650 0.0363  -0.1108 822  GLU B OE2 
3979 N N   . GLN B 573 ? 0.6726 0.8829 0.9291 -0.0812 0.0509  -0.1387 823  GLN B N   
3980 C CA  . GLN B 573 ? 0.6499 0.8498 0.8910 -0.0875 0.0524  -0.1482 823  GLN B CA  
3981 C C   . GLN B 573 ? 0.6331 0.8476 0.8673 -0.0981 0.0449  -0.1484 823  GLN B C   
3982 O O   . GLN B 573 ? 0.6991 0.9203 0.9400 -0.1047 0.0421  -0.1439 823  GLN B O   
3983 C CB  . GLN B 573 ? 0.8240 0.9954 1.0629 -0.0917 0.0602  -0.1549 823  GLN B CB  
3984 C CG  . GLN B 573 ? 0.9253 1.0841 1.1467 -0.1005 0.0625  -0.1653 823  GLN B CG  
3985 C CD  . GLN B 573 ? 1.0255 1.1556 1.2458 -0.1055 0.0712  -0.1723 823  GLN B CD  
3986 O OE1 . GLN B 573 ? 0.9938 1.1124 1.2273 -0.0997 0.0758  -0.1695 823  GLN B OE1 
3987 N NE2 . GLN B 573 ? 1.0868 1.2050 1.2911 -0.1162 0.0735  -0.1815 823  GLN B NE2 
3988 N N   . THR B 574 ? 0.7023 0.9218 0.9226 -0.0999 0.0418  -0.1539 824  THR B N   
3989 C CA  . THR B 574 ? 0.7369 0.9725 0.9511 -0.1095 0.0337  -0.1556 824  THR B CA  
3990 C C   . THR B 574 ? 0.6889 0.9176 0.8834 -0.1126 0.0323  -0.1639 824  THR B C   
3991 O O   . THR B 574 ? 0.7616 0.9792 0.9469 -0.1053 0.0362  -0.1664 824  THR B O   
3992 C CB  . THR B 574 ? 0.6872 0.9532 0.9102 -0.1046 0.0259  -0.1488 824  THR B CB  
3993 O OG1 . THR B 574 ? 0.9048 1.1885 1.1265 -0.1149 0.0183  -0.1512 824  THR B OG1 
3994 C CG2 . THR B 574 ? 0.7401 1.0131 0.9562 -0.0930 0.0240  -0.1481 824  THR B CG2 
3995 N N   . CYS B 575 ? 0.7720 1.0071 0.9592 -0.1246 0.0270  -0.1686 825  CYS B N   
3996 C CA  . CYS B 575 ? 0.8977 1.1299 1.0648 -0.1291 0.0232  -0.1761 825  CYS B CA  
3997 C C   . CYS B 575 ? 0.8379 1.0995 1.0052 -0.1342 0.0110  -0.1760 825  CYS B C   
3998 O O   . CYS B 575 ? 0.9478 1.2209 1.1255 -0.1440 0.0091  -0.1762 825  CYS B O   
3999 C CB  . CYS B 575 ? 0.7476 0.9533 0.9031 -0.1412 0.0305  -0.1853 825  CYS B CB  
4000 S SG  . CYS B 575 ? 1.0160 1.1866 1.1693 -0.1356 0.0451  -0.1890 825  CYS B SG  
4001 N N   . LYS B 576 ? 0.7417 1.0150 0.8974 -0.1275 0.0030  -0.1760 826  LYS B N   
4002 C CA  . LYS B 576 ? 0.8115 1.1153 0.9686 -0.1300 -0.0099 -0.1764 826  LYS B CA  
4003 C C   . LYS B 576 ? 0.7811 1.0825 0.9145 -0.1279 -0.0172 -0.1805 826  LYS B C   
4004 O O   . LYS B 576 ? 0.8446 1.1287 0.9638 -0.1183 -0.0139 -0.1790 826  LYS B O   
4005 C CB  . LYS B 576 ? 0.7566 1.0869 0.9316 -0.1188 -0.0149 -0.1680 826  LYS B CB  
4006 C CG  . LYS B 576 ? 0.9506 1.2905 1.1478 -0.1239 -0.0109 -0.1643 826  LYS B CG  
4007 C CD  . LYS B 576 ? 1.0117 1.3757 1.2169 -0.1370 -0.0178 -0.1688 826  LYS B CD  
4008 C CE  . LYS B 576 ? 1.0845 1.4398 1.3002 -0.1494 -0.0098 -0.1690 826  LYS B CE  
4009 N NZ  . LYS B 576 ? 0.9384 1.2886 1.1672 -0.1414 -0.0034 -0.1601 826  LYS B NZ  
4010 N N   . ASN B 577 ? 0.8517 1.1703 0.9799 -0.1375 -0.0270 -0.1860 827  ASN B N   
4011 C CA  . ASN B 577 ? 0.8822 1.2029 0.9875 -0.1352 -0.0370 -0.1890 827  ASN B CA  
4012 C C   . ASN B 577 ? 0.8914 1.2358 1.0010 -0.1189 -0.0477 -0.1818 827  ASN B C   
4013 O O   . ASN B 577 ? 1.0626 1.4368 1.1946 -0.1165 -0.0532 -0.1787 827  ASN B O   
4014 C CB  . ASN B 577 ? 0.8764 1.2105 0.9757 -0.1512 -0.0448 -0.1979 827  ASN B CB  
4015 C CG  . ASN B 577 ? 1.0347 1.3378 1.1154 -0.1655 -0.0357 -0.2065 827  ASN B CG  
4016 O OD1 . ASN B 577 ? 1.1164 1.4007 1.1715 -0.1649 -0.0361 -0.2095 827  ASN B OD1 
4017 N ND2 . ASN B 577 ? 1.1260 1.4223 1.2183 -0.1789 -0.0267 -0.2107 827  ASN B ND2 
4018 N N   . VAL B 578 ? 0.9585 1.2882 1.0461 -0.1081 -0.0498 -0.1794 828  VAL B N   
4019 C CA  . VAL B 578 ? 1.0002 1.3467 1.0878 -0.0914 -0.0592 -0.1723 828  VAL B CA  
4020 C C   . VAL B 578 ? 0.9554 1.3036 1.0169 -0.0896 -0.0725 -0.1747 828  VAL B C   
4021 O O   . VAL B 578 ? 1.0139 1.3370 1.0494 -0.0973 -0.0699 -0.1799 828  VAL B O   
4022 C CB  . VAL B 578 ? 0.8025 1.1280 0.8864 -0.0780 -0.0489 -0.1658 828  VAL B CB  
4023 C CG1 . VAL B 578 ? 0.8586 1.1786 0.9648 -0.0813 -0.0357 -0.1644 828  VAL B CG1 
4024 C CG2 . VAL B 578 ? 0.8461 1.1360 0.8971 -0.0773 -0.0433 -0.1684 828  VAL B CG2 
4025 N N   . ASP B 579 ? 0.9890 1.3677 1.0578 -0.0796 -0.0870 -0.1712 829  ASP B N   
4026 C CA  . ASP B 579 ? 1.0018 1.3823 1.0451 -0.0731 -0.1014 -0.1711 829  ASP B CA  
4027 C C   . ASP B 579 ? 1.0827 1.4719 1.1273 -0.0517 -0.1077 -0.1619 829  ASP B C   
4028 O O   . ASP B 579 ? 1.1769 1.5632 1.2368 -0.0435 -0.0981 -0.1565 829  ASP B O   
4029 C CB  . ASP B 579 ? 1.0799 1.4921 1.1288 -0.0833 -0.1162 -0.1780 829  ASP B CB  
4030 C CG  . ASP B 579 ? 1.1537 1.6100 1.2381 -0.0796 -0.1239 -0.1771 829  ASP B CG  
4031 O OD1 . ASP B 579 ? 1.2273 1.6940 1.3361 -0.0911 -0.1158 -0.1805 829  ASP B OD1 
4032 O OD2 . ASP B 579 ? 1.1613 1.6407 1.2487 -0.0650 -0.1377 -0.1732 829  ASP B OD2 
4033 N N   . SER B 580 ? 1.0875 1.4869 1.1155 -0.0425 -0.1240 -0.1602 830  SER B N   
4034 C CA  . SER B 580 ? 1.1521 1.5546 1.1771 -0.0209 -0.1298 -0.1513 830  SER B CA  
4035 C C   . SER B 580 ? 1.2724 1.7129 1.3367 -0.0133 -0.1324 -0.1487 830  SER B C   
4036 O O   . SER B 580 ? 1.2112 1.6473 1.2829 0.0002  -0.1261 -0.1420 830  SER B O   
4037 C CB  . SER B 580 ? 1.1753 1.5800 1.1728 -0.0122 -0.1481 -0.1499 830  SER B CB  
4038 O OG  . SER B 580 ? 1.2692 1.6360 1.2271 -0.0199 -0.1447 -0.1522 830  SER B OG  
4039 N N   . ASN B 581 ? 1.2675 1.7450 1.3566 -0.0228 -0.1407 -0.1549 831  ASN B N   
4040 C CA  . ASN B 581 ? 1.2417 1.7581 1.3679 -0.0170 -0.1439 -0.1540 831  ASN B CA  
4041 C C   . ASN B 581 ? 1.1609 1.6804 1.3135 -0.0291 -0.1287 -0.1558 831  ASN B C   
4042 O O   . ASN B 581 ? 1.2472 1.7952 1.4295 -0.0255 -0.1285 -0.1549 831  ASN B O   
4043 C CB  . ASN B 581 ? 1.2082 1.7674 1.3483 -0.0201 -0.1621 -0.1606 831  ASN B CB  
4044 C CG  . ASN B 581 ? 1.2698 1.8333 1.3890 -0.0037 -0.1801 -0.1572 831  ASN B CG  
4045 O OD1 . ASN B 581 ? 1.3555 1.9050 1.4642 0.0155  -0.1806 -0.1486 831  ASN B OD1 
4046 N ND2 . ASN B 581 ? 1.1438 1.7258 1.2556 -0.0114 -0.1950 -0.1640 831  ASN B ND2 
4047 N N   . ASP B 582 ? 1.2189 1.7095 1.3612 -0.0431 -0.1160 -0.1584 832  ASP B N   
4048 C CA  . ASP B 582 ? 1.1935 1.6838 1.3579 -0.0547 -0.1023 -0.1596 832  ASP B CA  
4049 C C   . ASP B 582 ? 1.1899 1.6406 1.3410 -0.0523 -0.0867 -0.1551 832  ASP B C   
4050 O O   . ASP B 582 ? 1.0945 1.5200 1.2340 -0.0640 -0.0782 -0.1589 832  ASP B O   
4051 C CB  . ASP B 582 ? 1.2778 1.7756 1.4471 -0.0757 -0.1025 -0.1687 832  ASP B CB  
4052 C CG  . ASP B 582 ? 1.3131 1.8131 1.5056 -0.0871 -0.0902 -0.1695 832  ASP B CG  
4053 O OD1 . ASP B 582 ? 1.2334 1.7331 1.4397 -0.0789 -0.0829 -0.1630 832  ASP B OD1 
4054 O OD2 . ASP B 582 ? 1.2780 1.7789 1.4732 -0.1048 -0.0878 -0.1765 832  ASP B OD2 
4055 N N   . CYS B 583 ? 1.1884 1.6344 1.3419 -0.0372 -0.0824 -0.1478 833  CYS B N   
4056 C CA  . CYS B 583 ? 0.9882 1.4021 1.1336 -0.0350 -0.0672 -0.1444 833  CYS B CA  
4057 C C   . CYS B 583 ? 0.8704 1.2856 1.0378 -0.0462 -0.0563 -0.1453 833  CYS B C   
4058 O O   . CYS B 583 ? 0.9051 1.3477 1.0969 -0.0509 -0.0589 -0.1457 833  CYS B O   
4059 C CB  . CYS B 583 ? 0.8734 1.2846 1.0178 -0.0175 -0.0646 -0.1370 833  CYS B CB  
4060 S SG  . CYS B 583 ? 1.3073 1.7002 1.4171 -0.0021 -0.0725 -0.1338 833  CYS B SG  
4061 N N   . LEU B 584 ? 0.8042 1.1889 0.9622 -0.0504 -0.0440 -0.1458 834  LEU B N   
4062 C CA  . LEU B 584 ? 0.7424 1.1240 0.9189 -0.0579 -0.0335 -0.1451 834  LEU B CA  
4063 C C   . LEU B 584 ? 0.8058 1.1942 0.9964 -0.0471 -0.0279 -0.1382 834  LEU B C   
4064 O O   . LEU B 584 ? 0.7578 1.1293 0.9365 -0.0371 -0.0224 -0.1355 834  LEU B O   
4065 C CB  . LEU B 584 ? 0.6357 0.9838 0.7990 -0.0647 -0.0229 -0.1487 834  LEU B CB  
4066 C CG  . LEU B 584 ? 0.7292 1.0707 0.9100 -0.0707 -0.0127 -0.1475 834  LEU B CG  
4067 C CD1 . LEU B 584 ? 0.6227 0.9839 0.8207 -0.0825 -0.0167 -0.1489 834  LEU B CD1 
4068 C CD2 . LEU B 584 ? 0.6892 0.9982 0.8577 -0.0755 -0.0026 -0.1520 834  LEU B CD2 
4069 N N   . VAL B 585 ? 0.7564 1.1690 0.9711 -0.0502 -0.0287 -0.1360 835  VAL B N   
4070 C CA  . VAL B 585 ? 0.5801 1.0022 0.8093 -0.0418 -0.0235 -0.1300 835  VAL B CA  
4071 C C   . VAL B 585 ? 0.6648 1.0852 0.9098 -0.0512 -0.0157 -0.1285 835  VAL B C   
4072 O O   . VAL B 585 ? 0.6107 1.0489 0.8703 -0.0609 -0.0186 -0.1297 835  VAL B O   
4073 C CB  . VAL B 585 ? 0.6817 1.1362 0.9245 -0.0352 -0.0321 -0.1284 835  VAL B CB  
4074 C CG1 . VAL B 585 ? 0.5306 0.9945 0.7892 -0.0293 -0.0251 -0.1230 835  VAL B CG1 
4075 C CG2 . VAL B 585 ? 0.6797 1.1330 0.9052 -0.0233 -0.0404 -0.1286 835  VAL B CG2 
4076 N N   . THR B 586 ? 0.6898 1.0887 0.9313 -0.0486 -0.0059 -0.1262 836  THR B N   
4077 C CA  . THR B 586 ? 0.5459 0.9421 0.8014 -0.0541 0.0011  -0.1231 836  THR B CA  
4078 C C   . THR B 586 ? 0.6943 1.0982 0.9585 -0.0452 0.0061  -0.1175 836  THR B C   
4079 O O   . THR B 586 ? 0.8323 1.2409 1.0912 -0.0350 0.0054  -0.1165 836  THR B O   
4080 C CB  . THR B 586 ? 0.6313 0.9987 0.8784 -0.0582 0.0080  -0.1256 836  THR B CB  
4081 O OG1 . THR B 586 ? 0.7036 1.0537 0.9385 -0.0489 0.0138  -0.1262 836  THR B OG1 
4082 C CG2 . THR B 586 ? 0.6407 0.9992 0.8772 -0.0678 0.0041  -0.1320 836  THR B CG2 
4083 N N   . THR B 587 ? 0.6636 1.0679 0.9402 -0.0493 0.0112  -0.1137 837  THR B N   
4084 C CA  . THR B 587 ? 0.6885 1.1018 0.9737 -0.0428 0.0161  -0.1088 837  THR B CA  
4085 C C   . THR B 587 ? 0.6091 1.0056 0.8836 -0.0331 0.0229  -0.1092 837  THR B C   
4086 O O   . THR B 587 ? 0.6940 1.0982 0.9698 -0.0256 0.0260  -0.1070 837  THR B O   
4087 C CB  . THR B 587 ? 0.6150 1.0302 0.9128 -0.0499 0.0194  -0.1044 837  THR B CB  
4088 O OG1 . THR B 587 ? 0.8397 1.2313 1.1328 -0.0510 0.0238  -0.1049 837  THR B OG1 
4089 C CG2 . THR B 587 ? 0.6369 1.0656 0.9429 -0.0614 0.0143  -0.1048 837  THR B CG2 
4090 N N   . SER B 588 ? 0.6207 0.9939 0.8844 -0.0339 0.0262  -0.1129 838  SER B N   
4091 C CA  . SER B 588 ? 0.5597 0.9162 0.8135 -0.0267 0.0341  -0.1150 838  SER B CA  
4092 C C   . SER B 588 ? 0.6276 0.9673 0.8604 -0.0237 0.0338  -0.1203 838  SER B C   
4093 O O   . SER B 588 ? 0.6666 0.9960 0.8882 -0.0169 0.0399  -0.1219 838  SER B O   
4094 C CB  . SER B 588 ? 0.6067 0.9493 0.8665 -0.0293 0.0404  -0.1158 838  SER B CB  
4095 O OG  . SER B 588 ? 0.7836 1.1394 1.0595 -0.0306 0.0411  -0.1100 838  SER B OG  
4096 N N   . VAL B 589 ? 0.6050 0.9407 0.8303 -0.0295 0.0274  -0.1235 839  VAL B N   
4097 C CA  . VAL B 589 ? 0.6481 0.9657 0.8509 -0.0284 0.0268  -0.1287 839  VAL B CA  
4098 C C   . VAL B 589 ? 0.6659 0.9975 0.8626 -0.0282 0.0154  -0.1284 839  VAL B C   
4099 O O   . VAL B 589 ? 0.6576 1.0075 0.8671 -0.0345 0.0084  -0.1276 839  VAL B O   
4100 C CB  . VAL B 589 ? 0.5637 0.8600 0.7609 -0.0365 0.0307  -0.1347 839  VAL B CB  
4101 C CG1 . VAL B 589 ? 0.6552 0.9297 0.8267 -0.0357 0.0325  -0.1406 839  VAL B CG1 
4102 C CG2 . VAL B 589 ? 0.6414 0.9293 0.8510 -0.0363 0.0401  -0.1347 839  VAL B CG2 
4103 N N   . LYS B 590 ? 0.6712 0.9939 0.8476 -0.0210 0.0135  -0.1294 840  LYS B N   
4104 C CA  . LYS B 590 ? 0.7115 1.0452 0.8788 -0.0192 0.0014  -0.1295 840  LYS B CA  
4105 C C   . LYS B 590 ? 0.7018 1.0102 0.8400 -0.0200 0.0010  -0.1342 840  LYS B C   
4106 O O   . LYS B 590 ? 0.7983 1.0853 0.9186 -0.0141 0.0084  -0.1347 840  LYS B O   
4107 C CB  . LYS B 590 ? 0.6362 0.9864 0.8064 -0.0071 -0.0025 -0.1244 840  LYS B CB  
4108 C CG  . LYS B 590 ? 0.7125 1.0782 0.8769 -0.0034 -0.0166 -0.1244 840  LYS B CG  
4109 C CD  . LYS B 590 ? 0.8895 1.2478 1.0360 0.0111  -0.0186 -0.1210 840  LYS B CD  
4110 C CE  . LYS B 590 ? 0.8183 1.1932 0.9820 0.0203  -0.0150 -0.1161 840  LYS B CE  
4111 N NZ  . LYS B 590 ? 0.7879 1.1548 0.9339 0.0352  -0.0173 -0.1127 840  LYS B NZ  
4112 N N   . VAL B 591 ? 0.7076 1.0177 0.8399 -0.0285 -0.0069 -0.1382 841  VAL B N   
4113 C CA  . VAL B 591 ? 0.7568 1.0443 0.8601 -0.0312 -0.0086 -0.1431 841  VAL B CA  
4114 C C   . VAL B 591 ? 0.8189 1.1231 0.9133 -0.0276 -0.0241 -0.1419 841  VAL B C   
4115 O O   . VAL B 591 ? 0.8231 1.1512 0.9321 -0.0341 -0.0332 -0.1433 841  VAL B O   
4116 C CB  . VAL B 591 ? 0.7453 1.0182 0.8470 -0.0454 -0.0039 -0.1501 841  VAL B CB  
4117 C CG1 . VAL B 591 ? 0.7853 1.0318 0.8548 -0.0490 -0.0033 -0.1558 841  VAL B CG1 
4118 C CG2 . VAL B 591 ? 0.7163 0.9786 0.8332 -0.0474 0.0095  -0.1507 841  VAL B CG2 
4119 N N   . CYS B 592 ? 0.8065 1.0982 0.8766 -0.0173 -0.0271 -0.1396 842  CYS B N   
4120 C CA  . CYS B 592 ? 0.8484 1.1551 0.9084 -0.0105 -0.0429 -0.1374 842  CYS B CA  
4121 C C   . CYS B 592 ? 0.8796 1.1593 0.9023 -0.0128 -0.0461 -0.1407 842  CYS B C   
4122 O O   . CYS B 592 ? 1.0328 1.2822 1.0310 -0.0083 -0.0374 -0.1400 842  CYS B O   
4123 C CB  . CYS B 592 ? 0.9042 1.2206 0.9677 0.0063  -0.0453 -0.1302 842  CYS B CB  
4124 S SG  . CYS B 592 ? 1.3029 1.6667 1.4046 0.0112  -0.0551 -0.1269 842  CYS B SG  
4125 N N   . LEU B 593 ? 1.0461 1.3368 1.0634 -0.0207 -0.0580 -0.1447 843  LEU B N   
4126 C CA  . LEU B 593 ? 0.9552 1.2252 0.9356 -0.0224 -0.0646 -0.1471 843  LEU B CA  
4127 C C   . LEU B 593 ? 1.1123 1.3964 1.0830 -0.0067 -0.0804 -0.1407 843  LEU B C   
4128 O O   . LEU B 593 ? 1.1313 1.4490 1.1177 -0.0055 -0.0953 -0.1408 843  LEU B O   
4129 C CB  . LEU B 593 ? 0.9028 1.1783 0.8817 -0.0394 -0.0696 -0.1552 843  LEU B CB  
4130 C CG  . LEU B 593 ? 1.0220 1.2819 0.9635 -0.0429 -0.0792 -0.1582 843  LEU B CG  
4131 C CD1 . LEU B 593 ? 1.1606 1.3756 1.0681 -0.0440 -0.0662 -0.1596 843  LEU B CD1 
4132 C CD2 . LEU B 593 ? 0.9856 1.2573 0.9304 -0.0605 -0.0846 -0.1667 843  LEU B CD2 
4133 N N   . ILE B 594 ? 1.0405 1.2989 0.9853 0.0055  -0.0770 -0.1355 844  ILE B N   
4134 C CA  . ILE B 594 ? 1.0766 1.3463 1.0150 0.0236  -0.0902 -0.1280 844  ILE B CA  
4135 C C   . ILE B 594 ? 1.1106 1.3750 1.0168 0.0257  -0.1070 -0.1277 844  ILE B C   
4136 O O   . ILE B 594 ? 1.2985 1.5870 1.2092 0.0382  -0.1238 -0.1233 844  ILE B O   
4137 C CB  . ILE B 594 ? 1.1437 1.3879 1.0692 0.0367  -0.0784 -0.1219 844  ILE B CB  
4138 C CG1 . ILE B 594 ? 1.3057 1.5028 1.1858 0.0338  -0.0700 -0.1231 844  ILE B CG1 
4139 C CG2 . ILE B 594 ? 0.9600 1.2099 0.9159 0.0332  -0.0621 -0.1228 844  ILE B CG2 
4140 C CD1 . ILE B 594 ? 1.1942 1.3644 1.0565 0.0465  -0.0591 -0.1175 844  ILE B CD1 
4141 N N   . GLY B 595 ? 1.0112 1.2453 0.8851 0.0139  -0.1031 -0.1327 845  GLY B N   
4142 C CA  . GLY B 595 ? 1.2071 1.4330 1.0460 0.0153  -0.1188 -0.1321 845  GLY B CA  
4143 C C   . GLY B 595 ? 1.1990 1.4018 1.0137 -0.0043 -0.1137 -0.1408 845  GLY B C   
4144 O O   . GLY B 595 ? 1.2559 1.4387 1.0735 -0.0164 -0.0954 -0.1465 845  GLY B O   
4145 N N   . THR B 596 ? 1.0933 1.3000 0.8842 -0.0072 -0.1304 -0.1421 846  THR B N   
4146 C CA  . THR B 596 ? 1.2480 1.4338 1.0128 -0.0266 -0.1273 -0.1509 846  THR B CA  
4147 C C   . THR B 596 ? 1.1861 1.3579 0.9060 -0.0221 -0.1438 -0.1478 846  THR B C   
4148 O O   . THR B 596 ? 1.1524 1.3548 0.8773 -0.0126 -0.1651 -0.1440 846  THR B O   
4149 C CB  . THR B 596 ? 1.2815 1.4996 1.0769 -0.0432 -0.1304 -0.1598 846  THR B CB  
4150 O OG1 . THR B 596 ? 1.1624 1.3970 1.0005 -0.0443 -0.1182 -0.1606 846  THR B OG1 
4151 C CG2 . THR B 596 ? 1.1285 1.3204 0.8994 -0.0645 -0.1219 -0.1700 846  THR B CG2 
4152 N N   . VAL B 597 ? 1.1939 1.3198 0.8698 -0.0291 -0.1340 -0.1497 847  VAL B N   
4153 C CA  . VAL B 597 ? 1.3409 1.4465 0.9673 -0.0281 -0.1479 -0.1474 847  VAL B CA  
4154 C C   . VAL B 597 ? 1.3332 1.4372 0.9468 -0.0513 -0.1487 -0.1587 847  VAL B C   
4155 O O   . VAL B 597 ? 1.4203 1.5102 1.0421 -0.0684 -0.1299 -0.1681 847  VAL B O   
4156 C CB  . VAL B 597 ? 1.4630 1.5160 1.0441 -0.0219 -0.1360 -0.1425 847  VAL B CB  
4157 C CG1 . VAL B 597 ? 1.4287 1.4511 1.0101 -0.0372 -0.1085 -0.1512 847  VAL B CG1 
4158 C CG2 . VAL B 597 ? 1.3621 1.3895 0.8872 -0.0234 -0.1495 -0.1403 847  VAL B CG2 
4159 N N   . SER B 598 ? 1.3637 1.2792 1.0030 -0.2163 -0.0493 -0.2233 848  SER B N   
4160 C CA  . SER B 598 ? 1.2676 1.2240 0.9484 -0.2033 -0.0415 -0.2063 848  SER B CA  
4161 C C   . SER B 598 ? 1.2430 1.1638 0.9231 -0.2078 -0.0426 -0.1985 848  SER B C   
4162 O O   . SER B 598 ? 1.4041 1.2624 1.0532 -0.2087 -0.0478 -0.2057 848  SER B O   
4163 C CB  . SER B 598 ? 1.3048 1.2811 1.0043 -0.1687 -0.0339 -0.2038 848  SER B CB  
4164 O OG  . SER B 598 ? 1.0600 1.0694 0.7964 -0.1579 -0.0285 -0.1873 848  SER B OG  
4165 N N   . LYS B 599 ? 1.0954 1.0557 0.8085 -0.2095 -0.0385 -0.1840 849  LYS B N   
4166 C CA  . LYS B 599 ? 1.1330 1.0700 0.8525 -0.2073 -0.0375 -0.1747 849  LYS B CA  
4167 C C   . LYS B 599 ? 1.1860 1.1188 0.9228 -0.1739 -0.0316 -0.1696 849  LYS B C   
4168 O O   . LYS B 599 ? 1.2079 1.1096 0.9433 -0.1680 -0.0316 -0.1644 849  LYS B O   
4169 C CB  . LYS B 599 ? 1.0288 1.0121 0.7744 -0.2232 -0.0362 -0.1630 849  LYS B CB  
4170 C CG  . LYS B 599 ? 1.1479 1.1795 0.9331 -0.2005 -0.0299 -0.1524 849  LYS B CG  
4171 C CD  . LYS B 599 ? 1.1752 1.2608 0.9834 -0.2137 -0.0299 -0.1451 849  LYS B CD  
4172 C CE  . LYS B 599 ? 1.2679 1.3408 1.0684 -0.2352 -0.0319 -0.1412 849  LYS B CE  
4173 N NZ  . LYS B 599 ? 1.2480 1.3814 1.0709 -0.2460 -0.0315 -0.1357 849  LYS B NZ  
4174 N N   . PHE B 600 ? 1.1304 1.0957 0.8828 -0.1537 -0.0270 -0.1699 850  PHE B N   
4175 C CA  . PHE B 600 ? 1.1444 1.1143 0.9140 -0.1245 -0.0217 -0.1640 850  PHE B CA  
4176 C C   . PHE B 600 ? 1.0753 1.0099 0.8192 -0.1067 -0.0218 -0.1766 850  PHE B C   
4177 O O   . PHE B 600 ? 1.0914 1.0201 0.8132 -0.1111 -0.0242 -0.1894 850  PHE B O   
4178 C CB  . PHE B 600 ? 1.0967 1.1256 0.8981 -0.1142 -0.0176 -0.1547 850  PHE B CB  
4179 C CG  . PHE B 600 ? 1.0212 1.0874 0.8459 -0.1277 -0.0188 -0.1448 850  PHE B CG  
4180 C CD1 . PHE B 600 ? 0.9894 1.0620 0.8361 -0.1217 -0.0177 -0.1330 850  PHE B CD1 
4181 C CD2 . PHE B 600 ? 0.9667 1.0636 0.7906 -0.1448 -0.0215 -0.1482 850  PHE B CD2 
4182 C CE1 . PHE B 600 ? 0.8389 0.9465 0.7053 -0.1305 -0.0193 -0.1260 850  PHE B CE1 
4183 C CE2 . PHE B 600 ? 1.0436 1.1789 0.8889 -0.1537 -0.0230 -0.1403 850  PHE B CE2 
4184 C CZ  . PHE B 600 ? 0.9318 1.0718 0.7978 -0.1454 -0.0218 -0.1298 850  PHE B CZ  
4185 N N   . GLN B 601 ? 1.0452 0.9585 0.7916 -0.0855 -0.0195 -0.1736 851  GLN B N   
4186 C CA  . GLN B 601 ? 1.0786 0.9617 0.8026 -0.0628 -0.0195 -0.1855 851  GLN B CA  
4187 C C   . GLN B 601 ? 1.0711 0.9900 0.8212 -0.0359 -0.0124 -0.1769 851  GLN B C   
4188 O O   . GLN B 601 ? 1.0527 0.9997 0.8333 -0.0356 -0.0096 -0.1611 851  GLN B O   
4189 C CB  . GLN B 601 ? 1.1986 1.0143 0.8940 -0.0623 -0.0256 -0.1912 851  GLN B CB  
4190 C CG  . GLN B 601 ? 1.3148 1.0873 0.9772 -0.0909 -0.0346 -0.2000 851  GLN B CG  
4191 C CD  . GLN B 601 ? 1.4318 1.1926 1.0652 -0.0922 -0.0383 -0.2178 851  GLN B CD  
4192 O OE1 . GLN B 601 ? 1.4132 1.1667 1.0347 -0.0659 -0.0368 -0.2289 851  GLN B OE1 
4193 N NE2 . GLN B 601 ? 1.4770 1.2395 1.0985 -0.1228 -0.0433 -0.2211 851  GLN B NE2 
4194 N N   . PRO B 602 ? 1.0989 1.0198 0.8369 -0.0136 -0.0100 -0.1870 852  PRO B N   
4195 C CA  . PRO B 602 ? 1.0652 1.0203 0.8256 0.0112  -0.0037 -0.1783 852  PRO B CA  
4196 C C   . PRO B 602 ? 1.0424 0.9716 0.8096 0.0211  -0.0045 -0.1706 852  PRO B C   
4197 O O   . PRO B 602 ? 1.0602 0.9358 0.8057 0.0160  -0.0101 -0.1763 852  PRO B O   
4198 C CB  . PRO B 602 ? 1.0748 1.0288 0.8120 0.0331  -0.0021 -0.1950 852  PRO B CB  
4199 C CG  . PRO B 602 ? 1.1588 1.0996 0.8714 0.0159  -0.0062 -0.2088 852  PRO B CG  
4200 C CD  . PRO B 602 ? 1.1577 1.0581 0.8617 -0.0110 -0.0129 -0.2068 852  PRO B CD  
4201 N N   . SER B 603 ? 1.1076 1.0758 0.9041 0.0336  0.0002  -0.1564 853  SER B N   
4202 C CA  . SER B 603 ? 1.0793 1.0369 0.8892 0.0431  0.0001  -0.1460 853  SER B CA  
4203 C C   . SER B 603 ? 1.0766 1.0192 0.8977 0.0219  -0.0033 -0.1354 853  SER B C   
4204 O O   . SER B 603 ? 1.1328 1.0661 0.9648 0.0272  -0.0040 -0.1262 853  SER B O   
4205 C CB  . SER B 603 ? 1.1230 1.0344 0.9066 0.0637  -0.0026 -0.1580 853  SER B CB  
4206 O OG  . SER B 603 ? 1.4224 1.3340 1.2219 0.0756  -0.0022 -0.1468 853  SER B OG  
4207 N N   . ASP B 604 ? 0.9767 0.9206 0.7955 -0.0014 -0.0054 -0.1365 854  ASP B N   
4208 C CA  . ASP B 604 ? 1.0079 0.9511 0.8408 -0.0198 -0.0077 -0.1262 854  ASP B CA  
4209 C C   . ASP B 604 ? 1.0323 1.0192 0.8998 -0.0155 -0.0056 -0.1102 854  ASP B C   
4210 O O   . ASP B 604 ? 1.0268 1.0514 0.9076 -0.0081 -0.0031 -0.1060 854  ASP B O   
4211 C CB  . ASP B 604 ? 0.9397 0.8855 0.7640 -0.0443 -0.0103 -0.1314 854  ASP B CB  
4212 C CG  . ASP B 604 ? 1.1382 1.0328 0.9270 -0.0565 -0.0152 -0.1442 854  ASP B CG  
4213 O OD1 . ASP B 604 ? 1.1735 1.0255 0.9428 -0.0441 -0.0173 -0.1495 854  ASP B OD1 
4214 O OD2 . ASP B 604 ? 0.9381 0.8346 0.7174 -0.0789 -0.0180 -0.1486 854  ASP B OD2 
4215 N N   . THR B 605 ? 1.0592 1.0391 0.9390 -0.0211 -0.0075 -0.1009 855  THR B N   
4216 C CA  . THR B 605 ? 0.8927 0.9054 0.8017 -0.0191 -0.0079 -0.0864 855  THR B CA  
4217 C C   . THR B 605 ? 0.9243 0.9507 0.8417 -0.0364 -0.0106 -0.0840 855  THR B C   
4218 O O   . THR B 605 ? 0.8410 0.8469 0.7494 -0.0488 -0.0122 -0.0872 855  THR B O   
4219 C CB  . THR B 605 ? 0.7920 0.7901 0.7092 -0.0098 -0.0088 -0.0783 855  THR B CB  
4220 O OG1 . THR B 605 ? 0.8364 0.8326 0.7495 0.0091  -0.0063 -0.0796 855  THR B OG1 
4221 C CG2 . THR B 605 ? 0.8545 0.8802 0.7984 -0.0107 -0.0113 -0.0643 855  THR B CG2 
4222 N N   . LEU B 606 ? 0.8593 0.9221 0.7931 -0.0370 -0.0118 -0.0782 856  LEU B N   
4223 C CA  . LEU B 606 ? 0.8199 0.9020 0.7632 -0.0488 -0.0151 -0.0763 856  LEU B CA  
4224 C C   . LEU B 606 ? 0.8139 0.9057 0.7781 -0.0431 -0.0191 -0.0644 856  LEU B C   
4225 O O   . LEU B 606 ? 0.8779 0.9838 0.8551 -0.0336 -0.0210 -0.0548 856  LEU B O   
4226 C CB  . LEU B 606 ? 0.7930 0.9059 0.7384 -0.0518 -0.0159 -0.0778 856  LEU B CB  
4227 C CG  . LEU B 606 ? 0.8967 1.0031 0.8206 -0.0572 -0.0130 -0.0903 856  LEU B CG  
4228 C CD1 . LEU B 606 ? 0.7248 0.8664 0.6528 -0.0610 -0.0146 -0.0902 856  LEU B CD1 
4229 C CD2 . LEU B 606 ? 0.9283 1.0070 0.8327 -0.0725 -0.0132 -0.1006 856  LEU B CD2 
4230 N N   . LEU B 607 ? 0.8187 0.9033 0.7846 -0.0498 -0.0209 -0.0651 857  LEU B N   
4231 C CA  . LEU B 607 ? 0.7488 0.8397 0.7312 -0.0442 -0.0256 -0.0566 857  LEU B CA  
4232 C C   . LEU B 607 ? 0.7780 0.8955 0.7687 -0.0481 -0.0300 -0.0577 857  LEU B C   
4233 O O   . LEU B 607 ? 0.8024 0.9283 0.7855 -0.0595 -0.0283 -0.0658 857  LEU B O   
4234 C CB  . LEU B 607 ? 0.7614 0.8272 0.7389 -0.0460 -0.0247 -0.0569 857  LEU B CB  
4235 C CG  . LEU B 607 ? 0.6903 0.7609 0.6817 -0.0410 -0.0299 -0.0506 857  LEU B CG  
4236 C CD1 . LEU B 607 ? 0.6553 0.7270 0.6595 -0.0291 -0.0341 -0.0399 857  LEU B CD1 
4237 C CD2 . LEU B 607 ? 0.7132 0.7625 0.6965 -0.0459 -0.0282 -0.0523 857  LEU B CD2 
4238 N N   . PHE B 608 ? 0.7552 0.8862 0.7605 -0.0388 -0.0367 -0.0495 858  PHE B N   
4239 C CA  . PHE B 608 ? 0.7067 0.8620 0.7198 -0.0371 -0.0430 -0.0505 858  PHE B CA  
4240 C C   . PHE B 608 ? 0.7585 0.9078 0.7804 -0.0286 -0.0496 -0.0468 858  PHE B C   
4241 O O   . PHE B 608 ? 0.8349 0.9751 0.8639 -0.0199 -0.0562 -0.0374 858  PHE B O   
4242 C CB  . PHE B 608 ? 0.7827 0.9557 0.8007 -0.0326 -0.0478 -0.0445 858  PHE B CB  
4243 C CG  . PHE B 608 ? 0.7744 0.9601 0.7830 -0.0409 -0.0424 -0.0505 858  PHE B CG  
4244 C CD1 . PHE B 608 ? 0.8366 1.0467 0.8433 -0.0469 -0.0433 -0.0576 858  PHE B CD1 
4245 C CD2 . PHE B 608 ? 0.8215 0.9970 0.8223 -0.0419 -0.0367 -0.0499 858  PHE B CD2 
4246 C CE1 . PHE B 608 ? 0.7836 1.0046 0.7801 -0.0558 -0.0392 -0.0637 858  PHE B CE1 
4247 C CE2 . PHE B 608 ? 0.7847 0.9700 0.7742 -0.0485 -0.0324 -0.0571 858  PHE B CE2 
4248 C CZ  . PHE B 608 ? 0.7894 0.9959 0.7765 -0.0565 -0.0339 -0.0638 858  PHE B CZ  
4249 N N   . LEU B 609 ? 0.7940 0.9497 0.8141 -0.0320 -0.0483 -0.0542 859  LEU B N   
4250 C CA  . LEU B 609 ? 0.7395 0.8914 0.7658 -0.0227 -0.0544 -0.0532 859  LEU B CA  
4251 C C   . LEU B 609 ? 0.7336 0.8981 0.7685 -0.0090 -0.0658 -0.0506 859  LEU B C   
4252 O O   . LEU B 609 ? 0.9300 1.0800 0.9687 0.0015  -0.0742 -0.0463 859  LEU B O   
4253 C CB  . LEU B 609 ? 0.6980 0.8624 0.7196 -0.0299 -0.0500 -0.0622 859  LEU B CB  
4254 C CG  . LEU B 609 ? 0.7032 0.8444 0.7163 -0.0384 -0.0439 -0.0621 859  LEU B CG  
4255 C CD1 . LEU B 609 ? 0.9440 1.0671 0.9624 -0.0271 -0.0493 -0.0570 859  LEU B CD1 
4256 C CD2 . LEU B 609 ? 0.7190 0.8366 0.7224 -0.0470 -0.0377 -0.0597 859  LEU B CD2 
4257 N N   . GLY B 610 ? 0.8334 1.0223 0.8694 -0.0088 -0.0676 -0.0530 860  GLY B N   
4258 C CA  . GLY B 610 ? 0.8401 1.0382 0.8816 0.0053  -0.0799 -0.0501 860  GLY B CA  
4259 C C   . GLY B 610 ? 0.7721 0.9779 0.8136 0.0032  -0.0821 -0.0435 860  GLY B C   
4260 O O   . GLY B 610 ? 0.8739 1.0687 0.9127 -0.0050 -0.0768 -0.0373 860  GLY B O   
4261 N N   . PRO B 611 ? 0.8001 1.0273 0.8438 0.0118  -0.0904 -0.0450 861  PRO B N   
4262 C CA  . PRO B 611 ? 0.8966 1.1348 0.9390 0.0091  -0.0929 -0.0385 861  PRO B CA  
4263 C C   . PRO B 611 ? 0.9116 1.1662 0.9490 -0.0069 -0.0800 -0.0444 861  PRO B C   
4264 O O   . PRO B 611 ? 0.8685 1.1288 0.9028 -0.0162 -0.0708 -0.0540 861  PRO B O   
4265 C CB  . PRO B 611 ? 0.8410 1.1013 0.8861 0.0233  -0.1045 -0.0416 861  PRO B CB  
4266 C CG  . PRO B 611 ? 0.8719 1.1208 0.9191 0.0378  -0.1118 -0.0461 861  PRO B CG  
4267 C CD  . PRO B 611 ? 0.9342 1.1761 0.9810 0.0273  -0.0994 -0.0521 861  PRO B CD  
4268 N N   . LEU B 612 ? 0.9102 1.1712 0.9448 -0.0109 -0.0803 -0.0382 862  LEU B N   
4269 C CA  . LEU B 612 ? 0.8897 1.1616 0.9165 -0.0250 -0.0693 -0.0443 862  LEU B CA  
4270 C C   . LEU B 612 ? 0.9923 1.2938 1.0172 -0.0317 -0.0666 -0.0565 862  LEU B C   
4271 O O   . LEU B 612 ? 0.9790 1.2799 0.9959 -0.0457 -0.0573 -0.0652 862  LEU B O   
4272 C CB  . LEU B 612 ? 0.7729 1.0517 0.7966 -0.0262 -0.0713 -0.0357 862  LEU B CB  
4273 C CG  . LEU B 612 ? 0.6660 0.9240 0.6894 -0.0256 -0.0703 -0.0243 862  LEU B CG  
4274 C CD1 . LEU B 612 ? 0.7093 0.9834 0.7290 -0.0282 -0.0719 -0.0160 862  LEU B CD1 
4275 C CD2 . LEU B 612 ? 0.7629 1.0031 0.7808 -0.0318 -0.0585 -0.0310 862  LEU B CD2 
4276 N N   . GLU B 613 ? 0.9753 1.3029 1.0063 -0.0223 -0.0755 -0.0569 863  GLU B N   
4277 C CA  . GLU B 613 ? 0.9184 1.2837 0.9493 -0.0285 -0.0737 -0.0675 863  GLU B CA  
4278 C C   . GLU B 613 ? 0.8913 1.2657 0.9252 -0.0300 -0.0705 -0.0761 863  GLU B C   
4279 O O   . GLU B 613 ? 0.9676 1.3809 1.0039 -0.0330 -0.0707 -0.0839 863  GLU B O   
4280 C CB  . GLU B 613 ? 0.9318 1.3263 0.9683 -0.0151 -0.0852 -0.0648 863  GLU B CB  
4281 C CG  . GLU B 613 ? 1.1061 1.4945 1.1502 0.0074  -0.0976 -0.0613 863  GLU B CG  
4282 C CD  . GLU B 613 ? 1.2022 1.5519 1.2450 0.0160  -0.1058 -0.0473 863  GLU B CD  
4283 O OE1 . GLU B 613 ? 1.1522 1.4882 1.1902 0.0053  -0.1013 -0.0397 863  GLU B OE1 
4284 O OE2 . GLU B 613 ? 1.1504 1.4847 1.1959 0.0332  -0.1175 -0.0440 863  GLU B OE2 
4285 N N   . GLN B 614 ? 0.7834 1.1272 0.8169 -0.0288 -0.0675 -0.0746 864  GLN B N   
4286 C CA  . GLN B 614 ? 0.8143 1.1665 0.8490 -0.0315 -0.0638 -0.0818 864  GLN B CA  
4287 C C   . GLN B 614 ? 0.8838 1.2206 0.9074 -0.0535 -0.0527 -0.0856 864  GLN B C   
4288 O O   . GLN B 614 ? 0.8768 1.2202 0.8989 -0.0602 -0.0491 -0.0902 864  GLN B O   
4289 C CB  . GLN B 614 ? 0.8844 1.2135 0.9248 -0.0142 -0.0699 -0.0781 864  GLN B CB  
4290 C CG  . GLN B 614 ? 0.8307 1.1846 0.8751 -0.0074 -0.0708 -0.0865 864  GLN B CG  
4291 C CD  . GLN B 614 ? 1.0800 1.4058 1.1266 0.0075  -0.0761 -0.0842 864  GLN B CD  
4292 O OE1 . GLN B 614 ? 1.0904 1.3763 1.1347 0.0070  -0.0766 -0.0760 864  GLN B OE1 
4293 N NE2 . GLN B 614 ? 0.9165 1.2657 0.9669 0.0212  -0.0804 -0.0920 864  GLN B NE2 
4294 N N   . GLY B 615 ? 0.8451 1.1609 0.8590 -0.0643 -0.0481 -0.0838 865  GLY B N   
4295 C CA  . GLY B 615 ? 0.8785 1.1718 0.8778 -0.0832 -0.0398 -0.0878 865  GLY B CA  
4296 C C   . GLY B 615 ? 0.7780 1.0265 0.7732 -0.0781 -0.0371 -0.0822 865  GLY B C   
4297 O O   . GLY B 615 ? 0.9013 1.1383 0.9060 -0.0623 -0.0412 -0.0747 865  GLY B O   
4298 N N   . GLY B 616 ? 0.8746 1.0971 0.8538 -0.0922 -0.0311 -0.0860 866  GLY B N   
4299 C CA  . GLY B 616 ? 0.8289 1.0114 0.8024 -0.0869 -0.0283 -0.0821 866  GLY B CA  
4300 C C   . GLY B 616 ? 0.7773 0.9312 0.7332 -0.1015 -0.0240 -0.0865 866  GLY B C   
4301 O O   . GLY B 616 ? 0.8196 0.9843 0.7665 -0.1192 -0.0233 -0.0919 866  GLY B O   
4302 N N   . LEU B 617 ? 0.8216 0.9396 0.7721 -0.0946 -0.0222 -0.0833 867  LEU B N   
4303 C CA  . LEU B 617 ? 0.8166 0.8984 0.7477 -0.1053 -0.0198 -0.0862 867  LEU B CA  
4304 C C   . LEU B 617 ? 0.9328 0.9825 0.8502 -0.0982 -0.0179 -0.0885 867  LEU B C   
4305 O O   . LEU B 617 ? 0.8858 0.9408 0.8138 -0.0819 -0.0175 -0.0844 867  LEU B O   
4306 C CB  . LEU B 617 ? 0.8525 0.9218 0.7891 -0.1010 -0.0203 -0.0804 867  LEU B CB  
4307 C CG  . LEU B 617 ? 0.8546 0.9543 0.8011 -0.1070 -0.0217 -0.0799 867  LEU B CG  
4308 C CD1 . LEU B 617 ? 0.7242 0.8102 0.6760 -0.0993 -0.0225 -0.0743 867  LEU B CD1 
4309 C CD2 . LEU B 617 ? 0.8868 0.9953 0.8179 -0.1315 -0.0205 -0.0853 867  LEU B CD2 
4310 N N   . ILE B 618 ? 0.9511 0.9678 0.8435 -0.1106 -0.0176 -0.0951 868  ILE B N   
4311 C CA  . ILE B 618 ? 0.9706 0.9537 0.8450 -0.1023 -0.0167 -0.1004 868  ILE B CA  
4312 C C   . ILE B 618 ? 0.8947 0.8366 0.7587 -0.0961 -0.0174 -0.0976 868  ILE B C   
4313 O O   . ILE B 618 ? 1.0914 1.0135 0.9436 -0.1109 -0.0194 -0.0966 868  ILE B O   
4314 C CB  . ILE B 618 ? 0.8913 0.8602 0.7400 -0.1189 -0.0184 -0.1115 868  ILE B CB  
4315 C CG1 . ILE B 618 ? 0.9709 0.9848 0.8308 -0.1249 -0.0181 -0.1138 868  ILE B CG1 
4316 C CG2 . ILE B 618 ? 0.8900 0.8217 0.7174 -0.1064 -0.0184 -0.1194 868  ILE B CG2 
4317 C CD1 . ILE B 618 ? 1.0325 1.0363 0.8675 -0.1425 -0.0204 -0.1249 868  ILE B CD1 
4318 N N   . PHE B 619 ? 0.8379 0.7699 0.7059 -0.0748 -0.0159 -0.0957 869  PHE B N   
4319 C CA  . PHE B 619 ? 0.9479 0.8437 0.8069 -0.0646 -0.0169 -0.0931 869  PHE B CA  
4320 C C   . PHE B 619 ? 1.0970 0.9623 0.9341 -0.0515 -0.0172 -0.1023 869  PHE B C   
4321 O O   . PHE B 619 ? 0.9808 0.8675 0.8262 -0.0359 -0.0142 -0.1041 869  PHE B O   
4322 C CB  . PHE B 619 ? 0.8794 0.7953 0.7644 -0.0488 -0.0158 -0.0820 869  PHE B CB  
4323 C CG  . PHE B 619 ? 0.9057 0.8395 0.8067 -0.0582 -0.0172 -0.0745 869  PHE B CG  
4324 C CD1 . PHE B 619 ? 0.9024 0.8154 0.8001 -0.0598 -0.0189 -0.0696 869  PHE B CD1 
4325 C CD2 . PHE B 619 ? 1.0133 0.9854 0.9312 -0.0638 -0.0173 -0.0731 869  PHE B CD2 
4326 C CE1 . PHE B 619 ? 1.0110 0.9428 0.9219 -0.0668 -0.0201 -0.0643 869  PHE B CE1 
4327 C CE2 . PHE B 619 ? 0.8037 0.7928 0.7345 -0.0688 -0.0191 -0.0683 869  PHE B CE2 
4328 C CZ  . PHE B 619 ? 0.7819 0.7518 0.7091 -0.0704 -0.0201 -0.0645 869  PHE B CZ  
4329 N N   . LYS B 620 ? 1.1010 0.9164 0.9083 -0.0577 -0.0215 -0.1080 870  LYS B N   
4330 C CA  . LYS B 620 ? 1.0274 0.8065 0.8100 -0.0411 -0.0235 -0.1183 870  LYS B CA  
4331 C C   . LYS B 620 ? 1.0592 0.8312 0.8493 -0.0151 -0.0227 -0.1134 870  LYS B C   
4332 O O   . LYS B 620 ? 1.2555 1.0271 1.0403 0.0075  -0.0214 -0.1201 870  LYS B O   
4333 C CB  . LYS B 620 ? 1.1794 0.9006 0.9230 -0.0577 -0.0310 -0.1263 870  LYS B CB  
4334 C CG  . LYS B 620 ? 1.0245 0.7508 0.7554 -0.0832 -0.0327 -0.1335 870  LYS B CG  
4335 C CD  . LYS B 620 ? 1.0390 0.7702 0.7597 -0.0713 -0.0317 -0.1467 870  LYS B CD  
4336 C CE  . LYS B 620 ? 1.1236 0.8547 0.8274 -0.0980 -0.0350 -0.1546 870  LYS B CE  
4337 N NZ  . LYS B 620 ? 1.3417 1.0673 1.0277 -0.0869 -0.0356 -0.1696 870  LYS B NZ  
4338 N N   . GLN B 621 ? 1.1100 0.8799 0.9120 -0.0174 -0.0237 -0.1021 871  GLN B N   
4339 C CA  . GLN B 621 ? 1.1347 0.9021 0.9459 0.0052  -0.0236 -0.0958 871  GLN B CA  
4340 C C   . GLN B 621 ? 1.1088 0.9261 0.9569 0.0065  -0.0198 -0.0832 871  GLN B C   
4341 O O   . GLN B 621 ? 1.2423 1.0637 1.1004 -0.0064 -0.0210 -0.0751 871  GLN B O   
4342 C CB  . GLN B 621 ? 1.2437 0.9611 1.0339 0.0017  -0.0299 -0.0930 871  GLN B CB  
4343 C CG  . GLN B 621 ? 1.4458 1.1041 1.1955 0.0050  -0.0365 -0.1048 871  GLN B CG  
4344 C CD  . GLN B 621 ? 1.4698 1.1213 1.2128 0.0384  -0.0366 -0.1128 871  GLN B CD  
4345 O OE1 . GLN B 621 ? 1.5159 1.1776 1.2721 0.0589  -0.0359 -0.1064 871  GLN B OE1 
4346 N NE2 . GLN B 621 ? 1.4811 1.1184 1.2030 0.0446  -0.0376 -0.1275 871  GLN B NE2 
4347 N N   . TRP B 622 ? 1.0491 0.9039 0.9154 0.0216  -0.0159 -0.0817 872  TRP B N   
4348 C CA  . TRP B 622 ? 1.0096 0.9070 0.9075 0.0240  -0.0143 -0.0691 872  TRP B CA  
4349 C C   . TRP B 622 ? 0.8942 0.8012 0.8005 0.0461  -0.0138 -0.0640 872  TRP B C   
4350 O O   . TRP B 622 ? 0.9391 0.8455 0.8350 0.0631  -0.0120 -0.0715 872  TRP B O   
4351 C CB  . TRP B 622 ? 0.9410 0.8789 0.8534 0.0187  -0.0115 -0.0686 872  TRP B CB  
4352 C CG  . TRP B 622 ? 0.9360 0.9094 0.8766 0.0157  -0.0127 -0.0554 872  TRP B CG  
4353 C CD1 . TRP B 622 ? 0.9680 0.9732 0.9269 0.0260  -0.0123 -0.0460 872  TRP B CD1 
4354 C CD2 . TRP B 622 ? 0.8132 0.7929 0.7646 0.0013  -0.0157 -0.0505 872  TRP B CD2 
4355 N NE1 . TRP B 622 ? 0.8387 0.8627 0.8170 0.0177  -0.0163 -0.0352 872  TRP B NE1 
4356 C CE2 . TRP B 622 ? 0.8039 0.8126 0.7779 0.0048  -0.0183 -0.0388 872  TRP B CE2 
4357 C CE3 . TRP B 622 ? 0.9008 0.8664 0.8439 -0.0140 -0.0169 -0.0548 872  TRP B CE3 
4358 C CZ2 . TRP B 622 ? 0.6783 0.6966 0.6651 -0.0036 -0.0229 -0.0331 872  TRP B CZ2 
4359 C CZ3 . TRP B 622 ? 0.8538 0.8371 0.8121 -0.0215 -0.0199 -0.0493 872  TRP B CZ3 
4360 C CH2 . TRP B 622 ? 0.7739 0.7806 0.7530 -0.0147 -0.0232 -0.0393 872  TRP B CH2 
4361 N N   . CYS B 623 ? 0.9105 0.8282 0.8348 0.0464  -0.0159 -0.0521 873  CYS B N   
4362 C CA  . CYS B 623 ? 0.9941 0.9220 0.9265 0.0655  -0.0165 -0.0462 873  CYS B CA  
4363 C C   . CYS B 623 ? 1.0467 1.0179 0.9915 0.0779  -0.0126 -0.0449 873  CYS B C   
4364 O O   . CYS B 623 ? 0.8942 0.8969 0.8529 0.0683  -0.0111 -0.0406 873  CYS B O   
4365 C CB  . CYS B 623 ? 0.8944 0.8317 0.8456 0.0601  -0.0201 -0.0330 873  CYS B CB  
4366 S SG  . CYS B 623 ? 1.3231 1.3142 1.3040 0.0669  -0.0205 -0.0190 873  CYS B SG  
4367 N N   . THR B 624 ? 1.0811 1.0554 1.0198 0.1000  -0.0114 -0.0485 874  THR B N   
4368 C CA  . THR B 624 ? 1.0030 1.0244 0.9522 0.1137  -0.0071 -0.0476 874  THR B CA  
4369 C C   . THR B 624 ? 1.0294 1.0744 0.9899 0.1323  -0.0078 -0.0401 874  THR B C   
4370 O O   . THR B 624 ? 1.0062 1.0867 0.9907 0.1256  -0.0093 -0.0250 874  THR B O   
4371 C CB  . THR B 624 ? 1.0177 1.0281 0.9435 0.1260  -0.0037 -0.0647 874  THR B CB  
4372 O OG1 . THR B 624 ? 1.1168 1.0787 1.0168 0.1416  -0.0068 -0.0759 874  THR B OG1 
4373 C CG2 . THR B 624 ? 0.8370 0.8344 0.7541 0.1060  -0.0029 -0.0710 874  THR B CG2 
4374 N N   . THR B 625 ? 0.9473 0.9721 0.8895 0.1559  -0.0080 -0.0507 875  THR B N   
4375 C CA  . THR B 625 ? 1.0684 1.1218 1.0207 0.1776  -0.0085 -0.0452 875  THR B CA  
4376 C C   . THR B 625 ? 1.0855 1.1173 1.0437 0.1732  -0.0146 -0.0351 875  THR B C   
4377 O O   . THR B 625 ? 1.1400 1.2100 1.1211 0.1724  -0.0159 -0.0212 875  THR B O   
4378 C CB  . THR B 625 ? 1.2445 1.2837 1.1731 0.2088  -0.0076 -0.0619 875  THR B CB  
4379 O OG1 . THR B 625 ? 1.2300 1.1992 1.1311 0.2127  -0.0138 -0.0705 875  THR B OG1 
4380 C CG2 . THR B 625 ? 1.0154 1.0656 0.9322 0.2115  -0.0024 -0.0749 875  THR B CG2 
4381 N N   . THR B 626 ? 1.1938 1.1653 1.1303 0.1690  -0.0188 -0.0412 876  THR B N   
4382 C CA  . THR B 626 ? 1.1847 1.1318 1.1228 0.1640  -0.0247 -0.0324 876  THR B CA  
4383 C C   . THR B 626 ? 1.2256 1.1542 1.1671 0.1342  -0.0260 -0.0275 876  THR B C   
4384 O O   . THR B 626 ? 1.3296 1.2186 1.2507 0.1233  -0.0263 -0.0361 876  THR B O   
4385 C CB  . THR B 626 ? 1.3838 1.2773 1.2927 0.1817  -0.0297 -0.0414 876  THR B CB  
4386 O OG1 . THR B 626 ? 1.3924 1.2322 1.2747 0.1675  -0.0313 -0.0510 876  THR B OG1 
4387 C CG2 . THR B 626 ? 1.2998 1.2080 1.1998 0.2149  -0.0284 -0.0514 876  THR B CG2 
4388 N N   . CYS B 627 ? 1.1017 1.0600 1.0676 0.1214  -0.0274 -0.0142 877  CYS B N   
4389 C CA  . CYS B 627 ? 0.9342 0.8837 0.9058 0.0968  -0.0290 -0.0101 877  CYS B CA  
4390 C C   . CYS B 627 ? 0.8250 0.7572 0.7985 0.0915  -0.0346 -0.0023 877  CYS B C   
4391 O O   . CYS B 627 ? 0.8311 0.7854 0.8188 0.0987  -0.0376 0.0071  877  CYS B O   
4392 C CB  . CYS B 627 ? 0.9177 0.9112 0.9125 0.0861  -0.0280 -0.0022 877  CYS B CB  
4393 S SG  . CYS B 627 ? 1.5077 1.4933 1.5025 0.0632  -0.0277 -0.0053 877  CYS B SG  
4394 N N   . GLN B 628 ? 0.8524 0.7487 0.8114 0.0779  -0.0361 -0.0058 878  GLN B N   
4395 C CA  . GLN B 628 ? 0.8542 0.7320 0.8108 0.0721  -0.0410 0.0004  878  GLN B CA  
4396 C C   . GLN B 628 ? 0.8366 0.7166 0.7991 0.0511  -0.0418 0.0017  878  GLN B C   
4397 O O   . GLN B 628 ? 0.8172 0.6960 0.7755 0.0404  -0.0386 -0.0048 878  GLN B O   
4398 C CB  . GLN B 628 ? 0.8939 0.7241 0.8224 0.0771  -0.0433 -0.0045 878  GLN B CB  
4399 C CG  . GLN B 628 ? 0.9812 0.8018 0.8978 0.1013  -0.0433 -0.0099 878  GLN B CG  
4400 C CD  . GLN B 628 ? 1.1726 0.9779 1.0828 0.1169  -0.0491 -0.0042 878  GLN B CD  
4401 O OE1 . GLN B 628 ? 1.3032 1.0754 1.1992 0.1084  -0.0537 -0.0008 878  GLN B OE1 
4402 N NE2 . GLN B 628 ? 1.3092 1.1420 1.2297 0.1400  -0.0491 -0.0028 878  GLN B NE2 
4403 N N   . PHE B 629 ? 0.8260 0.7111 0.7977 0.0466  -0.0464 0.0095  879  PHE B N   
4404 C CA  . PHE B 629 ? 0.7776 0.6670 0.7544 0.0306  -0.0481 0.0096  879  PHE B CA  
4405 C C   . PHE B 629 ? 0.7652 0.6279 0.7216 0.0187  -0.0458 0.0026  879  PHE B C   
4406 O O   . PHE B 629 ? 0.8949 0.7309 0.8348 0.0178  -0.0475 0.0038  879  PHE B O   
4407 C CB  . PHE B 629 ? 0.7136 0.6094 0.6998 0.0301  -0.0545 0.0178  879  PHE B CB  
4408 C CG  . PHE B 629 ? 0.7266 0.6293 0.7182 0.0179  -0.0574 0.0166  879  PHE B CG  
4409 C CD1 . PHE B 629 ? 0.7021 0.6249 0.7063 0.0141  -0.0583 0.0153  879  PHE B CD1 
4410 C CD2 . PHE B 629 ? 0.7053 0.5950 0.6878 0.0116  -0.0599 0.0164  879  PHE B CD2 
4411 C CE1 . PHE B 629 ? 0.7257 0.6532 0.7330 0.0068  -0.0623 0.0126  879  PHE B CE1 
4412 C CE2 . PHE B 629 ? 0.7676 0.6667 0.7540 0.0037  -0.0627 0.0132  879  PHE B CE2 
4413 C CZ  . PHE B 629 ? 0.7614 0.6783 0.7599 0.0026  -0.0642 0.0107  879  PHE B CZ  
4414 N N   . GLY B 630 ? 0.7994 0.6711 0.7563 0.0083  -0.0427 -0.0037 880  GLY B N   
4415 C CA  . GLY B 630 ? 0.7505 0.6044 0.6890 -0.0058 -0.0402 -0.0102 880  GLY B CA  
4416 C C   . GLY B 630 ? 0.7641 0.6108 0.6920 -0.0075 -0.0361 -0.0180 880  GLY B C   
4417 O O   . GLY B 630 ? 0.9239 0.7651 0.8401 -0.0225 -0.0343 -0.0235 880  GLY B O   
4418 N N   . ASP B 631 ? 0.7666 0.6161 0.6978 0.0070  -0.0349 -0.0188 881  ASP B N   
4419 C CA  . ASP B 631 ? 0.8281 0.6716 0.7483 0.0074  -0.0314 -0.0275 881  ASP B CA  
4420 C C   . ASP B 631 ? 0.8528 0.7287 0.7876 -0.0002 -0.0288 -0.0301 881  ASP B C   
4421 O O   . ASP B 631 ? 0.7434 0.6469 0.6989 0.0007  -0.0304 -0.0243 881  ASP B O   
4422 C CB  . ASP B 631 ? 0.8911 0.7334 0.8103 0.0281  -0.0307 -0.0284 881  ASP B CB  
4423 C CG  . ASP B 631 ? 1.0291 0.8349 0.9295 0.0388  -0.0343 -0.0278 881  ASP B CG  
4424 O OD1 . ASP B 631 ? 0.9650 0.7408 0.8491 0.0269  -0.0373 -0.0267 881  ASP B OD1 
4425 O OD2 . ASP B 631 ? 1.0831 0.8919 0.9842 0.0594  -0.0345 -0.0281 881  ASP B OD2 
4426 N N   . PRO B 632 ? 0.8711 0.7419 0.7935 -0.0079 -0.0261 -0.0387 882  PRO B N   
4427 C CA  . PRO B 632 ? 0.8120 0.7149 0.7476 -0.0124 -0.0241 -0.0410 882  PRO B CA  
4428 C C   . PRO B 632 ? 0.8942 0.8223 0.8461 0.0021  -0.0232 -0.0368 882  PRO B C   
4429 O O   . PRO B 632 ? 0.8728 0.7960 0.8168 0.0133  -0.0209 -0.0406 882  PRO B O   
4430 C CB  . PRO B 632 ? 0.8870 0.7742 0.8017 -0.0224 -0.0219 -0.0515 882  PRO B CB  
4431 C CG  . PRO B 632 ? 0.8738 0.7212 0.7651 -0.0308 -0.0242 -0.0529 882  PRO B CG  
4432 C CD  . PRO B 632 ? 0.8301 0.6633 0.7239 -0.0154 -0.0264 -0.0462 882  PRO B CD  
4433 N N   . GLY B 633 ? 0.8107 0.7658 0.7836 0.0021  -0.0259 -0.0289 883  GLY B N   
4434 C CA  . GLY B 633 ? 0.7090 0.6899 0.6973 0.0119  -0.0266 -0.0216 883  GLY B CA  
4435 C C   . GLY B 633 ? 0.7322 0.7144 0.7293 0.0213  -0.0295 -0.0124 883  GLY B C   
4436 O O   . GLY B 633 ? 0.7722 0.7750 0.7775 0.0306  -0.0288 -0.0072 883  GLY B O   
4437 N N   . ASP B 634 ? 0.6859 0.6507 0.6815 0.0185  -0.0329 -0.0099 884  ASP B N   
4438 C CA  . ASP B 634 ? 0.7093 0.6752 0.7122 0.0269  -0.0363 -0.0013 884  ASP B CA  
4439 C C   . ASP B 634 ? 0.8245 0.8203 0.8478 0.0263  -0.0413 0.0098  884  ASP B C   
4440 O O   . ASP B 634 ? 0.7575 0.7721 0.7890 0.0345  -0.0416 0.0168  884  ASP B O   
4441 C CB  . ASP B 634 ? 0.7298 0.6723 0.7259 0.0221  -0.0394 -0.0009 884  ASP B CB  
4442 C CG  . ASP B 634 ? 0.7684 0.7114 0.7655 0.0093  -0.0413 -0.0040 884  ASP B CG  
4443 O OD1 . ASP B 634 ? 0.7530 0.7138 0.7578 0.0053  -0.0416 -0.0054 884  ASP B OD1 
4444 O OD2 . ASP B 634 ? 0.7472 0.6749 0.7367 0.0040  -0.0428 -0.0051 884  ASP B OD2 
4445 N N   . ILE B 635 ? 0.7095 0.7105 0.7398 0.0167  -0.0461 0.0116  885  ILE B N   
4446 C CA  . ILE B 635 ? 0.7146 0.7356 0.7602 0.0134  -0.0538 0.0227  885  ILE B CA  
4447 C C   . ILE B 635 ? 0.6540 0.6919 0.7026 0.0093  -0.0532 0.0225  885  ILE B C   
4448 O O   . ILE B 635 ? 0.7722 0.8038 0.8159 0.0048  -0.0528 0.0150  885  ILE B O   
4449 C CB  . ILE B 635 ? 0.6724 0.6811 0.7206 0.0079  -0.0626 0.0248  885  ILE B CB  
4450 C CG1 . ILE B 635 ? 0.7338 0.7233 0.7748 0.0109  -0.0616 0.0224  885  ILE B CG1 
4451 C CG2 . ILE B 635 ? 0.6275 0.6490 0.6878 0.0042  -0.0729 0.0377  885  ILE B CG2 
4452 C CD1 . ILE B 635 ? 0.6391 0.6175 0.6801 0.0067  -0.0695 0.0222  885  ILE B CD1 
4453 N N   . MET B 636 ? 0.6594 0.7226 0.7161 0.0105  -0.0535 0.0313  886  MET B N   
4454 C CA  . MET B 636 ? 0.6804 0.7628 0.7394 0.0063  -0.0533 0.0331  886  MET B CA  
4455 C C   . MET B 636 ? 0.6936 0.7942 0.7641 -0.0012 -0.0632 0.0492  886  MET B C   
4456 O O   . MET B 636 ? 0.7016 0.8160 0.7795 -0.0011 -0.0657 0.0594  886  MET B O   
4457 C CB  . MET B 636 ? 0.6319 0.7307 0.6855 0.0137  -0.0432 0.0277  886  MET B CB  
4458 C CG  . MET B 636 ? 0.6509 0.7261 0.6888 0.0190  -0.0354 0.0119  886  MET B CG  
4459 S SD  . MET B 636 ? 0.9131 0.9744 0.9434 0.0089  -0.0358 0.0021  886  MET B SD  
4460 C CE  . MET B 636 ? 0.7233 0.8154 0.7575 0.0061  -0.0353 0.0052  886  MET B CE  
4461 N N   . SER B 637 ? 0.6996 0.8004 0.7706 -0.0082 -0.0699 0.0521  887  SER B N   
4462 C CA  . SER B 637 ? 0.7870 0.8993 0.8648 -0.0179 -0.0817 0.0684  887  SER B CA  
4463 C C   . SER B 637 ? 0.7260 0.8683 0.8047 -0.0209 -0.0778 0.0739  887  SER B C   
4464 O O   . SER B 637 ? 0.7094 0.8505 0.7830 -0.0213 -0.0771 0.0683  887  SER B O   
4465 C CB  . SER B 637 ? 0.8035 0.8907 0.8782 -0.0218 -0.0945 0.0684  887  SER B CB  
4466 O OG  . SER B 637 ? 0.7974 0.8873 0.8748 -0.0323 -0.1086 0.0850  887  SER B OG  
4467 N N   . THR B 638 ? 0.7840 0.9571 0.8691 -0.0230 -0.0754 0.0847  888  THR B N   
4468 C CA  . THR B 638 ? 0.9412 1.1502 1.0269 -0.0253 -0.0704 0.0902  888  THR B CA  
4469 C C   . THR B 638 ? 0.9558 1.1818 1.0465 -0.0417 -0.0831 0.1117  888  THR B C   
4470 O O   . THR B 638 ? 0.8941 1.1064 0.9883 -0.0507 -0.0953 0.1227  888  THR B O   
4471 C CB  . THR B 638 ? 0.8931 1.1318 0.9812 -0.0144 -0.0582 0.0866  888  THR B CB  
4472 O OG1 . THR B 638 ? 0.8637 1.1195 0.9618 -0.0183 -0.0631 0.1001  888  THR B OG1 
4473 C CG2 . THR B 638 ? 0.7714 0.9843 0.8508 0.0007  -0.0486 0.0668  888  THR B CG2 
4474 N N   . PRO B 639 ? 0.9753 1.2294 1.0643 -0.0474 -0.0818 0.1185  889  PRO B N   
4475 C CA  . PRO B 639 ? 0.9327 1.2046 1.0244 -0.0660 -0.0947 0.1418  889  PRO B CA  
4476 C C   . PRO B 639 ? 0.9841 1.2852 1.0855 -0.0739 -0.0967 0.1567  889  PRO B C   
4477 O O   . PRO B 639 ? 1.0845 1.3808 1.1871 -0.0917 -0.1120 0.1753  889  PRO B O   
4478 C CB  . PRO B 639 ? 0.9562 1.2612 1.0440 -0.0679 -0.0887 0.1440  889  PRO B CB  
4479 C CG  . PRO B 639 ? 1.0608 1.3464 1.1413 -0.0532 -0.0790 0.1217  889  PRO B CG  
4480 C CD  . PRO B 639 ? 0.9480 1.2139 1.0302 -0.0395 -0.0709 0.1060  889  PRO B CD  
4481 N N   . VAL B 640 ? 1.0322 1.3632 1.1392 -0.0609 -0.0827 0.1489  890  VAL B N   
4482 C CA  . VAL B 640 ? 0.9237 1.2889 1.0414 -0.0663 -0.0841 0.1621  890  VAL B CA  
4483 C C   . VAL B 640 ? 0.9741 1.3030 1.0943 -0.0688 -0.0938 0.1630  890  VAL B C   
4484 O O   . VAL B 640 ? 1.0156 1.3599 1.1426 -0.0835 -0.1036 0.1802  890  VAL B O   
4485 C CB  . VAL B 640 ? 0.8973 1.3041 1.0189 -0.0468 -0.0670 0.1513  890  VAL B CB  
4486 C CG1 . VAL B 640 ? 0.9214 1.3130 1.0322 -0.0293 -0.0549 0.1295  890  VAL B CG1 
4487 C CG2 . VAL B 640 ? 0.8634 1.2654 0.9914 -0.0356 -0.0650 0.1465  890  VAL B CG2 
4488 N N   . GLY B 641 ? 0.9772 1.2597 1.0913 -0.0565 -0.0918 0.1454  891  GLY B N   
4489 C CA  . GLY B 641 ? 0.8160 1.0645 0.9308 -0.0578 -0.1006 0.1447  891  GLY B CA  
4490 C C   . GLY B 641 ? 0.7997 1.0137 0.9084 -0.0400 -0.0919 0.1230  891  GLY B C   
4491 O O   . GLY B 641 ? 0.8008 1.0060 0.9026 -0.0311 -0.0834 0.1095  891  GLY B O   
4492 N N   . MET B 642 ? 0.7337 0.9300 0.8442 -0.0368 -0.0950 0.1209  892  MET B N   
4493 C CA  . MET B 642 ? 0.7007 0.8635 0.8043 -0.0233 -0.0889 0.1032  892  MET B CA  
4494 C C   . MET B 642 ? 0.7518 0.9316 0.8561 -0.0073 -0.0755 0.0951  892  MET B C   
4495 O O   . MET B 642 ? 0.9315 1.1359 1.0438 -0.0052 -0.0758 0.1032  892  MET B O   
4496 C CB  . MET B 642 ? 0.7986 0.9317 0.9014 -0.0282 -0.1003 0.1052  892  MET B CB  
4497 C CG  . MET B 642 ? 0.7565 0.8533 0.8502 -0.0186 -0.0966 0.0884  892  MET B CG  
4498 S SD  . MET B 642 ? 0.9069 0.9716 0.9923 -0.0237 -0.1068 0.0828  892  MET B SD  
4499 C CE  . MET B 642 ? 0.8003 0.8617 0.8784 -0.0133 -0.0919 0.0650  892  MET B CE  
4500 N N   . LYS B 643 ? 0.7607 0.9270 0.8554 0.0042  -0.0650 0.0792  893  LYS B N   
4501 C CA  . LYS B 643 ? 0.8256 0.9939 0.9153 0.0213  -0.0544 0.0688  893  LYS B CA  
4502 C C   . LYS B 643 ? 0.7477 0.8746 0.8284 0.0257  -0.0547 0.0589  893  LYS B C   
4503 O O   . LYS B 643 ? 0.8082 0.9071 0.8807 0.0213  -0.0551 0.0505  893  LYS B O   
4504 C CB  . LYS B 643 ? 0.8326 1.0086 0.9134 0.0297  -0.0441 0.0576  893  LYS B CB  
4505 C CG  . LYS B 643 ? 0.9192 1.0952 0.9914 0.0495  -0.0351 0.0465  893  LYS B CG  
4506 C CD  . LYS B 643 ? 1.0398 1.2578 1.1234 0.0581  -0.0347 0.0562  893  LYS B CD  
4507 C CE  . LYS B 643 ? 1.2360 1.5045 1.3268 0.0559  -0.0315 0.0632  893  LYS B CE  
4508 N NZ  . LYS B 643 ? 1.3050 1.5758 1.3823 0.0707  -0.0215 0.0476  893  LYS B NZ  
4509 N N   . CYS B 644 ? 0.6715 0.7980 0.7536 0.0342  -0.0548 0.0606  894  CYS B N   
4510 C CA  . CYS B 644 ? 0.7683 0.8588 0.8428 0.0351  -0.0574 0.0552  894  CYS B CA  
4511 C C   . CYS B 644 ? 0.7771 0.8517 0.8396 0.0513  -0.0505 0.0456  894  CYS B C   
4512 O O   . CYS B 644 ? 0.7996 0.8959 0.8631 0.0650  -0.0459 0.0455  894  CYS B O   
4513 C CB  . CYS B 644 ? 0.8527 0.9486 0.9373 0.0280  -0.0676 0.0673  894  CYS B CB  
4514 S SG  . CYS B 644 ? 0.9637 1.0564 1.0545 0.0088  -0.0799 0.0760  894  CYS B SG  
4515 N N   . PRO B 645 ? 0.8169 0.8539 0.8664 0.0505  -0.0504 0.0377  895  PRO B N   
4516 C CA  . PRO B 645 ? 0.8823 0.8955 0.9160 0.0640  -0.0461 0.0297  895  PRO B CA  
4517 C C   . PRO B 645 ? 0.7340 0.7454 0.7701 0.0713  -0.0509 0.0365  895  PRO B C   
4518 O O   . PRO B 645 ? 0.8553 0.8780 0.9034 0.0631  -0.0577 0.0460  895  PRO B O   
4519 C CB  . PRO B 645 ? 0.7870 0.7636 0.8051 0.0542  -0.0449 0.0203  895  PRO B CB  
4520 C CG  . PRO B 645 ? 0.8336 0.8141 0.8620 0.0402  -0.0511 0.0258  895  PRO B CG  
4521 C CD  . PRO B 645 ? 0.7578 0.7727 0.8044 0.0372  -0.0547 0.0355  895  PRO B CD  
4522 N N   . GLU B 646 ? 0.8889 0.8837 0.9114 0.0874  -0.0484 0.0311  896  GLU B N   
4523 C CA  . GLU B 646 ? 0.8317 0.8164 0.8518 0.0951  -0.0533 0.0362  896  GLU B CA  
4524 C C   . GLU B 646 ? 0.7816 0.7292 0.7899 0.0821  -0.0565 0.0346  896  GLU B C   
4525 O O   . GLU B 646 ? 0.8760 0.7952 0.8689 0.0748  -0.0533 0.0261  896  GLU B O   
4526 C CB  . GLU B 646 ? 0.9202 0.8934 0.9261 0.1185  -0.0513 0.0305  896  GLU B CB  
4527 C CG  . GLU B 646 ? 1.1980 1.2188 1.2189 0.1357  -0.0502 0.0352  896  GLU B CG  
4528 C CD  . GLU B 646 ? 1.3374 1.3957 1.3808 0.1282  -0.0561 0.0499  896  GLU B CD  
4529 O OE1 . GLU B 646 ? 1.3274 1.4346 1.3891 0.1271  -0.0552 0.0569  896  GLU B OE1 
4530 O OE2 . GLU B 646 ? 1.3599 1.3992 1.4015 0.1217  -0.0621 0.0548  896  GLU B OE2 
4531 N N   . LEU B 647 ? 0.8386 0.7901 0.8540 0.0781  -0.0630 0.0430  897  LEU B N   
4532 C CA  . LEU B 647 ? 1.0144 0.9368 1.0187 0.0669  -0.0662 0.0420  897  LEU B CA  
4533 C C   . LEU B 647 ? 0.8797 0.7718 0.8646 0.0779  -0.0671 0.0411  897  LEU B C   
4534 O O   . LEU B 647 ? 1.0122 0.9075 0.9991 0.0850  -0.0725 0.0482  897  LEU B O   
4535 C CB  . LEU B 647 ? 0.8094 0.7485 0.8278 0.0575  -0.0737 0.0503  897  LEU B CB  
4536 C CG  . LEU B 647 ? 0.7264 0.6834 0.7581 0.0451  -0.0752 0.0506  897  LEU B CG  
4537 C CD1 . LEU B 647 ? 0.8043 0.7772 0.8489 0.0378  -0.0851 0.0597  897  LEU B CD1 
4538 C CD2 . LEU B 647 ? 0.7810 0.7175 0.8021 0.0347  -0.0724 0.0412  897  LEU B CD2 
4539 N N   . SER B 648 ? 0.8613 0.7219 0.8256 0.0785  -0.0631 0.0326  898  SER B N   
4540 C CA  . SER B 648 ? 1.0110 0.8347 0.9519 0.0889  -0.0656 0.0316  898  SER B CA  
4541 C C   . SER B 648 ? 0.9970 0.8026 0.9294 0.0795  -0.0710 0.0379  898  SER B C   
4542 O O   . SER B 648 ? 1.0794 0.8832 1.0112 0.0609  -0.0704 0.0373  898  SER B O   
4543 C CB  . SER B 648 ? 1.0234 0.8121 0.9410 0.0854  -0.0620 0.0215  898  SER B CB  
4544 O OG  . SER B 648 ? 1.2797 1.0667 1.1964 0.0630  -0.0589 0.0181  898  SER B OG  
4545 N N   . GLY B 649 ? 0.9981 0.7930 0.9234 0.0938  -0.0765 0.0437  899  GLY B N   
4546 C CA  . GLY B 649 ? 0.8530 0.6322 0.7690 0.0870  -0.0824 0.0508  899  GLY B CA  
4547 C C   . GLY B 649 ? 0.8915 0.6914 0.8189 0.1030  -0.0885 0.0596  899  GLY B C   
4548 O O   . GLY B 649 ? 1.0437 0.8646 0.9814 0.1220  -0.0882 0.0597  899  GLY B O   
4549 N N   . SER B 650 ? 0.9241 0.7220 0.8497 0.0952  -0.0941 0.0668  900  SER B N   
4550 C CA  . SER B 650 ? 0.9319 0.7506 0.8677 0.1078  -0.1010 0.0759  900  SER B CA  
4551 C C   . SER B 650 ? 0.8395 0.6699 0.7817 0.0914  -0.1054 0.0813  900  SER B C   
4552 O O   . SER B 650 ? 0.8895 0.7041 0.8216 0.0739  -0.1037 0.0781  900  SER B O   
4553 C CB  . SER B 650 ? 0.8995 0.6865 0.8132 0.1260  -0.1065 0.0794  900  SER B CB  
4554 O OG  . SER B 650 ? 1.1143 0.8627 1.0036 0.1129  -0.1100 0.0823  900  SER B OG  
4555 N N   . PHE B 651 ? 0.9002 0.7611 0.8587 0.0976  -0.1115 0.0891  901  PHE B N   
4556 C CA  . PHE B 651 ? 0.8110 0.6832 0.7744 0.0843  -0.1177 0.0939  901  PHE B CA  
4557 C C   . PHE B 651 ? 0.9513 0.8047 0.8976 0.0896  -0.1245 0.1010  901  PHE B C   
4558 O O   . PHE B 651 ? 0.9507 0.7944 0.8890 0.1081  -0.1270 0.1050  901  PHE B O   
4559 C CB  . PHE B 651 ? 0.7862 0.7023 0.7759 0.0836  -0.1224 0.0991  901  PHE B CB  
4560 C CG  . PHE B 651 ? 0.7612 0.6940 0.7660 0.0729  -0.1184 0.0941  901  PHE B CG  
4561 C CD1 . PHE B 651 ? 0.7502 0.6739 0.7528 0.0558  -0.1188 0.0886  901  PHE B CD1 
4562 C CD2 . PHE B 651 ? 0.7511 0.7103 0.7713 0.0812  -0.1149 0.0951  901  PHE B CD2 
4563 C CE1 . PHE B 651 ? 0.7698 0.7058 0.7845 0.0475  -0.1167 0.0845  901  PHE B CE1 
4564 C CE2 . PHE B 651 ? 0.7308 0.7043 0.7632 0.0704  -0.1122 0.0920  901  PHE B CE2 
4565 C CZ  . PHE B 651 ? 0.7216 0.6812 0.7510 0.0538  -0.1137 0.0870  901  PHE B CZ  
4566 N N   . ARG B 652 ? 0.9104 0.7589 0.8499 0.0745  -0.1281 0.1022  902  ARG B N   
4567 C CA  . ARG B 652 ? 0.9309 0.7654 0.8541 0.0762  -0.1353 0.1099  902  ARG B CA  
4568 C C   . ARG B 652 ? 0.9195 0.7792 0.8534 0.0658  -0.1422 0.1127  902  ARG B C   
4569 O O   . ARG B 652 ? 0.9285 0.7911 0.8635 0.0504  -0.1406 0.1060  902  ARG B O   
4570 C CB  . ARG B 652 ? 0.9104 0.7059 0.8051 0.0658  -0.1325 0.1082  902  ARG B CB  
4571 C CG  . ARG B 652 ? 1.0166 0.7757 0.8897 0.0791  -0.1336 0.1120  902  ARG B CG  
4572 C CD  . ARG B 652 ? 0.9472 0.6677 0.7922 0.0634  -0.1303 0.1101  902  ARG B CD  
4573 N NE  . ARG B 652 ? 0.9996 0.7246 0.8358 0.0439  -0.1314 0.1121  902  ARG B NE  
4574 C CZ  . ARG B 652 ? 0.9758 0.7131 0.8150 0.0258  -0.1250 0.1042  902  ARG B CZ  
4575 N NH1 . ARG B 652 ? 0.9061 0.6503 0.7571 0.0238  -0.1174 0.0947  902  ARG B NH1 
4576 N NH2 . ARG B 652 ? 1.1820 0.9272 1.0120 0.0111  -0.1263 0.1054  902  ARG B NH2 
4577 N N   . LYS B 653 ? 0.9130 0.7912 0.8537 0.0752  -0.1506 0.1218  903  LYS B N   
4578 C CA  . LYS B 653 ? 0.9926 0.8941 0.9423 0.0654  -0.1591 0.1248  903  LYS B CA  
4579 C C   . LYS B 653 ? 1.0257 0.9069 0.9525 0.0570  -0.1627 0.1262  903  LYS B C   
4580 O O   . LYS B 653 ? 1.1560 1.0251 1.0689 0.0658  -0.1670 0.1346  903  LYS B O   
4581 C CB  . LYS B 653 ? 1.0368 0.9712 1.0031 0.0773  -0.1670 0.1347  903  LYS B CB  
4582 C CG  . LYS B 653 ? 0.8501 0.8160 0.8335 0.0643  -0.1754 0.1366  903  LYS B CG  
4583 C CD  . LYS B 653 ? 0.9729 0.9662 0.9630 0.0713  -0.1860 0.1481  903  LYS B CD  
4584 C CE  . LYS B 653 ? 0.8492 0.8592 0.8472 0.0945  -0.1841 0.1547  903  LYS B CE  
4585 N NZ  . LYS B 653 ? 0.8400 0.8821 0.8454 0.1028  -0.1949 0.1660  903  LYS B NZ  
4586 N N   . LYS B 654 ? 0.9898 0.8685 0.9118 0.0410  -0.1615 0.1181  904  LYS B N   
4587 C CA  . LYS B 654 ? 1.1442 1.0105 1.0447 0.0316  -0.1639 0.1180  904  LYS B CA  
4588 C C   . LYS B 654 ? 1.1007 0.9877 1.0067 0.0242  -0.1736 0.1167  904  LYS B C   
4589 O O   . LYS B 654 ? 1.0177 0.9253 0.9431 0.0242  -0.1792 0.1165  904  LYS B O   
4590 C CB  . LYS B 654 ? 1.0090 0.8592 0.8962 0.0203  -0.1546 0.1083  904  LYS B CB  
4591 C CG  . LYS B 654 ? 1.0225 0.8465 0.8978 0.0236  -0.1467 0.1100  904  LYS B CG  
4592 C CD  . LYS B 654 ? 1.1372 0.9369 0.9834 0.0176  -0.1476 0.1171  904  LYS B CD  
4593 C CE  . LYS B 654 ? 1.1084 0.8995 0.9473 0.0301  -0.1567 0.1303  904  LYS B CE  
4594 N NZ  . LYS B 654 ? 1.0049 0.7675 0.8126 0.0229  -0.1590 0.1390  904  LYS B NZ  
4595 N N   . CYS B 655 ? 1.0806 0.9616 0.9672 0.0165  -0.1764 0.1160  905  CYS B N   
4596 C CA  . CYS B 655 ? 0.9000 0.7965 0.7861 0.0097  -0.1864 0.1131  905  CYS B CA  
4597 C C   . CYS B 655 ? 1.0328 0.9243 0.9014 -0.0008 -0.1829 0.1015  905  CYS B C   
4598 O O   . CYS B 655 ? 1.1675 1.0480 1.0162 -0.0043 -0.1776 0.1040  905  CYS B O   
4599 C CB  . CYS B 655 ? 0.9554 0.8579 0.8346 0.0141  -0.1960 0.1256  905  CYS B CB  
4600 S SG  . CYS B 655 ? 1.1311 1.0534 1.0099 0.0053  -0.2103 0.1224  905  CYS B SG  
4601 N N   . ALA B 656 ? 1.0783 0.9783 0.9528 -0.0055 -0.1866 0.0891  906  ALA B N   
4602 C CA  . ALA B 656 ? 1.0459 0.9469 0.9051 -0.0117 -0.1840 0.0754  906  ALA B CA  
4603 C C   . ALA B 656 ? 1.1633 1.0731 1.0115 -0.0148 -0.1958 0.0720  906  ALA B C   
4604 O O   . ALA B 656 ? 1.1077 1.0219 0.9661 -0.0147 -0.2075 0.0724  906  ALA B O   
4605 C CB  . ALA B 656 ? 0.9727 0.8735 0.8424 -0.0115 -0.1809 0.0614  906  ALA B CB  
4606 N N   . PHE B 657 ? 1.1225 1.0361 0.9487 -0.0189 -0.1933 0.0692  907  PHE B N   
4607 C CA  . PHE B 657 ? 1.1588 1.0821 0.9701 -0.0216 -0.2034 0.0641  907  PHE B CA  
4608 C C   . PHE B 657 ? 1.1583 1.0841 0.9730 -0.0209 -0.2151 0.0778  907  PHE B C   
4609 O O   . PHE B 657 ? 1.2346 1.1674 1.0428 -0.0232 -0.2270 0.0730  907  PHE B O   
4610 C CB  . PHE B 657 ? 1.1064 1.0319 0.9188 -0.0202 -0.2103 0.0449  907  PHE B CB  
4611 C CG  . PHE B 657 ? 1.1437 1.0683 0.9589 -0.0175 -0.2004 0.0315  907  PHE B CG  
4612 C CD1 . PHE B 657 ? 1.1502 1.0654 0.9838 -0.0142 -0.2020 0.0270  907  PHE B CD1 
4613 C CD2 . PHE B 657 ? 1.2336 1.1700 1.0330 -0.0193 -0.1898 0.0245  907  PHE B CD2 
4614 C CE1 . PHE B 657 ? 1.1969 1.1124 1.0330 -0.0109 -0.1936 0.0151  907  PHE B CE1 
4615 C CE2 . PHE B 657 ? 1.3058 1.2466 1.1089 -0.0165 -0.1810 0.0124  907  PHE B CE2 
4616 C CZ  . PHE B 657 ? 1.2600 1.1892 1.0814 -0.0114 -0.1830 0.0074  907  PHE B CZ  
4617 N N   . ALA B 658 ? 1.1342 1.0550 0.9579 -0.0168 -0.2127 0.0941  908  ALA B N   
4618 C CA  . ALA B 658 ? 1.1059 1.0340 0.9353 -0.0135 -0.2233 0.1082  908  ALA B CA  
4619 C C   . ALA B 658 ? 1.1292 1.0686 0.9754 -0.0155 -0.2357 0.1046  908  ALA B C   
4620 O O   . ALA B 658 ? 1.0729 1.0245 0.9197 -0.0169 -0.2477 0.1120  908  ALA B O   
4621 C CB  . ALA B 658 ? 0.9535 0.8860 0.7600 -0.0167 -0.2285 0.1144  908  ALA B CB  
4622 N N   . THR B 659 ? 1.0604 0.9955 0.9194 -0.0171 -0.2339 0.0942  909  THR B N   
4623 C CA  . THR B 659 ? 1.0969 1.0375 0.9676 -0.0227 -0.2472 0.0906  909  THR B CA  
4624 C C   . THR B 659 ? 1.0039 0.9450 0.8980 -0.0217 -0.2440 0.0933  909  THR B C   
4625 O O   . THR B 659 ? 0.9992 0.9556 0.9104 -0.0233 -0.2510 0.1045  909  THR B O   
4626 C CB  . THR B 659 ? 1.1404 1.0712 0.9952 -0.0276 -0.2539 0.0718  909  THR B CB  
4627 O OG1 . THR B 659 ? 1.3238 1.2575 1.1552 -0.0275 -0.2534 0.0679  909  THR B OG1 
4628 C CG2 . THR B 659 ? 1.1034 1.0343 0.9629 -0.0359 -0.2722 0.0699  909  THR B CG2 
4629 N N   . THR B 660 ? 0.8982 0.8268 0.7932 -0.0194 -0.2335 0.0834  910  THR B N   
4630 C CA  . THR B 660 ? 1.0254 0.9536 0.9400 -0.0199 -0.2315 0.0838  910  THR B CA  
4631 C C   . THR B 660 ? 0.9633 0.8942 0.8886 -0.0114 -0.2174 0.0923  910  THR B C   
4632 O O   . THR B 660 ? 1.0350 0.9555 0.9490 -0.0071 -0.2059 0.0891  910  THR B O   
4633 C CB  . THR B 660 ? 0.9588 0.8711 0.8675 -0.0217 -0.2309 0.0668  910  THR B CB  
4634 O OG1 . THR B 660 ? 1.1544 1.0636 1.0741 -0.0173 -0.2182 0.0662  910  THR B OG1 
4635 C CG2 . THR B 660 ? 0.9220 0.8278 0.8073 -0.0197 -0.2283 0.0536  910  THR B CG2 
4636 N N   . PRO B 661 ? 0.9698 0.9155 0.9155 -0.0093 -0.2184 0.1030  911  PRO B N   
4637 C CA  . PRO B 661 ? 0.9633 0.9099 0.9178 0.0010  -0.2055 0.1085  911  PRO B CA  
4638 C C   . PRO B 661 ? 0.9164 0.8501 0.8733 0.0001  -0.1959 0.0981  911  PRO B C   
4639 O O   . PRO B 661 ? 0.8224 0.7573 0.7880 -0.0066 -0.2008 0.0932  911  PRO B O   
4640 C CB  . PRO B 661 ? 0.8430 0.8167 0.8189 0.0035  -0.2110 0.1212  911  PRO B CB  
4641 C CG  . PRO B 661 ? 0.8190 0.8065 0.7946 -0.0061 -0.2267 0.1254  911  PRO B CG  
4642 C CD  . PRO B 661 ? 0.9882 0.9540 0.9478 -0.0162 -0.2320 0.1115  911  PRO B CD  
4643 N N   . VAL B 662 ? 0.9502 0.8701 0.8977 0.0058  -0.1835 0.0953  912  VAL B N   
4644 C CA  . VAL B 662 ? 0.8752 0.7853 0.8245 0.0053  -0.1734 0.0861  912  VAL B CA  
4645 C C   . VAL B 662 ? 0.9442 0.8495 0.8959 0.0144  -0.1628 0.0919  912  VAL B C   
4646 O O   . VAL B 662 ? 0.9336 0.8319 0.8751 0.0205  -0.1616 0.0992  912  VAL B O   
4647 C CB  . VAL B 662 ? 0.9546 0.8526 0.8857 0.0004  -0.1693 0.0736  912  VAL B CB  
4648 C CG1 . VAL B 662 ? 0.9842 0.8776 0.9196 -0.0003 -0.1608 0.0638  912  VAL B CG1 
4649 C CG2 . VAL B 662 ? 1.1631 1.0638 1.0867 -0.0050 -0.1810 0.0668  912  VAL B CG2 
4650 N N   . CYS B 663 ? 0.8700 0.7766 0.8331 0.0158  -0.1563 0.0884  913  CYS B N   
4651 C CA  . CYS B 663 ? 0.8515 0.7516 0.8156 0.0249  -0.1467 0.0911  913  CYS B CA  
4652 C C   . CYS B 663 ? 0.9397 0.8212 0.8913 0.0204  -0.1367 0.0816  913  CYS B C   
4653 O O   . CYS B 663 ? 1.0223 0.9048 0.9734 0.0125  -0.1359 0.0721  913  CYS B O   
4654 C CB  . CYS B 663 ? 0.8083 0.7276 0.7936 0.0296  -0.1461 0.0944  913  CYS B CB  
4655 S SG  . CYS B 663 ? 1.1405 1.0816 1.1368 0.0443  -0.1498 0.1077  913  CYS B SG  
4656 N N   . GLN B 664 ? 0.8446 0.7088 0.7849 0.0259  -0.1301 0.0843  914  GLN B N   
4657 C CA  . GLN B 664 ? 0.9345 0.7820 0.8627 0.0201  -0.1208 0.0770  914  GLN B CA  
4658 C C   . GLN B 664 ? 0.8469 0.6864 0.7789 0.0292  -0.1149 0.0776  914  GLN B C   
4659 O O   . GLN B 664 ? 0.8316 0.6759 0.7709 0.0424  -0.1175 0.0842  914  GLN B O   
4660 C CB  . GLN B 664 ? 0.8752 0.7032 0.7783 0.0131  -0.1200 0.0794  914  GLN B CB  
4661 C CG  . GLN B 664 ? 0.8931 0.7324 0.7899 0.0033  -0.1238 0.0757  914  GLN B CG  
4662 C CD  . GLN B 664 ? 1.1552 0.9803 1.0266 -0.0050 -0.1233 0.0802  914  GLN B CD  
4663 O OE1 . GLN B 664 ? 1.1498 0.9520 1.0073 -0.0026 -0.1232 0.0889  914  GLN B OE1 
4664 N NE2 . GLN B 664 ? 1.1578 0.9959 1.0211 -0.0145 -0.1238 0.0744  914  GLN B NE2 
4665 N N   . PHE B 665 ? 0.7996 0.6297 0.7263 0.0229  -0.1070 0.0699  915  PHE B N   
4666 C CA  . PHE B 665 ? 0.9266 0.7502 0.8565 0.0304  -0.1012 0.0677  915  PHE B CA  
4667 C C   . PHE B 665 ? 0.8275 0.6206 0.7338 0.0241  -0.0961 0.0652  915  PHE B C   
4668 O O   . PHE B 665 ? 0.8261 0.6169 0.7226 0.0091  -0.0931 0.0607  915  PHE B O   
4669 C CB  . PHE B 665 ? 0.7730 0.6177 0.7217 0.0274  -0.0978 0.0608  915  PHE B CB  
4670 C CG  . PHE B 665 ? 0.8215 0.6669 0.7764 0.0364  -0.0926 0.0591  915  PHE B CG  
4671 C CD1 . PHE B 665 ? 0.8037 0.6672 0.7733 0.0496  -0.0950 0.0647  915  PHE B CD1 
4672 C CD2 . PHE B 665 ? 0.8607 0.6925 0.8063 0.0313  -0.0853 0.0516  915  PHE B CD2 
4673 C CE1 . PHE B 665 ? 0.8314 0.6998 0.8057 0.0592  -0.0898 0.0621  915  PHE B CE1 
4674 C CE2 . PHE B 665 ? 0.8913 0.7239 0.8409 0.0401  -0.0809 0.0488  915  PHE B CE2 
4675 C CZ  . PHE B 665 ? 0.8491 0.7001 0.8127 0.0549  -0.0828 0.0536  915  PHE B CZ  
4676 N N   . ASP B 666 ? 0.8962 0.6670 0.7923 0.0354  -0.0960 0.0678  916  ASP B N   
4677 C CA  . ASP B 666 ? 0.8800 0.6143 0.7501 0.0291  -0.0935 0.0662  916  ASP B CA  
4678 C C   . ASP B 666 ? 0.8763 0.6082 0.7508 0.0341  -0.0876 0.0582  916  ASP B C   
4679 O O   . ASP B 666 ? 0.8833 0.6128 0.7617 0.0526  -0.0886 0.0582  916  ASP B O   
4680 C CB  . ASP B 666 ? 0.9196 0.6206 0.7681 0.0394  -0.1006 0.0748  916  ASP B CB  
4681 C CG  . ASP B 666 ? 0.9826 0.6853 0.8240 0.0330  -0.1066 0.0834  916  ASP B CG  
4682 O OD1 . ASP B 666 ? 1.0101 0.7241 0.8493 0.0146  -0.1043 0.0818  916  ASP B OD1 
4683 O OD2 . ASP B 666 ? 1.0843 0.7795 0.9219 0.0475  -0.1138 0.0914  916  ASP B OD2 
4684 N N   . GLY B 667 ? 0.8814 0.6172 0.7547 0.0184  -0.0817 0.0509  917  GLY B N   
4685 C CA  . GLY B 667 ? 0.8627 0.5980 0.7393 0.0209  -0.0762 0.0429  917  GLY B CA  
4686 C C   . GLY B 667 ? 0.8653 0.6215 0.7499 0.0042  -0.0705 0.0357  917  GLY B C   
4687 O O   . GLY B 667 ? 0.8976 0.6642 0.7806 -0.0091 -0.0706 0.0361  917  GLY B O   
4688 N N   . ASN B 668 ? 0.8286 0.5930 0.7214 0.0069  -0.0658 0.0288  918  ASN B N   
4689 C CA  . ASN B 668 ? 0.9080 0.6927 0.8082 -0.0065 -0.0608 0.0216  918  ASN B CA  
4690 C C   . ASN B 668 ? 0.8560 0.6754 0.7804 -0.0041 -0.0622 0.0215  918  ASN B C   
4691 O O   . ASN B 668 ? 0.7596 0.5924 0.7004 0.0081  -0.0649 0.0250  918  ASN B O   
4692 C CB  . ASN B 668 ? 0.8601 0.6421 0.7600 -0.0041 -0.0562 0.0146  918  ASN B CB  
4693 C CG  . ASN B 668 ? 0.8630 0.6691 0.7718 -0.0162 -0.0518 0.0075  918  ASN B CG  
4694 O OD1 . ASN B 668 ? 0.9299 0.7454 0.8354 -0.0299 -0.0512 0.0062  918  ASN B OD1 
4695 N ND2 . ASN B 668 ? 0.9744 0.7939 0.8945 -0.0103 -0.0487 0.0029  918  ASN B ND2 
4696 N N   . THR B 669 ? 0.8641 0.6985 0.7894 -0.0160 -0.0613 0.0174  919  THR B N   
4697 C CA  . THR B 669 ? 0.8055 0.6668 0.7494 -0.0135 -0.0643 0.0151  919  THR B CA  
4698 C C   . THR B 669 ? 0.7907 0.6705 0.7403 -0.0195 -0.0607 0.0063  919  THR B C   
4699 O O   . THR B 669 ? 0.8579 0.7564 0.8182 -0.0177 -0.0642 0.0026  919  THR B O   
4700 C CB  . THR B 669 ? 0.7395 0.6047 0.6792 -0.0166 -0.0690 0.0170  919  THR B CB  
4701 O OG1 . THR B 669 ? 0.7944 0.6598 0.7181 -0.0299 -0.0652 0.0133  919  THR B OG1 
4702 C CG2 . THR B 669 ? 0.8147 0.6639 0.7495 -0.0100 -0.0736 0.0264  919  THR B CG2 
4703 N N   . ILE B 670 ? 0.7716 0.6455 0.7128 -0.0260 -0.0548 0.0024  920  ILE B N   
4704 C CA  . ILE B 670 ? 0.7881 0.6819 0.7341 -0.0321 -0.0513 -0.0057 920  ILE B CA  
4705 C C   . ILE B 670 ? 0.8381 0.7336 0.7937 -0.0252 -0.0496 -0.0067 920  ILE B C   
4706 O O   . ILE B 670 ? 0.9162 0.7929 0.8639 -0.0225 -0.0474 -0.0048 920  ILE B O   
4707 C CB  . ILE B 670 ? 0.8447 0.7356 0.7726 -0.0487 -0.0465 -0.0093 920  ILE B CB  
4708 C CG1 . ILE B 670 ? 0.9092 0.7954 0.8239 -0.0567 -0.0481 -0.0054 920  ILE B CG1 
4709 C CG2 . ILE B 670 ? 0.7549 0.6761 0.6899 -0.0543 -0.0437 -0.0178 920  ILE B CG2 
4710 C CD1 . ILE B 670 ? 0.7762 0.6581 0.6701 -0.0770 -0.0444 -0.0056 920  ILE B CD1 
4711 N N   . SER B 671 ? 0.8955 0.8129 0.8663 -0.0214 -0.0513 -0.0098 921  SER B N   
4712 C CA  . SER B 671 ? 0.7364 0.6599 0.7169 -0.0158 -0.0502 -0.0095 921  SER B CA  
4713 C C   . SER B 671 ? 0.6937 0.6141 0.6637 -0.0233 -0.0437 -0.0155 921  SER B C   
4714 O O   . SER B 671 ? 0.7579 0.6772 0.7159 -0.0350 -0.0408 -0.0202 921  SER B O   
4715 C CB  . SER B 671 ? 0.8047 0.7489 0.8008 -0.0117 -0.0554 -0.0103 921  SER B CB  
4716 O OG  . SER B 671 ? 0.7874 0.7463 0.7815 -0.0170 -0.0543 -0.0185 921  SER B OG  
4717 N N   . GLY B 672 ? 0.7016 0.6226 0.6754 -0.0174 -0.0417 -0.0152 922  GLY B N   
4718 C CA  . GLY B 672 ? 0.7043 0.6207 0.6670 -0.0239 -0.0365 -0.0218 922  GLY B CA  
4719 C C   . GLY B 672 ? 0.7756 0.7140 0.7412 -0.0335 -0.0353 -0.0281 922  GLY B C   
4720 O O   . GLY B 672 ? 0.8436 0.7783 0.7959 -0.0455 -0.0319 -0.0337 922  GLY B O   
4721 N N   . TYR B 673 ? 0.6738 0.6349 0.6558 -0.0283 -0.0393 -0.0271 923  TYR B N   
4722 C CA  . TYR B 673 ? 0.6656 0.6505 0.6511 -0.0336 -0.0393 -0.0336 923  TYR B CA  
4723 C C   . TYR B 673 ? 0.6726 0.6635 0.6493 -0.0435 -0.0380 -0.0380 923  TYR B C   
4724 O O   . TYR B 673 ? 0.6766 0.6833 0.6478 -0.0542 -0.0347 -0.0440 923  TYR B O   
4725 C CB  . TYR B 673 ? 0.6720 0.6735 0.6738 -0.0235 -0.0463 -0.0313 923  TYR B CB  
4726 C CG  . TYR B 673 ? 0.6425 0.6687 0.6476 -0.0244 -0.0483 -0.0386 923  TYR B CG  
4727 C CD1 . TYR B 673 ? 0.6405 0.6837 0.6461 -0.0281 -0.0457 -0.0430 923  TYR B CD1 
4728 C CD2 . TYR B 673 ? 0.6408 0.6755 0.6477 -0.0200 -0.0530 -0.0419 923  TYR B CD2 
4729 C CE1 . TYR B 673 ? 0.6359 0.7059 0.6451 -0.0270 -0.0480 -0.0498 923  TYR B CE1 
4730 C CE2 . TYR B 673 ? 0.6376 0.6987 0.6472 -0.0173 -0.0551 -0.0498 923  TYR B CE2 
4731 C CZ  . TYR B 673 ? 0.7592 0.8389 0.7707 -0.0206 -0.0526 -0.0534 923  TYR B CZ  
4732 O OH  . TYR B 673 ? 0.7843 0.8943 0.7992 -0.0160 -0.0552 -0.0613 923  TYR B OH  
4733 N N   . LYS B 674 ? 0.6748 0.6571 0.6500 -0.0412 -0.0406 -0.0347 924  LYS B N   
4734 C CA  . LYS B 674 ? 0.6823 0.6750 0.6485 -0.0510 -0.0392 -0.0382 924  LYS B CA  
4735 C C   . LYS B 674 ? 0.7326 0.7091 0.6793 -0.0680 -0.0341 -0.0374 924  LYS B C   
4736 O O   . LYS B 674 ? 0.7326 0.7268 0.6711 -0.0823 -0.0314 -0.0409 924  LYS B O   
4737 C CB  . LYS B 674 ? 0.7644 0.7515 0.7324 -0.0440 -0.0438 -0.0348 924  LYS B CB  
4738 C CG  . LYS B 674 ? 0.7190 0.7187 0.7018 -0.0293 -0.0513 -0.0366 924  LYS B CG  
4739 C CD  . LYS B 674 ? 0.9886 0.9828 0.9697 -0.0242 -0.0564 -0.0351 924  LYS B CD  
4740 C CE  . LYS B 674 ? 0.7881 0.7886 0.7796 -0.0102 -0.0661 -0.0381 924  LYS B CE  
4741 N NZ  . LYS B 674 ? 0.8789 0.8637 0.8803 -0.0042 -0.0717 -0.0301 924  LYS B NZ  
4742 N N   . ARG B 675 ? 0.7199 0.6633 0.6575 -0.0670 -0.0336 -0.0328 925  ARG B N   
4743 C CA  . ARG B 675 ? 0.7497 0.6686 0.6646 -0.0827 -0.0312 -0.0323 925  ARG B CA  
4744 C C   . ARG B 675 ? 0.8355 0.7630 0.7454 -0.0933 -0.0282 -0.0387 925  ARG B C   
4745 O O   . ARG B 675 ? 0.8331 0.7509 0.7238 -0.1126 -0.0272 -0.0397 925  ARG B O   
4746 C CB  . ARG B 675 ? 0.8122 0.6908 0.7169 -0.0742 -0.0331 -0.0270 925  ARG B CB  
4747 C CG  . ARG B 675 ? 0.9019 0.7731 0.8110 -0.0645 -0.0366 -0.0200 925  ARG B CG  
4748 C CD  . ARG B 675 ? 1.0277 0.8626 0.9263 -0.0545 -0.0390 -0.0148 925  ARG B CD  
4749 N NE  . ARG B 675 ? 0.8695 0.6712 0.7414 -0.0670 -0.0407 -0.0115 925  ARG B NE  
4750 C CZ  . ARG B 675 ? 1.1239 0.8906 0.9740 -0.0709 -0.0417 -0.0132 925  ARG B CZ  
4751 N NH1 . ARG B 675 ? 1.0729 0.8372 0.9259 -0.0617 -0.0399 -0.0194 925  ARG B NH1 
4752 N NH2 . ARG B 675 ? 1.2281 0.9603 1.0514 -0.0840 -0.0455 -0.0087 925  ARG B NH2 
4753 N N   . MET B 676 ? 0.7490 0.6947 0.6746 -0.0827 -0.0277 -0.0423 926  MET B N   
4754 C CA  . MET B 676 ? 0.7849 0.7448 0.7074 -0.0925 -0.0253 -0.0487 926  MET B CA  
4755 C C   . MET B 676 ? 0.8821 0.8818 0.8094 -0.1039 -0.0244 -0.0528 926  MET B C   
4756 O O   . MET B 676 ? 0.9488 0.9575 0.8648 -0.1221 -0.0225 -0.0565 926  MET B O   
4757 C CB  . MET B 676 ? 0.7345 0.7039 0.6716 -0.0776 -0.0255 -0.0501 926  MET B CB  
4758 C CG  . MET B 676 ? 0.7827 0.7689 0.7175 -0.0861 -0.0235 -0.0568 926  MET B CG  
4759 S SD  . MET B 676 ? 0.9417 0.9794 0.8938 -0.0869 -0.0246 -0.0608 926  MET B SD  
4760 C CE  . MET B 676 ? 0.6985 0.7432 0.6727 -0.0633 -0.0295 -0.0556 926  MET B CE  
4761 N N   . ILE B 677 ? 0.7922 0.8171 0.7352 -0.0929 -0.0264 -0.0528 927  ILE B N   
4762 C CA  . ILE B 677 ? 0.7955 0.8636 0.7439 -0.0986 -0.0258 -0.0581 927  ILE B CA  
4763 C C   . ILE B 677 ? 0.7788 0.8509 0.7100 -0.1208 -0.0230 -0.0569 927  ILE B C   
4764 O O   . ILE B 677 ? 0.9112 1.0165 0.8393 -0.1359 -0.0208 -0.0609 927  ILE B O   
4765 C CB  . ILE B 677 ? 0.7764 0.8628 0.7411 -0.0791 -0.0302 -0.0594 927  ILE B CB  
4766 C CG1 . ILE B 677 ? 0.7105 0.8030 0.6908 -0.0624 -0.0344 -0.0608 927  ILE B CG1 
4767 C CG2 . ILE B 677 ? 0.7008 0.8295 0.6668 -0.0829 -0.0295 -0.0654 927  ILE B CG2 
4768 C CD1 . ILE B 677 ? 0.9099 1.0348 0.8941 -0.0664 -0.0333 -0.0670 927  ILE B CD1 
4769 N N   . ALA B 678 ? 0.8077 0.8481 0.7268 -0.1243 -0.0237 -0.0504 928  ALA B N   
4770 C CA  . ALA B 678 ? 0.8342 0.8754 0.7346 -0.1471 -0.0222 -0.0468 928  ALA B CA  
4771 C C   . ALA B 678 ? 0.9191 0.9408 0.7985 -0.1712 -0.0214 -0.0457 928  ALA B C   
4772 O O   . ALA B 678 ? 1.1414 1.1729 1.0049 -0.1958 -0.0208 -0.0427 928  ALA B O   
4773 C CB  . ALA B 678 ? 0.8392 0.8473 0.7303 -0.1437 -0.0244 -0.0390 928  ALA B CB  
4774 N N   . THR B 679 ? 1.0070 1.0019 0.8844 -0.1656 -0.0222 -0.0481 929  THR B N   
4775 C CA  . THR B 679 ? 0.9535 0.9239 0.8087 -0.1863 -0.0231 -0.0490 929  THR B CA  
4776 C C   . THR B 679 ? 0.9857 0.9759 0.8512 -0.1820 -0.0217 -0.0569 929  THR B C   
4777 O O   . THR B 679 ? 1.0588 1.0169 0.9119 -0.1831 -0.0231 -0.0595 929  THR B O   
4778 C CB  . THR B 679 ? 1.1126 1.0188 0.9468 -0.1832 -0.0268 -0.0448 929  THR B CB  
4779 O OG1 . THR B 679 ? 0.9256 0.8197 0.7743 -0.1559 -0.0265 -0.0473 929  THR B OG1 
4780 C CG2 . THR B 679 ? 0.9736 0.8595 0.7972 -0.1865 -0.0290 -0.0360 929  THR B CG2 
4781 N N   . LYS B 680 ? 1.0310 1.0746 0.9181 -0.1758 -0.0197 -0.0612 930  LYS B N   
4782 C CA  . LYS B 680 ? 0.9447 1.0095 0.8435 -0.1687 -0.0192 -0.0676 930  LYS B CA  
4783 C C   . LYS B 680 ? 0.9870 1.0553 0.8689 -0.1942 -0.0193 -0.0711 930  LYS B C   
4784 O O   . LYS B 680 ? 1.0080 1.0677 0.8884 -0.1912 -0.0197 -0.0757 930  LYS B O   
4785 C CB  . LYS B 680 ? 0.9296 1.0480 0.8531 -0.1544 -0.0189 -0.0711 930  LYS B CB  
4786 C CG  . LYS B 680 ? 0.7442 0.8802 0.6822 -0.1407 -0.0200 -0.0756 930  LYS B CG  
4787 C CD  . LYS B 680 ? 0.8980 1.0777 0.8575 -0.1230 -0.0222 -0.0786 930  LYS B CD  
4788 C CE  . LYS B 680 ? 0.8508 1.0402 0.8235 -0.1072 -0.0251 -0.0806 930  LYS B CE  
4789 N NZ  . LYS B 680 ? 1.1053 1.3269 1.0956 -0.0869 -0.0299 -0.0830 930  LYS B NZ  
4790 N N   . ASP B 681 ? 1.0256 1.1074 0.8935 -0.2209 -0.0193 -0.0688 931  ASP B N   
4791 C CA  . ASP B 681 ? 1.1179 1.2039 0.9678 -0.2497 -0.0207 -0.0711 931  ASP B CA  
4792 C C   . ASP B 681 ? 1.0807 1.1003 0.9029 -0.2578 -0.0247 -0.0715 931  ASP B C   
4793 O O   . ASP B 681 ? 1.1204 1.1357 0.9265 -0.2784 -0.0273 -0.0753 931  ASP B O   
4794 C CB  . ASP B 681 ? 1.1864 1.3016 1.0255 -0.2793 -0.0206 -0.0662 931  ASP B CB  
4795 C CG  . ASP B 681 ? 1.2625 1.4496 1.1270 -0.2699 -0.0167 -0.0682 931  ASP B CG  
4796 O OD1 . ASP B 681 ? 1.2201 1.4440 1.1062 -0.2517 -0.0156 -0.0750 931  ASP B OD1 
4797 O OD2 . ASP B 681 ? 1.3950 1.6013 1.2565 -0.2797 -0.0154 -0.0632 931  ASP B OD2 
4798 N N   . SER B 682 ? 1.1462 1.1151 0.9617 -0.2412 -0.0261 -0.0683 932  SER B N   
4799 C CA  . SER B 682 ? 1.1465 1.0505 0.9346 -0.2430 -0.0308 -0.0700 932  SER B CA  
4800 C C   . SER B 682 ? 1.1799 1.0764 0.9765 -0.2200 -0.0296 -0.0780 932  SER B C   
4801 O O   . SER B 682 ? 1.2167 1.0626 0.9912 -0.2163 -0.0332 -0.0818 932  SER B O   
4802 C CB  . SER B 682 ? 1.1480 1.0039 0.9239 -0.2343 -0.0334 -0.0629 932  SER B CB  
4803 O OG  . SER B 682 ? 1.2297 1.0928 0.9962 -0.2563 -0.0347 -0.0544 932  SER B OG  
4804 N N   . PHE B 683 ? 1.1417 1.0865 0.9677 -0.2039 -0.0253 -0.0805 933  PHE B N   
4805 C CA  . PHE B 683 ? 1.0817 1.0263 0.9174 -0.1828 -0.0240 -0.0860 933  PHE B CA  
4806 C C   . PHE B 683 ? 1.0496 1.0297 0.8883 -0.1941 -0.0236 -0.0926 933  PHE B C   
4807 O O   . PHE B 683 ? 1.1701 1.1987 1.0226 -0.2039 -0.0226 -0.0918 933  PHE B O   
4808 C CB  . PHE B 683 ? 1.0154 0.9822 0.8804 -0.1553 -0.0212 -0.0818 933  PHE B CB  
4809 C CG  . PHE B 683 ? 1.0030 0.9362 0.8662 -0.1418 -0.0219 -0.0757 933  PHE B CG  
4810 C CD1 . PHE B 683 ? 0.9363 0.8792 0.8072 -0.1430 -0.0220 -0.0693 933  PHE B CD1 
4811 C CD2 . PHE B 683 ? 0.9116 0.8065 0.7647 -0.1268 -0.0227 -0.0769 933  PHE B CD2 
4812 C CE1 . PHE B 683 ? 0.8898 0.8033 0.7587 -0.1311 -0.0231 -0.0634 933  PHE B CE1 
4813 C CE2 . PHE B 683 ? 1.0378 0.9058 0.8898 -0.1135 -0.0238 -0.0711 933  PHE B CE2 
4814 C CZ  . PHE B 683 ? 1.0352 0.9117 0.8953 -0.1165 -0.0242 -0.0639 933  PHE B CZ  
4815 N N   . GLN B 684 ? 1.0445 1.0031 0.8701 -0.1914 -0.0248 -0.0996 934  GLN B N   
4816 C CA  . GLN B 684 ? 1.0842 1.0742 0.9110 -0.2013 -0.0251 -0.1063 934  GLN B CA  
4817 C C   . GLN B 684 ? 1.0259 1.0687 0.8853 -0.1829 -0.0221 -0.1043 934  GLN B C   
4818 O O   . GLN B 684 ? 0.9748 1.0142 0.8467 -0.1591 -0.0205 -0.1026 934  GLN B O   
4819 C CB  . GLN B 684 ? 1.1268 1.0789 0.9307 -0.1985 -0.0273 -0.1151 934  GLN B CB  
4820 C CG  . GLN B 684 ? 1.3601 1.2780 1.1288 -0.2276 -0.0332 -0.1209 934  GLN B CG  
4821 C CD  . GLN B 684 ? 1.4700 1.4303 1.2397 -0.2499 -0.0345 -0.1251 934  GLN B CD  
4822 O OE1 . GLN B 684 ? 1.3739 1.3911 1.1715 -0.2424 -0.0309 -0.1234 934  GLN B OE1 
4823 N NE2 . GLN B 684 ? 1.4909 1.4222 1.2286 -0.2774 -0.0409 -0.1305 934  GLN B NE2 
4824 N N   . SER B 685 ? 0.9865 1.0787 0.8585 -0.1939 -0.0221 -0.1040 935  SER B N   
4825 C CA  . SER B 685 ? 0.9843 1.1248 0.8833 -0.1773 -0.0216 -0.1029 935  SER B CA  
4826 C C   . SER B 685 ? 1.0098 1.1738 0.9060 -0.1842 -0.0229 -0.1091 935  SER B C   
4827 O O   . SER B 685 ? 0.9398 1.0898 0.8139 -0.2056 -0.0244 -0.1148 935  SER B O   
4828 C CB  . SER B 685 ? 0.8684 1.0526 0.7838 -0.1796 -0.0217 -0.1000 935  SER B CB  
4829 O OG  . SER B 685 ? 1.0829 1.2884 0.9863 -0.2077 -0.0221 -0.1026 935  SER B OG  
4830 N N   . PHE B 686 ? 0.8634 1.0607 0.7802 -0.1664 -0.0237 -0.1076 936  PHE B N   
4831 C CA  . PHE B 686 ? 0.9025 1.1266 0.8186 -0.1706 -0.0254 -0.1123 936  PHE B CA  
4832 C C   . PHE B 686 ? 0.8612 1.1314 0.8025 -0.1530 -0.0280 -0.1084 936  PHE B C   
4833 O O   . PHE B 686 ? 1.0188 1.2839 0.9749 -0.1323 -0.0290 -0.1020 936  PHE B O   
4834 C CB  . PHE B 686 ? 0.9370 1.1281 0.8392 -0.1643 -0.0245 -0.1157 936  PHE B CB  
4835 C CG  . PHE B 686 ? 0.8962 1.0750 0.8116 -0.1386 -0.0232 -0.1091 936  PHE B CG  
4836 C CD1 . PHE B 686 ? 0.8982 1.0384 0.8097 -0.1303 -0.0211 -0.1059 936  PHE B CD1 
4837 C CD2 . PHE B 686 ? 0.8581 1.0648 0.7886 -0.1242 -0.0249 -0.1051 936  PHE B CD2 
4838 C CE1 . PHE B 686 ? 0.9581 1.0919 0.8820 -0.1091 -0.0203 -0.0990 936  PHE B CE1 
4839 C CE2 . PHE B 686 ? 0.8012 0.9983 0.7425 -0.1045 -0.0247 -0.0973 936  PHE B CE2 
4840 C CZ  . PHE B 686 ? 0.8118 0.9744 0.7504 -0.0975 -0.0221 -0.0943 936  PHE B CZ  
4841 N N   . ASN B 687 ? 0.9426 1.2561 0.8871 -0.1618 -0.0305 -0.1121 937  ASN B N   
4842 C CA  . ASN B 687 ? 1.0294 1.3866 0.9948 -0.1446 -0.0349 -0.1092 937  ASN B CA  
4843 C C   . ASN B 687 ? 0.9017 1.2569 0.8677 -0.1338 -0.0371 -0.1073 937  ASN B C   
4844 O O   . ASN B 687 ? 0.9236 1.2584 0.8732 -0.1436 -0.0348 -0.1114 937  ASN B O   
4845 C CB  . ASN B 687 ? 0.9592 1.3709 0.9290 -0.1579 -0.0370 -0.1138 937  ASN B CB  
4846 C CG  . ASN B 687 ? 1.0255 1.4531 0.9997 -0.1638 -0.0353 -0.1140 937  ASN B CG  
4847 O OD1 . ASN B 687 ? 1.0185 1.4436 1.0054 -0.1444 -0.0362 -0.1105 937  ASN B OD1 
4848 N ND2 . ASN B 687 ? 1.0987 1.5431 1.0610 -0.1919 -0.0335 -0.1179 937  ASN B ND2 
4849 N N   . VAL B 688 ? 0.9593 1.3348 0.9425 -0.1130 -0.0424 -0.1011 938  VAL B N   
4850 C CA  . VAL B 688 ? 0.9032 1.2766 0.8881 -0.1014 -0.0454 -0.0958 938  VAL B CA  
4851 C C   . VAL B 688 ? 0.9811 1.3984 0.9783 -0.0913 -0.0535 -0.0934 938  VAL B C   
4852 O O   . VAL B 688 ? 1.1346 1.5712 1.1446 -0.0795 -0.0584 -0.0922 938  VAL B O   
4853 C CB  . VAL B 688 ? 0.8107 1.1502 0.8011 -0.0848 -0.0458 -0.0864 938  VAL B CB  
4854 C CG1 . VAL B 688 ? 0.7882 1.1334 0.7816 -0.0742 -0.0502 -0.0783 938  VAL B CG1 
4855 C CG2 . VAL B 688 ? 0.8378 1.1360 0.8151 -0.0922 -0.0383 -0.0890 938  VAL B CG2 
4856 N N   . THR B 689 ? 0.9513 1.3845 0.9435 -0.0943 -0.0554 -0.0934 939  THR B N   
4857 C CA  . THR B 689 ? 0.9043 1.3760 0.9062 -0.0832 -0.0643 -0.0897 939  THR B CA  
4858 C C   . THR B 689 ? 0.9435 1.4062 0.9419 -0.0759 -0.0674 -0.0811 939  THR B C   
4859 O O   . THR B 689 ? 0.9611 1.4069 0.9464 -0.0860 -0.0613 -0.0834 939  THR B O   
4860 C CB  . THR B 689 ? 0.8969 1.4131 0.8957 -0.0983 -0.0648 -0.0985 939  THR B CB  
4861 O OG1 . THR B 689 ? 0.9779 1.4791 0.9583 -0.1216 -0.0578 -0.1063 939  THR B OG1 
4862 C CG2 . THR B 689 ? 0.9383 1.4836 0.9468 -0.0990 -0.0655 -0.1035 939  THR B CG2 
4863 N N   . GLU B 690 ? 0.9071 1.3814 0.9157 -0.0581 -0.0776 -0.0713 940  GLU B N   
4864 C CA  . GLU B 690 ? 1.0083 1.4776 1.0145 -0.0508 -0.0831 -0.0596 940  GLU B CA  
4865 C C   . GLU B 690 ? 0.9604 1.3935 0.9599 -0.0540 -0.0760 -0.0546 940  GLU B C   
4866 O O   . GLU B 690 ? 0.9323 1.3664 0.9206 -0.0630 -0.0706 -0.0564 940  GLU B O   
4867 C CB  . GLU B 690 ? 0.9908 1.4935 0.9894 -0.0597 -0.0842 -0.0627 940  GLU B CB  
4868 C CG  . GLU B 690 ? 0.9669 1.5120 0.9735 -0.0532 -0.0933 -0.0650 940  GLU B CG  
4869 C CD  . GLU B 690 ? 1.2369 1.8121 1.2375 -0.0561 -0.0985 -0.0622 940  GLU B CD  
4870 O OE1 . GLU B 690 ? 1.2226 1.7879 1.2113 -0.0658 -0.0935 -0.0607 940  GLU B OE1 
4871 O OE2 . GLU B 690 ? 1.3724 1.9834 1.3797 -0.0473 -0.1079 -0.0617 940  GLU B OE2 
4872 N N   . PRO B 691 ? 0.9248 1.3285 0.9305 -0.0461 -0.0763 -0.0490 941  PRO B N   
4873 C CA  . PRO B 691 ? 0.9568 1.3319 0.9576 -0.0481 -0.0699 -0.0439 941  PRO B CA  
4874 C C   . PRO B 691 ? 1.0055 1.3808 1.0075 -0.0417 -0.0769 -0.0275 941  PRO B C   
4875 O O   . PRO B 691 ? 1.0502 1.4305 1.0581 -0.0323 -0.0892 -0.0172 941  PRO B O   
4876 C CB  . PRO B 691 ? 0.9665 1.3144 0.9742 -0.0430 -0.0687 -0.0440 941  PRO B CB  
4877 C CG  . PRO B 691 ? 1.0180 1.3773 1.0359 -0.0314 -0.0796 -0.0418 941  PRO B CG  
4878 C CD  . PRO B 691 ? 0.9177 1.3151 0.9343 -0.0347 -0.0822 -0.0485 941  PRO B CD  
4879 N N   . HIS B 692 ? 0.9782 1.3479 0.9725 -0.0468 -0.0695 -0.0252 942  HIS B N   
4880 C CA  . HIS B 692 ? 0.9080 1.2811 0.9023 -0.0443 -0.0744 -0.0084 942  HIS B CA  
4881 C C   . HIS B 692 ? 0.9352 1.2926 0.9272 -0.0456 -0.0651 -0.0070 942  HIS B C   
4882 O O   . HIS B 692 ? 0.9034 1.2614 0.8856 -0.0498 -0.0542 -0.0194 942  HIS B O   
4883 C CB  . HIS B 692 ? 0.9455 1.3490 0.9310 -0.0491 -0.0757 -0.0067 942  HIS B CB  
4884 C CG  . HIS B 692 ? 1.0651 1.4887 1.0530 -0.0465 -0.0855 -0.0075 942  HIS B CG  
4885 N ND1 . HIS B 692 ? 1.1439 1.5724 1.1355 -0.0392 -0.1001 0.0083  942  HIS B ND1 
4886 C CD2 . HIS B 692 ? 1.0734 1.5146 1.0595 -0.0503 -0.0838 -0.0218 942  HIS B CD2 
4887 C CE1 . HIS B 692 ? 1.1647 1.6140 1.1575 -0.0356 -0.1067 0.0029  942  HIS B CE1 
4888 N NE2 . HIS B 692 ? 1.1562 1.6169 1.1468 -0.0430 -0.0965 -0.0152 942  HIS B NE2 
4889 N N   . ILE B 693 ? 0.9542 1.2970 0.9539 -0.0416 -0.0704 0.0076  943  ILE B N   
4890 C CA  . ILE B 693 ? 0.9616 1.2925 0.9618 -0.0414 -0.0626 0.0097  943  ILE B CA  
4891 C C   . ILE B 693 ? 0.9241 1.2685 0.9258 -0.0436 -0.0677 0.0297  943  ILE B C   
4892 O O   . ILE B 693 ? 0.9614 1.3058 0.9663 -0.0445 -0.0809 0.0451  943  ILE B O   
4893 C CB  . ILE B 693 ? 0.9116 1.2125 0.9199 -0.0370 -0.0633 0.0077  943  ILE B CB  
4894 C CG1 . ILE B 693 ? 0.7839 1.0750 0.7921 -0.0359 -0.0545 0.0079  943  ILE B CG1 
4895 C CG2 . ILE B 693 ? 0.7849 1.0741 0.8017 -0.0332 -0.0781 0.0222  943  ILE B CG2 
4896 C CD1 . ILE B 693 ? 0.7916 1.0541 0.8057 -0.0323 -0.0539 0.0041  943  ILE B CD1 
4897 N N   . SER B 694 ? 0.9299 1.2866 0.9277 -0.0446 -0.0579 0.0296  944  SER B N   
4898 C CA  . SER B 694 ? 0.8108 1.1862 0.8107 -0.0486 -0.0606 0.0488  944  SER B CA  
4899 C C   . SER B 694 ? 0.8904 1.2565 0.8962 -0.0452 -0.0542 0.0496  944  SER B C   
4900 O O   . SER B 694 ? 0.9768 1.3168 0.9853 -0.0397 -0.0502 0.0376  944  SER B O   
4901 C CB  . SER B 694 ? 0.9449 1.3577 0.9345 -0.0518 -0.0547 0.0485  944  SER B CB  
4902 O OG  . SER B 694 ? 0.8724 1.2917 0.8546 -0.0458 -0.0403 0.0315  944  SER B OG  
4903 N N   . ALA B 695 ? 0.9272 1.3185 0.9348 -0.0491 -0.0535 0.0645  945  ALA B N   
4904 C CA  . ALA B 695 ? 0.8234 1.2154 0.8372 -0.0453 -0.0473 0.0661  945  ALA B CA  
4905 C C   . ALA B 695 ? 0.9535 1.3541 0.9593 -0.0343 -0.0319 0.0459  945  ALA B C   
4906 O O   . ALA B 695 ? 0.8139 1.2146 0.8238 -0.0276 -0.0262 0.0444  945  ALA B O   
4907 C CB  . ALA B 695 ? 1.0231 1.4459 1.0417 -0.0549 -0.0523 0.0901  945  ALA B CB  
4908 N N   . SER B 696 ? 0.9116 1.3177 0.9048 -0.0318 -0.0264 0.0302  946  SER B N   
4909 C CA  . SER B 696 ? 0.9302 1.3406 0.9111 -0.0208 -0.0139 0.0103  946  SER B CA  
4910 C C   . SER B 696 ? 0.9882 1.3734 0.9554 -0.0194 -0.0110 -0.0117 946  SER B C   
4911 O O   . SER B 696 ? 1.0162 1.3935 0.9696 -0.0103 -0.0027 -0.0297 946  SER B O   
4912 C CB  . SER B 696 ? 0.9228 1.3813 0.8968 -0.0192 -0.0084 0.0140  946  SER B CB  
4913 O OG  . SER B 696 ? 1.0639 1.5417 1.0334 -0.0292 -0.0137 0.0206  946  SER B OG  
4914 N N   . SER B 697 ? 1.0046 1.3772 0.9737 -0.0279 -0.0182 -0.0111 947  SER B N   
4915 C CA  . SER B 697 ? 0.8466 1.2022 0.8027 -0.0301 -0.0160 -0.0305 947  SER B CA  
4916 C C   . SER B 697 ? 0.8222 1.1593 0.7870 -0.0368 -0.0241 -0.0283 947  SER B C   
4917 O O   . SER B 697 ? 0.9198 1.2613 0.8978 -0.0389 -0.0330 -0.0122 947  SER B O   
4918 C CB  . SER B 697 ? 0.8913 1.2756 0.8341 -0.0334 -0.0143 -0.0362 947  SER B CB  
4919 O OG  . SER B 697 ? 0.9765 1.3869 0.9276 -0.0402 -0.0226 -0.0185 947  SER B OG  
4920 N N   . LEU B 698 ? 0.8539 1.1705 0.8097 -0.0401 -0.0218 -0.0450 948  LEU B N   
4921 C CA  . LEU B 698 ? 0.7450 1.0517 0.7073 -0.0462 -0.0280 -0.0461 948  LEU B CA  
4922 C C   . LEU B 698 ? 0.8970 1.2145 0.8469 -0.0549 -0.0277 -0.0592 948  LEU B C   
4923 O O   . LEU B 698 ? 0.9681 1.2757 0.9007 -0.0576 -0.0215 -0.0742 948  LEU B O   
4924 C CB  . LEU B 698 ? 0.9113 1.1850 0.8760 -0.0452 -0.0260 -0.0519 948  LEU B CB  
4925 C CG  . LEU B 698 ? 0.8155 1.0839 0.7866 -0.0509 -0.0313 -0.0543 948  LEU B CG  
4926 C CD1 . LEU B 698 ? 0.8365 1.1196 0.8233 -0.0467 -0.0413 -0.0396 948  LEU B CD1 
4927 C CD2 . LEU B 698 ? 0.6724 0.9102 0.6432 -0.0511 -0.0283 -0.0597 948  LEU B CD2 
4928 N N   . GLU B 699 ? 1.0063 1.3430 0.9639 -0.0587 -0.0354 -0.0538 949  GLU B N   
4929 C CA  . GLU B 699 ? 0.8763 1.2320 0.8244 -0.0676 -0.0367 -0.0636 949  GLU B CA  
4930 C C   . GLU B 699 ? 0.9064 1.2654 0.8636 -0.0717 -0.0424 -0.0656 949  GLU B C   
4931 O O   . GLU B 699 ? 0.9236 1.2883 0.8955 -0.0645 -0.0502 -0.0540 949  GLU B O   
4932 C CB  . GLU B 699 ? 0.8731 1.2615 0.8207 -0.0667 -0.0411 -0.0541 949  GLU B CB  
4933 C CG  . GLU B 699 ? 1.0066 1.4149 0.9387 -0.0754 -0.0397 -0.0662 949  GLU B CG  
4934 C CD  . GLU B 699 ? 1.2570 1.6990 1.1885 -0.0742 -0.0445 -0.0550 949  GLU B CD  
4935 O OE1 . GLU B 699 ? 1.2179 1.6802 1.1559 -0.0757 -0.0534 -0.0486 949  GLU B OE1 
4936 O OE2 . GLU B 699 ? 1.3569 1.8068 1.2808 -0.0711 -0.0397 -0.0521 949  GLU B OE2 
4937 N N   . TRP B 700 ? 0.8718 1.2278 0.8187 -0.0832 -0.0395 -0.0802 950  TRP B N   
4938 C CA  . TRP B 700 ? 0.9784 1.3463 0.9336 -0.0883 -0.0439 -0.0829 950  TRP B CA  
4939 C C   . TRP B 700 ? 0.9660 1.3453 0.9065 -0.1056 -0.0422 -0.0972 950  TRP B C   
4940 O O   . TRP B 700 ? 0.9503 1.3202 0.8725 -0.1128 -0.0381 -0.1059 950  TRP B O   
4941 C CB  . TRP B 700 ? 0.9940 1.3363 0.9567 -0.0855 -0.0422 -0.0824 950  TRP B CB  
4942 C CG  . TRP B 700 ? 0.9084 1.2218 0.8558 -0.0972 -0.0352 -0.0942 950  TRP B CG  
4943 C CD1 . TRP B 700 ? 0.9014 1.2159 0.8424 -0.1124 -0.0346 -0.1032 950  TRP B CD1 
4944 C CD2 . TRP B 700 ? 0.8805 1.1592 0.8156 -0.0946 -0.0291 -0.0973 950  TRP B CD2 
4945 N NE1 . TRP B 700 ? 0.8563 1.1332 0.7798 -0.1208 -0.0295 -0.1110 950  TRP B NE1 
4946 C CE2 . TRP B 700 ? 0.9193 1.1729 0.8388 -0.1081 -0.0261 -0.1084 950  TRP B CE2 
4947 C CE3 . TRP B 700 ? 0.8639 1.1326 0.7989 -0.0820 -0.0263 -0.0915 950  TRP B CE3 
4948 C CZ2 . TRP B 700 ? 0.8057 1.0195 0.7086 -0.1069 -0.0216 -0.1145 950  TRP B CZ2 
4949 C CZ3 . TRP B 700 ? 0.8038 1.0399 0.7246 -0.0797 -0.0205 -0.0985 950  TRP B CZ3 
4950 C CH2 . TRP B 700 ? 0.7850 0.9914 0.6893 -0.0908 -0.0187 -0.1102 950  TRP B CH2 
4951 N N   . ILE B 701 ? 0.9528 1.3544 0.9008 -0.1121 -0.0460 -0.0998 951  ILE B N   
4952 C CA  . ILE B 701 ? 0.9265 1.3452 0.8625 -0.1320 -0.0459 -0.1116 951  ILE B CA  
4953 C C   . ILE B 701 ? 1.0018 1.4099 0.9381 -0.1430 -0.0438 -0.1164 951  ILE B C   
4954 O O   . ILE B 701 ? 1.0170 1.4418 0.9704 -0.1352 -0.0465 -0.1112 951  ILE B O   
4955 C CB  . ILE B 701 ? 0.9867 1.4558 0.9316 -0.1319 -0.0531 -0.1095 951  ILE B CB  
4956 C CG1 . ILE B 701 ? 1.0303 1.5100 0.9750 -0.1205 -0.0563 -0.1018 951  ILE B CG1 
4957 C CG2 . ILE B 701 ? 0.8996 1.3891 0.8311 -0.1554 -0.0533 -0.1215 951  ILE B CG2 
4958 C CD1 . ILE B 701 ? 0.8907 1.4179 0.8425 -0.1188 -0.0647 -0.0987 951  ILE B CD1 
4959 N N   . ASP B 702 ? 1.0126 1.3921 0.9281 -0.1608 -0.0398 -0.1262 952  ASP B N   
4960 C CA  . ASP B 702 ? 1.0098 1.3791 0.9216 -0.1760 -0.0384 -0.1296 952  ASP B CA  
4961 C C   . ASP B 702 ? 1.0660 1.4839 0.9816 -0.1932 -0.0423 -0.1330 952  ASP B C   
4962 O O   . ASP B 702 ? 1.1648 1.5997 1.0686 -0.2072 -0.0448 -0.1393 952  ASP B O   
4963 C CB  . ASP B 702 ? 1.1120 1.4303 0.9965 -0.1907 -0.0352 -0.1381 952  ASP B CB  
4964 C CG  . ASP B 702 ? 1.1489 1.4531 1.0263 -0.2095 -0.0349 -0.1397 952  ASP B CG  
4965 O OD1 . ASP B 702 ? 1.1591 1.4920 1.0323 -0.2319 -0.0377 -0.1432 952  ASP B OD1 
4966 O OD2 . ASP B 702 ? 1.3196 1.5867 1.1954 -0.2029 -0.0320 -0.1367 952  ASP B OD2 
4967 N N   . PRO B 703 ? 1.1014 1.5461 1.0330 -0.1922 -0.0432 -0.1295 953  PRO B N   
4968 C CA  . PRO B 703 ? 1.0761 1.5777 1.0139 -0.2064 -0.0468 -0.1324 953  PRO B CA  
4969 C C   . PRO B 703 ? 1.1358 1.6373 1.0612 -0.2355 -0.0451 -0.1367 953  PRO B C   
4970 O O   . PRO B 703 ? 1.1917 1.7464 1.1247 -0.2480 -0.0473 -0.1378 953  PRO B O   
4971 C CB  . PRO B 703 ? 0.9369 1.4745 0.9015 -0.1808 -0.0499 -0.1258 953  PRO B CB  
4972 C CG  . PRO B 703 ? 0.9596 1.4497 0.9289 -0.1607 -0.0472 -0.1195 953  PRO B CG  
4973 C CD  . PRO B 703 ? 1.0314 1.4655 0.9794 -0.1729 -0.0419 -0.1223 953  PRO B CD  
4974 N N   . ASP B 704 ? 1.1969 1.6409 1.1023 -0.2469 -0.0418 -0.1385 954  ASP B N   
4975 C CA  . ASP B 704 ? 1.1559 1.5903 1.0468 -0.2751 -0.0412 -0.1399 954  ASP B CA  
4976 C C   . ASP B 704 ? 1.1913 1.5917 1.0495 -0.3054 -0.0441 -0.1473 954  ASP B C   
4977 O O   . ASP B 704 ? 1.2865 1.6559 1.1250 -0.3290 -0.0448 -0.1475 954  ASP B O   
4978 C CB  . ASP B 704 ? 1.2993 1.6912 1.1909 -0.2653 -0.0372 -0.1349 954  ASP B CB  
4979 C CG  . ASP B 704 ? 1.2376 1.6699 1.1557 -0.2487 -0.0358 -0.1291 954  ASP B CG  
4980 O OD1 . ASP B 704 ? 1.1167 1.6079 1.0533 -0.2405 -0.0383 -0.1293 954  ASP B OD1 
4981 O OD2 . ASP B 704 ? 1.1893 1.5939 1.1083 -0.2428 -0.0330 -0.1251 954  ASP B OD2 
4982 N N   . SER B 705 ? 1.2532 1.6563 1.1027 -0.3055 -0.0468 -0.1533 955  SER B N   
4983 C CA  . SER B 705 ? 1.3557 1.7234 1.1710 -0.3324 -0.0511 -0.1624 955  SER B CA  
4984 C C   . SER B 705 ? 1.4341 1.7212 1.2235 -0.3318 -0.0502 -0.1655 955  SER B C   
4985 O O   . SER B 705 ? 1.3639 1.6098 1.1206 -0.3578 -0.0553 -0.1720 955  SER B O   
4986 C CB  . SER B 705 ? 1.2631 1.6640 1.0684 -0.3711 -0.0561 -0.1635 955  SER B CB  
4987 O OG  . SER B 705 ? 1.5369 1.8863 1.3035 -0.4000 -0.0619 -0.1713 955  SER B OG  
4988 N N   . SER B 706 ? 1.3497 1.6130 1.1524 -0.3020 -0.0449 -0.1606 956  SER B N   
4989 C CA  . SER B 706 ? 1.3838 1.5751 1.1644 -0.2968 -0.0441 -0.1632 956  SER B CA  
4990 C C   . SER B 706 ? 1.4740 1.6264 1.2294 -0.2909 -0.0461 -0.1744 956  SER B C   
4991 O O   . SER B 706 ? 1.5756 1.6651 1.3025 -0.2933 -0.0484 -0.1804 956  SER B O   
4992 C CB  . SER B 706 ? 1.4852 1.6690 1.2888 -0.2666 -0.0382 -0.1546 956  SER B CB  
4993 O OG  . SER B 706 ? 1.5277 1.7424 1.3509 -0.2708 -0.0368 -0.1460 956  SER B OG  
4994 N N   . LEU B 707 ? 1.5440 1.7325 1.3078 -0.2820 -0.0459 -0.1776 957  LEU B N   
4995 C CA  . LEU B 707 ? 1.5547 1.7160 1.2959 -0.2743 -0.0472 -0.1889 957  LEU B CA  
4996 C C   . LEU B 707 ? 1.5554 1.7308 1.2757 -0.3023 -0.0542 -0.1985 957  LEU B C   
4997 O O   . LEU B 707 ? 1.5552 1.7836 1.2899 -0.3194 -0.0564 -0.1941 957  LEU B O   
4998 C CB  . LEU B 707 ? 1.5673 1.7592 1.3316 -0.2434 -0.0419 -0.1846 957  LEU B CB  
4999 C CG  . LEU B 707 ? 1.4718 1.6525 1.2554 -0.2133 -0.0357 -0.1756 957  LEU B CG  
5000 C CD1 . LEU B 707 ? 1.4502 1.5699 1.2089 -0.2029 -0.0344 -0.1837 957  LEU B CD1 
5001 C CD2 . LEU B 707 ? 1.4572 1.6520 1.2661 -0.2114 -0.0339 -0.1633 957  LEU B CD2 
5002 N N   . ARG B 708 ? 1.3644 2.1355 1.1928 -0.1318 -0.1835 -0.1219 958  ARG B N   
5003 C CA  . ARG B 708 ? 1.2997 2.0091 1.1509 -0.1343 -0.1551 -0.0890 958  ARG B CA  
5004 C C   . ARG B 708 ? 1.2348 1.9142 1.1387 -0.1492 -0.1595 -0.0782 958  ARG B C   
5005 O O   . ARG B 708 ? 1.1352 1.8474 1.0497 -0.1440 -0.1748 -0.0651 958  ARG B O   
5006 C CB  . ARG B 708 ? 1.1801 1.8982 1.0021 -0.1075 -0.1322 -0.0381 958  ARG B CB  
5007 C CG  . ARG B 708 ? 1.2279 1.8895 1.0856 -0.1113 -0.1057 -0.0035 958  ARG B CG  
5008 C CD  . ARG B 708 ? 1.2659 1.9284 1.0999 -0.0882 -0.0760 0.0404  958  ARG B CD  
5009 N NE  . ARG B 708 ? 1.1478 1.8106 0.9500 -0.0839 -0.0609 0.0257  958  ARG B NE  
5010 C CZ  . ARG B 708 ? 1.2100 1.8288 1.0341 -0.0976 -0.0435 0.0124  958  ARG B CZ  
5011 N NH1 . ARG B 708 ? 1.2625 1.8865 1.0577 -0.0914 -0.0290 0.0000  958  ARG B NH1 
5012 N NH2 . ARG B 708 ? 1.2990 1.8720 1.1731 -0.1158 -0.0409 0.0111  958  ARG B NH2 
5013 N N   . ASP B 709 ? 1.3611 1.9817 1.2966 -0.1655 -0.1460 -0.0835 959  ASP B N   
5014 C CA  . ASP B 709 ? 1.2556 1.8431 1.2370 -0.1790 -0.1473 -0.0760 959  ASP B CA  
5015 C C   . ASP B 709 ? 1.2486 1.7963 1.2444 -0.1732 -0.1238 -0.0394 959  ASP B C   
5016 O O   . ASP B 709 ? 1.2822 1.8162 1.2627 -0.1655 -0.1048 -0.0285 959  ASP B O   
5017 C CB  . ASP B 709 ? 1.2907 1.8442 1.2982 -0.2014 -0.1519 -0.1144 959  ASP B CB  
5018 C CG  . ASP B 709 ? 1.3501 1.9356 1.3458 -0.2095 -0.1696 -0.1584 959  ASP B CG  
5019 O OD1 . ASP B 709 ? 1.3382 1.9756 1.3293 -0.2065 -0.1895 -0.1650 959  ASP B OD1 
5020 O OD2 . ASP B 709 ? 1.3634 1.9243 1.3565 -0.2180 -0.1637 -0.1879 959  ASP B OD2 
5021 N N   . HIS B 710 ? 1.0526 1.5831 1.0814 -0.1777 -0.1243 -0.0230 960  HIS B N   
5022 C CA  . HIS B 710 ? 0.9922 1.4841 1.0417 -0.1752 -0.1041 0.0045  960  HIS B CA  
5023 C C   . HIS B 710 ? 1.0002 1.4535 1.0831 -0.1913 -0.1065 -0.0098 960  HIS B C   
5024 O O   . HIS B 710 ? 0.9654 1.4262 1.0666 -0.1974 -0.1187 -0.0133 960  HIS B O   
5025 C CB  . HIS B 710 ? 1.0091 1.5190 1.0626 -0.1593 -0.0983 0.0438  960  HIS B CB  
5026 C CG  . HIS B 710 ? 1.0519 1.5244 1.1264 -0.1557 -0.0738 0.0700  960  HIS B CG  
5027 N ND1 . HIS B 710 ? 1.2316 1.7115 1.3085 -0.1388 -0.0585 0.1084  960  HIS B ND1 
5028 C CD2 . HIS B 710 ? 1.0698 1.4989 1.1668 -0.1665 -0.0618 0.0613  960  HIS B CD2 
5029 C CE1 . HIS B 710 ? 1.1471 1.5870 1.2507 -0.1422 -0.0369 0.1193  960  HIS B CE1 
5030 N NE2 . HIS B 710 ? 1.1032 1.5153 1.2186 -0.1588 -0.0404 0.0897  960  HIS B NE2 
5031 N N   . ILE B 711 ? 0.8679 1.2830 0.9589 -0.1965 -0.0942 -0.0173 961  ILE B N   
5032 C CA  . ILE B 711 ? 0.8723 1.2523 0.9862 -0.2080 -0.0960 -0.0322 961  ILE B CA  
5033 C C   . ILE B 711 ? 0.8905 1.2412 1.0232 -0.2051 -0.0818 -0.0160 961  ILE B C   
5034 O O   . ILE B 711 ? 0.9337 1.2815 1.0646 -0.1991 -0.0680 -0.0054 961  ILE B O   
5035 C CB  . ILE B 711 ? 0.9444 1.3097 1.0507 -0.2150 -0.0977 -0.0623 961  ILE B CB  
5036 C CG1 . ILE B 711 ? 0.9952 1.3915 1.0840 -0.2186 -0.1108 -0.0840 961  ILE B CG1 
5037 C CG2 . ILE B 711 ? 0.9032 1.2334 1.0305 -0.2229 -0.0982 -0.0731 961  ILE B CG2 
5038 C CD1 . ILE B 711 ? 1.0700 1.4490 1.1554 -0.2259 -0.1107 -0.1160 961  ILE B CD1 
5039 N N   . ASN B 712 ? 0.8442 1.1745 0.9967 -0.2096 -0.0839 -0.0156 962  ASN B N   
5040 C CA  . ASN B 712 ? 0.7616 1.0657 0.9316 -0.2074 -0.0733 -0.0075 962  ASN B CA  
5041 C C   . ASN B 712 ? 0.7064 0.9843 0.8814 -0.2116 -0.0768 -0.0252 962  ASN B C   
5042 O O   . ASN B 712 ? 0.8158 1.0903 0.9920 -0.2165 -0.0841 -0.0322 962  ASN B O   
5043 C CB  . ASN B 712 ? 0.8503 1.1570 1.0360 -0.2035 -0.0700 0.0138  962  ASN B CB  
5044 C CG  . ASN B 712 ? 0.8187 1.1032 1.0228 -0.2005 -0.0564 0.0206  962  ASN B CG  
5045 O OD1 . ASN B 712 ? 0.8827 1.1465 1.0956 -0.2024 -0.0570 0.0108  962  ASN B OD1 
5046 N ND2 . ASN B 712 ? 0.9083 1.1976 1.1190 -0.1952 -0.0427 0.0367  962  ASN B ND2 
5047 N N   . VAL B 713 ? 0.6097 0.8711 0.7897 -0.2087 -0.0705 -0.0318 963  VAL B N   
5048 C CA  . VAL B 713 ? 0.6582 0.8983 0.8384 -0.2074 -0.0735 -0.0461 963  VAL B CA  
5049 C C   . VAL B 713 ? 0.6188 0.8473 0.8120 -0.2021 -0.0692 -0.0442 963  VAL B C   
5050 O O   . VAL B 713 ? 0.6963 0.9302 0.9017 -0.2013 -0.0623 -0.0432 963  VAL B O   
5051 C CB  . VAL B 713 ? 0.6999 0.9385 0.8716 -0.2060 -0.0737 -0.0624 963  VAL B CB  
5052 C CG1 . VAL B 713 ? 0.6884 0.9058 0.8601 -0.1999 -0.0758 -0.0727 963  VAL B CG1 
5053 C CG2 . VAL B 713 ? 0.6729 0.9237 0.8310 -0.2114 -0.0777 -0.0697 963  VAL B CG2 
5054 N N   . ILE B 714 ? 0.7484 0.9619 0.9403 -0.1985 -0.0718 -0.0451 964  ILE B N   
5055 C CA  . ILE B 714 ? 0.7227 0.9280 0.9217 -0.1916 -0.0698 -0.0478 964  ILE B CA  
5056 C C   . ILE B 714 ? 0.5923 0.7852 0.7785 -0.1818 -0.0744 -0.0577 964  ILE B C   
5057 O O   . ILE B 714 ? 0.7713 0.9518 0.9474 -0.1801 -0.0744 -0.0526 964  ILE B O   
5058 C CB  . ILE B 714 ? 0.7153 0.9168 0.9209 -0.1917 -0.0657 -0.0351 964  ILE B CB  
5059 C CG1 . ILE B 714 ? 0.6879 0.9017 0.9077 -0.1969 -0.0594 -0.0218 964  ILE B CG1 
5060 C CG2 . ILE B 714 ? 0.6071 0.8002 0.8150 -0.1833 -0.0643 -0.0432 964  ILE B CG2 
5061 C CD1 . ILE B 714 ? 0.6377 0.8530 0.8751 -0.1968 -0.0513 -0.0264 964  ILE B CD1 
5062 N N   . VAL B 715 ? 0.6420 0.8399 0.8316 -0.1744 -0.0773 -0.0709 965  VAL B N   
5063 C CA  . VAL B 715 ? 0.6597 0.8513 0.8358 -0.1595 -0.0827 -0.0783 965  VAL B CA  
5064 C C   . VAL B 715 ? 0.7159 0.9117 0.8928 -0.1509 -0.0849 -0.0841 965  VAL B C   
5065 O O   . VAL B 715 ? 0.6591 0.8688 0.8556 -0.1546 -0.0857 -0.0966 965  VAL B O   
5066 C CB  . VAL B 715 ? 0.6980 0.8998 0.8778 -0.1540 -0.0870 -0.0917 965  VAL B CB  
5067 C CG1 . VAL B 715 ? 0.5924 0.7908 0.7567 -0.1337 -0.0929 -0.0958 965  VAL B CG1 
5068 C CG2 . VAL B 715 ? 0.6238 0.8215 0.8013 -0.1624 -0.0833 -0.0893 965  VAL B CG2 
5069 N N   . GLY B 716 ? 0.7286 0.9120 0.8858 -0.1396 -0.0839 -0.0764 966  GLY B N   
5070 C CA  . GLY B 716 ? 0.5992 0.7875 0.7513 -0.1299 -0.0854 -0.0833 966  GLY B CA  
5071 C C   . GLY B 716 ? 0.6806 0.8900 0.8343 -0.1178 -0.0968 -0.1057 966  GLY B C   
5072 O O   . GLY B 716 ? 0.7734 0.9897 0.9210 -0.1081 -0.1034 -0.1099 966  GLY B O   
5073 N N   . ARG B 717 ? 0.7141 0.9359 0.8797 -0.1182 -0.0990 -0.1224 967  ARG B N   
5074 C CA  . ARG B 717 ? 0.6648 0.9143 0.8403 -0.1095 -0.1118 -0.1504 967  ARG B CA  
5075 C C   . ARG B 717 ? 0.7343 0.9935 0.8735 -0.0818 -0.1225 -0.1526 967  ARG B C   
5076 O O   . ARG B 717 ? 0.7934 1.0770 0.9338 -0.0692 -0.1356 -0.1674 967  ARG B O   
5077 C CB  . ARG B 717 ? 0.6920 0.9507 0.8944 -0.1190 -0.1096 -0.1717 967  ARG B CB  
5078 C CG  . ARG B 717 ? 0.9652 1.2577 1.1829 -0.1113 -0.1243 -0.2078 967  ARG B CG  
5079 C CD  . ARG B 717 ? 0.8365 1.1353 1.0395 -0.1006 -0.1277 -0.2253 967  ARG B CD  
5080 N NE  . ARG B 717 ? 1.0500 1.3261 1.2716 -0.1165 -0.1108 -0.2205 967  ARG B NE  
5081 C CZ  . ARG B 717 ? 0.9099 1.1789 1.1142 -0.1087 -0.1065 -0.2251 967  ARG B CZ  
5082 N NH1 . ARG B 717 ? 0.7098 0.9937 0.8732 -0.0846 -0.1178 -0.2341 967  ARG B NH1 
5083 N NH2 . ARG B 717 ? 0.9440 1.1917 1.1703 -0.1225 -0.0895 -0.2191 967  ARG B NH2 
5084 N N   . ASP B 718 ? 0.8112 1.0535 0.9182 -0.0699 -0.1160 -0.1362 968  ASP B N   
5085 C CA  . ASP B 718 ? 0.8496 1.1004 0.9164 -0.0394 -0.1226 -0.1336 968  ASP B CA  
5086 C C   . ASP B 718 ? 0.8340 1.0636 0.8804 -0.0282 -0.1157 -0.1057 968  ASP B C   
5087 O O   . ASP B 718 ? 0.9821 1.1859 1.0057 -0.0209 -0.1016 -0.0807 968  ASP B O   
5088 C CB  . ASP B 718 ? 0.9435 1.1876 0.9855 -0.0298 -0.1153 -0.1305 968  ASP B CB  
5089 C CG  . ASP B 718 ? 0.9515 1.2242 1.0036 -0.0288 -0.1264 -0.1663 968  ASP B CG  
5090 O OD1 . ASP B 718 ? 1.1143 1.3783 1.1919 -0.0480 -0.1179 -0.1747 968  ASP B OD1 
5091 O OD2 . ASP B 718 ? 1.0982 1.4036 1.1349 -0.0079 -0.1435 -0.1874 968  ASP B OD2 
5092 N N   . LEU B 719 ? 0.9261 1.1664 0.9858 -0.0271 -0.1236 -0.1115 969  LEU B N   
5093 C CA  . LEU B 719 ? 0.7689 0.9900 0.8128 -0.0135 -0.1170 -0.0896 969  LEU B CA  
5094 C C   . LEU B 719 ? 0.8366 1.0677 0.8416 0.0243  -0.1216 -0.0814 969  LEU B C   
5095 O O   . LEU B 719 ? 1.0427 1.3098 1.0378 0.0410  -0.1380 -0.1015 969  LEU B O   
5096 C CB  . LEU B 719 ? 0.7225 0.9531 0.7931 -0.0218 -0.1227 -0.0997 969  LEU B CB  
5097 C CG  . LEU B 719 ? 0.6648 0.8839 0.7663 -0.0543 -0.1154 -0.1018 969  LEU B CG  
5098 C CD1 . LEU B 719 ? 0.7171 0.9586 0.8456 -0.0594 -0.1230 -0.1194 969  LEU B CD1 
5099 C CD2 . LEU B 719 ? 0.6915 0.8744 0.7863 -0.0623 -0.1000 -0.0794 969  LEU B CD2 
5100 N N   . SER B 720 ? 0.9402 1.1401 0.9240 0.0388  -0.1059 -0.0517 970  SER B N   
5101 C CA  . SER B 720 ? 0.9412 1.1456 0.8851 0.0793  -0.1053 -0.0351 970  SER B CA  
5102 C C   . SER B 720 ? 0.9429 1.1653 0.8940 0.0965  -0.1166 -0.0400 970  SER B C   
5103 O O   . SER B 720 ? 1.0830 1.2777 1.0317 0.1074  -0.1029 -0.0178 970  SER B O   
5104 C CB  . SER B 720 ? 0.9255 1.0844 0.8495 0.0872  -0.0779 0.0018  970  SER B CB  
5105 O OG  . SER B 720 ? 0.9675 1.1138 0.8896 0.0714  -0.0671 0.0058  970  SER B OG  
5106 N N   . PHE B 721 ? 0.9759 1.2462 0.9408 0.0989  -0.1408 -0.0714 971  PHE B N   
5107 C CA  . PHE B 721 ? 0.9823 1.2775 0.9639 0.1121  -0.1532 -0.0807 971  PHE B CA  
5108 C C   . PHE B 721 ? 1.1324 1.4280 1.0776 0.1577  -0.1509 -0.0552 971  PHE B C   
5109 O O   . PHE B 721 ? 1.0612 1.3479 1.0171 0.1688  -0.1463 -0.0447 971  PHE B O   
5110 C CB  . PHE B 721 ? 0.8118 1.1639 0.8188 0.1075  -0.1792 -0.1209 971  PHE B CB  
5111 C CG  . PHE B 721 ? 0.8583 1.2087 0.9098 0.0647  -0.1777 -0.1431 971  PHE B CG  
5112 C CD1 . PHE B 721 ? 0.8545 1.2040 0.9095 0.0456  -0.1769 -0.1556 971  PHE B CD1 
5113 C CD2 . PHE B 721 ? 0.7947 1.1441 0.8840 0.0462  -0.1750 -0.1497 971  PHE B CD2 
5114 C CE1 . PHE B 721 ? 0.8508 1.1967 0.9469 0.0098  -0.1726 -0.1713 971  PHE B CE1 
5115 C CE2 . PHE B 721 ? 0.7833 1.1312 0.9101 0.0105  -0.1708 -0.1654 971  PHE B CE2 
5116 C CZ  . PHE B 721 ? 0.8509 1.1963 0.9814 -0.0071 -0.1692 -0.1747 971  PHE B CZ  
5117 N N   . GLN B 722 ? 1.0974 1.4026 0.9980 0.1869  -0.1521 -0.0436 972  GLN B N   
5118 C CA  . GLN B 722 ? 1.1093 1.4193 0.9701 0.2363  -0.1495 -0.0157 972  GLN B CA  
5119 C C   . GLN B 722 ? 1.1774 1.4239 1.0337 0.2404  -0.1164 0.0261  972  GLN B C   
5120 O O   . GLN B 722 ? 1.2190 1.4592 1.0715 0.2688  -0.1108 0.0454  972  GLN B O   
5121 C CB  . GLN B 722 ? 1.2479 1.5832 1.0568 0.2672  -0.1561 -0.0120 972  GLN B CB  
5122 C CG  . GLN B 722 ? 1.2551 1.6434 1.0301 0.3196  -0.1770 -0.0112 972  GLN B CG  
5123 C CD  . GLN B 722 ? 1.4171 1.7738 1.1635 0.3599  -0.1552 0.0379  972  GLN B CD  
5124 O OE1 . GLN B 722 ? 1.5344 1.8421 1.2514 0.3694  -0.1248 0.0763  972  GLN B OE1 
5125 N NE2 . GLN B 722 ? 1.3132 1.6968 1.0722 0.3843  -0.1680 0.0378  972  GLN B NE2 
5126 N N   . ASP B 723 ? 1.1281 1.3277 0.9895 0.2124  -0.0932 0.0392  973  ASP B N   
5127 C CA  . ASP B 723 ? 1.1999 1.3390 1.0661 0.2110  -0.0603 0.0736  973  ASP B CA  
5128 C C   . ASP B 723 ? 1.1926 1.3101 1.1056 0.1811  -0.0560 0.0619  973  ASP B C   
5129 O O   . ASP B 723 ? 1.2721 1.3459 1.1936 0.1865  -0.0321 0.0846  973  ASP B O   
5130 C CB  . ASP B 723 ? 1.1526 1.2559 1.0126 0.1917  -0.0377 0.0891  973  ASP B CB  
5131 C CG  . ASP B 723 ? 1.2386 1.2817 1.1041 0.1948  -0.0007 0.1258  973  ASP B CG  
5132 O OD1 . ASP B 723 ? 1.3195 1.3487 1.1518 0.2355  0.0162  0.1596  973  ASP B OD1 
5133 O OD2 . ASP B 723 ? 1.0895 1.1002 0.9938 0.1574  0.0122  0.1205  973  ASP B OD2 
5134 N N   . LEU B 724 ? 1.1853 1.3311 1.1288 0.1508  -0.0763 0.0269  974  LEU B N   
5135 C CA  . LEU B 724 ? 1.1671 1.2978 1.1499 0.1239  -0.0727 0.0139  974  LEU B CA  
5136 C C   . LEU B 724 ? 1.2135 1.3707 1.2077 0.1452  -0.0850 0.0046  974  LEU B C   
5137 O O   . LEU B 724 ? 1.1174 1.2596 1.1404 0.1292  -0.0786 -0.0037 974  LEU B O   
5138 C CB  . LEU B 724 ? 0.9205 1.0659 0.9304 0.0816  -0.0835 -0.0143 974  LEU B CB  
5139 C CG  . LEU B 724 ? 0.8962 1.0136 0.9073 0.0543  -0.0700 -0.0069 974  LEU B CG  
5140 C CD1 . LEU B 724 ? 0.8038 0.9426 0.8390 0.0202  -0.0824 -0.0323 974  LEU B CD1 
5141 C CD2 . LEU B 724 ? 0.9512 1.0195 0.9753 0.0423  -0.0453 0.0098  974  LEU B CD2 
5142 N N   . SER B 725 ? 1.1685 1.3680 1.1410 0.1818  -0.1028 0.0043  975  SER B N   
5143 C CA  . SER B 725 ? 1.1613 1.3947 1.1475 0.2056  -0.1166 -0.0048 975  SER B CA  
5144 C C   . SER B 725 ? 1.2124 1.4429 1.1661 0.2585  -0.1099 0.0276  975  SER B C   
5145 O O   . SER B 725 ? 1.1962 1.4731 1.1508 0.2896  -0.1287 0.0209  975  SER B O   
5146 C CB  . SER B 725 ? 1.0703 1.3716 1.0715 0.2017  -0.1488 -0.0415 975  SER B CB  
5147 O OG  . SER B 725 ? 1.2521 1.5852 1.2180 0.2243  -0.1634 -0.0422 975  SER B OG  
5148 N N   . GLU B 726 ? 1.3247 1.5034 1.2524 0.2708  -0.0822 0.0639  976  GLU B N   
5149 C CA  . GLU B 726 ? 1.4117 1.5810 1.3062 0.3240  -0.0697 0.1020  976  GLU B CA  
5150 C C   . GLU B 726 ? 1.4412 1.6032 1.3607 0.3428  -0.0637 0.1079  976  GLU B C   
5151 O O   . GLU B 726 ? 1.4848 1.6977 1.3997 0.3779  -0.0848 0.1036  976  GLU B O   
5152 C CB  . GLU B 726 ? 1.4563 1.5618 1.3292 0.3271  -0.0332 0.1409  976  GLU B CB  
5153 C CG  . GLU B 726 ? 1.5292 1.6483 1.3622 0.3316  -0.0365 0.1472  976  GLU B CG  
5154 C CD  . GLU B 726 ? 1.6645 1.8331 1.4465 0.3871  -0.0533 0.1605  976  GLU B CD  
5155 O OE1 . GLU B 726 ? 1.7532 1.9300 1.4942 0.3999  -0.0514 0.1709  976  GLU B OE1 
5156 O OE2 . GLU B 726 ? 1.5761 1.7786 1.3585 0.4197  -0.0686 0.1599  976  GLU B OE2 
5157 N N   . THR B 727 ? 1.2940 1.3954 1.2422 0.3201  -0.0352 0.1155  977  THR B N   
5158 C CA  . THR B 727 ? 1.1923 1.2790 1.1698 0.3320  -0.0253 0.1169  977  THR B CA  
5159 C C   . THR B 727 ? 1.1601 1.2436 1.1811 0.2815  -0.0297 0.0788  977  THR B C   
5160 O O   . THR B 727 ? 1.1812 1.2111 1.2210 0.2504  -0.0060 0.0781  977  THR B O   
5161 C CB  . THR B 727 ? 1.4780 1.4931 1.4530 0.3526  0.0161  0.1575  977  THR B CB  
5162 O OG1 . THR B 727 ? 1.5854 1.5438 1.5820 0.3069  0.0401  0.1523  977  THR B OG1 
5163 C CG2 . THR B 727 ? 1.2532 1.2665 1.1792 0.4002  0.0257  0.2005  977  THR B CG2 
5164 N N   . PRO B 728 ? 1.1602 1.3022 1.1990 0.2721  -0.0589 0.0457  978  PRO B N   
5165 C CA  . PRO B 728 ? 1.0607 1.2020 1.1364 0.2266  -0.0611 0.0126  978  PRO B CA  
5166 C C   . PRO B 728 ? 1.2220 1.3214 1.3236 0.2254  -0.0373 0.0145  978  PRO B C   
5167 O O   . PRO B 728 ? 1.1997 1.2965 1.3038 0.2633  -0.0300 0.0305  978  PRO B O   
5168 C CB  . PRO B 728 ? 1.0360 1.2507 1.1278 0.2283  -0.0931 -0.0168 978  PRO B CB  
5169 C CG  . PRO B 728 ? 1.1300 1.3851 1.1892 0.2619  -0.1125 -0.0066 978  PRO B CG  
5170 C CD  . PRO B 728 ? 1.1269 1.3416 1.1543 0.3019  -0.0909 0.0358  978  PRO B CD  
5171 N N   . CYS B 729 ? 1.0811 1.1489 1.2016 0.1831  -0.0253 -0.0029 979  CYS B N   
5172 C CA  . CYS B 729 ? 1.0606 1.0889 1.2062 0.1769  -0.0027 -0.0088 979  CYS B CA  
5173 C C   . CYS B 729 ? 1.2906 1.3599 1.4595 0.1885  -0.0144 -0.0282 979  CYS B C   
5174 O O   . CYS B 729 ? 1.1684 1.2802 1.3502 0.1655  -0.0325 -0.0548 979  CYS B O   
5175 C CB  . CYS B 729 ? 0.9635 0.9618 1.1211 0.1288  0.0073  -0.0288 979  CYS B CB  
5176 S SG  . CYS B 729 ? 1.2963 1.2582 1.4356 0.1097  0.0179  -0.0109 979  CYS B SG  
5177 N N   . GLN B 730 ? 1.3386 1.3946 1.5157 0.2251  -0.0014 -0.0133 980  GLN B N   
5178 C CA  . GLN B 730 ? 1.2470 1.3428 1.4497 0.2426  -0.0099 -0.0282 980  GLN B CA  
5179 C C   . GLN B 730 ? 1.2240 1.2765 1.4521 0.2301  0.0161  -0.0415 980  GLN B C   
5180 O O   . GLN B 730 ? 1.3101 1.3043 1.5390 0.2436  0.0437  -0.0236 980  GLN B O   
5181 C CB  . GLN B 730 ? 1.2931 1.4146 1.4879 0.2988  -0.0164 -0.0021 980  GLN B CB  
5182 C CG  . GLN B 730 ? 1.3481 1.5323 1.5217 0.3139  -0.0488 -0.0001 980  GLN B CG  
5183 C CD  . GLN B 730 ? 1.5135 1.7643 1.7130 0.2903  -0.0761 -0.0374 980  GLN B CD  
5184 O OE1 . GLN B 730 ? 1.5701 1.8343 1.8042 0.2808  -0.0728 -0.0579 980  GLN B OE1 
5185 N NE2 . GLN B 730 ? 1.4031 1.6944 1.5883 0.2807  -0.1005 -0.0468 980  GLN B NE2 
5186 N N   . VAL B 731 ? 1.1013 1.1817 1.3510 0.2050  0.0097  -0.0733 981  VAL B N   
5187 C CA  . VAL B 731 ? 1.2126 1.2613 1.4841 0.1936  0.0324  -0.0918 981  VAL B CA  
5188 C C   . VAL B 731 ? 1.3470 1.4385 1.6459 0.2187  0.0281  -0.1013 981  VAL B C   
5189 O O   . VAL B 731 ? 1.1448 1.3001 1.4519 0.2266  0.0036  -0.1064 981  VAL B O   
5190 C CB  . VAL B 731 ? 1.0721 1.1146 1.3425 0.1438  0.0332  -0.1206 981  VAL B CB  
5191 C CG1 . VAL B 731 ? 1.0649 1.0829 1.3118 0.1196  0.0304  -0.1115 981  VAL B CG1 
5192 C CG2 . VAL B 731 ? 0.9353 1.0404 1.2170 0.1288  0.0136  -0.1419 981  VAL B CG2 
5193 N N   . ASP B 732 ? 1.2412 1.2977 1.5587 0.2315  0.0532  -0.1053 982  ASP B N   
5194 C CA  . ASP B 732 ? 1.1325 1.2240 1.4804 0.2549  0.0546  -0.1157 982  ASP B CA  
5195 C C   . ASP B 732 ? 1.1351 1.2019 1.4977 0.2288  0.0760  -0.1463 982  ASP B C   
5196 O O   . ASP B 732 ? 1.1511 1.1564 1.5067 0.2135  0.0986  -0.1518 982  ASP B O   
5197 C CB  . ASP B 732 ? 1.2169 1.2932 1.5741 0.3083  0.0665  -0.0869 982  ASP B CB  
5198 C CG  . ASP B 732 ? 1.4886 1.6360 1.8722 0.3420  0.0489  -0.0877 982  ASP B CG  
5199 O OD1 . ASP B 732 ? 1.5568 1.7191 1.9384 0.3888  0.0430  -0.0591 982  ASP B OD1 
5200 O OD2 . ASP B 732 ? 1.4445 1.6359 1.8516 0.3226  0.0411  -0.1162 982  ASP B OD2 
5201 N N   . LEU B 733 ? 1.1783 1.2950 1.5627 0.2237  0.0699  -0.1680 983  LEU B N   
5202 C CA  . LEU B 733 ? 1.1846 1.2899 1.5767 0.1978  0.0877  -0.1988 983  LEU B CA  
5203 C C   . LEU B 733 ? 1.1765 1.2941 1.6020 0.2271  0.1040  -0.2066 983  LEU B C   
5204 O O   . LEU B 733 ? 1.2103 1.3821 1.6606 0.2537  0.0907  -0.1987 983  LEU B O   
5205 C CB  . LEU B 733 ? 1.0942 1.2456 1.4809 0.1621  0.0719  -0.2171 983  LEU B CB  
5206 C CG  . LEU B 733 ? 1.1716 1.2985 1.5260 0.1220  0.0682  -0.2237 983  LEU B CG  
5207 C CD1 . LEU B 733 ? 1.2474 1.3478 1.5812 0.1250  0.0577  -0.1993 983  LEU B CD1 
5208 C CD2 . LEU B 733 ? 1.2454 1.4224 1.5990 0.0952  0.0539  -0.2351 983  LEU B CD2 
5209 N N   . THR B 734 ? 1.3091 1.3788 1.7379 0.2225  0.1326  -0.2244 984  THR B N   
5210 C CA  . THR B 734 ? 1.2690 1.3447 1.7289 0.2466  0.1530  -0.2367 984  THR B CA  
5211 C C   . THR B 734 ? 1.2714 1.3327 1.7237 0.2152  0.1716  -0.2734 984  THR B C   
5212 O O   . THR B 734 ? 1.3251 1.3331 1.7566 0.1930  0.1845  -0.2875 984  THR B O   
5213 C CB  . THR B 734 ? 1.3518 1.3738 1.8259 0.2850  0.1757  -0.2187 984  THR B CB  
5214 O OG1 . THR B 734 ? 1.5052 1.4527 1.9652 0.2641  0.1998  -0.2326 984  THR B OG1 
5215 C CG2 . THR B 734 ? 1.2807 1.3091 1.7494 0.3164  0.1589  -0.1782 984  THR B CG2 
5216 N N   . THR B 735 ? 1.2212 1.3326 1.6912 0.2141  0.1736  -0.2899 985  THR B N   
5217 C CA  . THR B 735 ? 1.2893 1.3932 1.7484 0.1903  0.1932  -0.3236 985  THR B CA  
5218 C C   . THR B 735 ? 1.4226 1.4826 1.8989 0.2126  0.2255  -0.3391 985  THR B C   
5219 O O   . THR B 735 ? 1.3671 1.4403 1.8787 0.2493  0.2340  -0.3284 985  THR B O   
5220 C CB  . THR B 735 ? 1.2107 1.3829 1.6836 0.1821  0.1883  -0.3322 985  THR B CB  
5221 O OG1 . THR B 735 ? 1.3269 1.5366 1.7906 0.1630  0.1603  -0.3175 985  THR B OG1 
5222 C CG2 . THR B 735 ? 1.3144 1.4809 1.7656 0.1583  0.2088  -0.3638 985  THR B CG2 
5223 N N   . THR B 736 ? 1.3147 1.3243 1.7684 0.1910  0.2433  -0.3664 986  THR B N   
5224 C CA  . THR B 736 ? 1.4243 1.3799 1.8946 0.2088  0.2758  -0.3848 986  THR B CA  
5225 C C   . THR B 736 ? 1.4085 1.3672 1.8675 0.1935  0.2969  -0.4277 986  THR B C   
5226 O O   . THR B 736 ? 1.3886 1.3529 1.8733 0.2181  0.3193  -0.4384 986  THR B O   
5227 C CB  . THR B 736 ? 1.4115 1.2944 1.8736 0.2006  0.2832  -0.3827 986  THR B CB  
5228 O OG1 . THR B 736 ? 1.5280 1.4060 1.9541 0.1575  0.2711  -0.4028 986  THR B OG1 
5229 C CG2 . THR B 736 ? 1.4544 1.3310 1.9265 0.2240  0.2685  -0.3367 986  THR B CG2 
5230 N N   . SER B 737 ? 1.4691 1.4272 1.8894 0.1560  0.2907  -0.4525 987  SER B N   
5231 C CA  . SER B 737 ? 1.3885 1.3463 1.7893 0.1426  0.3108  -0.4960 987  SER B CA  
5232 C C   . SER B 737 ? 1.3455 1.3578 1.7085 0.1152  0.2944  -0.5015 987  SER B C   
5233 O O   . SER B 737 ? 1.3294 1.3679 1.6811 0.1009  0.2679  -0.4759 987  SER B O   
5234 C CB  . SER B 737 ? 1.4179 1.3104 1.8077 0.1266  0.3255  -0.5302 987  SER B CB  
5235 O OG  . SER B 737 ? 1.5311 1.3658 1.9576 0.1501  0.3412  -0.5171 987  SER B OG  
5236 N N   . ILE B 738 ? 1.3610 1.3893 1.7035 0.1098  0.3126  -0.5345 988  ILE B N   
5237 C CA  . ILE B 738 ? 1.3958 1.4732 1.6983 0.0876  0.3035  -0.5396 988  ILE B CA  
5238 C C   . ILE B 738 ? 1.3955 1.4682 1.6632 0.0803  0.3250  -0.5860 988  ILE B C   
5239 O O   . ILE B 738 ? 1.3981 1.4618 1.6816 0.1004  0.3529  -0.6071 988  ILE B O   
5240 C CB  . ILE B 738 ? 1.2844 1.4217 1.6083 0.0996  0.3021  -0.5115 988  ILE B CB  
5241 C CG1 . ILE B 738 ? 1.3409 1.5236 1.6246 0.0801  0.3024  -0.5164 988  ILE B CG1 
5242 C CG2 . ILE B 738 ? 1.2822 1.4251 1.6481 0.1318  0.3284  -0.5162 988  ILE B CG2 
5243 C CD1 . ILE B 738 ? 1.3174 1.5568 1.6285 0.0878  0.3052  -0.4902 988  ILE B CD1 
5244 N N   . ASP B 739 ? 1.4212 1.5024 1.6406 0.0533  0.3117  -0.6031 989  ASP B N   
5245 C CA  . ASP B 739 ? 1.4128 1.4997 1.5893 0.0455  0.3267  -0.6488 989  ASP B CA  
5246 C C   . ASP B 739 ? 1.4044 1.5522 1.5371 0.0373  0.3220  -0.6379 989  ASP B C   
5247 O O   . ASP B 739 ? 1.4463 1.6246 1.5836 0.0320  0.3054  -0.5979 989  ASP B O   
5248 C CB  . ASP B 739 ? 1.4980 1.5463 1.6551 0.0229  0.3158  -0.6839 989  ASP B CB  
5249 C CG  . ASP B 739 ? 1.7296 1.7784 1.8501 0.0187  0.3328  -0.7414 989  ASP B CG  
5250 O OD1 . ASP B 739 ? 1.8035 1.8992 1.8711 0.0096  0.3263  -0.7513 989  ASP B OD1 
5251 O OD2 . ASP B 739 ? 1.5688 1.5715 1.7129 0.0265  0.3540  -0.7768 989  ASP B OD2 
5252 N N   . GLY B 740 ? 1.5450 1.7098 1.6349 0.0379  0.3391  -0.6742 990  GLY B N   
5253 C CA  . GLY B 740 ? 1.5543 1.7755 1.5997 0.0357  0.3418  -0.6620 990  GLY B CA  
5254 C C   . GLY B 740 ? 1.6353 1.8877 1.7115 0.0562  0.3648  -0.6336 990  GLY B C   
5255 O O   . GLY B 740 ? 1.6544 1.8895 1.7833 0.0743  0.3787  -0.6292 990  GLY B O   
5256 N N   . ALA B 741 ? 1.6293 1.9302 1.6743 0.0540  0.3700  -0.6131 991  ALA B N   
5257 C CA  . ALA B 741 ? 1.6899 2.0270 1.7662 0.0693  0.3937  -0.5850 991  ALA B CA  
5258 C C   . ALA B 741 ? 1.6693 2.0362 1.7577 0.0565  0.3768  -0.5380 991  ALA B C   
5259 O O   . ALA B 741 ? 1.6908 2.0482 1.7639 0.0383  0.3467  -0.5263 991  ALA B O   
5260 C CB  . ALA B 741 ? 1.8110 2.1776 1.8440 0.0821  0.4280  -0.6049 991  ALA B CB  
5261 N N   . TRP B 742 ? 1.6177 2.0212 1.7383 0.0659  0.3984  -0.5125 992  TRP B N   
5262 C CA  . TRP B 742 ? 1.6086 2.0380 1.7576 0.0545  0.3866  -0.4703 992  TRP B CA  
5263 C C   . TRP B 742 ? 1.6814 2.1419 1.7788 0.0460  0.3964  -0.4524 992  TRP B C   
5264 O O   . TRP B 742 ? 1.7954 2.2541 1.8238 0.0444  0.3966  -0.4715 992  TRP B O   
5265 C CB  . TRP B 742 ? 1.4683 1.9224 1.6940 0.0674  0.4037  -0.4530 992  TRP B CB  
5266 C CG  . TRP B 742 ? 1.5477 2.0355 1.7770 0.0820  0.4468  -0.4549 992  TRP B CG  
5267 C CD1 . TRP B 742 ? 1.7201 2.2170 1.8857 0.0873  0.4726  -0.4694 992  TRP B CD1 
5268 C CD2 . TRP B 742 ? 1.6757 2.1959 1.9774 0.0940  0.4699  -0.4418 992  TRP B CD2 
5269 N NE1 . TRP B 742 ? 1.6565 2.1860 1.8485 0.1023  0.5130  -0.4636 992  TRP B NE1 
5270 C CE2 . TRP B 742 ? 1.5754 2.1201 1.8548 0.1055  0.5123  -0.4472 992  TRP B CE2 
5271 C CE3 . TRP B 742 ? 1.7339 2.2694 2.1179 0.0970  0.4583  -0.4274 992  TRP B CE3 
5272 C CZ2 . TRP B 742 ? 1.4364 2.0174 1.7782 0.1180  0.5455  -0.4377 992  TRP B CZ2 
5273 C CZ3 . TRP B 742 ? 1.6082 2.1837 2.0553 0.1092  0.4877  -0.4210 992  TRP B CZ3 
5274 C CH2 . TRP B 742 ? 1.4550 2.0519 1.8836 0.1187  0.5319  -0.4255 992  TRP B CH2 
5275 N N   . GLY B 743 ? 1.5502 2.0406 1.6827 0.0416  0.4052  -0.4161 993  GLY B N   
5276 C CA  . GLY B 743 ? 1.4977 2.0172 1.5898 0.0379  0.4233  -0.3922 993  GLY B CA  
5277 C C   . GLY B 743 ? 1.6732 2.1845 1.7147 0.0218  0.3938  -0.3807 993  GLY B C   
5278 O O   . GLY B 743 ? 1.6641 2.1472 1.6994 0.0115  0.3595  -0.3939 993  GLY B O   
5279 N N   . SER B 744 ? 1.7402 2.2776 1.7469 0.0213  0.4103  -0.3530 994  SER B N   
5280 C CA  . SER B 744 ? 1.7411 2.2786 1.6979 0.0101  0.3871  -0.3371 994  SER B CA  
5281 C C   . SER B 744 ? 1.8165 2.3595 1.6857 0.0178  0.3827  -0.3639 994  SER B C   
5282 O O   . SER B 744 ? 1.7697 2.3247 1.5889 0.0139  0.3689  -0.3492 994  SER B O   
5283 C CB  . SER B 744 ? 1.6777 2.2399 1.6437 0.0079  0.4084  -0.2897 994  SER B CB  
5284 O OG  . SER B 744 ? 1.7062 2.2957 1.6363 0.0256  0.4504  -0.2810 994  SER B OG  
5285 N N   . GLY B 745 ? 1.7796 2.3163 1.6308 0.0295  0.3935  -0.4047 995  GLY B N   
5286 C CA  . GLY B 745 ? 1.8117 2.3603 1.5807 0.0380  0.3920  -0.4364 995  GLY B CA  
5287 C C   . GLY B 745 ? 1.8897 2.4087 1.6465 0.0282  0.3596  -0.4839 995  GLY B C   
5288 O O   . GLY B 745 ? 1.8175 2.3414 1.5303 0.0188  0.3315  -0.4930 995  GLY B O   
5289 N N   . VAL B 746 ? 2.0120 2.5004 1.8117 0.0306  0.3646  -0.5139 996  VAL B N   
5290 C CA  . VAL B 746 ? 1.9663 2.4234 1.7551 0.0235  0.3437  -0.5637 996  VAL B CA  
5291 C C   . VAL B 746 ? 1.8455 2.2670 1.6788 0.0040  0.3090  -0.5566 996  VAL B C   
5292 O O   . VAL B 746 ? 1.9385 2.3394 1.7560 -0.0078 0.2862  -0.5894 996  VAL B O   
5293 C CB  . VAL B 746 ? 1.9007 2.3380 1.7111 0.0386  0.3703  -0.6007 996  VAL B CB  
5294 C CG1 . VAL B 746 ? 1.8835 2.3577 1.6515 0.0595  0.4084  -0.6046 996  VAL B CG1 
5295 C CG2 . VAL B 746 ? 1.8327 2.2446 1.7267 0.0413  0.3756  -0.5806 996  VAL B CG2 
5296 N N   . GLY B 747 ? 1.6178 2.0330 1.5076 0.0002  0.3053  -0.5166 997  GLY B N   
5297 C CA  . GLY B 747 ? 1.5329 1.9145 1.4640 -0.0144 0.2758  -0.5091 997  GLY B CA  
5298 C C   . GLY B 747 ? 1.4995 1.8385 1.4716 -0.0088 0.2785  -0.5373 997  GLY B C   
5299 O O   . GLY B 747 ? 1.7023 2.0339 1.6632 0.0031  0.2994  -0.5725 997  GLY B O   
5300 N N   . PHE B 748 ? 1.3540 1.6639 1.3727 -0.0151 0.2595  -0.5217 998  PHE B N   
5301 C CA  . PHE B 748 ? 1.4172 1.6850 1.4785 -0.0058 0.2642  -0.5396 998  PHE B CA  
5302 C C   . PHE B 748 ? 1.4143 1.6445 1.4905 -0.0201 0.2371  -0.5369 998  PHE B C   
5303 O O   . PHE B 748 ? 1.3327 1.5728 1.3950 -0.0363 0.2140  -0.5167 998  PHE B O   
5304 C CB  . PHE B 748 ? 1.4041 1.6807 1.5218 0.0127  0.2788  -0.5154 998  PHE B CB  
5305 C CG  . PHE B 748 ? 1.3240 1.6134 1.4751 0.0066  0.2586  -0.4741 998  PHE B CG  
5306 C CD1 . PHE B 748 ? 1.3712 1.7019 1.5168 0.0000  0.2595  -0.4466 998  PHE B CD1 
5307 C CD2 . PHE B 748 ? 1.3138 1.5736 1.5023 0.0089  0.2408  -0.4630 998  PHE B CD2 
5308 C CE1 . PHE B 748 ? 1.3117 1.6536 1.4911 -0.0067 0.2417  -0.4139 998  PHE B CE1 
5309 C CE2 . PHE B 748 ? 1.2084 1.4832 1.4242 0.0044  0.2215  -0.4293 998  PHE B CE2 
5310 C CZ  . PHE B 748 ? 1.1873 1.5031 1.4001 -0.0045 0.2213  -0.4072 998  PHE B CZ  
5311 N N   . ASN B 749 ? 1.4792 1.6643 1.5858 -0.0124 0.2432  -0.5561 999  ASN B N   
5312 C CA  . ASN B 749 ? 1.4579 1.6009 1.5872 -0.0214 0.2250  -0.5506 999  ASN B CA  
5313 C C   . ASN B 749 ? 1.4129 1.5334 1.5961 -0.0002 0.2314  -0.5279 999  ASN B C   
5314 O O   . ASN B 749 ? 1.4277 1.5430 1.6329 0.0210  0.2545  -0.5385 999  ASN B O   
5315 C CB  . ASN B 749 ? 1.5151 1.6194 1.6320 -0.0324 0.2282  -0.5961 999  ASN B CB  
5316 C CG  . ASN B 749 ? 1.4980 1.5549 1.6443 -0.0417 0.2153  -0.5888 999  ASN B CG  
5317 O OD1 . ASN B 749 ? 1.5169 1.5774 1.6489 -0.0625 0.1932  -0.5831 999  ASN B OD1 
5318 N ND2 . ASN B 749 ? 1.5134 1.5260 1.7019 -0.0242 0.2312  -0.5869 999  ASN B ND2 
5319 N N   . LEU B 750 ? 1.3635 1.4736 1.5667 -0.0036 0.2111  -0.4965 1000 LEU B N   
5320 C CA  . LEU B 750 ? 1.3114 1.4081 1.5605 0.0191  0.2121  -0.4706 1000 LEU B CA  
5321 C C   . LEU B 750 ? 1.2479 1.2906 1.5104 0.0177  0.2059  -0.4672 1000 LEU B C   
5322 O O   . LEU B 750 ? 1.3469 1.3837 1.5949 -0.0017 0.1861  -0.4564 1000 LEU B O   
5323 C CB  . LEU B 750 ? 1.2891 1.4299 1.5513 0.0208  0.1949  -0.4335 1000 LEU B CB  
5324 C CG  . LEU B 750 ? 1.2680 1.4314 1.5755 0.0483  0.2014  -0.4156 1000 LEU B CG  
5325 C CD1 . LEU B 750 ? 1.0693 1.2780 1.3906 0.0435  0.1816  -0.3861 1000 LEU B CD1 
5326 C CD2 . LEU B 750 ? 1.3871 1.5098 1.7248 0.0721  0.2045  -0.4086 1000 LEU B CD2 
5327 N N   . ILE B 751 ? 1.3415 1.3440 1.6336 0.0393  0.2254  -0.4745 1001 ILE B N   
5328 C CA  . ILE B 751 ? 1.4962 1.4428 1.8083 0.0440  0.2267  -0.4650 1001 ILE B CA  
5329 C C   . ILE B 751 ? 1.3766 1.3319 1.7163 0.0705  0.2175  -0.4213 1001 ILE B C   
5330 O O   . ILE B 751 ? 1.3236 1.3077 1.6849 0.0957  0.2233  -0.4112 1001 ILE B O   
5331 C CB  . ILE B 751 ? 1.4296 1.3224 1.7604 0.0542  0.2570  -0.4972 1001 ILE B CB  
5332 C CG1 . ILE B 751 ? 1.3316 1.2211 1.6329 0.0268  0.2628  -0.5469 1001 ILE B CG1 
5333 C CG2 . ILE B 751 ? 1.3903 1.2212 1.7485 0.0625  0.2643  -0.4811 1001 ILE B CG2 
5334 C CD1 . ILE B 751 ? 1.4030 1.2374 1.7244 0.0322  0.2927  -0.5864 1001 ILE B CD1 
5335 N N   . CYS B 752 ? 1.3904 1.3247 1.7300 0.0662  0.2029  -0.3963 1002 CYS B N   
5336 C CA  . CYS B 752 ? 1.3884 1.3363 1.7464 0.0920  0.1907  -0.3555 1002 CYS B CA  
5337 C C   . CYS B 752 ? 1.4085 1.3028 1.7728 0.0983  0.1934  -0.3348 1002 CYS B C   
5338 O O   . CYS B 752 ? 1.3996 1.2711 1.7476 0.0712  0.1878  -0.3402 1002 CYS B O   
5339 C CB  . CYS B 752 ? 1.4390 1.4454 1.7826 0.0796  0.1623  -0.3378 1002 CYS B CB  
5340 S SG  . CYS B 752 ? 1.9216 1.9932 2.2916 0.1033  0.1590  -0.3293 1002 CYS B SG  
5341 N N   . SER B 753 ? 1.3763 1.2531 1.7655 0.1360  0.2034  -0.3095 1003 SER B N   
5342 C CA  . SER B 753 ? 1.4241 1.2537 1.8191 0.1502  0.2086  -0.2798 1003 SER B CA  
5343 C C   . SER B 753 ? 1.3114 1.1818 1.6913 0.1560  0.1788  -0.2451 1003 SER B C   
5344 O O   . SER B 753 ? 1.2799 1.1971 1.6686 0.1828  0.1654  -0.2275 1003 SER B O   
5345 C CB  . SER B 753 ? 1.5016 1.2944 1.9274 0.1929  0.2350  -0.2651 1003 SER B CB  
5346 O OG  . SER B 753 ? 1.4787 1.2267 1.9082 0.2111  0.2429  -0.2299 1003 SER B OG  
5347 N N   . VAL B 754 ? 1.3566 1.2122 1.7168 0.1309  0.1684  -0.2382 1004 VAL B N   
5348 C CA  . VAL B 754 ? 1.2435 1.1320 1.5864 0.1335  0.1420  -0.2087 1004 VAL B CA  
5349 C C   . VAL B 754 ? 1.2820 1.1224 1.6253 0.1539  0.1533  -0.1754 1004 VAL B C   
5350 O O   . VAL B 754 ? 1.3909 1.1752 1.7380 0.1371  0.1726  -0.1810 1004 VAL B O   
5351 C CB  . VAL B 754 ? 1.1959 1.1087 1.5151 0.0915  0.1223  -0.2230 1004 VAL B CB  
5352 C CG1 . VAL B 754 ? 1.2492 1.1882 1.5525 0.0948  0.0986  -0.1937 1004 VAL B CG1 
5353 C CG2 . VAL B 754 ? 1.2454 1.2069 1.5623 0.0760  0.1143  -0.2493 1004 VAL B CG2 
5354 N N   . SER B 755 ? 1.2536 1.1181 1.5944 0.1906  0.1422  -0.1413 1005 SER B N   
5355 C CA  . SER B 755 ? 1.2809 1.1051 1.6173 0.2188  0.1544  -0.1028 1005 SER B CA  
5356 C C   . SER B 755 ? 1.2729 1.1351 1.5812 0.2195  0.1265  -0.0796 1005 SER B C   
5357 O O   . SER B 755 ? 1.2727 1.1942 1.5755 0.2411  0.1022  -0.0708 1005 SER B O   
5358 C CB  . SER B 755 ? 1.3437 1.1611 1.6985 0.2713  0.1692  -0.0797 1005 SER B CB  
5359 O OG  . SER B 755 ? 1.5201 1.2933 1.8684 0.3015  0.1862  -0.0385 1005 SER B OG  
5360 N N   . LEU B 756 ? 1.2100 1.0401 1.5035 0.1958  0.1304  -0.0725 1006 LEU B N   
5361 C CA  . LEU B 756 ? 1.2868 1.1438 1.5527 0.1975  0.1091  -0.0496 1006 LEU B CA  
5362 C C   . LEU B 756 ? 1.3237 1.1444 1.5797 0.2367  0.1264  -0.0055 1006 LEU B C   
5363 O O   . LEU B 756 ? 1.3676 1.1249 1.6404 0.2466  0.1602  0.0060  1006 LEU B O   
5364 C CB  . LEU B 756 ? 1.3117 1.1611 1.5671 0.1501  0.1029  -0.0657 1006 LEU B CB  
5365 C CG  . LEU B 756 ? 1.3546 1.1380 1.6158 0.1356  0.1296  -0.0561 1006 LEU B CG  
5366 C CD1 . LEU B 756 ? 1.2073 1.0006 1.4571 0.0941  0.1164  -0.0683 1006 LEU B CD1 
5367 C CD2 . LEU B 756 ? 1.2795 1.0126 1.5714 0.1264  0.1587  -0.0787 1006 LEU B CD2 
5368 N N   . THR B 757 ? 1.4183 1.2800 1.6472 0.2602  0.1046  0.0189  1007 THR B N   
5369 C CA  . THR B 757 ? 1.4082 1.2467 1.6183 0.3036  0.1182  0.0648  1007 THR B CA  
5370 C C   . THR B 757 ? 1.5088 1.3561 1.6866 0.2921  0.1065  0.0797  1007 THR B C   
5371 O O   . THR B 757 ? 1.4534 1.3273 1.6261 0.2526  0.0863  0.0545  1007 THR B O   
5372 C CB  . THR B 757 ? 1.4170 1.3046 1.6206 0.3576  0.1028  0.0835  1007 THR B CB  
5373 O OG1 . THR B 757 ? 1.5650 1.5310 1.7518 0.3537  0.0619  0.0692  1007 THR B OG1 
5374 C CG2 . THR B 757 ? 1.2626 1.1495 1.5017 0.3682  0.1127  0.0659  1007 THR B CG2 
5375 N N   . GLU B 758 ? 1.6103 1.4336 1.7658 0.3297  0.1222  0.1233  1008 GLU B N   
5376 C CA  . GLU B 758 ? 1.5508 1.3842 1.6704 0.3306  0.1141  0.1441  1008 GLU B CA  
5377 C C   . GLU B 758 ? 1.5080 1.3018 1.6368 0.2802  0.1276  0.1316  1008 GLU B C   
5378 O O   . GLU B 758 ? 1.5309 1.2793 1.6518 0.2855  0.1539  0.1612  1008 GLU B O   
5379 C CB  . GLU B 758 ? 1.5048 1.4219 1.6003 0.3350  0.0695  0.1287  1008 GLU B CB  
5380 C CG  . GLU B 758 ? 1.5365 1.5083 1.6338 0.3773  0.0493  0.1288  1008 GLU B CG  
5381 C CD  . GLU B 758 ? 1.6292 1.5935 1.7013 0.4406  0.0623  0.1764  1008 GLU B CD  
5382 O OE1 . GLU B 758 ? 1.5309 1.5613 1.5799 0.4775  0.0336  0.1824  1008 GLU B OE1 
5383 O OE2 . GLU B 758 ? 1.6152 1.5092 1.6917 0.4545  0.1019  0.2077  1008 GLU B OE2 
5384 N N   . CYS B 759 ? 1.4906 1.3034 1.6372 0.2332  0.1109  0.0895  1009 CYS B N   
5385 C CA  . CYS B 759 ? 1.4905 1.2784 1.6461 0.1864  0.1177  0.0749  1009 CYS B CA  
5386 C C   . CYS B 759 ? 1.4735 1.1952 1.6664 0.1662  0.1527  0.0663  1009 CYS B C   
5387 O O   . CYS B 759 ? 1.4194 1.1225 1.6349 0.1753  0.1651  0.0555  1009 CYS B O   
5388 C CB  . CYS B 759 ? 1.3358 1.1739 1.4929 0.1478  0.0860  0.0361  1009 CYS B CB  
5389 S SG  . CYS B 759 ? 1.5554 1.4665 1.6779 0.1606  0.0475  0.0390  1009 CYS B SG  
5390 N N   . SER B 760 ? 1.5300 1.2174 1.7329 0.1380  0.1692  0.0686  1010 SER B N   
5391 C CA  . SER B 760 ? 1.4183 1.0470 1.6635 0.1116  0.2006  0.0527  1010 SER B CA  
5392 C C   . SER B 760 ? 1.4009 1.0509 1.6653 0.0692  0.1835  0.0010  1010 SER B C   
5393 O O   . SER B 760 ? 1.2216 0.8434 1.5146 0.0620  0.1994  -0.0223 1010 SER B O   
5394 C CB  . SER B 760 ? 1.2982 0.8903 1.5538 0.0946  0.2231  0.0705  1010 SER B CB  
5395 O OG  . SER B 760 ? 1.4088 0.9533 1.7125 0.0608  0.2489  0.0454  1010 SER B OG  
5396 N N   . THR B 761 ? 1.4301 1.1293 1.6779 0.0427  0.1529  -0.0166 1011 THR B N   
5397 C CA  . THR B 761 ? 1.2557 0.9839 1.5125 0.0075  0.1344  -0.0605 1011 THR B CA  
5398 C C   . THR B 761 ? 1.1452 0.9387 1.3729 0.0092  0.0990  -0.0645 1011 THR B C   
5399 O O   . THR B 761 ? 1.3247 1.1406 1.5282 0.0297  0.0871  -0.0391 1011 THR B O   
5400 C CB  . THR B 761 ? 1.2401 0.9554 1.5179 -0.0353 0.1389  -0.0820 1011 THR B CB  
5401 O OG1 . THR B 761 ? 1.2204 0.9316 1.4898 -0.0358 0.1415  -0.0541 1011 THR B OG1 
5402 C CG2 . THR B 761 ? 1.2542 0.9132 1.5729 -0.0472 0.1707  -0.0999 1011 THR B CG2 
5403 N N   . PHE B 762 ? 1.0783 0.9023 1.3093 -0.0120 0.0838  -0.0979 1012 PHE B N   
5404 C CA  . PHE B 762 ? 1.0250 0.9076 1.2366 -0.0126 0.0549  -0.1036 1012 PHE B CA  
5405 C C   . PHE B 762 ? 1.1037 1.0096 1.3203 -0.0443 0.0455  -0.1384 1012 PHE B C   
5406 O O   . PHE B 762 ? 1.1023 0.9971 1.3316 -0.0466 0.0558  -0.1604 1012 PHE B O   
5407 C CB  . PHE B 762 ? 1.0216 0.9253 1.2288 0.0235  0.0496  -0.0936 1012 PHE B CB  
5408 C CG  . PHE B 762 ? 0.9301 0.8934 1.1247 0.0247  0.0220  -0.0974 1012 PHE B CG  
5409 C CD1 . PHE B 762 ? 0.9158 0.9002 1.0930 0.0203  0.0068  -0.0847 1012 PHE B CD1 
5410 C CD2 . PHE B 762 ? 0.9318 0.9289 1.1359 0.0299  0.0139  -0.1146 1012 PHE B CD2 
5411 C CE1 . PHE B 762 ? 1.0306 1.0667 1.2026 0.0197  -0.0162 -0.0915 1012 PHE B CE1 
5412 C CE2 . PHE B 762 ? 0.9967 1.0472 1.1979 0.0289  -0.0083 -0.1196 1012 PHE B CE2 
5413 C CZ  . PHE B 762 ? 0.9807 1.0496 1.1670 0.0231  -0.0234 -0.1091 1012 PHE B CZ  
5414 N N   . LEU B 763 ? 1.0556 0.9937 1.2607 -0.0663 0.0274  -0.1424 1013 LEU B N   
5415 C CA  . LEU B 763 ? 0.9378 0.9051 1.1409 -0.0918 0.0172  -0.1694 1013 LEU B CA  
5416 C C   . LEU B 763 ? 1.0002 1.0126 1.1947 -0.0824 0.0023  -0.1699 1013 LEU B C   
5417 O O   . LEU B 763 ? 1.0809 1.1176 1.2673 -0.0768 -0.0113 -0.1543 1013 LEU B O   
5418 C CB  . LEU B 763 ? 0.9037 0.8808 1.1025 -0.1190 0.0083  -0.1711 1013 LEU B CB  
5419 C CG  . LEU B 763 ? 0.9065 0.9220 1.0964 -0.1405 -0.0049 -0.1911 1013 LEU B CG  
5420 C CD1 . LEU B 763 ? 0.8384 0.8470 1.0338 -0.1503 0.0039  -0.2223 1013 LEU B CD1 
5421 C CD2 . LEU B 763 ? 0.7909 0.8193 0.9776 -0.1613 -0.0148 -0.1864 1013 LEU B CD2 
5422 N N   . THR B 764 ? 0.9293 0.9529 1.1289 -0.0811 0.0065  -0.1895 1014 THR B N   
5423 C CA  . THR B 764 ? 0.8792 0.9450 1.0791 -0.0732 -0.0030 -0.1916 1014 THR B CA  
5424 C C   . THR B 764 ? 0.9711 1.0486 1.1713 -0.0841 0.0044  -0.2171 1014 THR B C   
5425 O O   . THR B 764 ? 0.9776 1.0356 1.1735 -0.0994 0.0124  -0.2349 1014 THR B O   
5426 C CB  . THR B 764 ? 0.8466 0.9163 1.0571 -0.0408 -0.0026 -0.1785 1014 THR B CB  
5427 O OG1 . THR B 764 ? 0.8311 0.9467 1.0506 -0.0362 -0.0121 -0.1840 1014 THR B OG1 
5428 C CG2 . THR B 764 ? 0.8696 0.9049 1.0917 -0.0242 0.0167  -0.1848 1014 THR B CG2 
5429 N N   . SER B 765 ? 0.8821 0.9939 1.0888 -0.0761 0.0024  -0.2205 1015 SER B N   
5430 C CA  . SER B 765 ? 0.9160 1.0431 1.1210 -0.0825 0.0120  -0.2417 1015 SER B CA  
5431 C C   . SER B 765 ? 0.8992 1.0394 1.1248 -0.0592 0.0200  -0.2445 1015 SER B C   
5432 O O   . SER B 765 ? 0.9369 1.0999 1.1782 -0.0446 0.0111  -0.2309 1015 SER B O   
5433 C CB  . SER B 765 ? 0.8429 1.0065 1.0361 -0.1006 0.0051  -0.2414 1015 SER B CB  
5434 O OG  . SER B 765 ? 0.9844 1.1415 1.1614 -0.1191 -0.0041 -0.2359 1015 SER B OG  
5435 N N   . ILE B 766 ? 0.9782 1.1072 1.2057 -0.0554 0.0363  -0.2646 1016 ILE B N   
5436 C CA  . ILE B 766 ? 1.0065 1.1515 1.2554 -0.0343 0.0468  -0.2702 1016 ILE B CA  
5437 C C   . ILE B 766 ? 0.9808 1.1593 1.2237 -0.0457 0.0545  -0.2846 1016 ILE B C   
5438 O O   . ILE B 766 ? 0.9335 1.1077 1.1509 -0.0640 0.0586  -0.2986 1016 ILE B O   
5439 C CB  . ILE B 766 ? 1.0904 1.1948 1.3488 -0.0171 0.0644  -0.2810 1016 ILE B CB  
5440 C CG1 . ILE B 766 ? 0.9859 1.0510 1.2470 -0.0065 0.0616  -0.2625 1016 ILE B CG1 
5441 C CG2 . ILE B 766 ? 1.0448 1.1690 1.3298 0.0092  0.0740  -0.2827 1016 ILE B CG2 
5442 C CD1 . ILE B 766 ? 1.1933 1.2790 1.4676 0.0182  0.0487  -0.2362 1016 ILE B CD1 
5443 N N   . LYS B 767 ? 0.9596 1.1746 1.2270 -0.0340 0.0571  -0.2809 1017 LYS B N   
5444 C CA  . LYS B 767 ? 1.0121 1.2620 1.2788 -0.0434 0.0674  -0.2880 1017 LYS B CA  
5445 C C   . LYS B 767 ? 1.0477 1.3066 1.3339 -0.0257 0.0876  -0.3028 1017 LYS B C   
5446 O O   . LYS B 767 ? 1.1004 1.3497 1.4108 -0.0034 0.0895  -0.3028 1017 LYS B O   
5447 C CB  . LYS B 767 ? 0.8552 1.1435 1.1426 -0.0493 0.0568  -0.2718 1017 LYS B CB  
5448 C CG  . LYS B 767 ? 0.9515 1.2545 1.2175 -0.0719 0.0583  -0.2662 1017 LYS B CG  
5449 C CD  . LYS B 767 ? 0.8988 1.2195 1.1813 -0.0805 0.0430  -0.2489 1017 LYS B CD  
5450 C CE  . LYS B 767 ? 0.7279 1.0769 1.0579 -0.0665 0.0383  -0.2481 1017 LYS B CE  
5451 N NZ  . LYS B 767 ? 0.9231 1.2920 1.2724 -0.0766 0.0248  -0.2376 1017 LYS B NZ  
5452 N N   . ALA B 768 ? 0.9333 1.2121 1.2079 -0.0334 0.1041  -0.3136 1018 ALA B N   
5453 C CA  . ALA B 768 ? 0.9449 1.2354 1.2353 -0.0180 0.1271  -0.3288 1018 ALA B CA  
5454 C C   . ALA B 768 ? 1.2153 1.5547 1.5358 -0.0184 0.1354  -0.3193 1018 ALA B C   
5455 O O   . ALA B 768 ? 1.2196 1.5775 1.5218 -0.0311 0.1477  -0.3180 1018 ALA B O   
5456 C CB  . ALA B 768 ? 0.9559 1.2296 1.2067 -0.0244 0.1436  -0.3524 1018 ALA B CB  
5457 N N   . CYS B 769 ? 1.2024 1.5642 1.5713 -0.0034 0.1296  -0.3123 1019 CYS B N   
5458 C CA  . CYS B 769 ? 1.1082 1.5188 1.5209 -0.0040 0.1376  -0.3069 1019 CYS B CA  
5459 C C   . CYS B 769 ? 1.1225 1.5524 1.5665 0.0153  0.1612  -0.3197 1019 CYS B C   
5460 O O   . CYS B 769 ? 1.1088 1.5138 1.5455 0.0329  0.1684  -0.3317 1019 CYS B O   
5461 C CB  . CYS B 769 ? 1.1688 1.6025 1.6214 -0.0007 0.1132  -0.2958 1019 CYS B CB  
5462 S SG  . CYS B 769 ? 1.6225 2.0622 2.0658 -0.0273 0.0951  -0.2802 1019 CYS B SG  
5463 N N   . ASP B 770 ? 1.0973 1.5714 1.5812 0.0118  0.1758  -0.3171 1020 ASP B N   
5464 C CA  . ASP B 770 ? 1.1441 1.6492 1.6781 0.0318  0.1936  -0.3266 1020 ASP B CA  
5465 C C   . ASP B 770 ? 1.0307 1.5825 1.6320 0.0353  0.1773  -0.3215 1020 ASP B C   
5466 O O   . ASP B 770 ? 1.0278 1.5760 1.6299 0.0340  0.1477  -0.3147 1020 ASP B O   
5467 C CB  . ASP B 770 ? 1.1156 1.6371 1.6452 0.0270  0.2302  -0.3317 1020 ASP B CB  
5468 C CG  . ASP B 770 ? 1.1401 1.6908 1.6855 0.0050  0.2399  -0.3173 1020 ASP B CG  
5469 O OD1 . ASP B 770 ? 1.1138 1.6680 1.6692 -0.0094 0.2176  -0.3060 1020 ASP B OD1 
5470 O OD2 . ASP B 770 ? 1.0278 1.5967 1.5766 0.0033  0.2730  -0.3166 1020 ASP B OD2 
5471 N N   . SER B 771 ? 1.0928 1.6914 1.7520 0.0394  0.1966  -0.3266 1021 SER B N   
5472 C CA  . SER B 771 ? 0.9955 1.6460 1.7262 0.0406  0.1803  -0.3277 1021 SER B CA  
5473 C C   . SER B 771 ? 0.9305 1.5918 1.6693 0.0115  0.1725  -0.3193 1021 SER B C   
5474 O O   . SER B 771 ? 0.8935 1.5843 1.6732 0.0093  0.1474  -0.3223 1021 SER B O   
5475 C CB  . SER B 771 ? 0.9310 1.6314 1.7301 0.0521  0.2051  -0.3379 1021 SER B CB  
5476 O OG  . SER B 771 ? 0.8897 1.5903 1.6808 0.0368  0.2429  -0.3350 1021 SER B OG  
5477 N N   . ALA B 772 ? 0.9773 1.6161 1.6770 -0.0090 0.1934  -0.3093 1022 ALA B N   
5478 C CA  . ALA B 772 ? 0.8786 1.5280 1.5945 -0.0352 0.1948  -0.2990 1022 ALA B CA  
5479 C C   . ALA B 772 ? 0.8813 1.4861 1.5274 -0.0504 0.1841  -0.2847 1022 ALA B C   
5480 O O   . ALA B 772 ? 1.0087 1.6152 1.6659 -0.0659 0.1680  -0.2784 1022 ALA B O   
5481 C CB  . ALA B 772 ? 0.9316 1.6062 1.6819 -0.0454 0.2364  -0.2943 1022 ALA B CB  
5482 N N   . MET B 773 ? 0.9736 1.5413 1.5512 -0.0466 0.1923  -0.2818 1023 MET B N   
5483 C CA  . MET B 773 ? 1.0436 1.5766 1.5588 -0.0612 0.1841  -0.2690 1023 MET B CA  
5484 C C   . MET B 773 ? 1.0798 1.5727 1.5352 -0.0513 0.1706  -0.2768 1023 MET B C   
5485 O O   . MET B 773 ? 1.1544 1.6415 1.6082 -0.0339 0.1779  -0.2909 1023 MET B O   
5486 C CB  . MET B 773 ? 1.0241 1.5600 1.5160 -0.0727 0.2156  -0.2549 1023 MET B CB  
5487 C CG  . MET B 773 ? 0.9762 1.5359 1.5172 -0.0894 0.2279  -0.2401 1023 MET B CG  
5488 S SD  . MET B 773 ? 1.2221 1.7770 1.7229 -0.0985 0.2655  -0.2146 1023 MET B SD  
5489 C CE  . MET B 773 ? 1.1975 1.7686 1.7664 -0.1194 0.2736  -0.1981 1023 MET B CE  
5490 N N   . CYS B 774 ? 1.1551 1.6199 1.5659 -0.0632 0.1528  -0.2683 1024 CYS B N   
5491 C CA  . CYS B 774 ? 1.0903 1.5164 1.4469 -0.0596 0.1420  -0.2762 1024 CYS B CA  
5492 C C   . CYS B 774 ? 1.0728 1.4908 1.3750 -0.0682 0.1577  -0.2754 1024 CYS B C   
5493 O O   . CYS B 774 ? 0.9988 1.4287 1.2906 -0.0808 0.1639  -0.2586 1024 CYS B O   
5494 C CB  . CYS B 774 ? 1.0038 1.4073 1.3488 -0.0660 0.1118  -0.2687 1024 CYS B CB  
5495 S SG  . CYS B 774 ? 1.2834 1.6686 1.6464 -0.0451 0.0922  -0.2764 1024 CYS B SG  
5496 N N   . TYR B 775 ? 1.0854 1.4841 1.3532 -0.0598 0.1643  -0.2942 1025 TYR B N   
5497 C CA  . TYR B 775 ? 1.1666 1.5649 1.3802 -0.0639 0.1786  -0.3000 1025 TYR B CA  
5498 C C   . TYR B 775 ? 1.1998 1.5686 1.3654 -0.0717 0.1593  -0.3115 1025 TYR B C   
5499 O O   . TYR B 775 ? 1.2207 1.5952 1.3381 -0.0761 0.1648  -0.3170 1025 TYR B O   
5500 C CB  . TYR B 775 ? 1.1431 1.5503 1.3546 -0.0486 0.2064  -0.3191 1025 TYR B CB  
5501 C CG  . TYR B 775 ? 1.2155 1.6553 1.4817 -0.0406 0.2282  -0.3100 1025 TYR B CG  
5502 C CD1 . TYR B 775 ? 1.1106 1.5542 1.4312 -0.0276 0.2252  -0.3174 1025 TYR B CD1 
5503 C CD2 . TYR B 775 ? 1.2517 1.7204 1.5184 -0.0450 0.2529  -0.2929 1025 TYR B CD2 
5504 C CE1 . TYR B 775 ? 1.1162 1.5957 1.4938 -0.0211 0.2437  -0.3121 1025 TYR B CE1 
5505 C CE2 . TYR B 775 ? 1.1632 1.6627 1.4884 -0.0400 0.2754  -0.2860 1025 TYR B CE2 
5506 C CZ  . TYR B 775 ? 1.1044 1.6114 1.4870 -0.0291 0.2694  -0.2977 1025 TYR B CZ  
5507 O OH  . TYR B 775 ? 1.1612 1.7049 1.6088 -0.0249 0.2904  -0.2939 1025 TYR B OH  
5508 N N   . GLY B 776 ? 1.1227 1.4632 1.3011 -0.0727 0.1378  -0.3153 1026 GLY B N   
5509 C CA  . GLY B 776 ? 1.0442 1.3567 1.1878 -0.0823 0.1211  -0.3265 1026 GLY B CA  
5510 C C   . GLY B 776 ? 0.9966 1.2826 1.1638 -0.0834 0.1002  -0.3183 1026 GLY B C   
5511 O O   . GLY B 776 ? 0.9846 1.2733 1.1907 -0.0725 0.0979  -0.3086 1026 GLY B O   
5512 N N   . SER B 777 ? 0.9313 1.1949 1.0745 -0.0955 0.0850  -0.3226 1027 SER B N   
5513 C CA  . SER B 777 ? 0.8710 1.1069 1.0313 -0.0965 0.0681  -0.3131 1027 SER B CA  
5514 C C   . SER B 777 ? 0.9773 1.1819 1.1169 -0.1069 0.0622  -0.3313 1027 SER B C   
5515 O O   . SER B 777 ? 1.0174 1.2319 1.1259 -0.1186 0.0620  -0.3467 1027 SER B O   
5516 C CB  . SER B 777 ? 0.9501 1.2013 1.1172 -0.1053 0.0525  -0.2860 1027 SER B CB  
5517 O OG  . SER B 777 ? 1.0095 1.2611 1.1471 -0.1222 0.0423  -0.2833 1027 SER B OG  
5518 N N   . THR B 778 ? 1.0008 1.1697 1.1596 -0.1017 0.0579  -0.3293 1028 THR B N   
5519 C CA  . THR B 778 ? 0.9216 1.0561 1.0736 -0.1129 0.0549  -0.3451 1028 THR B CA  
5520 C C   . THR B 778 ? 0.9915 1.1033 1.1592 -0.1128 0.0432  -0.3213 1028 THR B C   
5521 O O   . THR B 778 ? 1.0342 1.1367 1.2230 -0.0944 0.0448  -0.3041 1028 THR B O   
5522 C CB  . THR B 778 ? 1.0763 1.1782 1.2388 -0.1035 0.0732  -0.3729 1028 THR B CB  
5523 O OG1 . THR B 778 ? 1.1577 1.2809 1.2981 -0.1060 0.0837  -0.4002 1028 THR B OG1 
5524 C CG2 . THR B 778 ? 0.9934 1.0531 1.1633 -0.1152 0.0729  -0.3870 1028 THR B CG2 
5525 N N   . THR B 779 ? 0.9890 1.0960 1.1460 -0.1314 0.0317  -0.3203 1029 THR B N   
5526 C CA  . THR B 779 ? 1.0449 1.1309 1.2136 -0.1327 0.0228  -0.2981 1029 THR B CA  
5527 C C   . THR B 779 ? 0.9752 1.0172 1.1563 -0.1395 0.0314  -0.3137 1029 THR B C   
5528 O O   . THR B 779 ? 1.0336 1.0751 1.2081 -0.1563 0.0328  -0.3425 1029 THR B O   
5529 C CB  . THR B 779 ? 0.8415 0.9542 0.9959 -0.1483 0.0059  -0.2827 1029 THR B CB  
5530 O OG1 . THR B 779 ? 0.8534 0.9542 1.0043 -0.1670 0.0012  -0.2952 1029 THR B OG1 
5531 C CG2 . THR B 779 ? 0.9068 1.0625 1.0422 -0.1520 0.0037  -0.2845 1029 THR B CG2 
5532 N N   . ALA B 780 ? 0.9549 0.9617 1.1552 -0.1257 0.0381  -0.2953 1030 ALA B N   
5533 C CA  . ALA B 780 ? 1.1490 1.1073 1.3689 -0.1304 0.0526  -0.3059 1030 ALA B CA  
5534 C C   . ALA B 780 ? 1.0149 0.9461 1.2464 -0.1182 0.0547  -0.2720 1030 ALA B C   
5535 O O   . ALA B 780 ? 0.9522 0.8988 1.1775 -0.0988 0.0471  -0.2446 1030 ALA B O   
5536 C CB  . ALA B 780 ? 1.0538 0.9830 1.2887 -0.1173 0.0741  -0.3278 1030 ALA B CB  
5537 N N   . ASN B 781 ? 1.1235 1.0159 1.3732 -0.1297 0.0660  -0.2756 1031 ASN B N   
5538 C CA  . ASN B 781 ? 1.1505 1.0107 1.4110 -0.1174 0.0744  -0.2426 1031 ASN B CA  
5539 C C   . ASN B 781 ? 1.1560 0.9699 1.4355 -0.0909 0.0995  -0.2347 1031 ASN B C   
5540 O O   . ASN B 781 ? 1.1837 0.9559 1.4887 -0.0987 0.1212  -0.2551 1031 ASN B O   
5541 C CB  . ASN B 781 ? 1.2411 1.0839 1.5175 -0.1435 0.0775  -0.2482 1031 ASN B CB  
5542 C CG  . ASN B 781 ? 1.2963 1.1253 1.5724 -0.1338 0.0795  -0.2094 1031 ASN B CG  
5543 O OD1 . ASN B 781 ? 1.3599 1.2001 1.6379 -0.1533 0.0714  -0.2063 1031 ASN B OD1 
5544 N ND2 . ASN B 781 ? 1.2908 1.0989 1.5631 -0.1013 0.0902  -0.1793 1031 ASN B ND2 
5545 N N   . LEU B 782 ? 1.1447 0.9673 1.4145 -0.0585 0.0971  -0.2061 1032 LEU B N   
5546 C CA  . LEU B 782 ? 1.0834 0.8688 1.3689 -0.0267 0.1195  -0.1936 1032 LEU B CA  
5547 C C   . LEU B 782 ? 1.2947 1.0267 1.5951 -0.0169 0.1418  -0.1664 1032 LEU B C   
5548 O O   . LEU B 782 ? 1.2940 1.0329 1.5806 -0.0134 0.1340  -0.1382 1032 LEU B O   
5549 C CB  . LEU B 782 ? 1.1082 0.9301 1.3798 0.0066  0.1063  -0.1723 1032 LEU B CB  
5550 C CG  . LEU B 782 ? 1.0113 0.8870 1.2737 -0.0004 0.0880  -0.1943 1032 LEU B CG  
5551 C CD1 . LEU B 782 ? 0.9968 0.9085 1.2564 0.0325  0.0766  -0.1744 1032 LEU B CD1 
5552 C CD2 . LEU B 782 ? 1.0379 0.8994 1.3134 -0.0101 0.1035  -0.2298 1032 LEU B CD2 
5553 N N   . VAL B 783 ? 1.2754 0.9525 1.6053 -0.0121 0.1725  -0.1749 1033 VAL B N   
5554 C CA  . VAL B 783 ? 1.2095 0.8274 1.5600 0.0007  0.2023  -0.1465 1033 VAL B CA  
5555 C C   . VAL B 783 ? 1.2443 0.8448 1.5919 0.0504  0.2167  -0.1112 1033 VAL B C   
5556 O O   . VAL B 783 ? 1.3262 0.9378 1.6763 0.0675  0.2162  -0.1237 1033 VAL B O   
5557 C CB  . VAL B 783 ? 1.3533 0.9178 1.7463 -0.0268 0.2308  -0.1790 1033 VAL B CB  
5558 C CG1 . VAL B 783 ? 1.2934 0.8473 1.7014 -0.0234 0.2412  -0.2141 1033 VAL B CG1 
5559 C CG2 . VAL B 783 ? 1.5313 1.0290 1.9528 -0.0131 0.2681  -0.1467 1033 VAL B CG2 
5560 N N   . ARG B 784 ? 1.3764 0.9524 1.7178 0.0759  0.2301  -0.0661 1034 ARG B N   
5561 C CA  . ARG B 784 ? 1.3886 0.9601 1.7179 0.1290  0.2382  -0.0255 1034 ARG B CA  
5562 C C   . ARG B 784 ? 1.4613 0.9944 1.8200 0.1496  0.2650  -0.0343 1034 ARG B C   
5563 O O   . ARG B 784 ? 1.5423 1.0170 1.9378 0.1321  0.2966  -0.0526 1034 ARG B O   
5564 C CB  . ARG B 784 ? 1.4273 0.9627 1.7495 0.1513  0.2595  0.0232  1034 ARG B CB  
5565 C CG  . ARG B 784 ? 1.4091 0.9528 1.7076 0.2108  0.2620  0.0699  1034 ARG B CG  
5566 C CD  . ARG B 784 ? 1.5029 1.0413 1.7733 0.2303  0.2674  0.1157  1034 ARG B CD  
5567 N NE  . ARG B 784 ? 1.6449 1.2217 1.8783 0.2849  0.2527  0.1526  1034 ARG B NE  
5568 C CZ  . ARG B 784 ? 1.7045 1.3050 1.8982 0.3068  0.2426  0.1863  1034 ARG B CZ  
5569 N NH1 . ARG B 784 ? 1.5536 1.1405 1.7416 0.2783  0.2478  0.1898  1034 ARG B NH1 
5570 N NH2 . ARG B 784 ? 1.6780 1.3200 1.8383 0.3580  0.2265  0.2144  1034 ARG B NH2 
5571 N N   . GLY B 785 ? 1.5220 1.0899 1.8682 0.1865  0.2526  -0.0236 1035 GLY B N   
5572 C CA  . GLY B 785 ? 1.4967 1.0359 1.8699 0.2105  0.2759  -0.0307 1035 GLY B CA  
5573 C C   . GLY B 785 ? 1.4871 1.0749 1.8616 0.1984  0.2547  -0.0717 1035 GLY B C   
5574 O O   . GLY B 785 ? 1.3197 0.9760 1.6701 0.2006  0.2200  -0.0731 1035 GLY B O   
5575 N N   . GLN B 786 ? 1.5682 1.1203 1.9727 0.1856  0.2775  -0.1062 1036 GLN B N   
5576 C CA  . GLN B 786 ? 1.4733 1.0652 1.8796 0.1748  0.2643  -0.1462 1036 GLN B CA  
5577 C C   . GLN B 786 ? 1.4550 1.0564 1.8572 0.1207  0.2538  -0.1934 1036 GLN B C   
5578 O O   . GLN B 786 ? 1.4125 0.9668 1.8317 0.0937  0.2717  -0.2093 1036 GLN B O   
5579 C CB  . GLN B 786 ? 1.4225 0.9735 1.8615 0.2007  0.2968  -0.1554 1036 GLN B CB  
5580 C CG  . GLN B 786 ? 1.4611 1.0429 1.9050 0.1868  0.2913  -0.2016 1036 GLN B CG  
5581 C CD  . GLN B 786 ? 1.6090 1.1525 2.0681 0.1450  0.3085  -0.2526 1036 GLN B CD  
5582 O OE1 . GLN B 786 ? 1.5548 1.1376 1.9980 0.1141  0.2907  -0.2912 1036 GLN B OE1 
5583 N NE2 . GLN B 786 ? 1.6096 1.0772 2.1005 0.1447  0.3442  -0.2534 1036 GLN B NE2 
5584 N N   . ASN B 787 ? 1.4177 1.0828 1.7995 0.1062  0.2254  -0.2151 1037 ASN B N   
5585 C CA  . ASN B 787 ? 1.3341 1.0191 1.7055 0.0611  0.2130  -0.2572 1037 ASN B CA  
5586 C C   . ASN B 787 ? 1.3415 1.0579 1.7117 0.0605  0.2117  -0.2909 1037 ASN B C   
5587 O O   . ASN B 787 ? 1.4496 1.2029 1.8179 0.0873  0.2040  -0.2774 1037 ASN B O   
5588 C CB  . ASN B 787 ? 1.2507 0.9852 1.5923 0.0409  0.1800  -0.2455 1037 ASN B CB  
5589 C CG  . ASN B 787 ? 1.2354 0.9397 1.5770 0.0345  0.1827  -0.2192 1037 ASN B CG  
5590 O OD1 . ASN B 787 ? 1.1889 0.8805 1.5334 0.0003  0.1825  -0.2377 1037 ASN B OD1 
5591 N ND2 . ASN B 787 ? 1.2020 0.8980 1.5405 0.0689  0.1856  -0.1757 1037 ASN B ND2 
5592 N N   . THR B 788 ? 1.2767 0.9816 1.6488 0.0303  0.2195  -0.3361 1038 THR B N   
5593 C CA  . THR B 788 ? 1.2629 0.9984 1.6276 0.0264  0.2201  -0.3718 1038 THR B CA  
5594 C C   . THR B 788 ? 1.2518 1.0357 1.5845 -0.0087 0.1950  -0.3934 1038 THR B C   
5595 O O   . THR B 788 ? 1.2822 1.0515 1.6119 -0.0389 0.1936  -0.4181 1038 THR B O   
5596 C CB  . THR B 788 ? 1.3293 1.0130 1.7193 0.0252  0.2521  -0.4098 1038 THR B CB  
5597 O OG1 . THR B 788 ? 1.3741 1.0034 1.7968 0.0580  0.2787  -0.3837 1038 THR B OG1 
5598 C CG2 . THR B 788 ? 1.3353 1.0514 1.7162 0.0300  0.2562  -0.4416 1038 THR B CG2 
5599 N N   . VAL B 789 ? 1.3154 1.1583 1.6278 -0.0038 0.1764  -0.3838 1039 VAL B N   
5600 C CA  . VAL B 789 ? 1.2875 1.1784 1.5686 -0.0314 0.1545  -0.3957 1039 VAL B CA  
5601 C C   . VAL B 789 ? 1.2672 1.1913 1.5351 -0.0307 0.1609  -0.4239 1039 VAL B C   
5602 O O   . VAL B 789 ? 1.2332 1.1649 1.5156 -0.0055 0.1729  -0.4195 1039 VAL B O   
5603 C CB  . VAL B 789 ? 1.1927 1.1232 1.4622 -0.0292 0.1297  -0.3581 1039 VAL B CB  
5604 C CG1 . VAL B 789 ? 1.0752 0.9738 1.3528 -0.0285 0.1252  -0.3306 1039 VAL B CG1 
5605 C CG2 . VAL B 789 ? 1.3536 1.3163 1.6342 -0.0006 0.1284  -0.3386 1039 VAL B CG2 
5606 N N   . HIS B 790 ? 1.2507 1.1968 1.4909 -0.0566 0.1535  -0.4523 1040 HIS B N   
5607 C CA  . HIS B 790 ? 1.2678 1.2494 1.4861 -0.0569 0.1599  -0.4779 1040 HIS B CA  
5608 C C   . HIS B 790 ? 1.2246 1.2627 1.4136 -0.0678 0.1398  -0.4603 1040 HIS B C   
5609 O O   . HIS B 790 ? 1.1067 1.1538 1.2802 -0.0876 0.1211  -0.4530 1040 HIS B O   
5610 C CB  . HIS B 790 ? 1.3590 1.3239 1.5645 -0.0740 0.1699  -0.5282 1040 HIS B CB  
5611 C CG  . HIS B 790 ? 1.4056 1.3101 1.6450 -0.0655 0.1941  -0.5501 1040 HIS B CG  
5612 N ND1 . HIS B 790 ? 1.4178 1.3095 1.6648 -0.0503 0.2188  -0.5790 1040 HIS B ND1 
5613 C CD2 . HIS B 790 ? 1.4243 1.2750 1.6947 -0.0692 0.2009  -0.5462 1040 HIS B CD2 
5614 C CE1 . HIS B 790 ? 1.3571 1.1879 1.6396 -0.0450 0.2395  -0.5926 1040 HIS B CE1 
5615 N NE2 . HIS B 790 ? 1.4267 1.2310 1.7246 -0.0565 0.2300  -0.5719 1040 HIS B NE2 
5616 N N   . ILE B 791 ? 1.3840 1.4592 1.5697 -0.0544 0.1461  -0.4526 1041 ILE B N   
5617 C CA  . ILE B 791 ? 1.2402 1.3657 1.4056 -0.0621 0.1334  -0.4327 1041 ILE B CA  
5618 C C   . ILE B 791 ? 1.2672 1.4242 1.4050 -0.0615 0.1480  -0.4548 1041 ILE B C   
5619 O O   . ILE B 791 ? 1.2241 1.3776 1.3735 -0.0449 0.1692  -0.4703 1041 ILE B O   
5620 C CB  . ILE B 791 ? 1.0829 1.2283 1.2776 -0.0468 0.1283  -0.3973 1041 ILE B CB  
5621 C CG1 . ILE B 791 ? 1.0444 1.1566 1.2643 -0.0387 0.1185  -0.3777 1041 ILE B CG1 
5622 C CG2 . ILE B 791 ? 0.9748 1.1626 1.1548 -0.0595 0.1150  -0.3760 1041 ILE B CG2 
5623 C CD1 . ILE B 791 ? 1.0764 1.2124 1.3250 -0.0204 0.1113  -0.3489 1041 ILE B CD1 
5624 N N   . VAL B 792 ? 1.2945 1.4835 1.3951 -0.0769 0.1382  -0.4541 1042 VAL B N   
5625 C CA  . VAL B 792 ? 1.2332 1.4578 1.2988 -0.0745 0.1519  -0.4686 1042 VAL B CA  
5626 C C   . VAL B 792 ? 1.2174 1.4820 1.2858 -0.0710 0.1536  -0.4326 1042 VAL B C   
5627 O O   . VAL B 792 ? 1.2589 1.5333 1.3282 -0.0816 0.1361  -0.4057 1042 VAL B O   
5628 C CB  . VAL B 792 ? 1.2349 1.4707 1.2536 -0.0906 0.1412  -0.4943 1042 VAL B CB  
5629 C CG1 . VAL B 792 ? 1.2959 1.5810 1.2706 -0.0873 0.1487  -0.4887 1042 VAL B CG1 
5630 C CG2 . VAL B 792 ? 1.2046 1.4101 1.2209 -0.0917 0.1501  -0.5427 1042 VAL B CG2 
5631 N N   . GLY B 793 ? 1.5035 1.7898 1.5776 -0.0564 0.1771  -0.4331 1043 GLY B N   
5632 C CA  . GLY B 793 ? 1.4343 1.7575 1.5203 -0.0537 0.1850  -0.4018 1043 GLY B CA  
5633 C C   . GLY B 793 ? 1.4685 1.8234 1.5248 -0.0454 0.2115  -0.4086 1043 GLY B C   
5634 O O   . GLY B 793 ? 1.6213 1.9730 1.6397 -0.0418 0.2206  -0.4398 1043 GLY B O   
5635 N N   . LYS B 794 ? 1.2073 1.5933 1.2822 -0.0422 0.2259  -0.3804 1044 LYS B N   
5636 C CA  . LYS B 794 ? 1.3635 1.7813 1.4113 -0.0332 0.2558  -0.3789 1044 LYS B CA  
5637 C C   . LYS B 794 ? 1.3757 1.8188 1.4753 -0.0291 0.2751  -0.3501 1044 LYS B C   
5638 O O   . LYS B 794 ? 1.3637 1.8160 1.4831 -0.0400 0.2658  -0.3212 1044 LYS B O   
5639 C CB  . LYS B 794 ? 1.3446 1.7803 1.3293 -0.0403 0.2508  -0.3707 1044 LYS B CB  
5640 C CG  . LYS B 794 ? 1.6086 2.0808 1.5693 -0.0302 0.2827  -0.3512 1044 LYS B CG  
5641 C CD  . LYS B 794 ? 1.5926 2.0837 1.5029 -0.0356 0.2741  -0.3282 1044 LYS B CD  
5642 C CE  . LYS B 794 ? 1.6152 2.1376 1.5189 -0.0260 0.3084  -0.2932 1044 LYS B CE  
5643 N NZ  . LYS B 794 ? 1.5583 2.0981 1.4155 -0.0276 0.3021  -0.2643 1044 LYS B NZ  
5644 N N   . GLY B 795 ? 1.3943 1.8495 1.5195 -0.0140 0.3028  -0.3599 1045 GLY B N   
5645 C CA  . GLY B 795 ? 1.3313 1.8148 1.5152 -0.0104 0.3240  -0.3382 1045 GLY B CA  
5646 C C   . GLY B 795 ? 1.3427 1.8249 1.5853 0.0038  0.3299  -0.3537 1045 GLY B C   
5647 O O   . GLY B 795 ? 1.3788 1.8328 1.6185 0.0114  0.3173  -0.3769 1045 GLY B O   
5648 N N   . GLY B 796 ? 1.3703 1.8848 1.6709 0.0079  0.3512  -0.3395 1046 GLY B N   
5649 C CA  . GLY B 796 ? 1.4460 1.9708 1.8116 0.0232  0.3569  -0.3508 1046 GLY B CA  
5650 C C   . GLY B 796 ? 1.5826 2.1407 1.9756 0.0357  0.3994  -0.3519 1046 GLY B C   
5651 O O   . GLY B 796 ? 1.6081 2.1708 1.9520 0.0391  0.4273  -0.3537 1046 GLY B O   
5652 N N   . HIS B 797 ? 1.6459 2.2315 2.1191 0.0439  0.4046  -0.3509 1047 HIS B N   
5653 C CA  . HIS B 797 ? 1.6759 2.2981 2.1917 0.0555  0.4456  -0.3514 1047 HIS B CA  
5654 C C   . HIS B 797 ? 1.7246 2.3587 2.3041 0.0763  0.4427  -0.3682 1047 HIS B C   
5655 O O   . HIS B 797 ? 1.7022 2.3192 2.2956 0.0814  0.4088  -0.3742 1047 HIS B O   
5656 C CB  . HIS B 797 ? 1.5575 2.2167 2.1230 0.0395  0.4624  -0.3256 1047 HIS B CB  
5657 C CG  . HIS B 797 ? 1.6421 2.2879 2.1496 0.0216  0.4636  -0.3038 1047 HIS B CG  
5658 N ND1 . HIS B 797 ? 1.6961 2.3253 2.1173 0.0263  0.4801  -0.3040 1047 HIS B ND1 
5659 C CD2 . HIS B 797 ? 1.5977 2.2460 2.1212 0.0012  0.4501  -0.2816 1047 HIS B CD2 
5660 C CE1 . HIS B 797 ? 1.6211 2.2451 2.0075 0.0113  0.4762  -0.2799 1047 HIS B CE1 
5661 N NE2 . HIS B 797 ? 1.5853 2.2178 2.0337 -0.0045 0.4595  -0.2654 1047 HIS B NE2 
5662 N N   . SER B 798 ? 1.8184 2.4833 2.4361 0.0908  0.4804  -0.3737 1048 SER B N   
5663 C CA  . SER B 798 ? 1.8632 2.5391 2.5328 0.1162  0.4846  -0.3914 1048 SER B CA  
5664 C C   . SER B 798 ? 2.0047 2.6992 2.7438 0.1191  0.4481  -0.3876 1048 SER B C   
5665 O O   . SER B 798 ? 2.1383 2.8765 2.9433 0.1081  0.4447  -0.3760 1048 SER B O   
5666 C CB  . SER B 798 ? 1.8596 2.5779 2.5756 0.1275  0.5321  -0.3927 1048 SER B CB  
5667 O OG  . SER B 798 ? 1.8511 2.5514 2.4959 0.1329  0.5665  -0.4006 1048 SER B OG  
5668 N N   . GLY B 799 ? 1.8249 2.4866 2.5492 0.1348  0.4219  -0.3981 1049 GLY B N   
5669 C CA  . GLY B 799 ? 1.7771 2.4529 2.5520 0.1428  0.3849  -0.3931 1049 GLY B CA  
5670 C C   . GLY B 799 ? 1.7084 2.3528 2.4429 0.1257  0.3456  -0.3826 1049 GLY B C   
5671 O O   . GLY B 799 ? 1.7937 2.4473 2.5601 0.1346  0.3137  -0.3779 1049 GLY B O   
5672 N N   . SER B 800 ? 1.7666 2.3776 2.4314 0.1035  0.3470  -0.3784 1050 SER B N   
5673 C CA  . SER B 800 ? 1.6594 2.2403 2.2852 0.0866  0.3121  -0.3683 1050 SER B CA  
5674 C C   . SER B 800 ? 1.5454 2.0743 2.1319 0.1009  0.2967  -0.3784 1050 SER B C   
5675 O O   . SER B 800 ? 1.5454 2.0323 2.0690 0.0945  0.3029  -0.3885 1050 SER B O   
5676 C CB  . SER B 800 ? 1.6227 2.1918 2.1935 0.0603  0.3202  -0.3591 1050 SER B CB  
5677 O OG  . SER B 800 ? 1.5866 2.1341 2.1013 0.0643  0.3469  -0.3719 1050 SER B OG  
5678 N N   . LYS B 801 ? 1.3454 1.8792 1.9728 0.1217  0.2772  -0.3760 1051 LYS B N   
5679 C CA  . LYS B 801 ? 1.1665 1.6491 1.7661 0.1372  0.2642  -0.3799 1051 LYS B CA  
5680 C C   . LYS B 801 ? 1.2296 1.6772 1.7802 0.1154  0.2376  -0.3702 1051 LYS B C   
5681 O O   . LYS B 801 ? 1.1771 1.6438 1.7446 0.1083  0.2111  -0.3548 1051 LYS B O   
5682 C CB  . LYS B 801 ? 1.0936 1.5964 1.7492 0.1686  0.2503  -0.3734 1051 LYS B CB  
5683 C CG  . LYS B 801 ? 1.1373 1.6803 1.8498 0.1928  0.2750  -0.3824 1051 LYS B CG  
5684 C CD  . LYS B 801 ? 1.0098 1.5692 1.7705 0.2293  0.2594  -0.3749 1051 LYS B CD  
5685 C CE  . LYS B 801 ? 1.0271 1.6308 1.8498 0.2551  0.2838  -0.3840 1051 LYS B CE  
5686 N NZ  . LYS B 801 ? 1.0365 1.6565 1.9032 0.2961  0.2690  -0.3751 1051 LYS B NZ  
5687 N N   . PHE B 802 ? 1.2032 1.6025 1.6954 0.1046  0.2445  -0.3817 1052 PHE B N   
5688 C CA  . PHE B 802 ? 1.0276 1.3955 1.4758 0.0834  0.2213  -0.3740 1052 PHE B CA  
5689 C C   . PHE B 802 ? 1.0707 1.4080 1.5276 0.0980  0.1998  -0.3640 1052 PHE B C   
5690 O O   . PHE B 802 ? 1.1790 1.4898 1.6481 0.1219  0.2096  -0.3708 1052 PHE B O   
5691 C CB  . PHE B 802 ? 1.0288 1.3610 1.4174 0.0683  0.2340  -0.3932 1052 PHE B CB  
5692 C CG  . PHE B 802 ? 1.1165 1.4784 1.4857 0.0577  0.2565  -0.4001 1052 PHE B CG  
5693 C CD1 . PHE B 802 ? 1.1076 1.4917 1.4569 0.0356  0.2493  -0.3847 1052 PHE B CD1 
5694 C CD2 . PHE B 802 ? 1.2199 1.5867 1.5902 0.0722  0.2874  -0.4202 1052 PHE B CD2 
5695 C CE1 . PHE B 802 ? 1.2288 1.6392 1.5579 0.0294  0.2734  -0.3859 1052 PHE B CE1 
5696 C CE2 . PHE B 802 ? 1.1802 1.5752 1.5285 0.0654  0.3110  -0.4238 1052 PHE B CE2 
5697 C CZ  . PHE B 802 ? 1.3421 1.7589 1.6689 0.0446  0.3045  -0.4050 1052 PHE B CZ  
5698 N N   . MET B 803 ? 1.1080 1.4482 1.5584 0.0853  0.1727  -0.3463 1053 MET B N   
5699 C CA  . MET B 803 ? 1.1397 1.4543 1.5932 0.0994  0.1523  -0.3322 1053 MET B CA  
5700 C C   . MET B 803 ? 1.0933 1.3831 1.5069 0.0743  0.1334  -0.3232 1053 MET B C   
5701 O O   . MET B 803 ? 0.9864 1.2872 1.3766 0.0481  0.1325  -0.3254 1053 MET B O   
5702 C CB  . MET B 803 ? 0.9968 1.3583 1.4997 0.1208  0.1357  -0.3176 1053 MET B CB  
5703 C CG  . MET B 803 ? 1.0724 1.4929 1.6036 0.1044  0.1300  -0.3167 1053 MET B CG  
5704 S SD  . MET B 803 ? 1.1768 1.6623 1.7764 0.1306  0.1111  -0.3101 1053 MET B SD  
5705 C CE  . MET B 803 ? 1.0763 1.6206 1.7142 0.1033  0.1180  -0.3174 1053 MET B CE  
5706 N N   . CYS B 804 ? 1.0404 1.2965 1.4470 0.0847  0.1204  -0.3109 1054 CYS B N   
5707 C CA  . CYS B 804 ? 1.0981 1.3290 1.4717 0.0641  0.1036  -0.3010 1054 CYS B CA  
5708 C C   . CYS B 804 ? 1.1819 1.4433 1.5706 0.0691  0.0781  -0.2798 1054 CYS B C   
5709 O O   . CYS B 804 ? 1.1768 1.4509 1.5909 0.0976  0.0708  -0.2689 1054 CYS B O   
5710 C CB  . CYS B 804 ? 1.2867 1.4559 1.6429 0.0701  0.1106  -0.3022 1054 CYS B CB  
5711 S SG  . CYS B 804 ? 1.2944 1.4284 1.6398 0.0667  0.1409  -0.3351 1054 CYS B SG  
5712 N N   . CYS B 805 ? 1.1832 1.4583 1.5557 0.0434  0.0646  -0.2748 1055 CYS B N   
5713 C CA  . CYS B 805 ? 1.0925 1.3995 1.4791 0.0441  0.0413  -0.2603 1055 CYS B CA  
5714 C C   . CYS B 805 ? 1.0947 1.3720 1.4471 0.0279  0.0276  -0.2485 1055 CYS B C   
5715 O O   . CYS B 805 ? 1.0983 1.3593 1.4240 0.0025  0.0319  -0.2529 1055 CYS B O   
5716 C CB  . CYS B 805 ? 1.0737 1.4316 1.4859 0.0285  0.0411  -0.2660 1055 CYS B CB  
5717 S SG  . CYS B 805 ? 1.2000 1.5997 1.6603 0.0447  0.0604  -0.2799 1055 CYS B SG  
5718 N N   . HIS B 806 ? 1.1074 1.3808 1.4601 0.0449  0.0116  -0.2330 1056 HIS B N   
5719 C CA  . HIS B 806 ? 1.0325 1.2860 1.3582 0.0323  -0.0021 -0.2197 1056 HIS B CA  
5720 C C   . HIS B 806 ? 0.9711 1.2710 1.3118 0.0256  -0.0214 -0.2173 1056 HIS B C   
5721 O O   . HIS B 806 ? 1.0181 1.3489 1.3788 0.0478  -0.0355 -0.2135 1056 HIS B O   
5722 C CB  . HIS B 806 ? 0.9644 1.1825 1.2780 0.0567  -0.0036 -0.2028 1056 HIS B CB  
5723 C CG  . HIS B 806 ? 0.9898 1.1842 1.2760 0.0448  -0.0132 -0.1883 1056 HIS B CG  
5724 N ND1 . HIS B 806 ? 0.9102 1.1100 1.1896 0.0653  -0.0272 -0.1694 1056 HIS B ND1 
5725 C CD2 . HIS B 806 ? 0.9887 1.1572 1.2530 0.0163  -0.0105 -0.1902 1056 HIS B CD2 
5726 C CE1 . HIS B 806 ? 0.9812 1.1563 1.2363 0.0490  -0.0303 -0.1597 1056 HIS B CE1 
5727 N NE2 . HIS B 806 ? 0.8781 1.0348 1.1263 0.0188  -0.0209 -0.1721 1056 HIS B NE2 
5728 N N   . ASP B 807 ? 0.9844 1.2906 1.3170 -0.0037 -0.0217 -0.2207 1057 ASP B N   
5729 C CA  . ASP B 807 ? 0.9444 1.2920 1.2990 -0.0148 -0.0338 -0.2226 1057 ASP B CA  
5730 C C   . ASP B 807 ? 1.0042 1.3992 1.4053 -0.0053 -0.0305 -0.2354 1057 ASP B C   
5731 O O   . ASP B 807 ? 0.9863 1.3959 1.4033 -0.0203 -0.0148 -0.2434 1057 ASP B O   
5732 C CB  . ASP B 807 ? 0.8622 1.2139 1.2094 -0.0055 -0.0554 -0.2127 1057 ASP B CB  
5733 C CG  . ASP B 807 ? 0.8913 1.2051 1.2010 -0.0216 -0.0573 -0.2006 1057 ASP B CG  
5734 O OD1 . ASP B 807 ? 0.7349 1.0279 1.0287 -0.0428 -0.0454 -0.2017 1057 ASP B OD1 
5735 O OD2 . ASP B 807 ? 0.9023 1.2107 1.1982 -0.0115 -0.0707 -0.1902 1057 ASP B OD2 
5736 N N   . THR B 808 ? 0.9430 1.3653 1.3672 0.0211  -0.0446 -0.2366 1058 THR B N   
5737 C CA  . THR B 808 ? 0.9321 1.4048 1.4072 0.0332  -0.0432 -0.2503 1058 THR B CA  
5738 C C   . THR B 808 ? 1.0078 1.4828 1.4916 0.0691  -0.0426 -0.2481 1058 THR B C   
5739 O O   . THR B 808 ? 0.9736 1.4888 1.5011 0.0808  -0.0378 -0.2595 1058 THR B O   
5740 C CB  . THR B 808 ? 0.8717 1.3971 1.3835 0.0306  -0.0642 -0.2603 1058 THR B CB  
5741 O OG1 . THR B 808 ? 0.9984 1.5174 1.4831 0.0452  -0.0870 -0.2512 1058 THR B OG1 
5742 C CG2 . THR B 808 ? 0.7666 1.2972 1.2904 -0.0048 -0.0562 -0.2658 1058 THR B CG2 
5743 N N   . LYS B 809 ? 1.0153 1.4484 1.4629 0.0878  -0.0447 -0.2325 1059 LYS B N   
5744 C CA  . LYS B 809 ? 0.9720 1.3988 1.4262 0.1246  -0.0399 -0.2257 1059 LYS B CA  
5745 C C   . LYS B 809 ? 1.0458 1.4399 1.4994 0.1201  -0.0113 -0.2331 1059 LYS B C   
5746 O O   . LYS B 809 ? 1.1406 1.4806 1.5594 0.1058  0.0022  -0.2301 1059 LYS B O   
5747 C CB  . LYS B 809 ? 1.0022 1.3901 1.4189 0.1457  -0.0470 -0.2032 1059 LYS B CB  
5748 C CG  . LYS B 809 ? 1.0127 1.4366 1.4415 0.1883  -0.0651 -0.1923 1059 LYS B CG  
5749 C CD  . LYS B 809 ? 1.0347 1.4084 1.4237 0.2130  -0.0615 -0.1644 1059 LYS B CD  
5750 C CE  . LYS B 809 ? 1.1628 1.5776 1.5520 0.2566  -0.0834 -0.1496 1059 LYS B CE  
5751 N NZ  . LYS B 809 ? 1.0913 1.5540 1.4765 0.2461  -0.1121 -0.1586 1059 LYS B NZ  
5752 N N   . CYS B 810 ? 0.9593 1.3887 1.4532 0.1322  -0.0019 -0.2451 1060 CYS B N   
5753 C CA  . CYS B 810 ? 1.0332 1.4371 1.5285 0.1321  0.0264  -0.2549 1060 CYS B CA  
5754 C C   . CYS B 810 ? 1.0953 1.4903 1.6061 0.1728  0.0338  -0.2485 1060 CYS B C   
5755 O O   . CYS B 810 ? 1.0877 1.5207 1.6231 0.2026  0.0167  -0.2398 1060 CYS B O   
5756 C CB  . CYS B 810 ? 0.9394 1.3866 1.4694 0.1157  0.0388  -0.2723 1060 CYS B CB  
5757 S SG  . CYS B 810 ? 1.3030 1.7649 1.8238 0.0721  0.0346  -0.2758 1060 CYS B SG  
5758 N N   . SER B 811 ? 1.1005 1.4464 1.5972 0.1754  0.0596  -0.2537 1061 SER B N   
5759 C CA  . SER B 811 ? 1.1797 1.5081 1.6927 0.2144  0.0724  -0.2470 1061 SER B CA  
5760 C C   . SER B 811 ? 1.1601 1.5495 1.7259 0.2363  0.0745  -0.2557 1061 SER B C   
5761 O O   . SER B 811 ? 1.1406 1.5692 1.7286 0.2160  0.0793  -0.2726 1061 SER B O   
5762 C CB  . SER B 811 ? 1.1785 1.4404 1.6703 0.2080  0.1023  -0.2576 1061 SER B CB  
5763 O OG  . SER B 811 ? 1.1984 1.4753 1.7025 0.1943  0.1218  -0.2818 1061 SER B OG  
5764 N N   . SER B 812 ? 1.1727 1.5712 1.7610 0.2800  0.0726  -0.2419 1062 SER B N   
5765 C CA  . SER B 812 ? 1.1283 1.5910 1.7726 0.3053  0.0722  -0.2492 1062 SER B CA  
5766 C C   . SER B 812 ? 1.1849 1.6364 1.8474 0.2996  0.1057  -0.2694 1062 SER B C   
5767 O O   . SER B 812 ? 1.1795 1.6884 1.8865 0.2979  0.1095  -0.2837 1062 SER B O   
5768 C CB  . SER B 812 ? 1.0550 1.5285 1.7149 0.3582  0.0629  -0.2269 1062 SER B CB  
5769 O OG  . SER B 812 ? 1.1700 1.5703 1.8100 0.3781  0.0896  -0.2153 1062 SER B OG  
5770 N N   . THR B 813 ? 1.4013 1.7809 2.0321 0.2961  0.1314  -0.2729 1063 THR B N   
5771 C CA  . THR B 813 ? 1.4278 1.7927 2.0694 0.2930  0.1645  -0.2948 1063 THR B CA  
5772 C C   . THR B 813 ? 1.3222 1.6866 1.9376 0.2477  0.1725  -0.3148 1063 THR B C   
5773 O O   . THR B 813 ? 1.3004 1.6441 1.8767 0.2185  0.1592  -0.3116 1063 THR B O   
5774 C CB  . THR B 813 ? 1.5002 1.7885 2.1231 0.3101  0.1899  -0.2947 1063 THR B CB  
5775 O OG1 . THR B 813 ? 1.5624 1.7936 2.1355 0.2748  0.1952  -0.3046 1063 THR B OG1 
5776 C CG2 . THR B 813 ? 1.4575 1.7300 2.0881 0.3507  0.1796  -0.2647 1063 THR B CG2 
5777 N N   . GLY B 814 ? 1.2024 1.5914 1.8394 0.2447  0.1957  -0.3336 1064 GLY B N   
5778 C CA  . GLY B 814 ? 1.1495 1.5401 1.7595 0.2081  0.2083  -0.3502 1064 GLY B CA  
5779 C C   . GLY B 814 ? 1.1422 1.5079 1.7437 0.2122  0.2443  -0.3732 1064 GLY B C   
5780 O O   . GLY B 814 ? 1.2724 1.6508 1.9124 0.2415  0.2620  -0.3782 1064 GLY B O   
5781 N N   . LEU B 815 ? 1.1484 1.4815 1.6987 0.1842  0.2547  -0.3885 1065 LEU B N   
5782 C CA  . LEU B 815 ? 1.1891 1.4939 1.7189 0.1855  0.2871  -0.4157 1065 LEU B CA  
5783 C C   . LEU B 815 ? 1.1906 1.5274 1.6976 0.1616  0.3010  -0.4269 1065 LEU B C   
5784 O O   . LEU B 815 ? 1.1762 1.5216 1.6530 0.1343  0.2854  -0.4187 1065 LEU B O   
5785 C CB  . LEU B 815 ? 1.1927 1.4269 1.6787 0.1771  0.2886  -0.4291 1065 LEU B CB  
5786 C CG  . LEU B 815 ? 1.2143 1.3986 1.7210 0.2068  0.3007  -0.4313 1065 LEU B CG  
5787 C CD1 . LEU B 815 ? 1.1938 1.3983 1.7453 0.2371  0.2838  -0.3996 1065 LEU B CD1 
5788 C CD2 . LEU B 815 ? 1.2777 1.3951 1.7471 0.1903  0.2985  -0.4418 1065 LEU B CD2 
5789 N N   . VAL B 816 ? 1.2809 1.6349 1.8020 0.1742  0.3325  -0.4438 1066 VAL B N   
5790 C CA  . VAL B 816 ? 1.3556 1.7386 1.8520 0.1570  0.3525  -0.4528 1066 VAL B CA  
5791 C C   . VAL B 816 ? 1.4357 1.7763 1.8682 0.1475  0.3682  -0.4818 1066 VAL B C   
5792 O O   . VAL B 816 ? 1.4850 1.7782 1.9097 0.1589  0.3741  -0.5014 1066 VAL B O   
5793 C CB  . VAL B 816 ? 1.2608 1.6929 1.8090 0.1757  0.3806  -0.4542 1066 VAL B CB  
5794 C CG1 . VAL B 816 ? 1.2681 1.7509 1.8842 0.1819  0.3619  -0.4304 1066 VAL B CG1 
5795 C CG2 . VAL B 816 ? 1.2209 1.6278 1.7854 0.2056  0.4053  -0.4752 1066 VAL B CG2 
5796 N N   . ALA B 817 ? 1.4596 1.8189 1.8471 0.1273  0.3759  -0.4855 1067 ALA B N   
5797 C CA  . ALA B 817 ? 1.5071 1.8392 1.8290 0.1177  0.3872  -0.5153 1067 ALA B CA  
5798 C C   . ALA B 817 ? 1.5646 1.9143 1.8807 0.1338  0.4271  -0.5375 1067 ALA B C   
5799 O O   . ALA B 817 ? 1.5218 1.8951 1.8909 0.1546  0.4467  -0.5320 1067 ALA B O   
5800 C CB  . ALA B 817 ? 1.5388 1.8831 1.8083 0.0902  0.3701  -0.5045 1067 ALA B CB  
5801 N N   . ALA B 818 ? 1.6978 2.0399 1.9489 0.1254  0.4391  -0.5642 1068 ALA B N   
5802 C CA  . ALA B 818 ? 1.8719 2.2280 2.1035 0.1408  0.4775  -0.5898 1068 ALA B CA  
5803 C C   . ALA B 818 ? 1.9021 2.3053 2.0929 0.1321  0.4915  -0.5745 1068 ALA B C   
5804 O O   . ALA B 818 ? 1.8895 2.3136 2.0781 0.1154  0.4731  -0.5422 1068 ALA B O   
5805 C CB  . ALA B 818 ? 1.9006 2.2122 2.0885 0.1420  0.4833  -0.6379 1068 ALA B CB  
5806 N N   . ALA B 819 ? 1.8696 2.2885 2.0276 0.1456  0.5274  -0.5970 1069 ALA B N   
5807 C CA  . ALA B 819 ? 1.8327 2.2946 1.9456 0.1439  0.5495  -0.5831 1069 ALA B CA  
5808 C C   . ALA B 819 ? 1.9461 2.4026 1.9693 0.1300  0.5335  -0.6000 1069 ALA B C   
5809 O O   . ALA B 819 ? 1.9317 2.3533 1.9255 0.1261  0.5181  -0.6387 1069 ALA B O   
5810 C CB  . ALA B 819 ? 1.8206 2.3032 1.9356 0.1680  0.5972  -0.6000 1069 ALA B CB  
5811 N N   . PRO B 820 ? 1.9603 2.4526 1.9417 0.1229  0.5373  -0.5717 1070 PRO B N   
5812 C CA  . PRO B 820 ? 1.9353 2.4323 1.8312 0.1125  0.5194  -0.5828 1070 PRO B CA  
5813 C C   . PRO B 820 ? 1.9365 2.4290 1.7669 0.1244  0.5331  -0.6363 1070 PRO B C   
5814 O O   . PRO B 820 ? 1.9960 2.4938 1.8344 0.1442  0.5690  -0.6548 1070 PRO B O   
5815 C CB  . PRO B 820 ? 1.9409 2.4822 1.8132 0.1136  0.5377  -0.5378 1070 PRO B CB  
5816 C CG  . PRO B 820 ? 1.8478 2.3971 1.8086 0.1113  0.5468  -0.4997 1070 PRO B CG  
5817 C CD  . PRO B 820 ? 1.8610 2.3923 1.8794 0.1248  0.5595  -0.5259 1070 PRO B CD  
5818 N N   . SER B 833 ? 1.3772 1.8536 1.1409 -0.1164 0.0644  -0.4162 1083 SER B N   
5819 C CA  . SER B 833 ? 1.5657 2.0210 1.3606 -0.1350 0.0381  -0.4189 1083 SER B CA  
5820 C C   . SER B 833 ? 1.6433 2.1224 1.4304 -0.1365 0.0243  -0.3776 1083 SER B C   
5821 O O   . SER B 833 ? 1.5678 2.0747 1.3294 -0.1229 0.0370  -0.3446 1083 SER B O   
5822 C CB  . SER B 833 ? 1.4089 1.8125 1.2630 -0.1420 0.0432  -0.4135 1083 SER B CB  
5823 O OG  . SER B 833 ? 1.3636 1.7639 1.2409 -0.1364 0.0538  -0.3691 1083 SER B OG  
5824 N N   . ASP B 834 ? 1.7264 2.1927 1.5384 -0.1522 0.0011  -0.3783 1084 ASP B N   
5825 C CA  . ASP B 834 ? 1.7461 2.2313 1.5569 -0.1543 -0.0131 -0.3417 1084 ASP B CA  
5826 C C   . ASP B 834 ? 1.7451 2.1902 1.6084 -0.1674 -0.0200 -0.3236 1084 ASP B C   
5827 O O   . ASP B 834 ? 1.6015 2.0464 1.4781 -0.1791 -0.0400 -0.3234 1084 ASP B O   
5828 C CB  . ASP B 834 ? 1.8222 2.3488 1.6011 -0.1575 -0.0376 -0.3625 1084 ASP B CB  
5829 C CG  . ASP B 834 ? 1.8973 2.4088 1.6950 -0.1748 -0.0528 -0.4151 1084 ASP B CG  
5830 O OD1 . ASP B 834 ? 1.7749 2.2365 1.6161 -0.1853 -0.0461 -0.4249 1084 ASP B OD1 
5831 O OD2 . ASP B 834 ? 1.9729 2.5238 1.7434 -0.1770 -0.0708 -0.4472 1084 ASP B OD2 
5832 N N   . LYS B 835 ? 1.5824 1.9965 1.4767 -0.1643 -0.0033 -0.3089 1085 LYS B N   
5833 C CA  . LYS B 835 ? 1.3407 1.7192 1.2802 -0.1726 -0.0085 -0.2925 1085 LYS B CA  
5834 C C   . LYS B 835 ? 1.1524 1.5339 1.1071 -0.1662 0.0028  -0.2522 1085 LYS B C   
5835 O O   . LYS B 835 ? 1.2541 1.6538 1.1961 -0.1554 0.0215  -0.2403 1085 LYS B O   
5836 C CB  . LYS B 835 ? 1.2954 1.6345 1.2643 -0.1735 -0.0014 -0.3156 1085 LYS B CB  
5837 C CG  . LYS B 835 ? 1.3015 1.6372 1.2551 -0.1753 0.0004  -0.3604 1085 LYS B CG  
5838 C CD  . LYS B 835 ? 1.5663 1.9058 1.5168 -0.1906 -0.0199 -0.3835 1085 LYS B CD  
5839 C CE  . LYS B 835 ? 1.5975 1.9350 1.5371 -0.1943 -0.0174 -0.4343 1085 LYS B CE  
5840 N NZ  . LYS B 835 ? 1.5488 1.9279 1.4400 -0.1824 -0.0107 -0.4478 1085 LYS B NZ  
5841 N N   . ILE B 836 ? 1.0923 1.4559 1.0769 -0.1731 -0.0066 -0.2324 1086 ILE B N   
5842 C CA  . ILE B 836 ? 1.0705 1.4340 1.0777 -0.1700 0.0025  -0.1997 1086 ILE B CA  
5843 C C   . ILE B 836 ? 0.9685 1.3015 1.0160 -0.1713 0.0014  -0.2020 1086 ILE B C   
5844 O O   . ILE B 836 ? 0.9619 1.2723 1.0206 -0.1774 -0.0124 -0.2094 1086 ILE B O   
5845 C CB  . ILE B 836 ? 0.9911 1.3664 0.9949 -0.1742 -0.0074 -0.1730 1086 ILE B CB  
5846 C CG1 . ILE B 836 ? 1.0898 1.5012 1.0503 -0.1684 -0.0085 -0.1691 1086 ILE B CG1 
5847 C CG2 . ILE B 836 ? 0.8395 1.2116 0.8717 -0.1721 0.0051  -0.1435 1086 ILE B CG2 
5848 C CD1 . ILE B 836 ? 1.2017 1.6280 1.1589 -0.1683 -0.0160 -0.1390 1086 ILE B CD1 
5849 N N   . PHE B 837 ? 0.8324 1.1675 0.9024 -0.1643 0.0167  -0.1950 1087 PHE B N   
5850 C CA  . PHE B 837 ? 0.8134 1.1295 0.9207 -0.1613 0.0147  -0.1975 1087 PHE B CA  
5851 C C   . PHE B 837 ? 0.9573 1.2835 1.0949 -0.1622 0.0195  -0.1757 1087 PHE B C   
5852 O O   . PHE B 837 ? 0.9253 1.2713 1.0656 -0.1612 0.0363  -0.1635 1087 PHE B O   
5853 C CB  . PHE B 837 ? 0.8828 1.1960 0.9984 -0.1509 0.0272  -0.2173 1087 PHE B CB  
5854 C CG  . PHE B 837 ? 0.8123 1.1064 0.9601 -0.1437 0.0215  -0.2224 1087 PHE B CG  
5855 C CD1 . PHE B 837 ? 0.7527 1.0175 0.8974 -0.1432 0.0106  -0.2325 1087 PHE B CD1 
5856 C CD2 . PHE B 837 ? 0.7300 1.0377 0.9133 -0.1361 0.0280  -0.2167 1087 PHE B CD2 
5857 C CE1 . PHE B 837 ? 0.7449 0.9932 0.9146 -0.1317 0.0070  -0.2325 1087 PHE B CE1 
5858 C CE2 . PHE B 837 ? 0.7446 1.0418 0.9542 -0.1254 0.0203  -0.2209 1087 PHE B CE2 
5859 C CZ  . PHE B 837 ? 0.7633 1.0300 0.9628 -0.1214 0.0101  -0.2266 1087 PHE B CZ  
5860 N N   . ASP B 838 ? 0.8899 1.2022 1.0513 -0.1638 0.0066  -0.1718 1088 ASP B N   
5861 C CA  . ASP B 838 ? 0.8090 1.1304 1.0026 -0.1665 0.0086  -0.1573 1088 ASP B CA  
5862 C C   . ASP B 838 ? 0.7801 1.0912 0.9991 -0.1607 -0.0045 -0.1654 1088 ASP B C   
5863 O O   . ASP B 838 ? 0.8637 1.1593 1.0772 -0.1624 -0.0191 -0.1612 1088 ASP B O   
5864 C CB  . ASP B 838 ? 0.8454 1.1665 1.0287 -0.1753 0.0046  -0.1379 1088 ASP B CB  
5865 C CG  . ASP B 838 ? 0.8098 1.1393 1.0285 -0.1794 0.0129  -0.1246 1088 ASP B CG  
5866 O OD1 . ASP B 838 ? 0.7356 1.0702 0.9902 -0.1772 0.0133  -0.1344 1088 ASP B OD1 
5867 O OD2 . ASP B 838 ? 0.8109 1.1433 1.0244 -0.1843 0.0191  -0.1053 1088 ASP B OD2 
5868 N N   . ASP B 839 ? 0.6945 1.0177 0.9410 -0.1517 0.0013  -0.1761 1089 ASP B N   
5869 C CA  . ASP B 839 ? 0.7390 1.0619 1.0097 -0.1415 -0.0117 -0.1834 1089 ASP B CA  
5870 C C   . ASP B 839 ? 0.7019 1.0512 1.0166 -0.1436 -0.0107 -0.1846 1089 ASP B C   
5871 O O   . ASP B 839 ? 0.7847 1.1461 1.1239 -0.1327 -0.0217 -0.1945 1089 ASP B O   
5872 C CB  . ASP B 839 ? 0.7514 1.0708 1.0238 -0.1259 -0.0092 -0.1971 1089 ASP B CB  
5873 C CG  . ASP B 839 ? 0.8150 1.1611 1.1152 -0.1218 0.0074  -0.2052 1089 ASP B CG  
5874 O OD1 . ASP B 839 ? 0.8898 1.2530 1.2226 -0.1089 0.0040  -0.2139 1089 ASP B OD1 
5875 O OD2 . ASP B 839 ? 1.0086 1.3618 1.2984 -0.1299 0.0244  -0.2021 1089 ASP B OD2 
5876 N N   . GLY B 840 ? 0.7503 1.1100 1.0775 -0.1565 0.0029  -0.1753 1090 GLY B N   
5877 C CA  . GLY B 840 ? 0.7596 1.1413 1.1359 -0.1626 0.0070  -0.1788 1090 GLY B CA  
5878 C C   . GLY B 840 ? 0.8443 1.2551 1.2648 -0.1583 0.0191  -0.1923 1090 GLY B C   
5879 O O   . GLY B 840 ? 0.9370 1.3705 1.4079 -0.1637 0.0201  -0.2017 1090 GLY B O   
5880 N N   . ALA B 841 ? 0.8844 1.2969 1.2916 -0.1492 0.0290  -0.1959 1091 ALA B N   
5881 C CA  . ALA B 841 ? 0.8961 1.3382 1.3477 -0.1436 0.0423  -0.2084 1091 ALA B CA  
5882 C C   . ALA B 841 ? 0.8643 1.3211 1.3466 -0.1571 0.0711  -0.1992 1091 ALA B C   
5883 O O   . ALA B 841 ? 0.8742 1.3150 1.3257 -0.1649 0.0849  -0.1802 1091 ALA B O   
5884 C CB  . ALA B 841 ? 0.8971 1.3335 1.3242 -0.1291 0.0482  -0.2145 1091 ALA B CB  
5885 N N   . PRO B 842 ? 0.8505 1.3393 1.3962 -0.1591 0.0817  -0.2114 1092 PRO B N   
5886 C CA  . PRO B 842 ? 0.8884 1.3889 1.4710 -0.1723 0.1149  -0.2009 1092 PRO B CA  
5887 C C   . PRO B 842 ? 0.9639 1.4590 1.5115 -0.1664 0.1425  -0.1866 1092 PRO B C   
5888 O O   . PRO B 842 ? 1.0498 1.5463 1.5736 -0.1525 0.1399  -0.1958 1092 PRO B O   
5889 C CB  . PRO B 842 ? 0.8493 1.3899 1.5129 -0.1742 0.1172  -0.2235 1092 PRO B CB  
5890 C CG  . PRO B 842 ? 0.6678 1.2178 1.3335 -0.1640 0.0789  -0.2439 1092 PRO B CG  
5891 C CD  . PRO B 842 ? 0.8914 1.4102 1.4827 -0.1494 0.0634  -0.2350 1092 PRO B CD  
5892 N N   . GLU B 843 ? 1.0923 1.5808 1.6357 -0.1753 0.1706  -0.1636 1093 GLU B N   
5893 C CA  . GLU B 843 ? 1.2026 1.6900 1.7077 -0.1678 0.1991  -0.1478 1093 GLU B CA  
5894 C C   . GLU B 843 ? 1.1523 1.6681 1.7119 -0.1662 0.2307  -0.1531 1093 GLU B C   
5895 O O   . GLU B 843 ? 1.0396 1.5773 1.6730 -0.1739 0.2313  -0.1680 1093 GLU B O   
5896 C CB  . GLU B 843 ? 1.3536 1.8248 1.8265 -0.1730 0.2173  -0.1160 1093 GLU B CB  
5897 C CG  . GLU B 843 ? 1.4088 1.8560 1.8377 -0.1757 0.1884  -0.1094 1093 GLU B CG  
5898 C CD  . GLU B 843 ? 1.5618 1.9977 1.9564 -0.1762 0.2061  -0.0761 1093 GLU B CD  
5899 O OE1 . GLU B 843 ? 1.5061 1.9418 1.8382 -0.1652 0.2096  -0.0656 1093 GLU B OE1 
5900 O OE2 . GLU B 843 ? 1.5542 1.9830 1.9853 -0.1862 0.2169  -0.0613 1093 GLU B OE2 
5901 N N   . GLN C 3   ? 1.5444 1.2159 1.3191 -0.0423 0.0079  0.1662  1    GLN H N   
5902 C CA  . GLN C 3   ? 1.6001 1.2266 1.3702 -0.0272 -0.0057 0.1552  1    GLN H CA  
5903 C C   . GLN C 3   ? 1.4298 1.0550 1.1809 -0.0314 0.0252  0.1478  1    GLN H C   
5904 O O   . GLN C 3   ? 1.3998 1.0606 1.1457 -0.0464 0.0564  0.1525  1    GLN H O   
5905 C CB  . GLN C 3   ? 1.6279 1.2426 1.4554 -0.0200 -0.0396 0.1735  1    GLN H CB  
5906 C CG  . GLN C 3   ? 1.5574 1.1990 1.4290 -0.0308 -0.0288 0.1945  1    GLN H CG  
5907 C CD  . GLN C 3   ? 1.6395 1.2631 1.5633 -0.0220 -0.0614 0.2092  1    GLN H CD  
5908 O OE1 . GLN C 3   ? 1.6531 1.2614 1.5953 -0.0130 -0.0939 0.2133  1    GLN H OE1 
5909 N NE2 . GLN C 3   ? 1.5716 1.1970 1.5202 -0.0244 -0.0527 0.2166  1    GLN H NE2 
5910 N N   . VAL C 4   ? 1.4062 0.9902 1.1475 -0.0183 0.0160  0.1363  2    VAL H N   
5911 C CA  . VAL C 4   ? 1.3966 0.9734 1.1236 -0.0201 0.0407  0.1292  2    VAL H CA  
5912 C C   . VAL C 4   ? 1.4351 1.0063 1.2153 -0.0168 0.0256  0.1456  2    VAL H C   
5913 O O   . VAL C 4   ? 1.5149 1.0635 1.3249 -0.0057 -0.0087 0.1523  2    VAL H O   
5914 C CB  . VAL C 4   ? 1.2667 0.8003 0.9388 -0.0085 0.0439  0.1028  2    VAL H CB  
5915 C CG1 . VAL C 4   ? 1.4036 0.9447 1.0232 -0.0126 0.0602  0.0861  2    VAL H CG1 
5916 C CG2 . VAL C 4   ? 1.3089 0.7972 0.9907 0.0092  0.0059  0.0987  2    VAL H CG2 
5917 N N   . GLN C 5   ? 1.3766 0.9695 1.1699 -0.0268 0.0513  0.1518  3    GLN H N   
5918 C CA  . GLN C 5   ? 1.2954 0.8860 1.1391 -0.0250 0.0407  0.1662  3    GLN H CA  
5919 C C   . GLN C 5   ? 1.3379 0.9475 1.1783 -0.0352 0.0759  0.1644  3    GLN H C   
5920 O O   . GLN C 5   ? 1.3795 1.0158 1.1902 -0.0473 0.1080  0.1583  3    GLN H O   
5921 C CB  . GLN C 5   ? 1.3498 0.9693 1.2507 -0.0316 0.0219  0.1915  3    GLN H CB  
5922 C CG  . GLN C 5   ? 1.4088 1.0826 1.3220 -0.0522 0.0484  0.2052  3    GLN H CG  
5923 C CD  . GLN C 5   ? 1.4153 1.1153 1.3838 -0.0590 0.0279  0.2306  3    GLN H CD  
5924 O OE1 . GLN C 5   ? 1.4605 1.1390 1.4524 -0.0481 -0.0070 0.2367  3    GLN H OE1 
5925 N NE2 . GLN C 5   ? 1.3361 1.0826 1.3255 -0.0776 0.0496  0.2455  3    GLN H NE2 
5926 N N   . LEU C 6   ? 1.3860 0.9819 1.2586 -0.0300 0.0692  0.1692  4    LEU H N   
5927 C CA  . LEU C 6   ? 1.3060 0.9179 1.1845 -0.0384 0.0989  0.1682  4    LEU H CA  
5928 C C   . LEU C 6   ? 1.2276 0.8610 1.1714 -0.0435 0.0897  0.1895  4    LEU H C   
5929 O O   . LEU C 6   ? 1.4096 1.0195 1.3866 -0.0323 0.0578  0.1970  4    LEU H O   
5930 C CB  . LEU C 6   ? 1.3540 0.9224 1.2015 -0.0257 0.1020  0.1488  4    LEU H CB  
5931 C CG  . LEU C 6   ? 1.3260 0.8658 1.1073 -0.0190 0.1080  0.1262  4    LEU H CG  
5932 C CD1 . LEU C 6   ? 1.2331 0.7218 0.9942 -0.0034 0.0972  0.1112  4    LEU H CD1 
5933 C CD2 . LEU C 6   ? 1.4677 1.0371 1.2107 -0.0332 0.1487  0.1171  4    LEU H CD2 
5934 N N   . VAL C 7   ? 1.2296 0.9079 1.1918 -0.0610 0.1176  0.1989  5    VAL H N   
5935 C CA  . VAL C 7   ? 1.3340 1.0382 1.3573 -0.0687 0.1133  0.2187  5    VAL H CA  
5936 C C   . VAL C 7   ? 1.2784 0.9961 1.3066 -0.0759 0.1442  0.2132  5    VAL H C   
5937 O O   . VAL C 7   ? 1.3328 1.0723 1.3293 -0.0869 0.1781  0.2043  5    VAL H O   
5938 C CB  . VAL C 7   ? 1.2620 1.0130 1.3111 -0.0853 0.1150  0.2387  5    VAL H CB  
5939 C CG1 . VAL C 7   ? 1.1196 0.8548 1.1798 -0.0766 0.0778  0.2474  5    VAL H CG1 
5940 C CG2 . VAL C 7   ? 1.4089 1.1922 1.4181 -0.1001 0.1489  0.2325  5    VAL H CG2 
5941 N N   . GLU C 8   ? 1.2486 0.9530 1.3167 -0.0694 0.1322  0.2177  6    GLU H N   
5942 C CA  . GLU C 8   ? 1.3484 1.0642 1.4288 -0.0750 0.1581  0.2128  6    GLU H CA  
5943 C C   . GLU C 8   ? 1.2812 1.0453 1.4161 -0.0920 0.1676  0.2321  6    GLU H C   
5944 O O   . GLU C 8   ? 1.2394 1.0186 1.4104 -0.0958 0.1468  0.2505  6    GLU H O   
5945 C CB  . GLU C 8   ? 1.3664 1.0366 1.4559 -0.0571 0.1403  0.2038  6    GLU H CB  
5946 C CG  . GLU C 8   ? 1.2861 0.9078 1.3195 -0.0415 0.1346  0.1831  6    GLU H CG  
5947 C CD  . GLU C 8   ? 1.4246 1.0079 1.4574 -0.0253 0.0942  0.1847  6    GLU H CD  
5948 O OE1 . GLU C 8   ? 1.2066 0.7433 1.2146 -0.0096 0.0806  0.1708  6    GLU H OE1 
5949 O OE2 . GLU C 8   ? 1.3627 0.9622 1.4203 -0.0287 0.0757  0.1999  6    GLU H OE2 
5950 N N   . SER C 9   ? 1.2170 1.0052 1.3572 -0.1027 0.1998  0.2274  7    SER H N   
5951 C CA  . SER C 9   ? 1.3385 1.1745 1.5280 -0.1204 0.2135  0.2433  7    SER H CA  
5952 C C   . SER C 9   ? 1.3576 1.2023 1.5517 -0.1248 0.2432  0.2319  7    SER H C   
5953 O O   . SER C 9   ? 1.2458 1.0603 1.4034 -0.1146 0.2529  0.2129  7    SER H O   
5954 C CB  . SER C 9   ? 1.3187 1.2016 1.5008 -0.1402 0.2300  0.2545  7    SER H CB  
5955 O OG  . SER C 9   ? 1.3105 1.2011 1.4392 -0.1459 0.2606  0.2394  7    SER H OG  
5956 N N   . GLY C 10  ? 1.3529 1.2392 1.5927 -0.1404 0.2574  0.2435  8    GLY H N   
5957 C CA  . GLY C 10  ? 1.3381 1.2390 1.5887 -0.1466 0.2866  0.2338  8    GLY H CA  
5958 C C   . GLY C 10  ? 1.3246 1.1980 1.6123 -0.1331 0.2706  0.2304  8    GLY H C   
5959 O O   . GLY C 10  ? 1.1519 1.0376 1.4542 -0.1378 0.2935  0.2224  8    GLY H O   
5960 N N   . GLY C 11  ? 1.3276 1.1645 1.6314 -0.1166 0.2322  0.2360  9    GLY H N   
5961 C CA  . GLY C 11  ? 1.2260 1.0355 1.5650 -0.1032 0.2154  0.2330  9    GLY H CA  
5962 C C   . GLY C 11  ? 1.4521 1.2992 1.8561 -0.1155 0.2181  0.2472  9    GLY H C   
5963 O O   . GLY C 11  ? 1.2838 1.1697 1.7121 -0.1311 0.2189  0.2642  9    GLY H O   
5964 N N   . GLY C 12  ? 1.4330 1.2682 1.8655 -0.1087 0.2191  0.2398  10   GLY H N   
5965 C CA  . GLY C 12  ? 1.4412 1.3109 1.9360 -0.1199 0.2231  0.2506  10   GLY H CA  
5966 C C   . GLY C 12  ? 1.4520 1.2935 1.9756 -0.1056 0.2134  0.2413  10   GLY H C   
5967 O O   . GLY C 12  ? 1.4953 1.2860 1.9983 -0.0852 0.1923  0.2317  10   GLY H O   
5968 N N   . VAL C 13  ? 1.4819 1.3575 2.0537 -0.1171 0.2292  0.2438  11   VAL H N   
5969 C CA  . VAL C 13  ? 1.4227 1.2785 2.0293 -0.1058 0.2227  0.2352  11   VAL H CA  
5970 C C   . VAL C 13  ? 1.3533 1.2499 1.9800 -0.1216 0.2607  0.2274  11   VAL H C   
5971 O O   . VAL C 13  ? 1.2924 1.2399 1.9503 -0.1421 0.2767  0.2385  11   VAL H O   
5972 C CB  . VAL C 13  ? 1.3838 1.2352 2.0484 -0.1003 0.1895  0.2500  11   VAL H CB  
5973 C CG1 . VAL C 13  ? 1.2864 1.1344 1.9959 -0.0950 0.1914  0.2420  11   VAL H CG1 
5974 C CG2 . VAL C 13  ? 1.5189 1.3200 2.1651 -0.0801 0.1499  0.2533  11   VAL H CG2 
5975 N N   . VAL C 14  ? 1.4214 1.2958 2.0308 -0.1125 0.2750  0.2081  12   VAL H N   
5976 C CA  . VAL C 14  ? 1.4344 1.3428 2.0629 -0.1252 0.3106  0.1978  12   VAL H CA  
5977 C C   . VAL C 14  ? 1.3542 1.2291 2.0026 -0.1086 0.3036  0.1835  12   VAL H C   
5978 O O   . VAL C 14  ? 1.3305 1.1589 1.9819 -0.0886 0.2703  0.1835  12   VAL H O   
5979 C CB  . VAL C 14  ? 1.4934 1.4191 2.0688 -0.1364 0.3471  0.1869  12   VAL H CB  
5980 C CG1 . VAL C 14  ? 1.4674 1.4380 2.0340 -0.1571 0.3593  0.2016  12   VAL H CG1 
5981 C CG2 . VAL C 14  ? 1.2688 1.1414 1.7821 -0.1182 0.3383  0.1738  12   VAL H CG2 
5982 N N   . GLN C 15  ? 1.2945 1.1928 1.9567 -0.1170 0.3348  0.1709  13   GLN H N   
5983 C CA  . GLN C 15  ? 1.2853 1.1585 1.9703 -0.1038 0.3329  0.1563  13   GLN H CA  
5984 C C   . GLN C 15  ? 1.4304 1.2649 2.0585 -0.0919 0.3438  0.1374  13   GLN H C   
5985 O O   . GLN C 15  ? 1.5097 1.3506 2.0859 -0.0992 0.3636  0.1335  13   GLN H O   
5986 C CB  . GLN C 15  ? 1.2480 1.1707 1.9839 -0.1204 0.3611  0.1528  13   GLN H CB  
5987 C CG  . GLN C 15  ? 1.1071 1.0706 1.9016 -0.1339 0.3526  0.1708  13   GLN H CG  
5988 C CD  . GLN C 15  ? 1.1345 1.1501 1.9761 -0.1524 0.3834  0.1661  13   GLN H CD  
5989 O OE1 . GLN C 15  ? 1.0699 1.0888 1.9665 -0.1488 0.3744  0.1647  13   GLN H OE1 
5990 N NE2 . GLN C 15  ? 1.1922 1.2495 2.0128 -0.1725 0.4200  0.1631  13   GLN H NE2 
5991 N N   . PRO C 16  ? 1.5267 1.3197 2.1625 -0.0737 0.3306  0.1254  14   PRO H N   
5992 C CA  . PRO C 16  ? 1.3040 1.0599 1.8869 -0.0631 0.3416  0.1071  14   PRO H CA  
5993 C C   . PRO C 16  ? 1.3393 1.1324 1.9094 -0.0796 0.3867  0.0950  14   PRO H C   
5994 O O   . PRO C 16  ? 1.3021 1.1382 1.9187 -0.0931 0.4071  0.0943  14   PRO H O   
5995 C CB  . PRO C 16  ? 1.1878 0.9013 1.7979 -0.0432 0.3191  0.0988  14   PRO H CB  
5996 C CG  . PRO C 16  ? 1.4711 1.1828 2.1292 -0.0379 0.2850  0.1149  14   PRO H CG  
5997 C CD  . PRO C 16  ? 1.5156 1.2884 2.2048 -0.0603 0.3005  0.1291  14   PRO H CD  
5998 N N   . GLY C 17  ? 1.3214 1.0981 1.8275 -0.0790 0.4024  0.0849  15   GLY H N   
5999 C CA  . GLY C 17  ? 1.3487 1.1564 1.8345 -0.0937 0.4449  0.0725  15   GLY H CA  
6000 C C   . GLY C 17  ? 1.4801 1.3368 1.9471 -0.1154 0.4690  0.0810  15   GLY H C   
6001 O O   . GLY C 17  ? 1.4351 1.3134 1.8729 -0.1270 0.5038  0.0704  15   GLY H O   
6002 N N   . ARG C 18  ? 1.4236 1.2984 1.9064 -0.1213 0.4513  0.0999  16   ARG H N   
6003 C CA  . ARG C 18  ? 1.4859 1.4082 1.9538 -0.1424 0.4722  0.1097  16   ARG H CA  
6004 C C   . ARG C 18  ? 1.5562 1.4550 1.9543 -0.1384 0.4705  0.1078  16   ARG H C   
6005 O O   . ARG C 18  ? 1.5373 1.3929 1.8920 -0.1243 0.4689  0.0935  16   ARG H O   
6006 C CB  . ARG C 18  ? 1.4623 1.4150 1.9777 -0.1514 0.4541  0.1312  16   ARG H CB  
6007 C CG  . ARG C 18  ? 1.3499 1.3364 1.9348 -0.1602 0.4610  0.1335  16   ARG H CG  
6008 C CD  . ARG C 18  ? 1.3814 1.4232 1.9997 -0.1820 0.4667  0.1521  16   ARG H CD  
6009 N NE  . ARG C 18  ? 1.4067 1.4916 2.0826 -0.1961 0.4861  0.1505  16   ARG H NE  
6010 C CZ  . ARG C 18  ? 1.3174 1.4582 2.0243 -0.2192 0.5007  0.1631  16   ARG H CZ  
6011 N NH1 . ARG C 18  ? 1.2668 1.4265 1.9528 -0.2304 0.4974  0.1789  16   ARG H NH1 
6012 N NH2 . ARG C 18  ? 1.2071 1.3851 1.9660 -0.2314 0.5183  0.1596  16   ARG H NH2 
6013 N N   . SER C 19  ? 1.4977 1.4248 1.8850 -0.1508 0.4706  0.1220  17   SER H N   
6014 C CA  . SER C 19  ? 1.4466 1.3584 1.7702 -0.1493 0.4715  0.1204  17   SER H CA  
6015 C C   . SER C 19  ? 1.4231 1.3372 1.7512 -0.1496 0.4434  0.1397  17   SER H C   
6016 O O   . SER C 19  ? 1.4658 1.4093 1.8435 -0.1583 0.4337  0.1557  17   SER H O   
6017 C CB  . SER C 19  ? 1.5042 1.4571 1.7968 -0.1690 0.5139  0.1135  17   SER H CB  
6018 O OG  . SER C 19  ? 1.4107 1.3576 1.6492 -0.1703 0.5131  0.1156  17   SER H OG  
6019 N N   . LEU C 20  ? 1.5189 1.4012 1.7944 -0.1401 0.4304  0.1374  18   LEU H N   
6020 C CA  . LEU C 20  ? 1.4159 1.2987 1.6865 -0.1402 0.4057  0.1536  18   LEU H CA  
6021 C C   . LEU C 20  ? 1.3418 1.2016 1.5437 -0.1354 0.4084  0.1449  18   LEU H C   
6022 O O   . LEU C 20  ? 1.3608 1.1842 1.5228 -0.1239 0.4134  0.1277  18   LEU H O   
6023 C CB  . LEU C 20  ? 1.4111 1.2588 1.7149 -0.1231 0.3626  0.1629  18   LEU H CB  
6024 C CG  . LEU C 20  ? 1.3652 1.2425 1.7193 -0.1317 0.3441  0.1853  18   LEU H CG  
6025 C CD1 . LEU C 20  ? 1.1617 0.9964 1.5348 -0.1124 0.2999  0.1924  18   LEU H CD1 
6026 C CD2 . LEU C 20  ? 1.2888 1.2000 1.6210 -0.1474 0.3532  0.1963  18   LEU H CD2 
6027 N N   . ARG C 21  ? 1.3724 1.2538 1.5610 -0.1445 0.4048  0.1570  19   ARG H N   
6028 C CA  . ARG C 21  ? 1.2909 1.1560 1.4170 -0.1417 0.4073  0.1498  19   ARG H CA  
6029 C C   . ARG C 21  ? 1.2353 1.0872 1.3624 -0.1352 0.3726  0.1638  19   ARG H C   
6030 O O   . ARG C 21  ? 1.3469 1.2332 1.5085 -0.1467 0.3662  0.1820  19   ARG H O   
6031 C CB  . ARG C 21  ? 1.2397 1.1511 1.3402 -0.1624 0.4461  0.1473  19   ARG H CB  
6032 C CG  . ARG C 21  ? 1.2443 1.1471 1.2866 -0.1620 0.4470  0.1434  19   ARG H CG  
6033 C CD  . ARG C 21  ? 1.4026 1.3454 1.4144 -0.1806 0.4883  0.1366  19   ARG H CD  
6034 N NE  . ARG C 21  ? 1.4921 1.4707 1.4980 -0.1946 0.4902  0.1503  19   ARG H NE  
6035 C CZ  . ARG C 21  ? 1.6022 1.6154 1.5774 -0.2107 0.5216  0.1466  19   ARG H CZ  
6036 N NH1 . ARG C 21  ? 1.5525 1.5711 1.5009 -0.2119 0.5460  0.1280  19   ARG H NH1 
6037 N NH2 . ARG C 21  ? 1.6271 1.6711 1.5996 -0.2227 0.5199  0.1602  19   ARG H NH2 
6038 N N   . LEU C 22  ? 1.2715 1.0739 1.3610 -0.1173 0.3505  0.1552  20   LEU H N   
6039 C CA  . LEU C 22  ? 1.1480 0.9346 1.2317 -0.1100 0.3184  0.1655  20   LEU H CA  
6040 C C   . LEU C 22  ? 1.2730 1.0700 1.3036 -0.1170 0.3320  0.1611  20   LEU H C   
6041 O O   . LEU C 22  ? 1.3688 1.1704 1.3575 -0.1221 0.3617  0.1464  20   LEU H O   
6042 C CB  . LEU C 22  ? 1.1940 0.9206 1.2689 -0.0866 0.2845  0.1586  20   LEU H CB  
6043 C CG  . LEU C 22  ? 1.2942 1.0022 1.4156 -0.0768 0.2696  0.1599  20   LEU H CG  
6044 C CD1 . LEU C 22  ? 1.2982 0.9465 1.4051 -0.0541 0.2350  0.1533  20   LEU H CD1 
6045 C CD2 . LEU C 22  ? 1.1898 0.9328 1.3766 -0.0859 0.2592  0.1804  20   LEU H CD2 
6046 N N   . SER C 23  ? 1.3792 1.1803 1.4128 -0.1170 0.3096  0.1738  21   SER H N   
6047 C CA  . SER C 23  ? 1.2279 1.0380 1.2148 -0.1224 0.3178  0.1706  21   SER H CA  
6048 C C   . SER C 23  ? 1.2236 0.9982 1.1991 -0.1075 0.2803  0.1733  21   SER H C   
6049 O O   . SER C 23  ? 1.2557 1.0183 1.2717 -0.0998 0.2491  0.1858  21   SER H O   
6050 C CB  . SER C 23  ? 1.1166 0.9852 1.1208 -0.1447 0.3368  0.1856  21   SER H CB  
6051 O OG  . SER C 23  ? 1.2869 1.1691 1.3393 -0.1470 0.3102  0.2069  21   SER H OG  
6052 N N   . CYS C 24  ? 1.2777 1.0360 1.1976 -0.1036 0.2838  0.1607  22   CYS H N   
6053 C CA  . CYS C 24  ? 1.2869 1.0121 1.1898 -0.0899 0.2508  0.1603  22   CYS H CA  
6054 C C   . CYS C 24  ? 1.2934 1.0405 1.1596 -0.0991 0.2618  0.1590  22   CYS H C   
6055 O O   . CYS C 24  ? 1.3171 1.0597 1.1317 -0.1008 0.2847  0.1422  22   CYS H O   
6056 C CB  . CYS C 24  ? 1.3405 1.0090 1.2084 -0.0708 0.2382  0.1415  22   CYS H CB  
6057 S SG  . CYS C 24  ? 1.3147 0.9427 1.1526 -0.0551 0.2019  0.1368  22   CYS H SG  
6058 N N   . ALA C 25  ? 1.2045 0.9749 1.0973 -0.1051 0.2453  0.1766  23   ALA H N   
6059 C CA  . ALA C 25  ? 1.1549 0.9482 1.0190 -0.1139 0.2527  0.1775  23   ALA H CA  
6060 C C   . ALA C 25  ? 1.1964 0.9499 1.0303 -0.0980 0.2245  0.1685  23   ALA H C   
6061 O O   . ALA C 25  ? 1.1939 0.9269 1.0565 -0.0873 0.1896  0.1777  23   ALA H O   
6062 C CB  . ALA C 25  ? 1.1568 0.9957 1.0646 -0.1292 0.2490  0.2013  23   ALA H CB  
6063 N N   . ALA C 26  ? 1.2489 0.9921 1.0254 -0.0967 0.2401  0.1502  24   ALA H N   
6064 C CA  . ALA C 26  ? 1.2249 0.9333 0.9671 -0.0832 0.2176  0.1389  24   ALA H CA  
6065 C C   . ALA C 26  ? 1.1855 0.9227 0.9164 -0.0922 0.2182  0.1445  24   ALA H C   
6066 O O   . ALA C 26  ? 1.1998 0.9808 0.9308 -0.1092 0.2441  0.1510  24   ALA H O   
6067 C CB  . ALA C 26  ? 1.2694 0.9438 0.9533 -0.0752 0.2325  0.1135  24   ALA H CB  
6068 N N   . SER C 27  ? 1.3369 1.0491 1.0583 -0.0807 0.1888  0.1415  25   SER H N   
6069 C CA  . SER C 27  ? 1.1779 0.9130 0.8909 -0.0869 0.1842  0.1462  25   SER H CA  
6070 C C   . SER C 27  ? 1.2822 0.9778 0.9711 -0.0706 0.1553  0.1338  25   SER H C   
6071 O O   . SER C 27  ? 1.1609 0.8200 0.8662 -0.0561 0.1271  0.1334  25   SER H O   
6072 C CB  . SER C 27  ? 1.1168 0.8874 0.8862 -0.0968 0.1711  0.1731  25   SER H CB  
6073 O OG  . SER C 27  ? 1.2660 1.0151 1.0810 -0.0867 0.1405  0.1845  25   SER H OG  
6074 N N   . GLY C 28  ? 1.2489 0.9524 0.8989 -0.0735 0.1630  0.1232  26   GLY H N   
6075 C CA  . GLY C 28  ? 1.1596 0.8315 0.7864 -0.0601 0.1374  0.1109  26   GLY H CA  
6076 C C   . GLY C 28  ? 1.4472 1.0845 1.0139 -0.0516 0.1483  0.0834  26   GLY H C   
6077 O O   . GLY C 28  ? 1.4100 1.0240 0.9514 -0.0422 0.1308  0.0706  26   GLY H O   
6078 N N   . PHE C 29  ? 1.0922 1.1266 0.9715 -0.0508 -0.1306 0.1195  27   PHE H N   
6079 C CA  . PHE C 29  ? 1.1095 1.1593 0.9959 -0.0528 -0.1458 0.1067  27   PHE H CA  
6080 C C   . PHE C 29  ? 1.3063 1.3676 1.1825 -0.0571 -0.1289 0.0934  27   PHE H C   
6081 O O   . PHE C 29  ? 1.2870 1.3432 1.1668 -0.0604 -0.1051 0.0951  27   PHE H O   
6082 C CB  . PHE C 29  ? 1.0046 1.0521 0.9436 -0.0574 -0.1559 0.1101  27   PHE H CB  
6083 C CG  . PHE C 29  ? 1.0882 1.1313 1.0689 -0.0648 -0.1350 0.1134  27   PHE H CG  
6084 C CD1 . PHE C 29  ? 1.0158 1.0680 1.0143 -0.0693 -0.1266 0.1038  27   PHE H CD1 
6085 C CD2 . PHE C 29  ? 0.9975 1.0271 1.0005 -0.0670 -0.1229 0.1261  27   PHE H CD2 
6086 C CE1 . PHE C 29  ? 0.8760 0.9247 0.9126 -0.0750 -0.1071 0.1071  27   PHE H CE1 
6087 C CE2 . PHE C 29  ? 0.9661 0.9935 1.0091 -0.0735 -0.1035 0.1291  27   PHE H CE2 
6088 C CZ  . PHE C 29  ? 1.1567 1.1941 1.2162 -0.0770 -0.0960 0.1198  27   PHE H CZ  
6089 N N   . THR C 30  ? 1.3956 1.4717 1.2591 -0.0572 -0.1408 0.0798  28   THR H N   
6090 C CA  . THR C 30  ? 1.4415 1.5286 1.2949 -0.0622 -0.1260 0.0648  28   THR H CA  
6091 C C   . THR C 30  ? 1.3780 1.4601 1.2762 -0.0700 -0.1105 0.0649  28   THR H C   
6092 O O   . THR C 30  ? 1.3973 1.4776 1.3313 -0.0712 -0.1211 0.0682  28   THR H O   
6093 C CB  . THR C 30  ? 1.4914 1.5949 1.3250 -0.0614 -0.1425 0.0503  28   THR H CB  
6094 O OG1 . THR C 30  ? 1.6742 1.7828 1.4710 -0.0528 -0.1598 0.0520  28   THR H OG1 
6095 C CG2 . THR C 30  ? 1.3358 1.4511 1.1514 -0.0668 -0.1265 0.0330  28   THR H CG2 
6096 N N   . PHE C 31  ? 1.2695 1.3497 1.1645 -0.0740 -0.0854 0.0614  29   PHE H N   
6097 C CA  . PHE C 31  ? 1.2293 1.3042 1.1643 -0.0805 -0.0677 0.0621  29   PHE H CA  
6098 C C   . PHE C 31  ? 1.3157 1.3988 1.2607 -0.0848 -0.0683 0.0480  29   PHE H C   
6099 O O   . PHE C 31  ? 1.2800 1.3586 1.2619 -0.0884 -0.0577 0.0496  29   PHE H O   
6100 C CB  . PHE C 31  ? 1.3895 1.4584 1.3145 -0.0826 -0.0396 0.0629  29   PHE H CB  
6101 C CG  . PHE C 31  ? 1.3705 1.4284 1.3404 -0.0862 -0.0226 0.0739  29   PHE H CG  
6102 C CD1 . PHE C 31  ? 1.2818 1.3378 1.2622 -0.0910 0.0023  0.0687  29   PHE H CD1 
6103 C CD2 . PHE C 31  ? 1.1735 1.2239 1.1762 -0.0849 -0.0316 0.0888  29   PHE H CD2 
6104 C CE1 . PHE C 31  ? 1.2840 1.3315 1.3067 -0.0936 0.0181  0.0790  29   PHE H CE1 
6105 C CE2 . PHE C 31  ? 1.1072 1.1505 1.1538 -0.0884 -0.0164 0.0981  29   PHE H CE2 
6106 C CZ  . PHE C 31  ? 1.1822 1.2245 1.2390 -0.0924 0.0085  0.0936  29   PHE H CZ  
6107 N N   . SER C 32  ? 1.3356 1.4307 1.2496 -0.0842 -0.0795 0.0346  30   SER H N   
6108 C CA  . SER C 32  ? 1.0053 1.1070 0.9263 -0.0887 -0.0792 0.0206  30   SER H CA  
6109 C C   . SER C 32  ? 0.9815 1.0856 0.9179 -0.0852 -0.1031 0.0226  30   SER H C   
6110 O O   . SER C 32  ? 1.0577 1.1650 1.0025 -0.0878 -0.1030 0.0128  30   SER H O   
6111 C CB  . SER C 32  ? 1.0366 1.1512 0.9162 -0.0916 -0.0745 0.0022  30   SER H CB  
6112 O OG  . SER C 32  ? 0.9944 1.1192 0.8403 -0.0857 -0.0944 0.0011  30   SER H OG  
6113 N N   . SER C 33  ? 0.9544 1.0558 0.8935 -0.0789 -0.1227 0.0349  31   SER H N   
6114 C CA  . SER C 33  ? 0.7028 0.8054 0.6559 -0.0745 -0.1461 0.0377  31   SER H CA  
6115 C C   . SER C 33  ? 0.7518 0.8453 0.7519 -0.0730 -0.1489 0.0498  31   SER H C   
6116 O O   . SER C 33  ? 0.7763 0.8708 0.7932 -0.0693 -0.1642 0.0502  31   SER H O   
6117 C CB  . SER C 33  ? 0.7286 0.8345 0.6541 -0.0678 -0.1684 0.0423  31   SER H CB  
6118 O OG  . SER C 33  ? 0.8964 1.0146 0.7790 -0.0676 -0.1692 0.0302  31   SER H OG  
6119 N N   . TYR C 34  ? 0.8415 0.9272 0.8631 -0.0751 -0.1344 0.0592  32   TYR H N   
6120 C CA  . TYR C 34  ? 0.8772 0.9570 0.9453 -0.0739 -0.1370 0.0703  32   TYR H CA  
6121 C C   . TYR C 34  ? 0.7258 0.8027 0.8218 -0.0785 -0.1118 0.0697  32   TYR H C   
6122 O O   . TYR C 34  ? 0.8145 0.8897 0.8948 -0.0830 -0.0902 0.0658  32   TYR H O   
6123 C CB  . TYR C 34  ? 0.7789 0.8519 0.8541 -0.0724 -0.1432 0.0836  32   TYR H CB  
6124 C CG  . TYR C 34  ? 0.7470 0.8203 0.7993 -0.0669 -0.1686 0.0863  32   TYR H CG  
6125 C CD1 . TYR C 34  ? 0.8824 0.9578 0.8880 -0.0649 -0.1708 0.0827  32   TYR H CD1 
6126 C CD2 . TYR C 34  ? 0.8385 0.9107 0.9153 -0.0626 -0.1905 0.0921  32   TYR H CD2 
6127 C CE1 . TYR C 34  ? 0.8778 0.9530 0.8618 -0.0588 -0.1934 0.0856  32   TYR H CE1 
6128 C CE2 . TYR C 34  ? 0.8616 0.9326 0.9167 -0.0572 -0.2132 0.0945  32   TYR H CE2 
6129 C CZ  . TYR C 34  ? 0.8410 0.9131 0.8498 -0.0553 -0.2141 0.0916  32   TYR H CZ  
6130 O OH  . TYR C 34  ? 1.0372 1.1078 1.0238 -0.0489 -0.2361 0.0945  32   TYR H OH  
6131 N N   . ALA C 35  ? 0.7563 0.8330 0.8927 -0.0762 -0.1146 0.0735  33   ALA H N   
6132 C CA  . ALA C 35  ? 0.7813 0.8552 0.9503 -0.0789 -0.0921 0.0759  33   ALA H CA  
6133 C C   . ALA C 35  ? 0.8256 0.8959 1.0207 -0.0806 -0.0861 0.0884  33   ALA H C   
6134 O O   . ALA C 35  ? 0.8614 0.9311 1.0633 -0.0785 -0.1037 0.0962  33   ALA H O   
6135 C CB  . ALA C 35  ? 0.6915 0.7678 0.8934 -0.0740 -0.0973 0.0755  33   ALA H CB  
6136 N N   . MET C 36  ? 0.7427 0.8097 0.9527 -0.0846 -0.0601 0.0901  34   MET H N   
6137 C CA  . MET C 36  ? 0.7582 0.8212 0.9929 -0.0872 -0.0493 0.1015  34   MET H CA  
6138 C C   . MET C 36  ? 0.8354 0.9015 1.1210 -0.0866 -0.0380 0.1059  34   MET H C   
6139 O O   . MET C 36  ? 0.7890 0.8543 1.0776 -0.0875 -0.0184 0.1007  34   MET H O   
6140 C CB  . MET C 36  ? 0.8128 0.8691 1.0165 -0.0915 -0.0266 0.1006  34   MET H CB  
6141 C CG  . MET C 36  ? 0.9041 0.9590 1.0570 -0.0904 -0.0373 0.0971  34   MET H CG  
6142 S SD  . MET C 36  ? 0.9998 1.0510 1.1564 -0.0874 -0.0605 0.1090  34   MET H SD  
6143 C CE  . MET C 36  ? 0.9368 0.9788 1.1253 -0.0916 -0.0374 0.1224  34   MET H CE  
6144 N N   . HIS C 37  ? 0.8589 0.9290 1.1843 -0.0850 -0.0501 0.1150  35   HIS H N   
6145 C CA  . HIS C 37  ? 0.7698 0.8467 1.1471 -0.0830 -0.0435 0.1193  35   HIS H CA  
6146 C C   . HIS C 37  ? 0.8340 0.9093 1.2407 -0.0882 -0.0257 0.1287  35   HIS H C   
6147 O O   . HIS C 37  ? 0.8964 0.9653 1.2907 -0.0924 -0.0257 0.1339  35   HIS H O   
6148 C CB  . HIS C 37  ? 0.8121 0.8983 1.2185 -0.0766 -0.0715 0.1212  35   HIS H CB  
6149 C CG  . HIS C 37  ? 0.8112 0.8989 1.1955 -0.0701 -0.0876 0.1133  35   HIS H CG  
6150 N ND1 . HIS C 37  ? 0.8150 0.9086 1.2227 -0.0627 -0.0894 0.1113  35   HIS H ND1 
6151 C CD2 . HIS C 37  ? 0.7394 0.8234 1.0808 -0.0692 -0.1019 0.1072  35   HIS H CD2 
6152 C CE1 . HIS C 37  ? 0.7960 0.8880 1.1758 -0.0580 -0.1032 0.1045  35   HIS H CE1 
6153 N NE2 . HIS C 37  ? 0.8822 0.9693 1.2226 -0.0623 -0.1112 0.1016  35   HIS H NE2 
6154 N N   . TRP C 38  ? 0.8655 0.9464 1.3113 -0.0874 -0.0093 0.1312  36   TRP H N   
6155 C CA  . TRP C 38  ? 0.6823 0.7657 1.1692 -0.0914 0.0055  0.1403  36   TRP H CA  
6156 C C   . TRP C 38  ? 0.6516 0.7506 1.1938 -0.0866 -0.0088 0.1433  36   TRP H C   
6157 O O   . TRP C 38  ? 0.7038 0.8098 1.2599 -0.0797 -0.0091 0.1398  36   TRP H O   
6158 C CB  . TRP C 38  ? 0.7842 0.8622 1.2706 -0.0940 0.0396  0.1408  36   TRP H CB  
6159 C CG  . TRP C 38  ? 0.7885 0.8526 1.2275 -0.0989 0.0562  0.1396  36   TRP H CG  
6160 C CD1 . TRP C 38  ? 0.8789 0.9359 1.2711 -0.0988 0.0652  0.1303  36   TRP H CD1 
6161 C CD2 . TRP C 38  ? 0.8977 0.9537 1.3313 -0.1039 0.0664  0.1478  36   TRP H CD2 
6162 N NE1 . TRP C 38  ? 1.0129 1.0596 1.3699 -0.1025 0.0789  0.1319  36   TRP H NE1 
6163 C CE2 . TRP C 38  ? 0.9444 0.9890 1.3249 -0.1051 0.0806  0.1433  36   TRP H CE2 
6164 C CE3 . TRP C 38  ? 0.9864 1.0433 1.4551 -0.1075 0.0655  0.1580  36   TRP H CE3 
6165 C CZ2 . TRP C 38  ? 0.9231 0.9565 1.2821 -0.1079 0.0939  0.1499  36   TRP H CZ2 
6166 C CZ3 . TRP C 38  ? 0.9847 1.0286 1.4334 -0.1116 0.0801  0.1647  36   TRP H CZ3 
6167 C CH2 . TRP C 38  ? 1.0524 1.0844 1.4456 -0.1109 0.0942  0.1613  36   TRP H CH2 
6168 N N   . VAL C 39  ? 0.7683 0.8725 1.3411 -0.0898 -0.0205 0.1494  37   VAL H N   
6169 C CA  . VAL C 39  ? 0.7707 0.8924 1.3983 -0.0858 -0.0358 0.1512  37   VAL H CA  
6170 C C   . VAL C 39  ? 0.7412 0.8680 1.4137 -0.0931 -0.0214 0.1587  37   VAL H C   
6171 O O   . VAL C 39  ? 0.9222 1.0390 1.5854 -0.1009 -0.0185 0.1630  37   VAL H O   
6172 C CB  . VAL C 39  ? 0.8154 0.9412 1.4393 -0.0822 -0.0709 0.1485  37   VAL H CB  
6173 C CG1 . VAL C 39  ? 0.7375 0.8833 1.4197 -0.0781 -0.0868 0.1496  37   VAL H CG1 
6174 C CG2 . VAL C 39  ? 0.6257 0.7475 1.2083 -0.0745 -0.0841 0.1413  37   VAL H CG2 
6175 N N   . ARG C 40  ? 0.6463 0.7883 1.3673 -0.0901 -0.0115 0.1606  38   ARG H N   
6176 C CA  . ARG C 40  ? 0.7309 0.8808 1.5007 -0.0968 0.0039  0.1671  38   ARG H CA  
6177 C C   . ARG C 40  ? 0.7479 0.9203 1.5740 -0.0945 -0.0189 0.1664  38   ARG H C   
6178 O O   . ARG C 40  ? 0.7600 0.9433 1.5899 -0.0851 -0.0432 0.1613  38   ARG H O   
6179 C CB  . ARG C 40  ? 0.7350 0.8868 1.5203 -0.0955 0.0358  0.1699  38   ARG H CB  
6180 C CG  . ARG C 40  ? 0.6685 0.8373 1.4824 -0.0841 0.0320  0.1670  38   ARG H CG  
6181 C CD  . ARG C 40  ? 0.6832 0.8498 1.5041 -0.0826 0.0655  0.1696  38   ARG H CD  
6182 N NE  . ARG C 40  ? 0.8483 1.0304 1.6980 -0.0705 0.0642  0.1680  38   ARG H NE  
6183 C CZ  . ARG C 40  ? 0.7396 0.9201 1.5948 -0.0661 0.0907  0.1695  38   ARG H CZ  
6184 N NH1 . ARG C 40  ? 0.7714 0.9360 1.6052 -0.0733 0.1201  0.1720  38   ARG H NH1 
6185 N NH2 . ARG C 40  ? 0.9235 1.1175 1.8041 -0.0536 0.0884  0.1687  38   ARG H NH2 
6186 N N   . GLN C 41  ? 0.7137 0.8932 1.5838 -0.1030 -0.0105 0.1711  39   GLN H N   
6187 C CA  . GLN C 41  ? 0.9195 1.1224 1.8479 -0.1030 -0.0308 0.1691  39   GLN H CA  
6188 C C   . GLN C 41  ? 0.8890 1.1052 1.8736 -0.1092 -0.0071 0.1741  39   GLN H C   
6189 O O   . GLN C 41  ? 0.9234 1.1290 1.9141 -0.1209 0.0092  0.1793  39   GLN H O   
6190 C CB  . GLN C 41  ? 0.7705 0.9667 1.6914 -0.1098 -0.0539 0.1675  39   GLN H CB  
6191 C CG  . GLN C 41  ? 0.7446 0.9647 1.7262 -0.1114 -0.0749 0.1638  39   GLN H CG  
6192 C CD  . GLN C 41  ? 0.9074 1.1179 1.8790 -0.1183 -0.0971 0.1614  39   GLN H CD  
6193 O OE1 . GLN C 41  ? 0.8635 1.0529 1.8141 -0.1286 -0.0843 0.1662  39   GLN H OE1 
6194 N NE2 . GLN C 41  ? 0.7619 0.9869 1.7468 -0.1118 -0.1299 0.1542  39   GLN H NE2 
6195 N N   . ALA C 42  ? 0.7807 1.0196 1.8057 -0.1007 -0.0042 0.1730  40   ALA H N   
6196 C CA  . ALA C 42  ? 0.7911 1.0467 1.8740 -0.1053 0.0170  0.1773  40   ALA H CA  
6197 C C   . ALA C 42  ? 0.8661 1.1359 1.9985 -0.1156 0.0033  0.1757  40   ALA H C   
6198 O O   . ALA C 42  ? 0.9323 1.2080 2.0657 -0.1145 -0.0279 0.1696  40   ALA H O   
6199 C CB  . ALA C 42  ? 0.8621 1.1418 1.9789 -0.0918 0.0183  0.1758  40   ALA H CB  
6200 N N   . PRO C 43  ? 0.9386 1.2134 2.1126 -0.1261 0.0270  0.1807  41   PRO H N   
6201 C CA  . PRO C 43  ? 0.7322 1.0193 1.9557 -0.1379 0.0168  0.1785  41   PRO H CA  
6202 C C   . PRO C 43  ? 0.7056 1.0267 1.9780 -0.1315 -0.0156 0.1692  41   PRO H C   
6203 O O   . PRO C 43  ? 0.7607 1.1090 2.0718 -0.1218 -0.0150 0.1675  41   PRO H O   
6204 C CB  . PRO C 43  ? 0.6600 0.9517 1.9255 -0.1469 0.0518  0.1855  41   PRO H CB  
6205 C CG  . PRO C 43  ? 0.7618 1.0284 1.9758 -0.1437 0.0811  0.1930  41   PRO H CG  
6206 C CD  . PRO C 43  ? 0.8669 1.1329 2.0404 -0.1286 0.0658  0.1887  41   PRO H CD  
6207 N N   . GLY C 44  ? 0.9078 1.2273 2.1771 -0.1358 -0.0440 0.1630  42   GLY H N   
6208 C CA  . GLY C 44  ? 0.9568 1.3072 2.2683 -0.1297 -0.0772 0.1529  42   GLY H CA  
6209 C C   . GLY C 44  ? 0.8360 1.1957 2.1230 -0.1103 -0.0997 0.1488  42   GLY H C   
6210 O O   . GLY C 44  ? 0.8631 1.2501 2.1836 -0.1024 -0.1276 0.1406  42   GLY H O   
6211 N N   . LYS C 45  ? 0.8304 1.1684 2.0602 -0.1022 -0.0881 0.1538  43   LYS H N   
6212 C CA  . LYS C 45  ? 0.9534 1.2967 2.1576 -0.0838 -0.1048 0.1508  43   LYS H CA  
6213 C C   . LYS C 45  ? 0.8893 1.2074 2.0295 -0.0820 -0.1240 0.1486  43   LYS H C   
6214 O O   . LYS C 45  ? 0.9614 1.2594 2.0779 -0.0940 -0.1254 0.1495  43   LYS H O   
6215 C CB  . LYS C 45  ? 0.8939 1.2329 2.0844 -0.0754 -0.0766 0.1567  43   LYS H CB  
6216 C CG  . LYS C 45  ? 0.8385 1.1993 2.0878 -0.0775 -0.0530 0.1603  43   LYS H CG  
6217 C CD  . LYS C 45  ? 0.8231 1.2240 2.1384 -0.0706 -0.0750 0.1539  43   LYS H CD  
6218 C CE  . LYS C 45  ? 0.8994 1.3135 2.2041 -0.0491 -0.0967 0.1501  43   LYS H CE  
6219 N NZ  . LYS C 45  ? 0.9288 1.3356 2.2134 -0.0371 -0.0724 0.1561  43   LYS H NZ  
6220 N N   . GLY C 46  ? 0.8283 1.1473 1.9401 -0.0660 -0.1377 0.1463  44   GLY H N   
6221 C CA  . GLY C 46  ? 0.8125 1.1101 1.8650 -0.0623 -0.1559 0.1440  44   GLY H CA  
6222 C C   . GLY C 46  ? 0.8274 1.0942 1.8207 -0.0672 -0.1330 0.1488  44   GLY H C   
6223 O O   . GLY C 46  ? 0.9509 1.2070 1.9444 -0.0781 -0.1053 0.1542  44   GLY H O   
6224 N N   . LEU C 47  ? 0.7822 1.0354 1.7245 -0.0586 -0.1446 0.1465  45   LEU H N   
6225 C CA  . LEU C 47  ? 0.7748 1.0005 1.6564 -0.0624 -0.1288 0.1486  45   LEU H CA  
6226 C C   . LEU C 47  ? 0.8733 1.0965 1.7360 -0.0517 -0.1137 0.1486  45   LEU H C   
6227 O O   . LEU C 47  ? 0.7325 0.9684 1.6064 -0.0378 -0.1272 0.1459  45   LEU H O   
6228 C CB  . LEU C 47  ? 0.7696 0.9809 1.6054 -0.0621 -0.1534 0.1450  45   LEU H CB  
6229 C CG  . LEU C 47  ? 0.8792 1.0679 1.6768 -0.0744 -0.1479 0.1474  45   LEU H CG  
6230 C CD1 . LEU C 47  ? 0.7675 0.9555 1.5969 -0.0876 -0.1276 0.1528  45   LEU H CD1 
6231 C CD2 . LEU C 47  ? 0.7739 0.9586 1.5536 -0.0732 -0.1795 0.1436  45   LEU H CD2 
6232 N N   . GLU C 48  ? 0.8235 1.0294 1.6568 -0.0576 -0.0849 0.1514  46   GLU H N   
6233 C CA  . GLU C 48  ? 0.7369 0.9372 1.5508 -0.0496 -0.0666 0.1506  46   GLU H CA  
6234 C C   . GLU C 48  ? 0.6918 0.8672 1.4435 -0.0553 -0.0543 0.1486  46   GLU H C   
6235 O O   . GLU C 48  ? 0.7424 0.9060 1.4790 -0.0664 -0.0381 0.1513  46   GLU H O   
6236 C CB  . GLU C 48  ? 0.6562 0.8659 1.5092 -0.0499 -0.0384 0.1553  46   GLU H CB  
6237 C CG  . GLU C 48  ? 0.6849 0.8908 1.5257 -0.0392 -0.0216 0.1543  46   GLU H CG  
6238 C CD  . GLU C 48  ? 0.7662 0.9782 1.6401 -0.0398 0.0089  0.1593  46   GLU H CD  
6239 O OE1 . GLU C 48  ? 0.7885 1.0064 1.6918 -0.0496 0.0190  0.1635  46   GLU H OE1 
6240 O OE2 . GLU C 48  ? 0.8468 1.0568 1.7173 -0.0302 0.0240  0.1590  46   GLU H OE2 
6241 N N   . TRP C 49  ? 0.6736 0.8416 1.3899 -0.0471 -0.0615 0.1436  47   TRP H N   
6242 C CA  . TRP C 49  ? 0.7312 0.8788 1.3904 -0.0519 -0.0498 0.1396  47   TRP H CA  
6243 C C   . TRP C 49  ? 0.7106 0.8506 1.3653 -0.0542 -0.0152 0.1402  47   TRP H C   
6244 O O   . TRP C 49  ? 0.6250 0.7728 1.3087 -0.0468 -0.0036 0.1417  47   TRP H O   
6245 C CB  . TRP C 49  ? 0.7668 0.9099 1.3939 -0.0429 -0.0675 0.1334  47   TRP H CB  
6246 C CG  . TRP C 49  ? 0.7378 0.8632 1.3099 -0.0475 -0.0556 0.1275  47   TRP H CG  
6247 C CD1 . TRP C 49  ? 0.6502 0.7656 1.1808 -0.0547 -0.0630 0.1246  47   TRP H CD1 
6248 C CD2 . TRP C 49  ? 0.7890 0.9055 1.3420 -0.0448 -0.0341 0.1228  47   TRP H CD2 
6249 N NE1 . TRP C 49  ? 0.6877 0.7911 1.1758 -0.0570 -0.0485 0.1176  47   TRP H NE1 
6250 C CE2 . TRP C 49  ? 0.7397 0.8427 1.2409 -0.0518 -0.0303 0.1160  47   TRP H CE2 
6251 C CE3 . TRP C 49  ? 0.8617 0.9803 1.4364 -0.0370 -0.0174 0.1234  47   TRP H CE3 
6252 C CZ2 . TRP C 49  ? 0.7274 0.8193 1.1995 -0.0526 -0.0106 0.1085  47   TRP H CZ2 
6253 C CZ3 . TRP C 49  ? 0.7645 0.8693 1.3088 -0.0374 0.0033  0.1170  47   TRP H CZ3 
6254 C CH2 . TRP C 49  ? 0.8577 0.9495 1.3519 -0.0458 0.0064  0.1090  47   TRP H CH2 
6255 N N   . VAL C 50  ? 0.6775 0.8021 1.2942 -0.0637 0.0013  0.1387  48   VAL H N   
6256 C CA  . VAL C 50  ? 0.6448 0.7611 1.2557 -0.0670 0.0349  0.1390  48   VAL H CA  
6257 C C   . VAL C 50  ? 0.8038 0.9054 1.3634 -0.0670 0.0442  0.1300  48   VAL H C   
6258 O O   . VAL C 50  ? 0.8932 0.9923 1.4546 -0.0614 0.0582  0.1268  48   VAL H O   
6259 C CB  . VAL C 50  ? 0.7316 0.8426 1.3434 -0.0775 0.0514  0.1446  48   VAL H CB  
6260 C CG1 . VAL C 50  ? 0.6921 0.7943 1.2971 -0.0799 0.0865  0.1448  48   VAL H CG1 
6261 C CG2 . VAL C 50  ? 0.7167 0.8425 1.3827 -0.0790 0.0432  0.1525  48   VAL H CG2 
6262 N N   . ALA C 51  ? 0.7469 0.8390 1.2612 -0.0730 0.0369  0.1255  49   ALA H N   
6263 C CA  . ALA C 51  ? 0.8377 0.9178 1.3032 -0.0748 0.0459  0.1154  49   ALA H CA  
6264 C C   . ALA C 51  ? 0.7474 0.8250 1.1736 -0.0767 0.0223  0.1106  49   ALA H C   
6265 O O   . ALA C 51  ? 0.7674 0.8504 1.2028 -0.0765 0.0006  0.1156  49   ALA H O   
6266 C CB  . ALA C 51  ? 0.8197 0.8896 1.2660 -0.0818 0.0768  0.1139  49   ALA H CB  
6267 N N   . VAL C 52  ? 0.7153 0.7851 1.0979 -0.0786 0.0271  0.1000  50   VAL H N   
6268 C CA  . VAL C 52  ? 0.7629 0.8316 1.1055 -0.0800 0.0066  0.0941  50   VAL H CA  
6269 C C   . VAL C 52  ? 0.7200 0.7810 1.0172 -0.0850 0.0220  0.0818  50   VAL H C   
6270 O O   . VAL C 52  ? 0.8390 0.8952 1.1375 -0.0856 0.0432  0.0761  50   VAL H O   
6271 C CB  . VAL C 52  ? 0.8382 0.9127 1.1894 -0.0721 -0.0202 0.0931  50   VAL H CB  
6272 C CG1 . VAL C 52  ? 0.7387 0.8097 1.0878 -0.0676 -0.0107 0.0856  50   VAL H CG1 
6273 C CG2 . VAL C 52  ? 0.7007 0.7754 1.0158 -0.0731 -0.0434 0.0895  50   VAL H CG2 
6274 N N   . THR C 53  ? 0.7212 0.7818 0.9783 -0.0884 0.0114  0.0772  51   THR H N   
6275 C CA  . THR C 53  ? 0.7977 0.8554 1.0098 -0.0927 0.0194  0.0632  51   THR H CA  
6276 C C   . THR C 53  ? 0.7674 0.8301 0.9506 -0.0911 -0.0072 0.0584  51   THR H C   
6277 O O   . THR C 53  ? 0.7920 0.8577 0.9771 -0.0886 -0.0265 0.0666  51   THR H O   
6278 C CB  . THR C 53  ? 0.8239 0.8772 1.0107 -0.0984 0.0398  0.0616  51   THR H CB  
6279 O OG1 . THR C 53  ? 1.0112 1.0649 1.1533 -0.1023 0.0439  0.0463  51   THR H OG1 
6280 C CG2 . THR C 53  ? 0.7230 0.7771 0.9048 -0.0979 0.0290  0.0722  51   THR H CG2 
6281 N N   . TRP C 54  ? 0.7321 0.7955 0.8897 -0.0926 -0.0074 0.0450  52   TRP H N   
6282 C CA  . TRP C 54  ? 0.7622 0.8316 0.8943 -0.0906 -0.0318 0.0398  52   TRP H CA  
6283 C C   . TRP C 54  ? 0.7490 0.8204 0.8429 -0.0962 -0.0234 0.0225  52   TRP H C   
6284 O O   . TRP C 54  ? 0.8965 0.9634 0.9858 -0.1015 0.0006  0.0140  52   TRP H O   
6285 C CB  . TRP C 54  ? 0.6465 0.7172 0.8038 -0.0832 -0.0507 0.0441  52   TRP H CB  
6286 C CG  . TRP C 54  ? 0.7836 0.8500 0.9495 -0.0822 -0.0390 0.0364  52   TRP H CG  
6287 C CD1 . TRP C 54  ? 0.8196 0.8862 0.9642 -0.0825 -0.0438 0.0250  52   TRP H CD1 
6288 C CD2 . TRP C 54  ? 0.8317 0.8918 1.0299 -0.0801 -0.0195 0.0398  52   TRP H CD2 
6289 N NE1 . TRP C 54  ? 0.7745 0.8334 0.9353 -0.0809 -0.0276 0.0213  52   TRP H NE1 
6290 C CE2 . TRP C 54  ? 0.8114 0.8662 1.0044 -0.0788 -0.0128 0.0305  52   TRP H CE2 
6291 C CE3 . TRP C 54  ? 0.7121 0.7707 0.9437 -0.0788 -0.0063 0.0500  52   TRP H CE3 
6292 C CZ2 . TRP C 54  ? 0.7619 0.8086 0.9798 -0.0754 0.0068  0.0315  52   TRP H CZ2 
6293 C CZ3 . TRP C 54  ? 0.8977 0.9506 1.1551 -0.0754 0.0121  0.0507  52   TRP H CZ3 
6294 C CH2 . TRP C 54  ? 0.8482 0.8945 1.0976 -0.0733 0.0185  0.0418  52   TRP H CH2 
6295 N N   . PHE C 55  A 0.7814 0.8601 0.8485 -0.0951 -0.0437 0.0165  52   PHE H N   
6296 C CA  . PHE C 55  A 0.8165 0.9013 0.8461 -0.1006 -0.0400 -0.0009 52   PHE H CA  
6297 C C   . PHE C 55  A 0.9853 1.0713 0.9901 -0.1062 -0.0218 -0.0067 52   PHE H C   
6298 O O   . PHE C 55  A 0.9289 1.0108 0.9318 -0.1120 0.0014  -0.0166 52   PHE H O   
6299 C CB  . PHE C 55  A 0.8111 0.8914 0.8493 -0.1035 -0.0281 -0.0121 52   PHE H CB  
6300 C CG  . PHE C 55  A 0.8399 0.9285 0.8467 -0.1080 -0.0335 -0.0292 52   PHE H CG  
6301 C CD1 . PHE C 55  A 0.7273 0.8239 0.7232 -0.1034 -0.0590 -0.0284 52   PHE H CD1 
6302 C CD2 . PHE C 55  A 0.9220 1.0109 0.9111 -0.1170 -0.0129 -0.0468 52   PHE H CD2 
6303 C CE1 . PHE C 55  A 0.8034 0.9094 0.7726 -0.1077 -0.0636 -0.0443 52   PHE H CE1 
6304 C CE2 . PHE C 55  A 0.8341 0.9327 0.7973 -0.1221 -0.0177 -0.0639 52   PHE H CE2 
6305 C CZ  . PHE C 55  A 0.8261 0.9339 0.7800 -0.1174 -0.0430 -0.0624 52   PHE H CZ  
6306 N N   . ASP C 56  ? 1.0604 1.1511 1.0445 -0.1036 -0.0319 -0.0007 53   ASP H N   
6307 C CA  . ASP C 56  ? 1.1256 1.2151 1.0904 -0.1057 -0.0150 -0.0007 53   ASP H CA  
6308 C C   . ASP C 56  ? 1.2553 1.3329 1.2539 -0.1070 0.0070  0.0084  53   ASP H C   
6309 O O   . ASP C 56  ? 1.2319 1.3043 1.2655 -0.1033 0.0012  0.0232  53   ASP H O   
6310 C CB  . ASP C 56  ? 1.2276 1.3255 1.1545 -0.1114 -0.0043 -0.0207 53   ASP H CB  
6311 C CG  . ASP C 56  ? 1.2431 1.3467 1.1325 -0.1092 -0.0026 -0.0212 53   ASP H CG  
6312 O OD1 . ASP C 56  ? 1.3011 1.3996 1.1938 -0.1034 -0.0081 -0.0050 53   ASP H OD1 
6313 O OD2 . ASP C 56  ? 1.1239 1.2370 0.9803 -0.1128 0.0046  -0.0380 53   ASP H OD2 
6314 N N   . VAL C 57  ? 1.5143 1.5884 1.5035 -0.1122 0.0322  -0.0008 54   VAL H N   
6315 C CA  . VAL C 57  ? 1.4824 1.5455 1.5044 -0.1134 0.0550  0.0060  54   VAL H CA  
6316 C C   . VAL C 57  ? 1.3578 1.4173 1.3772 -0.1193 0.0745  -0.0099 54   VAL H C   
6317 O O   . VAL C 57  ? 1.3850 1.4412 1.3879 -0.1236 0.0966  -0.0181 54   VAL H O   
6318 C CB  . VAL C 57  ? 1.5634 1.6214 1.5793 -0.1128 0.0710  0.0148  54   VAL H CB  
6319 C CG1 . VAL C 57  ? 1.3533 1.4012 1.4098 -0.1130 0.0921  0.0244  54   VAL H CG1 
6320 C CG2 . VAL C 57  ? 1.4235 1.4835 1.4342 -0.1075 0.0528  0.0286  54   VAL H CG2 
6321 N N   . SER C 58  ? 1.1715 1.2307 1.2060 -0.1193 0.0671  -0.0147 55   SER H N   
6322 C CA  . SER C 58  ? 1.1757 1.2283 1.2123 -0.1245 0.0864  -0.0285 55   SER H CA  
6323 C C   . SER C 58  ? 1.1296 1.1725 1.2081 -0.1201 0.0920  -0.0198 55   SER H C   
6324 O O   . SER C 58  ? 1.1135 1.1465 1.1998 -0.1231 0.1149  -0.0268 55   SER H O   
6325 C CB  . SER C 58  ? 1.2106 1.2712 1.2188 -0.1293 0.0765  -0.0468 55   SER H CB  
6326 O OG  . SER C 58  ? 1.0067 1.0730 1.0223 -0.1240 0.0502  -0.0407 55   SER H OG  
6327 N N   . LYS C 59  ? 1.0501 1.0955 1.1549 -0.1125 0.0720  -0.0051 56   LYS H N   
6328 C CA  . LYS C 59  ? 0.7999 0.8388 0.9451 -0.1058 0.0745  0.0044  56   LYS H CA  
6329 C C   . LYS C 59  ? 0.8350 0.8757 1.0130 -0.1004 0.0712  0.0226  56   LYS H C   
6330 O O   . LYS C 59  ? 0.9838 1.0312 1.1565 -0.0997 0.0548  0.0300  56   LYS H O   
6331 C CB  . LYS C 59  ? 0.8024 0.8441 0.9513 -0.1005 0.0522  0.0040  56   LYS H CB  
6332 C CG  . LYS C 59  ? 0.7869 0.8291 0.9037 -0.1064 0.0521  -0.0139 56   LYS H CG  
6333 C CD  . LYS C 59  ? 0.8901 0.9194 1.0124 -0.1093 0.0778  -0.0238 56   LYS H CD  
6334 C CE  . LYS C 59  ? 0.8932 0.9231 0.9872 -0.1162 0.0777  -0.0423 56   LYS H CE  
6335 N NZ  . LYS C 59  ? 1.0685 1.1086 1.1257 -0.1260 0.0784  -0.0564 56   LYS H NZ  
6336 N N   . LYS C 60  ? 0.8981 0.9327 1.1106 -0.0967 0.0877  0.0295  57   LYS H N   
6337 C CA  . LYS C 60  ? 0.7645 0.8023 1.0135 -0.0923 0.0876  0.0456  57   LYS H CA  
6338 C C   . LYS C 60  ? 0.8627 0.8996 1.1534 -0.0834 0.0893  0.0531  57   LYS H C   
6339 O O   . LYS C 60  ? 0.8496 0.8784 1.1403 -0.0816 0.1030  0.0463  57   LYS H O   
6340 C CB  . LYS C 60  ? 0.7690 0.8021 1.0153 -0.0975 0.1134  0.0470  57   LYS H CB  
6341 C CG  . LYS C 60  ? 0.8630 0.8969 1.0662 -0.1043 0.1138  0.0402  57   LYS H CG  
6342 C CD  . LYS C 60  ? 1.0912 1.1176 1.2839 -0.1088 0.1439  0.0370  57   LYS H CD  
6343 C CE  . LYS C 60  ? 1.0624 1.0904 1.2066 -0.1141 0.1446  0.0275  57   LYS H CE  
6344 N NZ  . LYS C 60  ? 1.1177 1.1377 1.2475 -0.1178 0.1742  0.0227  57   LYS H NZ  
6345 N N   . ASP C 61  ? 0.7394 0.7847 1.0657 -0.0775 0.0756  0.0667  58   ASP H N   
6346 C CA  . ASP C 61  ? 0.8369 0.8852 1.2059 -0.0674 0.0756  0.0748  58   ASP H CA  
6347 C C   . ASP C 61  ? 0.7749 0.8318 1.1836 -0.0661 0.0779  0.0876  58   ASP H C   
6348 O O   . ASP C 61  ? 0.9512 1.0117 1.3556 -0.0718 0.0719  0.0918  58   ASP H O   
6349 C CB  . ASP C 61  ? 0.8017 0.8554 1.1764 -0.0587 0.0478  0.0760  58   ASP H CB  
6350 C CG  . ASP C 61  ? 1.0195 1.0656 1.3986 -0.0507 0.0567  0.0721  58   ASP H CG  
6351 O OD1 . ASP C 61  ? 0.9987 1.0410 1.3543 -0.0491 0.0455  0.0651  58   ASP H OD1 
6352 O OD2 . ASP C 61  ? 0.9186 0.9620 1.3241 -0.0456 0.0763  0.0764  58   ASP H OD2 
6353 N N   . TYR C 62  ? 0.7791 1.0067 1.2802 0.0379  0.1387  0.0546  59   TYR H N   
6354 C CA  . TYR C 62  ? 0.7470 1.0059 1.3328 0.0256  0.1397  0.0460  59   TYR H CA  
6355 C C   . TYR C 62  ? 0.8084 1.1121 1.4204 0.0224  0.0996  0.0297  59   TYR H C   
6356 O O   . TYR C 62  ? 0.8400 1.1527 1.4072 0.0328  0.0732  0.0298  59   TYR H O   
6357 C CB  . TYR C 62  ? 0.6906 0.9560 1.3145 0.0356  0.1645  0.0687  59   TYR H CB  
6358 C CG  . TYR C 62  ? 0.6727 0.8953 1.2686 0.0415  0.2041  0.0880  59   TYR H CG  
6359 C CD1 . TYR C 62  ? 0.6888 0.8865 1.2162 0.0596  0.2109  0.1073  59   TYR H CD1 
6360 C CD2 . TYR C 62  ? 0.6465 0.8538 1.2847 0.0290  0.2346  0.0871  59   TYR H CD2 
6361 C CE1 . TYR C 62  ? 0.7221 0.8807 1.2237 0.0650  0.2468  0.1249  59   TYR H CE1 
6362 C CE2 . TYR C 62  ? 0.8024 0.9706 1.4153 0.0343  0.2706  0.1048  59   TYR H CE2 
6363 C CZ  . TYR C 62  ? 0.8105 0.9546 1.3550 0.0523  0.2766  0.1236  59   TYR H CZ  
6364 O OH  . TYR C 62  ? 0.8897 0.9949 1.4087 0.0576  0.3124  0.1413  59   TYR H OH  
6365 N N   . ALA C 63  ? 0.6631 0.9948 1.3486 0.0078  0.0955  0.0158  60   ALA H N   
6366 C CA  . ALA C 63  ? 0.6898 1.0669 1.4106 0.0042  0.0595  0.0011  60   ALA H CA  
6367 C C   . ALA C 63  ? 0.7704 1.1781 1.5226 0.0184  0.0562  0.0183  60   ALA H C   
6368 O O   . ALA C 63  ? 0.8474 1.2453 1.6147 0.0264  0.0845  0.0383  60   ALA H O   
6369 C CB  . ALA C 63  ? 0.6872 1.0817 1.4735 -0.0180 0.0557  -0.0220 60   ALA H CB  
6370 N N   . ASP C 64  ? 0.7196 1.1649 1.4818 0.0214  0.0207  0.0101  61   ASP H N   
6371 C CA  . ASP C 64  ? 0.8461 1.3217 1.6330 0.0359  0.0137  0.0259  61   ASP H CA  
6372 C C   . ASP C 64  ? 0.8274 1.3233 1.6965 0.0291  0.0316  0.0289  61   ASP H C   
6373 O O   . ASP C 64  ? 0.8360 1.3367 1.7209 0.0416  0.0475  0.0496  61   ASP H O   
6374 C CB  . ASP C 64  ? 0.7984 1.3110 1.5817 0.0388  -0.0293 0.0143  61   ASP H CB  
6375 C CG  . ASP C 64  ? 0.9571 1.4523 1.6577 0.0486  -0.0476 0.0146  61   ASP H CG  
6376 O OD1 . ASP C 64  ? 1.0214 1.5169 1.7029 0.0379  -0.0693 -0.0063 61   ASP H OD1 
6377 O OD2 . ASP C 64  ? 1.2056 1.6862 1.8599 0.0669  -0.0401 0.0357  61   ASP H OD2 
6378 N N   . SER C 65  ? 0.9075 1.4152 1.8296 0.0092  0.0296  0.0085  62   SER H N   
6379 C CA  . SER C 65  ? 0.9889 1.5182 1.9920 0.0013  0.0443  0.0092  62   SER H CA  
6380 C C   . SER C 65  ? 0.9409 1.4398 1.9528 0.0032  0.0876  0.0270  62   SER H C   
6381 O O   . SER C 65  ? 0.8674 1.3826 1.9435 -0.0007 0.1030  0.0317  62   SER H O   
6382 C CB  . SER C 65  ? 0.9431 1.4891 1.9964 -0.0212 0.0323  -0.0178 62   SER H CB  
6383 O OG  . SER C 65  ? 0.9356 1.4459 1.9588 -0.0330 0.0448  -0.0287 62   SER H OG  
6384 N N   . VAL C 66  ? 0.8796 1.3351 1.8293 0.0089  0.1076  0.0370  63   VAL H N   
6385 C CA  . VAL C 66  ? 0.8656 1.2892 1.8216 0.0088  0.1491  0.0520  63   VAL H CA  
6386 C C   . VAL C 66  ? 0.9126 1.3079 1.8054 0.0290  0.1651  0.0771  63   VAL H C   
6387 O O   . VAL C 66  ? 0.8928 1.2633 1.7871 0.0328  0.1995  0.0939  63   VAL H O   
6388 C CB  . VAL C 66  ? 0.9154 1.3086 1.8665 -0.0091 0.1643  0.0368  63   VAL H CB  
6389 C CG1 . VAL C 66  ? 0.8715 1.2490 1.8659 -0.0154 0.2027  0.0460  63   VAL H CG1 
6390 C CG2 . VAL C 66  ? 0.9652 1.3825 1.9489 -0.0273 0.1370  0.0082  63   VAL H CG2 
6391 N N   . LYS C 67  ? 0.9832 1.3822 1.8202 0.0420  0.1403  0.0800  64   LYS H N   
6392 C CA  . LYS C 67  ? 0.8735 1.2430 1.6424 0.0606  0.1531  0.1019  64   LYS H CA  
6393 C C   . LYS C 67  ? 0.9415 1.3153 1.7346 0.0742  0.1760  0.1268  64   LYS H C   
6394 O O   . LYS C 67  ? 0.9535 1.3643 1.7915 0.0789  0.1635  0.1301  64   LYS H O   
6395 C CB  . LYS C 67  ? 0.8081 1.1880 1.5214 0.0721  0.1188  0.0998  64   LYS H CB  
6396 C CG  . LYS C 67  ? 0.8811 1.2249 1.5127 0.0883  0.1290  0.1174  64   LYS H CG  
6397 C CD  . LYS C 67  ? 0.9950 1.3392 1.5667 0.0915  0.0962  0.1062  64   LYS H CD  
6398 C CE  . LYS C 67  ? 1.0233 1.3316 1.5127 0.1076  0.1057  0.1234  64   LYS H CE  
6399 N NZ  . LYS C 67  ? 1.1345 1.4522 1.6140 0.1282  0.1088  0.1477  64   LYS H NZ  
6400 N N   . GLY C 68  ? 0.8497 1.1853 1.6131 0.0804  0.2099  0.1443  65   GLY H N   
6401 C CA  . GLY C 68  ? 0.8975 1.2318 1.6807 0.0926  0.2357  0.1683  65   GLY H CA  
6402 C C   . GLY C 68  ? 0.9524 1.2861 1.8026 0.0804  0.2648  0.1687  65   GLY H C   
6403 O O   . GLY C 68  ? 1.0600 1.3810 1.9181 0.0890  0.2938  0.1893  65   GLY H O   
6404 N N   . ARG C 69  ? 0.9479 1.2951 1.8464 0.0606  0.2581  0.1466  66   ARG H N   
6405 C CA  . ARG C 69  ? 0.8948 1.2431 1.8598 0.0475  0.2842  0.1450  66   ARG H CA  
6406 C C   . ARG C 69  ? 0.9685 1.2755 1.9163 0.0351  0.3103  0.1397  66   ARG H C   
6407 O O   . ARG C 69  ? 0.8933 1.1831 1.8663 0.0325  0.3439  0.1506  66   ARG H O   
6408 C CB  . ARG C 69  ? 0.7539 1.1450 1.7902 0.0331  0.2619  0.1246  66   ARG H CB  
6409 C CG  . ARG C 69  ? 0.8093 1.2432 1.8639 0.0442  0.2330  0.1275  66   ARG H CG  
6410 C CD  . ARG C 69  ? 0.7876 1.2637 1.9248 0.0312  0.2197  0.1126  66   ARG H CD  
6411 N NE  . ARG C 69  ? 0.8788 1.3630 2.0282 0.0129  0.1987  0.0852  66   ARG H NE  
6412 C CZ  . ARG C 69  ? 0.8033 1.2814 1.9949 -0.0061 0.2126  0.0712  66   ARG H CZ  
6413 N NH1 . ARG C 69  ? 0.8012 1.2652 2.0274 -0.0094 0.2475  0.0822  66   ARG H NH1 
6414 N NH2 . ARG C 69  ? 0.8391 1.3254 2.0386 -0.0219 0.1915  0.0464  66   ARG H NH2 
6415 N N   . PHE C 70  ? 0.8349 1.1256 1.7404 0.0274  0.2958  0.1233  67   PHE H N   
6416 C CA  . PHE C 70  ? 0.8659 1.1155 1.7473 0.0167  0.3191  0.1184  67   PHE H CA  
6417 C C   . PHE C 70  ? 0.7870 0.9979 1.5835 0.0309  0.3279  0.1329  67   PHE H C   
6418 O O   . PHE C 70  ? 0.8656 1.0834 1.6163 0.0452  0.3066  0.1386  67   PHE H O   
6419 C CB  . PHE C 70  ? 0.7786 1.0322 1.6690 -0.0026 0.2996  0.0899  67   PHE H CB  
6420 C CG  . PHE C 70  ? 0.7538 1.0406 1.7273 -0.0193 0.2937  0.0737  67   PHE H CG  
6421 C CD1 . PHE C 70  ? 0.8701 1.1595 1.8599 -0.0383 0.2806  0.0482  67   PHE H CD1 
6422 C CD2 . PHE C 70  ? 0.7958 1.1112 1.8306 -0.0160 0.3006  0.0835  67   PHE H CD2 
6423 C CE1 . PHE C 70  ? 0.9281 1.2478 1.9933 -0.0538 0.2746  0.0330  67   PHE H CE1 
6424 C CE2 . PHE C 70  ? 0.8442 1.1903 1.9548 -0.0314 0.2946  0.0683  67   PHE H CE2 
6425 C CZ  . PHE C 70  ? 0.8904 1.2386 2.0162 -0.0503 0.2816  0.0431  67   PHE H CZ  
6426 N N   . THR C 71  ? 0.8349 1.0050 1.6109 0.0268  0.3594  0.1387  68   THR H N   
6427 C CA  . THR C 71  ? 0.9039 1.0333 1.5996 0.0376  0.3700  0.1502  68   THR H CA  
6428 C C   . THR C 71  ? 0.9060 1.0014 1.5850 0.0221  0.3837  0.1366  68   THR H C   
6429 O O   . THR C 71  ? 0.9719 1.0520 1.6845 0.0113  0.4071  0.1354  68   THR H O   
6430 C CB  . THR C 71  ? 0.8669 0.9678 1.5311 0.0536  0.3904  0.1756  68   THR H CB  
6431 O OG1 . THR C 71  ? 1.1356 1.2708 1.8195 0.0677  0.3797  0.1889  68   THR H OG1 
6432 C CG2 . THR C 71  ? 0.8359 0.8875 1.4045 0.0644  0.3908  0.1835  68   THR H CG2 
6433 N N   . ILE C 72  ? 1.1547 1.2447 1.1433 -0.3867 0.0933  0.2415  69   ILE H N   
6434 C CA  . ILE C 72  ? 1.1798 1.2715 1.1275 -0.3599 0.0993  0.2332  69   ILE H CA  
6435 C C   . ILE C 72  ? 1.1317 1.2662 1.0951 -0.3347 0.0916  0.2091  69   ILE H C   
6436 O O   . ILE C 72  ? 1.1566 1.3380 1.1605 -0.3446 0.0871  0.2011  69   ILE H O   
6437 C CB  . ILE C 72  ? 1.0968 1.1968 1.0390 -0.3770 0.1081  0.2437  69   ILE H CB  
6438 C CG1 . ILE C 72  ? 1.1799 1.2886 1.0845 -0.3484 0.1135  0.2328  69   ILE H CG1 
6439 C CG2 . ILE C 72  ? 1.1755 1.3204 1.1740 -0.4057 0.1039  0.2441  69   ILE H CG2 
6440 C CD1 . ILE C 72  ? 1.1258 1.2366 1.0177 -0.3629 0.1231  0.2439  69   ILE H CD1 
6441 N N   . SER C 73  ? 1.3136 1.4318 1.2452 -0.3020 0.0898  0.1977  70   SER H N   
6442 C CA  . SER C 73  ? 1.2118 1.3665 1.1533 -0.2750 0.0825  0.1747  70   SER H CA  
6443 C C   . SER C 73  ? 1.2733 1.4401 1.1814 -0.2516 0.0887  0.1661  70   SER H C   
6444 O O   . SER C 73  ? 1.3536 1.4920 1.2229 -0.2514 0.0988  0.1775  70   SER H O   
6445 C CB  . SER C 73  ? 1.2617 1.3939 1.1888 -0.2517 0.0766  0.1660  70   SER H CB  
6446 O OG  . SER C 73  ? 1.3371 1.4950 1.2563 -0.2191 0.0722  0.1446  70   SER H OG  
6447 N N   . LYS C 78  ? 1.3097 1.5247 0.9646 0.0390  0.0929  0.0406  75   LYS H N   
6448 C CA  . LYS C 78  ? 1.3317 1.4913 0.9327 0.0458  0.1026  0.0537  75   LYS H CA  
6449 C C   . LYS C 78  ? 1.3352 1.4862 0.9227 0.0261  0.1134  0.0695  75   LYS H C   
6450 O O   . LYS C 78  ? 1.4967 1.6088 1.0357 0.0348  0.1229  0.0787  75   LYS H O   
6451 C CB  . LYS C 78  ? 1.3251 1.4439 0.9264 0.0335  0.1001  0.0648  75   LYS H CB  
6452 C CG  . LYS C 78  ? 1.3472 1.4827 0.9830 0.0378  0.0877  0.0527  75   LYS H CG  
6453 C CD  . LYS C 78  ? 1.3914 1.4940 1.0406 0.0140  0.0857  0.0674  75   LYS H CD  
6454 C CE  . LYS C 78  ? 1.3714 1.4811 1.0449 0.0228  0.0743  0.0557  75   LYS H CE  
6455 N NZ  . LYS C 78  ? 1.3098 1.3940 0.9407 0.0591  0.0741  0.0457  75   LYS H NZ  
6456 N N   . ASN C 79  ? 1.4173 1.2269 1.1655 -0.0233 0.2450  0.1407  76   ASN H N   
6457 C CA  . ASN C 79  ? 1.3473 1.1589 1.1349 -0.0236 0.2249  0.1364  76   ASN H CA  
6458 C C   . ASN C 79  ? 1.2189 1.0314 1.0594 -0.0334 0.2365  0.1391  76   ASN H C   
6459 O O   . ASN C 79  ? 1.2154 1.0193 1.0836 -0.0361 0.2255  0.1444  76   ASN H O   
6460 C CB  . ASN C 79  ? 1.2974 1.0935 1.0670 -0.0176 0.2054  0.1458  76   ASN H CB  
6461 C CG  . ASN C 79  ? 1.3823 1.1869 1.1723 -0.0125 0.1792  0.1358  76   ASN H CG  
6462 O OD1 . ASN C 79  ? 1.4416 1.2552 1.2760 -0.0173 0.1758  0.1285  76   ASN H OD1 
6463 N ND2 . ASN C 79  ? 1.4728 1.2764 1.2302 -0.0024 0.1607  0.1359  76   ASN H ND2 
6464 N N   . THR C 80  ? 1.2670 1.0901 1.1218 -0.0386 0.2586  0.1351  77   THR H N   
6465 C CA  . THR C 80  ? 1.2860 1.1139 1.1925 -0.0480 0.2717  0.1376  77   THR H CA  
6466 C C   . THR C 80  ? 1.4123 1.2603 1.3514 -0.0488 0.2713  0.1202  77   THR H C   
6467 O O   . THR C 80  ? 1.4025 1.2599 1.3194 -0.0432 0.2698  0.1077  77   THR H O   
6468 C CB  . THR C 80  ? 1.3359 1.1611 1.2369 -0.0536 0.3010  0.1507  77   THR H CB  
6469 O OG1 . THR C 80  ? 1.4343 1.2734 1.3190 -0.0507 0.3185  0.1401  77   THR H OG1 
6470 C CG2 . THR C 80  ? 1.2294 1.0362 1.0881 -0.0520 0.3019  0.1678  77   THR H CG2 
6471 N N   . LEU C 81  ? 1.5514 1.4050 1.5442 -0.0562 0.2716  0.1201  78   LEU H N   
6472 C CA  . LEU C 81  ? 1.4443 1.3166 1.4759 -0.0582 0.2712  0.1056  78   LEU H CA  
6473 C C   . LEU C 81  ? 1.4827 1.3627 1.5472 -0.0653 0.2982  0.1095  78   LEU H C   
6474 O O   . LEU C 81  ? 1.5836 1.4563 1.6673 -0.0724 0.3083  0.1244  78   LEU H O   
6475 C CB  . LEU C 81  ? 1.3610 1.2372 1.4314 -0.0609 0.2472  0.1016  78   LEU H CB  
6476 C CG  . LEU C 81  ? 1.3140 1.2103 1.4247 -0.0631 0.2417  0.0872  78   LEU H CG  
6477 C CD1 . LEU C 81  ? 1.3543 1.2601 1.4369 -0.0552 0.2281  0.0737  78   LEU H CD1 
6478 C CD2 . LEU C 81  ? 1.1931 1.0924 1.3495 -0.0688 0.2239  0.0878  78   LEU H CD2 
6479 N N   . TYR C 82  ? 1.2038 1.0987 1.2758 -0.0630 0.3093  0.0963  79   TYR H N   
6480 C CA  . TYR C 82  ? 1.1640 1.0694 1.2652 -0.0673 0.3363  0.0979  79   TYR H CA  
6481 C C   . TYR C 82  ? 1.1350 1.0562 1.2927 -0.0710 0.3316  0.0870  79   TYR H C   
6482 O O   . TYR C 82  ? 1.2631 1.1892 1.4299 -0.0691 0.3091  0.0754  79   TYR H O   
6483 C CB  . TYR C 82  ? 1.2721 1.1815 1.3338 -0.0602 0.3570  0.0911  79   TYR H CB  
6484 C CG  . TYR C 82  ? 1.3664 1.2621 1.3724 -0.0573 0.3645  0.1031  79   TYR H CG  
6485 C CD1 . TYR C 82  ? 1.2990 1.1854 1.2551 -0.0502 0.3481  0.0985  79   TYR H CD1 
6486 C CD2 . TYR C 82  ? 1.4900 1.3836 1.4945 -0.0620 0.3877  0.1204  79   TYR H CD2 
6487 C CE1 . TYR C 82  ? 1.4684 1.3426 1.3743 -0.0477 0.3543  0.1101  79   TYR H CE1 
6488 C CE2 . TYR C 82  ? 1.4625 1.3443 1.4168 -0.0599 0.3940  0.1327  79   TYR H CE2 
6489 C CZ  . TYR C 82  ? 1.5600 1.4316 1.4650 -0.0526 0.3771  0.1272  79   TYR H CZ  
6490 O OH  . TYR C 82  ? 1.3068 1.1669 1.1624 -0.0508 0.3827  0.1401  79   TYR H OH  
6491 N N   . LEU C 83  ? 1.0848 1.0158 1.2818 -0.0767 0.3531  0.0921  80   LEU H N   
6492 C CA  . LEU C 83  ? 1.1120 1.0592 1.3657 -0.0804 0.3520  0.0831  80   LEU H CA  
6493 C C   . LEU C 83  ? 1.1378 1.0981 1.4091 -0.0802 0.3839  0.0838  80   LEU H C   
6494 O O   . LEU C 83  ? 1.2347 1.1972 1.5287 -0.0871 0.4005  0.0996  80   LEU H O   
6495 C CB  . LEU C 83  ? 1.0535 0.9994 1.3539 -0.0904 0.3368  0.0923  80   LEU H CB  
6496 C CG  . LEU C 83  ? 1.0791 1.0423 1.4427 -0.0961 0.3364  0.0863  80   LEU H CG  
6497 C CD1 . LEU C 83  ? 1.0747 1.0484 1.4400 -0.0899 0.3230  0.0667  80   LEU H CD1 
6498 C CD2 . LEU C 83  ? 1.0769 1.0368 1.4810 -0.1062 0.3189  0.0958  80   LEU H CD2 
6499 N N   . GLN C 84  ? 1.0244 0.9936 1.2852 -0.0719 0.3916  0.0669  81   GLN H N   
6500 C CA  . GLN C 84  ? 1.2232 1.2065 1.4986 -0.0689 0.4218  0.0642  81   GLN H CA  
6501 C C   . GLN C 84  ? 1.1843 1.1837 1.5288 -0.0742 0.4228  0.0612  81   GLN H C   
6502 O O   . GLN C 84  ? 1.0788 1.0825 1.4450 -0.0730 0.4043  0.0472  81   GLN H O   
6503 C CB  . GLN C 84  ? 1.1546 1.1384 1.3888 -0.0567 0.4282  0.0457  81   GLN H CB  
6504 C CG  . GLN C 84  ? 1.2802 1.2762 1.5121 -0.0508 0.4622  0.0434  81   GLN H CG  
6505 C CD  . GLN C 84  ? 1.3465 1.3366 1.5299 -0.0496 0.4814  0.0573  81   GLN H CD  
6506 O OE1 . GLN C 84  ? 1.2672 1.2676 1.4665 -0.0532 0.5058  0.0720  81   GLN H OE1 
6507 N NE2 . GLN C 84  ? 1.3921 1.3671 1.5166 -0.0447 0.4700  0.0541  81   GLN H NE2 
6508 N N   . MET C 85  ? 1.1255 1.1349 1.5052 -0.0805 0.4438  0.0755  82   MET H N   
6509 C CA  . MET C 85  ? 1.1245 1.1505 1.5727 -0.0866 0.4467  0.0759  82   MET H CA  
6510 C C   . MET C 85  ? 1.2345 1.2788 1.6950 -0.0790 0.4773  0.0690  82   MET H C   
6511 O O   . MET C 85  ? 1.2946 1.3477 1.7584 -0.0806 0.5036  0.0830  82   MET H O   
6512 C CB  . MET C 85  ? 1.1758 1.2005 1.6592 -0.1001 0.4455  0.0982  82   MET H CB  
6513 C CG  . MET C 85  ? 0.9890 0.9942 1.4571 -0.1059 0.4157  0.1040  82   MET H CG  
6514 S SD  . MET C 85  ? 1.1712 1.1662 1.6574 -0.1197 0.4165  0.1315  82   MET H SD  
6515 C CE  . MET C 85  ? 0.9642 0.9753 1.5333 -0.1312 0.4120  0.1354  82   MET H CE  
6516 N N   . ASN C 86  A 1.2005 1.2509 1.6680 -0.0704 0.4734  0.0478  82   ASN H N   
6517 C CA  . ASN C 86  A 1.2124 1.2787 1.6900 -0.0605 0.5000  0.0369  82   ASN H CA  
6518 C C   . ASN C 86  A 1.2286 1.3132 1.7791 -0.0643 0.5018  0.0351  82   ASN H C   
6519 O O   . ASN C 86  A 1.2166 1.2997 1.8018 -0.0714 0.4766  0.0332  82   ASN H O   
6520 C CB  . ASN C 86  A 1.1694 1.2281 1.6037 -0.0471 0.4948  0.0131  82   ASN H CB  
6521 C CG  . ASN C 86  A 1.3286 1.3744 1.6906 -0.0410 0.5030  0.0144  82   ASN H CG  
6522 O OD1 . ASN C 86  A 1.2059 1.2465 1.5482 -0.0473 0.5087  0.0335  82   ASN H OD1 
6523 N ND2 . ASN C 86  A 1.3690 1.4088 1.6911 -0.0290 0.5025  -0.0056 82   ASN H ND2 
6524 N N   . SER C 87  B 1.2340 1.3376 1.8073 -0.0590 0.5322  0.0360  82   SER H N   
6525 C CA  . SER C 87  B 1.1266 1.2506 1.7711 -0.0618 0.5385  0.0362  82   SER H CA  
6526 C C   . SER C 87  B 1.1864 1.3115 1.8781 -0.0789 0.5232  0.0558  82   SER H C   
6527 O O   . SER C 87  B 1.2013 1.3334 1.9453 -0.0843 0.5079  0.0527  82   SER H O   
6528 C CB  . SER C 87  B 1.1809 1.3055 1.8429 -0.0535 0.5239  0.0120  82   SER H CB  
6529 O OG  . SER C 87  B 1.1073 1.2503 1.8410 -0.0575 0.5260  0.0137  82   SER H OG  
6530 N N   . LEU C 88  C 1.3391 1.4566 2.0118 -0.0877 0.5262  0.0764  82   LEU H N   
6531 C CA  . LEU C 88  C 1.3024 1.4155 2.0108 -0.1039 0.5087  0.0946  82   LEU H CA  
6532 C C   . LEU C 88  C 1.1177 1.2540 1.8977 -0.1110 0.5221  0.1053  82   LEU H C   
6533 O O   . LEU C 88  C 1.0221 1.1723 1.8149 -0.1135 0.5482  0.1215  82   LEU H O   
6534 C CB  . LEU C 88  C 1.1798 1.2783 1.8507 -0.1106 0.5107  0.1141  82   LEU H CB  
6535 C CG  . LEU C 88  C 1.2462 1.3468 1.8691 -0.1029 0.5393  0.1196  82   LEU H CG  
6536 C CD1 . LEU C 88  C 1.3756 1.5005 2.0352 -0.1063 0.5709  0.1366  82   LEU H CD1 
6537 C CD2 . LEU C 88  C 1.2501 1.3277 1.8235 -0.1076 0.5280  0.1318  82   LEU H CD2 
6538 N N   . ARG C 89  ? 1.2330 1.3751 2.0610 -0.1146 0.5039  0.0972  83   ARG H N   
6539 C CA  . ARG C 89  ? 1.1577 1.3214 2.0572 -0.1226 0.5124  0.1079  83   ARG H CA  
6540 C C   . ARG C 89  ? 1.1565 1.3149 2.0792 -0.1402 0.5035  0.1326  83   ARG H C   
6541 O O   . ARG C 89  ? 1.1764 1.3130 2.0616 -0.1454 0.4877  0.1391  83   ARG H O   
6542 C CB  . ARG C 89  ? 1.3303 1.5007 2.2720 -0.1216 0.4934  0.0921  83   ARG H CB  
6543 C CG  . ARG C 89  ? 1.4042 1.5732 2.3169 -0.1048 0.4955  0.0666  83   ARG H CG  
6544 C CD  . ARG C 89  ? 1.3247 1.4966 2.2740 -0.1051 0.4710  0.0520  83   ARG H CD  
6545 N NE  . ARG C 89  ? 1.3998 1.5592 2.3521 -0.1173 0.4373  0.0570  83   ARG H NE  
6546 C CZ  . ARG C 89  ? 1.5486 1.7163 2.5566 -0.1305 0.4227  0.0673  83   ARG H CZ  
6547 N NH1 . ARG C 89  ? 1.6116 1.8002 2.6789 -0.1335 0.4387  0.0746  83   ARG H NH1 
6548 N NH2 . ARG C 89  ? 1.4397 1.5960 2.4442 -0.1400 0.3922  0.0702  83   ARG H NH2 
6549 N N   . ALA C 90  ? 1.3005 1.4786 2.2864 -0.1492 0.5130  0.1466  84   ALA H N   
6550 C CA  . ALA C 90  ? 1.2700 1.4460 2.2795 -0.1656 0.5115  0.1728  84   ALA H CA  
6551 C C   . ALA C 90  ? 1.1339 1.2914 2.1569 -0.1786 0.4751  0.1760  84   ALA H C   
6552 O O   . ALA C 90  ? 1.2485 1.3957 2.2735 -0.1887 0.4634  0.1937  84   ALA H O   
6553 C CB  . ALA C 90  ? 1.1663 1.3663 2.2232 -0.1669 0.5255  0.1844  84   ALA H CB  
6554 N N   . GLU C 91  ? 1.2127 1.3628 2.2319 -0.1751 0.4503  0.1573  85   GLU H N   
6555 C CA  . GLU C 91  ? 1.2294 1.3641 2.2560 -0.1843 0.4130  0.1578  85   GLU H CA  
6556 C C   . GLU C 91  ? 1.1209 1.2302 2.0944 -0.1842 0.3958  0.1544  85   GLU H C   
6557 O O   . GLU C 91  ? 1.0374 1.1355 2.0157 -0.1908 0.3665  0.1523  85   GLU H O   
6558 C CB  . GLU C 91  ? 1.3768 1.5198 2.4277 -0.1796 0.3905  0.1407  85   GLU H CB  
6559 C CG  . GLU C 91  ? 1.2781 1.4335 2.3294 -0.1690 0.4064  0.1223  85   GLU H CG  
6560 C CD  . GLU C 91  ? 1.3807 1.5575 2.4598 -0.1609 0.4333  0.1213  85   GLU H CD  
6561 O OE1 . GLU C 91  ? 1.5335 1.7189 2.6465 -0.1600 0.4205  0.1204  85   GLU H OE1 
6562 O OE2 . GLU C 91  ? 1.3383 1.5210 2.3955 -0.1528 0.4642  0.1205  85   GLU H OE2 
6563 N N   . ASP C 92  ? 0.9527 1.0522 1.8689 -0.1747 0.4104  0.1526  86   ASP H N   
6564 C CA  . ASP C 92  ? 0.9414 1.0155 1.7990 -0.1718 0.3926  0.1496  86   ASP H CA  
6565 C C   . ASP C 92  ? 1.1484 1.2062 1.9940 -0.1813 0.3934  0.1709  86   ASP H C   
6566 O O   . ASP C 92  ? 1.1234 1.1599 1.9178 -0.1779 0.3829  0.1707  86   ASP H O   
6567 C CB  . ASP C 92  ? 1.1189 1.1895 1.9178 -0.1563 0.4044  0.1353  86   ASP H CB  
6568 C CG  . ASP C 92  ? 1.0411 1.1265 1.8518 -0.1466 0.4052  0.1146  86   ASP H CG  
6569 O OD1 . ASP C 92  ? 1.0245 1.1235 1.8354 -0.1382 0.4315  0.1100  86   ASP H OD1 
6570 O OD2 . ASP C 92  ? 0.9821 1.0660 1.8026 -0.1473 0.3792  0.1033  86   ASP H OD2 
6571 N N   . THR C 93  ? 1.2010 1.2685 2.0937 -0.1930 0.4050  0.1899  87   THR H N   
6572 C CA  . THR C 93  ? 1.1142 1.1659 2.0011 -0.2036 0.4044  0.2121  87   THR H CA  
6573 C C   . THR C 93  ? 1.0625 1.0887 1.9385 -0.2095 0.3695  0.2107  87   THR H C   
6574 O O   . THR C 93  ? 1.0959 1.1244 2.0119 -0.2170 0.3490  0.2076  87   THR H O   
6575 C CB  . THR C 93  ? 1.1688 1.2382 2.1168 -0.2167 0.4196  0.2328  87   THR H CB  
6576 O OG1 . THR C 93  ? 1.1866 1.2786 2.1351 -0.2102 0.4552  0.2375  87   THR H OG1 
6577 C CG2 . THR C 93  ? 1.0321 1.0815 1.9775 -0.2290 0.4076  0.2542  87   THR H CG2 
6578 N N   . ALA C 94  ? 1.1059 1.1084 1.9275 -0.2054 0.3627  0.2129  88   ALA H N   
6579 C CA  . ALA C 94  ? 1.0522 1.0296 1.8546 -0.2073 0.3303  0.2090  88   ALA H CA  
6580 C C   . ALA C 94  ? 0.9841 0.9377 1.7292 -0.2029 0.3311  0.2164  88   ALA H C   
6581 O O   . ALA C 94  ? 0.9099 0.8677 1.6263 -0.1974 0.3555  0.2219  88   ALA H O   
6582 C CB  . ALA C 94  ? 0.9226 0.9035 1.7129 -0.1982 0.3098  0.1854  88   ALA H CB  
6583 N N   . VAL C 95  ? 0.8840 0.8126 1.6127 -0.2048 0.3039  0.2165  89   VAL H N   
6584 C CA  . VAL C 95  ? 1.0863 0.9904 1.7568 -0.1980 0.2980  0.2189  89   VAL H CA  
6585 C C   . VAL C 95  ? 1.0297 0.9321 1.6600 -0.1839 0.2820  0.1965  89   VAL H C   
6586 O O   . VAL C 95  ? 0.9782 0.8805 1.6225 -0.1837 0.2577  0.1845  89   VAL H O   
6587 C CB  . VAL C 95  ? 1.0331 0.9093 1.7091 -0.2074 0.2777  0.2328  89   VAL H CB  
6588 C CG1 . VAL C 95  ? 1.0300 0.9046 1.7466 -0.2143 0.2511  0.2257  89   VAL H CG1 
6589 C CG2 . VAL C 95  ? 0.9465 0.7967 1.5623 -0.1976 0.2649  0.2300  89   VAL H CG2 
6590 N N   . TYR C 96  ? 1.0496 0.9525 1.6308 -0.1726 0.2953  0.1914  90   TYR H N   
6591 C CA  . TYR C 96  ? 0.8942 0.7995 1.4379 -0.1595 0.2832  0.1713  90   TYR H CA  
6592 C C   . TYR C 96  ? 0.9489 0.8291 1.4434 -0.1530 0.2644  0.1716  90   TYR H C   
6593 O O   . TYR C 96  ? 1.0509 0.9160 1.5142 -0.1523 0.2742  0.1842  90   TYR H O   
6594 C CB  . TYR C 96  ? 0.8980 0.8190 1.4171 -0.1505 0.3075  0.1640  90   TYR H CB  
6595 C CG  . TYR C 96  ? 1.0203 0.9674 1.5837 -0.1523 0.3201  0.1560  90   TYR H CG  
6596 C CD1 . TYR C 96  ? 0.9014 0.8601 1.5170 -0.1631 0.3351  0.1685  90   TYR H CD1 
6597 C CD2 . TYR C 96  ? 0.8553 0.8156 1.4097 -0.1431 0.3164  0.1365  90   TYR H CD2 
6598 C CE1 . TYR C 96  ? 1.0183 1.0012 1.6758 -0.1637 0.3467  0.1614  90   TYR H CE1 
6599 C CE2 . TYR C 96  ? 0.8371 0.8197 1.4330 -0.1441 0.3270  0.1290  90   TYR H CE2 
6600 C CZ  . TYR C 96  ? 1.0285 1.0224 1.6759 -0.1539 0.3425  0.1411  90   TYR H CZ  
6601 O OH  . TYR C 96  ? 0.8791 0.8956 1.5694 -0.1539 0.3530  0.1337  90   TYR H OH  
6602 N N   . TYR C 97  ? 1.0440 0.9213 1.5322 -0.1480 0.2375  0.1582  91   TYR H N   
6603 C CA  . TYR C 97  ? 1.0462 0.9022 1.4907 -0.1401 0.2173  0.1563  91   TYR H CA  
6604 C C   . TYR C 97  ? 0.9625 0.8262 1.3611 -0.1263 0.2140  0.1418  91   TYR H C   
6605 O O   . TYR C 97  ? 0.9723 0.8572 1.3798 -0.1235 0.2181  0.1297  91   TYR H O   
6606 C CB  . TYR C 97  ? 1.0578 0.9057 1.5251 -0.1431 0.1881  0.1518  91   TYR H CB  
6607 C CG  . TYR C 97  ? 0.9310 0.7665 1.4400 -0.1570 0.1865  0.1664  91   TYR H CG  
6608 C CD1 . TYR C 97  ? 1.0660 0.8724 1.5591 -0.1587 0.1773  0.1781  91   TYR H CD1 
6609 C CD2 . TYR C 97  ? 1.0564 0.9086 1.6216 -0.1685 0.1928  0.1690  91   TYR H CD2 
6610 C CE1 . TYR C 97  ? 1.0998 0.8933 1.6316 -0.1723 0.1739  0.1921  91   TYR H CE1 
6611 C CE2 . TYR C 97  ? 1.0949 0.9362 1.6993 -0.1821 0.1902  0.1834  91   TYR H CE2 
6612 C CZ  . TYR C 97  ? 1.0642 0.8757 1.6515 -0.1843 0.1803  0.1949  91   TYR H CZ  
6613 O OH  . TYR C 97  ? 1.0218 0.8210 1.6488 -0.1988 0.1759  0.2099  91   TYR H OH  
6614 N N   . CYS C 98  ? 1.0518 0.8974 1.4020 -0.1179 0.2055  0.1438  92   CYS H N   
6615 C CA  . CYS C 98  ? 0.9478 0.7983 1.2515 -0.1049 0.1985  0.1320  92   CYS H CA  
6616 C C   . CYS C 98  ? 0.9603 0.8010 1.2485 -0.0980 0.1689  0.1260  92   CYS H C   
6617 O O   . CYS C 98  ? 0.9917 0.8096 1.2706 -0.0981 0.1600  0.1348  92   CYS H O   
6618 C CB  . CYS C 98  ? 1.0417 0.8820 1.2976 -0.0997 0.2163  0.1401  92   CYS H CB  
6619 S SG  . CYS C 98  ? 1.4867 1.3324 1.6838 -0.0847 0.2084  0.1276  92   CYS H SG  
6620 N N   . ALA C 99  ? 0.9653 0.8237 1.2510 -0.0916 0.1535  0.1113  93   ALA H N   
6621 C CA  . ALA C 99  ? 0.9311 0.7865 1.2057 -0.0844 0.1256  0.1045  93   ALA H CA  
6622 C C   . ALA C 99  ? 0.9764 0.8467 1.2142 -0.0725 0.1165  0.0939  93   ALA H C   
6623 O O   . ALA C 99  ? 0.9927 0.8796 1.2270 -0.0722 0.1273  0.0886  93   ALA H O   
6624 C CB  . ALA C 99  ? 0.8946 0.7606 1.2181 -0.0914 0.1100  0.0989  93   ALA H CB  
6625 N N   . ARG C 100 ? 0.8808 0.7450 1.0914 -0.0625 0.0957  0.0909  94   ARG H N   
6626 C CA  . ARG C 100 ? 0.8484 0.7287 1.0263 -0.0511 0.0829  0.0822  94   ARG H CA  
6627 C C   . ARG C 100 ? 0.8488 0.7441 1.0435 -0.0476 0.0571  0.0733  94   ARG H C   
6628 O O   . ARG C 100 ? 0.8981 0.7847 1.1190 -0.0514 0.0474  0.0738  94   ARG H O   
6629 C CB  . ARG C 100 ? 0.8986 0.7618 1.0232 -0.0400 0.0816  0.0877  94   ARG H CB  
6630 C CG  . ARG C 100 ? 0.9324 0.7811 1.0479 -0.0322 0.0609  0.0880  94   ARG H CG  
6631 C CD  . ARG C 100 ? 1.0021 0.8416 1.0656 -0.0184 0.0541  0.0905  94   ARG H CD  
6632 N NE  . ARG C 100 ? 1.0414 0.8770 1.0993 -0.0081 0.0301  0.0858  94   ARG H NE  
6633 C CZ  . ARG C 100 ? 0.9967 0.8185 1.0166 0.0048  0.0208  0.0886  94   ARG H CZ  
6634 N NH1 . ARG C 100 ? 1.0200 0.8302 1.0037 0.0079  0.0330  0.0973  94   ARG H NH1 
6635 N NH2 . ARG C 100 ? 1.0129 0.8329 1.0307 0.0152  -0.0009 0.0824  94   ARG H NH2 
6636 N N   . ASN C 101 ? 0.8066 0.7253 0.9852 -0.0403 0.0454  0.0655  95   ASN H N   
6637 C CA  . ASN C 101 ? 0.7440 0.6809 0.9308 -0.0348 0.0205  0.0579  95   ASN H CA  
6638 C C   . ASN C 101 ? 0.7476 0.7056 0.9006 -0.0243 0.0105  0.0539  95   ASN H C   
6639 O O   . ASN C 101 ? 0.8441 0.8085 0.9825 -0.0254 0.0217  0.0543  95   ASN H O   
6640 C CB  . ASN C 101 ? 0.8566 0.8126 1.0956 -0.0456 0.0156  0.0529  95   ASN H CB  
6641 C CG  . ASN C 101 ? 0.7448 0.7287 0.9948 -0.0491 0.0177  0.0482  95   ASN H CG  
6642 O OD1 . ASN C 101 ? 0.7729 0.7537 1.0230 -0.0538 0.0367  0.0499  95   ASN H OD1 
6643 N ND2 . ASN C 101 ? 0.6545 0.6658 0.9139 -0.0466 -0.0023 0.0422  95   ASN H ND2 
6644 N N   . LEU C 102 ? 0.7969 0.7659 0.9372 -0.0140 -0.0110 0.0500  96   LEU H N   
6645 C CA  . LEU C 102 ? 0.7481 0.7394 0.8568 -0.0035 -0.0228 0.0479  96   LEU H CA  
6646 C C   . LEU C 102 ? 0.7313 0.7582 0.8671 -0.0089 -0.0328 0.0425  96   LEU H C   
6647 O O   . LEU C 102 ? 0.7016 0.7409 0.8743 -0.0146 -0.0422 0.0386  96   LEU H O   
6648 C CB  . LEU C 102 ? 0.7194 0.7095 0.8023 0.0114  -0.0409 0.0467  96   LEU H CB  
6649 C CG  . LEU C 102 ? 0.7542 0.7648 0.7988 0.0241  -0.0519 0.0472  96   LEU H CG  
6650 C CD1 . LEU C 102 ? 0.7772 0.7742 0.7880 0.0246  -0.0362 0.0536  96   LEU H CD1 
6651 C CD2 . LEU C 102 ? 0.7269 0.7347 0.7489 0.0400  -0.0683 0.0456  96   LEU H CD2 
6652 N N   . ILE C 103 ? 0.7668 0.8098 0.8843 -0.0077 -0.0318 0.0429  97   ILE H N   
6653 C CA  . ILE C 103 ? 0.7068 0.7829 0.8476 -0.0131 -0.0421 0.0394  97   ILE H CA  
6654 C C   . ILE C 103 ? 0.6807 0.7799 0.7882 -0.0030 -0.0573 0.0410  97   ILE H C   
6655 O O   . ILE C 103 ? 0.7711 0.8587 0.8368 0.0067  -0.0552 0.0446  97   ILE H O   
6656 C CB  . ILE C 103 ? 0.7084 0.7818 0.8688 -0.0246 -0.0255 0.0383  97   ILE H CB  
6657 C CG1 . ILE C 103 ? 0.7981 0.8610 0.9167 -0.0203 -0.0146 0.0407  97   ILE H CG1 
6658 C CG2 . ILE C 103 ? 0.7184 0.7694 0.9096 -0.0339 -0.0080 0.0387  97   ILE H CG2 
6659 C CD1 . ILE C 103 ? 0.7472 0.8135 0.8795 -0.0287 -0.0033 0.0373  97   ILE H CD1 
6660 N N   . ARG C 104 ? 0.6733 0.8070 0.8014 -0.0060 -0.0734 0.0394  98   ARG H N   
6661 C CA  . ARG C 104 ? 0.6462 0.8064 0.7484 0.0009  -0.0879 0.0425  98   ARG H CA  
6662 C C   . ARG C 104 ? 0.6249 0.7744 0.7039 -0.0017 -0.0762 0.0444  98   ARG H C   
6663 O O   . ARG C 104 ? 0.7838 0.9201 0.8811 -0.0117 -0.0616 0.0416  98   ARG H O   
6664 C CB  . ARG C 104 ? 0.5635 0.7637 0.6978 -0.0044 -0.1068 0.0421  98   ARG H CB  
6665 C CG  . ARG C 104 ? 0.6578 0.8707 0.8182 -0.0032 -0.1185 0.0392  98   ARG H CG  
6666 C CD  . ARG C 104 ? 0.6837 0.9327 0.8841 -0.0129 -0.1329 0.0394  98   ARG H CD  
6667 N NE  . ARG C 104 ? 0.7437 1.0328 0.9320 -0.0060 -0.1540 0.0440  98   ARG H NE  
6668 C CZ  . ARG C 104 ? 0.6013 0.9205 0.8060 -0.0035 -0.1709 0.0438  98   ARG H CZ  
6669 N NH1 . ARG C 104 ? 0.4510 0.7627 0.6847 -0.0078 -0.1703 0.0384  98   ARG H NH1 
6670 N NH2 . ARG C 104 ? 0.7046 1.0628 0.8969 0.0031  -0.1888 0.0494  98   ARG H NH2 
6671 N N   . TYR C 105 ? 0.6087 0.7640 0.6466 0.0077  -0.0827 0.0490  99   TYR H N   
6672 C CA  . TYR C 105 ? 0.7346 0.8775 0.7438 0.0064  -0.0728 0.0508  99   TYR H CA  
6673 C C   . TYR C 105 ? 0.7730 0.9396 0.8013 -0.0025 -0.0819 0.0496  99   TYR H C   
6674 O O   . TYR C 105 ? 0.6285 0.8213 0.6441 0.0004  -0.0993 0.0542  99   TYR H O   
6675 C CB  . TYR C 105 ? 0.6475 0.7889 0.6075 0.0191  -0.0780 0.0571  99   TYR H CB  
6676 C CG  . TYR C 105 ? 0.6944 0.8192 0.6209 0.0179  -0.0670 0.0590  99   TYR H CG  
6677 C CD1 . TYR C 105 ? 0.7052 0.7948 0.6131 0.0177  -0.0455 0.0588  99   TYR H CD1 
6678 C CD2 . TYR C 105 ? 0.7088 0.8537 0.6222 0.0164  -0.0788 0.0615  99   TYR H CD2 
6679 C CE1 . TYR C 105 ? 0.7300 0.8054 0.6053 0.0169  -0.0354 0.0602  99   TYR H CE1 
6680 C CE2 . TYR C 105 ? 0.6899 0.8185 0.5711 0.0153  -0.0698 0.0623  99   TYR H CE2 
6681 C CZ  . TYR C 105 ? 0.7227 0.8168 0.5841 0.0158  -0.0478 0.0611  99   TYR H CZ  
6682 O OH  . TYR C 105 ? 0.9520 1.0310 0.7794 0.0150  -0.0388 0.0615  99   TYR H OH  
6683 N N   . SER C 106 ? 0.6887 0.8462 0.7492 -0.0136 -0.0705 0.0440  100  SER H N   
6684 C CA  . SER C 106 ? 0.7801 0.9542 0.8606 -0.0224 -0.0779 0.0419  100  SER H CA  
6685 C C   . SER C 106 ? 0.8114 0.9636 0.9162 -0.0312 -0.0578 0.0347  100  SER H C   
6686 O O   . SER C 106 ? 0.6453 0.7764 0.7601 -0.0320 -0.0407 0.0327  100  SER H O   
6687 C CB  . SER C 106 ? 0.7201 0.9310 0.8369 -0.0267 -0.1000 0.0440  100  SER H CB  
6688 O OG  . SER C 106 ? 0.8571 1.0667 1.0214 -0.0359 -0.0944 0.0392  100  SER H OG  
6689 N N   . GLY C 107 A 0.8431 1.0008 0.9578 -0.0376 -0.0606 0.0310  100  GLY H N   
6690 C CA  . GLY C 107 A 0.6810 0.8226 0.8233 -0.0451 -0.0433 0.0232  100  GLY H CA  
6691 C C   . GLY C 107 A 0.6478 0.7999 0.8451 -0.0528 -0.0445 0.0215  100  GLY H C   
6692 O O   . GLY C 107 A 0.7057 0.8423 0.9278 -0.0577 -0.0264 0.0162  100  GLY H O   
6693 N N   . SER C 108 B 0.7200 0.8996 0.9370 -0.0539 -0.0653 0.0262  100  SER H N   
6694 C CA  . SER C 108 B 0.6679 0.8596 0.9355 -0.0613 -0.0689 0.0255  100  SER H CA  
6695 C C   . SER C 108 B 0.6311 0.8093 0.8957 -0.0571 -0.0603 0.0270  100  SER H C   
6696 O O   . SER C 108 B 0.8512 1.0361 1.0903 -0.0489 -0.0705 0.0311  100  SER H O   
6697 C CB  . SER C 108 B 0.7272 0.9569 1.0166 -0.0648 -0.0961 0.0303  100  SER H CB  
6698 O OG  . SER C 108 B 0.7155 0.9569 1.0046 -0.0687 -0.1068 0.0306  100  SER H OG  
6699 N N   . TYR C 109 C 0.7262 0.8857 1.0176 -0.0625 -0.0423 0.0239  100  TYR H N   
6700 C CA  . TYR C 109 C 0.5954 0.7379 0.8864 -0.0601 -0.0336 0.0257  100  TYR H CA  
6701 C C   . TYR C 109 C 0.7214 0.8855 1.0358 -0.0610 -0.0533 0.0275  100  TYR H C   
6702 O O   . TYR C 109 C 0.6751 0.8590 1.0324 -0.0696 -0.0625 0.0266  100  TYR H O   
6703 C CB  . TYR C 109 C 0.5711 0.6925 0.8906 -0.0674 -0.0106 0.0234  100  TYR H CB  
6704 C CG  . TYR C 109 C 0.6122 0.7155 0.9380 -0.0674 -0.0026 0.0265  100  TYR H CG  
6705 C CD1 . TYR C 109 C 0.5866 0.7003 0.9518 -0.0733 -0.0131 0.0270  100  TYR H CD1 
6706 C CD2 . TYR C 109 C 0.7144 0.7898 1.0072 -0.0622 0.0142  0.0295  100  TYR H CD2 
6707 C CE1 . TYR C 109 C 0.6941 0.7894 1.0651 -0.0738 -0.0078 0.0298  100  TYR H CE1 
6708 C CE2 . TYR C 109 C 0.6984 0.7558 0.9982 -0.0631 0.0198  0.0334  100  TYR H CE2 
6709 C CZ  . TYR C 109 C 0.7088 0.7754 1.0477 -0.0689 0.0084  0.0331  100  TYR H CZ  
6710 O OH  . TYR C 109 C 0.6375 0.6842 0.9833 -0.0702 0.0121  0.0368  100  TYR H OH  
6711 N N   . PHE C 110 D 0.8264 0.9866 1.1127 -0.0516 -0.0599 0.0298  100  PHE H N   
6712 C CA  . PHE C 110 D 0.7321 0.9095 1.0366 -0.0507 -0.0772 0.0301  100  PHE H CA  
6713 C C   . PHE C 110 D 0.7436 0.8974 1.0169 -0.0406 -0.0734 0.0307  100  PHE H C   
6714 O O   . PHE C 110 D 0.7490 0.8975 0.9782 -0.0299 -0.0740 0.0328  100  PHE H O   
6715 C CB  . PHE C 110 D 0.6526 0.8685 0.9542 -0.0473 -0.1016 0.0321  100  PHE H CB  
6716 C CG  . PHE C 110 D 0.6794 0.9166 1.0092 -0.0490 -0.1180 0.0314  100  PHE H CG  
6717 C CD1 . PHE C 110 D 0.7034 0.9602 1.0811 -0.0613 -0.1247 0.0313  100  PHE H CD1 
6718 C CD2 . PHE C 110 D 0.6680 0.9044 0.9766 -0.0381 -0.1268 0.0303  100  PHE H CD2 
6719 C CE1 . PHE C 110 D 0.6820 0.9589 1.0851 -0.0635 -0.1399 0.0308  100  PHE H CE1 
6720 C CE2 . PHE C 110 D 0.6661 0.9219 0.9993 -0.0393 -0.1421 0.0283  100  PHE H CE2 
6721 C CZ  . PHE C 110 D 0.7575 1.0341 1.1375 -0.0525 -0.1486 0.0289  100  PHE H CZ  
6722 N N   . PRO C 111 E 0.7403 0.8795 1.0356 -0.0438 -0.0707 0.0295  100  PRO H N   
6723 C CA  . PRO C 111 E 0.7067 0.8185 0.9746 -0.0351 -0.0669 0.0303  100  PRO H CA  
6724 C C   . PRO C 111 E 0.7611 0.8878 1.0076 -0.0225 -0.0879 0.0285  100  PRO H C   
6725 O O   . PRO C 111 E 0.6383 0.7969 0.9017 -0.0227 -0.1056 0.0264  100  PRO H O   
6726 C CB  . PRO C 111 E 0.6229 0.7157 0.9287 -0.0453 -0.0585 0.0299  100  PRO H CB  
6727 C CG  . PRO C 111 E 0.6528 0.7747 1.0038 -0.0551 -0.0700 0.0275  100  PRO H CG  
6728 C CD  . PRO C 111 E 0.6467 0.7924 0.9946 -0.0564 -0.0714 0.0279  100  PRO H CD  
6729 N N   . VAL C 112 F 0.6961 0.8000 0.9049 -0.0108 -0.0855 0.0296  100  VAL H N   
6730 C CA  . VAL C 112 F 0.7060 0.8179 0.8945 0.0031  -0.1035 0.0266  100  VAL H CA  
6731 C C   . VAL C 112 F 0.7144 0.7985 0.9170 0.0023  -0.1037 0.0235  100  VAL H C   
6732 O O   . VAL C 112 F 0.9468 1.0403 1.1529 0.0090  -0.1207 0.0181  100  VAL H O   
6733 C CB  . VAL C 112 F 0.7145 0.8216 0.8517 0.0183  -0.1042 0.0297  100  VAL H CB  
6734 C CG1 . VAL C 112 F 0.6749 0.7787 0.7964 0.0137  -0.0896 0.0349  100  VAL H CG1 
6735 C CG2 . VAL C 112 F 0.7161 0.7871 0.8303 0.0277  -0.1010 0.0296  100  VAL H CG2 
6736 N N   . HIS C 113 G 0.7071 0.7576 0.9180 -0.0060 -0.0854 0.0272  100  HIS H N   
6737 C CA  . HIS C 113 G 0.8643 0.8882 1.0970 -0.0111 -0.0849 0.0261  100  HIS H CA  
6738 C C   . HIS C 113 G 0.8058 0.8099 1.0642 -0.0263 -0.0629 0.0320  100  HIS H C   
6739 O O   . HIS C 113 G 0.7337 0.7404 0.9851 -0.0300 -0.0475 0.0358  100  HIS H O   
6740 C CB  . HIS C 113 G 0.6959 0.6913 0.8949 0.0025  -0.0904 0.0256  100  HIS H CB  
6741 C CG  . HIS C 113 G 0.7626 0.7324 0.9271 0.0065  -0.0744 0.0332  100  HIS H CG  
6742 N ND1 . HIS C 113 G 0.7924 0.7369 0.9674 -0.0049 -0.0535 0.0407  100  HIS H ND1 
6743 C CD2 . HIS C 113 G 0.7368 0.7035 0.8566 0.0209  -0.0765 0.0350  100  HIS H CD2 
6744 C CE1 . HIS C 113 G 0.7568 0.6840 0.8939 0.0019  -0.0435 0.0468  100  HIS H CE1 
6745 N NE2 . HIS C 113 G 0.7566 0.6959 0.8601 0.0174  -0.0575 0.0435  100  HIS H NE2 
6746 N N   . GLY C 114 H 0.7967 0.7817 1.0851 -0.0349 -0.0620 0.0327  100  GLY H N   
6747 C CA  . GLY C 114 H 0.7166 0.6872 1.0362 -0.0500 -0.0422 0.0390  100  GLY H CA  
6748 C C   . GLY C 114 H 0.8264 0.7650 1.1209 -0.0490 -0.0233 0.0475  100  GLY H C   
6749 O O   . GLY C 114 H 0.7650 0.6919 1.0165 -0.0369 -0.0248 0.0488  100  GLY H O   
6750 N N   . MET C 115 I 0.7823 0.7083 1.1057 -0.0622 -0.0050 0.0543  100  MET H N   
6751 C CA  . MET C 115 I 0.8512 0.7495 1.1563 -0.0636 0.0149  0.0644  100  MET H CA  
6752 C C   . MET C 115 I 0.9571 0.8240 1.2495 -0.0596 0.0056  0.0683  100  MET H C   
6753 O O   . MET C 115 I 0.9390 0.7934 1.2639 -0.0683 0.0006  0.0704  100  MET H O   
6754 C CB  . MET C 115 I 0.8973 0.7949 1.2406 -0.0787 0.0364  0.0711  100  MET H CB  
6755 C CG  . MET C 115 I 0.8979 0.8249 1.2598 -0.0828 0.0441  0.0659  100  MET H CG  
6756 S SD  . MET C 115 I 0.9021 0.8289 1.3087 -0.0981 0.0707  0.0732  100  MET H SD  
6757 C CE  . MET C 115 I 0.7420 0.7047 1.1866 -0.1028 0.0636  0.0634  100  MET H CE  
6758 N N   . ASP C 116 ? 0.9475 0.8007 1.1935 -0.0466 0.0025  0.0697  101  ASP H N   
6759 C CA  . ASP C 116 ? 0.8993 0.7230 1.1298 -0.0398 -0.0103 0.0716  101  ASP H CA  
6760 C C   . ASP C 116 ? 0.9726 0.7632 1.1996 -0.0466 0.0056  0.0858  101  ASP H C   
6761 O O   . ASP C 116 ? 1.0258 0.7914 1.2696 -0.0514 -0.0017 0.0899  101  ASP H O   
6762 C CB  . ASP C 116 ? 0.8855 0.7124 1.0693 -0.0209 -0.0244 0.0657  101  ASP H CB  
6763 C CG  . ASP C 116 ? 1.0025 0.8362 1.1500 -0.0156 -0.0098 0.0705  101  ASP H CG  
6764 O OD1 . ASP C 116 ? 1.1358 0.9729 1.2931 -0.0260 0.0110  0.0765  101  ASP H OD1 
6765 O OD2 . ASP C 116 ? 0.9146 0.7507 1.0233 -0.0008 -0.0195 0.0680  101  ASP H OD2 
6766 N N   . VAL C 117 ? 0.9151 0.7049 1.1203 -0.0474 0.0264  0.0939  102  VAL H N   
6767 C CA  . VAL C 117 ? 1.0534 0.8158 1.2531 -0.0540 0.0429  0.1093  102  VAL H CA  
6768 C C   . VAL C 117 ? 0.9970 0.7721 1.2223 -0.0676 0.0685  0.1159  102  VAL H C   
6769 O O   . VAL C 117 ? 1.0950 0.8942 1.3136 -0.0660 0.0782  0.1103  102  VAL H O   
6770 C CB  . VAL C 117 ? 0.9436 0.6918 1.0905 -0.0419 0.0455  0.1147  102  VAL H CB  
6771 C CG1 . VAL C 117 ? 1.0830 0.8577 1.2008 -0.0329 0.0483  0.1070  102  VAL H CG1 
6772 C CG2 . VAL C 117 ? 1.1783 0.9057 1.3196 -0.0505 0.0669  0.1321  102  VAL H CG2 
6773 N N   . TRP C 118 ? 1.1589 0.9182 1.4141 -0.0806 0.0786  0.1278  103  TRP H N   
6774 C CA  . TRP C 118 ? 1.0177 0.7889 1.3021 -0.0936 0.1034  0.1354  103  TRP H CA  
6775 C C   . TRP C 118 ? 0.9778 0.7295 1.2460 -0.0980 0.1230  0.1532  103  TRP H C   
6776 O O   . TRP C 118 ? 1.1052 0.8306 1.3490 -0.0940 0.1151  0.1612  103  TRP H O   
6777 C CB  . TRP C 118 ? 0.9644 0.7400 1.3059 -0.1070 0.0993  0.1360  103  TRP H CB  
6778 C CG  . TRP C 118 ? 0.9508 0.7484 1.3131 -0.1048 0.0812  0.1201  103  TRP H CG  
6779 C CD1 . TRP C 118 ? 0.9687 0.7679 1.3121 -0.0934 0.0565  0.1081  103  TRP H CD1 
6780 C CD2 . TRP C 118 ? 0.9127 0.7354 1.3200 -0.1142 0.0861  0.1156  103  TRP H CD2 
6781 N NE1 . TRP C 118 ? 1.0306 0.8554 1.4035 -0.0959 0.0459  0.0970  103  TRP H NE1 
6782 C CE2 . TRP C 118 ? 1.0082 0.8467 1.4211 -0.1089 0.0632  0.1015  103  TRP H CE2 
6783 C CE3 . TRP C 118 ? 0.8311 0.6657 1.2750 -0.1262 0.1077  0.1225  103  TRP H CE3 
6784 C CZ2 . TRP C 118 ? 1.0557 0.9202 1.5096 -0.1161 0.0605  0.0949  103  TRP H CZ2 
6785 C CZ3 . TRP C 118 ? 0.9771 0.8365 1.4622 -0.1324 0.1051  0.1150  103  TRP H CZ3 
6786 C CH2 . TRP C 118 ? 0.9472 0.8207 1.4372 -0.1278 0.0813  0.1017  103  TRP H CH2 
6787 N N   . GLY C 119 ? 1.0114 0.7770 1.2938 -0.1061 0.1489  0.1597  104  GLY H N   
6788 C CA  . GLY C 119 ? 1.0663 0.8188 1.3422 -0.1129 0.1698  0.1785  104  GLY H CA  
6789 C C   . GLY C 119 ? 1.0607 0.8023 1.3835 -0.1281 0.1715  0.1922  104  GLY H C   
6790 O O   . GLY C 119 ? 1.1572 0.9054 1.5215 -0.1345 0.1605  0.1864  104  GLY H O   
6791 N N   . GLN C 120 ? 1.3225 1.0478 1.6384 -0.1345 0.1848  0.2120  105  GLN H N   
6792 C CA  . GLN C 120 ? 1.4084 1.1233 1.7686 -0.1502 0.1868  0.2284  105  GLN H CA  
6793 C C   . GLN C 120 ? 1.3369 1.0792 1.7432 -0.1611 0.2072  0.2305  105  GLN H C   
6794 O O   . GLN C 120 ? 1.3045 1.0441 1.7571 -0.1744 0.2050  0.2403  105  GLN H O   
6795 C CB  . GLN C 120 ? 1.2577 0.9507 1.5992 -0.1550 0.1963  0.2512  105  GLN H CB  
6796 C CG  . GLN C 120 ? 1.3181 1.0294 1.6602 -0.1615 0.2300  0.2658  105  GLN H CG  
6797 C CD  . GLN C 120 ? 1.4196 1.1477 1.7164 -0.1489 0.2452  0.2554  105  GLN H CD  
6798 O OE1 . GLN C 120 ? 1.5013 1.2271 1.7655 -0.1359 0.2302  0.2390  105  GLN H OE1 
6799 N NE2 . GLN C 120 ? 1.3706 1.1164 1.6650 -0.1528 0.2747  0.2652  105  GLN H NE2 
6800 N N   . GLY C 121 ? 1.1379 0.9060 1.5332 -0.1555 0.2259  0.2214  106  GLY H N   
6801 C CA  . GLY C 121 ? 1.0106 0.8061 1.4484 -0.1631 0.2447  0.2206  106  GLY H CA  
6802 C C   . GLY C 121 ? 1.1923 0.9974 1.6308 -0.1688 0.2766  0.2378  106  GLY H C   
6803 O O   . GLY C 121 ? 1.1971 0.9855 1.6208 -0.1733 0.2823  0.2566  106  GLY H O   
6804 N N   . THR C 122 ? 1.1794 1.0127 1.6353 -0.1683 0.2976  0.2314  107  THR H N   
6805 C CA  . THR C 122 ? 1.1084 0.9573 1.5711 -0.1731 0.3299  0.2458  107  THR H CA  
6806 C C   . THR C 122 ? 1.2426 1.1162 1.7656 -0.1816 0.3415  0.2458  107  THR H C   
6807 O O   . THR C 122 ? 1.2138 1.0982 1.7603 -0.1794 0.3298  0.2289  107  THR H O   
6808 C CB  . THR C 122 ? 1.1576 1.0173 1.5711 -0.1605 0.3485  0.2368  107  THR H CB  
6809 O OG1 . THR C 122 ? 1.1220 0.9998 1.5440 -0.1645 0.3808  0.2499  107  THR H OG1 
6810 C CG2 . THR C 122 ? 1.0741 0.9498 1.4866 -0.1508 0.3425  0.2114  107  THR H CG2 
6811 N N   . THR C 123 ? 1.2620 1.1459 1.8109 -0.1914 0.3643  0.2659  108  THR H N   
6812 C CA  . THR C 123 ? 1.1952 1.1021 1.8060 -0.2011 0.3757  0.2707  108  THR H CA  
6813 C C   . THR C 123 ? 1.2084 1.1454 1.8188 -0.1946 0.4084  0.2666  108  THR H C   
6814 O O   . THR C 123 ? 1.2362 1.1768 1.8141 -0.1912 0.4303  0.2764  108  THR H O   
6815 C CB  . THR C 123 ? 1.2281 1.1278 1.8755 -0.2178 0.3771  0.2980  108  THR H CB  
6816 O OG1 . THR C 123 ? 1.2301 1.0969 1.8679 -0.2220 0.3469  0.3015  108  THR H OG1 
6817 C CG2 . THR C 123 ? 1.1551 1.0766 1.8710 -0.2286 0.3818  0.3020  108  THR H CG2 
6818 N N   . VAL C 124 ? 1.2184 1.1768 1.8646 -0.1926 0.4111  0.2520  109  VAL H N   
6819 C CA  . VAL C 124 ? 1.3027 1.2902 1.9569 -0.1860 0.4411  0.2465  109  VAL H CA  
6820 C C   . VAL C 124 ? 1.2541 1.2636 1.9778 -0.1938 0.4445  0.2473  109  VAL H C   
6821 O O   . VAL C 124 ? 1.1763 1.1844 1.9252 -0.1949 0.4226  0.2340  109  VAL H O   
6822 C CB  . VAL C 124 ? 1.1870 1.1773 1.7980 -0.1695 0.4411  0.2209  109  VAL H CB  
6823 C CG1 . VAL C 124 ? 1.0766 1.0533 1.6839 -0.1667 0.4080  0.2034  109  VAL H CG1 
6824 C CG2 . VAL C 124 ? 1.0510 1.0708 1.6857 -0.1630 0.4654  0.2104  109  VAL H CG2 
6825 N N   . THR C 125 ? 1.3454 1.3768 2.1004 -0.1994 0.4719  0.2639  110  THR H N   
6826 C CA  . THR C 125 ? 1.4364 1.4921 2.2595 -0.2068 0.4791  0.2678  110  THR H CA  
6827 C C   . THR C 125 ? 1.3602 1.4469 2.1887 -0.1967 0.5132  0.2626  110  THR H C   
6828 O O   . THR C 125 ? 1.3299 1.4239 2.1286 -0.1926 0.5380  0.2725  110  THR H O   
6829 C CB  . THR C 125 ? 1.3591 1.4134 2.2249 -0.2251 0.4782  0.2966  110  THR H CB  
6830 O OG1 . THR C 125 ? 1.3557 1.3799 2.2201 -0.2337 0.4441  0.2984  110  THR H OG1 
6831 C CG2 . THR C 125 ? 1.3193 1.4018 2.2491 -0.2305 0.4856  0.3005  110  THR H CG2 
6832 N N   . VAL C 126 ? 1.5250 1.6302 2.3908 -0.1923 0.5141  0.2469  111  VAL H N   
6833 C CA  . VAL C 126 ? 1.5559 1.6905 2.4319 -0.1811 0.5445  0.2388  111  VAL H CA  
6834 C C   . VAL C 126 ? 1.5198 1.6793 2.4721 -0.1893 0.5501  0.2461  111  VAL H C   
6835 O O   . VAL C 126 ? 1.6653 1.8245 2.6484 -0.1901 0.5295  0.2325  111  VAL H O   
6836 C CB  . VAL C 126 ? 1.6115 1.7433 2.4521 -0.1641 0.5403  0.2084  111  VAL H CB  
6837 C CG1 . VAL C 126 ? 1.4890 1.6502 2.3489 -0.1525 0.5691  0.1983  111  VAL H CG1 
6838 C CG2 . VAL C 126 ? 1.6280 1.7385 2.3927 -0.1558 0.5382  0.2030  111  VAL H CG2 
6839 N N   . SER C 127 ? 1.3726 1.5520 2.3442 -0.1925 0.5705  0.2653  112  SER H N   
6840 C CA  . SER C 127 ? 1.4149 1.6143 2.4357 -0.1941 0.5647  0.2685  112  SER H CA  
6841 C C   . SER C 127 ? 1.4649 1.6920 2.4903 -0.1910 0.5972  0.2843  112  SER H C   
6842 O O   . SER C 127 ? 1.4815 1.7055 2.4877 -0.1984 0.6056  0.3057  112  SER H O   
6843 C CB  . SER C 127 ? 1.4675 1.6497 2.5104 -0.2087 0.5296  0.2803  112  SER H CB  
6844 O OG  . SER C 127 ? 1.4849 1.6437 2.5213 -0.2105 0.4990  0.2651  112  SER H OG  
6845 N N   . SER C 128 ? 1.5546 1.8092 2.6051 -0.1799 0.6147  0.2742  113  SER H N   
6846 C CA  . SER C 128 ? 1.5340 1.8191 2.5895 -0.1749 0.6467  0.2873  113  SER H CA  
6847 C C   . SER C 128 ? 1.4595 1.7701 2.5650 -0.1704 0.6483  0.2840  113  SER H C   
6848 O O   . SER C 128 ? 1.5238 1.8367 2.6465 -0.1610 0.6431  0.2621  113  SER H O   
6849 C CB  . SER C 128 ? 1.5939 1.8896 2.6074 -0.1594 0.6804  0.2757  113  SER H CB  
6850 O OG  . SER C 128 ? 1.5864 1.8580 2.5512 -0.1632 0.6793  0.2795  113  SER H OG  
6851 N N   . ASP D 149 ? 1.1058 1.5905 1.6263 0.1754  -0.1662 0.1876  1    ASP L N   
6852 C CA  . ASP D 149 ? 1.1345 1.6106 1.6710 0.1717  -0.1658 0.1870  1    ASP L CA  
6853 C C   . ASP D 149 ? 1.2501 1.7294 1.7823 0.1790  -0.1890 0.1765  1    ASP L C   
6854 O O   . ASP D 149 ? 1.1957 1.6802 1.7062 0.1882  -0.2029 0.1679  1    ASP L O   
6855 C CB  . ASP D 149 ? 1.1167 1.6055 1.6941 0.1571  -0.1698 0.2019  1    ASP L CB  
6856 N N   . ILE D 150 ? 1.1683 1.6424 1.7213 0.1742  -0.1936 0.1780  2    ILE L N   
6857 C CA  . ILE D 150 ? 1.1123 1.5846 1.6621 0.1797  -0.2148 0.1696  2    ILE L CA  
6858 C C   . ILE D 150 ? 1.0797 1.5535 1.6722 0.1648  -0.2289 0.1777  2    ILE L C   
6859 O O   . ILE D 150 ? 1.1291 1.5915 1.7408 0.1575  -0.2112 0.1846  2    ILE L O   
6860 C CB  . ILE D 150 ? 1.1730 1.6197 1.6888 0.1946  -0.1984 0.1570  2    ILE L CB  
6861 C CG1 . ILE D 150 ? 1.0322 1.4695 1.5559 0.1973  -0.2137 0.1530  2    ILE L CG1 
6862 C CG2 . ILE D 150 ? 1.1252 1.5523 1.6349 0.1918  -0.1652 0.1589  2    ILE L CG2 
6863 C CD1 . ILE D 150 ? 1.0701 1.5169 1.5830 0.2017  -0.2463 0.1467  2    ILE L CD1 
6864 N N   . VAL D 151 ? 0.9884 1.4728 1.5949 0.1580  -0.2628 0.1756  3    VAL L N   
6865 C CA  . VAL D 151 ? 1.1335 1.6135 1.7817 0.1405  -0.2829 0.1797  3    VAL L CA  
6866 C C   . VAL D 151 ? 1.1180 1.5878 1.7586 0.1399  -0.3179 0.1666  3    VAL L C   
6867 O O   . VAL D 151 ? 1.0615 1.5370 1.6691 0.1488  -0.3314 0.1580  3    VAL L O   
6868 C CB  . VAL D 151 ? 1.0743 1.5778 1.7585 0.1215  -0.2940 0.1921  3    VAL L CB  
6869 C CG1 . VAL D 151 ? 0.9823 1.5075 1.6614 0.1153  -0.3272 0.1880  3    VAL L CG1 
6870 C CG2 . VAL D 151 ? 1.0093 1.5033 1.7384 0.1038  -0.3007 0.1985  3    VAL L CG2 
6871 N N   . MET D 152 ? 1.0598 1.5096 1.7285 0.1290  -0.3337 0.1631  4    MET L N   
6872 C CA  . MET D 152 ? 0.9918 1.4121 1.6346 0.1235  -0.3619 0.1414  4    MET L CA  
6873 C C   . MET D 152 ? 0.9466 1.3723 1.6146 0.0964  -0.3922 0.1400  4    MET L C   
6874 O O   . MET D 152 ? 0.9807 1.4206 1.7013 0.0821  -0.3922 0.1550  4    MET L O   
6875 C CB  . MET D 152 ? 1.1325 1.5058 1.7541 0.1289  -0.3442 0.1274  4    MET L CB  
6876 C CG  . MET D 152 ? 1.0471 1.4170 1.6514 0.1540  -0.3119 0.1311  4    MET L CG  
6877 S SD  . MET D 152 ? 1.2249 1.5971 1.7667 0.1758  -0.3109 0.1189  4    MET L SD  
6878 C CE  . MET D 152 ? 1.1058 1.4280 1.5902 0.1691  -0.3322 0.0868  4    MET L CE  
6879 N N   . THR D 153 ? 0.9988 1.4133 1.6288 0.0891  -0.4180 0.1217  5    THR L N   
6880 C CA  . THR D 153 ? 1.1202 1.5394 1.7670 0.0625  -0.4492 0.1178  5    THR L CA  
6881 C C   . THR D 153 ? 1.0421 1.4081 1.6442 0.0529  -0.4617 0.0895  5    THR L C   
6882 O O   . THR D 153 ? 1.0854 1.4277 1.6305 0.0644  -0.4645 0.0706  5    THR L O   
6883 C CB  . THR D 153 ? 1.1225 1.5814 1.7670 0.0601  -0.4716 0.1231  5    THR L CB  
6884 O OG1 . THR D 153 ? 0.9515 1.4587 1.6400 0.0674  -0.4590 0.1506  5    THR L OG1 
6885 C CG2 . THR D 153 ? 1.0266 1.4881 1.6821 0.0320  -0.5054 0.1162  5    THR L CG2 
6886 N N   . GLN D 154 ? 0.9479 1.2946 1.5752 0.0318  -0.4686 0.0870  6    GLN L N   
6887 C CA  . GLN D 154 ? 1.1276 1.4222 1.7166 0.0196  -0.4809 0.0612  6    GLN L CA  
6888 C C   . GLN D 154 ? 1.1333 1.4360 1.7282 -0.0080 -0.5163 0.0547  6    GLN L C   
6889 O O   . GLN D 154 ? 1.0723 1.4147 1.7195 -0.0241 -0.5278 0.0726  6    GLN L O   
6890 C CB  . GLN D 154 ? 1.1045 1.3658 1.7126 0.0148  -0.4631 0.0609  6    GLN L CB  
6891 C CG  . GLN D 154 ? 1.0979 1.3309 1.6771 0.0404  -0.4320 0.0559  6    GLN L CG  
6892 C CD  . GLN D 154 ? 1.1225 1.3348 1.7326 0.0374  -0.4117 0.0623  6    GLN L CD  
6893 O OE1 . GLN D 154 ? 1.2471 1.4724 1.9070 0.0177  -0.4182 0.0742  6    GLN L OE1 
6894 N NE2 . GLN D 154 ? 1.0522 1.2331 1.6330 0.0572  -0.3869 0.0547  6    GLN L NE2 
6895 N N   . SER D 155 ? 1.2191 1.4847 1.7597 -0.0133 -0.5333 0.0291  7    SER L N   
6896 C CA  . SER D 155 ? 1.3030 1.5702 1.8425 -0.0407 -0.5674 0.0196  7    SER L CA  
6897 C C   . SER D 155 ? 1.3903 1.6127 1.9327 -0.0620 -0.5712 0.0071  7    SER L C   
6898 O O   . SER D 155 ? 1.4116 1.6034 1.9546 -0.0527 -0.5467 0.0062  7    SER L O   
6899 C CB  . SER D 155 ? 1.2954 1.5520 1.7743 -0.0347 -0.5852 0.0002  7    SER L CB  
6900 O OG  . SER D 155 ? 1.3886 1.5867 1.8079 -0.0251 -0.5774 -0.0245 7    SER L OG  
6901 N N   . PRO D 156 ? 1.4413 1.6538 1.9778 -0.0897 -0.6008 -0.0053 8    PRO L N   
6902 C CA  . PRO D 156 ? 1.4757 1.6870 2.0584 -0.1181 -0.6095 0.0006  8    PRO L CA  
6903 C C   . PRO D 156 ? 1.3566 1.5641 1.9824 -0.1127 -0.5815 0.0161  8    PRO L C   
6904 O O   . PRO D 156 ? 1.4264 1.5885 2.0264 -0.1000 -0.5601 0.0058  8    PRO L O   
6905 C CB  . PRO D 156 ? 1.4970 1.6495 2.0313 -0.1358 -0.6256 -0.0285 8    PRO L CB  
6906 C CG  . PRO D 156 ? 1.4533 1.5707 1.9179 -0.1121 -0.6180 -0.0483 8    PRO L CG  
6907 C CD  . PRO D 156 ? 1.4808 1.6502 1.9507 -0.0933 -0.6177 -0.0340 8    PRO L CD  
6908 N N   . LEU D 157 ? 1.3705 1.6259 2.0623 -0.1225 -0.5819 0.0414  9    LEU L N   
6909 C CA  . LEU D 157 ? 1.3072 1.5587 2.0446 -0.1233 -0.5594 0.0560  9    LEU L CA  
6910 C C   . LEU D 157 ? 1.3386 1.5345 2.0632 -0.1419 -0.5615 0.0383  9    LEU L C   
6911 O O   . LEU D 157 ? 1.3842 1.5560 2.1228 -0.1358 -0.5378 0.0421  9    LEU L O   
6912 C CB  . LEU D 157 ? 1.3205 1.6309 2.1304 -0.1365 -0.5652 0.0841  9    LEU L CB  
6913 C CG  . LEU D 157 ? 1.3681 1.7343 2.2072 -0.1159 -0.5531 0.1090  9    LEU L CG  
6914 C CD1 . LEU D 157 ? 1.2659 1.6645 2.0837 -0.1144 -0.5757 0.1070  9    LEU L CD1 
6915 C CD2 . LEU D 157 ? 1.3595 1.7680 2.2730 -0.1262 -0.5477 0.1372  9    LEU L CD2 
6916 N N   . SER D 158 ? 1.3009 1.4752 1.9977 -0.1648 -0.5893 0.0190  10   SER L N   
6917 C CA  . SER D 158 ? 1.3453 1.4622 2.0216 -0.1836 -0.5933 -0.0006 10   SER L CA  
6918 C C   . SER D 158 ? 1.3966 1.4731 2.0025 -0.1866 -0.6115 -0.0295 10   SER L C   
6919 O O   . SER D 158 ? 1.3602 1.4624 1.9551 -0.1959 -0.6371 -0.0331 10   SER L O   
6920 C CB  . SER D 158 ? 1.2758 1.4100 2.0043 -0.2181 -0.6115 0.0083  10   SER L CB  
6921 O OG  . SER D 158 ? 1.3045 1.3814 2.0073 -0.2386 -0.6185 -0.0129 10   SER L OG  
6922 N N   . LEU D 159 ? 1.4579 1.4713 2.0159 -0.1782 -0.5979 -0.0498 11   LEU L N   
6923 C CA  . LEU D 159 ? 1.5143 1.4811 2.0010 -0.1791 -0.6116 -0.0784 11   LEU L CA  
6924 C C   . LEU D 159 ? 1.4363 1.3406 1.9033 -0.1989 -0.6132 -0.0969 11   LEU L C   
6925 O O   . LEU D 159 ? 1.4731 1.3260 1.9042 -0.1830 -0.5919 -0.1089 11   LEU L O   
6926 C CB  . LEU D 159 ? 1.3413 1.2907 1.7774 -0.1434 -0.5914 -0.0862 11   LEU L CB  
6927 C CG  . LEU D 159 ? 1.3393 1.2496 1.7008 -0.1395 -0.6054 -0.1134 11   LEU L CG  
6928 C CD1 . LEU D 159 ? 1.3375 1.2883 1.6965 -0.1511 -0.6357 -0.1133 11   LEU L CD1 
6929 C CD2 . LEU D 159 ? 1.3100 1.1991 1.6257 -0.1034 -0.5803 -0.1197 11   LEU L CD2 
6930 N N   . PRO D 160 ? 1.5122 1.4194 2.0014 -0.2337 -0.6378 -0.0994 12   PRO L N   
6931 C CA  . PRO D 160 ? 1.5839 1.4291 2.0507 -0.2547 -0.6409 -0.1184 12   PRO L CA  
6932 C C   . PRO D 160 ? 1.6628 1.4584 2.0539 -0.2576 -0.6563 -0.1483 12   PRO L C   
6933 O O   . PRO D 160 ? 1.5894 1.4077 1.9604 -0.2622 -0.6796 -0.1541 12   PRO L O   
6934 C CB  . PRO D 160 ? 1.4440 1.3201 1.9667 -0.2916 -0.6630 -0.1077 12   PRO L CB  
6935 C CG  . PRO D 160 ? 1.4181 1.3606 1.9623 -0.2938 -0.6841 -0.0951 12   PRO L CG  
6936 C CD  . PRO D 160 ? 1.5077 1.4767 2.0470 -0.2557 -0.6626 -0.0833 12   PRO L CD  
6937 N N   . VAL D 161 ? 1.7370 1.4634 2.0850 -0.2543 -0.6427 -0.1671 13   VAL L N   
6938 C CA  . VAL D 161 ? 1.9179 1.5892 2.1895 -0.2542 -0.6531 -0.1960 13   VAL L CA  
6939 C C   . VAL D 161 ? 2.0115 1.6096 2.2560 -0.2633 -0.6417 -0.2126 13   VAL L C   
6940 O O   . VAL D 161 ? 1.9039 1.4931 2.1822 -0.2606 -0.6202 -0.2016 13   VAL L O   
6941 C CB  . VAL D 161 ? 1.8806 1.5505 2.1054 -0.2165 -0.6390 -0.2008 13   VAL L CB  
6942 C CG1 . VAL D 161 ? 1.8417 1.4722 2.0488 -0.1883 -0.6036 -0.2017 13   VAL L CG1 
6943 C CG2 . VAL D 161 ? 1.9658 1.6040 2.1213 -0.2200 -0.6599 -0.2264 13   VAL L CG2 
6944 N N   . THR D 162 ? 2.1539 1.6982 2.3361 -0.2742 -0.6559 -0.2393 14   THR L N   
6945 C CA  . THR D 162 ? 2.3581 1.8261 2.5034 -0.2822 -0.6460 -0.2581 14   THR L CA  
6946 C C   . THR D 162 ? 2.4554 1.8838 2.5593 -0.2440 -0.6135 -0.2634 14   THR L C   
6947 O O   . THR D 162 ? 2.4914 1.9515 2.5929 -0.2136 -0.6011 -0.2541 14   THR L O   
6948 C CB  . THR D 162 ? 2.3551 1.7826 2.4476 -0.3080 -0.6741 -0.2843 14   THR L CB  
6949 O OG1 . THR D 162 ? 2.3663 1.7190 2.3855 -0.2926 -0.6606 -0.3078 14   THR L OG1 
6950 C CG2 . THR D 162 ? 2.3244 1.7988 2.4077 -0.3097 -0.7003 -0.2849 14   THR L CG2 
6951 N N   . PRO D 163 ? 2.2856 1.6457 2.3587 -0.2441 -0.5977 -0.2771 15   PRO L N   
6952 C CA  . PRO D 163 ? 2.2275 1.5479 2.2549 -0.2073 -0.5679 -0.2838 15   PRO L CA  
6953 C C   . PRO D 163 ? 2.1792 1.4538 2.1247 -0.1964 -0.5750 -0.3093 15   PRO L C   
6954 O O   . PRO D 163 ? 2.0034 1.2238 1.9076 -0.2172 -0.5884 -0.3306 15   PRO L O   
6955 C CB  . PRO D 163 ? 2.1353 1.4041 2.1694 -0.2135 -0.5481 -0.2857 15   PRO L CB  
6956 C CG  . PRO D 163 ? 2.0746 1.3699 2.1714 -0.2501 -0.5641 -0.2742 15   PRO L CG  
6957 C CD  . PRO D 163 ? 2.1074 1.4354 2.2037 -0.2742 -0.5996 -0.2793 15   PRO L CD  
6958 N N   . GLY D 164 ? 2.1919 1.4866 2.1122 -0.1640 -0.5655 -0.3075 16   GLY L N   
6959 C CA  . GLY D 164 ? 2.0864 1.3362 1.9277 -0.1480 -0.5669 -0.3303 16   GLY L CA  
6960 C C   . GLY D 164 ? 2.0748 1.3620 1.8969 -0.1457 -0.5897 -0.3339 16   GLY L C   
6961 O O   . GLY D 164 ? 2.0266 1.2756 1.7863 -0.1473 -0.6027 -0.3559 16   GLY L O   
6962 N N   . GLU D 165 ? 2.3204 1.6808 2.1941 -0.1413 -0.5940 -0.3125 17   GLU L N   
6963 C CA  . GLU D 165 ? 2.2781 1.6828 2.1435 -0.1402 -0.6159 -0.3122 17   GLU L CA  
6964 C C   . GLU D 165 ? 2.1556 1.6135 2.0442 -0.1081 -0.5977 -0.2927 17   GLU L C   
6965 O O   . GLU D 165 ? 2.0792 1.5464 1.9997 -0.0919 -0.5712 -0.2775 17   GLU L O   
6966 C CB  . GLU D 165 ? 2.2291 1.6762 2.1413 -0.1768 -0.6471 -0.3049 17   GLU L CB  
6967 C CG  . GLU D 165 ? 2.3335 1.7346 2.2352 -0.2133 -0.6650 -0.3210 17   GLU L CG  
6968 C CD  . GLU D 165 ? 2.4637 1.8459 2.4059 -0.2233 -0.6475 -0.3121 17   GLU L CD  
6969 O OE1 . GLU D 165 ? 2.5886 1.9181 2.5124 -0.2471 -0.6537 -0.3272 17   GLU L OE1 
6970 O OE2 . GLU D 165 ? 2.3901 1.8093 2.3812 -0.2068 -0.6268 -0.2900 17   GLU L OE2 
6971 N N   . PRO D 166 ? 1.9909 1.4837 1.8626 -0.0981 -0.6106 -0.2928 18   PRO L N   
6972 C CA  . PRO D 166 ? 1.9405 1.4885 1.8385 -0.0706 -0.5950 -0.2728 18   PRO L CA  
6973 C C   . PRO D 166 ? 1.8434 1.4578 1.8207 -0.0843 -0.6005 -0.2468 18   PRO L C   
6974 O O   . PRO D 166 ? 1.7349 1.3658 1.7432 -0.1154 -0.6243 -0.2445 18   PRO L O   
6975 C CB  . PRO D 166 ? 1.8398 1.3990 1.6907 -0.0596 -0.6105 -0.2835 18   PRO L CB  
6976 C CG  . PRO D 166 ? 1.9436 1.4812 1.7727 -0.0912 -0.6428 -0.3007 18   PRO L CG  
6977 C CD  . PRO D 166 ? 1.9940 1.4699 1.8121 -0.1074 -0.6369 -0.3132 18   PRO L CD  
6978 N N   . ALA D 167 ? 1.7691 1.4220 1.7785 -0.0602 -0.5775 -0.2267 19   ALA L N   
6979 C CA  . ALA D 167 ? 1.5317 1.2500 1.6138 -0.0673 -0.5787 -0.2002 19   ALA L CA  
6980 C C   . ALA D 167 ? 1.4291 1.1924 1.5155 -0.0374 -0.5642 -0.1860 19   ALA L C   
6981 O O   . ALA D 167 ? 1.4844 1.2263 1.5318 -0.0092 -0.5432 -0.1921 19   ALA L O   
6982 C CB  . ALA D 167 ? 1.5247 1.2386 1.6579 -0.0745 -0.5606 -0.1864 19   ALA L CB  
6983 N N   . SER D 168 ? 1.5582 1.3842 1.6921 -0.0437 -0.5753 -0.1667 20   SER L N   
6984 C CA  . SER D 168 ? 1.3710 1.2428 1.5112 -0.0181 -0.5638 -0.1523 20   SER L CA  
6985 C C   . SER D 168 ? 1.3153 1.2442 1.5299 -0.0215 -0.5563 -0.1234 20   SER L C   
6986 O O   . SER D 168 ? 1.4871 1.4401 1.7462 -0.0475 -0.5743 -0.1143 20   SER L O   
6987 C CB  . SER D 168 ? 1.3376 1.2295 1.4455 -0.0180 -0.5878 -0.1603 20   SER L CB  
6988 O OG  . SER D 168 ? 1.3924 1.2327 1.4281 -0.0101 -0.5914 -0.1861 20   SER L OG  
6989 N N   . ILE D 169 ? 1.2344 1.1846 1.4613 0.0048  -0.5294 -0.1090 21   ILE L N   
6990 C CA  . ILE D 169 ? 1.1947 1.1984 1.4872 0.0064  -0.5183 -0.0811 21   ILE L CA  
6991 C C   . ILE D 169 ? 1.2547 1.2970 1.5387 0.0318  -0.5084 -0.0710 21   ILE L C   
6992 O O   . ILE D 169 ? 1.3444 1.3660 1.5853 0.0565  -0.4907 -0.0797 21   ILE L O   
6993 C CB  . ILE D 169 ? 1.2287 1.2166 1.5516 0.0118  -0.4906 -0.0715 21   ILE L CB  
6994 C CG1 . ILE D 169 ? 1.3611 1.3144 1.6985 -0.0154 -0.5007 -0.0792 21   ILE L CG1 
6995 C CG2 . ILE D 169 ? 1.2989 1.3416 1.6833 0.0182  -0.4759 -0.0427 21   ILE L CG2 
6996 C CD1 . ILE D 169 ? 1.2564 1.1890 1.6194 -0.0104 -0.4740 -0.0716 21   ILE L CD1 
6997 N N   . SER D 170 ? 1.2925 1.3904 1.6167 0.0260  -0.5194 -0.0525 22   SER L N   
6998 C CA  . SER D 170 ? 1.2840 1.4214 1.6044 0.0482  -0.5106 -0.0411 22   SER L CA  
6999 C C   . SER D 170 ? 1.1941 1.3696 1.5704 0.0574  -0.4872 -0.0143 22   SER L C   
7000 O O   . SER D 170 ? 1.2118 1.3988 1.6402 0.0415  -0.4864 -0.0009 22   SER L O   
7001 C CB  . SER D 170 ? 1.2266 1.3997 1.5459 0.0381  -0.5392 -0.0396 22   SER L CB  
7002 O OG  . SER D 170 ? 1.3172 1.4555 1.5800 0.0319  -0.5600 -0.0648 22   SER L OG  
7003 N N   . CYS D 171 ? 1.1662 1.3608 1.5302 0.0830  -0.4678 -0.0067 23   CYS L N   
7004 C CA  . CYS D 171 ? 1.2168 1.4474 1.6277 0.0942  -0.4440 0.0182  23   CYS L CA  
7005 C C   . CYS D 171 ? 1.1815 1.4477 1.5788 0.1138  -0.4388 0.0267  23   CYS L C   
7006 O O   . CYS D 171 ? 1.1944 1.4428 1.5417 0.1335  -0.4291 0.0143  23   CYS L O   
7007 C CB  . CYS D 171 ? 1.1983 1.3983 1.6062 0.1076  -0.4138 0.0172  23   CYS L CB  
7008 S SG  . CYS D 171 ? 1.1963 1.4353 1.6598 0.1206  -0.3828 0.0467  23   CYS L SG  
7009 N N   . ARG D 172 ? 1.2404 1.7727 1.3097 0.2271  -0.3789 0.0315  24   ARG L N   
7010 C CA  . ARG D 172 ? 1.2628 1.7531 1.3245 0.2342  -0.3895 0.0555  24   ARG L CA  
7011 C C   . ARG D 172 ? 1.1946 1.6857 1.3171 0.2510  -0.3872 0.0469  24   ARG L C   
7012 O O   . ARG D 172 ? 1.2067 1.7317 1.3814 0.2642  -0.3959 0.0302  24   ARG L O   
7013 C CB  . ARG D 172 ? 1.3390 1.8222 1.3836 0.2407  -0.4230 0.0766  24   ARG L CB  
7014 C CG  . ARG D 172 ? 1.4413 1.9276 1.4288 0.2251  -0.4278 0.0840  24   ARG L CG  
7015 C CD  . ARG D 172 ? 1.7290 2.2153 1.7072 0.2329  -0.4622 0.1017  24   ARG L CD  
7016 N NE  . ARG D 172 ? 1.8523 2.3040 1.7654 0.2206  -0.4679 0.1268  24   ARG L NE  
7017 C CZ  . ARG D 172 ? 1.8447 2.2551 1.7400 0.2240  -0.4759 0.1508  24   ARG L CZ  
7018 N NH1 . ARG D 172 ? 1.8066 2.2053 1.7447 0.2393  -0.4792 0.1530  24   ARG L NH1 
7019 N NH2 . ARG D 172 ? 1.8605 2.2415 1.6953 0.2120  -0.4805 0.1726  24   ARG L NH2 
7020 N N   . SER D 173 ? 1.1522 1.6056 1.2675 0.2505  -0.3755 0.0583  25   SER L N   
7021 C CA  . SER D 173 ? 1.1432 1.5924 1.3115 0.2646  -0.3700 0.0509  25   SER L CA  
7022 C C   . SER D 173 ? 1.1552 1.5757 1.3329 0.2791  -0.3940 0.0735  25   SER L C   
7023 O O   . SER D 173 ? 1.1808 1.5741 1.3152 0.2751  -0.4085 0.0976  25   SER L O   
7024 C CB  . SER D 173 ? 1.1352 1.5636 1.2938 0.2541  -0.3378 0.0458  25   SER L CB  
7025 O OG  . SER D 173 ? 1.3247 1.7074 1.4329 0.2451  -0.3354 0.0706  25   SER L OG  
7026 N N   . SER D 174 ? 1.2116 1.6387 1.4471 0.2961  -0.3978 0.0652  26   SER L N   
7027 C CA  . SER D 174 ? 1.2201 1.6202 1.4702 0.3111  -0.4189 0.0851  26   SER L CA  
7028 C C   . SER D 174 ? 1.2316 1.5828 1.4501 0.3046  -0.4067 0.1038  26   SER L C   
7029 O O   . SER D 174 ? 1.1629 1.4825 1.3564 0.3074  -0.4239 0.1290  26   SER L O   
7030 C CB  . SER D 174 ? 1.1464 1.5671 1.4674 0.3307  -0.4244 0.0698  26   SER L CB  
7031 O OG  . SER D 174 ? 1.2171 1.6852 1.5702 0.3322  -0.4201 0.0436  26   SER L OG  
7032 N N   . GLN D 175 ? 1.2326 1.5772 1.4521 0.2959  -0.3772 0.0921  27   GLN L N   
7033 C CA  . GLN D 175 ? 1.1492 1.4494 1.3402 0.2887  -0.3622 0.1074  27   GLN L CA  
7034 C C   . GLN D 175 ? 1.1719 1.4677 1.3159 0.2670  -0.3357 0.1030  27   GLN L C   
7035 O O   . GLN D 175 ? 1.2550 1.5835 1.3953 0.2586  -0.3267 0.0855  27   GLN L O   
7036 C CB  . GLN D 175 ? 1.1400 1.4321 1.3807 0.3002  -0.3512 0.0988  27   GLN L CB  
7037 C CG  . GLN D 175 ? 1.1719 1.5035 1.4614 0.3033  -0.3348 0.0676  27   GLN L CG  
7038 C CD  . GLN D 175 ? 1.3005 1.6271 1.6452 0.3181  -0.3304 0.0597  27   GLN L CD  
7039 O OE1 . GLN D 175 ? 1.3606 1.6610 1.7161 0.3299  -0.3457 0.0764  27   GLN L OE1 
7040 N NE2 . GLN D 175 ? 1.1942 1.5459 1.5742 0.3176  -0.3094 0.0342  27   GLN L NE2 
7041 N N   . SER D 176 A 1.2101 1.4647 1.3179 0.2579  -0.3230 0.1194  27   SER L N   
7042 C CA  . SER D 176 A 1.1188 1.3637 1.1758 0.2370  -0.2993 0.1195  27   SER L CA  
7043 C C   . SER D 176 A 1.1278 1.3950 1.2101 0.2311  -0.2696 0.0931  27   SER L C   
7044 O O   . SER D 176 A 1.1703 1.4374 1.2968 0.2403  -0.2604 0.0829  27   SER L O   
7045 C CB  . SER D 176 A 1.1406 1.3347 1.1546 0.2297  -0.2940 0.1446  27   SER L CB  
7046 O OG  . SER D 176 A 1.2967 1.4804 1.2563 0.2094  -0.2742 0.1474  27   SER L OG  
7047 N N   . LEU D 177 B 1.1059 1.3925 1.1597 0.2157  -0.2546 0.0820  27   LEU L N   
7048 C CA  . LEU D 177 B 1.0600 1.3680 1.1306 0.2078  -0.2253 0.0577  27   LEU L CA  
7049 C C   . LEU D 177 B 1.1207 1.3993 1.1463 0.1901  -0.1984 0.0648  27   LEU L C   
7050 O O   . LEU D 177 B 1.1236 1.4180 1.1547 0.1808  -0.1724 0.0464  27   LEU L O   
7051 C CB  . LEU D 177 B 1.0198 1.3731 1.0942 0.2030  -0.2250 0.0379  27   LEU L CB  
7052 C CG  . LEU D 177 B 1.0671 1.4572 1.1927 0.2198  -0.2471 0.0251  27   LEU L CG  
7053 C CD1 . LEU D 177 B 0.8803 1.3137 1.0054 0.2129  -0.2434 0.0053  27   LEU L CD1 
7054 C CD2 . LEU D 177 B 1.0025 1.4009 1.1916 0.2348  -0.2421 0.0109  27   LEU L CD2 
7055 N N   . LEU D 178 C 1.1273 1.3640 1.1087 0.1852  -0.2041 0.0911  27   LEU L N   
7056 C CA  . LEU D 178 C 1.1160 1.3219 1.0527 0.1687  -0.1798 0.1001  27   LEU L CA  
7057 C C   . LEU D 178 C 1.0771 1.2650 1.0455 0.1738  -0.1633 0.0965  27   LEU L C   
7058 O O   . LEU D 178 C 1.1606 1.3238 1.1454 0.1857  -0.1765 0.1103  27   LEU L O   
7059 C CB  . LEU D 178 C 1.2229 1.3908 1.1019 0.1622  -0.1931 0.1298  27   LEU L CB  
7060 C CG  . LEU D 178 C 1.2159 1.3587 1.0331 0.1417  -0.1722 0.1403  27   LEU L CG  
7061 C CD1 . LEU D 178 C 1.2884 1.3985 1.1046 0.1382  -0.1506 0.1457  27   LEU L CD1 
7062 C CD2 . LEU D 178 C 1.1530 1.3283 0.9568 0.1281  -0.1540 0.1204  27   LEU L CD2 
7063 N N   . HIS D 179 D 1.1022 1.3027 1.0794 0.1648  -0.1344 0.0781  27   HIS L N   
7064 C CA  . HIS D 179 D 1.0837 1.2702 1.0921 0.1687  -0.1169 0.0724  27   HIS L CA  
7065 C C   . HIS D 179 D 0.9881 1.1281 0.9514 0.1574  -0.1034 0.0932  27   HIS L C   
7066 O O   . HIS D 179 D 1.0134 1.1372 0.9203 0.1434  -0.1003 0.1070  27   HIS L O   
7067 C CB  . HIS D 179 D 0.9822 1.2029 1.0208 0.1639  -0.0916 0.0435  27   HIS L CB  
7068 C CG  . HIS D 179 D 0.9503 1.1670 1.0365 0.1723  -0.0786 0.0329  27   HIS L CG  
7069 N ND1 . HIS D 179 D 0.9052 1.0954 0.9776 0.1630  -0.0540 0.0364  27   HIS L ND1 
7070 C CD2 . HIS D 179 D 0.8418 1.0777 0.9890 0.1891  -0.0866 0.0190  27   HIS L CD2 
7071 C CE1 . HIS D 179 D 0.8851 1.0783 1.0079 0.1735  -0.0477 0.0250  27   HIS L CE1 
7072 N NE2 . HIS D 179 D 0.8901 1.1106 1.0588 0.1894  -0.0670 0.0142  27   HIS L NE2 
7073 N N   . THR D 180 E 0.9943 1.1126 0.9834 0.1638  -0.0952 0.0954  27   THR L N   
7074 C CA  . THR D 180 E 1.0358 1.1095 0.9869 0.1542  -0.0818 0.1146  27   THR L CA  
7075 C C   . THR D 180 E 0.9994 1.0741 0.9144 0.1342  -0.0519 0.1079  27   THR L C   
7076 O O   . THR D 180 E 1.0658 1.1067 0.9312 0.1221  -0.0432 0.1263  27   THR L O   
7077 C CB  . THR D 180 E 1.0228 1.0774 1.0139 0.1651  -0.0771 0.1148  27   THR L CB  
7078 O OG1 . THR D 180 E 1.0914 1.1547 1.1264 0.1848  -0.1031 0.1148  27   THR L OG1 
7079 C CG2 . THR D 180 E 1.0909 1.0951 1.0428 0.1587  -0.0724 0.1401  27   THR L CG2 
7080 N N   . TYR D 181 ? 1.0352 1.1482 0.9739 0.1304  -0.0358 0.0819  28   TYR L N   
7081 C CA  . TYR D 181 ? 1.0244 1.1417 0.9301 0.1115  -0.0075 0.0744  28   TYR L CA  
7082 C C   . TYR D 181 ? 1.0381 1.1546 0.8864 0.0987  -0.0126 0.0850  28   TYR L C   
7083 O O   . TYR D 181 ? 1.1453 1.2549 0.9540 0.0818  0.0093  0.0856  28   TYR L O   
7084 C CB  . TYR D 181 ? 0.8540 1.0144 0.8018 0.1115  0.0097  0.0436  28   TYR L CB  
7085 C CG  . TYR D 181 ? 0.8427 1.0042 0.8439 0.1212  0.0203  0.0312  28   TYR L CG  
7086 C CD1 . TYR D 181 ? 0.9714 1.0936 0.9720 0.1244  0.0226  0.0469  28   TYR L CD1 
7087 C CD2 . TYR D 181 ? 0.7719 0.9739 0.8240 0.1270  0.0281  0.0036  28   TYR L CD2 
7088 C CE1 . TYR D 181 ? 0.8335 0.9564 0.8826 0.1330  0.0322  0.0355  28   TYR L CE1 
7089 C CE2 . TYR D 181 ? 0.8632 1.0663 0.9638 0.1357  0.0378  -0.0079 28   TYR L CE2 
7090 C CZ  . TYR D 181 ? 0.9406 1.1040 1.0394 0.1386  0.0399  0.0080  28   TYR L CZ  
7091 O OH  . TYR D 181 ? 0.9819 1.1461 1.1287 0.1471  0.0496  -0.0036 28   TYR L OH  
7092 N N   . GLY D 182 ? 1.0065 1.1299 0.8493 0.1062  -0.0407 0.0932  29   GLY L N   
7093 C CA  . GLY D 182 ? 1.1212 1.2441 0.9106 0.0949  -0.0477 0.1036  29   GLY L CA  
7094 C C   . GLY D 182 ? 1.0748 1.2430 0.8729 0.0929  -0.0507 0.0839  29   GLY L C   
7095 O O   . GLY D 182 ? 1.3054 1.4754 1.0572 0.0809  -0.0513 0.0895  29   GLY L O   
7096 N N   . TYR D 183 ? 0.9790 1.1832 0.8344 0.1042  -0.0524 0.0611  30   TYR L N   
7097 C CA  . TYR D 183 ? 1.0691 1.3185 0.9385 0.1038  -0.0557 0.0411  30   TYR L CA  
7098 C C   . TYR D 183 ? 1.0893 1.3571 0.9938 0.1214  -0.0873 0.0405  30   TYR L C   
7099 O O   . TYR D 183 ? 1.2176 1.4778 1.1621 0.1368  -0.0987 0.0429  30   TYR L O   
7100 C CB  . TYR D 183 ? 0.9425 1.2236 0.8507 0.1018  -0.0308 0.0129  30   TYR L CB  
7101 C CG  . TYR D 183 ? 1.0631 1.3330 0.9391 0.0837  0.0016  0.0102  30   TYR L CG  
7102 C CD1 . TYR D 183 ? 1.0484 1.3327 0.8855 0.0680  0.0136  0.0049  30   TYR L CD1 
7103 C CD2 . TYR D 183 ? 0.9785 1.2238 0.8634 0.0824  0.0203  0.0127  30   TYR L CD2 
7104 C CE1 . TYR D 183 ? 0.9199 1.1943 0.7279 0.0516  0.0434  0.0026  30   TYR L CE1 
7105 C CE2 . TYR D 183 ? 0.9176 1.1531 0.7736 0.0659  0.0500  0.0104  30   TYR L CE2 
7106 C CZ  . TYR D 183 ? 0.9391 1.1894 0.7569 0.0507  0.0615  0.0054  30   TYR L CZ  
7107 O OH  . TYR D 183 ? 0.9627 1.2034 0.7519 0.0344  0.0912  0.0034  30   TYR L OH  
7108 N N   . ASN D 184 ? 0.6598 1.4032 1.0765 0.0906  -0.1800 -0.0207 31   ASN L N   
7109 C CA  . ASN D 184 ? 0.6722 1.4346 1.1220 0.0709  -0.1781 -0.0048 31   ASN L CA  
7110 C C   . ASN D 184 ? 0.6838 1.3805 1.1444 0.0658  -0.1631 0.0138  31   ASN L C   
7111 O O   . ASN D 184 ? 0.7466 1.3900 1.2083 0.0606  -0.1642 -0.0045 31   ASN L O   
7112 C CB  . ASN D 184 ? 0.7034 1.4938 1.1732 0.0528  -0.1946 -0.0352 31   ASN L CB  
7113 C CG  . ASN D 184 ? 0.8284 1.6907 1.2903 0.0561  -0.2091 -0.0505 31   ASN L CG  
7114 O OD1 . ASN D 184 ? 0.8704 1.7709 1.3374 0.0497  -0.2077 -0.0332 31   ASN L OD1 
7115 N ND2 . ASN D 184 ? 0.7817 1.6436 1.2231 0.0648  -0.2200 -0.0823 31   ASN L ND2 
7116 N N   . CYS D 185 ? 0.6687 1.3688 1.1370 0.0672  -0.1493 0.0503  32   CYS L N   
7117 C CA  . CYS D 185 ? 0.6507 1.2904 1.1266 0.0644  -0.1333 0.0714  32   CYS L CA  
7118 C C   . CYS D 185 ? 0.6673 1.3037 1.1782 0.0395  -0.1343 0.0695  32   CYS L C   
7119 O O   . CYS D 185 ? 0.6479 1.3031 1.1811 0.0301  -0.1266 0.0947  32   CYS L O   
7120 C CB  . CYS D 185 ? 0.5520 1.1978 1.0219 0.0767  -0.1186 0.1100  32   CYS L CB  
7121 S SG  . CYS D 185 ? 0.7369 1.3803 1.1662 0.1058  -0.1160 0.1143  32   CYS L SG  
7122 N N   . LEU D 186 ? 0.7261 1.3377 1.2422 0.0289  -0.1445 0.0383  33   LEU L N   
7123 C CA  . LEU D 186 ? 0.6611 1.2648 1.2097 0.0046  -0.1468 0.0326  33   LEU L CA  
7124 C C   . LEU D 186 ? 0.6546 1.1920 1.1988 -0.0005 -0.1498 0.0086  33   LEU L C   
7125 O O   . LEU D 186 ? 0.6875 1.2136 1.2111 0.0091  -0.1605 -0.0195 33   LEU L O   
7126 C CB  . LEU D 186 ? 0.6522 1.3230 1.2209 -0.0091 -0.1630 0.0151  33   LEU L CB  
7127 C CG  . LEU D 186 ? 0.8186 1.4856 1.4229 -0.0351 -0.1665 0.0078  33   LEU L CG  
7128 C CD1 . LEU D 186 ? 0.8358 1.5352 1.4669 -0.0456 -0.1570 0.0391  33   LEU L CD1 
7129 C CD2 . LEU D 186 ? 0.7966 1.5005 1.4099 -0.0454 -0.1872 -0.0279 33   LEU L CD2 
7130 N N   . ASP D 187 ? 0.6026 1.0968 1.1661 -0.0155 -0.1406 0.0195  34   ASP L N   
7131 C CA  . ASP D 187 ? 0.6392 1.0686 1.2022 -0.0235 -0.1435 -0.0008 34   ASP L CA  
7132 C C   . ASP D 187 ? 0.6922 1.1320 1.2900 -0.0505 -0.1515 -0.0134 34   ASP L C   
7133 O O   . ASP D 187 ? 0.6873 1.1778 1.3107 -0.0630 -0.1514 -0.0015 34   ASP L O   
7134 C CB  . ASP D 187 ? 0.6936 1.0533 1.2466 -0.0181 -0.1253 0.0225  34   ASP L CB  
7135 C CG  . ASP D 187 ? 0.7749 1.1204 1.2939 0.0087  -0.1173 0.0348  34   ASP L CG  
7136 O OD1 . ASP D 187 ? 0.8262 1.2008 1.3255 0.0232  -0.1276 0.0174  34   ASP L OD1 
7137 O OD2 . ASP D 187 ? 0.9280 1.2336 1.4401 0.0153  -0.1006 0.0618  34   ASP L OD2 
7138 N N   . TRP D 188 ? 0.8361 1.2266 1.4349 -0.0594 -0.1590 -0.0383 35   TRP L N   
7139 C CA  . TRP D 188 ? 0.7662 1.1552 1.3973 -0.0855 -0.1666 -0.0514 35   TRP L CA  
7140 C C   . TRP D 188 ? 0.7806 1.0903 1.4136 -0.0945 -0.1577 -0.0467 35   TRP L C   
7141 O O   . TRP D 188 ? 0.7514 1.0064 1.3599 -0.0834 -0.1597 -0.0606 35   TRP L O   
7142 C CB  . TRP D 188 ? 0.8119 1.2257 1.4446 -0.0898 -0.1893 -0.0922 35   TRP L CB  
7143 C CG  . TRP D 188 ? 0.7012 1.1981 1.3426 -0.0896 -0.1993 -0.0971 35   TRP L CG  
7144 C CD1 . TRP D 188 ? 0.7232 1.2612 1.3415 -0.0712 -0.2075 -0.1085 35   TRP L CD1 
7145 C CD2 . TRP D 188 ? 0.7186 1.2680 1.3939 -0.1088 -0.2025 -0.0908 35   TRP L CD2 
7146 N NE1 . TRP D 188 ? 0.7713 1.3833 1.4062 -0.0779 -0.2157 -0.1092 35   TRP L NE1 
7147 C CE2 . TRP D 188 ? 0.7467 1.3669 1.4168 -0.1005 -0.2131 -0.0988 35   TRP L CE2 
7148 C CE3 . TRP D 188 ? 0.7727 1.3166 1.4824 -0.1323 -0.1974 -0.0794 35   TRP L CE3 
7149 C CZ2 . TRP D 188 ? 0.7357 1.4194 1.4331 -0.1144 -0.2193 -0.0957 35   TRP L CZ2 
7150 C CZ3 . TRP D 188 ? 0.6753 1.2835 1.4134 -0.1460 -0.2033 -0.0769 35   TRP L CZ3 
7151 C CH2 . TRP D 188 ? 0.7516 1.4282 1.4832 -0.1368 -0.2144 -0.0852 35   TRP L CH2 
7152 N N   . TYR D 189 ? 0.7684 1.0720 1.4302 -0.1147 -0.1480 -0.0272 36   TYR L N   
7153 C CA  . TYR D 189 ? 0.7640 0.9952 1.4297 -0.1256 -0.1380 -0.0189 36   TYR L CA  
7154 C C   . TYR D 189 ? 0.9041 1.1324 1.6035 -0.1543 -0.1467 -0.0337 36   TYR L C   
7155 O O   . TYR D 189 ? 1.0061 1.2932 1.7314 -0.1673 -0.1548 -0.0394 36   TYR L O   
7156 C CB  . TYR D 189 ? 0.7398 0.9569 1.4074 -0.1231 -0.1150 0.0222  36   TYR L CB  
7157 C CG  . TYR D 189 ? 0.7423 0.9491 1.3759 -0.0952 -0.1053 0.0382  36   TYR L CG  
7158 C CD1 . TYR D 189 ? 0.7724 0.9091 1.3780 -0.0822 -0.0998 0.0372  36   TYR L CD1 
7159 C CD2 . TYR D 189 ? 0.6653 0.9319 1.2950 -0.0819 -0.1020 0.0543  36   TYR L CD2 
7160 C CE1 . TYR D 189 ? 0.8173 0.9446 1.3926 -0.0566 -0.0912 0.0514  36   TYR L CE1 
7161 C CE2 . TYR D 189 ? 0.7558 1.0131 1.3554 -0.0568 -0.0935 0.0691  36   TYR L CE2 
7162 C CZ  . TYR D 189 ? 0.7931 0.9810 1.3658 -0.0442 -0.0879 0.0674  36   TYR L CZ  
7163 O OH  . TYR D 189 ? 0.8158 0.9944 1.3590 -0.0192 -0.0797 0.0816  36   TYR L OH  
7164 N N   . LEU D 190 ? 0.9332 1.0913 1.6314 -0.1639 -0.1452 -0.0399 37   LEU L N   
7165 C CA  . LEU D 190 ? 0.9223 1.0655 1.6506 -0.1916 -0.1529 -0.0535 37   LEU L CA  
7166 C C   . LEU D 190 ? 0.9862 1.0691 1.7217 -0.2042 -0.1356 -0.0289 37   LEU L C   
7167 O O   . LEU D 190 ? 1.0726 1.0960 1.7815 -0.1913 -0.1266 -0.0202 37   LEU L O   
7168 C CB  . LEU D 190 ? 0.9610 1.0765 1.6801 -0.1924 -0.1740 -0.0942 37   LEU L CB  
7169 C CG  . LEU D 190 ? 1.0106 1.0824 1.7520 -0.2182 -0.1813 -0.1090 37   LEU L CG  
7170 C CD1 . LEU D 190 ? 0.9653 1.0910 1.7478 -0.2430 -0.1870 -0.1112 37   LEU L CD1 
7171 C CD2 . LEU D 190 ? 1.1447 1.1801 1.8688 -0.2125 -0.2012 -0.1477 37   LEU L CD2 
7172 N N   . GLN D 191 ? 1.0265 1.1249 1.7976 -0.2295 -0.1310 -0.0178 38   GLN L N   
7173 C CA  . GLN D 191 ? 1.0530 1.0990 1.8344 -0.2447 -0.1145 0.0056  38   GLN L CA  
7174 C C   . GLN D 191 ? 1.0251 1.0501 1.8342 -0.2733 -0.1251 -0.0132 38   GLN L C   
7175 O O   . GLN D 191 ? 1.0152 1.0903 1.8577 -0.2919 -0.1310 -0.0176 38   GLN L O   
7176 C CB  . GLN D 191 ? 0.9452 1.0286 1.7441 -0.2482 -0.0952 0.0424  38   GLN L CB  
7177 C CG  . GLN D 191 ? 0.9668 0.9959 1.7719 -0.2605 -0.0758 0.0693  38   GLN L CG  
7178 C CD  . GLN D 191 ? 0.8954 0.9646 1.7201 -0.2646 -0.0574 0.1040  38   GLN L CD  
7179 O OE1 . GLN D 191 ? 1.0566 1.1963 1.9015 -0.2670 -0.0612 0.1055  38   GLN L OE1 
7180 N NE2 . GLN D 191 ? 0.9278 0.9523 1.7464 -0.2650 -0.0376 0.1318  38   GLN L NE2 
7181 N N   . ARG D 192 ? 1.1472 1.0977 1.9425 -0.2768 -0.1282 -0.0244 39   ARG L N   
7182 C CA  . ARG D 192 ? 1.0605 0.9813 1.8804 -0.3045 -0.1372 -0.0397 39   ARG L CA  
7183 C C   . ARG D 192 ? 1.1194 1.0325 1.9667 -0.3272 -0.1188 -0.0091 39   ARG L C   
7184 O O   . ARG D 192 ? 1.0521 0.9629 1.8918 -0.3189 -0.0984 0.0232  39   ARG L O   
7185 C CB  . ARG D 192 ? 1.1104 0.9515 1.9048 -0.2998 -0.1462 -0.0596 39   ARG L CB  
7186 C CG  . ARG D 192 ? 1.1186 0.9726 1.8992 -0.2874 -0.1703 -0.0994 39   ARG L CG  
7187 C CD  . ARG D 192 ? 1.1445 0.9312 1.8868 -0.2679 -0.1751 -0.1132 39   ARG L CD  
7188 N NE  . ARG D 192 ? 1.3634 1.1726 2.0917 -0.2532 -0.1968 -0.1500 39   ARG L NE  
7189 C CZ  . ARG D 192 ? 1.5439 1.3096 2.2391 -0.2331 -0.2051 -0.1687 39   ARG L CZ  
7190 N NH1 . ARG D 192 ? 1.6343 1.3298 2.3062 -0.2250 -0.1938 -0.1540 39   ARG L NH1 
7191 N NH2 . ARG D 192 ? 1.5282 1.3215 2.2134 -0.2207 -0.2248 -0.2026 39   ARG L NH2 
7192 N N   . PRO D 193 ? 1.2922 1.2035 2.1725 -0.3563 -0.1257 -0.0188 40   PRO L N   
7193 C CA  . PRO D 193 ? 1.2034 1.1217 2.1147 -0.3796 -0.1086 0.0095  40   PRO L CA  
7194 C C   . PRO D 193 ? 1.2573 1.1203 2.1526 -0.3763 -0.0855 0.0421  40   PRO L C   
7195 O O   . PRO D 193 ? 1.3561 1.2476 2.2614 -0.3762 -0.0669 0.0727  40   PRO L O   
7196 C CB  . PRO D 193 ? 1.1489 1.0493 2.0888 -0.4093 -0.1225 -0.0120 40   PRO L CB  
7197 C CG  . PRO D 193 ? 1.1530 1.0823 2.0898 -0.4020 -0.1476 -0.0498 40   PRO L CG  
7198 C CD  . PRO D 193 ? 1.1388 1.0505 2.0321 -0.3694 -0.1499 -0.0564 40   PRO L CD  
7199 N N   . GLY D 194 ? 1.1357 0.9204 2.0061 -0.3732 -0.0866 0.0363  41   GLY L N   
7200 C CA  . GLY D 194 ? 1.2043 0.9318 2.0570 -0.3697 -0.0658 0.0658  41   GLY L CA  
7201 C C   . GLY D 194 ? 1.4204 1.1187 2.2295 -0.3371 -0.0605 0.0716  41   GLY L C   
7202 O O   . GLY D 194 ? 1.2992 0.9419 2.0896 -0.3326 -0.0449 0.0933  41   GLY L O   
7203 N N   . GLN D 195 ? 1.1740 0.9084 1.9664 -0.3145 -0.0727 0.0533  42   GLN L N   
7204 C CA  . GLN D 195 ? 1.2132 0.9193 1.9639 -0.2836 -0.0706 0.0539  42   GLN L CA  
7205 C C   . GLN D 195 ? 1.3041 1.0686 2.0482 -0.2629 -0.0593 0.0746  42   GLN L C   
7206 O O   . GLN D 195 ? 1.2763 1.1103 2.0464 -0.2701 -0.0586 0.0807  42   GLN L O   
7207 C CB  . GLN D 195 ? 1.1782 0.8738 1.9106 -0.2717 -0.0942 0.0147  42   GLN L CB  
7208 C CG  . GLN D 195 ? 1.2199 0.8643 1.9609 -0.2919 -0.1093 -0.0103 42   GLN L CG  
7209 C CD  . GLN D 195 ? 1.4231 0.9800 2.1477 -0.2963 -0.0990 0.0036  42   GLN L CD  
7210 O OE1 . GLN D 195 ? 1.5728 1.1114 2.3163 -0.3174 -0.0853 0.0263  42   GLN L OE1 
7211 N NE2 . GLN D 195 ? 1.3998 0.9025 2.0889 -0.2763 -0.1056 -0.0101 42   GLN L NE2 
7212 N N   . SER D 196 ? 1.2055 0.9397 1.9142 -0.2369 -0.0511 0.0853  43   SER L N   
7213 C CA  . SER D 196 ? 1.1047 0.8886 1.8015 -0.2138 -0.0431 0.1014  43   SER L CA  
7214 C C   . SER D 196 ? 1.0441 0.8805 1.7356 -0.2010 -0.0625 0.0730  43   SER L C   
7215 O O   . SER D 196 ? 1.1654 0.9865 1.8538 -0.2046 -0.0811 0.0405  43   SER L O   
7216 C CB  . SER D 196 ? 1.1203 0.8525 1.7804 -0.1900 -0.0298 0.1192  43   SER L CB  
7217 O OG  . SER D 196 ? 1.1891 0.8734 1.8528 -0.2014 -0.0116 0.1460  43   SER L OG  
7218 N N   . PRO D 197 ? 1.1078 1.0073 1.7983 -0.1863 -0.0588 0.0846  44   PRO L N   
7219 C CA  . PRO D 197 ? 1.0910 1.0412 1.7737 -0.1731 -0.0764 0.0591  44   PRO L CA  
7220 C C   . PRO D 197 ? 0.8916 0.7987 1.5372 -0.1516 -0.0859 0.0373  44   PRO L C   
7221 O O   . PRO D 197 ? 0.9256 0.7726 1.5463 -0.1395 -0.0761 0.0482  44   PRO L O   
7222 C CB  . PRO D 197 ? 0.8188 0.8309 1.5018 -0.1591 -0.0662 0.0836  44   PRO L CB  
7223 C CG  . PRO D 197 ? 0.8644 0.8791 1.5724 -0.1752 -0.0484 0.1151  44   PRO L CG  
7224 C CD  . PRO D 197 ? 1.0597 0.9930 1.7608 -0.1842 -0.0397 0.1207  44   PRO L CD  
7225 N N   . GLN D 198 ? 0.8936 0.8334 1.5360 -0.1467 -0.1057 0.0053  45   GLN L N   
7226 C CA  . GLN D 198 ? 1.0046 0.9147 1.6137 -0.1258 -0.1170 -0.0194 45   GLN L CA  
7227 C C   . GLN D 198 ? 0.9224 0.9009 1.5222 -0.1086 -0.1266 -0.0314 45   GLN L C   
7228 O O   . GLN D 198 ? 0.9357 0.9820 1.5577 -0.1169 -0.1298 -0.0289 45   GLN L O   
7229 C CB  . GLN D 198 ? 1.0188 0.8861 1.6308 -0.1383 -0.1347 -0.0535 45   GLN L CB  
7230 C CG  . GLN D 198 ? 1.0436 0.9659 1.6755 -0.1490 -0.1552 -0.0843 45   GLN L CG  
7231 C CD  . GLN D 198 ? 1.3124 1.1895 1.9473 -0.1609 -0.1731 -0.1179 45   GLN L CD  
7232 O OE1 . GLN D 198 ? 1.4323 1.2531 2.0764 -0.1776 -0.1692 -0.1127 45   GLN L OE1 
7233 N NE2 . GLN D 198 ? 1.2993 1.2007 1.9259 -0.1523 -0.1931 -0.1528 45   GLN L NE2 
7234 N N   . LEU D 199 ? 0.9392 0.8992 1.5055 -0.0845 -0.1314 -0.0447 46   LEU L N   
7235 C CA  . LEU D 199 ? 0.8354 0.8551 1.3880 -0.0660 -0.1395 -0.0554 46   LEU L CA  
7236 C C   . LEU D 199 ? 0.9394 0.9790 1.4942 -0.0695 -0.1629 -0.0972 46   LEU L C   
7237 O O   . LEU D 199 ? 0.9600 0.9474 1.5050 -0.0701 -0.1730 -0.1218 46   LEU L O   
7238 C CB  . LEU D 199 ? 0.8194 0.8123 1.3348 -0.0375 -0.1318 -0.0472 46   LEU L CB  
7239 C CG  . LEU D 199 ? 0.8627 0.9109 1.3596 -0.0165 -0.1395 -0.0582 46   LEU L CG  
7240 C CD1 . LEU D 199 ? 0.7668 0.8933 1.2823 -0.0208 -0.1357 -0.0394 46   LEU L CD1 
7241 C CD2 . LEU D 199 ? 0.7739 0.7880 1.2355 0.0102  -0.1304 -0.0482 46   LEU L CD2 
7242 N N   . LEU D 200 ? 0.8335 0.9488 1.4010 -0.0716 -0.1719 -0.1052 47   LEU L N   
7243 C CA  . LEU D 200 ? 0.8844 1.0295 1.4532 -0.0730 -0.1941 -0.1442 47   LEU L CA  
7244 C C   . LEU D 200 ? 0.9591 1.1503 1.5029 -0.0492 -0.1998 -0.1539 47   LEU L C   
7245 O O   . LEU D 200 ? 0.9630 1.1339 1.4834 -0.0349 -0.2106 -0.1808 47   LEU L O   
7246 C CB  . LEU D 200 ? 0.8504 1.0473 1.4561 -0.0971 -0.2024 -0.1497 47   LEU L CB  
7247 C CG  . LEU D 200 ? 0.8851 1.0450 1.5199 -0.1241 -0.2013 -0.1479 47   LEU L CG  
7248 C CD1 . LEU D 200 ? 0.9961 1.2195 1.6666 -0.1446 -0.2073 -0.1483 47   LEU L CD1 
7249 C CD2 . LEU D 200 ? 1.0838 1.1873 1.7122 -0.1284 -0.2163 -0.1813 47   LEU L CD2 
7250 N N   . ILE D 201 ? 0.8173 1.0708 1.3656 -0.0449 -0.1930 -0.1326 48   ILE L N   
7251 C CA  . ILE D 201 ? 0.8055 1.1096 1.3322 -0.0244 -0.1978 -0.1386 48   ILE L CA  
7252 C C   . ILE D 201 ? 0.8349 1.1453 1.3487 -0.0097 -0.1789 -0.1009 48   ILE L C   
7253 O O   . ILE D 201 ? 0.7911 1.1078 1.3237 -0.0199 -0.1658 -0.0706 48   ILE L O   
7254 C CB  . ILE D 201 ? 0.7798 1.1635 1.3248 -0.0337 -0.2116 -0.1525 48   ILE L CB  
7255 C CG1 . ILE D 201 ? 0.8102 1.1879 1.3684 -0.0478 -0.2313 -0.1912 48   ILE L CG1 
7256 C CG2 . ILE D 201 ? 0.7801 1.2168 1.3017 -0.0129 -0.2155 -0.1559 48   ILE L CG2 
7257 C CD1 . ILE D 201 ? 0.8806 1.2429 1.4116 -0.0314 -0.2452 -0.2261 48   ILE L CD1 
7258 N N   . SER D 202 ? 0.8029 1.1116 1.2851 0.0143  -0.1778 -0.1032 49   SER L N   
7259 C CA  . SER D 202 ? 0.6601 0.9800 1.1276 0.0306  -0.1621 -0.0703 49   SER L CA  
7260 C C   . SER D 202 ? 0.8546 1.2412 1.3076 0.0451  -0.1697 -0.0769 49   SER L C   
7261 O O   . SER D 202 ? 0.8113 1.2091 1.2498 0.0528  -0.1840 -0.1085 49   SER L O   
7262 C CB  . SER D 202 ? 0.6579 0.9070 1.0990 0.0473  -0.1511 -0.0619 49   SER L CB  
7263 O OG  . SER D 202 ? 0.9894 1.1807 1.4251 0.0437  -0.1599 -0.0896 49   SER L OG  
7264 N N   . LEU D 203 ? 0.7264 1.1576 1.1836 0.0486  -0.1603 -0.0469 50   LEU L N   
7265 C CA  . LEU D 203 ? 0.5917 1.0867 1.0347 0.0622  -0.1654 -0.0468 50   LEU L CA  
7266 C C   . LEU D 203 ? 0.6634 1.2150 1.1167 0.0526  -0.1846 -0.0768 50   LEU L C   
7267 O O   . LEU D 203 ? 0.7642 1.3478 1.1981 0.0651  -0.1946 -0.0960 50   LEU L O   
7268 C CB  . LEU D 203 ? 0.7236 1.1949 1.1307 0.0873  -0.1630 -0.0516 50   LEU L CB  
7269 C CG  . LEU D 203 ? 0.6288 1.0540 1.0228 0.1001  -0.1440 -0.0194 50   LEU L CG  
7270 C CD1 . LEU D 203 ? 0.6074 1.0248 0.9670 0.1254  -0.1429 -0.0235 50   LEU L CD1 
7271 C CD2 . LEU D 203 ? 0.6861 1.1453 1.0967 0.0951  -0.1322 0.0184  50   LEU L CD2 
7272 N N   . GLY D 204 ? 0.6673 1.2324 1.1515 0.0302  -0.1898 -0.0810 51   GLY L N   
7273 C CA  . GLY D 204 ? 0.7319 1.3570 1.2295 0.0198  -0.2071 -0.1049 51   GLY L CA  
7274 C C   . GLY D 204 ? 0.7949 1.4003 1.2927 0.0138  -0.2236 -0.1464 51   GLY L C   
7275 O O   . GLY D 204 ? 0.7706 1.3887 1.2945 -0.0058 -0.2332 -0.1606 51   GLY L O   
7276 N N   . SER D 205 ? 0.7853 1.3600 1.2549 0.0305  -0.2277 -0.1670 52   SER L N   
7277 C CA  . SER D 205 ? 0.8441 1.4066 1.3113 0.0276  -0.2453 -0.2091 52   SER L CA  
7278 C C   . SER D 205 ? 0.8237 1.3106 1.2711 0.0381  -0.2442 -0.2238 52   SER L C   
7279 O O   . SER D 205 ? 0.8351 1.3058 1.2803 0.0363  -0.2593 -0.2595 52   SER L O   
7280 C CB  . SER D 205 ? 0.9083 1.5355 1.3608 0.0380  -0.2594 -0.2319 52   SER L CB  
7281 O OG  . SER D 205 ? 0.8001 1.4370 1.2235 0.0602  -0.2514 -0.2190 52   SER L OG  
7282 N N   . TYR D 206 ? 0.8652 1.3052 1.2982 0.0493  -0.2277 -0.1983 53   TYR L N   
7283 C CA  . TYR D 206 ? 0.8496 1.2178 1.2614 0.0612  -0.2267 -0.2115 53   TYR L CA  
7284 C C   . TYR D 206 ? 0.8411 1.1473 1.2719 0.0431  -0.2256 -0.2131 53   TYR L C   
7285 O O   . TYR D 206 ? 0.8449 1.1240 1.2876 0.0349  -0.2104 -0.1823 53   TYR L O   
7286 C CB  . TYR D 206 ? 0.7423 1.0874 1.1299 0.0814  -0.2099 -0.1839 53   TYR L CB  
7287 C CG  . TYR D 206 ? 0.9252 1.3285 1.2927 0.0994  -0.2113 -0.1827 53   TYR L CG  
7288 C CD1 . TYR D 206 ? 0.7184 1.1209 1.0597 0.1171  -0.2206 -0.2106 53   TYR L CD1 
7289 C CD2 . TYR D 206 ? 0.7864 1.2462 1.1614 0.0982  -0.2036 -0.1541 53   TYR L CD2 
7290 C CE1 . TYR D 206 ? 0.7235 1.1802 1.0464 0.1326  -0.2215 -0.2093 53   TYR L CE1 
7291 C CE2 . TYR D 206 ? 0.6695 1.1821 1.0259 0.1137  -0.2052 -0.1522 53   TYR L CE2 
7292 C CZ  . TYR D 206 ? 0.7169 1.2280 1.0473 0.1305  -0.2138 -0.1796 53   TYR L CZ  
7293 O OH  . TYR D 206 ? 0.8082 1.3726 1.1200 0.1451  -0.2151 -0.1774 53   TYR L OH  
7294 N N   . ARG D 207 ? 0.9474 1.2315 1.3812 0.0368  -0.2420 -0.2493 54   ARG L N   
7295 C CA  . ARG D 207 ? 0.9017 1.1269 1.3534 0.0186  -0.2435 -0.2543 54   ARG L CA  
7296 C C   . ARG D 207 ? 0.9374 1.0835 1.3715 0.0280  -0.2302 -0.2385 54   ARG L C   
7297 O O   . ARG D 207 ? 0.8494 0.9685 1.2547 0.0488  -0.2314 -0.2498 54   ARG L O   
7298 C CB  . ARG D 207 ? 0.8730 1.0920 1.3285 0.0126  -0.2656 -0.2986 54   ARG L CB  
7299 C CG  . ARG D 207 ? 0.9333 1.1081 1.4144 -0.0112 -0.2704 -0.3054 54   ARG L CG  
7300 C CD  . ARG D 207 ? 1.1629 1.3405 1.6496 -0.0173 -0.2941 -0.3501 54   ARG L CD  
7301 N NE  . ARG D 207 ? 1.2610 1.5202 1.7555 -0.0183 -0.3061 -0.3660 54   ARG L NE  
7302 C CZ  . ARG D 207 ? 1.1730 1.4642 1.6476 -0.0016 -0.3188 -0.3942 54   ARG L CZ  
7303 N NH1 . ARG D 207 ? 1.0011 1.2497 1.4476 0.0175  -0.3216 -0.4107 54   ARG L NH1 
7304 N NH2 . ARG D 207 ? 0.9749 1.3411 1.4575 -0.0041 -0.3290 -0.4063 54   ARG L NH2 
7305 N N   . ALA D 208 ? 0.9455 1.1085 1.2227 0.0568  -0.3339 -0.1246 55   ALA L N   
7306 C CA  . ALA D 208 ? 0.9759 1.1233 1.2813 0.0624  -0.3115 -0.1163 55   ALA L CA  
7307 C C   . ALA D 208 ? 1.0572 1.1369 1.3057 0.0731  -0.2877 -0.1333 55   ALA L C   
7308 O O   . ALA D 208 ? 1.1156 1.1549 1.3119 0.0664  -0.2913 -0.1574 55   ALA L O   
7309 C CB  . ALA D 208 ? 0.8678 1.0261 1.2357 0.0331  -0.3224 -0.1212 55   ALA L CB  
7310 N N   . SER D 209 ? 0.9165 0.9847 1.1755 0.0901  -0.2627 -0.1203 56   SER L N   
7311 C CA  . SER D 209 ? 1.0012 1.0065 1.2105 0.1021  -0.2378 -0.1339 56   SER L CA  
7312 C C   . SER D 209 ? 1.1092 1.0685 1.3175 0.0746  -0.2406 -0.1618 56   SER L C   
7313 O O   . SER D 209 ? 1.0570 1.0334 1.3204 0.0508  -0.2519 -0.1634 56   SER L O   
7314 C CB  . SER D 209 ? 0.9670 0.9753 1.1956 0.1246  -0.2116 -0.1128 56   SER L CB  
7315 O OG  . SER D 209 ? 0.8910 0.8386 1.0716 0.1371  -0.1868 -0.1253 56   SER L OG  
7316 N N   . GLY D 210 ? 1.0406 0.9405 1.1852 0.0777  -0.2298 -0.1841 57   GLY L N   
7317 C CA  . GLY D 210 ? 0.9487 0.8006 1.0839 0.0521  -0.2318 -0.2126 57   GLY L CA  
7318 C C   . GLY D 210 ? 1.2716 1.1303 1.4035 0.0241  -0.2602 -0.2326 57   GLY L C   
7319 O O   . GLY D 210 ? 1.1671 0.9860 1.2890 0.0011  -0.2631 -0.2580 57   GLY L O   
7320 N N   . VAL D 211 ? 1.2174 1.1255 1.3571 0.0252  -0.2809 -0.2222 58   VAL L N   
7321 C CA  . VAL D 211 ? 1.1375 1.0566 1.2723 0.0004  -0.3087 -0.2400 58   VAL L CA  
7322 C C   . VAL D 211 ? 1.3025 1.1891 1.3605 0.0109  -0.3077 -0.2555 58   VAL L C   
7323 O O   . VAL D 211 ? 1.2436 1.1421 1.2725 0.0383  -0.2998 -0.2403 58   VAL L O   
7324 C CB  . VAL D 211 ? 1.1411 1.1330 1.3291 -0.0053 -0.3325 -0.2201 58   VAL L CB  
7325 C CG1 . VAL D 211 ? 1.1626 1.1674 1.3352 -0.0255 -0.3603 -0.2370 58   VAL L CG1 
7326 C CG2 . VAL D 211 ? 1.0571 1.0768 1.3208 -0.0213 -0.3359 -0.2095 58   VAL L CG2 
7327 N N   . PRO D 212 ? 1.3736 1.2195 1.3968 -0.0100 -0.3151 -0.2855 59   PRO L N   
7328 C CA  . PRO D 212 ? 1.4489 1.2593 1.3965 -0.0003 -0.3125 -0.3016 59   PRO L CA  
7329 C C   . PRO D 212 ? 1.4889 1.3465 1.4277 0.0053  -0.3336 -0.2926 59   PRO L C   
7330 O O   . PRO D 212 ? 1.3561 1.2712 1.3457 -0.0040 -0.3540 -0.2787 59   PRO L O   
7331 C CB  . PRO D 212 ? 1.3919 1.1551 1.3176 -0.0299 -0.3188 -0.3358 59   PRO L CB  
7332 C CG  . PRO D 212 ? 1.3857 1.1807 1.3805 -0.0584 -0.3364 -0.3358 59   PRO L CG  
7333 C CD  . PRO D 212 ? 1.2797 1.1081 1.3304 -0.0439 -0.3254 -0.3067 59   PRO L CD  
7334 N N   . ASP D 213 ? 1.4737 1.3047 1.3451 0.0212  -0.3279 -0.3008 60   ASP L N   
7335 C CA  . ASP D 213 ? 1.4766 1.3464 1.3294 0.0318  -0.3438 -0.2917 60   ASP L CA  
7336 C C   . ASP D 213 ? 1.5282 1.4241 1.3928 0.0034  -0.3750 -0.3063 60   ASP L C   
7337 O O   . ASP D 213 ? 1.6495 1.5878 1.5116 0.0095  -0.3917 -0.2961 60   ASP L O   
7338 C CB  . ASP D 213 ? 1.5828 1.4109 1.3569 0.0543  -0.3288 -0.2998 60   ASP L CB  
7339 C CG  . ASP D 213 ? 1.6775 1.4504 1.4238 0.0713  -0.2968 -0.3020 60   ASP L CG  
7340 O OD1 . ASP D 213 ? 1.6916 1.4775 1.4456 0.0985  -0.2793 -0.2782 60   ASP L OD1 
7341 O OD2 . ASP D 213 ? 1.7262 1.4431 1.4438 0.0571  -0.2890 -0.3275 60   ASP L OD2 
7342 N N   . ARG D 214 ? 1.5568 1.4290 1.4334 -0.0270 -0.3832 -0.3298 61   ARG L N   
7343 C CA  . ARG D 214 ? 1.6289 1.5237 1.5120 -0.0542 -0.4125 -0.3457 61   ARG L CA  
7344 C C   . ARG D 214 ? 1.5221 1.4888 1.4742 -0.0623 -0.4343 -0.3247 61   ARG L C   
7345 O O   . ARG D 214 ? 1.5543 1.5566 1.5089 -0.0733 -0.4588 -0.3276 61   ARG L O   
7346 C CB  . ARG D 214 ? 1.6002 1.4502 1.4782 -0.0850 -0.4145 -0.3766 61   ARG L CB  
7347 C CG  . ARG D 214 ? 1.6483 1.5194 1.5972 -0.1086 -0.4228 -0.3743 61   ARG L CG  
7348 C CD  . ARG D 214 ? 1.4882 1.3116 1.4252 -0.1385 -0.4241 -0.4066 61   ARG L CD  
7349 N NE  . ARG D 214 ? 1.3755 1.1322 1.2752 -0.1288 -0.3951 -0.4172 61   ARG L NE  
7350 C CZ  . ARG D 214 ? 1.4534 1.1899 1.3860 -0.1333 -0.3800 -0.4154 61   ARG L CZ  
7351 N NH1 . ARG D 214 ? 1.4114 1.1888 1.4149 -0.1481 -0.3914 -0.4037 61   ARG L NH1 
7352 N NH2 . ARG D 214 ? 1.4652 1.1403 1.3595 -0.1231 -0.3533 -0.4253 61   ARG L NH2 
7353 N N   . PHE D 215 ? 1.4622 1.4515 1.4701 -0.0567 -0.4255 -0.3034 62   PHE L N   
7354 C CA  . PHE D 215 ? 1.3490 1.4064 1.4222 -0.0613 -0.4436 -0.2809 62   PHE L CA  
7355 C C   . PHE D 215 ? 1.3552 1.4522 1.4205 -0.0320 -0.4424 -0.2545 62   PHE L C   
7356 O O   . PHE D 215 ? 1.3298 1.4041 1.3573 -0.0048 -0.4210 -0.2463 62   PHE L O   
7357 C CB  . PHE D 215 ? 1.3343 1.4004 1.4705 -0.0672 -0.4342 -0.2685 62   PHE L CB  
7358 C CG  . PHE D 215 ? 1.3798 1.4057 1.5257 -0.0948 -0.4331 -0.2932 62   PHE L CG  
7359 C CD1 . PHE D 215 ? 1.3684 1.3331 1.4836 -0.0892 -0.4079 -0.3053 62   PHE L CD1 
7360 C CD2 . PHE D 215 ? 1.3708 1.4202 1.5564 -0.1261 -0.4570 -0.3040 62   PHE L CD2 
7361 C CE1 . PHE D 215 ? 1.3463 1.2732 1.4700 -0.1146 -0.4064 -0.3280 62   PHE L CE1 
7362 C CE2 . PHE D 215 ? 1.3183 1.3309 1.5129 -0.1518 -0.4559 -0.3269 62   PHE L CE2 
7363 C CZ  . PHE D 215 ? 1.3419 1.2928 1.5054 -0.1462 -0.4305 -0.3390 62   PHE L CZ  
7364 N N   . SER D 216 ? 1.3677 1.5244 1.4685 -0.0376 -0.4655 -0.2410 63   SER L N   
7365 C CA  . SER D 216 ? 1.3835 1.5810 1.4777 -0.0121 -0.4672 -0.2168 63   SER L CA  
7366 C C   . SER D 216 ? 1.1605 1.4264 1.3179 -0.0214 -0.4893 -0.1977 63   SER L C   
7367 O O   . SER D 216 ? 1.0916 1.3750 1.2715 -0.0476 -0.5120 -0.2100 63   SER L O   
7368 C CB  . SER D 216 ? 1.3432 1.5260 1.3696 -0.0042 -0.4737 -0.2299 63   SER L CB  
7369 O OG  . SER D 216 ? 1.4424 1.6717 1.4685 0.0166  -0.4801 -0.2068 63   SER L OG  
7370 N N   . GLY D 217 ? 1.1289 1.4332 1.3141 0.0003  -0.4821 -0.1677 64   GLY L N   
7371 C CA  . GLY D 217 ? 1.0142 1.3839 1.2583 -0.0047 -0.5003 -0.1465 64   GLY L CA  
7372 C C   . GLY D 217 ? 1.0722 1.4793 1.2950 0.0152  -0.5086 -0.1303 64   GLY L C   
7373 O O   . GLY D 217 ? 1.0872 1.4773 1.2644 0.0409  -0.4929 -0.1244 64   GLY L O   
7374 N N   . SER D 218 ? 1.0092 1.4664 1.2642 0.0032  -0.5298 -0.1214 65   SER L N   
7375 C CA  . SER D 218 ? 1.0072 1.4988 1.2415 0.0176  -0.5303 -0.1023 65   SER L CA  
7376 C C   . SER D 218 ? 0.9380 1.4744 1.2116 -0.0007 -0.5149 -0.0742 65   SER L C   
7377 O O   . SER D 218 ? 0.9422 1.4818 1.2475 -0.0238 -0.5071 -0.0761 65   SER L O   
7378 C CB  . SER D 218 ? 1.0066 1.4819 1.1821 0.0184  -0.5543 -0.1294 65   SER L CB  
7379 O OG  . SER D 218 ? 1.1748 1.6409 1.3545 -0.0133 -0.5686 -0.1514 65   SER L OG  
7380 N N   . GLY D 219 ? 1.1318 1.4435 1.0186 0.1806  -0.3742 0.0142  66   GLY L N   
7381 C CA  . GLY D 219 ? 1.2526 1.5679 1.1470 0.1929  -0.3832 0.0251  66   GLY L CA  
7382 C C   . GLY D 219 ? 1.2792 1.5674 1.1242 0.1933  -0.3740 0.0593  66   GLY L C   
7383 O O   . GLY D 219 ? 1.2719 1.5374 1.0779 0.1822  -0.3590 0.0752  66   GLY L O   
7384 N N   . SER D 220 ? 1.2395 1.5313 1.0883 0.2064  -0.3831 0.0708  67   SER L N   
7385 C CA  . SER D 220 ? 1.2860 1.5532 1.0922 0.2081  -0.3749 0.1024  67   SER L CA  
7386 C C   . SER D 220 ? 1.4244 1.6945 1.2586 0.2191  -0.3792 0.1075  67   SER L C   
7387 O O   . SER D 220 ? 1.4623 1.7616 1.3360 0.2319  -0.3976 0.0910  67   SER L O   
7388 C CB  . SER D 220 ? 1.2886 1.5635 1.0365 0.2205  -0.3915 0.1201  67   SER L CB  
7389 O OG  . SER D 220 ? 1.4267 1.6772 1.1335 0.2217  -0.3829 0.1505  67   SER L OG  
7390 N N   . GLY D 221 ? 1.3622 1.6021 1.1764 0.2135  -0.3614 0.1307  68   GLY L N   
7391 C CA  . GLY D 221 ? 1.3760 1.6139 1.2136 0.2236  -0.3621 0.1388  68   GLY L CA  
7392 C C   . GLY D 221 ? 1.2944 1.5331 1.1966 0.2161  -0.3515 0.1180  68   GLY L C   
7393 O O   . GLY D 221 ? 1.3127 1.5231 1.2256 0.1972  -0.3246 0.1189  68   GLY L O   
7394 N N   . THR D 222 ? 1.2683 1.5406 1.2138 0.2303  -0.3725 0.0990  69   THR L N   
7395 C CA  . THR D 222 ? 1.3442 1.6214 1.3539 0.2258  -0.3653 0.0786  69   THR L CA  
7396 C C   . THR D 222 ? 1.2933 1.5990 1.3413 0.2238  -0.3767 0.0469  69   THR L C   
7397 O O   . THR D 222 ? 1.3022 1.6073 1.4010 0.2148  -0.3661 0.0280  69   THR L O   
7398 C CB  . THR D 222 ? 1.3034 1.5944 1.3415 0.2448  -0.3773 0.0858  69   THR L CB  
7399 O OG1 . THR D 222 ? 1.2794 1.6086 1.3101 0.2666  -0.4097 0.0855  69   THR L OG1 
7400 C CG2 . THR D 222 ? 1.2573 1.5169 1.2655 0.2451  -0.3618 0.1151  69   THR L CG2 
7401 N N   . ASP D 223 ? 1.2658 1.5960 1.2917 0.2314  -0.3971 0.0400  70   ASP L N   
7402 C CA  . ASP D 223 ? 1.3852 1.7459 1.4468 0.2310  -0.4099 0.0091  70   ASP L CA  
7403 C C   . ASP D 223 ? 1.3245 1.6718 1.3645 0.2138  -0.3971 0.0008  70   ASP L C   
7404 O O   . ASP D 223 ? 1.2455 1.5956 1.2392 0.2171  -0.4053 0.0096  70   ASP L O   
7405 C CB  . ASP D 223 ? 1.3631 1.7661 1.4211 0.2525  -0.4435 0.0052  70   ASP L CB  
7406 C CG  . ASP D 223 ? 1.5236 1.9618 1.6280 0.2531  -0.4574 -0.0281 70   ASP L CG  
7407 O OD1 . ASP D 223 ? 1.5776 2.0293 1.6673 0.2494  -0.4647 -0.0425 70   ASP L OD1 
7408 O OD2 . ASP D 223 ? 1.4657 1.9177 1.6223 0.2566  -0.4601 -0.0403 70   ASP L OD2 
7409 N N   . PHE D 224 ? 1.2885 1.6219 1.3634 0.1957  -0.3768 -0.0158 71   PHE L N   
7410 C CA  . PHE D 224 ? 1.3335 1.6527 1.3953 0.1781  -0.3615 -0.0231 71   PHE L CA  
7411 C C   . PHE D 224 ? 1.2426 1.5851 1.3519 0.1738  -0.3667 -0.0572 71   PHE L C   
7412 O O   . PHE D 224 ? 1.2191 1.5802 1.3778 0.1786  -0.3741 -0.0752 71   PHE L O   
7413 C CB  . PHE D 224 ? 1.2936 1.5734 1.3506 0.1573  -0.3296 -0.0100 71   PHE L CB  
7414 C CG  . PHE D 224 ? 1.3222 1.5775 1.3309 0.1588  -0.3218 0.0228  71   PHE L CG  
7415 C CD1 . PHE D 224 ? 1.2788 1.5209 1.3006 0.1606  -0.3139 0.0342  71   PHE L CD1 
7416 C CD2 . PHE D 224 ? 1.2776 1.5234 1.2284 0.1584  -0.3220 0.0420  71   PHE L CD2 
7417 C CE1 . PHE D 224 ? 1.2761 1.4952 1.2536 0.1614  -0.3057 0.0636  71   PHE L CE1 
7418 C CE2 . PHE D 224 ? 1.2800 1.5038 1.1859 0.1593  -0.3148 0.0718  71   PHE L CE2 
7419 C CZ  . PHE D 224 ? 1.3081 1.5182 1.2269 0.1605  -0.3064 0.0823  71   PHE L CZ  
7420 N N   . THR D 225 ? 1.3074 1.6488 1.4019 0.1647  -0.3622 -0.0660 72   THR L N   
7421 C CA  . THR D 225 ? 1.2254 1.5906 1.3584 0.1617  -0.3688 -0.0986 72   THR L CA  
7422 C C   . THR D 225 ? 1.1079 1.4524 1.2375 0.1422  -0.3466 -0.1037 72   THR L C   
7423 O O   . THR D 225 ? 1.2096 1.5355 1.2931 0.1375  -0.3377 -0.0838 72   THR L O   
7424 C CB  . THR D 225 ? 1.1708 1.5718 1.2882 0.1784  -0.3976 -0.1080 72   THR L CB  
7425 O OG1 . THR D 225 ? 1.1594 1.5739 1.2603 0.1969  -0.4169 -0.0912 72   THR L OG1 
7426 C CG2 . THR D 225 ? 1.1887 1.6212 1.3568 0.1784  -0.4085 -0.1437 72   THR L CG2 
7427 N N   . LEU D 226 ? 1.1067 1.4557 1.2864 0.1311  -0.3376 -0.1298 73   LEU L N   
7428 C CA  . LEU D 226 ? 1.0720 1.4044 1.2573 0.1127  -0.3165 -0.1371 73   LEU L CA  
7429 C C   . LEU D 226 ? 1.1631 1.5228 1.3721 0.1150  -0.3283 -0.1678 73   LEU L C   
7430 O O   . LEU D 226 ? 1.2504 1.6315 1.5072 0.1169  -0.3365 -0.1940 73   LEU L O   
7431 C CB  . LEU D 226 ? 1.0087 1.3200 1.2324 0.0950  -0.2922 -0.1407 73   LEU L CB  
7432 C CG  . LEU D 226 ? 1.1603 1.4567 1.3990 0.0752  -0.2698 -0.1495 73   LEU L CG  
7433 C CD1 . LEU D 226 ? 1.1522 1.4295 1.3383 0.0696  -0.2594 -0.1251 73   LEU L CD1 
7434 C CD2 . LEU D 226 ? 0.9734 1.2502 1.2481 0.0578  -0.2469 -0.1510 73   LEU L CD2 
7435 N N   . LYS D 227 ? 1.1471 1.5061 1.3230 0.1142  -0.3284 -0.1648 74   LYS L N   
7436 C CA  . LYS D 227 ? 1.2057 1.5880 1.3996 0.1149  -0.3369 -0.1934 74   LYS L CA  
7437 C C   . LYS D 227 ? 1.2790 1.6428 1.4933 0.0961  -0.3119 -0.2028 74   LYS L C   
7438 O O   . LYS D 227 ? 1.3574 1.6933 1.5450 0.0859  -0.2925 -0.1803 74   LYS L O   
7439 C CB  . LYS D 227 ? 1.2640 1.6605 1.4105 0.1271  -0.3541 -0.1868 74   LYS L CB  
7440 C CG  . LYS D 227 ? 1.3105 1.7333 1.4745 0.1278  -0.3636 -0.2180 74   LYS L CG  
7441 C CD  . LYS D 227 ? 1.3958 1.8194 1.5104 0.1323  -0.3683 -0.2086 74   LYS L CD  
7442 C CE  . LYS D 227 ? 1.4377 1.8257 1.5291 0.1192  -0.3419 -0.1879 74   LYS L CE  
7443 N NZ  . LYS D 227 ? 1.4089 1.7835 1.5456 0.1019  -0.3187 -0.2041 74   LYS L NZ  
7444 N N   . ILE D 228 ? 1.3297 1.7104 1.5919 0.0914  -0.3123 -0.2355 75   ILE L N   
7445 C CA  . ILE D 228 ? 1.3354 1.7027 1.6223 0.0747  -0.2902 -0.2482 75   ILE L CA  
7446 C C   . ILE D 228 ? 1.3331 1.7275 1.6387 0.0781  -0.3016 -0.2803 75   ILE L C   
7447 O O   . ILE D 228 ? 1.2217 1.6435 1.5618 0.0837  -0.3171 -0.3063 75   ILE L O   
7448 C CB  . ILE D 228 ? 1.2535 1.6080 1.5894 0.0606  -0.2724 -0.2566 75   ILE L CB  
7449 C CG1 . ILE D 228 ? 1.3169 1.6704 1.6923 0.0468  -0.2567 -0.2812 75   ILE L CG1 
7450 C CG2 . ILE D 228 ? 1.1747 1.5495 1.5425 0.0696  -0.2888 -0.2702 75   ILE L CG2 
7451 C CD1 . ILE D 228 ? 1.2087 1.5530 1.6350 0.0331  -0.2408 -0.2926 75   ILE L CD1 
7452 N N   . SER D 229 ? 1.3265 1.7141 1.6093 0.0745  -0.2936 -0.2784 76   SER L N   
7453 C CA  . SER D 229 ? 1.4247 1.8356 1.7201 0.0766  -0.3020 -0.3079 76   SER L CA  
7454 C C   . SER D 229 ? 1.3855 1.7869 1.7264 0.0604  -0.2797 -0.3290 76   SER L C   
7455 O O   . SER D 229 ? 1.4011 1.7736 1.7433 0.0479  -0.2555 -0.3124 76   SER L O   
7456 C CB  . SER D 229 ? 1.3909 1.8012 1.6346 0.0831  -0.3067 -0.2945 76   SER L CB  
7457 O OG  . SER D 229 ? 1.2724 1.6505 1.4959 0.0728  -0.2825 -0.2708 76   SER L OG  
7458 N N   . ARG D 230 ? 1.2544 1.6815 1.6325 0.0603  -0.2880 -0.3654 77   ARG L N   
7459 C CA  . ARG D 230 ? 1.3363 1.7581 1.7638 0.0457  -0.2688 -0.3901 77   ARG L CA  
7460 C C   . ARG D 230 ? 1.2502 1.6506 1.7091 0.0342  -0.2510 -0.3815 77   ARG L C   
7461 O O   . ARG D 230 ? 1.2382 1.6097 1.6930 0.0225  -0.2273 -0.3626 77   ARG L O   
7462 C CB  . ARG D 230 ? 1.2538 1.6592 1.6679 0.0381  -0.2500 -0.3869 77   ARG L CB  
7463 C CG  . ARG D 230 ? 1.2509 1.6808 1.6677 0.0419  -0.2599 -0.4165 77   ARG L CG  
7464 C CD  . ARG D 230 ? 1.2881 1.6991 1.6987 0.0334  -0.2376 -0.4141 77   ARG L CD  
7465 N NE  . ARG D 230 ? 1.4472 1.8596 1.9109 0.0212  -0.2217 -0.4454 77   ARG L NE  
7466 C CZ  . ARG D 230 ? 1.3492 1.7509 1.8197 0.0139  -0.2031 -0.4527 77   ARG L CZ  
7467 N NH1 . ARG D 230 ? 1.2619 1.6651 1.7832 0.0029  -0.1886 -0.4818 77   ARG L NH1 
7468 N NH2 . ARG D 230 ? 1.3420 1.7315 1.7695 0.0176  -0.1982 -0.4308 77   ARG L NH2 
7469 N N   . VAL D 231 ? 1.2446 1.6603 1.7351 0.0370  -0.2623 -0.3948 78   VAL L N   
7470 C CA  . VAL D 231 ? 1.2472 1.6445 1.7696 0.0259  -0.2461 -0.3892 78   VAL L CA  
7471 C C   . VAL D 231 ? 1.2325 1.6182 1.7966 0.0091  -0.2225 -0.4070 78   VAL L C   
7472 O O   . VAL D 231 ? 1.3574 1.7614 1.9513 0.0076  -0.2255 -0.4388 78   VAL L O   
7473 C CB  . VAL D 231 ? 1.3072 1.7263 1.8594 0.0332  -0.2636 -0.4036 78   VAL L CB  
7474 C CG1 . VAL D 231 ? 1.1762 1.5766 1.7649 0.0205  -0.2456 -0.4010 78   VAL L CG1 
7475 C CG2 . VAL D 231 ? 1.3478 1.7764 1.8593 0.0500  -0.2852 -0.3825 78   VAL L CG2 
7476 N N   . GLU D 232 ? 1.1360 1.4918 1.7021 -0.0044 -0.1984 -0.3861 79   GLU L N   
7477 C CA  . GLU D 232 ? 1.1297 1.4715 1.7338 -0.0212 -0.1737 -0.3970 79   GLU L CA  
7478 C C   . GLU D 232 ? 1.1509 1.4891 1.8015 -0.0314 -0.1653 -0.4069 79   GLU L C   
7479 O O   . GLU D 232 ? 1.0699 1.4145 1.7221 -0.0254 -0.1773 -0.4037 79   GLU L O   
7480 C CB  . GLU D 232 ? 1.1543 1.4672 1.7284 -0.0305 -0.1517 -0.3654 79   GLU L CB  
7481 C CG  . GLU D 232 ? 1.1972 1.5112 1.7195 -0.0199 -0.1598 -0.3501 79   GLU L CG  
7482 C CD  . GLU D 232 ? 1.2831 1.5930 1.8139 -0.0256 -0.1454 -0.3598 79   GLU L CD  
7483 O OE1 . GLU D 232 ? 1.2838 1.6105 1.8010 -0.0158 -0.1586 -0.3750 79   GLU L OE1 
7484 O OE2 . GLU D 232 ? 1.1821 1.4724 1.7339 -0.0404 -0.1205 -0.3520 79   GLU L OE2 
7485 N N   . ALA D 233 ? 1.2320 1.5594 1.9219 -0.0470 -0.1437 -0.4187 80   ALA L N   
7486 C CA  . ALA D 233 ? 1.1527 1.4763 1.8891 -0.0582 -0.1339 -0.4296 80   ALA L CA  
7487 C C   . ALA D 233 ? 1.1576 1.4568 1.8771 -0.0670 -0.1202 -0.3970 80   ALA L C   
7488 O O   . ALA D 233 ? 1.1860 1.4844 1.9319 -0.0718 -0.1186 -0.4014 80   ALA L O   
7489 C CB  . ALA D 233 ? 1.0144 1.3339 1.7976 -0.0726 -0.1144 -0.4514 80   ALA L CB  
7490 N N   . GLU D 234 ? 1.2712 1.5509 1.9468 -0.0697 -0.1097 -0.3645 81   GLU L N   
7491 C CA  . GLU D 234 ? 1.2955 1.5525 1.9524 -0.0803 -0.0950 -0.3328 81   GLU L CA  
7492 C C   . GLU D 234 ? 1.3087 1.5688 1.9368 -0.0688 -0.1116 -0.3193 81   GLU L C   
7493 O O   . GLU D 234 ? 1.3382 1.5819 1.9588 -0.0779 -0.1005 -0.2991 81   GLU L O   
7494 C CB  . GLU D 234 ? 1.3260 1.5637 1.9448 -0.0871 -0.0788 -0.3019 81   GLU L CB  
7495 C CG  . GLU D 234 ? 1.3526 1.5945 1.9162 -0.0711 -0.0948 -0.2859 81   GLU L CG  
7496 C CD  . GLU D 234 ? 1.4663 1.6930 2.0001 -0.0769 -0.0793 -0.2617 81   GLU L CD  
7497 O OE1 . GLU D 234 ? 1.3839 1.6188 1.9148 -0.0701 -0.0833 -0.2732 81   GLU L OE1 
7498 O OE2 . GLU D 234 ? 1.5142 1.7215 2.0283 -0.0889 -0.0625 -0.2312 81   GLU L OE2 
7499 N N   . ASP D 235 ? 1.2136 1.4948 1.8266 -0.0498 -0.1371 -0.3300 82   ASP L N   
7500 C CA  . ASP D 235 ? 1.1340 1.4190 1.7170 -0.0369 -0.1538 -0.3149 82   ASP L CA  
7501 C C   . ASP D 235 ? 1.1841 1.4767 1.8048 -0.0365 -0.1588 -0.3287 82   ASP L C   
7502 O O   . ASP D 235 ? 1.1272 1.4228 1.7288 -0.0257 -0.1715 -0.3168 82   ASP L O   
7503 C CB  . ASP D 235 ? 1.1405 1.4479 1.6950 -0.0166 -0.1798 -0.3209 82   ASP L CB  
7504 C CG  . ASP D 235 ? 1.2899 1.5906 1.8067 -0.0159 -0.1755 -0.3083 82   ASP L CG  
7505 O OD1 . ASP D 235 ? 1.3133 1.5904 1.8183 -0.0295 -0.1533 -0.2879 82   ASP L OD1 
7506 O OD2 . ASP D 235 ? 1.2515 1.5716 1.7511 -0.0023 -0.1941 -0.3186 82   ASP L OD2 
7507 N N   . VAL D 236 ? 1.2178 1.5132 1.8921 -0.0478 -0.1486 -0.3529 83   VAL L N   
7508 C CA  . VAL D 236 ? 1.2049 1.5087 1.9184 -0.0475 -0.1531 -0.3676 83   VAL L CA  
7509 C C   . VAL D 236 ? 1.0892 1.3697 1.7884 -0.0562 -0.1392 -0.3412 83   VAL L C   
7510 O O   . VAL D 236 ? 1.1341 1.3906 1.8161 -0.0717 -0.1175 -0.3200 83   VAL L O   
7511 C CB  . VAL D 236 ? 1.1696 1.4797 1.9426 -0.0596 -0.1431 -0.3986 83   VAL L CB  
7512 C CG1 . VAL D 236 ? 1.1737 1.5125 1.9657 -0.0488 -0.1611 -0.4297 83   VAL L CG1 
7513 C CG2 . VAL D 236 ? 1.2024 1.4889 1.9796 -0.0798 -0.1153 -0.3888 83   VAL L CG2 
7514 N N   . GLY D 237 ? 1.1306 1.4188 1.8374 -0.0466 -0.1512 -0.3420 84   GLY L N   
7515 C CA  . GLY D 237 ? 1.1643 1.4316 1.8594 -0.0539 -0.1387 -0.3196 84   GLY L CA  
7516 C C   . GLY D 237 ? 1.0899 1.3679 1.7690 -0.0349 -0.1588 -0.3120 84   GLY L C   
7517 O O   . GLY D 237 ? 1.0565 1.3612 1.7453 -0.0174 -0.1824 -0.3282 84   GLY L O   
7518 N N   . VAL D 238 ? 1.0225 1.2798 1.6774 -0.0392 -0.1483 -0.2867 85   VAL L N   
7519 C CA  . VAL D 238 ? 1.0823 1.3447 1.7209 -0.0226 -0.1633 -0.2750 85   VAL L CA  
7520 C C   . VAL D 238 ? 1.0879 1.3358 1.6621 -0.0182 -0.1638 -0.2427 85   VAL L C   
7521 O O   . VAL D 238 ? 1.0207 1.2445 1.5687 -0.0345 -0.1431 -0.2231 85   VAL L O   
7522 C CB  . VAL D 238 ? 1.0858 1.3360 1.7539 -0.0309 -0.1501 -0.2744 85   VAL L CB  
7523 C CG1 . VAL D 238 ? 1.0364 1.3011 1.7077 -0.0101 -0.1697 -0.2725 85   VAL L CG1 
7524 C CG2 . VAL D 238 ? 1.0865 1.3416 1.8142 -0.0442 -0.1396 -0.3022 85   VAL L CG2 
7525 N N   . TYR D 239 ? 1.0842 1.3478 1.6329 0.0033  -0.1873 -0.2366 86   TYR L N   
7526 C CA  . TYR D 239 ? 1.0418 1.2945 1.5291 0.0101  -0.1908 -0.2071 86   TYR L CA  
7527 C C   . TYR D 239 ? 1.0697 1.3118 1.5422 0.0165  -0.1909 -0.1874 86   TYR L C   
7528 O O   . TYR D 239 ? 1.0596 1.3171 1.5614 0.0290  -0.2038 -0.1979 86   TYR L O   
7529 C CB  . TYR D 239 ? 1.0139 1.2912 1.4784 0.0293  -0.2166 -0.2122 86   TYR L CB  
7530 C CG  . TYR D 239 ? 1.0655 1.3459 1.5255 0.0222  -0.2129 -0.2223 86   TYR L CG  
7531 C CD1 . TYR D 239 ? 1.1591 1.4496 1.6677 0.0135  -0.2080 -0.2513 86   TYR L CD1 
7532 C CD2 . TYR D 239 ? 0.9924 1.2654 1.4005 0.0244  -0.2137 -0.2029 86   TYR L CD2 
7533 C CE1 . TYR D 239 ? 1.0698 1.3620 1.5763 0.0071  -0.2031 -0.2606 86   TYR L CE1 
7534 C CE2 . TYR D 239 ? 1.0680 1.3431 1.4738 0.0184  -0.2091 -0.2117 86   TYR L CE2 
7535 C CZ  . TYR D 239 ? 1.0242 1.3086 1.4798 0.0098  -0.2034 -0.2405 86   TYR L CZ  
7536 O OH  . TYR D 239 ? 1.0169 1.3023 1.4720 0.0038  -0.1973 -0.2492 86   TYR L OH  
7537 N N   . TYR D 240 ? 1.0597 1.2761 1.4874 0.0077  -0.1759 -0.1586 87   TYR L N   
7538 C CA  . TYR D 240 ? 0.8569 1.0587 1.2665 0.0112  -0.1719 -0.1381 87   TYR L CA  
7539 C C   . TYR D 240 ? 0.9123 1.1047 1.2570 0.0183  -0.1767 -0.1090 87   TYR L C   
7540 O O   . TYR D 240 ? 1.0967 1.2751 1.4080 0.0060  -0.1644 -0.0952 87   TYR L O   
7541 C CB  . TYR D 240 ? 0.8729 1.0485 1.2974 -0.0124 -0.1424 -0.1323 87   TYR L CB  
7542 C CG  . TYR D 240 ? 0.9388 1.1206 1.4268 -0.0217 -0.1347 -0.1595 87   TYR L CG  
7543 C CD1 . TYR D 240 ? 1.0447 1.2295 1.5686 -0.0160 -0.1361 -0.1678 87   TYR L CD1 
7544 C CD2 . TYR D 240 ? 1.0356 1.2197 1.5485 -0.0363 -0.1253 -0.1762 87   TYR L CD2 
7545 C CE1 . TYR D 240 ? 1.0727 1.2634 1.6548 -0.0247 -0.1288 -0.1927 87   TYR L CE1 
7546 C CE2 . TYR D 240 ? 1.0971 1.2868 1.6677 -0.0452 -0.1180 -0.2011 87   TYR L CE2 
7547 C CZ  . TYR D 240 ? 1.1241 1.3172 1.7285 -0.0394 -0.1201 -0.2095 87   TYR L CZ  
7548 O OH  . TYR D 240 ? 1.0489 1.2479 1.7111 -0.0483 -0.1129 -0.2345 87   TYR L OH  
7549 N N   . CYS D 241 ? 0.9608 1.1616 1.2886 0.0383  -0.1943 -0.0990 88   CYS L N   
7550 C CA  . CYS D 241 ? 1.0572 1.2447 1.3252 0.0439  -0.1957 -0.0690 88   CYS L CA  
7551 C C   . CYS D 241 ? 0.9386 1.0989 1.1991 0.0325  -0.1745 -0.0508 88   CYS L C   
7552 O O   . CYS D 241 ? 0.9745 1.1341 1.2756 0.0320  -0.1696 -0.0608 88   CYS L O   
7553 C CB  . CYS D 241 ? 1.0673 1.2780 1.3191 0.0710  -0.2254 -0.0660 88   CYS L CB  
7554 S SG  . CYS D 241 ? 1.3171 1.5509 1.6241 0.0885  -0.2419 -0.0835 88   CYS L SG  
7555 N N   . MET D 242 ? 0.9114 1.0495 1.1203 0.0227  -0.1612 -0.0244 89   MET L N   
7556 C CA  . MET D 242 ? 0.9734 1.0845 1.1702 0.0087  -0.1386 -0.0067 89   MET L CA  
7557 C C   . MET D 242 ? 0.9694 1.0690 1.1056 0.0166  -0.1419 0.0229  89   MET L C   
7558 O O   . MET D 242 ? 0.8438 0.9453 0.9374 0.0191  -0.1486 0.0349  89   MET L O   
7559 C CB  . MET D 242 ? 0.8349 0.9265 1.0352 -0.0213 -0.1096 -0.0050 89   MET L CB  
7560 C CG  . MET D 242 ? 0.9443 1.0105 1.1423 -0.0387 -0.0844 0.0075  89   MET L CG  
7561 S SD  . MET D 242 ? 1.0296 1.0731 1.2052 -0.0740 -0.0520 0.0217  89   MET L SD  
7562 C CE  . MET D 242 ? 0.9219 0.9615 1.0234 -0.0683 -0.0594 0.0512  89   MET L CE  
7563 N N   . GLN D 243 ? 0.9355 1.0228 1.0691 0.0204  -0.1366 0.0342  90   GLN L N   
7564 C CA  . GLN D 243 ? 0.9404 1.0125 1.0177 0.0246  -0.1352 0.0630  90   GLN L CA  
7565 C C   . GLN D 243 ? 1.0782 1.1252 1.1190 -0.0021 -0.1085 0.0808  90   GLN L C   
7566 O O   . GLN D 243 ? 1.0046 1.0377 1.0685 -0.0248 -0.0847 0.0753  90   GLN L O   
7567 C CB  . GLN D 243 ? 1.0506 1.1149 1.1406 0.0342  -0.1335 0.0692  90   GLN L CB  
7568 C CG  . GLN D 243 ? 1.1395 1.1882 1.1740 0.0402  -0.1325 0.0983  90   GLN L CG  
7569 C CD  . GLN D 243 ? 1.0962 1.1372 1.1483 0.0506  -0.1300 0.1036  90   GLN L CD  
7570 O OE1 . GLN D 243 ? 1.0364 1.0823 1.1426 0.0517  -0.1270 0.0860  90   GLN L OE1 
7571 N NE2 . GLN D 243 ? 1.2529 1.2817 1.2603 0.0584  -0.1308 0.1281  90   GLN L NE2 
7572 N N   . ALA D 244 ? 1.0611 1.1036 1.0448 0.0000  -0.1125 0.1024  91   ALA L N   
7573 C CA  . ALA D 244 ? 1.0162 1.0395 0.9624 -0.0244 -0.0899 0.1207  91   ALA L CA  
7574 C C   . ALA D 244 ? 1.0343 1.0321 0.9511 -0.0371 -0.0694 0.1422  91   ALA L C   
7575 O O   . ALA D 244 ? 1.1317 1.1138 1.0167 -0.0596 -0.0489 0.1585  91   ALA L O   
7576 C CB  . ALA D 244 ? 1.0632 1.0940 0.9624 -0.0173 -0.1026 0.1340  91   ALA L CB  
7577 N N   . LEU D 245 ? 1.0994 1.0931 1.0263 -0.0239 -0.0736 0.1431  92   LEU L N   
7578 C CA  . LEU D 245 ? 0.9663 0.9350 0.8702 -0.0358 -0.0527 0.1610  92   LEU L CA  
7579 C C   . LEU D 245 ? 0.9714 0.9328 0.9288 -0.0428 -0.0383 0.1447  92   LEU L C   
7580 O O   . LEU D 245 ? 1.1934 1.1696 1.2035 -0.0385 -0.0451 0.1206  92   LEU L O   
7581 C CB  . LEU D 245 ? 1.1041 1.0708 0.9665 -0.0144 -0.0676 0.1808  92   LEU L CB  
7582 C CG  . LEU D 245 ? 0.8999 0.8702 0.7038 -0.0106 -0.0781 0.1996  92   LEU L CG  
7583 C CD1 . LEU D 245 ? 1.0030 0.9688 0.7640 0.0081  -0.0900 0.2205  92   LEU L CD1 
7584 C CD2 . LEU D 245 ? 0.9831 0.9374 0.7560 -0.0406 -0.0531 0.2128  92   LEU L CD2 
7585 N N   . HIS D 246 ? 1.0895 1.0277 1.0330 -0.0537 -0.0178 0.1577  93   HIS L N   
7586 C CA  . HIS D 246 ? 1.1251 1.0491 1.1095 -0.0714 0.0064  0.1459  93   HIS L CA  
7587 C C   . HIS D 246 ? 1.2874 1.2260 1.3389 -0.0570 -0.0040 0.1202  93   HIS L C   
7588 O O   . HIS D 246 ? 1.3952 1.3350 1.4880 -0.0732 0.0085  0.1014  93   HIS L O   
7589 C CB  . HIS D 246 ? 1.1344 1.0334 1.0940 -0.0778 0.0252  0.1635  93   HIS L CB  
7590 C CG  . HIS D 246 ? 1.1953 1.0797 1.1987 -0.0939 0.0497  0.1504  93   HIS L CG  
7591 N ND1 . HIS D 246 ? 1.1471 1.0333 1.1946 -0.0760 0.0444  0.1396  93   HIS L ND1 
7592 C CD2 . HIS D 246 ? 1.1279 0.9973 1.1397 -0.1264 0.0796  0.1460  93   HIS L CD2 
7593 C CE1 . HIS D 246 ? 1.2058 1.0769 1.2867 -0.0967 0.0708  0.1286  93   HIS L CE1 
7594 N NE2 . HIS D 246 ? 1.1798 1.0406 1.2391 -0.1279 0.0924  0.1319  93   HIS L NE2 
7595 N N   . PRO D 247 ? 1.1550 1.1057 1.2207 -0.0275 -0.0260 0.1190  94   PRO L N   
7596 C CA  . PRO D 247 ? 1.1145 1.0759 1.2463 -0.0178 -0.0302 0.0965  94   PRO L CA  
7597 C C   . PRO D 247 ? 1.2738 1.2595 1.4465 -0.0157 -0.0439 0.0714  94   PRO L C   
7598 O O   . PRO D 247 ? 1.1000 1.0803 1.3043 -0.0369 -0.0257 0.0562  94   PRO L O   
7599 C CB  . PRO D 247 ? 1.1329 1.1052 1.2643 0.0142  -0.0531 0.1048  94   PRO L CB  
7600 C CG  . PRO D 247 ? 1.3110 1.2916 1.3863 0.0257  -0.0721 0.1219  94   PRO L CG  
7601 C CD  . PRO D 247 ? 1.1466 1.1052 1.1741 -0.0017 -0.0493 0.1364  94   PRO L CD  
7602 N N   . PHE D 248 ? 1.1603 1.1616 1.2687 -0.0303 -0.0558 0.0773  95   PHE L N   
7603 C CA  . PHE D 248 ? 1.0927 1.0974 1.2398 -0.0494 -0.0437 0.0572  95   PHE L CA  
7604 C C   . PHE D 248 ? 1.0725 1.0945 1.2853 -0.0374 -0.0544 0.0300  95   PHE L C   
7605 O O   . PHE D 248 ? 1.0850 1.1074 1.3391 -0.0531 -0.0418 0.0113  95   PHE L O   
7606 C CB  . PHE D 248 ? 0.9885 0.9677 1.1292 -0.0818 -0.0095 0.0648  95   PHE L CB  
7607 C CG  . PHE D 248 ? 1.0320 0.9965 1.1098 -0.0968 0.0024  0.0912  95   PHE L CG  
7608 C CD1 . PHE D 248 ? 1.0216 0.9618 1.0757 -0.1192 0.0294  0.1068  95   PHE L CD1 
7609 C CD2 . PHE D 248 ? 1.0197 0.9955 1.0626 -0.0892 -0.0129 0.1002  95   PHE L CD2 
7610 C CE1 . PHE D 248 ? 0.9084 0.8371 0.9046 -0.1337 0.0400  0.1315  95   PHE L CE1 
7611 C CE2 . PHE D 248 ? 1.1081 1.0717 1.0943 -0.1027 -0.0022 0.1253  95   PHE L CE2 
7612 C CZ  . PHE D 248 ? 0.9576 0.8982 0.9202 -0.1250 0.0240  0.1412  95   PHE L CZ  
7613 N N   . THR D 249 ? 1.0577 1.0950 1.2801 -0.0095 -0.0777 0.0284  96   THR L N   
7614 C CA  . THR D 249 ? 1.1133 1.1729 1.3960 0.0048  -0.0925 0.0033  96   THR L CA  
7615 C C   . THR D 249 ? 1.0097 1.0945 1.3050 0.0103  -0.1110 -0.0146 96   THR L C   
7616 O O   . THR D 249 ? 0.9745 1.0671 1.2299 0.0176  -0.1247 -0.0053 96   THR L O   
7617 C CB  . THR D 249 ? 1.0438 1.1150 1.3326 0.0330  -0.1124 0.0092  96   THR L CB  
7618 O OG1 . THR D 249 ? 1.1801 1.2547 1.4134 0.0475  -0.1287 0.0302  96   THR L OG1 
7619 C CG2 . THR D 249 ? 0.9327 0.9815 1.2351 0.0278  -0.0920 0.0173  96   THR L CG2 
7620 N N   . PHE D 250 ? 1.0186 1.1158 1.3702 0.0064  -0.1106 -0.0409 97   PHE L N   
7621 C CA  . PHE D 250 ? 0.9462 1.0670 1.3168 0.0100  -0.1259 -0.0612 97   PHE L CA  
7622 C C   . PHE D 250 ? 0.9383 1.0910 1.3387 0.0372  -0.1558 -0.0761 97   PHE L C   
7623 O O   . PHE D 250 ? 1.1170 1.2741 1.5390 0.0508  -0.1617 -0.0750 97   PHE L O   
7624 C CB  . PHE D 250 ? 1.0203 1.1362 1.4334 -0.0128 -0.1066 -0.0815 97   PHE L CB  
7625 C CG  . PHE D 250 ? 0.9133 1.0103 1.2956 -0.0379 -0.0853 -0.0705 97   PHE L CG  
7626 C CD1 . PHE D 250 ? 0.8994 0.9695 1.2701 -0.0612 -0.0568 -0.0573 97   PHE L CD1 
7627 C CD2 . PHE D 250 ? 0.9360 1.0433 1.3015 -0.0387 -0.0932 -0.0730 97   PHE L CD2 
7628 C CE1 . PHE D 250 ? 0.8666 0.9225 1.2092 -0.0848 -0.0377 -0.0456 97   PHE L CE1 
7629 C CE2 . PHE D 250 ? 0.8239 0.9155 1.1630 -0.0611 -0.0736 -0.0611 97   PHE L CE2 
7630 C CZ  . PHE D 250 ? 0.8360 0.9029 1.1635 -0.0842 -0.0464 -0.0467 97   PHE L CZ  
7631 N N   . GLY D 251 ? 1.0555 1.2313 1.4570 0.0446  -0.1742 -0.0896 98   GLY L N   
7632 C CA  . GLY D 251 ? 1.1372 1.3471 1.5627 0.0686  -0.2037 -0.1044 98   GLY L CA  
7633 C C   . GLY D 251 ? 1.2234 1.4495 1.7164 0.0701  -0.2058 -0.1306 98   GLY L C   
7634 O O   . GLY D 251 ? 1.3060 1.5540 1.8229 0.0900  -0.2248 -0.1350 98   GLY L O   
7635 N N   . GLY D 252 ? 1.1470 1.3637 1.6721 0.0494  -0.1868 -0.1474 99   GLY L N   
7636 C CA  . GLY D 252 ? 1.1808 1.4125 1.7710 0.0488  -0.1876 -0.1740 99   GLY L CA  
7637 C C   . GLY D 252 ? 1.0521 1.3004 1.6704 0.0411  -0.1912 -0.2008 99   GLY L C   
7638 O O   . GLY D 252 ? 0.9420 1.1965 1.6134 0.0341  -0.1852 -0.2230 99   GLY L O   
7639 N N   . GLY D 253 ? 0.9633 1.2186 1.5497 0.0420  -0.2000 -0.2001 100  GLY L N   
7640 C CA  . GLY D 253 ? 1.1059 1.3735 1.7181 0.0329  -0.2001 -0.2248 100  GLY L CA  
7641 C C   . GLY D 253 ? 1.1150 1.4196 1.7384 0.0521  -0.2295 -0.2429 100  GLY L C   
7642 O O   . GLY D 253 ? 1.1246 1.4521 1.7690 0.0700  -0.2486 -0.2483 100  GLY L O   
7643 N N   . THR D 254 ? 1.2074 1.5187 1.8168 0.0481  -0.2328 -0.2517 101  THR L N   
7644 C CA  . THR D 254 ? 1.1617 1.5080 1.7848 0.0614  -0.2573 -0.2736 101  THR L CA  
7645 C C   . THR D 254 ? 1.0520 1.3989 1.7016 0.0454  -0.2462 -0.2972 101  THR L C   
7646 O O   . THR D 254 ? 1.0380 1.3658 1.6604 0.0328  -0.2315 -0.2882 101  THR L O   
7647 C CB  . THR D 254 ? 1.1388 1.4950 1.7082 0.0762  -0.2757 -0.2581 101  THR L CB  
7648 O OG1 . THR D 254 ? 1.1910 1.5553 1.7453 0.0945  -0.2912 -0.2410 101  THR L OG1 
7649 C CG2 . THR D 254 ? 0.9621 1.3507 1.5427 0.0836  -0.2953 -0.2830 101  THR L CG2 
7650 N N   . LYS D 255 ? 1.0639 1.4327 1.7676 0.0458  -0.2525 -0.3266 102  LYS L N   
7651 C CA  . LYS D 255 ? 1.0358 1.4049 1.7717 0.0301  -0.2406 -0.3509 102  LYS L CA  
7652 C C   . LYS D 255 ? 1.1817 1.5746 1.9082 0.0371  -0.2570 -0.3670 102  LYS L C   
7653 O O   . LYS D 255 ? 1.3121 1.7358 2.0384 0.0545  -0.2824 -0.3755 102  LYS L O   
7654 C CB  . LYS D 255 ? 1.0283 1.4090 1.8278 0.0258  -0.2383 -0.3760 102  LYS L CB  
7655 C CG  . LYS D 255 ? 1.1161 1.4885 1.9500 0.0058  -0.2194 -0.3970 102  LYS L CG  
7656 C CD  . LYS D 255 ? 1.1350 1.4698 1.9470 -0.0141 -0.1908 -0.3762 102  LYS L CD  
7657 C CE  . LYS D 255 ? 1.1495 1.4770 1.9924 -0.0337 -0.1723 -0.3944 102  LYS L CE  
7658 N NZ  . LYS D 255 ? 1.1970 1.5399 2.0329 -0.0301 -0.1816 -0.4086 102  LYS L NZ  
7659 N N   . VAL D 256 ? 1.2418 1.6211 1.9610 0.0229  -0.2418 -0.3709 103  VAL L N   
7660 C CA  . VAL D 256 ? 1.1348 1.5329 1.8492 0.0261  -0.2521 -0.3885 103  VAL L CA  
7661 C C   . VAL D 256 ? 1.2083 1.6061 1.9702 0.0100  -0.2373 -0.4160 103  VAL L C   
7662 O O   . VAL D 256 ? 1.0702 1.4435 1.8488 -0.0069 -0.2136 -0.4114 103  VAL L O   
7663 C CB  . VAL D 256 ? 1.1268 1.5090 1.7837 0.0260  -0.2479 -0.3655 103  VAL L CB  
7664 C CG1 . VAL D 256 ? 1.0642 1.4480 1.6742 0.0424  -0.2635 -0.3391 103  VAL L CG1 
7665 C CG2 . VAL D 256 ? 1.2001 1.5469 1.8483 0.0061  -0.2182 -0.3487 103  VAL L CG2 
7666 N N   . GLU D 257 ? 1.3492 1.7750 2.1330 0.0147  -0.2510 -0.4447 104  GLU L N   
7667 C CA  . GLU D 257 ? 1.1426 1.5716 1.9752 0.0008  -0.2390 -0.4741 104  GLU L CA  
7668 C C   . GLU D 257 ? 1.0670 1.5238 1.9069 0.0057  -0.2529 -0.5013 104  GLU L C   
7669 O O   . GLU D 257 ? 1.1292 1.6156 1.9587 0.0213  -0.2779 -0.5079 104  GLU L O   
7670 C CB  . GLU D 257 ? 1.0200 1.4580 1.9047 -0.0015 -0.2392 -0.4901 104  GLU L CB  
7671 C CG  . GLU D 257 ? 1.0952 1.5616 1.9837 0.0176  -0.2653 -0.4914 104  GLU L CG  
7672 C CD  . GLU D 257 ? 1.2551 1.7209 2.1865 0.0153  -0.2611 -0.4961 104  GLU L CD  
7673 O OE1 . GLU D 257 ? 1.2595 1.7128 2.2288 -0.0009 -0.2420 -0.5099 104  GLU L OE1 
7674 O OE2 . GLU D 257 ? 1.2378 1.7157 2.1659 0.0297  -0.2761 -0.4855 104  GLU L OE2 
# 
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   ARG 1   18   ?    ?   ?   A . n 
A 1 2   SER 2   19   ?    ?   ?   A . n 
A 1 3   SER 3   20   ?    ?   ?   A . n 
A 1 4   ARG 4   21   ?    ?   ?   A . n 
A 1 5   GLY 5   22   ?    ?   ?   A . n 
A 1 6   ASP 6   23   ?    ?   ?   A . n 
A 1 7   THR 7   24   ?    ?   ?   A . n 
A 1 8   ARG 8   25   ?    ?   ?   A . n 
A 1 9   ASN 9   26   26   ASN ASN A . n 
A 1 10  LEU 10  27   27   LEU LEU A . n 
A 1 11  ASN 11  28   28   ASN ASN A . n 
A 1 12  GLU 12  29   29   GLU GLU A . n 
A 1 13  LEU 13  30   30   LEU LEU A . n 
A 1 14  LYS 14  31   31   LYS LYS A . n 
A 1 15  MET 15  32   32   MET MET A . n 
A 1 16  GLU 16  33   33   GLU GLU A . n 
A 1 17  CYS 17  34   34   CYS CYS A . n 
A 1 18  PRO 18  35   35   PRO PRO A . n 
A 1 19  HIS 19  36   36   HIS HIS A . n 
A 1 20  THR 20  37   37   THR THR A . n 
A 1 21  ILE 21  38   38   ILE ILE A . n 
A 1 22  GLY 22  39   39   GLY GLY A . n 
A 1 23  LEU 23  40   40   LEU LEU A . n 
A 1 24  GLY 24  41   41   GLY GLY A . n 
A 1 25  GLN 25  42   42   GLN GLN A . n 
A 1 26  GLY 26  43   43   GLY GLY A . n 
A 1 27  LEU 27  44   44   LEU LEU A . n 
A 1 28  VAL 28  45   45   VAL VAL A . n 
A 1 29  ILE 29  46   46   ILE ILE A . n 
A 1 30  GLY 30  47   47   GLY GLY A . n 
A 1 31  SER 31  48   48   SER SER A . n 
A 1 32  ILE 32  49   49   ILE ILE A . n 
A 1 33  GLU 33  50   50   GLU GLU A . n 
A 1 34  LEU 34  51   51   LEU LEU A . n 
A 1 35  PRO 35  52   52   PRO PRO A . n 
A 1 36  PRO 36  53   53   PRO PRO A . n 
A 1 37  VAL 37  54   54   VAL VAL A . n 
A 1 38  PRO 38  55   55   PRO PRO A . n 
A 1 39  LEU 39  56   56   LEU LEU A . n 
A 1 40  ILE 40  57   57   ILE ILE A . n 
A 1 41  GLN 41  58   58   GLN GLN A . n 
A 1 42  VAL 42  59   59   VAL VAL A . n 
A 1 43  GLU 43  60   60   GLU GLU A . n 
A 1 44  SER 44  61   61   SER SER A . n 
A 1 45  LEU 45  62   62   LEU LEU A . n 
A 1 46  LYS 46  63   63   LYS LYS A . n 
A 1 47  LEU 47  64   64   LEU LEU A . n 
A 1 48  GLU 48  65   65   GLU GLU A . n 
A 1 49  SER 49  66   66   SER SER A . n 
A 1 50  SER 50  67   67   SER SER A . n 
A 1 51  CYS 51  68   68   CYS CYS A . n 
A 1 52  ASN 52  69   69   ASN ASN A . n 
A 1 53  PHE 53  70   70   PHE PHE A . n 
A 1 54  ASP 54  71   71   ASP ASP A . n 
A 1 55  LEU 55  72   72   LEU LEU A . n 
A 1 56  HIS 56  73   73   HIS HIS A . n 
A 1 57  THR 57  74   74   THR THR A . n 
A 1 58  SER 58  75   75   SER SER A . n 
A 1 59  THR 59  76   76   THR THR A . n 
A 1 60  SER 60  77   77   SER SER A . n 
A 1 61  SER 61  78   78   SER SER A . n 
A 1 62  GLN 62  79   79   GLN GLN A . n 
A 1 63  GLN 63  80   80   GLN GLN A . n 
A 1 64  ALA 64  81   81   ALA ALA A . n 
A 1 65  PHE 65  82   82   PHE PHE A . n 
A 1 66  THR 66  83   83   THR THR A . n 
A 1 67  LYS 67  84   84   LYS LYS A . n 
A 1 68  TRP 68  85   85   TRP TRP A . n 
A 1 69  THR 69  86   86   THR THR A . n 
A 1 70  TRP 70  87   87   TRP TRP A . n 
A 1 71  GLU 71  88   88   GLU GLU A . n 
A 1 72  VAL 72  89   89   VAL VAL A . n 
A 1 73  LYS 73  90   90   LYS LYS A . n 
A 1 74  SER 74  91   91   SER SER A . n 
A 1 75  ASP 75  92   92   ASP ASP A . n 
A 1 76  LEU 76  93   93   LEU LEU A . n 
A 1 77  ALA 77  94   94   ALA ALA A . n 
A 1 78  GLU 78  95   95   GLU GLU A . n 
A 1 79  ASN 79  96   96   ASN ASN A . n 
A 1 80  THR 80  97   97   THR THR A . n 
A 1 81  GLN 81  98   98   GLN GLN A . n 
A 1 82  ALA 82  99   99   ALA ALA A . n 
A 1 83  SER 83  100  100  SER SER A . n 
A 1 84  SER 84  101  101  SER SER A . n 
A 1 85  THR 85  102  102  THR THR A . n 
A 1 86  SER 86  103  103  SER SER A . n 
A 1 87  PHE 87  104  104  PHE PHE A . n 
A 1 88  GLN 88  105  105  GLN GLN A . n 
A 1 89  THR 89  106  106  THR THR A . n 
A 1 90  LYS 90  107  107  LYS LYS A . n 
A 1 91  SER 91  108  108  SER SER A . n 
A 1 92  SER 92  109  109  SER SER A . n 
A 1 93  GLU 93  110  110  GLU GLU A . n 
A 1 94  VAL 94  111  111  VAL VAL A . n 
A 1 95  ASN 95  112  112  ASN ASN A . n 
A 1 96  LEU 96  113  113  LEU LEU A . n 
A 1 97  ARG 97  114  114  ARG ARG A . n 
A 1 98  GLY 98  115  115  GLY GLY A . n 
A 1 99  LEU 99  116  116  LEU LEU A . n 
A 1 100 CYS 100 117  117  CYS CYS A . n 
A 1 101 LEU 101 118  118  LEU LEU A . n 
A 1 102 VAL 102 119  119  VAL VAL A . n 
A 1 103 PRO 103 120  120  PRO PRO A . n 
A 1 104 PRO 104 121  121  PRO PRO A . n 
A 1 105 LEU 105 122  122  LEU LEU A . n 
A 1 106 VAL 106 123  123  VAL VAL A . n 
A 1 107 ILE 107 124  124  ILE ILE A . n 
A 1 108 GLU 108 125  125  GLU GLU A . n 
A 1 109 THR 109 126  126  THR THR A . n 
A 1 110 ALA 110 127  127  ALA ALA A . n 
A 1 111 ALA 111 128  128  ALA ALA A . n 
A 1 112 ARG 112 129  129  ARG ARG A . n 
A 1 113 THR 113 130  130  THR THR A . n 
A 1 114 ARG 114 131  131  ARG ARG A . n 
A 1 115 LYS 115 132  132  LYS LYS A . n 
A 1 116 THR 116 133  133  THR THR A . n 
A 1 117 ILE 117 134  134  ILE ILE A . n 
A 1 118 ALA 118 135  135  ALA ALA A . n 
A 1 119 CYS 119 136  136  CYS CYS A . n 
A 1 120 PHE 120 137  137  PHE PHE A . n 
A 1 121 ASP 121 138  138  ASP ASP A . n 
A 1 122 LEU 122 139  139  LEU LEU A . n 
A 1 123 SER 123 140  140  SER SER A . n 
A 1 124 CYS 124 141  141  CYS CYS A . n 
A 1 125 ASN 125 142  142  ASN ASN A . n 
A 1 126 GLN 126 143  143  GLN GLN A . n 
A 1 127 THR 127 144  144  THR THR A . n 
A 1 128 THR 128 145  145  THR THR A . n 
A 1 129 CYS 129 146  146  CYS CYS A . n 
A 1 130 GLN 130 147  147  GLN GLN A . n 
A 1 131 PRO 131 148  148  PRO PRO A . n 
A 1 132 THR 132 149  149  THR THR A . n 
A 1 133 VAL 133 150  150  VAL VAL A . n 
A 1 134 PHE 134 151  151  PHE PHE A . n 
A 1 135 LEU 135 152  152  LEU LEU A . n 
A 1 136 MET 136 153  153  MET MET A . n 
A 1 137 GLY 137 154  154  GLY GLY A . n 
A 1 138 PRO 138 155  155  PRO PRO A . n 
A 1 139 ILE 139 156  156  ILE ILE A . n 
A 1 140 GLN 140 157  157  GLN GLN A . n 
A 1 141 THR 141 158  158  THR THR A . n 
A 1 142 CYS 142 159  159  CYS CYS A . n 
A 1 143 ILE 143 160  160  ILE ILE A . n 
A 1 144 THR 144 161  161  THR THR A . n 
A 1 145 THR 145 162  162  THR THR A . n 
A 1 146 LYS 146 163  163  LYS LYS A . n 
A 1 147 SER 147 164  164  SER SER A . n 
A 1 148 CYS 148 165  165  CYS CYS A . n 
A 1 149 LEU 149 166  166  LEU LEU A . n 
A 1 150 LEU 150 167  167  LEU LEU A . n 
A 1 151 GLY 151 168  168  GLY GLY A . n 
A 1 152 LEU 152 169  169  LEU LEU A . n 
A 1 153 GLY 153 170  170  GLY GLY A . n 
A 1 154 ASP 154 171  171  ASP ASP A . n 
A 1 155 GLN 155 172  172  GLN GLN A . n 
A 1 156 ARG 156 173  173  ARG ARG A . n 
A 1 157 ILE 157 174  174  ILE ILE A . n 
A 1 158 GLN 158 175  175  GLN GLN A . n 
A 1 159 VAL 159 176  176  VAL VAL A . n 
A 1 160 ASN 160 177  177  ASN ASN A . n 
A 1 161 TYR 161 178  178  TYR TYR A . n 
A 1 162 GLU 162 179  179  GLU GLU A . n 
A 1 163 LYS 163 180  180  LYS LYS A . n 
A 1 164 THR 164 181  181  THR THR A . n 
A 1 165 TYR 165 182  182  TYR TYR A . n 
A 1 166 CYS 166 183  183  CYS CYS A . n 
A 1 167 VAL 167 184  184  VAL VAL A . n 
A 1 168 SER 168 185  185  SER SER A . n 
A 1 169 GLY 169 186  186  GLY GLY A . n 
A 1 170 GLN 170 187  187  GLN GLN A . n 
A 1 171 LEU 171 188  188  LEU LEU A . n 
A 1 172 ILE 172 189  189  ILE ILE A . n 
A 1 173 GLU 173 190  190  GLU GLU A . n 
A 1 174 GLY 174 191  191  GLY GLY A . n 
A 1 175 ILE 175 192  192  ILE ILE A . n 
A 1 176 CYS 176 193  193  CYS CYS A . n 
A 1 177 PHE 177 194  194  PHE PHE A . n 
A 1 178 ASN 178 195  195  ASN ASN A . n 
A 1 179 PRO 179 196  196  PRO PRO A . n 
A 1 180 VAL 180 197  197  VAL VAL A . n 
A 1 181 HIS 181 198  198  HIS HIS A . n 
A 1 182 THR 182 199  199  THR THR A . n 
A 1 183 MET 183 200  ?    ?   ?   A . n 
A 1 184 ALA 184 201  ?    ?   ?   A . n 
A 1 185 LEU 185 202  ?    ?   ?   A . n 
A 1 186 SER 186 203  ?    ?   ?   A . n 
A 1 187 GLN 187 204  204  GLN GLN A . n 
A 1 188 PRO 188 205  205  PRO PRO A . n 
A 1 189 SER 189 206  206  SER SER A . n 
A 1 190 HIS 190 207  207  HIS HIS A . n 
A 1 191 THR 191 208  208  THR THR A . n 
A 1 192 TYR 192 209  209  TYR TYR A . n 
A 1 193 ASP 193 210  210  ASP ASP A . n 
A 1 194 ILE 194 211  211  ILE ILE A . n 
A 1 195 VAL 195 212  212  VAL VAL A . n 
A 1 196 THR 196 213  213  THR THR A . n 
A 1 197 VAL 197 214  214  VAL VAL A . n 
A 1 198 MET 198 215  215  MET MET A . n 
A 1 199 VAL 199 216  216  VAL VAL A . n 
A 1 200 ARG 200 217  217  ARG ARG A . n 
A 1 201 CYS 201 218  218  CYS CYS A . n 
A 1 202 PHE 202 219  219  PHE PHE A . n 
A 1 203 LEU 203 220  220  LEU LEU A . n 
A 1 204 ILE 204 221  221  ILE ILE A . n 
A 1 205 VAL 205 222  222  VAL VAL A . n 
A 1 206 LYS 206 223  223  LYS LYS A . n 
A 1 207 LYS 207 224  224  LYS LYS A . n 
A 1 208 VAL 208 225  225  VAL VAL A . n 
A 1 209 THR 209 226  226  THR THR A . n 
A 1 210 THR 210 227  227  THR THR A . n 
A 1 211 GLY 211 228  228  GLY GLY A . n 
A 1 212 ASP 212 229  229  ASP ASP A . n 
A 1 213 SER 213 230  230  SER SER A . n 
A 1 214 MET 214 231  231  MET MET A . n 
A 1 215 LYS 215 232  232  LYS LYS A . n 
A 1 216 ILE 216 233  233  ILE ILE A . n 
A 1 217 GLU 217 234  234  GLU GLU A . n 
A 1 218 LYS 218 235  235  LYS LYS A . n 
A 1 219 SER 219 236  236  SER SER A . n 
A 1 220 PHE 220 237  237  PHE PHE A . n 
A 1 221 GLU 221 238  238  GLU GLU A . n 
A 1 222 THR 222 239  239  THR THR A . n 
A 1 223 LEU 223 240  240  LEU LEU A . n 
A 1 224 VAL 224 241  241  VAL VAL A . n 
A 1 225 GLN 225 242  242  GLN GLN A . n 
A 1 226 LYS 226 243  243  LYS LYS A . n 
A 1 227 THR 227 244  244  THR THR A . n 
A 1 228 GLY 228 245  245  GLY GLY A . n 
A 1 229 CYS 229 246  246  CYS CYS A . n 
A 1 230 THR 230 247  247  THR THR A . n 
A 1 231 ASP 231 248  248  ASP ASP A . n 
A 1 232 ASN 232 249  249  ASN ASN A . n 
A 1 233 GLY 233 250  250  GLY GLY A . n 
A 1 234 PHE 234 251  251  PHE PHE A . n 
A 1 235 GLN 235 252  252  GLN GLN A . n 
A 1 236 GLY 236 253  253  GLY GLY A . n 
A 1 237 TYR 237 254  254  TYR TYR A . n 
A 1 238 TYR 238 255  255  TYR TYR A . n 
A 1 239 VAL 239 256  256  VAL VAL A . n 
A 1 240 CYS 240 257  257  CYS CYS A . n 
A 1 241 LEU 241 258  258  LEU LEU A . n 
A 1 242 ILE 242 259  259  ILE ILE A . n 
A 1 243 GLY 243 260  260  GLY GLY A . n 
A 1 244 SER 244 261  261  SER SER A . n 
A 1 245 SER 245 262  262  SER SER A . n 
A 1 246 SER 246 263  263  SER SER A . n 
A 1 247 GLU 247 264  264  GLU GLU A . n 
A 1 248 PRO 248 265  265  PRO PRO A . n 
A 1 249 LEU 249 266  266  LEU LEU A . n 
A 1 250 TYR 250 267  267  TYR TYR A . n 
A 1 251 ILE 251 268  268  ILE ILE A . n 
A 1 252 PRO 252 269  269  PRO PRO A . n 
A 1 253 THR 253 270  270  THR THR A . n 
A 1 254 LEU 254 271  271  LEU LEU A . n 
A 1 255 ASP 255 272  272  ASP ASP A . n 
A 1 256 ASP 256 273  273  ASP ASP A . n 
A 1 257 TYR 257 274  274  TYR TYR A . n 
A 1 258 ARG 258 275  275  ARG ARG A . n 
A 1 259 SER 259 276  276  SER SER A . n 
A 1 260 ALA 260 277  277  ALA ALA A . n 
A 1 261 GLU 261 278  278  GLU GLU A . n 
A 1 262 VAL 262 279  279  VAL VAL A . n 
A 1 263 LEU 263 280  280  LEU LEU A . n 
A 1 264 SER 264 281  281  SER SER A . n 
A 1 265 ARG 265 282  282  ARG ARG A . n 
A 1 266 MET 266 283  283  MET MET A . n 
A 1 267 ALA 267 284  284  ALA ALA A . n 
A 1 268 PHE 268 285  285  PHE PHE A . n 
A 1 269 ALA 269 286  286  ALA ALA A . n 
A 1 270 PRO 270 287  287  PRO PRO A . n 
A 1 271 HIS 271 288  288  HIS HIS A . n 
A 1 272 GLY 272 289  289  GLY GLY A . n 
A 1 273 GLU 273 290  290  GLU GLU A . n 
A 1 274 ASP 274 291  291  ASP ASP A . n 
A 1 275 HIS 275 292  292  HIS HIS A . n 
A 1 276 ASP 276 293  293  ASP ASP A . n 
A 1 277 ILE 277 294  294  ILE ILE A . n 
A 1 278 GLU 278 295  295  GLU GLU A . n 
A 1 279 LYS 279 296  296  LYS LYS A . n 
A 1 280 ASN 280 297  297  ASN ASN A . n 
A 1 281 ALA 281 298  298  ALA ALA A . n 
A 1 282 ILE 282 299  299  ILE ILE A . n 
A 1 283 SER 283 300  300  SER SER A . n 
A 1 284 ALA 284 301  301  ALA ALA A . n 
A 1 285 MET 285 302  302  MET MET A . n 
A 1 286 ARG 286 303  303  ARG ARG A . n 
A 1 287 ILE 287 304  304  ILE ILE A . n 
A 1 288 VAL 288 305  305  VAL VAL A . n 
A 1 289 GLY 289 306  306  GLY GLY A . n 
A 1 290 LYS 290 307  307  LYS LYS A . n 
A 1 291 VAL 291 308  308  VAL VAL A . n 
A 1 292 THR 292 309  309  THR THR A . n 
A 1 293 GLY 293 310  310  GLY GLY A . n 
A 1 294 LYS 294 311  311  LYS LYS A . n 
A 1 295 ALA 295 312  312  ALA ALA A . n 
A 1 296 PRO 296 313  313  PRO PRO A . n 
A 1 297 SER 297 314  314  SER SER A . n 
A 1 298 THR 298 315  315  THR THR A . n 
A 1 299 GLU 299 316  316  GLU GLU A . n 
A 1 300 SER 300 317  317  SER SER A . n 
A 1 301 SER 301 318  318  SER SER A . n 
A 1 302 ASP 302 319  319  ASP ASP A . n 
A 1 303 THR 303 320  320  THR THR A . n 
A 1 304 VAL 304 321  321  VAL VAL A . n 
A 1 305 GLN 305 322  322  GLN GLN A . n 
A 1 306 GLY 306 323  323  GLY GLY A . n 
A 1 307 ILE 307 324  324  ILE ILE A . n 
A 1 308 ALA 308 325  325  ALA ALA A . n 
A 1 309 PHE 309 326  326  PHE PHE A . n 
A 1 310 SER 310 327  327  SER SER A . n 
A 1 311 GLY 311 328  328  GLY GLY A . n 
A 1 312 ASN 312 329  329  ASN ASN A . n 
A 1 313 PRO 313 330  330  PRO PRO A . n 
A 1 314 LEU 314 331  331  LEU LEU A . n 
A 1 315 TYR 315 332  332  TYR TYR A . n 
A 1 316 THR 316 333  333  THR THR A . n 
A 1 317 SER 317 334  334  SER SER A . n 
A 1 318 THR 318 335  335  THR THR A . n 
A 1 319 GLY 319 336  336  GLY GLY A . n 
A 1 320 VAL 320 337  337  VAL VAL A . n 
A 1 321 LEU 321 338  338  LEU LEU A . n 
A 1 322 THR 322 339  339  THR THR A . n 
A 1 323 ALA 323 340  340  ALA ALA A . n 
A 1 324 LYS 324 341  341  LYS LYS A . n 
A 1 325 ASP 325 342  342  ASP ASP A . n 
A 1 326 ASP 326 343  343  ASP ASP A . n 
A 1 327 PRO 327 344  344  PRO PRO A . n 
A 1 328 VAL 328 345  345  VAL VAL A . n 
A 1 329 TYR 329 346  346  TYR TYR A . n 
A 1 330 VAL 330 347  347  VAL VAL A . n 
A 1 331 TRP 331 348  348  TRP TRP A . n 
A 1 332 ALA 332 349  349  ALA ALA A . n 
A 1 333 PRO 333 350  350  PRO PRO A . n 
A 1 334 GLY 334 351  351  GLY GLY A . n 
A 1 335 ILE 335 352  352  ILE ILE A . n 
A 1 336 MET 336 353  353  MET MET A . n 
A 1 337 MET 337 354  354  MET MET A . n 
A 1 338 GLU 338 355  355  GLU GLU A . n 
A 1 339 GLY 339 356  356  GLY GLY A . n 
A 1 340 ASN 340 357  357  ASN ASN A . n 
A 1 341 HIS 341 358  358  HIS HIS A . n 
A 1 342 SER 342 359  359  SER SER A . n 
A 1 343 VAL 343 360  360  VAL VAL A . n 
A 1 344 CYS 344 361  361  CYS CYS A . n 
A 1 345 ASP 345 362  362  ASP ASP A . n 
A 1 346 LYS 346 363  363  LYS LYS A . n 
A 1 347 LYS 347 364  364  LYS LYS A . n 
A 1 348 THR 348 365  365  THR THR A . n 
A 1 349 LEU 349 366  366  LEU LEU A . n 
A 1 350 PRO 350 367  367  PRO PRO A . n 
A 1 351 LEU 351 368  368  LEU LEU A . n 
A 1 352 THR 352 369  369  THR THR A . n 
A 1 353 TRP 353 370  370  TRP TRP A . n 
A 1 354 THR 354 371  371  THR THR A . n 
A 1 355 GLY 355 372  372  GLY GLY A . n 
A 1 356 PHE 356 373  373  PHE PHE A . n 
A 1 357 ILE 357 374  374  ILE ILE A . n 
A 1 358 PRO 358 375  375  PRO PRO A . n 
A 1 359 LEU 359 376  376  LEU LEU A . n 
A 1 360 PRO 360 377  377  PRO PRO A . n 
A 1 361 GLY 361 378  378  GLY GLY A . n 
A 1 362 GLU 362 379  379  GLU GLU A . n 
A 1 363 ILE 363 380  380  ILE ILE A . n 
A 1 364 GLU 364 381  381  GLU GLU A . n 
A 1 365 GLY 365 382  ?    ?   ?   A . n 
A 1 366 GLY 366 383  ?    ?   ?   A . n 
A 1 367 SER 367 384  ?    ?   ?   A . n 
A 1 368 GLY 368 385  ?    ?   ?   A . n 
A 1 369 LEU 369 386  ?    ?   ?   A . n 
A 1 370 VAL 370 387  ?    ?   ?   A . n 
A 1 371 PRO 371 388  ?    ?   ?   A . n 
A 1 372 ARG 372 389  ?    ?   ?   A . n 
A 1 373 GLY 373 390  ?    ?   ?   A . n 
A 1 374 SER 374 391  ?    ?   ?   A . n 
A 1 375 GLY 375 392  ?    ?   ?   A . n 
A 1 376 GLY 376 393  ?    ?   ?   A . n 
A 1 377 GLY 377 394  ?    ?   ?   A . n 
A 1 378 SER 378 395  ?    ?   ?   A . n 
A 1 379 GLY 379 396  ?    ?   ?   A . n 
A 1 380 GLY 380 397  ?    ?   ?   A . n 
A 1 381 GLY 381 398  ?    ?   ?   A . n 
A 1 382 SER 382 399  ?    ?   ?   A . n 
A 1 383 TRP 383 400  ?    ?   ?   A . n 
A 1 384 SER 384 401  ?    ?   ?   A . n 
A 1 385 HIS 385 402  ?    ?   ?   A . n 
A 1 386 PRO 386 403  ?    ?   ?   A . n 
A 1 387 GLN 387 404  ?    ?   ?   A . n 
A 1 388 PHE 388 405  ?    ?   ?   A . n 
A 1 389 GLU 389 406  ?    ?   ?   A . n 
A 1 390 LYS 390 407  ?    ?   ?   A . n 
A 1 391 GLY 391 408  ?    ?   ?   A . n 
A 1 392 GLY 392 409  ?    ?   ?   A . n 
A 1 393 GLY 393 410  ?    ?   ?   A . n 
A 1 394 THR 394 411  ?    ?   ?   A . n 
A 1 395 GLY 395 412  ?    ?   ?   A . n 
A 1 396 GLY 396 413  ?    ?   ?   A . n 
A 1 397 GLY 397 414  ?    ?   ?   A . n 
A 1 398 THR 398 415  ?    ?   ?   A . n 
A 1 399 LEU 399 416  ?    ?   ?   A . n 
A 1 400 VAL 400 417  ?    ?   ?   A . n 
A 1 401 PRO 401 418  ?    ?   ?   A . n 
A 1 402 ARG 402 419  ?    ?   ?   A . n 
A 1 403 GLY 403 420  ?    ?   ?   A . n 
A 1 404 SER 404 421  ?    ?   ?   A . n 
A 1 405 GLY 405 422  ?    ?   ?   A . n 
A 1 406 THR 406 423  ?    ?   ?   A . n 
A 1 407 GLY 407 424  ?    ?   ?   A . n 
A 1 408 GLY 408 425  ?    ?   ?   A . n 
A 1 409 GLU 409 426  ?    ?   ?   A . n 
A 1 410 THR 410 427  ?    ?   ?   A . n 
A 1 411 GLN 411 428  ?    ?   ?   A . n 
A 1 412 ASN 412 429  ?    ?   ?   A . n 
A 1 413 LEU 413 430  ?    ?   ?   A . n 
A 1 414 ASN 414 431  ?    ?   ?   A . n 
A 1 415 SER 415 432  ?    ?   ?   A . n 
A 1 416 GLY 416 433  ?    ?   ?   A . n 
A 1 417 TRP 417 434  ?    ?   ?   A . n 
A 1 418 THR 418 435  ?    ?   ?   A . n 
A 1 419 ASP 419 436  ?    ?   ?   A . n 
A 1 420 THR 420 437  ?    ?   ?   A . n 
A 1 421 ALA 421 438  ?    ?   ?   A . n 
A 1 422 HIS 422 439  ?    ?   ?   A . n 
A 1 423 GLY 423 440  ?    ?   ?   A . n 
A 1 424 SER 424 441  ?    ?   ?   A . n 
A 1 425 GLY 425 442  ?    ?   ?   A . n 
A 1 426 VAL 426 443  ?    ?   ?   A . n 
A 1 427 ILE 427 444  ?    ?   ?   A . n 
A 1 428 PRO 428 445  ?    ?   ?   A . n 
A 1 429 MET 429 446  ?    ?   ?   A . n 
A 1 430 ARG 430 447  ?    ?   ?   A . n 
A 1 431 THR 431 448  ?    ?   ?   A . n 
A 1 432 ASP 432 449  ?    ?   ?   A . n 
A 1 433 LEU 433 450  ?    ?   ?   A . n 
A 1 434 GLU 434 451  ?    ?   ?   A . n 
A 1 435 LEU 435 452  ?    ?   ?   A . n 
A 1 436 ASP 436 453  ?    ?   ?   A . n 
A 1 437 PHE 437 454  ?    ?   ?   A . n 
A 1 438 SER 438 455  ?    ?   ?   A . n 
A 1 439 LEU 439 456  ?    ?   ?   A . n 
A 1 440 PRO 440 457  ?    ?   ?   A . n 
A 1 441 SER 441 458  ?    ?   ?   A . n 
A 1 442 SER 442 459  ?    ?   ?   A . n 
A 1 443 ALA 443 460  ?    ?   ?   A . n 
A 1 444 SER 444 461  ?    ?   ?   A . n 
A 1 445 TYR 445 462  ?    ?   ?   A . n 
A 1 446 THR 446 463  ?    ?   ?   A . n 
A 1 447 TYR 447 464  ?    ?   ?   A . n 
A 1 448 ARG 448 465  ?    ?   ?   A . n 
A 1 449 ARG 449 466  ?    ?   ?   A . n 
A 1 450 GLN 450 467  ?    ?   ?   A . n 
A 1 451 LEU 451 468  ?    ?   ?   A . n 
A 1 452 GLN 452 469  ?    ?   ?   A . n 
A 1 453 ASN 453 470  ?    ?   ?   A . n 
A 1 454 PRO 454 471  ?    ?   ?   A . n 
A 1 455 ALA 455 472  ?    ?   ?   A . n 
A 1 456 ASN 456 473  ?    ?   ?   A . n 
A 1 457 GLU 457 474  ?    ?   ?   A . n 
A 1 458 GLN 458 475  ?    ?   ?   A . n 
A 1 459 GLU 459 476  ?    ?   ?   A . n 
A 1 460 LYS 460 477  ?    ?   ?   A . n 
A 1 461 ILE 461 478  ?    ?   ?   A . n 
A 1 462 PRO 462 479  ?    ?   ?   A . n 
A 1 463 PHE 463 480  ?    ?   ?   A . n 
A 1 464 HIS 464 481  ?    ?   ?   A . n 
A 1 465 LEU 465 482  ?    ?   ?   A . n 
A 1 466 GLN 466 483  ?    ?   ?   A . n 
A 1 467 ILE 467 484  ?    ?   ?   A . n 
A 1 468 SER 468 485  ?    ?   ?   A . n 
A 1 469 LYS 469 486  ?    ?   ?   A . n 
A 1 470 GLN 470 487  ?    ?   ?   A . n 
A 1 471 VAL 471 488  ?    ?   ?   A . n 
A 1 472 ILE 472 489  ?    ?   ?   A . n 
A 1 473 HIS 473 490  ?    ?   ?   A . n 
A 1 474 ALA 474 491  ?    ?   ?   A . n 
A 1 475 GLU 475 492  ?    ?   ?   A . n 
A 1 476 ILE 476 493  ?    ?   ?   A . n 
A 1 477 GLN 477 494  ?    ?   ?   A . n 
A 1 478 HIS 478 495  ?    ?   ?   A . n 
A 1 479 LEU 479 496  ?    ?   ?   A . n 
A 1 480 GLY 480 497  ?    ?   ?   A . n 
A 1 481 HIS 481 498  ?    ?   ?   A . n 
A 1 482 TRP 482 499  ?    ?   ?   A . n 
A 1 483 MET 483 500  ?    ?   ?   A . n 
A 1 484 ASP 484 501  ?    ?   ?   A . n 
A 1 485 GLY 485 502  ?    ?   ?   A . n 
A 1 486 THR 486 503  ?    ?   ?   A . n 
A 1 487 PHE 487 504  ?    ?   ?   A . n 
A 1 488 ASN 488 505  ?    ?   ?   A . n 
A 1 489 LEU 489 506  ?    ?   ?   A . n 
A 1 490 LYS 490 507  ?    ?   ?   A . n 
A 1 491 THR 491 508  ?    ?   ?   A . n 
A 1 492 ALA 492 509  ?    ?   ?   A . n 
A 1 493 PHE 493 510  ?    ?   ?   A . n 
A 1 494 HIS 494 511  ?    ?   ?   A . n 
A 1 495 CYS 495 512  ?    ?   ?   A . n 
A 1 496 TYR 496 513  ?    ?   ?   A . n 
A 1 497 GLY 497 514  ?    ?   ?   A . n 
A 1 498 SER 498 515  ?    ?   ?   A . n 
A 1 499 CYS 499 516  ?    ?   ?   A . n 
A 1 500 GLU 500 517  ?    ?   ?   A . n 
A 1 501 LYS 501 518  ?    ?   ?   A . n 
A 1 502 TYR 502 519  ?    ?   ?   A . n 
A 1 503 ALA 503 520  ?    ?   ?   A . n 
A 1 504 TYR 504 521  ?    ?   ?   A . n 
A 1 505 PRO 505 522  ?    ?   ?   A . n 
A 1 506 TRP 506 523  ?    ?   ?   A . n 
A 1 507 GLN 507 524  ?    ?   ?   A . n 
A 1 508 THR 508 525  ?    ?   ?   A . n 
A 1 509 ALA 509 526  ?    ?   ?   A . n 
A 1 510 GLY 510 527  ?    ?   ?   A . n 
A 1 511 CYS 511 528  ?    ?   ?   A . n 
A 1 512 PHE 512 529  ?    ?   ?   A . n 
A 1 513 VAL 513 530  ?    ?   ?   A . n 
A 1 514 GLU 514 531  ?    ?   ?   A . n 
A 1 515 LYS 515 532  ?    ?   ?   A . n 
A 1 516 ASP 516 533  ?    ?   ?   A . n 
A 1 517 TYR 517 534  ?    ?   ?   A . n 
A 1 518 GLU 518 535  ?    ?   ?   A . n 
A 1 519 TYR 519 536  ?    ?   ?   A . n 
A 1 520 GLU 520 537  ?    ?   ?   A . n 
A 1 521 SER 521 538  ?    ?   ?   A . n 
A 1 522 GLY 522 539  ?    ?   ?   A . n 
A 1 523 TRP 523 540  ?    ?   ?   A . n 
A 1 524 GLY 524 541  ?    ?   ?   A . n 
A 1 525 CYS 525 542  ?    ?   ?   A . n 
A 1 526 ASN 526 543  ?    ?   ?   A . n 
A 1 527 PRO 527 544  ?    ?   ?   A . n 
A 1 528 ALA 528 545  ?    ?   ?   A . n 
A 1 529 ASP 529 546  ?    ?   ?   A . n 
A 1 530 CYS 530 547  ?    ?   ?   A . n 
A 1 531 PRO 531 548  ?    ?   ?   A . n 
A 1 532 GLY 532 549  ?    ?   ?   A . n 
A 1 533 VAL 533 550  ?    ?   ?   A . n 
A 1 534 GLY 534 551  ?    ?   ?   A . n 
A 1 535 THR 535 552  ?    ?   ?   A . n 
A 1 536 GLY 536 553  ?    ?   ?   A . n 
A 1 537 CYS 537 554  ?    ?   ?   A . n 
A 1 538 THR 538 555  ?    ?   ?   A . n 
A 1 539 ALA 539 556  ?    ?   ?   A . n 
A 1 540 CYS 540 557  ?    ?   ?   A . n 
A 1 541 GLY 541 558  ?    ?   ?   A . n 
A 1 542 VAL 542 559  ?    ?   ?   A . n 
A 1 543 TYR 543 560  ?    ?   ?   A . n 
A 1 544 LEU 544 561  ?    ?   ?   A . n 
A 1 545 ASP 545 562  ?    ?   ?   A . n 
A 1 546 LYS 546 563  ?    ?   ?   A . n 
A 1 547 LEU 547 564  ?    ?   ?   A . n 
A 1 548 LYS 548 565  ?    ?   ?   A . n 
A 1 549 SER 549 566  ?    ?   ?   A . n 
A 1 550 VAL 550 567  ?    ?   ?   A . n 
A 1 551 GLY 551 568  ?    ?   ?   A . n 
A 1 552 LYS 552 569  ?    ?   ?   A . n 
A 1 553 ALA 553 570  ?    ?   ?   A . n 
A 1 554 PHE 554 571  ?    ?   ?   A . n 
A 1 555 LYS 555 572  ?    ?   ?   A . n 
A 1 556 ILE 556 573  ?    ?   ?   A . n 
A 1 557 VAL 557 574  ?    ?   ?   A . n 
A 1 558 SER 558 575  ?    ?   ?   A . n 
A 1 559 LEU 559 576  ?    ?   ?   A . n 
A 1 560 ARG 560 577  ?    ?   ?   A . n 
A 1 561 TYR 561 578  ?    ?   ?   A . n 
A 1 562 THR 562 579  ?    ?   ?   A . n 
A 1 563 ARG 563 580  ?    ?   ?   A . n 
A 1 564 LYS 564 581  ?    ?   ?   A . n 
A 1 565 ALA 565 582  ?    ?   ?   A . n 
A 1 566 CYS 566 583  ?    ?   ?   A . n 
A 1 567 ILE 567 584  ?    ?   ?   A . n 
A 1 568 GLN 568 585  ?    ?   ?   A . n 
A 1 569 LEU 569 586  ?    ?   ?   A . n 
A 1 570 GLY 570 587  ?    ?   ?   A . n 
A 1 571 THR 571 588  ?    ?   ?   A . n 
A 1 572 GLU 572 589  ?    ?   ?   A . n 
A 1 573 GLN 573 590  ?    ?   ?   A . n 
A 1 574 THR 574 591  ?    ?   ?   A . n 
A 1 575 CYS 575 592  ?    ?   ?   A . n 
A 1 576 LYS 576 593  ?    ?   ?   A . n 
A 1 577 ASN 577 594  ?    ?   ?   A . n 
A 1 578 VAL 578 595  ?    ?   ?   A . n 
A 1 579 ASP 579 596  ?    ?   ?   A . n 
A 1 580 SER 580 597  ?    ?   ?   A . n 
A 1 581 ASN 581 598  ?    ?   ?   A . n 
A 1 582 ASP 582 599  ?    ?   ?   A . n 
A 1 583 CYS 583 600  ?    ?   ?   A . n 
A 1 584 LEU 584 601  ?    ?   ?   A . n 
A 1 585 VAL 585 602  ?    ?   ?   A . n 
A 1 586 THR 586 603  ?    ?   ?   A . n 
A 1 587 THR 587 604  ?    ?   ?   A . n 
A 1 588 SER 588 605  ?    ?   ?   A . n 
A 1 589 VAL 589 606  ?    ?   ?   A . n 
A 1 590 LYS 590 607  ?    ?   ?   A . n 
A 1 591 VAL 591 608  ?    ?   ?   A . n 
A 1 592 CYS 592 609  ?    ?   ?   A . n 
A 1 593 LEU 593 610  ?    ?   ?   A . n 
A 1 594 ILE 594 611  ?    ?   ?   A . n 
A 1 595 GLY 595 612  ?    ?   ?   A . n 
A 1 596 THR 596 613  ?    ?   ?   A . n 
A 1 597 VAL 597 614  ?    ?   ?   A . n 
A 1 598 SER 598 615  ?    ?   ?   A . n 
A 1 599 LYS 599 616  ?    ?   ?   A . n 
A 1 600 PHE 600 617  ?    ?   ?   A . n 
A 1 601 GLN 601 618  ?    ?   ?   A . n 
A 1 602 PRO 602 619  ?    ?   ?   A . n 
A 1 603 SER 603 620  ?    ?   ?   A . n 
A 1 604 ASP 604 621  ?    ?   ?   A . n 
A 1 605 THR 605 622  ?    ?   ?   A . n 
A 1 606 LEU 606 623  ?    ?   ?   A . n 
A 1 607 LEU 607 624  ?    ?   ?   A . n 
A 1 608 PHE 608 625  ?    ?   ?   A . n 
A 1 609 LEU 609 626  ?    ?   ?   A . n 
A 1 610 GLY 610 627  ?    ?   ?   A . n 
A 1 611 PRO 611 628  ?    ?   ?   A . n 
A 1 612 LEU 612 629  ?    ?   ?   A . n 
A 1 613 GLU 613 630  ?    ?   ?   A . n 
A 1 614 GLN 614 631  ?    ?   ?   A . n 
A 1 615 GLY 615 632  ?    ?   ?   A . n 
A 1 616 GLY 616 633  ?    ?   ?   A . n 
A 1 617 LEU 617 634  ?    ?   ?   A . n 
A 1 618 ILE 618 635  ?    ?   ?   A . n 
A 1 619 PHE 619 636  ?    ?   ?   A . n 
A 1 620 LYS 620 637  ?    ?   ?   A . n 
A 1 621 GLN 621 638  ?    ?   ?   A . n 
A 1 622 TRP 622 639  ?    ?   ?   A . n 
A 1 623 CYS 623 640  ?    ?   ?   A . n 
A 1 624 THR 624 641  ?    ?   ?   A . n 
A 1 625 THR 625 642  ?    ?   ?   A . n 
A 1 626 THR 626 643  ?    ?   ?   A . n 
A 1 627 CYS 627 644  ?    ?   ?   A . n 
A 1 628 GLN 628 645  ?    ?   ?   A . n 
A 1 629 PHE 629 646  ?    ?   ?   A . n 
A 1 630 GLY 630 647  ?    ?   ?   A . n 
A 1 631 ASP 631 648  ?    ?   ?   A . n 
A 1 632 PRO 632 649  ?    ?   ?   A . n 
A 1 633 GLY 633 650  ?    ?   ?   A . n 
A 1 634 ASP 634 651  ?    ?   ?   A . n 
A 1 635 ILE 635 652  ?    ?   ?   A . n 
A 1 636 MET 636 653  ?    ?   ?   A . n 
A 1 637 SER 637 654  ?    ?   ?   A . n 
A 1 638 THR 638 655  ?    ?   ?   A . n 
A 1 639 PRO 639 656  ?    ?   ?   A . n 
A 1 640 VAL 640 657  ?    ?   ?   A . n 
A 1 641 GLY 641 658  ?    ?   ?   A . n 
A 1 642 MET 642 659  ?    ?   ?   A . n 
A 1 643 LYS 643 660  ?    ?   ?   A . n 
A 1 644 CYS 644 661  ?    ?   ?   A . n 
A 1 645 PRO 645 662  ?    ?   ?   A . n 
A 1 646 GLU 646 663  ?    ?   ?   A . n 
A 1 647 LEU 647 664  ?    ?   ?   A . n 
A 1 648 SER 648 665  ?    ?   ?   A . n 
A 1 649 GLY 649 666  ?    ?   ?   A . n 
A 1 650 SER 650 667  ?    ?   ?   A . n 
A 1 651 PHE 651 668  ?    ?   ?   A . n 
A 1 652 ARG 652 669  ?    ?   ?   A . n 
A 1 653 LYS 653 670  ?    ?   ?   A . n 
A 1 654 LYS 654 671  ?    ?   ?   A . n 
A 1 655 CYS 655 672  ?    ?   ?   A . n 
A 1 656 ALA 656 673  ?    ?   ?   A . n 
A 1 657 PHE 657 674  ?    ?   ?   A . n 
A 1 658 ALA 658 675  ?    ?   ?   A . n 
A 1 659 THR 659 676  ?    ?   ?   A . n 
A 1 660 THR 660 677  ?    ?   ?   A . n 
A 1 661 PRO 661 678  ?    ?   ?   A . n 
A 1 662 VAL 662 679  ?    ?   ?   A . n 
A 1 663 CYS 663 680  ?    ?   ?   A . n 
A 1 664 GLN 664 681  ?    ?   ?   A . n 
A 1 665 PHE 665 682  ?    ?   ?   A . n 
A 1 666 ASP 666 683  ?    ?   ?   A . n 
A 1 667 GLY 667 684  ?    ?   ?   A . n 
A 1 668 ASN 668 685  ?    ?   ?   A . n 
A 1 669 THR 669 686  ?    ?   ?   A . n 
A 1 670 ILE 670 687  ?    ?   ?   A . n 
A 1 671 SER 671 688  ?    ?   ?   A . n 
A 1 672 GLY 672 689  ?    ?   ?   A . n 
A 1 673 TYR 673 690  ?    ?   ?   A . n 
A 1 674 LYS 674 691  ?    ?   ?   A . n 
A 1 675 ARG 675 692  ?    ?   ?   A . n 
A 1 676 MET 676 693  ?    ?   ?   A . n 
A 1 677 ILE 677 694  ?    ?   ?   A . n 
A 1 678 ALA 678 695  ?    ?   ?   A . n 
A 1 679 THR 679 696  ?    ?   ?   A . n 
A 1 680 LYS 680 697  ?    ?   ?   A . n 
A 1 681 ASP 681 698  ?    ?   ?   A . n 
A 1 682 SER 682 699  ?    ?   ?   A . n 
A 1 683 PHE 683 700  ?    ?   ?   A . n 
A 1 684 GLN 684 701  ?    ?   ?   A . n 
A 1 685 SER 685 702  ?    ?   ?   A . n 
A 1 686 PHE 686 703  ?    ?   ?   A . n 
A 1 687 ASN 687 704  ?    ?   ?   A . n 
A 1 688 VAL 688 705  ?    ?   ?   A . n 
A 1 689 THR 689 706  ?    ?   ?   A . n 
A 1 690 GLU 690 707  ?    ?   ?   A . n 
A 1 691 PRO 691 708  ?    ?   ?   A . n 
A 1 692 HIS 692 709  ?    ?   ?   A . n 
A 1 693 ILE 693 710  ?    ?   ?   A . n 
A 1 694 SER 694 711  ?    ?   ?   A . n 
A 1 695 ALA 695 712  ?    ?   ?   A . n 
A 1 696 SER 696 713  ?    ?   ?   A . n 
A 1 697 SER 697 714  ?    ?   ?   A . n 
A 1 698 LEU 698 715  ?    ?   ?   A . n 
A 1 699 GLU 699 716  ?    ?   ?   A . n 
A 1 700 TRP 700 717  ?    ?   ?   A . n 
A 1 701 ILE 701 718  ?    ?   ?   A . n 
A 1 702 ASP 702 719  ?    ?   ?   A . n 
A 1 703 PRO 703 720  ?    ?   ?   A . n 
A 1 704 ASP 704 721  ?    ?   ?   A . n 
A 1 705 SER 705 722  ?    ?   ?   A . n 
A 1 706 SER 706 723  ?    ?   ?   A . n 
A 1 707 LEU 707 724  ?    ?   ?   A . n 
A 1 708 ARG 708 725  ?    ?   ?   A . n 
A 1 709 ASP 709 726  ?    ?   ?   A . n 
A 1 710 HIS 710 727  ?    ?   ?   A . n 
A 1 711 ILE 711 728  ?    ?   ?   A . n 
A 1 712 ASN 712 729  ?    ?   ?   A . n 
A 1 713 VAL 713 730  ?    ?   ?   A . n 
A 1 714 ILE 714 731  ?    ?   ?   A . n 
A 1 715 VAL 715 732  ?    ?   ?   A . n 
A 1 716 GLY 716 733  ?    ?   ?   A . n 
A 1 717 ARG 717 734  ?    ?   ?   A . n 
A 1 718 ASP 718 735  ?    ?   ?   A . n 
A 1 719 LEU 719 736  ?    ?   ?   A . n 
A 1 720 SER 720 737  ?    ?   ?   A . n 
A 1 721 PHE 721 738  ?    ?   ?   A . n 
A 1 722 GLN 722 739  ?    ?   ?   A . n 
A 1 723 ASP 723 740  ?    ?   ?   A . n 
A 1 724 LEU 724 741  ?    ?   ?   A . n 
A 1 725 SER 725 742  ?    ?   ?   A . n 
A 1 726 GLU 726 743  ?    ?   ?   A . n 
A 1 727 THR 727 744  ?    ?   ?   A . n 
A 1 728 PRO 728 745  ?    ?   ?   A . n 
A 1 729 CYS 729 746  ?    ?   ?   A . n 
A 1 730 GLN 730 747  ?    ?   ?   A . n 
A 1 731 VAL 731 748  ?    ?   ?   A . n 
A 1 732 ASP 732 749  ?    ?   ?   A . n 
A 1 733 LEU 733 750  ?    ?   ?   A . n 
A 1 734 THR 734 751  ?    ?   ?   A . n 
A 1 735 THR 735 752  ?    ?   ?   A . n 
A 1 736 THR 736 753  ?    ?   ?   A . n 
A 1 737 SER 737 754  ?    ?   ?   A . n 
A 1 738 ILE 738 755  ?    ?   ?   A . n 
A 1 739 ASP 739 756  ?    ?   ?   A . n 
A 1 740 GLY 740 757  ?    ?   ?   A . n 
A 1 741 ALA 741 758  ?    ?   ?   A . n 
A 1 742 TRP 742 759  ?    ?   ?   A . n 
A 1 743 GLY 743 760  ?    ?   ?   A . n 
A 1 744 SER 744 761  ?    ?   ?   A . n 
A 1 745 GLY 745 762  ?    ?   ?   A . n 
A 1 746 VAL 746 763  ?    ?   ?   A . n 
A 1 747 GLY 747 764  ?    ?   ?   A . n 
A 1 748 PHE 748 765  ?    ?   ?   A . n 
A 1 749 ASN 749 766  ?    ?   ?   A . n 
A 1 750 LEU 750 767  ?    ?   ?   A . n 
A 1 751 ILE 751 768  ?    ?   ?   A . n 
A 1 752 CYS 752 769  ?    ?   ?   A . n 
A 1 753 SER 753 770  ?    ?   ?   A . n 
A 1 754 VAL 754 771  ?    ?   ?   A . n 
A 1 755 SER 755 772  ?    ?   ?   A . n 
A 1 756 LEU 756 773  ?    ?   ?   A . n 
A 1 757 THR 757 774  ?    ?   ?   A . n 
A 1 758 GLU 758 775  ?    ?   ?   A . n 
A 1 759 CYS 759 776  ?    ?   ?   A . n 
A 1 760 SER 760 777  ?    ?   ?   A . n 
A 1 761 THR 761 778  ?    ?   ?   A . n 
A 1 762 PHE 762 779  ?    ?   ?   A . n 
A 1 763 LEU 763 780  ?    ?   ?   A . n 
A 1 764 THR 764 781  ?    ?   ?   A . n 
A 1 765 SER 765 782  ?    ?   ?   A . n 
A 1 766 ILE 766 783  ?    ?   ?   A . n 
A 1 767 LYS 767 784  ?    ?   ?   A . n 
A 1 768 ALA 768 785  ?    ?   ?   A . n 
A 1 769 CYS 769 786  ?    ?   ?   A . n 
A 1 770 ASP 770 787  ?    ?   ?   A . n 
A 1 771 SER 771 788  ?    ?   ?   A . n 
A 1 772 ALA 772 789  ?    ?   ?   A . n 
A 1 773 MET 773 790  ?    ?   ?   A . n 
A 1 774 CYS 774 791  ?    ?   ?   A . n 
A 1 775 TYR 775 792  ?    ?   ?   A . n 
A 1 776 GLY 776 793  ?    ?   ?   A . n 
A 1 777 SER 777 794  ?    ?   ?   A . n 
A 1 778 THR 778 795  ?    ?   ?   A . n 
A 1 779 THR 779 796  ?    ?   ?   A . n 
A 1 780 ALA 780 797  ?    ?   ?   A . n 
A 1 781 ASN 781 798  ?    ?   ?   A . n 
A 1 782 LEU 782 799  ?    ?   ?   A . n 
A 1 783 VAL 783 800  ?    ?   ?   A . n 
A 1 784 ARG 784 801  ?    ?   ?   A . n 
A 1 785 GLY 785 802  ?    ?   ?   A . n 
A 1 786 GLN 786 803  ?    ?   ?   A . n 
A 1 787 ASN 787 804  ?    ?   ?   A . n 
A 1 788 THR 788 805  ?    ?   ?   A . n 
A 1 789 VAL 789 806  ?    ?   ?   A . n 
A 1 790 HIS 790 807  ?    ?   ?   A . n 
A 1 791 ILE 791 808  ?    ?   ?   A . n 
A 1 792 VAL 792 809  ?    ?   ?   A . n 
A 1 793 GLY 793 810  ?    ?   ?   A . n 
A 1 794 LYS 794 811  ?    ?   ?   A . n 
A 1 795 GLY 795 812  ?    ?   ?   A . n 
A 1 796 GLY 796 813  ?    ?   ?   A . n 
A 1 797 HIS 797 814  ?    ?   ?   A . n 
A 1 798 SER 798 815  ?    ?   ?   A . n 
A 1 799 GLY 799 816  ?    ?   ?   A . n 
A 1 800 SER 800 817  ?    ?   ?   A . n 
A 1 801 LYS 801 818  ?    ?   ?   A . n 
A 1 802 PHE 802 819  ?    ?   ?   A . n 
A 1 803 MET 803 820  ?    ?   ?   A . n 
A 1 804 CYS 804 821  ?    ?   ?   A . n 
A 1 805 CYS 805 822  ?    ?   ?   A . n 
A 1 806 HIS 806 823  ?    ?   ?   A . n 
A 1 807 ASP 807 824  ?    ?   ?   A . n 
A 1 808 THR 808 825  ?    ?   ?   A . n 
A 1 809 LYS 809 826  ?    ?   ?   A . n 
A 1 810 CYS 810 827  ?    ?   ?   A . n 
A 1 811 SER 811 828  ?    ?   ?   A . n 
A 1 812 SER 812 829  ?    ?   ?   A . n 
A 1 813 THR 813 830  ?    ?   ?   A . n 
A 1 814 GLY 814 831  ?    ?   ?   A . n 
A 1 815 LEU 815 832  ?    ?   ?   A . n 
A 1 816 VAL 816 833  ?    ?   ?   A . n 
A 1 817 ALA 817 834  ?    ?   ?   A . n 
A 1 818 ALA 818 835  ?    ?   ?   A . n 
A 1 819 ALA 819 836  ?    ?   ?   A . n 
A 1 820 PRO 820 837  ?    ?   ?   A . n 
A 1 821 HIS 821 838  ?    ?   ?   A . n 
A 1 822 LEU 822 839  ?    ?   ?   A . n 
A 1 823 ASP 823 840  ?    ?   ?   A . n 
A 1 824 ARG 824 841  ?    ?   ?   A . n 
A 1 825 VAL 825 842  ?    ?   ?   A . n 
A 1 826 THR 826 843  ?    ?   ?   A . n 
A 1 827 GLY 827 844  ?    ?   ?   A . n 
A 1 828 TYR 828 845  ?    ?   ?   A . n 
A 1 829 ASN 829 846  ?    ?   ?   A . n 
A 1 830 GLN 830 847  ?    ?   ?   A . n 
A 1 831 ALA 831 848  ?    ?   ?   A . n 
A 1 832 ASP 832 849  ?    ?   ?   A . n 
A 1 833 SER 833 850  ?    ?   ?   A . n 
A 1 834 ASP 834 851  ?    ?   ?   A . n 
A 1 835 LYS 835 852  ?    ?   ?   A . n 
A 1 836 ILE 836 853  ?    ?   ?   A . n 
A 1 837 PHE 837 854  ?    ?   ?   A . n 
A 1 838 ASP 838 855  ?    ?   ?   A . n 
A 1 839 ASP 839 856  ?    ?   ?   A . n 
A 1 840 GLY 840 857  ?    ?   ?   A . n 
A 1 841 ALA 841 858  ?    ?   ?   A . n 
A 1 842 PRO 842 859  ?    ?   ?   A . n 
A 1 843 GLU 843 860  ?    ?   ?   A . n 
A 1 844 GLY 844 861  ?    ?   ?   A . n 
A 1 845 LEU 845 862  ?    ?   ?   A . n 
A 1 846 VAL 846 863  ?    ?   ?   A . n 
A 1 847 PRO 847 864  ?    ?   ?   A . n 
A 1 848 ARG 848 865  ?    ?   ?   A . n 
A 1 849 GLY 849 866  ?    ?   ?   A . n 
A 1 850 SER 850 867  ?    ?   ?   A . n 
A 1 851 GLY 851 868  ?    ?   ?   A . n 
A 1 852 PRO 852 869  ?    ?   ?   A . n 
A 1 853 PHE 853 870  ?    ?   ?   A . n 
A 1 854 GLU 854 871  ?    ?   ?   A . n 
A 1 855 ASP 855 872  ?    ?   ?   A . n 
A 1 856 ASP 856 873  ?    ?   ?   A . n 
A 1 857 ASP 857 874  ?    ?   ?   A . n 
A 1 858 ASP 858 875  ?    ?   ?   A . n 
A 1 859 LYS 859 876  ?    ?   ?   A . n 
A 1 860 ALA 860 877  ?    ?   ?   A . n 
A 1 861 GLY 861 878  ?    ?   ?   A . n 
A 1 862 TRP 862 879  ?    ?   ?   A . n 
A 1 863 SER 863 880  ?    ?   ?   A . n 
A 1 864 HIS 864 881  ?    ?   ?   A . n 
A 1 865 PRO 865 882  ?    ?   ?   A . n 
A 1 866 GLN 866 883  ?    ?   ?   A . n 
A 1 867 PHE 867 884  ?    ?   ?   A . n 
A 1 868 GLU 868 885  ?    ?   ?   A . n 
A 1 869 LYS 869 886  ?    ?   ?   A . n 
A 1 870 GLY 870 887  ?    ?   ?   A . n 
A 1 871 GLY 871 888  ?    ?   ?   A . n 
A 1 872 GLY 872 889  ?    ?   ?   A . n 
A 1 873 SER 873 890  ?    ?   ?   A . n 
A 1 874 GLY 874 891  ?    ?   ?   A . n 
A 1 875 GLY 875 892  ?    ?   ?   A . n 
A 1 876 GLY 876 893  ?    ?   ?   A . n 
A 1 877 SER 877 894  ?    ?   ?   A . n 
A 1 878 GLY 878 895  ?    ?   ?   A . n 
A 1 879 GLY 879 896  ?    ?   ?   A . n 
A 1 880 GLY 880 897  ?    ?   ?   A . n 
A 1 881 SER 881 898  ?    ?   ?   A . n 
A 1 882 TRP 882 899  ?    ?   ?   A . n 
A 1 883 SER 883 900  ?    ?   ?   A . n 
A 1 884 HIS 884 901  ?    ?   ?   A . n 
A 1 885 PRO 885 902  ?    ?   ?   A . n 
A 1 886 GLN 886 903  ?    ?   ?   A . n 
A 1 887 PHE 887 904  ?    ?   ?   A . n 
A 1 888 GLU 888 905  ?    ?   ?   A . n 
A 1 889 LYS 889 906  ?    ?   ?   A . n 
B 1 1   ARG 1   251  ?    ?   ?   B . n 
B 1 2   SER 2   252  ?    ?   ?   B . n 
B 1 3   SER 3   253  ?    ?   ?   B . n 
B 1 4   ARG 4   254  ?    ?   ?   B . n 
B 1 5   GLY 5   255  ?    ?   ?   B . n 
B 1 6   ASP 6   256  ?    ?   ?   B . n 
B 1 7   THR 7   257  ?    ?   ?   B . n 
B 1 8   ARG 8   258  ?    ?   ?   B . n 
B 1 9   ASN 9   259  ?    ?   ?   B . n 
B 1 10  LEU 10  260  ?    ?   ?   B . n 
B 1 11  ASN 11  261  ?    ?   ?   B . n 
B 1 12  GLU 12  262  ?    ?   ?   B . n 
B 1 13  LEU 13  263  ?    ?   ?   B . n 
B 1 14  LYS 14  264  ?    ?   ?   B . n 
B 1 15  MET 15  265  ?    ?   ?   B . n 
B 1 16  GLU 16  266  ?    ?   ?   B . n 
B 1 17  CYS 17  267  ?    ?   ?   B . n 
B 1 18  PRO 18  268  ?    ?   ?   B . n 
B 1 19  HIS 19  269  ?    ?   ?   B . n 
B 1 20  THR 20  270  ?    ?   ?   B . n 
B 1 21  ILE 21  271  ?    ?   ?   B . n 
B 1 22  GLY 22  272  ?    ?   ?   B . n 
B 1 23  LEU 23  273  ?    ?   ?   B . n 
B 1 24  GLY 24  274  ?    ?   ?   B . n 
B 1 25  GLN 25  275  ?    ?   ?   B . n 
B 1 26  GLY 26  276  ?    ?   ?   B . n 
B 1 27  LEU 27  277  ?    ?   ?   B . n 
B 1 28  VAL 28  278  ?    ?   ?   B . n 
B 1 29  ILE 29  279  ?    ?   ?   B . n 
B 1 30  GLY 30  280  ?    ?   ?   B . n 
B 1 31  SER 31  281  ?    ?   ?   B . n 
B 1 32  ILE 32  282  ?    ?   ?   B . n 
B 1 33  GLU 33  283  ?    ?   ?   B . n 
B 1 34  LEU 34  284  ?    ?   ?   B . n 
B 1 35  PRO 35  285  ?    ?   ?   B . n 
B 1 36  PRO 36  286  ?    ?   ?   B . n 
B 1 37  VAL 37  287  ?    ?   ?   B . n 
B 1 38  PRO 38  288  ?    ?   ?   B . n 
B 1 39  LEU 39  289  ?    ?   ?   B . n 
B 1 40  ILE 40  290  ?    ?   ?   B . n 
B 1 41  GLN 41  291  ?    ?   ?   B . n 
B 1 42  VAL 42  292  ?    ?   ?   B . n 
B 1 43  GLU 43  293  ?    ?   ?   B . n 
B 1 44  SER 44  294  ?    ?   ?   B . n 
B 1 45  LEU 45  295  ?    ?   ?   B . n 
B 1 46  LYS 46  296  ?    ?   ?   B . n 
B 1 47  LEU 47  297  ?    ?   ?   B . n 
B 1 48  GLU 48  298  ?    ?   ?   B . n 
B 1 49  SER 49  299  ?    ?   ?   B . n 
B 1 50  SER 50  300  ?    ?   ?   B . n 
B 1 51  CYS 51  301  ?    ?   ?   B . n 
B 1 52  ASN 52  302  ?    ?   ?   B . n 
B 1 53  PHE 53  303  ?    ?   ?   B . n 
B 1 54  ASP 54  304  ?    ?   ?   B . n 
B 1 55  LEU 55  305  ?    ?   ?   B . n 
B 1 56  HIS 56  306  ?    ?   ?   B . n 
B 1 57  THR 57  307  ?    ?   ?   B . n 
B 1 58  SER 58  308  ?    ?   ?   B . n 
B 1 59  THR 59  309  ?    ?   ?   B . n 
B 1 60  SER 60  310  ?    ?   ?   B . n 
B 1 61  SER 61  311  ?    ?   ?   B . n 
B 1 62  GLN 62  312  ?    ?   ?   B . n 
B 1 63  GLN 63  313  ?    ?   ?   B . n 
B 1 64  ALA 64  314  ?    ?   ?   B . n 
B 1 65  PHE 65  315  ?    ?   ?   B . n 
B 1 66  THR 66  316  ?    ?   ?   B . n 
B 1 67  LYS 67  317  ?    ?   ?   B . n 
B 1 68  TRP 68  318  ?    ?   ?   B . n 
B 1 69  THR 69  319  ?    ?   ?   B . n 
B 1 70  TRP 70  320  ?    ?   ?   B . n 
B 1 71  GLU 71  321  ?    ?   ?   B . n 
B 1 72  VAL 72  322  ?    ?   ?   B . n 
B 1 73  LYS 73  323  ?    ?   ?   B . n 
B 1 74  SER 74  324  ?    ?   ?   B . n 
B 1 75  ASP 75  325  ?    ?   ?   B . n 
B 1 76  LEU 76  326  ?    ?   ?   B . n 
B 1 77  ALA 77  327  ?    ?   ?   B . n 
B 1 78  GLU 78  328  ?    ?   ?   B . n 
B 1 79  ASN 79  329  ?    ?   ?   B . n 
B 1 80  THR 80  330  ?    ?   ?   B . n 
B 1 81  GLN 81  331  ?    ?   ?   B . n 
B 1 82  ALA 82  332  ?    ?   ?   B . n 
B 1 83  SER 83  333  ?    ?   ?   B . n 
B 1 84  SER 84  334  ?    ?   ?   B . n 
B 1 85  THR 85  335  ?    ?   ?   B . n 
B 1 86  SER 86  336  ?    ?   ?   B . n 
B 1 87  PHE 87  337  ?    ?   ?   B . n 
B 1 88  GLN 88  338  ?    ?   ?   B . n 
B 1 89  THR 89  339  ?    ?   ?   B . n 
B 1 90  LYS 90  340  ?    ?   ?   B . n 
B 1 91  SER 91  341  ?    ?   ?   B . n 
B 1 92  SER 92  342  ?    ?   ?   B . n 
B 1 93  GLU 93  343  ?    ?   ?   B . n 
B 1 94  VAL 94  344  ?    ?   ?   B . n 
B 1 95  ASN 95  345  ?    ?   ?   B . n 
B 1 96  LEU 96  346  ?    ?   ?   B . n 
B 1 97  ARG 97  347  ?    ?   ?   B . n 
B 1 98  GLY 98  348  ?    ?   ?   B . n 
B 1 99  LEU 99  349  ?    ?   ?   B . n 
B 1 100 CYS 100 350  ?    ?   ?   B . n 
B 1 101 LEU 101 351  ?    ?   ?   B . n 
B 1 102 VAL 102 352  ?    ?   ?   B . n 
B 1 103 PRO 103 353  ?    ?   ?   B . n 
B 1 104 PRO 104 354  ?    ?   ?   B . n 
B 1 105 LEU 105 355  ?    ?   ?   B . n 
B 1 106 VAL 106 356  ?    ?   ?   B . n 
B 1 107 ILE 107 357  ?    ?   ?   B . n 
B 1 108 GLU 108 358  ?    ?   ?   B . n 
B 1 109 THR 109 359  ?    ?   ?   B . n 
B 1 110 ALA 110 360  ?    ?   ?   B . n 
B 1 111 ALA 111 361  ?    ?   ?   B . n 
B 1 112 ARG 112 362  ?    ?   ?   B . n 
B 1 113 THR 113 363  ?    ?   ?   B . n 
B 1 114 ARG 114 364  ?    ?   ?   B . n 
B 1 115 LYS 115 365  ?    ?   ?   B . n 
B 1 116 THR 116 366  ?    ?   ?   B . n 
B 1 117 ILE 117 367  ?    ?   ?   B . n 
B 1 118 ALA 118 368  ?    ?   ?   B . n 
B 1 119 CYS 119 369  ?    ?   ?   B . n 
B 1 120 PHE 120 370  ?    ?   ?   B . n 
B 1 121 ASP 121 371  ?    ?   ?   B . n 
B 1 122 LEU 122 372  ?    ?   ?   B . n 
B 1 123 SER 123 373  ?    ?   ?   B . n 
B 1 124 CYS 124 374  ?    ?   ?   B . n 
B 1 125 ASN 125 375  ?    ?   ?   B . n 
B 1 126 GLN 126 376  ?    ?   ?   B . n 
B 1 127 THR 127 377  ?    ?   ?   B . n 
B 1 128 THR 128 378  ?    ?   ?   B . n 
B 1 129 CYS 129 379  ?    ?   ?   B . n 
B 1 130 GLN 130 380  ?    ?   ?   B . n 
B 1 131 PRO 131 381  ?    ?   ?   B . n 
B 1 132 THR 132 382  ?    ?   ?   B . n 
B 1 133 VAL 133 383  ?    ?   ?   B . n 
B 1 134 PHE 134 384  ?    ?   ?   B . n 
B 1 135 LEU 135 385  ?    ?   ?   B . n 
B 1 136 MET 136 386  ?    ?   ?   B . n 
B 1 137 GLY 137 387  ?    ?   ?   B . n 
B 1 138 PRO 138 388  ?    ?   ?   B . n 
B 1 139 ILE 139 389  ?    ?   ?   B . n 
B 1 140 GLN 140 390  ?    ?   ?   B . n 
B 1 141 THR 141 391  ?    ?   ?   B . n 
B 1 142 CYS 142 392  ?    ?   ?   B . n 
B 1 143 ILE 143 393  ?    ?   ?   B . n 
B 1 144 THR 144 394  ?    ?   ?   B . n 
B 1 145 THR 145 395  ?    ?   ?   B . n 
B 1 146 LYS 146 396  ?    ?   ?   B . n 
B 1 147 SER 147 397  ?    ?   ?   B . n 
B 1 148 CYS 148 398  ?    ?   ?   B . n 
B 1 149 LEU 149 399  ?    ?   ?   B . n 
B 1 150 LEU 150 400  ?    ?   ?   B . n 
B 1 151 GLY 151 401  ?    ?   ?   B . n 
B 1 152 LEU 152 402  ?    ?   ?   B . n 
B 1 153 GLY 153 403  ?    ?   ?   B . n 
B 1 154 ASP 154 404  ?    ?   ?   B . n 
B 1 155 GLN 155 405  ?    ?   ?   B . n 
B 1 156 ARG 156 406  ?    ?   ?   B . n 
B 1 157 ILE 157 407  ?    ?   ?   B . n 
B 1 158 GLN 158 408  ?    ?   ?   B . n 
B 1 159 VAL 159 409  ?    ?   ?   B . n 
B 1 160 ASN 160 410  ?    ?   ?   B . n 
B 1 161 TYR 161 411  ?    ?   ?   B . n 
B 1 162 GLU 162 412  ?    ?   ?   B . n 
B 1 163 LYS 163 413  ?    ?   ?   B . n 
B 1 164 THR 164 414  ?    ?   ?   B . n 
B 1 165 TYR 165 415  ?    ?   ?   B . n 
B 1 166 CYS 166 416  ?    ?   ?   B . n 
B 1 167 VAL 167 417  ?    ?   ?   B . n 
B 1 168 SER 168 418  ?    ?   ?   B . n 
B 1 169 GLY 169 419  ?    ?   ?   B . n 
B 1 170 GLN 170 420  ?    ?   ?   B . n 
B 1 171 LEU 171 421  ?    ?   ?   B . n 
B 1 172 ILE 172 422  ?    ?   ?   B . n 
B 1 173 GLU 173 423  ?    ?   ?   B . n 
B 1 174 GLY 174 424  ?    ?   ?   B . n 
B 1 175 ILE 175 425  ?    ?   ?   B . n 
B 1 176 CYS 176 426  ?    ?   ?   B . n 
B 1 177 PHE 177 427  ?    ?   ?   B . n 
B 1 178 ASN 178 428  ?    ?   ?   B . n 
B 1 179 PRO 179 429  ?    ?   ?   B . n 
B 1 180 VAL 180 430  ?    ?   ?   B . n 
B 1 181 HIS 181 431  ?    ?   ?   B . n 
B 1 182 THR 182 432  ?    ?   ?   B . n 
B 1 183 MET 183 433  ?    ?   ?   B . n 
B 1 184 ALA 184 434  ?    ?   ?   B . n 
B 1 185 LEU 185 435  ?    ?   ?   B . n 
B 1 186 SER 186 436  ?    ?   ?   B . n 
B 1 187 GLN 187 437  ?    ?   ?   B . n 
B 1 188 PRO 188 438  ?    ?   ?   B . n 
B 1 189 SER 189 439  ?    ?   ?   B . n 
B 1 190 HIS 190 440  ?    ?   ?   B . n 
B 1 191 THR 191 441  ?    ?   ?   B . n 
B 1 192 TYR 192 442  ?    ?   ?   B . n 
B 1 193 ASP 193 443  ?    ?   ?   B . n 
B 1 194 ILE 194 444  ?    ?   ?   B . n 
B 1 195 VAL 195 445  ?    ?   ?   B . n 
B 1 196 THR 196 446  ?    ?   ?   B . n 
B 1 197 VAL 197 447  ?    ?   ?   B . n 
B 1 198 MET 198 448  ?    ?   ?   B . n 
B 1 199 VAL 199 449  ?    ?   ?   B . n 
B 1 200 ARG 200 450  ?    ?   ?   B . n 
B 1 201 CYS 201 451  ?    ?   ?   B . n 
B 1 202 PHE 202 452  ?    ?   ?   B . n 
B 1 203 LEU 203 453  ?    ?   ?   B . n 
B 1 204 ILE 204 454  ?    ?   ?   B . n 
B 1 205 VAL 205 455  ?    ?   ?   B . n 
B 1 206 LYS 206 456  ?    ?   ?   B . n 
B 1 207 LYS 207 457  ?    ?   ?   B . n 
B 1 208 VAL 208 458  ?    ?   ?   B . n 
B 1 209 THR 209 459  ?    ?   ?   B . n 
B 1 210 THR 210 460  ?    ?   ?   B . n 
B 1 211 GLY 211 461  ?    ?   ?   B . n 
B 1 212 ASP 212 462  ?    ?   ?   B . n 
B 1 213 SER 213 463  ?    ?   ?   B . n 
B 1 214 MET 214 464  ?    ?   ?   B . n 
B 1 215 LYS 215 465  ?    ?   ?   B . n 
B 1 216 ILE 216 466  ?    ?   ?   B . n 
B 1 217 GLU 217 467  ?    ?   ?   B . n 
B 1 218 LYS 218 468  ?    ?   ?   B . n 
B 1 219 SER 219 469  ?    ?   ?   B . n 
B 1 220 PHE 220 470  ?    ?   ?   B . n 
B 1 221 GLU 221 471  ?    ?   ?   B . n 
B 1 222 THR 222 472  ?    ?   ?   B . n 
B 1 223 LEU 223 473  ?    ?   ?   B . n 
B 1 224 VAL 224 474  ?    ?   ?   B . n 
B 1 225 GLN 225 475  ?    ?   ?   B . n 
B 1 226 LYS 226 476  ?    ?   ?   B . n 
B 1 227 THR 227 477  ?    ?   ?   B . n 
B 1 228 GLY 228 478  ?    ?   ?   B . n 
B 1 229 CYS 229 479  ?    ?   ?   B . n 
B 1 230 THR 230 480  ?    ?   ?   B . n 
B 1 231 ASP 231 481  ?    ?   ?   B . n 
B 1 232 ASN 232 482  ?    ?   ?   B . n 
B 1 233 GLY 233 483  ?    ?   ?   B . n 
B 1 234 PHE 234 484  ?    ?   ?   B . n 
B 1 235 GLN 235 485  ?    ?   ?   B . n 
B 1 236 GLY 236 486  ?    ?   ?   B . n 
B 1 237 TYR 237 487  ?    ?   ?   B . n 
B 1 238 TYR 238 488  ?    ?   ?   B . n 
B 1 239 VAL 239 489  ?    ?   ?   B . n 
B 1 240 CYS 240 490  ?    ?   ?   B . n 
B 1 241 LEU 241 491  ?    ?   ?   B . n 
B 1 242 ILE 242 492  ?    ?   ?   B . n 
B 1 243 GLY 243 493  ?    ?   ?   B . n 
B 1 244 SER 244 494  ?    ?   ?   B . n 
B 1 245 SER 245 495  ?    ?   ?   B . n 
B 1 246 SER 246 496  ?    ?   ?   B . n 
B 1 247 GLU 247 497  ?    ?   ?   B . n 
B 1 248 PRO 248 498  ?    ?   ?   B . n 
B 1 249 LEU 249 499  ?    ?   ?   B . n 
B 1 250 TYR 250 500  ?    ?   ?   B . n 
B 1 251 ILE 251 501  ?    ?   ?   B . n 
B 1 252 PRO 252 502  ?    ?   ?   B . n 
B 1 253 THR 253 503  ?    ?   ?   B . n 
B 1 254 LEU 254 504  ?    ?   ?   B . n 
B 1 255 ASP 255 505  ?    ?   ?   B . n 
B 1 256 ASP 256 506  ?    ?   ?   B . n 
B 1 257 TYR 257 507  ?    ?   ?   B . n 
B 1 258 ARG 258 508  ?    ?   ?   B . n 
B 1 259 SER 259 509  ?    ?   ?   B . n 
B 1 260 ALA 260 510  ?    ?   ?   B . n 
B 1 261 GLU 261 511  ?    ?   ?   B . n 
B 1 262 VAL 262 512  ?    ?   ?   B . n 
B 1 263 LEU 263 513  ?    ?   ?   B . n 
B 1 264 SER 264 514  ?    ?   ?   B . n 
B 1 265 ARG 265 515  ?    ?   ?   B . n 
B 1 266 MET 266 516  ?    ?   ?   B . n 
B 1 267 ALA 267 517  ?    ?   ?   B . n 
B 1 268 PHE 268 518  ?    ?   ?   B . n 
B 1 269 ALA 269 519  ?    ?   ?   B . n 
B 1 270 PRO 270 520  ?    ?   ?   B . n 
B 1 271 HIS 271 521  ?    ?   ?   B . n 
B 1 272 GLY 272 522  ?    ?   ?   B . n 
B 1 273 GLU 273 523  ?    ?   ?   B . n 
B 1 274 ASP 274 524  ?    ?   ?   B . n 
B 1 275 HIS 275 525  ?    ?   ?   B . n 
B 1 276 ASP 276 526  ?    ?   ?   B . n 
B 1 277 ILE 277 527  ?    ?   ?   B . n 
B 1 278 GLU 278 528  ?    ?   ?   B . n 
B 1 279 LYS 279 529  ?    ?   ?   B . n 
B 1 280 ASN 280 530  ?    ?   ?   B . n 
B 1 281 ALA 281 531  ?    ?   ?   B . n 
B 1 282 ILE 282 532  ?    ?   ?   B . n 
B 1 283 SER 283 533  ?    ?   ?   B . n 
B 1 284 ALA 284 534  ?    ?   ?   B . n 
B 1 285 MET 285 535  ?    ?   ?   B . n 
B 1 286 ARG 286 536  ?    ?   ?   B . n 
B 1 287 ILE 287 537  ?    ?   ?   B . n 
B 1 288 VAL 288 538  ?    ?   ?   B . n 
B 1 289 GLY 289 539  ?    ?   ?   B . n 
B 1 290 LYS 290 540  ?    ?   ?   B . n 
B 1 291 VAL 291 541  ?    ?   ?   B . n 
B 1 292 THR 292 542  ?    ?   ?   B . n 
B 1 293 GLY 293 543  ?    ?   ?   B . n 
B 1 294 LYS 294 544  ?    ?   ?   B . n 
B 1 295 ALA 295 545  ?    ?   ?   B . n 
B 1 296 PRO 296 546  ?    ?   ?   B . n 
B 1 297 SER 297 547  ?    ?   ?   B . n 
B 1 298 THR 298 548  ?    ?   ?   B . n 
B 1 299 GLU 299 549  ?    ?   ?   B . n 
B 1 300 SER 300 550  ?    ?   ?   B . n 
B 1 301 SER 301 551  ?    ?   ?   B . n 
B 1 302 ASP 302 552  ?    ?   ?   B . n 
B 1 303 THR 303 553  ?    ?   ?   B . n 
B 1 304 VAL 304 554  ?    ?   ?   B . n 
B 1 305 GLN 305 555  ?    ?   ?   B . n 
B 1 306 GLY 306 556  ?    ?   ?   B . n 
B 1 307 ILE 307 557  ?    ?   ?   B . n 
B 1 308 ALA 308 558  ?    ?   ?   B . n 
B 1 309 PHE 309 559  ?    ?   ?   B . n 
B 1 310 SER 310 560  ?    ?   ?   B . n 
B 1 311 GLY 311 561  ?    ?   ?   B . n 
B 1 312 ASN 312 562  ?    ?   ?   B . n 
B 1 313 PRO 313 563  ?    ?   ?   B . n 
B 1 314 LEU 314 564  ?    ?   ?   B . n 
B 1 315 TYR 315 565  ?    ?   ?   B . n 
B 1 316 THR 316 566  ?    ?   ?   B . n 
B 1 317 SER 317 567  ?    ?   ?   B . n 
B 1 318 THR 318 568  ?    ?   ?   B . n 
B 1 319 GLY 319 569  ?    ?   ?   B . n 
B 1 320 VAL 320 570  ?    ?   ?   B . n 
B 1 321 LEU 321 571  ?    ?   ?   B . n 
B 1 322 THR 322 572  ?    ?   ?   B . n 
B 1 323 ALA 323 573  ?    ?   ?   B . n 
B 1 324 LYS 324 574  ?    ?   ?   B . n 
B 1 325 ASP 325 575  ?    ?   ?   B . n 
B 1 326 ASP 326 576  ?    ?   ?   B . n 
B 1 327 PRO 327 577  ?    ?   ?   B . n 
B 1 328 VAL 328 578  ?    ?   ?   B . n 
B 1 329 TYR 329 579  ?    ?   ?   B . n 
B 1 330 VAL 330 580  ?    ?   ?   B . n 
B 1 331 TRP 331 581  ?    ?   ?   B . n 
B 1 332 ALA 332 582  ?    ?   ?   B . n 
B 1 333 PRO 333 583  ?    ?   ?   B . n 
B 1 334 GLY 334 584  ?    ?   ?   B . n 
B 1 335 ILE 335 585  ?    ?   ?   B . n 
B 1 336 MET 336 586  ?    ?   ?   B . n 
B 1 337 MET 337 587  ?    ?   ?   B . n 
B 1 338 GLU 338 588  ?    ?   ?   B . n 
B 1 339 GLY 339 589  ?    ?   ?   B . n 
B 1 340 ASN 340 590  ?    ?   ?   B . n 
B 1 341 HIS 341 591  ?    ?   ?   B . n 
B 1 342 SER 342 592  ?    ?   ?   B . n 
B 1 343 VAL 343 593  ?    ?   ?   B . n 
B 1 344 CYS 344 594  ?    ?   ?   B . n 
B 1 345 ASP 345 595  ?    ?   ?   B . n 
B 1 346 LYS 346 596  ?    ?   ?   B . n 
B 1 347 LYS 347 597  ?    ?   ?   B . n 
B 1 348 THR 348 598  ?    ?   ?   B . n 
B 1 349 LEU 349 599  ?    ?   ?   B . n 
B 1 350 PRO 350 600  ?    ?   ?   B . n 
B 1 351 LEU 351 601  ?    ?   ?   B . n 
B 1 352 THR 352 602  ?    ?   ?   B . n 
B 1 353 TRP 353 603  ?    ?   ?   B . n 
B 1 354 THR 354 604  ?    ?   ?   B . n 
B 1 355 GLY 355 605  ?    ?   ?   B . n 
B 1 356 PHE 356 606  ?    ?   ?   B . n 
B 1 357 ILE 357 607  ?    ?   ?   B . n 
B 1 358 PRO 358 608  ?    ?   ?   B . n 
B 1 359 LEU 359 609  ?    ?   ?   B . n 
B 1 360 PRO 360 610  ?    ?   ?   B . n 
B 1 361 GLY 361 611  ?    ?   ?   B . n 
B 1 362 GLU 362 612  ?    ?   ?   B . n 
B 1 363 ILE 363 613  ?    ?   ?   B . n 
B 1 364 GLU 364 614  ?    ?   ?   B . n 
B 1 365 GLY 365 615  ?    ?   ?   B . n 
B 1 366 GLY 366 616  ?    ?   ?   B . n 
B 1 367 SER 367 617  ?    ?   ?   B . n 
B 1 368 GLY 368 618  ?    ?   ?   B . n 
B 1 369 LEU 369 619  ?    ?   ?   B . n 
B 1 370 VAL 370 620  ?    ?   ?   B . n 
B 1 371 PRO 371 621  ?    ?   ?   B . n 
B 1 372 ARG 372 622  ?    ?   ?   B . n 
B 1 373 GLY 373 623  ?    ?   ?   B . n 
B 1 374 SER 374 624  ?    ?   ?   B . n 
B 1 375 GLY 375 625  ?    ?   ?   B . n 
B 1 376 GLY 376 626  ?    ?   ?   B . n 
B 1 377 GLY 377 627  ?    ?   ?   B . n 
B 1 378 SER 378 628  ?    ?   ?   B . n 
B 1 379 GLY 379 629  ?    ?   ?   B . n 
B 1 380 GLY 380 630  ?    ?   ?   B . n 
B 1 381 GLY 381 631  ?    ?   ?   B . n 
B 1 382 SER 382 632  ?    ?   ?   B . n 
B 1 383 TRP 383 633  ?    ?   ?   B . n 
B 1 384 SER 384 634  ?    ?   ?   B . n 
B 1 385 HIS 385 635  ?    ?   ?   B . n 
B 1 386 PRO 386 636  ?    ?   ?   B . n 
B 1 387 GLN 387 637  ?    ?   ?   B . n 
B 1 388 PHE 388 638  ?    ?   ?   B . n 
B 1 389 GLU 389 639  ?    ?   ?   B . n 
B 1 390 LYS 390 640  ?    ?   ?   B . n 
B 1 391 GLY 391 641  ?    ?   ?   B . n 
B 1 392 GLY 392 642  ?    ?   ?   B . n 
B 1 393 GLY 393 643  ?    ?   ?   B . n 
B 1 394 THR 394 644  ?    ?   ?   B . n 
B 1 395 GLY 395 645  ?    ?   ?   B . n 
B 1 396 GLY 396 646  ?    ?   ?   B . n 
B 1 397 GLY 397 647  ?    ?   ?   B . n 
B 1 398 THR 398 648  ?    ?   ?   B . n 
B 1 399 LEU 399 649  ?    ?   ?   B . n 
B 1 400 VAL 400 650  ?    ?   ?   B . n 
B 1 401 PRO 401 651  ?    ?   ?   B . n 
B 1 402 ARG 402 652  ?    ?   ?   B . n 
B 1 403 GLY 403 653  ?    ?   ?   B . n 
B 1 404 SER 404 654  ?    ?   ?   B . n 
B 1 405 GLY 405 655  ?    ?   ?   B . n 
B 1 406 THR 406 656  ?    ?   ?   B . n 
B 1 407 GLY 407 657  ?    ?   ?   B . n 
B 1 408 GLY 408 658  ?    ?   ?   B . n 
B 1 409 GLU 409 659  659  GLU GLU B . n 
B 1 410 THR 410 660  660  THR THR B . n 
B 1 411 GLN 411 661  661  GLN GLN B . n 
B 1 412 ASN 412 662  662  ASN ASN B . n 
B 1 413 LEU 413 663  663  LEU LEU B . n 
B 1 414 ASN 414 664  664  ASN ASN B . n 
B 1 415 SER 415 665  665  SER SER B . n 
B 1 416 GLY 416 666  666  GLY GLY B . n 
B 1 417 TRP 417 667  667  TRP TRP B . n 
B 1 418 THR 418 668  668  THR THR B . n 
B 1 419 ASP 419 669  669  ASP ASP B . n 
B 1 420 THR 420 670  670  THR THR B . n 
B 1 421 ALA 421 671  671  ALA ALA B . n 
B 1 422 HIS 422 672  672  HIS HIS B . n 
B 1 423 GLY 423 673  673  GLY GLY B . n 
B 1 424 SER 424 674  674  SER SER B . n 
B 1 425 GLY 425 675  675  GLY GLY B . n 
B 1 426 VAL 426 676  676  VAL VAL B . n 
B 1 427 ILE 427 677  677  ILE ILE B . n 
B 1 428 PRO 428 678  678  PRO PRO B . n 
B 1 429 MET 429 679  679  MET MET B . n 
B 1 430 ARG 430 680  680  ARG ARG B . n 
B 1 431 THR 431 681  681  THR THR B . n 
B 1 432 ASP 432 682  682  ASP ASP B . n 
B 1 433 LEU 433 683  683  LEU LEU B . n 
B 1 434 GLU 434 684  684  GLU GLU B . n 
B 1 435 LEU 435 685  685  LEU LEU B . n 
B 1 436 ASP 436 686  686  ASP ASP B . n 
B 1 437 PHE 437 687  687  PHE PHE B . n 
B 1 438 SER 438 688  688  SER SER B . n 
B 1 439 LEU 439 689  689  LEU LEU B . n 
B 1 440 PRO 440 690  690  PRO PRO B . n 
B 1 441 SER 441 691  691  SER SER B . n 
B 1 442 SER 442 692  692  SER SER B . n 
B 1 443 ALA 443 693  693  ALA ALA B . n 
B 1 444 SER 444 694  694  SER SER B . n 
B 1 445 TYR 445 695  695  TYR TYR B . n 
B 1 446 THR 446 696  696  THR THR B . n 
B 1 447 TYR 447 697  697  TYR TYR B . n 
B 1 448 ARG 448 698  698  ARG ARG B . n 
B 1 449 ARG 449 699  699  ARG ARG B . n 
B 1 450 GLN 450 700  700  GLN GLN B . n 
B 1 451 LEU 451 701  701  LEU LEU B . n 
B 1 452 GLN 452 702  702  GLN GLN B . n 
B 1 453 ASN 453 703  703  ASN ASN B . n 
B 1 454 PRO 454 704  704  PRO PRO B . n 
B 1 455 ALA 455 705  705  ALA ALA B . n 
B 1 456 ASN 456 706  706  ASN ASN B . n 
B 1 457 GLU 457 707  707  GLU GLU B . n 
B 1 458 GLN 458 708  708  GLN GLN B . n 
B 1 459 GLU 459 709  709  GLU GLU B . n 
B 1 460 LYS 460 710  710  LYS LYS B . n 
B 1 461 ILE 461 711  711  ILE ILE B . n 
B 1 462 PRO 462 712  712  PRO PRO B . n 
B 1 463 PHE 463 713  713  PHE PHE B . n 
B 1 464 HIS 464 714  714  HIS HIS B . n 
B 1 465 LEU 465 715  715  LEU LEU B . n 
B 1 466 GLN 466 716  716  GLN GLN B . n 
B 1 467 ILE 467 717  717  ILE ILE B . n 
B 1 468 SER 468 718  718  SER SER B . n 
B 1 469 LYS 469 719  719  LYS LYS B . n 
B 1 470 GLN 470 720  720  GLN GLN B . n 
B 1 471 VAL 471 721  721  VAL VAL B . n 
B 1 472 ILE 472 722  722  ILE ILE B . n 
B 1 473 HIS 473 723  723  HIS HIS B . n 
B 1 474 ALA 474 724  724  ALA ALA B . n 
B 1 475 GLU 475 725  725  GLU GLU B . n 
B 1 476 ILE 476 726  726  ILE ILE B . n 
B 1 477 GLN 477 727  727  GLN GLN B . n 
B 1 478 HIS 478 728  728  HIS HIS B . n 
B 1 479 LEU 479 729  729  LEU LEU B . n 
B 1 480 GLY 480 730  730  GLY GLY B . n 
B 1 481 HIS 481 731  731  HIS HIS B . n 
B 1 482 TRP 482 732  732  TRP TRP B . n 
B 1 483 MET 483 733  733  MET MET B . n 
B 1 484 ASP 484 734  734  ASP ASP B . n 
B 1 485 GLY 485 735  735  GLY GLY B . n 
B 1 486 THR 486 736  736  THR THR B . n 
B 1 487 PHE 487 737  737  PHE PHE B . n 
B 1 488 ASN 488 738  738  ASN ASN B . n 
B 1 489 LEU 489 739  739  LEU LEU B . n 
B 1 490 LYS 490 740  740  LYS LYS B . n 
B 1 491 THR 491 741  741  THR THR B . n 
B 1 492 ALA 492 742  742  ALA ALA B . n 
B 1 493 PHE 493 743  743  PHE PHE B . n 
B 1 494 HIS 494 744  744  HIS HIS B . n 
B 1 495 CYS 495 745  745  CYS CYS B . n 
B 1 496 TYR 496 746  746  TYR TYR B . n 
B 1 497 GLY 497 747  747  GLY GLY B . n 
B 1 498 SER 498 748  748  SER SER B . n 
B 1 499 CYS 499 749  749  CYS CYS B . n 
B 1 500 GLU 500 750  750  GLU GLU B . n 
B 1 501 LYS 501 751  751  LYS LYS B . n 
B 1 502 TYR 502 752  752  TYR TYR B . n 
B 1 503 ALA 503 753  753  ALA ALA B . n 
B 1 504 TYR 504 754  754  TYR TYR B . n 
B 1 505 PRO 505 755  755  PRO PRO B . n 
B 1 506 TRP 506 756  756  TRP TRP B . n 
B 1 507 GLN 507 757  757  GLN GLN B . n 
B 1 508 THR 508 758  758  THR THR B . n 
B 1 509 ALA 509 759  759  ALA ALA B . n 
B 1 510 GLY 510 760  760  GLY GLY B . n 
B 1 511 CYS 511 761  761  CYS CYS B . n 
B 1 512 PHE 512 762  762  PHE PHE B . n 
B 1 513 VAL 513 763  763  VAL VAL B . n 
B 1 514 GLU 514 764  764  GLU GLU B . n 
B 1 515 LYS 515 765  765  LYS LYS B . n 
B 1 516 ASP 516 766  766  ASP ASP B . n 
B 1 517 TYR 517 767  767  TYR TYR B . n 
B 1 518 GLU 518 768  768  GLU GLU B . n 
B 1 519 TYR 519 769  769  TYR TYR B . n 
B 1 520 GLU 520 770  770  GLU GLU B . n 
B 1 521 SER 521 771  771  SER SER B . n 
B 1 522 GLY 522 772  772  GLY GLY B . n 
B 1 523 TRP 523 773  773  TRP TRP B . n 
B 1 524 GLY 524 774  774  GLY GLY B . n 
B 1 525 CYS 525 775  775  CYS CYS B . n 
B 1 526 ASN 526 776  776  ASN ASN B . n 
B 1 527 PRO 527 777  777  PRO PRO B . n 
B 1 528 ALA 528 778  778  ALA ALA B . n 
B 1 529 ASP 529 779  779  ASP ASP B . n 
B 1 530 CYS 530 780  780  CYS CYS B . n 
B 1 531 PRO 531 781  781  PRO PRO B . n 
B 1 532 GLY 532 782  782  GLY GLY B . n 
B 1 533 VAL 533 783  783  VAL VAL B . n 
B 1 534 GLY 534 784  784  GLY GLY B . n 
B 1 535 THR 535 785  785  THR THR B . n 
B 1 536 GLY 536 786  786  GLY GLY B . n 
B 1 537 CYS 537 787  787  CYS CYS B . n 
B 1 538 THR 538 788  788  THR THR B . n 
B 1 539 ALA 539 789  789  ALA ALA B . n 
B 1 540 CYS 540 790  790  CYS CYS B . n 
B 1 541 GLY 541 791  791  GLY GLY B . n 
B 1 542 VAL 542 792  792  VAL VAL B . n 
B 1 543 TYR 543 793  793  TYR TYR B . n 
B 1 544 LEU 544 794  794  LEU LEU B . n 
B 1 545 ASP 545 795  795  ASP ASP B . n 
B 1 546 LYS 546 796  796  LYS LYS B . n 
B 1 547 LEU 547 797  797  LEU LEU B . n 
B 1 548 LYS 548 798  798  LYS LYS B . n 
B 1 549 SER 549 799  799  SER SER B . n 
B 1 550 VAL 550 800  800  VAL VAL B . n 
B 1 551 GLY 551 801  801  GLY GLY B . n 
B 1 552 LYS 552 802  802  LYS LYS B . n 
B 1 553 ALA 553 803  803  ALA ALA B . n 
B 1 554 PHE 554 804  804  PHE PHE B . n 
B 1 555 LYS 555 805  805  LYS LYS B . n 
B 1 556 ILE 556 806  806  ILE ILE B . n 
B 1 557 VAL 557 807  807  VAL VAL B . n 
B 1 558 SER 558 808  808  SER SER B . n 
B 1 559 LEU 559 809  809  LEU LEU B . n 
B 1 560 ARG 560 810  810  ARG ARG B . n 
B 1 561 TYR 561 811  811  TYR TYR B . n 
B 1 562 THR 562 812  812  THR THR B . n 
B 1 563 ARG 563 813  813  ARG ARG B . n 
B 1 564 LYS 564 814  814  LYS LYS B . n 
B 1 565 ALA 565 815  815  ALA ALA B . n 
B 1 566 CYS 566 816  816  CYS CYS B . n 
B 1 567 ILE 567 817  817  ILE ILE B . n 
B 1 568 GLN 568 818  818  GLN GLN B . n 
B 1 569 LEU 569 819  819  LEU LEU B . n 
B 1 570 GLY 570 820  820  GLY GLY B . n 
B 1 571 THR 571 821  821  THR THR B . n 
B 1 572 GLU 572 822  822  GLU GLU B . n 
B 1 573 GLN 573 823  823  GLN GLN B . n 
B 1 574 THR 574 824  824  THR THR B . n 
B 1 575 CYS 575 825  825  CYS CYS B . n 
B 1 576 LYS 576 826  826  LYS LYS B . n 
B 1 577 ASN 577 827  827  ASN ASN B . n 
B 1 578 VAL 578 828  828  VAL VAL B . n 
B 1 579 ASP 579 829  829  ASP ASP B . n 
B 1 580 SER 580 830  830  SER SER B . n 
B 1 581 ASN 581 831  831  ASN ASN B . n 
B 1 582 ASP 582 832  832  ASP ASP B . n 
B 1 583 CYS 583 833  833  CYS CYS B . n 
B 1 584 LEU 584 834  834  LEU LEU B . n 
B 1 585 VAL 585 835  835  VAL VAL B . n 
B 1 586 THR 586 836  836  THR THR B . n 
B 1 587 THR 587 837  837  THR THR B . n 
B 1 588 SER 588 838  838  SER SER B . n 
B 1 589 VAL 589 839  839  VAL VAL B . n 
B 1 590 LYS 590 840  840  LYS LYS B . n 
B 1 591 VAL 591 841  841  VAL VAL B . n 
B 1 592 CYS 592 842  842  CYS CYS B . n 
B 1 593 LEU 593 843  843  LEU LEU B . n 
B 1 594 ILE 594 844  844  ILE ILE B . n 
B 1 595 GLY 595 845  845  GLY GLY B . n 
B 1 596 THR 596 846  846  THR THR B . n 
B 1 597 VAL 597 847  847  VAL VAL B . n 
B 1 598 SER 598 848  848  SER SER B . n 
B 1 599 LYS 599 849  849  LYS LYS B . n 
B 1 600 PHE 600 850  850  PHE PHE B . n 
B 1 601 GLN 601 851  851  GLN GLN B . n 
B 1 602 PRO 602 852  852  PRO PRO B . n 
B 1 603 SER 603 853  853  SER SER B . n 
B 1 604 ASP 604 854  854  ASP ASP B . n 
B 1 605 THR 605 855  855  THR THR B . n 
B 1 606 LEU 606 856  856  LEU LEU B . n 
B 1 607 LEU 607 857  857  LEU LEU B . n 
B 1 608 PHE 608 858  858  PHE PHE B . n 
B 1 609 LEU 609 859  859  LEU LEU B . n 
B 1 610 GLY 610 860  860  GLY GLY B . n 
B 1 611 PRO 611 861  861  PRO PRO B . n 
B 1 612 LEU 612 862  862  LEU LEU B . n 
B 1 613 GLU 613 863  863  GLU GLU B . n 
B 1 614 GLN 614 864  864  GLN GLN B . n 
B 1 615 GLY 615 865  865  GLY GLY B . n 
B 1 616 GLY 616 866  866  GLY GLY B . n 
B 1 617 LEU 617 867  867  LEU LEU B . n 
B 1 618 ILE 618 868  868  ILE ILE B . n 
B 1 619 PHE 619 869  869  PHE PHE B . n 
B 1 620 LYS 620 870  870  LYS LYS B . n 
B 1 621 GLN 621 871  871  GLN GLN B . n 
B 1 622 TRP 622 872  872  TRP TRP B . n 
B 1 623 CYS 623 873  873  CYS CYS B . n 
B 1 624 THR 624 874  874  THR THR B . n 
B 1 625 THR 625 875  875  THR THR B . n 
B 1 626 THR 626 876  876  THR THR B . n 
B 1 627 CYS 627 877  877  CYS CYS B . n 
B 1 628 GLN 628 878  878  GLN GLN B . n 
B 1 629 PHE 629 879  879  PHE PHE B . n 
B 1 630 GLY 630 880  880  GLY GLY B . n 
B 1 631 ASP 631 881  881  ASP ASP B . n 
B 1 632 PRO 632 882  882  PRO PRO B . n 
B 1 633 GLY 633 883  883  GLY GLY B . n 
B 1 634 ASP 634 884  884  ASP ASP B . n 
B 1 635 ILE 635 885  885  ILE ILE B . n 
B 1 636 MET 636 886  886  MET MET B . n 
B 1 637 SER 637 887  887  SER SER B . n 
B 1 638 THR 638 888  888  THR THR B . n 
B 1 639 PRO 639 889  889  PRO PRO B . n 
B 1 640 VAL 640 890  890  VAL VAL B . n 
B 1 641 GLY 641 891  891  GLY GLY B . n 
B 1 642 MET 642 892  892  MET MET B . n 
B 1 643 LYS 643 893  893  LYS LYS B . n 
B 1 644 CYS 644 894  894  CYS CYS B . n 
B 1 645 PRO 645 895  895  PRO PRO B . n 
B 1 646 GLU 646 896  896  GLU GLU B . n 
B 1 647 LEU 647 897  897  LEU LEU B . n 
B 1 648 SER 648 898  898  SER SER B . n 
B 1 649 GLY 649 899  899  GLY GLY B . n 
B 1 650 SER 650 900  900  SER SER B . n 
B 1 651 PHE 651 901  901  PHE PHE B . n 
B 1 652 ARG 652 902  902  ARG ARG B . n 
B 1 653 LYS 653 903  903  LYS LYS B . n 
B 1 654 LYS 654 904  904  LYS LYS B . n 
B 1 655 CYS 655 905  905  CYS CYS B . n 
B 1 656 ALA 656 906  906  ALA ALA B . n 
B 1 657 PHE 657 907  907  PHE PHE B . n 
B 1 658 ALA 658 908  908  ALA ALA B . n 
B 1 659 THR 659 909  909  THR THR B . n 
B 1 660 THR 660 910  910  THR THR B . n 
B 1 661 PRO 661 911  911  PRO PRO B . n 
B 1 662 VAL 662 912  912  VAL VAL B . n 
B 1 663 CYS 663 913  913  CYS CYS B . n 
B 1 664 GLN 664 914  914  GLN GLN B . n 
B 1 665 PHE 665 915  915  PHE PHE B . n 
B 1 666 ASP 666 916  916  ASP ASP B . n 
B 1 667 GLY 667 917  917  GLY GLY B . n 
B 1 668 ASN 668 918  918  ASN ASN B . n 
B 1 669 THR 669 919  919  THR THR B . n 
B 1 670 ILE 670 920  920  ILE ILE B . n 
B 1 671 SER 671 921  921  SER SER B . n 
B 1 672 GLY 672 922  922  GLY GLY B . n 
B 1 673 TYR 673 923  923  TYR TYR B . n 
B 1 674 LYS 674 924  924  LYS LYS B . n 
B 1 675 ARG 675 925  925  ARG ARG B . n 
B 1 676 MET 676 926  926  MET MET B . n 
B 1 677 ILE 677 927  927  ILE ILE B . n 
B 1 678 ALA 678 928  928  ALA ALA B . n 
B 1 679 THR 679 929  929  THR THR B . n 
B 1 680 LYS 680 930  930  LYS LYS B . n 
B 1 681 ASP 681 931  931  ASP ASP B . n 
B 1 682 SER 682 932  932  SER SER B . n 
B 1 683 PHE 683 933  933  PHE PHE B . n 
B 1 684 GLN 684 934  934  GLN GLN B . n 
B 1 685 SER 685 935  935  SER SER B . n 
B 1 686 PHE 686 936  936  PHE PHE B . n 
B 1 687 ASN 687 937  937  ASN ASN B . n 
B 1 688 VAL 688 938  938  VAL VAL B . n 
B 1 689 THR 689 939  939  THR THR B . n 
B 1 690 GLU 690 940  940  GLU GLU B . n 
B 1 691 PRO 691 941  941  PRO PRO B . n 
B 1 692 HIS 692 942  942  HIS HIS B . n 
B 1 693 ILE 693 943  943  ILE ILE B . n 
B 1 694 SER 694 944  944  SER SER B . n 
B 1 695 ALA 695 945  945  ALA ALA B . n 
B 1 696 SER 696 946  946  SER SER B . n 
B 1 697 SER 697 947  947  SER SER B . n 
B 1 698 LEU 698 948  948  LEU LEU B . n 
B 1 699 GLU 699 949  949  GLU GLU B . n 
B 1 700 TRP 700 950  950  TRP TRP B . n 
B 1 701 ILE 701 951  951  ILE ILE B . n 
B 1 702 ASP 702 952  952  ASP ASP B . n 
B 1 703 PRO 703 953  953  PRO PRO B . n 
B 1 704 ASP 704 954  954  ASP ASP B . n 
B 1 705 SER 705 955  955  SER SER B . n 
B 1 706 SER 706 956  956  SER SER B . n 
B 1 707 LEU 707 957  957  LEU LEU B . n 
B 1 708 ARG 708 958  958  ARG ARG B . n 
B 1 709 ASP 709 959  959  ASP ASP B . n 
B 1 710 HIS 710 960  960  HIS HIS B . n 
B 1 711 ILE 711 961  961  ILE ILE B . n 
B 1 712 ASN 712 962  962  ASN ASN B . n 
B 1 713 VAL 713 963  963  VAL VAL B . n 
B 1 714 ILE 714 964  964  ILE ILE B . n 
B 1 715 VAL 715 965  965  VAL VAL B . n 
B 1 716 GLY 716 966  966  GLY GLY B . n 
B 1 717 ARG 717 967  967  ARG ARG B . n 
B 1 718 ASP 718 968  968  ASP ASP B . n 
B 1 719 LEU 719 969  969  LEU LEU B . n 
B 1 720 SER 720 970  970  SER SER B . n 
B 1 721 PHE 721 971  971  PHE PHE B . n 
B 1 722 GLN 722 972  972  GLN GLN B . n 
B 1 723 ASP 723 973  973  ASP ASP B . n 
B 1 724 LEU 724 974  974  LEU LEU B . n 
B 1 725 SER 725 975  975  SER SER B . n 
B 1 726 GLU 726 976  976  GLU GLU B . n 
B 1 727 THR 727 977  977  THR THR B . n 
B 1 728 PRO 728 978  978  PRO PRO B . n 
B 1 729 CYS 729 979  979  CYS CYS B . n 
B 1 730 GLN 730 980  980  GLN GLN B . n 
B 1 731 VAL 731 981  981  VAL VAL B . n 
B 1 732 ASP 732 982  982  ASP ASP B . n 
B 1 733 LEU 733 983  983  LEU LEU B . n 
B 1 734 THR 734 984  984  THR THR B . n 
B 1 735 THR 735 985  985  THR THR B . n 
B 1 736 THR 736 986  986  THR THR B . n 
B 1 737 SER 737 987  987  SER SER B . n 
B 1 738 ILE 738 988  988  ILE ILE B . n 
B 1 739 ASP 739 989  989  ASP ASP B . n 
B 1 740 GLY 740 990  990  GLY GLY B . n 
B 1 741 ALA 741 991  991  ALA ALA B . n 
B 1 742 TRP 742 992  992  TRP TRP B . n 
B 1 743 GLY 743 993  993  GLY GLY B . n 
B 1 744 SER 744 994  994  SER SER B . n 
B 1 745 GLY 745 995  995  GLY GLY B . n 
B 1 746 VAL 746 996  996  VAL VAL B . n 
B 1 747 GLY 747 997  997  GLY GLY B . n 
B 1 748 PHE 748 998  998  PHE PHE B . n 
B 1 749 ASN 749 999  999  ASN ASN B . n 
B 1 750 LEU 750 1000 1000 LEU LEU B . n 
B 1 751 ILE 751 1001 1001 ILE ILE B . n 
B 1 752 CYS 752 1002 1002 CYS CYS B . n 
B 1 753 SER 753 1003 1003 SER SER B . n 
B 1 754 VAL 754 1004 1004 VAL VAL B . n 
B 1 755 SER 755 1005 1005 SER SER B . n 
B 1 756 LEU 756 1006 1006 LEU LEU B . n 
B 1 757 THR 757 1007 1007 THR THR B . n 
B 1 758 GLU 758 1008 1008 GLU GLU B . n 
B 1 759 CYS 759 1009 1009 CYS CYS B . n 
B 1 760 SER 760 1010 1010 SER SER B . n 
B 1 761 THR 761 1011 1011 THR THR B . n 
B 1 762 PHE 762 1012 1012 PHE PHE B . n 
B 1 763 LEU 763 1013 1013 LEU LEU B . n 
B 1 764 THR 764 1014 1014 THR THR B . n 
B 1 765 SER 765 1015 1015 SER SER B . n 
B 1 766 ILE 766 1016 1016 ILE ILE B . n 
B 1 767 LYS 767 1017 1017 LYS LYS B . n 
B 1 768 ALA 768 1018 1018 ALA ALA B . n 
B 1 769 CYS 769 1019 1019 CYS CYS B . n 
B 1 770 ASP 770 1020 1020 ASP ASP B . n 
B 1 771 SER 771 1021 1021 SER SER B . n 
B 1 772 ALA 772 1022 1022 ALA ALA B . n 
B 1 773 MET 773 1023 1023 MET MET B . n 
B 1 774 CYS 774 1024 1024 CYS CYS B . n 
B 1 775 TYR 775 1025 1025 TYR TYR B . n 
B 1 776 GLY 776 1026 1026 GLY GLY B . n 
B 1 777 SER 777 1027 1027 SER SER B . n 
B 1 778 THR 778 1028 1028 THR THR B . n 
B 1 779 THR 779 1029 1029 THR THR B . n 
B 1 780 ALA 780 1030 1030 ALA ALA B . n 
B 1 781 ASN 781 1031 1031 ASN ASN B . n 
B 1 782 LEU 782 1032 1032 LEU LEU B . n 
B 1 783 VAL 783 1033 1033 VAL VAL B . n 
B 1 784 ARG 784 1034 1034 ARG ARG B . n 
B 1 785 GLY 785 1035 1035 GLY GLY B . n 
B 1 786 GLN 786 1036 1036 GLN GLN B . n 
B 1 787 ASN 787 1037 1037 ASN ASN B . n 
B 1 788 THR 788 1038 1038 THR THR B . n 
B 1 789 VAL 789 1039 1039 VAL VAL B . n 
B 1 790 HIS 790 1040 1040 HIS HIS B . n 
B 1 791 ILE 791 1041 1041 ILE ILE B . n 
B 1 792 VAL 792 1042 1042 VAL VAL B . n 
B 1 793 GLY 793 1043 1043 GLY GLY B . n 
B 1 794 LYS 794 1044 1044 LYS LYS B . n 
B 1 795 GLY 795 1045 1045 GLY GLY B . n 
B 1 796 GLY 796 1046 1046 GLY GLY B . n 
B 1 797 HIS 797 1047 1047 HIS HIS B . n 
B 1 798 SER 798 1048 1048 SER SER B . n 
B 1 799 GLY 799 1049 1049 GLY GLY B . n 
B 1 800 SER 800 1050 1050 SER SER B . n 
B 1 801 LYS 801 1051 1051 LYS LYS B . n 
B 1 802 PHE 802 1052 1052 PHE PHE B . n 
B 1 803 MET 803 1053 1053 MET MET B . n 
B 1 804 CYS 804 1054 1054 CYS CYS B . n 
B 1 805 CYS 805 1055 1055 CYS CYS B . n 
B 1 806 HIS 806 1056 1056 HIS HIS B . n 
B 1 807 ASP 807 1057 1057 ASP ASP B . n 
B 1 808 THR 808 1058 1058 THR THR B . n 
B 1 809 LYS 809 1059 1059 LYS LYS B . n 
B 1 810 CYS 810 1060 1060 CYS CYS B . n 
B 1 811 SER 811 1061 1061 SER SER B . n 
B 1 812 SER 812 1062 1062 SER SER B . n 
B 1 813 THR 813 1063 1063 THR THR B . n 
B 1 814 GLY 814 1064 1064 GLY GLY B . n 
B 1 815 LEU 815 1065 1065 LEU LEU B . n 
B 1 816 VAL 816 1066 1066 VAL VAL B . n 
B 1 817 ALA 817 1067 1067 ALA ALA B . n 
B 1 818 ALA 818 1068 1068 ALA ALA B . n 
B 1 819 ALA 819 1069 1069 ALA ALA B . n 
B 1 820 PRO 820 1070 1070 PRO PRO B . n 
B 1 821 HIS 821 1071 ?    ?   ?   B . n 
B 1 822 LEU 822 1072 ?    ?   ?   B . n 
B 1 823 ASP 823 1073 ?    ?   ?   B . n 
B 1 824 ARG 824 1074 ?    ?   ?   B . n 
B 1 825 VAL 825 1075 ?    ?   ?   B . n 
B 1 826 THR 826 1076 ?    ?   ?   B . n 
B 1 827 GLY 827 1077 ?    ?   ?   B . n 
B 1 828 TYR 828 1078 ?    ?   ?   B . n 
B 1 829 ASN 829 1079 ?    ?   ?   B . n 
B 1 830 GLN 830 1080 ?    ?   ?   B . n 
B 1 831 ALA 831 1081 ?    ?   ?   B . n 
B 1 832 ASP 832 1082 ?    ?   ?   B . n 
B 1 833 SER 833 1083 1083 SER SER B . n 
B 1 834 ASP 834 1084 1084 ASP ASP B . n 
B 1 835 LYS 835 1085 1085 LYS LYS B . n 
B 1 836 ILE 836 1086 1086 ILE ILE B . n 
B 1 837 PHE 837 1087 1087 PHE PHE B . n 
B 1 838 ASP 838 1088 1088 ASP ASP B . n 
B 1 839 ASP 839 1089 1089 ASP ASP B . n 
B 1 840 GLY 840 1090 1090 GLY GLY B . n 
B 1 841 ALA 841 1091 1091 ALA ALA B . n 
B 1 842 PRO 842 1092 1092 PRO PRO B . n 
B 1 843 GLU 843 1093 1093 GLU GLU B . n 
B 1 844 GLY 844 1094 ?    ?   ?   B . n 
B 1 845 LEU 845 1095 ?    ?   ?   B . n 
B 1 846 VAL 846 1096 ?    ?   ?   B . n 
B 1 847 PRO 847 1097 ?    ?   ?   B . n 
B 1 848 ARG 848 1098 ?    ?   ?   B . n 
B 1 849 GLY 849 1099 ?    ?   ?   B . n 
B 1 850 SER 850 1100 ?    ?   ?   B . n 
B 1 851 GLY 851 1101 ?    ?   ?   B . n 
B 1 852 PRO 852 1102 ?    ?   ?   B . n 
B 1 853 PHE 853 1103 ?    ?   ?   B . n 
B 1 854 GLU 854 1104 ?    ?   ?   B . n 
B 1 855 ASP 855 1105 ?    ?   ?   B . n 
B 1 856 ASP 856 1106 ?    ?   ?   B . n 
B 1 857 ASP 857 1107 ?    ?   ?   B . n 
B 1 858 ASP 858 1108 ?    ?   ?   B . n 
B 1 859 LYS 859 1109 ?    ?   ?   B . n 
B 1 860 ALA 860 1110 ?    ?   ?   B . n 
B 1 861 GLY 861 1111 ?    ?   ?   B . n 
B 1 862 TRP 862 1112 ?    ?   ?   B . n 
B 1 863 SER 863 1113 ?    ?   ?   B . n 
B 1 864 HIS 864 1114 ?    ?   ?   B . n 
B 1 865 PRO 865 1115 ?    ?   ?   B . n 
B 1 866 GLN 866 1116 ?    ?   ?   B . n 
B 1 867 PHE 867 1117 ?    ?   ?   B . n 
B 1 868 GLU 868 1118 ?    ?   ?   B . n 
B 1 869 LYS 869 1119 ?    ?   ?   B . n 
B 1 870 GLY 870 1120 ?    ?   ?   B . n 
B 1 871 GLY 871 1121 ?    ?   ?   B . n 
B 1 872 GLY 872 1122 ?    ?   ?   B . n 
B 1 873 SER 873 1123 ?    ?   ?   B . n 
B 1 874 GLY 874 1124 ?    ?   ?   B . n 
B 1 875 GLY 875 1125 ?    ?   ?   B . n 
B 1 876 GLY 876 1126 ?    ?   ?   B . n 
B 1 877 SER 877 1127 ?    ?   ?   B . n 
B 1 878 GLY 878 1128 ?    ?   ?   B . n 
B 1 879 GLY 879 1129 ?    ?   ?   B . n 
B 1 880 GLY 880 1130 ?    ?   ?   B . n 
B 1 881 SER 881 1131 ?    ?   ?   B . n 
B 1 882 TRP 882 1132 ?    ?   ?   B . n 
B 1 883 SER 883 1133 ?    ?   ?   B . n 
B 1 884 HIS 884 1134 ?    ?   ?   B . n 
B 1 885 PRO 885 1135 ?    ?   ?   B . n 
B 1 886 GLN 886 1136 ?    ?   ?   B . n 
B 1 887 PHE 887 1137 ?    ?   ?   B . n 
B 1 888 GLU 888 1138 ?    ?   ?   B . n 
B 1 889 LYS 889 1139 ?    ?   ?   B . n 
C 2 1   ARG 1   -1   ?    ?   ?   H . n 
C 2 2   SER 2   0    ?    ?   ?   H . n 
C 2 3   GLN 3   1    1    GLN GLN H . n 
C 2 4   VAL 4   2    2    VAL VAL H . n 
C 2 5   GLN 5   3    3    GLN GLN H . n 
C 2 6   LEU 6   4    4    LEU LEU H . n 
C 2 7   VAL 7   5    5    VAL VAL H . n 
C 2 8   GLU 8   6    6    GLU GLU H . n 
C 2 9   SER 9   7    7    SER SER H . n 
C 2 10  GLY 10  8    8    GLY GLY H . n 
C 2 11  GLY 11  9    9    GLY GLY H . n 
C 2 12  GLY 12  10   10   GLY GLY H . n 
C 2 13  VAL 13  11   11   VAL VAL H . n 
C 2 14  VAL 14  12   12   VAL VAL H . n 
C 2 15  GLN 15  13   13   GLN GLN H . n 
C 2 16  PRO 16  14   14   PRO PRO H . n 
C 2 17  GLY 17  15   15   GLY GLY H . n 
C 2 18  ARG 18  16   16   ARG ARG H . n 
C 2 19  SER 19  17   17   SER SER H . n 
C 2 20  LEU 20  18   18   LEU LEU H . n 
C 2 21  ARG 21  19   19   ARG ARG H . n 
C 2 22  LEU 22  20   20   LEU LEU H . n 
C 2 23  SER 23  21   21   SER SER H . n 
C 2 24  CYS 24  22   22   CYS CYS H . n 
C 2 25  ALA 25  23   23   ALA ALA H . n 
C 2 26  ALA 26  24   24   ALA ALA H . n 
C 2 27  SER 27  25   25   SER SER H . n 
C 2 28  GLY 28  26   26   GLY GLY H . n 
C 2 29  PHE 29  27   27   PHE PHE H . n 
C 2 30  THR 30  28   28   THR THR H . n 
C 2 31  PHE 31  29   29   PHE PHE H . n 
C 2 32  SER 32  30   30   SER SER H . n 
C 2 33  SER 33  31   31   SER SER H . n 
C 2 34  TYR 34  32   32   TYR TYR H . n 
C 2 35  ALA 35  33   33   ALA ALA H . n 
C 2 36  MET 36  34   34   MET MET H . n 
C 2 37  HIS 37  35   35   HIS HIS H . n 
C 2 38  TRP 38  36   36   TRP TRP H . n 
C 2 39  VAL 39  37   37   VAL VAL H . n 
C 2 40  ARG 40  38   38   ARG ARG H . n 
C 2 41  GLN 41  39   39   GLN GLN H . n 
C 2 42  ALA 42  40   40   ALA ALA H . n 
C 2 43  PRO 43  41   41   PRO PRO H . n 
C 2 44  GLY 44  42   42   GLY GLY H . n 
C 2 45  LYS 45  43   43   LYS LYS H . n 
C 2 46  GLY 46  44   44   GLY GLY H . n 
C 2 47  LEU 47  45   45   LEU LEU H . n 
C 2 48  GLU 48  46   46   GLU GLU H . n 
C 2 49  TRP 49  47   47   TRP TRP H . n 
C 2 50  VAL 50  48   48   VAL VAL H . n 
C 2 51  ALA 51  49   49   ALA ALA H . n 
C 2 52  VAL 52  50   50   VAL VAL H . n 
C 2 53  THR 53  51   51   THR THR H . n 
C 2 54  TRP 54  52   52   TRP TRP H . n 
C 2 55  PHE 55  52   52   PHE PHE H A n 
C 2 56  ASP 56  53   53   ASP ASP H . n 
C 2 57  VAL 57  54   54   VAL VAL H . n 
C 2 58  SER 58  55   55   SER SER H . n 
C 2 59  LYS 59  56   56   LYS LYS H . n 
C 2 60  LYS 60  57   57   LYS LYS H . n 
C 2 61  ASP 61  58   58   ASP ASP H . n 
C 2 62  TYR 62  59   59   TYR TYR H . n 
C 2 63  ALA 63  60   60   ALA ALA H . n 
C 2 64  ASP 64  61   61   ASP ASP H . n 
C 2 65  SER 65  62   62   SER SER H . n 
C 2 66  VAL 66  63   63   VAL VAL H . n 
C 2 67  LYS 67  64   64   LYS LYS H . n 
C 2 68  GLY 68  65   65   GLY GLY H . n 
C 2 69  ARG 69  66   66   ARG ARG H . n 
C 2 70  PHE 70  67   67   PHE PHE H . n 
C 2 71  THR 71  68   68   THR THR H . n 
C 2 72  ILE 72  69   69   ILE ILE H . n 
C 2 73  SER 73  70   70   SER SER H . n 
C 2 74  ARG 74  71   ?    ?   ?   H . n 
C 2 75  ASP 75  72   ?    ?   ?   H . n 
C 2 76  ASN 76  73   ?    ?   ?   H . n 
C 2 77  SER 77  74   ?    ?   ?   H . n 
C 2 78  LYS 78  75   75   LYS LYS H . n 
C 2 79  ASN 79  76   76   ASN ASN H . n 
C 2 80  THR 80  77   77   THR THR H . n 
C 2 81  LEU 81  78   78   LEU LEU H . n 
C 2 82  TYR 82  79   79   TYR TYR H . n 
C 2 83  LEU 83  80   80   LEU LEU H . n 
C 2 84  GLN 84  81   81   GLN GLN H . n 
C 2 85  MET 85  82   82   MET MET H . n 
C 2 86  ASN 86  82   82   ASN ASN H A n 
C 2 87  SER 87  82   82   SER SER H B n 
C 2 88  LEU 88  82   82   LEU LEU H C n 
C 2 89  ARG 89  83   83   ARG ARG H . n 
C 2 90  ALA 90  84   84   ALA ALA H . n 
C 2 91  GLU 91  85   85   GLU GLU H . n 
C 2 92  ASP 92  86   86   ASP ASP H . n 
C 2 93  THR 93  87   87   THR THR H . n 
C 2 94  ALA 94  88   88   ALA ALA H . n 
C 2 95  VAL 95  89   89   VAL VAL H . n 
C 2 96  TYR 96  90   90   TYR TYR H . n 
C 2 97  TYR 97  91   91   TYR TYR H . n 
C 2 98  CYS 98  92   92   CYS CYS H . n 
C 2 99  ALA 99  93   93   ALA ALA H . n 
C 2 100 ARG 100 94   94   ARG ARG H . n 
C 2 101 ASN 101 95   95   ASN ASN H . n 
C 2 102 LEU 102 96   96   LEU LEU H . n 
C 2 103 ILE 103 97   97   ILE ILE H . n 
C 2 104 ARG 104 98   98   ARG ARG H . n 
C 2 105 TYR 105 99   99   TYR TYR H . n 
C 2 106 SER 106 100  100  SER SER H . n 
C 2 107 GLY 107 100  100  GLY GLY H A n 
C 2 108 SER 108 100  100  SER SER H B n 
C 2 109 TYR 109 100  100  TYR TYR H C n 
C 2 110 PHE 110 100  100  PHE PHE H D n 
C 2 111 PRO 111 100  100  PRO PRO H E n 
C 2 112 VAL 112 100  100  VAL VAL H F n 
C 2 113 HIS 113 100  100  HIS HIS H G n 
C 2 114 GLY 114 100  100  GLY GLY H H n 
C 2 115 MET 115 100  100  MET MET H I n 
C 2 116 ASP 116 101  101  ASP ASP H . n 
C 2 117 VAL 117 102  102  VAL VAL H . n 
C 2 118 TRP 118 103  103  TRP TRP H . n 
C 2 119 GLY 119 104  104  GLY GLY H . n 
C 2 120 GLN 120 105  105  GLN GLN H . n 
C 2 121 GLY 121 106  106  GLY GLY H . n 
C 2 122 THR 122 107  107  THR THR H . n 
C 2 123 THR 123 108  108  THR THR H . n 
C 2 124 VAL 124 109  109  VAL VAL H . n 
C 2 125 THR 125 110  110  THR THR H . n 
C 2 126 VAL 126 111  111  VAL VAL H . n 
C 2 127 SER 127 112  112  SER SER H . n 
C 2 128 SER 128 113  113  SER SER H . n 
C 2 129 GLY 129 114  ?    ?   ?   H . n 
C 2 130 THR 130 115  ?    ?   ?   H . n 
C 2 131 GLY 131 116  ?    ?   ?   H . n 
C 2 132 GLY 132 117  ?    ?   ?   H . n 
C 2 133 SER 133 118  ?    ?   ?   H . n 
C 2 134 GLY 134 119  ?    ?   ?   H . n 
C 2 135 GLY 135 120  ?    ?   ?   H . n 
C 2 136 GLY 136 121  ?    ?   ?   H . n 
C 2 137 GLY 137 122  ?    ?   ?   H . n 
C 2 138 SER 138 123  ?    ?   ?   H . n 
C 2 139 GLY 139 124  ?    ?   ?   H . n 
C 2 140 GLY 140 125  ?    ?   ?   H . n 
C 2 141 GLY 141 126  ?    ?   ?   H . n 
C 2 142 GLY 142 127  ?    ?   ?   H . n 
C 2 143 SER 143 128  ?    ?   ?   H . n 
C 2 144 GLY 144 129  ?    ?   ?   H . n 
C 2 145 GLY 145 130  ?    ?   ?   H . n 
C 2 146 GLY 146 131  ?    ?   ?   H . n 
C 2 147 ALA 147 132  ?    ?   ?   H . n 
C 2 148 SER 148 133  ?    ?   ?   H . n 
C 2 149 ASP 149 134  ?    ?   ?   H . n 
C 2 150 ILE 150 135  ?    ?   ?   H . n 
C 2 151 VAL 151 136  ?    ?   ?   H . n 
C 2 152 MET 152 137  ?    ?   ?   H . n 
C 2 153 THR 153 138  ?    ?   ?   H . n 
C 2 154 GLN 154 139  ?    ?   ?   H . n 
C 2 155 SER 155 140  ?    ?   ?   H . n 
C 2 156 PRO 156 141  ?    ?   ?   H . n 
C 2 157 LEU 157 142  ?    ?   ?   H . n 
C 2 158 SER 158 143  ?    ?   ?   H . n 
C 2 159 LEU 159 144  ?    ?   ?   H . n 
C 2 160 PRO 160 145  ?    ?   ?   H . n 
C 2 161 VAL 161 146  ?    ?   ?   H . n 
C 2 162 THR 162 147  ?    ?   ?   H . n 
C 2 163 PRO 163 148  ?    ?   ?   H . n 
C 2 164 GLY 164 149  ?    ?   ?   H . n 
C 2 165 GLU 165 150  ?    ?   ?   H . n 
C 2 166 PRO 166 151  ?    ?   ?   H . n 
C 2 167 ALA 167 152  ?    ?   ?   H . n 
C 2 168 SER 168 153  ?    ?   ?   H . n 
C 2 169 ILE 169 154  ?    ?   ?   H . n 
C 2 170 SER 170 155  ?    ?   ?   H . n 
C 2 171 CYS 171 156  ?    ?   ?   H . n 
C 2 172 ARG 172 157  ?    ?   ?   H . n 
C 2 173 SER 173 158  ?    ?   ?   H . n 
C 2 174 SER 174 159  ?    ?   ?   H . n 
C 2 175 GLN 175 160  ?    ?   ?   H . n 
C 2 176 SER 176 161  ?    ?   ?   H . n 
C 2 177 LEU 177 162  ?    ?   ?   H . n 
C 2 178 LEU 178 163  ?    ?   ?   H . n 
C 2 179 HIS 179 164  ?    ?   ?   H . n 
C 2 180 THR 180 165  ?    ?   ?   H . n 
C 2 181 TYR 181 166  ?    ?   ?   H . n 
C 2 182 GLY 182 167  ?    ?   ?   H . n 
C 2 183 TYR 183 168  ?    ?   ?   H . n 
C 2 184 ASN 184 169  ?    ?   ?   H . n 
C 2 185 CYS 185 170  ?    ?   ?   H . n 
C 2 186 LEU 186 171  ?    ?   ?   H . n 
C 2 187 ASP 187 172  ?    ?   ?   H . n 
C 2 188 TRP 188 173  ?    ?   ?   H . n 
C 2 189 TYR 189 174  ?    ?   ?   H . n 
C 2 190 LEU 190 175  ?    ?   ?   H . n 
C 2 191 GLN 191 176  ?    ?   ?   H . n 
C 2 192 ARG 192 177  ?    ?   ?   H . n 
C 2 193 PRO 193 178  ?    ?   ?   H . n 
C 2 194 GLY 194 179  ?    ?   ?   H . n 
C 2 195 GLN 195 180  ?    ?   ?   H . n 
C 2 196 SER 196 181  ?    ?   ?   H . n 
C 2 197 PRO 197 182  ?    ?   ?   H . n 
C 2 198 GLN 198 183  ?    ?   ?   H . n 
C 2 199 LEU 199 184  ?    ?   ?   H . n 
C 2 200 LEU 200 185  ?    ?   ?   H . n 
C 2 201 ILE 201 186  ?    ?   ?   H . n 
C 2 202 SER 202 187  ?    ?   ?   H . n 
C 2 203 LEU 203 188  ?    ?   ?   H . n 
C 2 204 GLY 204 189  ?    ?   ?   H . n 
C 2 205 SER 205 190  ?    ?   ?   H . n 
C 2 206 TYR 206 191  ?    ?   ?   H . n 
C 2 207 ARG 207 192  ?    ?   ?   H . n 
C 2 208 ALA 208 193  ?    ?   ?   H . n 
C 2 209 SER 209 194  ?    ?   ?   H . n 
C 2 210 GLY 210 195  ?    ?   ?   H . n 
C 2 211 VAL 211 196  ?    ?   ?   H . n 
C 2 212 PRO 212 197  ?    ?   ?   H . n 
C 2 213 ASP 213 198  ?    ?   ?   H . n 
C 2 214 ARG 214 199  ?    ?   ?   H . n 
C 2 215 PHE 215 200  ?    ?   ?   H . n 
C 2 216 SER 216 201  ?    ?   ?   H . n 
C 2 217 GLY 217 202  ?    ?   ?   H . n 
C 2 218 SER 218 203  ?    ?   ?   H . n 
C 2 219 GLY 219 204  ?    ?   ?   H . n 
C 2 220 SER 220 205  ?    ?   ?   H . n 
C 2 221 GLY 221 206  ?    ?   ?   H . n 
C 2 222 THR 222 207  ?    ?   ?   H . n 
C 2 223 ASP 223 208  ?    ?   ?   H . n 
C 2 224 PHE 224 209  ?    ?   ?   H . n 
C 2 225 THR 225 210  ?    ?   ?   H . n 
C 2 226 LEU 226 211  ?    ?   ?   H . n 
C 2 227 LYS 227 212  ?    ?   ?   H . n 
C 2 228 ILE 228 213  ?    ?   ?   H . n 
C 2 229 SER 229 214  ?    ?   ?   H . n 
C 2 230 ARG 230 215  ?    ?   ?   H . n 
C 2 231 VAL 231 216  ?    ?   ?   H . n 
C 2 232 GLU 232 217  ?    ?   ?   H . n 
C 2 233 ALA 233 218  ?    ?   ?   H . n 
C 2 234 GLU 234 219  ?    ?   ?   H . n 
C 2 235 ASP 235 220  ?    ?   ?   H . n 
C 2 236 VAL 236 221  ?    ?   ?   H . n 
C 2 237 GLY 237 222  ?    ?   ?   H . n 
C 2 238 VAL 238 223  ?    ?   ?   H . n 
C 2 239 TYR 239 224  ?    ?   ?   H . n 
C 2 240 TYR 240 225  ?    ?   ?   H . n 
C 2 241 CYS 241 226  ?    ?   ?   H . n 
C 2 242 MET 242 227  ?    ?   ?   H . n 
C 2 243 GLN 243 228  ?    ?   ?   H . n 
C 2 244 ALA 244 229  ?    ?   ?   H . n 
C 2 245 LEU 245 230  ?    ?   ?   H . n 
C 2 246 HIS 246 231  ?    ?   ?   H . n 
C 2 247 PRO 247 232  ?    ?   ?   H . n 
C 2 248 PHE 248 233  ?    ?   ?   H . n 
C 2 249 THR 249 234  ?    ?   ?   H . n 
C 2 250 PHE 250 235  ?    ?   ?   H . n 
C 2 251 GLY 251 236  ?    ?   ?   H . n 
C 2 252 GLY 252 237  ?    ?   ?   H . n 
C 2 253 GLY 253 238  ?    ?   ?   H . n 
C 2 254 THR 254 239  ?    ?   ?   H . n 
C 2 255 LYS 255 240  ?    ?   ?   H . n 
C 2 256 VAL 256 241  ?    ?   ?   H . n 
C 2 257 GLU 257 242  ?    ?   ?   H . n 
C 2 258 ILE 258 243  ?    ?   ?   H . n 
C 2 259 LYS 259 244  ?    ?   ?   H . n 
C 2 260 GLY 260 245  ?    ?   ?   H . n 
C 2 261 PRO 261 246  ?    ?   ?   H . n 
C 2 262 PHE 262 247  ?    ?   ?   H . n 
C 2 263 GLU 263 248  ?    ?   ?   H . n 
C 2 264 ASP 264 249  ?    ?   ?   H . n 
C 2 265 ASP 265 250  ?    ?   ?   H . n 
C 2 266 ASP 266 251  ?    ?   ?   H . n 
C 2 267 ASP 267 252  ?    ?   ?   H . n 
C 2 268 LYS 268 253  ?    ?   ?   H . n 
C 2 269 ALA 269 254  ?    ?   ?   H . n 
C 2 270 GLY 270 255  ?    ?   ?   H . n 
C 2 271 TRP 271 256  ?    ?   ?   H . n 
C 2 272 SER 272 257  ?    ?   ?   H . n 
C 2 273 HIS 273 258  ?    ?   ?   H . n 
C 2 274 PRO 274 259  ?    ?   ?   H . n 
C 2 275 GLN 275 260  ?    ?   ?   H . n 
C 2 276 PHE 276 261  ?    ?   ?   H . n 
C 2 277 GLU 277 262  ?    ?   ?   H . n 
C 2 278 LYS 278 263  ?    ?   ?   H . n 
C 2 279 GLY 279 264  ?    ?   ?   H . n 
C 2 280 GLY 280 265  ?    ?   ?   H . n 
C 2 281 GLY 281 266  ?    ?   ?   H . n 
C 2 282 SER 282 267  ?    ?   ?   H . n 
C 2 283 GLY 283 268  ?    ?   ?   H . n 
C 2 284 GLY 284 269  ?    ?   ?   H . n 
C 2 285 GLY 285 270  ?    ?   ?   H . n 
C 2 286 SER 286 271  ?    ?   ?   H . n 
C 2 287 GLY 287 272  ?    ?   ?   H . n 
C 2 288 GLY 288 273  ?    ?   ?   H . n 
C 2 289 GLY 289 274  ?    ?   ?   H . n 
C 2 290 SER 290 275  ?    ?   ?   H . n 
C 2 291 TRP 291 276  ?    ?   ?   H . n 
C 2 292 SER 292 277  ?    ?   ?   H . n 
C 2 293 HIS 293 278  ?    ?   ?   H . n 
C 2 294 PRO 294 279  ?    ?   ?   H . n 
C 2 295 GLN 295 280  ?    ?   ?   H . n 
C 2 296 PHE 296 281  ?    ?   ?   H . n 
C 2 297 GLU 297 282  ?    ?   ?   H . n 
C 2 298 LYS 298 283  ?    ?   ?   H . n 
D 2 1   ARG 1   -147 ?    ?   ?   L . n 
D 2 2   SER 2   -146 ?    ?   ?   L . n 
D 2 3   GLN 3   -145 ?    ?   ?   L . n 
D 2 4   VAL 4   -144 ?    ?   ?   L . n 
D 2 5   GLN 5   -143 ?    ?   ?   L . n 
D 2 6   LEU 6   -142 ?    ?   ?   L . n 
D 2 7   VAL 7   -141 ?    ?   ?   L . n 
D 2 8   GLU 8   -140 ?    ?   ?   L . n 
D 2 9   SER 9   -139 ?    ?   ?   L . n 
D 2 10  GLY 10  -138 ?    ?   ?   L . n 
D 2 11  GLY 11  -137 ?    ?   ?   L . n 
D 2 12  GLY 12  -136 ?    ?   ?   L . n 
D 2 13  VAL 13  -135 ?    ?   ?   L . n 
D 2 14  VAL 14  -134 ?    ?   ?   L . n 
D 2 15  GLN 15  -133 ?    ?   ?   L . n 
D 2 16  PRO 16  -132 ?    ?   ?   L . n 
D 2 17  GLY 17  -131 ?    ?   ?   L . n 
D 2 18  ARG 18  -130 ?    ?   ?   L . n 
D 2 19  SER 19  -129 ?    ?   ?   L . n 
D 2 20  LEU 20  -128 ?    ?   ?   L . n 
D 2 21  ARG 21  -127 ?    ?   ?   L . n 
D 2 22  LEU 22  -126 ?    ?   ?   L . n 
D 2 23  SER 23  -125 ?    ?   ?   L . n 
D 2 24  CYS 24  -124 ?    ?   ?   L . n 
D 2 25  ALA 25  -123 ?    ?   ?   L . n 
D 2 26  ALA 26  -122 ?    ?   ?   L . n 
D 2 27  SER 27  -121 ?    ?   ?   L . n 
D 2 28  GLY 28  -120 ?    ?   ?   L . n 
D 2 29  PHE 29  -119 ?    ?   ?   L . n 
D 2 30  THR 30  -118 ?    ?   ?   L . n 
D 2 31  PHE 31  -117 ?    ?   ?   L . n 
D 2 32  SER 32  -116 ?    ?   ?   L . n 
D 2 33  SER 33  -115 ?    ?   ?   L . n 
D 2 34  TYR 34  -114 ?    ?   ?   L . n 
D 2 35  ALA 35  -113 ?    ?   ?   L . n 
D 2 36  MET 36  -112 ?    ?   ?   L . n 
D 2 37  HIS 37  -111 ?    ?   ?   L . n 
D 2 38  TRP 38  -110 ?    ?   ?   L . n 
D 2 39  VAL 39  -109 ?    ?   ?   L . n 
D 2 40  ARG 40  -108 ?    ?   ?   L . n 
D 2 41  GLN 41  -107 ?    ?   ?   L . n 
D 2 42  ALA 42  -106 ?    ?   ?   L . n 
D 2 43  PRO 43  -105 ?    ?   ?   L . n 
D 2 44  GLY 44  -104 ?    ?   ?   L . n 
D 2 45  LYS 45  -103 ?    ?   ?   L . n 
D 2 46  GLY 46  -102 ?    ?   ?   L . n 
D 2 47  LEU 47  -101 ?    ?   ?   L . n 
D 2 48  GLU 48  -100 ?    ?   ?   L . n 
D 2 49  TRP 49  -99  ?    ?   ?   L . n 
D 2 50  VAL 50  -98  ?    ?   ?   L . n 
D 2 51  ALA 51  -97  ?    ?   ?   L . n 
D 2 52  VAL 52  -96  ?    ?   ?   L . n 
D 2 53  THR 53  -95  ?    ?   ?   L . n 
D 2 54  TRP 54  -94  ?    ?   ?   L . n 
D 2 55  PHE 55  -93  ?    ?   ?   L . n 
D 2 56  ASP 56  -92  ?    ?   ?   L . n 
D 2 57  VAL 57  -91  ?    ?   ?   L . n 
D 2 58  SER 58  -90  ?    ?   ?   L . n 
D 2 59  LYS 59  -89  ?    ?   ?   L . n 
D 2 60  LYS 60  -88  ?    ?   ?   L . n 
D 2 61  ASP 61  -87  ?    ?   ?   L . n 
D 2 62  TYR 62  -86  ?    ?   ?   L . n 
D 2 63  ALA 63  -85  ?    ?   ?   L . n 
D 2 64  ASP 64  -84  ?    ?   ?   L . n 
D 2 65  SER 65  -83  ?    ?   ?   L . n 
D 2 66  VAL 66  -82  ?    ?   ?   L . n 
D 2 67  LYS 67  -81  ?    ?   ?   L . n 
D 2 68  GLY 68  -80  ?    ?   ?   L . n 
D 2 69  ARG 69  -79  ?    ?   ?   L . n 
D 2 70  PHE 70  -78  ?    ?   ?   L . n 
D 2 71  THR 71  -77  ?    ?   ?   L . n 
D 2 72  ILE 72  -76  ?    ?   ?   L . n 
D 2 73  SER 73  -75  ?    ?   ?   L . n 
D 2 74  ARG 74  -74  ?    ?   ?   L . n 
D 2 75  ASP 75  -73  ?    ?   ?   L . n 
D 2 76  ASN 76  -72  ?    ?   ?   L . n 
D 2 77  SER 77  -71  ?    ?   ?   L . n 
D 2 78  LYS 78  -70  ?    ?   ?   L . n 
D 2 79  ASN 79  -69  ?    ?   ?   L . n 
D 2 80  THR 80  -68  ?    ?   ?   L . n 
D 2 81  LEU 81  -67  ?    ?   ?   L . n 
D 2 82  TYR 82  -66  ?    ?   ?   L . n 
D 2 83  LEU 83  -65  ?    ?   ?   L . n 
D 2 84  GLN 84  -64  ?    ?   ?   L . n 
D 2 85  MET 85  -63  ?    ?   ?   L . n 
D 2 86  ASN 86  -62  ?    ?   ?   L . n 
D 2 87  SER 87  -61  ?    ?   ?   L . n 
D 2 88  LEU 88  -60  ?    ?   ?   L . n 
D 2 89  ARG 89  -59  ?    ?   ?   L . n 
D 2 90  ALA 90  -58  ?    ?   ?   L . n 
D 2 91  GLU 91  -57  ?    ?   ?   L . n 
D 2 92  ASP 92  -56  ?    ?   ?   L . n 
D 2 93  THR 93  -55  ?    ?   ?   L . n 
D 2 94  ALA 94  -54  ?    ?   ?   L . n 
D 2 95  VAL 95  -53  ?    ?   ?   L . n 
D 2 96  TYR 96  -52  ?    ?   ?   L . n 
D 2 97  TYR 97  -51  ?    ?   ?   L . n 
D 2 98  CYS 98  -50  ?    ?   ?   L . n 
D 2 99  ALA 99  -49  ?    ?   ?   L . n 
D 2 100 ARG 100 -48  ?    ?   ?   L . n 
D 2 101 ASN 101 -47  ?    ?   ?   L . n 
D 2 102 LEU 102 -46  ?    ?   ?   L . n 
D 2 103 ILE 103 -45  ?    ?   ?   L . n 
D 2 104 ARG 104 -44  ?    ?   ?   L . n 
D 2 105 TYR 105 -43  ?    ?   ?   L . n 
D 2 106 SER 106 -42  ?    ?   ?   L . n 
D 2 107 GLY 107 -41  ?    ?   ?   L . n 
D 2 108 SER 108 -40  ?    ?   ?   L . n 
D 2 109 TYR 109 -39  ?    ?   ?   L . n 
D 2 110 PHE 110 -38  ?    ?   ?   L . n 
D 2 111 PRO 111 -37  ?    ?   ?   L . n 
D 2 112 VAL 112 -36  ?    ?   ?   L . n 
D 2 113 HIS 113 -35  ?    ?   ?   L . n 
D 2 114 GLY 114 -34  ?    ?   ?   L . n 
D 2 115 MET 115 -33  ?    ?   ?   L . n 
D 2 116 ASP 116 -32  ?    ?   ?   L . n 
D 2 117 VAL 117 -31  ?    ?   ?   L . n 
D 2 118 TRP 118 -30  ?    ?   ?   L . n 
D 2 119 GLY 119 -29  ?    ?   ?   L . n 
D 2 120 GLN 120 -28  ?    ?   ?   L . n 
D 2 121 GLY 121 -27  ?    ?   ?   L . n 
D 2 122 THR 122 -26  ?    ?   ?   L . n 
D 2 123 THR 123 -25  ?    ?   ?   L . n 
D 2 124 VAL 124 -24  ?    ?   ?   L . n 
D 2 125 THR 125 -23  ?    ?   ?   L . n 
D 2 126 VAL 126 -22  ?    ?   ?   L . n 
D 2 127 SER 127 -21  ?    ?   ?   L . n 
D 2 128 SER 128 -20  ?    ?   ?   L . n 
D 2 129 GLY 129 -19  ?    ?   ?   L . n 
D 2 130 THR 130 -18  ?    ?   ?   L . n 
D 2 131 GLY 131 -17  ?    ?   ?   L . n 
D 2 132 GLY 132 -16  ?    ?   ?   L . n 
D 2 133 SER 133 -15  ?    ?   ?   L . n 
D 2 134 GLY 134 -14  ?    ?   ?   L . n 
D 2 135 GLY 135 -13  ?    ?   ?   L . n 
D 2 136 GLY 136 -12  ?    ?   ?   L . n 
D 2 137 GLY 137 -11  ?    ?   ?   L . n 
D 2 138 SER 138 -10  ?    ?   ?   L . n 
D 2 139 GLY 139 -9   ?    ?   ?   L . n 
D 2 140 GLY 140 -8   ?    ?   ?   L . n 
D 2 141 GLY 141 -7   ?    ?   ?   L . n 
D 2 142 GLY 142 -6   ?    ?   ?   L . n 
D 2 143 SER 143 -5   ?    ?   ?   L . n 
D 2 144 GLY 144 -4   ?    ?   ?   L . n 
D 2 145 GLY 145 -3   ?    ?   ?   L . n 
D 2 146 GLY 146 -2   ?    ?   ?   L . n 
D 2 147 ALA 147 -1   ?    ?   ?   L . n 
D 2 148 SER 148 0    ?    ?   ?   L . n 
D 2 149 ASP 149 1    1    ASP ALA L . n 
D 2 150 ILE 150 2    2    ILE ILE L . n 
D 2 151 VAL 151 3    3    VAL VAL L . n 
D 2 152 MET 152 4    4    MET MET L . n 
D 2 153 THR 153 5    5    THR THR L . n 
D 2 154 GLN 154 6    6    GLN GLN L . n 
D 2 155 SER 155 7    7    SER SER L . n 
D 2 156 PRO 156 8    8    PRO PRO L . n 
D 2 157 LEU 157 9    9    LEU LEU L . n 
D 2 158 SER 158 10   10   SER SER L . n 
D 2 159 LEU 159 11   11   LEU LEU L . n 
D 2 160 PRO 160 12   12   PRO PRO L . n 
D 2 161 VAL 161 13   13   VAL VAL L . n 
D 2 162 THR 162 14   14   THR THR L . n 
D 2 163 PRO 163 15   15   PRO PRO L . n 
D 2 164 GLY 164 16   16   GLY GLY L . n 
D 2 165 GLU 165 17   17   GLU GLU L . n 
D 2 166 PRO 166 18   18   PRO PRO L . n 
D 2 167 ALA 167 19   19   ALA ALA L . n 
D 2 168 SER 168 20   20   SER SER L . n 
D 2 169 ILE 169 21   21   ILE ILE L . n 
D 2 170 SER 170 22   22   SER SER L . n 
D 2 171 CYS 171 23   23   CYS CYS L . n 
D 2 172 ARG 172 24   24   ARG ARG L . n 
D 2 173 SER 173 25   25   SER SER L . n 
D 2 174 SER 174 26   26   SER SER L . n 
D 2 175 GLN 175 27   27   GLN GLN L . n 
D 2 176 SER 176 27   27   SER SER L A n 
D 2 177 LEU 177 27   27   LEU LEU L B n 
D 2 178 LEU 178 27   27   LEU LEU L C n 
D 2 179 HIS 179 27   27   HIS HIS L D n 
D 2 180 THR 180 27   27   THR THR L E n 
D 2 181 TYR 181 28   28   TYR TYR L . n 
D 2 182 GLY 182 29   29   GLY GLY L . n 
D 2 183 TYR 183 30   30   TYR TYR L . n 
D 2 184 ASN 184 31   31   ASN ASN L . n 
D 2 185 CYS 185 32   32   CYS CYS L . n 
D 2 186 LEU 186 33   33   LEU LEU L . n 
D 2 187 ASP 187 34   34   ASP ASP L . n 
D 2 188 TRP 188 35   35   TRP TRP L . n 
D 2 189 TYR 189 36   36   TYR TYR L . n 
D 2 190 LEU 190 37   37   LEU LEU L . n 
D 2 191 GLN 191 38   38   GLN GLN L . n 
D 2 192 ARG 192 39   39   ARG ARG L . n 
D 2 193 PRO 193 40   40   PRO PRO L . n 
D 2 194 GLY 194 41   41   GLY GLY L . n 
D 2 195 GLN 195 42   42   GLN GLN L . n 
D 2 196 SER 196 43   43   SER SER L . n 
D 2 197 PRO 197 44   44   PRO PRO L . n 
D 2 198 GLN 198 45   45   GLN GLN L . n 
D 2 199 LEU 199 46   46   LEU LEU L . n 
D 2 200 LEU 200 47   47   LEU LEU L . n 
D 2 201 ILE 201 48   48   ILE ILE L . n 
D 2 202 SER 202 49   49   SER SER L . n 
D 2 203 LEU 203 50   50   LEU LEU L . n 
D 2 204 GLY 204 51   51   GLY GLY L . n 
D 2 205 SER 205 52   52   SER SER L . n 
D 2 206 TYR 206 53   53   TYR TYR L . n 
D 2 207 ARG 207 54   54   ARG ARG L . n 
D 2 208 ALA 208 55   55   ALA ALA L . n 
D 2 209 SER 209 56   56   SER SER L . n 
D 2 210 GLY 210 57   57   GLY GLY L . n 
D 2 211 VAL 211 58   58   VAL VAL L . n 
D 2 212 PRO 212 59   59   PRO PRO L . n 
D 2 213 ASP 213 60   60   ASP ASP L . n 
D 2 214 ARG 214 61   61   ARG ARG L . n 
D 2 215 PHE 215 62   62   PHE PHE L . n 
D 2 216 SER 216 63   63   SER SER L . n 
D 2 217 GLY 217 64   64   GLY GLY L . n 
D 2 218 SER 218 65   65   SER SER L . n 
D 2 219 GLY 219 66   66   GLY GLY L . n 
D 2 220 SER 220 67   67   SER SER L . n 
D 2 221 GLY 221 68   68   GLY GLY L . n 
D 2 222 THR 222 69   69   THR THR L . n 
D 2 223 ASP 223 70   70   ASP ASP L . n 
D 2 224 PHE 224 71   71   PHE PHE L . n 
D 2 225 THR 225 72   72   THR THR L . n 
D 2 226 LEU 226 73   73   LEU LEU L . n 
D 2 227 LYS 227 74   74   LYS LYS L . n 
D 2 228 ILE 228 75   75   ILE ILE L . n 
D 2 229 SER 229 76   76   SER SER L . n 
D 2 230 ARG 230 77   77   ARG ARG L . n 
D 2 231 VAL 231 78   78   VAL VAL L . n 
D 2 232 GLU 232 79   79   GLU GLU L . n 
D 2 233 ALA 233 80   80   ALA ALA L . n 
D 2 234 GLU 234 81   81   GLU GLU L . n 
D 2 235 ASP 235 82   82   ASP ASP L . n 
D 2 236 VAL 236 83   83   VAL VAL L . n 
D 2 237 GLY 237 84   84   GLY GLY L . n 
D 2 238 VAL 238 85   85   VAL VAL L . n 
D 2 239 TYR 239 86   86   TYR TYR L . n 
D 2 240 TYR 240 87   87   TYR TYR L . n 
D 2 241 CYS 241 88   88   CYS CYS L . n 
D 2 242 MET 242 89   89   MET MET L . n 
D 2 243 GLN 243 90   90   GLN GLN L . n 
D 2 244 ALA 244 91   91   ALA ALA L . n 
D 2 245 LEU 245 92   92   LEU LEU L . n 
D 2 246 HIS 246 93   93   HIS HIS L . n 
D 2 247 PRO 247 94   94   PRO PRO L . n 
D 2 248 PHE 248 95   95   PHE PHE L . n 
D 2 249 THR 249 96   96   THR THR L . n 
D 2 250 PHE 250 97   97   PHE PHE L . n 
D 2 251 GLY 251 98   98   GLY GLY L . n 
D 2 252 GLY 252 99   99   GLY GLY L . n 
D 2 253 GLY 253 100  100  GLY GLY L . n 
D 2 254 THR 254 101  101  THR THR L . n 
D 2 255 LYS 255 102  102  LYS LYS L . n 
D 2 256 VAL 256 103  103  VAL VAL L . n 
D 2 257 GLU 257 104  104  GLU GLU L . n 
D 2 258 ILE 258 105  ?    ?   ?   L . n 
D 2 259 LYS 259 106  ?    ?   ?   L . n 
D 2 260 GLY 260 107  ?    ?   ?   L . n 
D 2 261 PRO 261 108  ?    ?   ?   L . n 
D 2 262 PHE 262 109  ?    ?   ?   L . n 
D 2 263 GLU 263 110  ?    ?   ?   L . n 
D 2 264 ASP 264 111  ?    ?   ?   L . n 
D 2 265 ASP 265 112  ?    ?   ?   L . n 
D 2 266 ASP 266 113  ?    ?   ?   L . n 
D 2 267 ASP 267 114  ?    ?   ?   L . n 
D 2 268 LYS 268 115  ?    ?   ?   L . n 
D 2 269 ALA 269 116  ?    ?   ?   L . n 
D 2 270 GLY 270 117  ?    ?   ?   L . n 
D 2 271 TRP 271 118  ?    ?   ?   L . n 
D 2 272 SER 272 119  ?    ?   ?   L . n 
D 2 273 HIS 273 120  ?    ?   ?   L . n 
D 2 274 PRO 274 121  ?    ?   ?   L . n 
D 2 275 GLN 275 122  ?    ?   ?   L . n 
D 2 276 PHE 276 123  ?    ?   ?   L . n 
D 2 277 GLU 277 124  ?    ?   ?   L . n 
D 2 278 LYS 278 125  ?    ?   ?   L . n 
D 2 279 GLY 279 126  ?    ?   ?   L . n 
D 2 280 GLY 280 127  ?    ?   ?   L . n 
D 2 281 GLY 281 128  ?    ?   ?   L . n 
D 2 282 SER 282 129  ?    ?   ?   L . n 
D 2 283 GLY 283 130  ?    ?   ?   L . n 
D 2 284 GLY 284 131  ?    ?   ?   L . n 
D 2 285 GLY 285 132  ?    ?   ?   L . n 
D 2 286 SER 286 133  ?    ?   ?   L . n 
D 2 287 GLY 287 134  ?    ?   ?   L . n 
D 2 288 GLY 288 135  ?    ?   ?   L . n 
D 2 289 GLY 289 136  ?    ?   ?   L . n 
D 2 290 SER 290 137  ?    ?   ?   L . n 
D 2 291 TRP 291 138  ?    ?   ?   L . n 
D 2 292 SER 292 139  ?    ?   ?   L . n 
D 2 293 HIS 293 140  ?    ?   ?   L . n 
D 2 294 PRO 294 141  ?    ?   ?   L . n 
D 2 295 GLN 295 142  ?    ?   ?   L . n 
D 2 296 PHE 296 143  ?    ?   ?   L . n 
D 2 297 GLU 297 144  ?    ?   ?   L . n 
D 2 298 LYS 298 145  ?    ?   ?   L . n 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              guardado@pasteur.fr 
_pdbx_contact_author.name_first         Pablo 
_pdbx_contact_author.name_last          GUARDADO-CALVO 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-7292-5270 
# 
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 
H 5 GOL 1  1001 1  GOL GOL A . 
I 6 HOH 1  1101 12 HOH HOH A . 
I 6 HOH 2  1102 11 HOH HOH A . 
I 6 HOH 3  1103 9  HOH HOH A . 
I 6 HOH 4  1104 4  HOH HOH A . 
I 6 HOH 5  1105 14 HOH HOH A . 
I 6 HOH 6  1106 19 HOH HOH A . 
I 6 HOH 7  1107 26 HOH HOH A . 
I 6 HOH 8  1108 24 HOH HOH A . 
I 6 HOH 9  1109 17 HOH HOH A . 
I 6 HOH 10 1110 23 HOH HOH A . 
I 6 HOH 11 1111 22 HOH HOH A . 
J 6 HOH 1  1201 8  HOH HOH B . 
J 6 HOH 2  1202 7  HOH HOH B . 
J 6 HOH 3  1203 15 HOH HOH B . 
J 6 HOH 4  1204 5  HOH HOH B . 
J 6 HOH 5  1205 3  HOH HOH B . 
J 6 HOH 6  1206 21 HOH HOH B . 
J 6 HOH 7  1207 2  HOH HOH B . 
J 6 HOH 8  1208 10 HOH HOH B . 
J 6 HOH 9  1209 6  HOH HOH B . 
J 6 HOH 10 1210 18 HOH HOH B . 
J 6 HOH 11 1211 20 HOH HOH B . 
J 6 HOH 12 1212 1  HOH HOH B . 
J 6 HOH 13 1213 16 HOH HOH B . 
K 6 HOH 1  301  25 HOH HOH H . 
L 6 HOH 1  201  27 HOH HOH L . 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L 
# 
_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 
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2023-06-21 
# 
_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_
_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 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .     1 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? Aimless     ? ? ? 0.7.4 2 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX      ? ? ? 1.18  3 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.27  4 
# 
_pdbx_entry_details.entry_id                 7QQB 
_pdbx_entry_details.has_ligand_of_interest   N 
_pdbx_entry_details.compound_details         ? 
_pdbx_entry_details.source_details           ? 
_pdbx_entry_details.nonpolymer_details       ? 
_pdbx_entry_details.sequence_details         ? 
# 
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 SER A 66   ? ? -94.96  -79.96  
2  1 ASN A 69   ? ? -105.47 58.69   
3  1 ASP A 92   ? ? -96.03  49.93   
4  1 LEU A 122  ? ? 70.30   -8.19   
5  1 ASN A 142  ? ? -107.90 -150.62 
6  1 LYS A 163  ? ? 63.30   -60.51  
7  1 SER A 206  ? ? -79.79  -159.33 
8  1 HIS A 207  ? ? -111.97 -92.59  
9  1 TYR A 209  ? ? -146.32 -141.10 
10 1 THR A 227  ? ? -131.96 -50.87  
11 1 ASP A 248  ? ? -98.55  49.07   
12 1 HIS A 292  ? ? -108.22 49.78   
13 1 GLU A 295  ? ? -68.36  9.93    
14 1 ASN A 297  ? ? 69.83   -41.51  
15 1 LEU A 331  ? ? -124.25 -70.17  
16 1 SER B 692  ? ? 57.91   16.46   
17 1 ASN B 706  ? ? 56.54   79.65   
18 1 SER B 853  ? ? 68.73   -0.38   
19 1 THR B 874  ? ? -134.86 -84.51  
20 1 THR B 909  ? ? -135.30 -59.70  
21 1 SER B 944  ? ? -122.28 -168.69 
22 1 SER B 946  ? ? -140.00 -6.54   
23 1 GLU B 976  ? ? -60.69  -72.31  
24 1 TRP B 992  ? ? -93.52  -152.74 
25 1 GLU B 1008 ? ? 63.23   -57.54  
26 1 ASP B 1020 ? ? -115.35 -143.77 
27 1 LYS B 1044 ? ? -161.19 116.83  
28 1 ASP B 1057 ? ? 57.96   -85.12  
29 1 ARG H 16   ? ? -83.11  -150.63 
30 1 PHE H 52   A ? 52.83   76.19   
31 1 ASP H 53   ? ? 52.85   -124.49 
32 1 PRO L 8    ? ? -12.57  116.49  
33 1 ARG L 77   ? ? 50.77   78.18   
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   SER 
_pdbx_validate_peptide_omega.auth_asym_id_1   L 
_pdbx_validate_peptide_omega.auth_seq_id_1    7 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   PRO 
_pdbx_validate_peptide_omega.auth_asym_id_2   L 
_pdbx_validate_peptide_omega.auth_seq_id_2    8 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            -133.26 
# 
_pdbx_validate_polymer_linkage.id               1 
_pdbx_validate_polymer_linkage.PDB_model_num    1 
_pdbx_validate_polymer_linkage.auth_atom_id_1   C 
_pdbx_validate_polymer_linkage.auth_asym_id_1   L 
_pdbx_validate_polymer_linkage.auth_comp_id_1   PRO 
_pdbx_validate_polymer_linkage.auth_seq_id_1    94 
_pdbx_validate_polymer_linkage.PDB_ins_code_1   ? 
_pdbx_validate_polymer_linkage.label_alt_id_1   ? 
_pdbx_validate_polymer_linkage.auth_atom_id_2   N 
_pdbx_validate_polymer_linkage.auth_asym_id_2   L 
_pdbx_validate_polymer_linkage.auth_comp_id_2   PHE 
_pdbx_validate_polymer_linkage.auth_seq_id_2    95 
_pdbx_validate_polymer_linkage.PDB_ins_code_2   ? 
_pdbx_validate_polymer_linkage.label_alt_id_2   ? 
_pdbx_validate_polymer_linkage.dist             3.01 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 L ASP 1 ? CG  ? D ASP 149 CG  
2 1 Y 1 L ASP 1 ? OD1 ? D ASP 149 OD1 
3 1 Y 1 L ASP 1 ? OD2 ? D ASP 149 OD2 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1    1 Y 1 A ARG 18   ? A ARG 1   
2    1 Y 1 A SER 19   ? A SER 2   
3    1 Y 1 A SER 20   ? A SER 3   
4    1 Y 1 A ARG 21   ? A ARG 4   
5    1 Y 1 A GLY 22   ? A GLY 5   
6    1 Y 1 A ASP 23   ? A ASP 6   
7    1 Y 1 A THR 24   ? A THR 7   
8    1 Y 1 A ARG 25   ? A ARG 8   
9    1 Y 1 A MET 200  ? A MET 183 
10   1 Y 1 A ALA 201  ? A ALA 184 
11   1 Y 1 A LEU 202  ? A LEU 185 
12   1 Y 1 A SER 203  ? A SER 186 
13   1 Y 1 A GLY 382  ? A GLY 365 
14   1 Y 1 A GLY 383  ? A GLY 366 
15   1 Y 1 A SER 384  ? A SER 367 
16   1 Y 1 A GLY 385  ? A GLY 368 
17   1 Y 1 A LEU 386  ? A LEU 369 
18   1 Y 1 A VAL 387  ? A VAL 370 
19   1 Y 1 A PRO 388  ? A PRO 371 
20   1 Y 1 A ARG 389  ? A ARG 372 
21   1 Y 1 A GLY 390  ? A GLY 373 
22   1 Y 1 A SER 391  ? A SER 374 
23   1 Y 1 A GLY 392  ? A GLY 375 
24   1 Y 1 A GLY 393  ? A GLY 376 
25   1 Y 1 A GLY 394  ? A GLY 377 
26   1 Y 1 A SER 395  ? A SER 378 
27   1 Y 1 A GLY 396  ? A GLY 379 
28   1 Y 1 A GLY 397  ? A GLY 380 
29   1 Y 1 A GLY 398  ? A GLY 381 
30   1 Y 1 A SER 399  ? A SER 382 
31   1 Y 1 A TRP 400  ? A TRP 383 
32   1 Y 1 A SER 401  ? A SER 384 
33   1 Y 1 A HIS 402  ? A HIS 385 
34   1 Y 1 A PRO 403  ? A PRO 386 
35   1 Y 1 A GLN 404  ? A GLN 387 
36   1 Y 1 A PHE 405  ? A PHE 388 
37   1 Y 1 A GLU 406  ? A GLU 389 
38   1 Y 1 A LYS 407  ? A LYS 390 
39   1 Y 1 A GLY 408  ? A GLY 391 
40   1 Y 1 A GLY 409  ? A GLY 392 
41   1 Y 1 A GLY 410  ? A GLY 393 
42   1 Y 1 A THR 411  ? A THR 394 
43   1 Y 1 A GLY 412  ? A GLY 395 
44   1 Y 1 A GLY 413  ? A GLY 396 
45   1 Y 1 A GLY 414  ? A GLY 397 
46   1 Y 1 A THR 415  ? A THR 398 
47   1 Y 1 A LEU 416  ? A LEU 399 
48   1 Y 1 A VAL 417  ? A VAL 400 
49   1 Y 1 A PRO 418  ? A PRO 401 
50   1 Y 1 A ARG 419  ? A ARG 402 
51   1 Y 1 A GLY 420  ? A GLY 403 
52   1 Y 1 A SER 421  ? A SER 404 
53   1 Y 1 A GLY 422  ? A GLY 405 
54   1 Y 1 A THR 423  ? A THR 406 
55   1 Y 1 A GLY 424  ? A GLY 407 
56   1 Y 1 A GLY 425  ? A GLY 408 
57   1 Y 1 A GLU 426  ? A GLU 409 
58   1 Y 1 A THR 427  ? A THR 410 
59   1 Y 1 A GLN 428  ? A GLN 411 
60   1 Y 1 A ASN 429  ? A ASN 412 
61   1 Y 1 A LEU 430  ? A LEU 413 
62   1 Y 1 A ASN 431  ? A ASN 414 
63   1 Y 1 A SER 432  ? A SER 415 
64   1 Y 1 A GLY 433  ? A GLY 416 
65   1 Y 1 A TRP 434  ? A TRP 417 
66   1 Y 1 A THR 435  ? A THR 418 
67   1 Y 1 A ASP 436  ? A ASP 419 
68   1 Y 1 A THR 437  ? A THR 420 
69   1 Y 1 A ALA 438  ? A ALA 421 
70   1 Y 1 A HIS 439  ? A HIS 422 
71   1 Y 1 A GLY 440  ? A GLY 423 
72   1 Y 1 A SER 441  ? A SER 424 
73   1 Y 1 A GLY 442  ? A GLY 425 
74   1 Y 1 A VAL 443  ? A VAL 426 
75   1 Y 1 A ILE 444  ? A ILE 427 
76   1 Y 1 A PRO 445  ? A PRO 428 
77   1 Y 1 A MET 446  ? A MET 429 
78   1 Y 1 A ARG 447  ? A ARG 430 
79   1 Y 1 A THR 448  ? A THR 431 
80   1 Y 1 A ASP 449  ? A ASP 432 
81   1 Y 1 A LEU 450  ? A LEU 433 
82   1 Y 1 A GLU 451  ? A GLU 434 
83   1 Y 1 A LEU 452  ? A LEU 435 
84   1 Y 1 A ASP 453  ? A ASP 436 
85   1 Y 1 A PHE 454  ? A PHE 437 
86   1 Y 1 A SER 455  ? A SER 438 
87   1 Y 1 A LEU 456  ? A LEU 439 
88   1 Y 1 A PRO 457  ? A PRO 440 
89   1 Y 1 A SER 458  ? A SER 441 
90   1 Y 1 A SER 459  ? A SER 442 
91   1 Y 1 A ALA 460  ? A ALA 443 
92   1 Y 1 A SER 461  ? A SER 444 
93   1 Y 1 A TYR 462  ? A TYR 445 
94   1 Y 1 A THR 463  ? A THR 446 
95   1 Y 1 A TYR 464  ? A TYR 447 
96   1 Y 1 A ARG 465  ? A ARG 448 
97   1 Y 1 A ARG 466  ? A ARG 449 
98   1 Y 1 A GLN 467  ? A GLN 450 
99   1 Y 1 A LEU 468  ? A LEU 451 
100  1 Y 1 A GLN 469  ? A GLN 452 
101  1 Y 1 A ASN 470  ? A ASN 453 
102  1 Y 1 A PRO 471  ? A PRO 454 
103  1 Y 1 A ALA 472  ? A ALA 455 
104  1 Y 1 A ASN 473  ? A ASN 456 
105  1 Y 1 A GLU 474  ? A GLU 457 
106  1 Y 1 A GLN 475  ? A GLN 458 
107  1 Y 1 A GLU 476  ? A GLU 459 
108  1 Y 1 A LYS 477  ? A LYS 460 
109  1 Y 1 A ILE 478  ? A ILE 461 
110  1 Y 1 A PRO 479  ? A PRO 462 
111  1 Y 1 A PHE 480  ? A PHE 463 
112  1 Y 1 A HIS 481  ? A HIS 464 
113  1 Y 1 A LEU 482  ? A LEU 465 
114  1 Y 1 A GLN 483  ? A GLN 466 
115  1 Y 1 A ILE 484  ? A ILE 467 
116  1 Y 1 A SER 485  ? A SER 468 
117  1 Y 1 A LYS 486  ? A LYS 469 
118  1 Y 1 A GLN 487  ? A GLN 470 
119  1 Y 1 A VAL 488  ? A VAL 471 
120  1 Y 1 A ILE 489  ? A ILE 472 
121  1 Y 1 A HIS 490  ? A HIS 473 
122  1 Y 1 A ALA 491  ? A ALA 474 
123  1 Y 1 A GLU 492  ? A GLU 475 
124  1 Y 1 A ILE 493  ? A ILE 476 
125  1 Y 1 A GLN 494  ? A GLN 477 
126  1 Y 1 A HIS 495  ? A HIS 478 
127  1 Y 1 A LEU 496  ? A LEU 479 
128  1 Y 1 A GLY 497  ? A GLY 480 
129  1 Y 1 A HIS 498  ? A HIS 481 
130  1 Y 1 A TRP 499  ? A TRP 482 
131  1 Y 1 A MET 500  ? A MET 483 
132  1 Y 1 A ASP 501  ? A ASP 484 
133  1 Y 1 A GLY 502  ? A GLY 485 
134  1 Y 1 A THR 503  ? A THR 486 
135  1 Y 1 A PHE 504  ? A PHE 487 
136  1 Y 1 A ASN 505  ? A ASN 488 
137  1 Y 1 A LEU 506  ? A LEU 489 
138  1 Y 1 A LYS 507  ? A LYS 490 
139  1 Y 1 A THR 508  ? A THR 491 
140  1 Y 1 A ALA 509  ? A ALA 492 
141  1 Y 1 A PHE 510  ? A PHE 493 
142  1 Y 1 A HIS 511  ? A HIS 494 
143  1 Y 1 A CYS 512  ? A CYS 495 
144  1 Y 1 A TYR 513  ? A TYR 496 
145  1 Y 1 A GLY 514  ? A GLY 497 
146  1 Y 1 A SER 515  ? A SER 498 
147  1 Y 1 A CYS 516  ? A CYS 499 
148  1 Y 1 A GLU 517  ? A GLU 500 
149  1 Y 1 A LYS 518  ? A LYS 501 
150  1 Y 1 A TYR 519  ? A TYR 502 
151  1 Y 1 A ALA 520  ? A ALA 503 
152  1 Y 1 A TYR 521  ? A TYR 504 
153  1 Y 1 A PRO 522  ? A PRO 505 
154  1 Y 1 A TRP 523  ? A TRP 506 
155  1 Y 1 A GLN 524  ? A GLN 507 
156  1 Y 1 A THR 525  ? A THR 508 
157  1 Y 1 A ALA 526  ? A ALA 509 
158  1 Y 1 A GLY 527  ? A GLY 510 
159  1 Y 1 A CYS 528  ? A CYS 511 
160  1 Y 1 A PHE 529  ? A PHE 512 
161  1 Y 1 A VAL 530  ? A VAL 513 
162  1 Y 1 A GLU 531  ? A GLU 514 
163  1 Y 1 A LYS 532  ? A LYS 515 
164  1 Y 1 A ASP 533  ? A ASP 516 
165  1 Y 1 A TYR 534  ? A TYR 517 
166  1 Y 1 A GLU 535  ? A GLU 518 
167  1 Y 1 A TYR 536  ? A TYR 519 
168  1 Y 1 A GLU 537  ? A GLU 520 
169  1 Y 1 A SER 538  ? A SER 521 
170  1 Y 1 A GLY 539  ? A GLY 522 
171  1 Y 1 A TRP 540  ? A TRP 523 
172  1 Y 1 A GLY 541  ? A GLY 524 
173  1 Y 1 A CYS 542  ? A CYS 525 
174  1 Y 1 A ASN 543  ? A ASN 526 
175  1 Y 1 A PRO 544  ? A PRO 527 
176  1 Y 1 A ALA 545  ? A ALA 528 
177  1 Y 1 A ASP 546  ? A ASP 529 
178  1 Y 1 A CYS 547  ? A CYS 530 
179  1 Y 1 A PRO 548  ? A PRO 531 
180  1 Y 1 A GLY 549  ? A GLY 532 
181  1 Y 1 A VAL 550  ? A VAL 533 
182  1 Y 1 A GLY 551  ? A GLY 534 
183  1 Y 1 A THR 552  ? A THR 535 
184  1 Y 1 A GLY 553  ? A GLY 536 
185  1 Y 1 A CYS 554  ? A CYS 537 
186  1 Y 1 A THR 555  ? A THR 538 
187  1 Y 1 A ALA 556  ? A ALA 539 
188  1 Y 1 A CYS 557  ? A CYS 540 
189  1 Y 1 A GLY 558  ? A GLY 541 
190  1 Y 1 A VAL 559  ? A VAL 542 
191  1 Y 1 A TYR 560  ? A TYR 543 
192  1 Y 1 A LEU 561  ? A LEU 544 
193  1 Y 1 A ASP 562  ? A ASP 545 
194  1 Y 1 A LYS 563  ? A LYS 546 
195  1 Y 1 A LEU 564  ? A LEU 547 
196  1 Y 1 A LYS 565  ? A LYS 548 
197  1 Y 1 A SER 566  ? A SER 549 
198  1 Y 1 A VAL 567  ? A VAL 550 
199  1 Y 1 A GLY 568  ? A GLY 551 
200  1 Y 1 A LYS 569  ? A LYS 552 
201  1 Y 1 A ALA 570  ? A ALA 553 
202  1 Y 1 A PHE 571  ? A PHE 554 
203  1 Y 1 A LYS 572  ? A LYS 555 
204  1 Y 1 A ILE 573  ? A ILE 556 
205  1 Y 1 A VAL 574  ? A VAL 557 
206  1 Y 1 A SER 575  ? A SER 558 
207  1 Y 1 A LEU 576  ? A LEU 559 
208  1 Y 1 A ARG 577  ? A ARG 560 
209  1 Y 1 A TYR 578  ? A TYR 561 
210  1 Y 1 A THR 579  ? A THR 562 
211  1 Y 1 A ARG 580  ? A ARG 563 
212  1 Y 1 A LYS 581  ? A LYS 564 
213  1 Y 1 A ALA 582  ? A ALA 565 
214  1 Y 1 A CYS 583  ? A CYS 566 
215  1 Y 1 A ILE 584  ? A ILE 567 
216  1 Y 1 A GLN 585  ? A GLN 568 
217  1 Y 1 A LEU 586  ? A LEU 569 
218  1 Y 1 A GLY 587  ? A GLY 570 
219  1 Y 1 A THR 588  ? A THR 571 
220  1 Y 1 A GLU 589  ? A GLU 572 
221  1 Y 1 A GLN 590  ? A GLN 573 
222  1 Y 1 A THR 591  ? A THR 574 
223  1 Y 1 A CYS 592  ? A CYS 575 
224  1 Y 1 A LYS 593  ? A LYS 576 
225  1 Y 1 A ASN 594  ? A ASN 577 
226  1 Y 1 A VAL 595  ? A VAL 578 
227  1 Y 1 A ASP 596  ? A ASP 579 
228  1 Y 1 A SER 597  ? A SER 580 
229  1 Y 1 A ASN 598  ? A ASN 581 
230  1 Y 1 A ASP 599  ? A ASP 582 
231  1 Y 1 A CYS 600  ? A CYS 583 
232  1 Y 1 A LEU 601  ? A LEU 584 
233  1 Y 1 A VAL 602  ? A VAL 585 
234  1 Y 1 A THR 603  ? A THR 586 
235  1 Y 1 A THR 604  ? A THR 587 
236  1 Y 1 A SER 605  ? A SER 588 
237  1 Y 1 A VAL 606  ? A VAL 589 
238  1 Y 1 A LYS 607  ? A LYS 590 
239  1 Y 1 A VAL 608  ? A VAL 591 
240  1 Y 1 A CYS 609  ? A CYS 592 
241  1 Y 1 A LEU 610  ? A LEU 593 
242  1 Y 1 A ILE 611  ? A ILE 594 
243  1 Y 1 A GLY 612  ? A GLY 595 
244  1 Y 1 A THR 613  ? A THR 596 
245  1 Y 1 A VAL 614  ? A VAL 597 
246  1 Y 1 A SER 615  ? A SER 598 
247  1 Y 1 A LYS 616  ? A LYS 599 
248  1 Y 1 A PHE 617  ? A PHE 600 
249  1 Y 1 A GLN 618  ? A GLN 601 
250  1 Y 1 A PRO 619  ? A PRO 602 
251  1 Y 1 A SER 620  ? A SER 603 
252  1 Y 1 A ASP 621  ? A ASP 604 
253  1 Y 1 A THR 622  ? A THR 605 
254  1 Y 1 A LEU 623  ? A LEU 606 
255  1 Y 1 A LEU 624  ? A LEU 607 
256  1 Y 1 A PHE 625  ? A PHE 608 
257  1 Y 1 A LEU 626  ? A LEU 609 
258  1 Y 1 A GLY 627  ? A GLY 610 
259  1 Y 1 A PRO 628  ? A PRO 611 
260  1 Y 1 A LEU 629  ? A LEU 612 
261  1 Y 1 A GLU 630  ? A GLU 613 
262  1 Y 1 A GLN 631  ? A GLN 614 
263  1 Y 1 A GLY 632  ? A GLY 615 
264  1 Y 1 A GLY 633  ? A GLY 616 
265  1 Y 1 A LEU 634  ? A LEU 617 
266  1 Y 1 A ILE 635  ? A ILE 618 
267  1 Y 1 A PHE 636  ? A PHE 619 
268  1 Y 1 A LYS 637  ? A LYS 620 
269  1 Y 1 A GLN 638  ? A GLN 621 
270  1 Y 1 A TRP 639  ? A TRP 622 
271  1 Y 1 A CYS 640  ? A CYS 623 
272  1 Y 1 A THR 641  ? A THR 624 
273  1 Y 1 A THR 642  ? A THR 625 
274  1 Y 1 A THR 643  ? A THR 626 
275  1 Y 1 A CYS 644  ? A CYS 627 
276  1 Y 1 A GLN 645  ? A GLN 628 
277  1 Y 1 A PHE 646  ? A PHE 629 
278  1 Y 1 A GLY 647  ? A GLY 630 
279  1 Y 1 A ASP 648  ? A ASP 631 
280  1 Y 1 A PRO 649  ? A PRO 632 
281  1 Y 1 A GLY 650  ? A GLY 633 
282  1 Y 1 A ASP 651  ? A ASP 634 
283  1 Y 1 A ILE 652  ? A ILE 635 
284  1 Y 1 A MET 653  ? A MET 636 
285  1 Y 1 A SER 654  ? A SER 637 
286  1 Y 1 A THR 655  ? A THR 638 
287  1 Y 1 A PRO 656  ? A PRO 639 
288  1 Y 1 A VAL 657  ? A VAL 640 
289  1 Y 1 A GLY 658  ? A GLY 641 
290  1 Y 1 A MET 659  ? A MET 642 
291  1 Y 1 A LYS 660  ? A LYS 643 
292  1 Y 1 A CYS 661  ? A CYS 644 
293  1 Y 1 A PRO 662  ? A PRO 645 
294  1 Y 1 A GLU 663  ? A GLU 646 
295  1 Y 1 A LEU 664  ? A LEU 647 
296  1 Y 1 A SER 665  ? A SER 648 
297  1 Y 1 A GLY 666  ? A GLY 649 
298  1 Y 1 A SER 667  ? A SER 650 
299  1 Y 1 A PHE 668  ? A PHE 651 
300  1 Y 1 A ARG 669  ? A ARG 652 
301  1 Y 1 A LYS 670  ? A LYS 653 
302  1 Y 1 A LYS 671  ? A LYS 654 
303  1 Y 1 A CYS 672  ? A CYS 655 
304  1 Y 1 A ALA 673  ? A ALA 656 
305  1 Y 1 A PHE 674  ? A PHE 657 
306  1 Y 1 A ALA 675  ? A ALA 658 
307  1 Y 1 A THR 676  ? A THR 659 
308  1 Y 1 A THR 677  ? A THR 660 
309  1 Y 1 A PRO 678  ? A PRO 661 
310  1 Y 1 A VAL 679  ? A VAL 662 
311  1 Y 1 A CYS 680  ? A CYS 663 
312  1 Y 1 A GLN 681  ? A GLN 664 
313  1 Y 1 A PHE 682  ? A PHE 665 
314  1 Y 1 A ASP 683  ? A ASP 666 
315  1 Y 1 A GLY 684  ? A GLY 667 
316  1 Y 1 A ASN 685  ? A ASN 668 
317  1 Y 1 A THR 686  ? A THR 669 
318  1 Y 1 A ILE 687  ? A ILE 670 
319  1 Y 1 A SER 688  ? A SER 671 
320  1 Y 1 A GLY 689  ? A GLY 672 
321  1 Y 1 A TYR 690  ? A TYR 673 
322  1 Y 1 A LYS 691  ? A LYS 674 
323  1 Y 1 A ARG 692  ? A ARG 675 
324  1 Y 1 A MET 693  ? A MET 676 
325  1 Y 1 A ILE 694  ? A ILE 677 
326  1 Y 1 A ALA 695  ? A ALA 678 
327  1 Y 1 A THR 696  ? A THR 679 
328  1 Y 1 A LYS 697  ? A LYS 680 
329  1 Y 1 A ASP 698  ? A ASP 681 
330  1 Y 1 A SER 699  ? A SER 682 
331  1 Y 1 A PHE 700  ? A PHE 683 
332  1 Y 1 A GLN 701  ? A GLN 684 
333  1 Y 1 A SER 702  ? A SER 685 
334  1 Y 1 A PHE 703  ? A PHE 686 
335  1 Y 1 A ASN 704  ? A ASN 687 
336  1 Y 1 A VAL 705  ? A VAL 688 
337  1 Y 1 A THR 706  ? A THR 689 
338  1 Y 1 A GLU 707  ? A GLU 690 
339  1 Y 1 A PRO 708  ? A PRO 691 
340  1 Y 1 A HIS 709  ? A HIS 692 
341  1 Y 1 A ILE 710  ? A ILE 693 
342  1 Y 1 A SER 711  ? A SER 694 
343  1 Y 1 A ALA 712  ? A ALA 695 
344  1 Y 1 A SER 713  ? A SER 696 
345  1 Y 1 A SER 714  ? A SER 697 
346  1 Y 1 A LEU 715  ? A LEU 698 
347  1 Y 1 A GLU 716  ? A GLU 699 
348  1 Y 1 A TRP 717  ? A TRP 700 
349  1 Y 1 A ILE 718  ? A ILE 701 
350  1 Y 1 A ASP 719  ? A ASP 702 
351  1 Y 1 A PRO 720  ? A PRO 703 
352  1 Y 1 A ASP 721  ? A ASP 704 
353  1 Y 1 A SER 722  ? A SER 705 
354  1 Y 1 A SER 723  ? A SER 706 
355  1 Y 1 A LEU 724  ? A LEU 707 
356  1 Y 1 A ARG 725  ? A ARG 708 
357  1 Y 1 A ASP 726  ? A ASP 709 
358  1 Y 1 A HIS 727  ? A HIS 710 
359  1 Y 1 A ILE 728  ? A ILE 711 
360  1 Y 1 A ASN 729  ? A ASN 712 
361  1 Y 1 A VAL 730  ? A VAL 713 
362  1 Y 1 A ILE 731  ? A ILE 714 
363  1 Y 1 A VAL 732  ? A VAL 715 
364  1 Y 1 A GLY 733  ? A GLY 716 
365  1 Y 1 A ARG 734  ? A ARG 717 
366  1 Y 1 A ASP 735  ? A ASP 718 
367  1 Y 1 A LEU 736  ? A LEU 719 
368  1 Y 1 A SER 737  ? A SER 720 
369  1 Y 1 A PHE 738  ? A PHE 721 
370  1 Y 1 A GLN 739  ? A GLN 722 
371  1 Y 1 A ASP 740  ? A ASP 723 
372  1 Y 1 A LEU 741  ? A LEU 724 
373  1 Y 1 A SER 742  ? A SER 725 
374  1 Y 1 A GLU 743  ? A GLU 726 
375  1 Y 1 A THR 744  ? A THR 727 
376  1 Y 1 A PRO 745  ? A PRO 728 
377  1 Y 1 A CYS 746  ? A CYS 729 
378  1 Y 1 A GLN 747  ? A GLN 730 
379  1 Y 1 A VAL 748  ? A VAL 731 
380  1 Y 1 A ASP 749  ? A ASP 732 
381  1 Y 1 A LEU 750  ? A LEU 733 
382  1 Y 1 A THR 751  ? A THR 734 
383  1 Y 1 A THR 752  ? A THR 735 
384  1 Y 1 A THR 753  ? A THR 736 
385  1 Y 1 A SER 754  ? A SER 737 
386  1 Y 1 A ILE 755  ? A ILE 738 
387  1 Y 1 A ASP 756  ? A ASP 739 
388  1 Y 1 A GLY 757  ? A GLY 740 
389  1 Y 1 A ALA 758  ? A ALA 741 
390  1 Y 1 A TRP 759  ? A TRP 742 
391  1 Y 1 A GLY 760  ? A GLY 743 
392  1 Y 1 A SER 761  ? A SER 744 
393  1 Y 1 A GLY 762  ? A GLY 745 
394  1 Y 1 A VAL 763  ? A VAL 746 
395  1 Y 1 A GLY 764  ? A GLY 747 
396  1 Y 1 A PHE 765  ? A PHE 748 
397  1 Y 1 A ASN 766  ? A ASN 749 
398  1 Y 1 A LEU 767  ? A LEU 750 
399  1 Y 1 A ILE 768  ? A ILE 751 
400  1 Y 1 A CYS 769  ? A CYS 752 
401  1 Y 1 A SER 770  ? A SER 753 
402  1 Y 1 A VAL 771  ? A VAL 754 
403  1 Y 1 A SER 772  ? A SER 755 
404  1 Y 1 A LEU 773  ? A LEU 756 
405  1 Y 1 A THR 774  ? A THR 757 
406  1 Y 1 A GLU 775  ? A GLU 758 
407  1 Y 1 A CYS 776  ? A CYS 759 
408  1 Y 1 A SER 777  ? A SER 760 
409  1 Y 1 A THR 778  ? A THR 761 
410  1 Y 1 A PHE 779  ? A PHE 762 
411  1 Y 1 A LEU 780  ? A LEU 763 
412  1 Y 1 A THR 781  ? A THR 764 
413  1 Y 1 A SER 782  ? A SER 765 
414  1 Y 1 A ILE 783  ? A ILE 766 
415  1 Y 1 A LYS 784  ? A LYS 767 
416  1 Y 1 A ALA 785  ? A ALA 768 
417  1 Y 1 A CYS 786  ? A CYS 769 
418  1 Y 1 A ASP 787  ? A ASP 770 
419  1 Y 1 A SER 788  ? A SER 771 
420  1 Y 1 A ALA 789  ? A ALA 772 
421  1 Y 1 A MET 790  ? A MET 773 
422  1 Y 1 A CYS 791  ? A CYS 774 
423  1 Y 1 A TYR 792  ? A TYR 775 
424  1 Y 1 A GLY 793  ? A GLY 776 
425  1 Y 1 A SER 794  ? A SER 777 
426  1 Y 1 A THR 795  ? A THR 778 
427  1 Y 1 A THR 796  ? A THR 779 
428  1 Y 1 A ALA 797  ? A ALA 780 
429  1 Y 1 A ASN 798  ? A ASN 781 
430  1 Y 1 A LEU 799  ? A LEU 782 
431  1 Y 1 A VAL 800  ? A VAL 783 
432  1 Y 1 A ARG 801  ? A ARG 784 
433  1 Y 1 A GLY 802  ? A GLY 785 
434  1 Y 1 A GLN 803  ? A GLN 786 
435  1 Y 1 A ASN 804  ? A ASN 787 
436  1 Y 1 A THR 805  ? A THR 788 
437  1 Y 1 A VAL 806  ? A VAL 789 
438  1 Y 1 A HIS 807  ? A HIS 790 
439  1 Y 1 A ILE 808  ? A ILE 791 
440  1 Y 1 A VAL 809  ? A VAL 792 
441  1 Y 1 A GLY 810  ? A GLY 793 
442  1 Y 1 A LYS 811  ? A LYS 794 
443  1 Y 1 A GLY 812  ? A GLY 795 
444  1 Y 1 A GLY 813  ? A GLY 796 
445  1 Y 1 A HIS 814  ? A HIS 797 
446  1 Y 1 A SER 815  ? A SER 798 
447  1 Y 1 A GLY 816  ? A GLY 799 
448  1 Y 1 A SER 817  ? A SER 800 
449  1 Y 1 A LYS 818  ? A LYS 801 
450  1 Y 1 A PHE 819  ? A PHE 802 
451  1 Y 1 A MET 820  ? A MET 803 
452  1 Y 1 A CYS 821  ? A CYS 804 
453  1 Y 1 A CYS 822  ? A CYS 805 
454  1 Y 1 A HIS 823  ? A HIS 806 
455  1 Y 1 A ASP 824  ? A ASP 807 
456  1 Y 1 A THR 825  ? A THR 808 
457  1 Y 1 A LYS 826  ? A LYS 809 
458  1 Y 1 A CYS 827  ? A CYS 810 
459  1 Y 1 A SER 828  ? A SER 811 
460  1 Y 1 A SER 829  ? A SER 812 
461  1 Y 1 A THR 830  ? A THR 813 
462  1 Y 1 A GLY 831  ? A GLY 814 
463  1 Y 1 A LEU 832  ? A LEU 815 
464  1 Y 1 A VAL 833  ? A VAL 816 
465  1 Y 1 A ALA 834  ? A ALA 817 
466  1 Y 1 A ALA 835  ? A ALA 818 
467  1 Y 1 A ALA 836  ? A ALA 819 
468  1 Y 1 A PRO 837  ? A PRO 820 
469  1 Y 1 A HIS 838  ? A HIS 821 
470  1 Y 1 A LEU 839  ? A LEU 822 
471  1 Y 1 A ASP 840  ? A ASP 823 
472  1 Y 1 A ARG 841  ? A ARG 824 
473  1 Y 1 A VAL 842  ? A VAL 825 
474  1 Y 1 A THR 843  ? A THR 826 
475  1 Y 1 A GLY 844  ? A GLY 827 
476  1 Y 1 A TYR 845  ? A TYR 828 
477  1 Y 1 A ASN 846  ? A ASN 829 
478  1 Y 1 A GLN 847  ? A GLN 830 
479  1 Y 1 A ALA 848  ? A ALA 831 
480  1 Y 1 A ASP 849  ? A ASP 832 
481  1 Y 1 A SER 850  ? A SER 833 
482  1 Y 1 A ASP 851  ? A ASP 834 
483  1 Y 1 A LYS 852  ? A LYS 835 
484  1 Y 1 A ILE 853  ? A ILE 836 
485  1 Y 1 A PHE 854  ? A PHE 837 
486  1 Y 1 A ASP 855  ? A ASP 838 
487  1 Y 1 A ASP 856  ? A ASP 839 
488  1 Y 1 A GLY 857  ? A GLY 840 
489  1 Y 1 A ALA 858  ? A ALA 841 
490  1 Y 1 A PRO 859  ? A PRO 842 
491  1 Y 1 A GLU 860  ? A GLU 843 
492  1 Y 1 A GLY 861  ? A GLY 844 
493  1 Y 1 A LEU 862  ? A LEU 845 
494  1 Y 1 A VAL 863  ? A VAL 846 
495  1 Y 1 A PRO 864  ? A PRO 847 
496  1 Y 1 A ARG 865  ? A ARG 848 
497  1 Y 1 A GLY 866  ? A GLY 849 
498  1 Y 1 A SER 867  ? A SER 850 
499  1 Y 1 A GLY 868  ? A GLY 851 
500  1 Y 1 A PRO 869  ? A PRO 852 
501  1 Y 1 A PHE 870  ? A PHE 853 
502  1 Y 1 A GLU 871  ? A GLU 854 
503  1 Y 1 A ASP 872  ? A ASP 855 
504  1 Y 1 A ASP 873  ? A ASP 856 
505  1 Y 1 A ASP 874  ? A ASP 857 
506  1 Y 1 A ASP 875  ? A ASP 858 
507  1 Y 1 A LYS 876  ? A LYS 859 
508  1 Y 1 A ALA 877  ? A ALA 860 
509  1 Y 1 A GLY 878  ? A GLY 861 
510  1 Y 1 A TRP 879  ? A TRP 862 
511  1 Y 1 A SER 880  ? A SER 863 
512  1 Y 1 A HIS 881  ? A HIS 864 
513  1 Y 1 A PRO 882  ? A PRO 865 
514  1 Y 1 A GLN 883  ? A GLN 866 
515  1 Y 1 A PHE 884  ? A PHE 867 
516  1 Y 1 A GLU 885  ? A GLU 868 
517  1 Y 1 A LYS 886  ? A LYS 869 
518  1 Y 1 A GLY 887  ? A GLY 870 
519  1 Y 1 A GLY 888  ? A GLY 871 
520  1 Y 1 A GLY 889  ? A GLY 872 
521  1 Y 1 A SER 890  ? A SER 873 
522  1 Y 1 A GLY 891  ? A GLY 874 
523  1 Y 1 A GLY 892  ? A GLY 875 
524  1 Y 1 A GLY 893  ? A GLY 876 
525  1 Y 1 A SER 894  ? A SER 877 
526  1 Y 1 A GLY 895  ? A GLY 878 
527  1 Y 1 A GLY 896  ? A GLY 879 
528  1 Y 1 A GLY 897  ? A GLY 880 
529  1 Y 1 A SER 898  ? A SER 881 
530  1 Y 1 A TRP 899  ? A TRP 882 
531  1 Y 1 A SER 900  ? A SER 883 
532  1 Y 1 A HIS 901  ? A HIS 884 
533  1 Y 1 A PRO 902  ? A PRO 885 
534  1 Y 1 A GLN 903  ? A GLN 886 
535  1 Y 1 A PHE 904  ? A PHE 887 
536  1 Y 1 A GLU 905  ? A GLU 888 
537  1 Y 1 A LYS 906  ? A LYS 889 
538  1 Y 1 B ARG 251  ? B ARG 1   
539  1 Y 1 B SER 252  ? B SER 2   
540  1 Y 1 B SER 253  ? B SER 3   
541  1 Y 1 B ARG 254  ? B ARG 4   
542  1 Y 1 B GLY 255  ? B GLY 5   
543  1 Y 1 B ASP 256  ? B ASP 6   
544  1 Y 1 B THR 257  ? B THR 7   
545  1 Y 1 B ARG 258  ? B ARG 8   
546  1 Y 1 B ASN 259  ? B ASN 9   
547  1 Y 1 B LEU 260  ? B LEU 10  
548  1 Y 1 B ASN 261  ? B ASN 11  
549  1 Y 1 B GLU 262  ? B GLU 12  
550  1 Y 1 B LEU 263  ? B LEU 13  
551  1 Y 1 B LYS 264  ? B LYS 14  
552  1 Y 1 B MET 265  ? B MET 15  
553  1 Y 1 B GLU 266  ? B GLU 16  
554  1 Y 1 B CYS 267  ? B CYS 17  
555  1 Y 1 B PRO 268  ? B PRO 18  
556  1 Y 1 B HIS 269  ? B HIS 19  
557  1 Y 1 B THR 270  ? B THR 20  
558  1 Y 1 B ILE 271  ? B ILE 21  
559  1 Y 1 B GLY 272  ? B GLY 22  
560  1 Y 1 B LEU 273  ? B LEU 23  
561  1 Y 1 B GLY 274  ? B GLY 24  
562  1 Y 1 B GLN 275  ? B GLN 25  
563  1 Y 1 B GLY 276  ? B GLY 26  
564  1 Y 1 B LEU 277  ? B LEU 27  
565  1 Y 1 B VAL 278  ? B VAL 28  
566  1 Y 1 B ILE 279  ? B ILE 29  
567  1 Y 1 B GLY 280  ? B GLY 30  
568  1 Y 1 B SER 281  ? B SER 31  
569  1 Y 1 B ILE 282  ? B ILE 32  
570  1 Y 1 B GLU 283  ? B GLU 33  
571  1 Y 1 B LEU 284  ? B LEU 34  
572  1 Y 1 B PRO 285  ? B PRO 35  
573  1 Y 1 B PRO 286  ? B PRO 36  
574  1 Y 1 B VAL 287  ? B VAL 37  
575  1 Y 1 B PRO 288  ? B PRO 38  
576  1 Y 1 B LEU 289  ? B LEU 39  
577  1 Y 1 B ILE 290  ? B ILE 40  
578  1 Y 1 B GLN 291  ? B GLN 41  
579  1 Y 1 B VAL 292  ? B VAL 42  
580  1 Y 1 B GLU 293  ? B GLU 43  
581  1 Y 1 B SER 294  ? B SER 44  
582  1 Y 1 B LEU 295  ? B LEU 45  
583  1 Y 1 B LYS 296  ? B LYS 46  
584  1 Y 1 B LEU 297  ? B LEU 47  
585  1 Y 1 B GLU 298  ? B GLU 48  
586  1 Y 1 B SER 299  ? B SER 49  
587  1 Y 1 B SER 300  ? B SER 50  
588  1 Y 1 B CYS 301  ? B CYS 51  
589  1 Y 1 B ASN 302  ? B ASN 52  
590  1 Y 1 B PHE 303  ? B PHE 53  
591  1 Y 1 B ASP 304  ? B ASP 54  
592  1 Y 1 B LEU 305  ? B LEU 55  
593  1 Y 1 B HIS 306  ? B HIS 56  
594  1 Y 1 B THR 307  ? B THR 57  
595  1 Y 1 B SER 308  ? B SER 58  
596  1 Y 1 B THR 309  ? B THR 59  
597  1 Y 1 B SER 310  ? B SER 60  
598  1 Y 1 B SER 311  ? B SER 61  
599  1 Y 1 B GLN 312  ? B GLN 62  
600  1 Y 1 B GLN 313  ? B GLN 63  
601  1 Y 1 B ALA 314  ? B ALA 64  
602  1 Y 1 B PHE 315  ? B PHE 65  
603  1 Y 1 B THR 316  ? B THR 66  
604  1 Y 1 B LYS 317  ? B LYS 67  
605  1 Y 1 B TRP 318  ? B TRP 68  
606  1 Y 1 B THR 319  ? B THR 69  
607  1 Y 1 B TRP 320  ? B TRP 70  
608  1 Y 1 B GLU 321  ? B GLU 71  
609  1 Y 1 B VAL 322  ? B VAL 72  
610  1 Y 1 B LYS 323  ? B LYS 73  
611  1 Y 1 B SER 324  ? B SER 74  
612  1 Y 1 B ASP 325  ? B ASP 75  
613  1 Y 1 B LEU 326  ? B LEU 76  
614  1 Y 1 B ALA 327  ? B ALA 77  
615  1 Y 1 B GLU 328  ? B GLU 78  
616  1 Y 1 B ASN 329  ? B ASN 79  
617  1 Y 1 B THR 330  ? B THR 80  
618  1 Y 1 B GLN 331  ? B GLN 81  
619  1 Y 1 B ALA 332  ? B ALA 82  
620  1 Y 1 B SER 333  ? B SER 83  
621  1 Y 1 B SER 334  ? B SER 84  
622  1 Y 1 B THR 335  ? B THR 85  
623  1 Y 1 B SER 336  ? B SER 86  
624  1 Y 1 B PHE 337  ? B PHE 87  
625  1 Y 1 B GLN 338  ? B GLN 88  
626  1 Y 1 B THR 339  ? B THR 89  
627  1 Y 1 B LYS 340  ? B LYS 90  
628  1 Y 1 B SER 341  ? B SER 91  
629  1 Y 1 B SER 342  ? B SER 92  
630  1 Y 1 B GLU 343  ? B GLU 93  
631  1 Y 1 B VAL 344  ? B VAL 94  
632  1 Y 1 B ASN 345  ? B ASN 95  
633  1 Y 1 B LEU 346  ? B LEU 96  
634  1 Y 1 B ARG 347  ? B ARG 97  
635  1 Y 1 B GLY 348  ? B GLY 98  
636  1 Y 1 B LEU 349  ? B LEU 99  
637  1 Y 1 B CYS 350  ? B CYS 100 
638  1 Y 1 B LEU 351  ? B LEU 101 
639  1 Y 1 B VAL 352  ? B VAL 102 
640  1 Y 1 B PRO 353  ? B PRO 103 
641  1 Y 1 B PRO 354  ? B PRO 104 
642  1 Y 1 B LEU 355  ? B LEU 105 
643  1 Y 1 B VAL 356  ? B VAL 106 
644  1 Y 1 B ILE 357  ? B ILE 107 
645  1 Y 1 B GLU 358  ? B GLU 108 
646  1 Y 1 B THR 359  ? B THR 109 
647  1 Y 1 B ALA 360  ? B ALA 110 
648  1 Y 1 B ALA 361  ? B ALA 111 
649  1 Y 1 B ARG 362  ? B ARG 112 
650  1 Y 1 B THR 363  ? B THR 113 
651  1 Y 1 B ARG 364  ? B ARG 114 
652  1 Y 1 B LYS 365  ? B LYS 115 
653  1 Y 1 B THR 366  ? B THR 116 
654  1 Y 1 B ILE 367  ? B ILE 117 
655  1 Y 1 B ALA 368  ? B ALA 118 
656  1 Y 1 B CYS 369  ? B CYS 119 
657  1 Y 1 B PHE 370  ? B PHE 120 
658  1 Y 1 B ASP 371  ? B ASP 121 
659  1 Y 1 B LEU 372  ? B LEU 122 
660  1 Y 1 B SER 373  ? B SER 123 
661  1 Y 1 B CYS 374  ? B CYS 124 
662  1 Y 1 B ASN 375  ? B ASN 125 
663  1 Y 1 B GLN 376  ? B GLN 126 
664  1 Y 1 B THR 377  ? B THR 127 
665  1 Y 1 B THR 378  ? B THR 128 
666  1 Y 1 B CYS 379  ? B CYS 129 
667  1 Y 1 B GLN 380  ? B GLN 130 
668  1 Y 1 B PRO 381  ? B PRO 131 
669  1 Y 1 B THR 382  ? B THR 132 
670  1 Y 1 B VAL 383  ? B VAL 133 
671  1 Y 1 B PHE 384  ? B PHE 134 
672  1 Y 1 B LEU 385  ? B LEU 135 
673  1 Y 1 B MET 386  ? B MET 136 
674  1 Y 1 B GLY 387  ? B GLY 137 
675  1 Y 1 B PRO 388  ? B PRO 138 
676  1 Y 1 B ILE 389  ? B ILE 139 
677  1 Y 1 B GLN 390  ? B GLN 140 
678  1 Y 1 B THR 391  ? B THR 141 
679  1 Y 1 B CYS 392  ? B CYS 142 
680  1 Y 1 B ILE 393  ? B ILE 143 
681  1 Y 1 B THR 394  ? B THR 144 
682  1 Y 1 B THR 395  ? B THR 145 
683  1 Y 1 B LYS 396  ? B LYS 146 
684  1 Y 1 B SER 397  ? B SER 147 
685  1 Y 1 B CYS 398  ? B CYS 148 
686  1 Y 1 B LEU 399  ? B LEU 149 
687  1 Y 1 B LEU 400  ? B LEU 150 
688  1 Y 1 B GLY 401  ? B GLY 151 
689  1 Y 1 B LEU 402  ? B LEU 152 
690  1 Y 1 B GLY 403  ? B GLY 153 
691  1 Y 1 B ASP 404  ? B ASP 154 
692  1 Y 1 B GLN 405  ? B GLN 155 
693  1 Y 1 B ARG 406  ? B ARG 156 
694  1 Y 1 B ILE 407  ? B ILE 157 
695  1 Y 1 B GLN 408  ? B GLN 158 
696  1 Y 1 B VAL 409  ? B VAL 159 
697  1 Y 1 B ASN 410  ? B ASN 160 
698  1 Y 1 B TYR 411  ? B TYR 161 
699  1 Y 1 B GLU 412  ? B GLU 162 
700  1 Y 1 B LYS 413  ? B LYS 163 
701  1 Y 1 B THR 414  ? B THR 164 
702  1 Y 1 B TYR 415  ? B TYR 165 
703  1 Y 1 B CYS 416  ? B CYS 166 
704  1 Y 1 B VAL 417  ? B VAL 167 
705  1 Y 1 B SER 418  ? B SER 168 
706  1 Y 1 B GLY 419  ? B GLY 169 
707  1 Y 1 B GLN 420  ? B GLN 170 
708  1 Y 1 B LEU 421  ? B LEU 171 
709  1 Y 1 B ILE 422  ? B ILE 172 
710  1 Y 1 B GLU 423  ? B GLU 173 
711  1 Y 1 B GLY 424  ? B GLY 174 
712  1 Y 1 B ILE 425  ? B ILE 175 
713  1 Y 1 B CYS 426  ? B CYS 176 
714  1 Y 1 B PHE 427  ? B PHE 177 
715  1 Y 1 B ASN 428  ? B ASN 178 
716  1 Y 1 B PRO 429  ? B PRO 179 
717  1 Y 1 B VAL 430  ? B VAL 180 
718  1 Y 1 B HIS 431  ? B HIS 181 
719  1 Y 1 B THR 432  ? B THR 182 
720  1 Y 1 B MET 433  ? B MET 183 
721  1 Y 1 B ALA 434  ? B ALA 184 
722  1 Y 1 B LEU 435  ? B LEU 185 
723  1 Y 1 B SER 436  ? B SER 186 
724  1 Y 1 B GLN 437  ? B GLN 187 
725  1 Y 1 B PRO 438  ? B PRO 188 
726  1 Y 1 B SER 439  ? B SER 189 
727  1 Y 1 B HIS 440  ? B HIS 190 
728  1 Y 1 B THR 441  ? B THR 191 
729  1 Y 1 B TYR 442  ? B TYR 192 
730  1 Y 1 B ASP 443  ? B ASP 193 
731  1 Y 1 B ILE 444  ? B ILE 194 
732  1 Y 1 B VAL 445  ? B VAL 195 
733  1 Y 1 B THR 446  ? B THR 196 
734  1 Y 1 B VAL 447  ? B VAL 197 
735  1 Y 1 B MET 448  ? B MET 198 
736  1 Y 1 B VAL 449  ? B VAL 199 
737  1 Y 1 B ARG 450  ? B ARG 200 
738  1 Y 1 B CYS 451  ? B CYS 201 
739  1 Y 1 B PHE 452  ? B PHE 202 
740  1 Y 1 B LEU 453  ? B LEU 203 
741  1 Y 1 B ILE 454  ? B ILE 204 
742  1 Y 1 B VAL 455  ? B VAL 205 
743  1 Y 1 B LYS 456  ? B LYS 206 
744  1 Y 1 B LYS 457  ? B LYS 207 
745  1 Y 1 B VAL 458  ? B VAL 208 
746  1 Y 1 B THR 459  ? B THR 209 
747  1 Y 1 B THR 460  ? B THR 210 
748  1 Y 1 B GLY 461  ? B GLY 211 
749  1 Y 1 B ASP 462  ? B ASP 212 
750  1 Y 1 B SER 463  ? B SER 213 
751  1 Y 1 B MET 464  ? B MET 214 
752  1 Y 1 B LYS 465  ? B LYS 215 
753  1 Y 1 B ILE 466  ? B ILE 216 
754  1 Y 1 B GLU 467  ? B GLU 217 
755  1 Y 1 B LYS 468  ? B LYS 218 
756  1 Y 1 B SER 469  ? B SER 219 
757  1 Y 1 B PHE 470  ? B PHE 220 
758  1 Y 1 B GLU 471  ? B GLU 221 
759  1 Y 1 B THR 472  ? B THR 222 
760  1 Y 1 B LEU 473  ? B LEU 223 
761  1 Y 1 B VAL 474  ? B VAL 224 
762  1 Y 1 B GLN 475  ? B GLN 225 
763  1 Y 1 B LYS 476  ? B LYS 226 
764  1 Y 1 B THR 477  ? B THR 227 
765  1 Y 1 B GLY 478  ? B GLY 228 
766  1 Y 1 B CYS 479  ? B CYS 229 
767  1 Y 1 B THR 480  ? B THR 230 
768  1 Y 1 B ASP 481  ? B ASP 231 
769  1 Y 1 B ASN 482  ? B ASN 232 
770  1 Y 1 B GLY 483  ? B GLY 233 
771  1 Y 1 B PHE 484  ? B PHE 234 
772  1 Y 1 B GLN 485  ? B GLN 235 
773  1 Y 1 B GLY 486  ? B GLY 236 
774  1 Y 1 B TYR 487  ? B TYR 237 
775  1 Y 1 B TYR 488  ? B TYR 238 
776  1 Y 1 B VAL 489  ? B VAL 239 
777  1 Y 1 B CYS 490  ? B CYS 240 
778  1 Y 1 B LEU 491  ? B LEU 241 
779  1 Y 1 B ILE 492  ? B ILE 242 
780  1 Y 1 B GLY 493  ? B GLY 243 
781  1 Y 1 B SER 494  ? B SER 244 
782  1 Y 1 B SER 495  ? B SER 245 
783  1 Y 1 B SER 496  ? B SER 246 
784  1 Y 1 B GLU 497  ? B GLU 247 
785  1 Y 1 B PRO 498  ? B PRO 248 
786  1 Y 1 B LEU 499  ? B LEU 249 
787  1 Y 1 B TYR 500  ? B TYR 250 
788  1 Y 1 B ILE 501  ? B ILE 251 
789  1 Y 1 B PRO 502  ? B PRO 252 
790  1 Y 1 B THR 503  ? B THR 253 
791  1 Y 1 B LEU 504  ? B LEU 254 
792  1 Y 1 B ASP 505  ? B ASP 255 
793  1 Y 1 B ASP 506  ? B ASP 256 
794  1 Y 1 B TYR 507  ? B TYR 257 
795  1 Y 1 B ARG 508  ? B ARG 258 
796  1 Y 1 B SER 509  ? B SER 259 
797  1 Y 1 B ALA 510  ? B ALA 260 
798  1 Y 1 B GLU 511  ? B GLU 261 
799  1 Y 1 B VAL 512  ? B VAL 262 
800  1 Y 1 B LEU 513  ? B LEU 263 
801  1 Y 1 B SER 514  ? B SER 264 
802  1 Y 1 B ARG 515  ? B ARG 265 
803  1 Y 1 B MET 516  ? B MET 266 
804  1 Y 1 B ALA 517  ? B ALA 267 
805  1 Y 1 B PHE 518  ? B PHE 268 
806  1 Y 1 B ALA 519  ? B ALA 269 
807  1 Y 1 B PRO 520  ? B PRO 270 
808  1 Y 1 B HIS 521  ? B HIS 271 
809  1 Y 1 B GLY 522  ? B GLY 272 
810  1 Y 1 B GLU 523  ? B GLU 273 
811  1 Y 1 B ASP 524  ? B ASP 274 
812  1 Y 1 B HIS 525  ? B HIS 275 
813  1 Y 1 B ASP 526  ? B ASP 276 
814  1 Y 1 B ILE 527  ? B ILE 277 
815  1 Y 1 B GLU 528  ? B GLU 278 
816  1 Y 1 B LYS 529  ? B LYS 279 
817  1 Y 1 B ASN 530  ? B ASN 280 
818  1 Y 1 B ALA 531  ? B ALA 281 
819  1 Y 1 B ILE 532  ? B ILE 282 
820  1 Y 1 B SER 533  ? B SER 283 
821  1 Y 1 B ALA 534  ? B ALA 284 
822  1 Y 1 B MET 535  ? B MET 285 
823  1 Y 1 B ARG 536  ? B ARG 286 
824  1 Y 1 B ILE 537  ? B ILE 287 
825  1 Y 1 B VAL 538  ? B VAL 288 
826  1 Y 1 B GLY 539  ? B GLY 289 
827  1 Y 1 B LYS 540  ? B LYS 290 
828  1 Y 1 B VAL 541  ? B VAL 291 
829  1 Y 1 B THR 542  ? B THR 292 
830  1 Y 1 B GLY 543  ? B GLY 293 
831  1 Y 1 B LYS 544  ? B LYS 294 
832  1 Y 1 B ALA 545  ? B ALA 295 
833  1 Y 1 B PRO 546  ? B PRO 296 
834  1 Y 1 B SER 547  ? B SER 297 
835  1 Y 1 B THR 548  ? B THR 298 
836  1 Y 1 B GLU 549  ? B GLU 299 
837  1 Y 1 B SER 550  ? B SER 300 
838  1 Y 1 B SER 551  ? B SER 301 
839  1 Y 1 B ASP 552  ? B ASP 302 
840  1 Y 1 B THR 553  ? B THR 303 
841  1 Y 1 B VAL 554  ? B VAL 304 
842  1 Y 1 B GLN 555  ? B GLN 305 
843  1 Y 1 B GLY 556  ? B GLY 306 
844  1 Y 1 B ILE 557  ? B ILE 307 
845  1 Y 1 B ALA 558  ? B ALA 308 
846  1 Y 1 B PHE 559  ? B PHE 309 
847  1 Y 1 B SER 560  ? B SER 310 
848  1 Y 1 B GLY 561  ? B GLY 311 
849  1 Y 1 B ASN 562  ? B ASN 312 
850  1 Y 1 B PRO 563  ? B PRO 313 
851  1 Y 1 B LEU 564  ? B LEU 314 
852  1 Y 1 B TYR 565  ? B TYR 315 
853  1 Y 1 B THR 566  ? B THR 316 
854  1 Y 1 B SER 567  ? B SER 317 
855  1 Y 1 B THR 568  ? B THR 318 
856  1 Y 1 B GLY 569  ? B GLY 319 
857  1 Y 1 B VAL 570  ? B VAL 320 
858  1 Y 1 B LEU 571  ? B LEU 321 
859  1 Y 1 B THR 572  ? B THR 322 
860  1 Y 1 B ALA 573  ? B ALA 323 
861  1 Y 1 B LYS 574  ? B LYS 324 
862  1 Y 1 B ASP 575  ? B ASP 325 
863  1 Y 1 B ASP 576  ? B ASP 326 
864  1 Y 1 B PRO 577  ? B PRO 327 
865  1 Y 1 B VAL 578  ? B VAL 328 
866  1 Y 1 B TYR 579  ? B TYR 329 
867  1 Y 1 B VAL 580  ? B VAL 330 
868  1 Y 1 B TRP 581  ? B TRP 331 
869  1 Y 1 B ALA 582  ? B ALA 332 
870  1 Y 1 B PRO 583  ? B PRO 333 
871  1 Y 1 B GLY 584  ? B GLY 334 
872  1 Y 1 B ILE 585  ? B ILE 335 
873  1 Y 1 B MET 586  ? B MET 336 
874  1 Y 1 B MET 587  ? B MET 337 
875  1 Y 1 B GLU 588  ? B GLU 338 
876  1 Y 1 B GLY 589  ? B GLY 339 
877  1 Y 1 B ASN 590  ? B ASN 340 
878  1 Y 1 B HIS 591  ? B HIS 341 
879  1 Y 1 B SER 592  ? B SER 342 
880  1 Y 1 B VAL 593  ? B VAL 343 
881  1 Y 1 B CYS 594  ? B CYS 344 
882  1 Y 1 B ASP 595  ? B ASP 345 
883  1 Y 1 B LYS 596  ? B LYS 346 
884  1 Y 1 B LYS 597  ? B LYS 347 
885  1 Y 1 B THR 598  ? B THR 348 
886  1 Y 1 B LEU 599  ? B LEU 349 
887  1 Y 1 B PRO 600  ? B PRO 350 
888  1 Y 1 B LEU 601  ? B LEU 351 
889  1 Y 1 B THR 602  ? B THR 352 
890  1 Y 1 B TRP 603  ? B TRP 353 
891  1 Y 1 B THR 604  ? B THR 354 
892  1 Y 1 B GLY 605  ? B GLY 355 
893  1 Y 1 B PHE 606  ? B PHE 356 
894  1 Y 1 B ILE 607  ? B ILE 357 
895  1 Y 1 B PRO 608  ? B PRO 358 
896  1 Y 1 B LEU 609  ? B LEU 359 
897  1 Y 1 B PRO 610  ? B PRO 360 
898  1 Y 1 B GLY 611  ? B GLY 361 
899  1 Y 1 B GLU 612  ? B GLU 362 
900  1 Y 1 B ILE 613  ? B ILE 363 
901  1 Y 1 B GLU 614  ? B GLU 364 
902  1 Y 1 B GLY 615  ? B GLY 365 
903  1 Y 1 B GLY 616  ? B GLY 366 
904  1 Y 1 B SER 617  ? B SER 367 
905  1 Y 1 B GLY 618  ? B GLY 368 
906  1 Y 1 B LEU 619  ? B LEU 369 
907  1 Y 1 B VAL 620  ? B VAL 370 
908  1 Y 1 B PRO 621  ? B PRO 371 
909  1 Y 1 B ARG 622  ? B ARG 372 
910  1 Y 1 B GLY 623  ? B GLY 373 
911  1 Y 1 B SER 624  ? B SER 374 
912  1 Y 1 B GLY 625  ? B GLY 375 
913  1 Y 1 B GLY 626  ? B GLY 376 
914  1 Y 1 B GLY 627  ? B GLY 377 
915  1 Y 1 B SER 628  ? B SER 378 
916  1 Y 1 B GLY 629  ? B GLY 379 
917  1 Y 1 B GLY 630  ? B GLY 380 
918  1 Y 1 B GLY 631  ? B GLY 381 
919  1 Y 1 B SER 632  ? B SER 382 
920  1 Y 1 B TRP 633  ? B TRP 383 
921  1 Y 1 B SER 634  ? B SER 384 
922  1 Y 1 B HIS 635  ? B HIS 385 
923  1 Y 1 B PRO 636  ? B PRO 386 
924  1 Y 1 B GLN 637  ? B GLN 387 
925  1 Y 1 B PHE 638  ? B PHE 388 
926  1 Y 1 B GLU 639  ? B GLU 389 
927  1 Y 1 B LYS 640  ? B LYS 390 
928  1 Y 1 B GLY 641  ? B GLY 391 
929  1 Y 1 B GLY 642  ? B GLY 392 
930  1 Y 1 B GLY 643  ? B GLY 393 
931  1 Y 1 B THR 644  ? B THR 394 
932  1 Y 1 B GLY 645  ? B GLY 395 
933  1 Y 1 B GLY 646  ? B GLY 396 
934  1 Y 1 B GLY 647  ? B GLY 397 
935  1 Y 1 B THR 648  ? B THR 398 
936  1 Y 1 B LEU 649  ? B LEU 399 
937  1 Y 1 B VAL 650  ? B VAL 400 
938  1 Y 1 B PRO 651  ? B PRO 401 
939  1 Y 1 B ARG 652  ? B ARG 402 
940  1 Y 1 B GLY 653  ? B GLY 403 
941  1 Y 1 B SER 654  ? B SER 404 
942  1 Y 1 B GLY 655  ? B GLY 405 
943  1 Y 1 B THR 656  ? B THR 406 
944  1 Y 1 B GLY 657  ? B GLY 407 
945  1 Y 1 B GLY 658  ? B GLY 408 
946  1 Y 1 B HIS 1071 ? B HIS 821 
947  1 Y 1 B LEU 1072 ? B LEU 822 
948  1 Y 1 B ASP 1073 ? B ASP 823 
949  1 Y 1 B ARG 1074 ? B ARG 824 
950  1 Y 1 B VAL 1075 ? B VAL 825 
951  1 Y 1 B THR 1076 ? B THR 826 
952  1 Y 1 B GLY 1077 ? B GLY 827 
953  1 Y 1 B TYR 1078 ? B TYR 828 
954  1 Y 1 B ASN 1079 ? B ASN 829 
955  1 Y 1 B GLN 1080 ? B GLN 830 
956  1 Y 1 B ALA 1081 ? B ALA 831 
957  1 Y 1 B ASP 1082 ? B ASP 832 
958  1 Y 1 B GLY 1094 ? B GLY 844 
959  1 Y 1 B LEU 1095 ? B LEU 845 
960  1 Y 1 B VAL 1096 ? B VAL 846 
961  1 Y 1 B PRO 1097 ? B PRO 847 
962  1 Y 1 B ARG 1098 ? B ARG 848 
963  1 Y 1 B GLY 1099 ? B GLY 849 
964  1 Y 1 B SER 1100 ? B SER 850 
965  1 Y 1 B GLY 1101 ? B GLY 851 
966  1 Y 1 B PRO 1102 ? B PRO 852 
967  1 Y 1 B PHE 1103 ? B PHE 853 
968  1 Y 1 B GLU 1104 ? B GLU 854 
969  1 Y 1 B ASP 1105 ? B ASP 855 
970  1 Y 1 B ASP 1106 ? B ASP 856 
971  1 Y 1 B ASP 1107 ? B ASP 857 
972  1 Y 1 B ASP 1108 ? B ASP 858 
973  1 Y 1 B LYS 1109 ? B LYS 859 
974  1 Y 1 B ALA 1110 ? B ALA 860 
975  1 Y 1 B GLY 1111 ? B GLY 861 
976  1 Y 1 B TRP 1112 ? B TRP 862 
977  1 Y 1 B SER 1113 ? B SER 863 
978  1 Y 1 B HIS 1114 ? B HIS 864 
979  1 Y 1 B PRO 1115 ? B PRO 865 
980  1 Y 1 B GLN 1116 ? B GLN 866 
981  1 Y 1 B PHE 1117 ? B PHE 867 
982  1 Y 1 B GLU 1118 ? B GLU 868 
983  1 Y 1 B LYS 1119 ? B LYS 869 
984  1 Y 1 B GLY 1120 ? B GLY 870 
985  1 Y 1 B GLY 1121 ? B GLY 871 
986  1 Y 1 B GLY 1122 ? B GLY 872 
987  1 Y 1 B SER 1123 ? B SER 873 
988  1 Y 1 B GLY 1124 ? B GLY 874 
989  1 Y 1 B GLY 1125 ? B GLY 875 
990  1 Y 1 B GLY 1126 ? B GLY 876 
991  1 Y 1 B SER 1127 ? B SER 877 
992  1 Y 1 B GLY 1128 ? B GLY 878 
993  1 Y 1 B GLY 1129 ? B GLY 879 
994  1 Y 1 B GLY 1130 ? B GLY 880 
995  1 Y 1 B SER 1131 ? B SER 881 
996  1 Y 1 B TRP 1132 ? B TRP 882 
997  1 Y 1 B SER 1133 ? B SER 883 
998  1 Y 1 B HIS 1134 ? B HIS 884 
999  1 Y 1 B PRO 1135 ? B PRO 885 
1000 1 Y 1 B GLN 1136 ? B GLN 886 
1001 1 Y 1 B PHE 1137 ? B PHE 887 
1002 1 Y 1 B GLU 1138 ? B GLU 888 
1003 1 Y 1 B LYS 1139 ? B LYS 889 
1004 1 Y 1 H ARG -1   ? C ARG 1   
1005 1 Y 1 H SER 0    ? C SER 2   
1006 1 Y 1 H ARG 71   ? C ARG 74  
1007 1 Y 1 H ASP 72   ? C ASP 75  
1008 1 Y 1 H ASN 73   ? C ASN 76  
1009 1 Y 1 H SER 74   ? C SER 77  
1010 1 Y 1 H GLY 114  ? C GLY 129 
1011 1 Y 1 H THR 115  ? C THR 130 
1012 1 Y 1 H GLY 116  ? C GLY 131 
1013 1 Y 1 H GLY 117  ? C GLY 132 
1014 1 Y 1 H SER 118  ? C SER 133 
1015 1 Y 1 H GLY 119  ? C GLY 134 
1016 1 Y 1 H GLY 120  ? C GLY 135 
1017 1 Y 1 H GLY 121  ? C GLY 136 
1018 1 Y 1 H GLY 122  ? C GLY 137 
1019 1 Y 1 H SER 123  ? C SER 138 
1020 1 Y 1 H GLY 124  ? C GLY 139 
1021 1 Y 1 H GLY 125  ? C GLY 140 
1022 1 Y 1 H GLY 126  ? C GLY 141 
1023 1 Y 1 H GLY 127  ? C GLY 142 
1024 1 Y 1 H SER 128  ? C SER 143 
1025 1 Y 1 H GLY 129  ? C GLY 144 
1026 1 Y 1 H GLY 130  ? C GLY 145 
1027 1 Y 1 H GLY 131  ? C GLY 146 
1028 1 Y 1 H ALA 132  ? C ALA 147 
1029 1 Y 1 H SER 133  ? C SER 148 
1030 1 Y 1 H ASP 134  ? C ASP 149 
1031 1 Y 1 H ILE 135  ? C ILE 150 
1032 1 Y 1 H VAL 136  ? C VAL 151 
1033 1 Y 1 H MET 137  ? C MET 152 
1034 1 Y 1 H THR 138  ? C THR 153 
1035 1 Y 1 H GLN 139  ? C GLN 154 
1036 1 Y 1 H SER 140  ? C SER 155 
1037 1 Y 1 H PRO 141  ? C PRO 156 
1038 1 Y 1 H LEU 142  ? C LEU 157 
1039 1 Y 1 H SER 143  ? C SER 158 
1040 1 Y 1 H LEU 144  ? C LEU 159 
1041 1 Y 1 H PRO 145  ? C PRO 160 
1042 1 Y 1 H VAL 146  ? C VAL 161 
1043 1 Y 1 H THR 147  ? C THR 162 
1044 1 Y 1 H PRO 148  ? C PRO 163 
1045 1 Y 1 H GLY 149  ? C GLY 164 
1046 1 Y 1 H GLU 150  ? C GLU 165 
1047 1 Y 1 H PRO 151  ? C PRO 166 
1048 1 Y 1 H ALA 152  ? C ALA 167 
1049 1 Y 1 H SER 153  ? C SER 168 
1050 1 Y 1 H ILE 154  ? C ILE 169 
1051 1 Y 1 H SER 155  ? C SER 170 
1052 1 Y 1 H CYS 156  ? C CYS 171 
1053 1 Y 1 H ARG 157  ? C ARG 172 
1054 1 Y 1 H SER 158  ? C SER 173 
1055 1 Y 1 H SER 159  ? C SER 174 
1056 1 Y 1 H GLN 160  ? C GLN 175 
1057 1 Y 1 H SER 161  ? C SER 176 
1058 1 Y 1 H LEU 162  ? C LEU 177 
1059 1 Y 1 H LEU 163  ? C LEU 178 
1060 1 Y 1 H HIS 164  ? C HIS 179 
1061 1 Y 1 H THR 165  ? C THR 180 
1062 1 Y 1 H TYR 166  ? C TYR 181 
1063 1 Y 1 H GLY 167  ? C GLY 182 
1064 1 Y 1 H TYR 168  ? C TYR 183 
1065 1 Y 1 H ASN 169  ? C ASN 184 
1066 1 Y 1 H CYS 170  ? C CYS 185 
1067 1 Y 1 H LEU 171  ? C LEU 186 
1068 1 Y 1 H ASP 172  ? C ASP 187 
1069 1 Y 1 H TRP 173  ? C TRP 188 
1070 1 Y 1 H TYR 174  ? C TYR 189 
1071 1 Y 1 H LEU 175  ? C LEU 190 
1072 1 Y 1 H GLN 176  ? C GLN 191 
1073 1 Y 1 H ARG 177  ? C ARG 192 
1074 1 Y 1 H PRO 178  ? C PRO 193 
1075 1 Y 1 H GLY 179  ? C GLY 194 
1076 1 Y 1 H GLN 180  ? C GLN 195 
1077 1 Y 1 H SER 181  ? C SER 196 
1078 1 Y 1 H PRO 182  ? C PRO 197 
1079 1 Y 1 H GLN 183  ? C GLN 198 
1080 1 Y 1 H LEU 184  ? C LEU 199 
1081 1 Y 1 H LEU 185  ? C LEU 200 
1082 1 Y 1 H ILE 186  ? C ILE 201 
1083 1 Y 1 H SER 187  ? C SER 202 
1084 1 Y 1 H LEU 188  ? C LEU 203 
1085 1 Y 1 H GLY 189  ? C GLY 204 
1086 1 Y 1 H SER 190  ? C SER 205 
1087 1 Y 1 H TYR 191  ? C TYR 206 
1088 1 Y 1 H ARG 192  ? C ARG 207 
1089 1 Y 1 H ALA 193  ? C ALA 208 
1090 1 Y 1 H SER 194  ? C SER 209 
1091 1 Y 1 H GLY 195  ? C GLY 210 
1092 1 Y 1 H VAL 196  ? C VAL 211 
1093 1 Y 1 H PRO 197  ? C PRO 212 
1094 1 Y 1 H ASP 198  ? C ASP 213 
1095 1 Y 1 H ARG 199  ? C ARG 214 
1096 1 Y 1 H PHE 200  ? C PHE 215 
1097 1 Y 1 H SER 201  ? C SER 216 
1098 1 Y 1 H GLY 202  ? C GLY 217 
1099 1 Y 1 H SER 203  ? C SER 218 
1100 1 Y 1 H GLY 204  ? C GLY 219 
1101 1 Y 1 H SER 205  ? C SER 220 
1102 1 Y 1 H GLY 206  ? C GLY 221 
1103 1 Y 1 H THR 207  ? C THR 222 
1104 1 Y 1 H ASP 208  ? C ASP 223 
1105 1 Y 1 H PHE 209  ? C PHE 224 
1106 1 Y 1 H THR 210  ? C THR 225 
1107 1 Y 1 H LEU 211  ? C LEU 226 
1108 1 Y 1 H LYS 212  ? C LYS 227 
1109 1 Y 1 H ILE 213  ? C ILE 228 
1110 1 Y 1 H SER 214  ? C SER 229 
1111 1 Y 1 H ARG 215  ? C ARG 230 
1112 1 Y 1 H VAL 216  ? C VAL 231 
1113 1 Y 1 H GLU 217  ? C GLU 232 
1114 1 Y 1 H ALA 218  ? C ALA 233 
1115 1 Y 1 H GLU 219  ? C GLU 234 
1116 1 Y 1 H ASP 220  ? C ASP 235 
1117 1 Y 1 H VAL 221  ? C VAL 236 
1118 1 Y 1 H GLY 222  ? C GLY 237 
1119 1 Y 1 H VAL 223  ? C VAL 238 
1120 1 Y 1 H TYR 224  ? C TYR 239 
1121 1 Y 1 H TYR 225  ? C TYR 240 
1122 1 Y 1 H CYS 226  ? C CYS 241 
1123 1 Y 1 H MET 227  ? C MET 242 
1124 1 Y 1 H GLN 228  ? C GLN 243 
1125 1 Y 1 H ALA 229  ? C ALA 244 
1126 1 Y 1 H LEU 230  ? C LEU 245 
1127 1 Y 1 H HIS 231  ? C HIS 246 
1128 1 Y 1 H PRO 232  ? C PRO 247 
1129 1 Y 1 H PHE 233  ? C PHE 248 
1130 1 Y 1 H THR 234  ? C THR 249 
1131 1 Y 1 H PHE 235  ? C PHE 250 
1132 1 Y 1 H GLY 236  ? C GLY 251 
1133 1 Y 1 H GLY 237  ? C GLY 252 
1134 1 Y 1 H GLY 238  ? C GLY 253 
1135 1 Y 1 H THR 239  ? C THR 254 
1136 1 Y 1 H LYS 240  ? C LYS 255 
1137 1 Y 1 H VAL 241  ? C VAL 256 
1138 1 Y 1 H GLU 242  ? C GLU 257 
1139 1 Y 1 H ILE 243  ? C ILE 258 
1140 1 Y 1 H LYS 244  ? C LYS 259 
1141 1 Y 1 H GLY 245  ? C GLY 260 
1142 1 Y 1 H PRO 246  ? C PRO 261 
1143 1 Y 1 H PHE 247  ? C PHE 262 
1144 1 Y 1 H GLU 248  ? C GLU 263 
1145 1 Y 1 H ASP 249  ? C ASP 264 
1146 1 Y 1 H ASP 250  ? C ASP 265 
1147 1 Y 1 H ASP 251  ? C ASP 266 
1148 1 Y 1 H ASP 252  ? C ASP 267 
1149 1 Y 1 H LYS 253  ? C LYS 268 
1150 1 Y 1 H ALA 254  ? C ALA 269 
1151 1 Y 1 H GLY 255  ? C GLY 270 
1152 1 Y 1 H TRP 256  ? C TRP 271 
1153 1 Y 1 H SER 257  ? C SER 272 
1154 1 Y 1 H HIS 258  ? C HIS 273 
1155 1 Y 1 H PRO 259  ? C PRO 274 
1156 1 Y 1 H GLN 260  ? C GLN 275 
1157 1 Y 1 H PHE 261  ? C PHE 276 
1158 1 Y 1 H GLU 262  ? C GLU 277 
1159 1 Y 1 H LYS 263  ? C LYS 278 
1160 1 Y 1 H GLY 264  ? C GLY 279 
1161 1 Y 1 H GLY 265  ? C GLY 280 
1162 1 Y 1 H GLY 266  ? C GLY 281 
1163 1 Y 1 H SER 267  ? C SER 282 
1164 1 Y 1 H GLY 268  ? C GLY 283 
1165 1 Y 1 H GLY 269  ? C GLY 284 
1166 1 Y 1 H GLY 270  ? C GLY 285 
1167 1 Y 1 H SER 271  ? C SER 286 
1168 1 Y 1 H GLY 272  ? C GLY 287 
1169 1 Y 1 H GLY 273  ? C GLY 288 
1170 1 Y 1 H GLY 274  ? C GLY 289 
1171 1 Y 1 H SER 275  ? C SER 290 
1172 1 Y 1 H TRP 276  ? C TRP 291 
1173 1 Y 1 H SER 277  ? C SER 292 
1174 1 Y 1 H HIS 278  ? C HIS 293 
1175 1 Y 1 H PRO 279  ? C PRO 294 
1176 1 Y 1 H GLN 280  ? C GLN 295 
1177 1 Y 1 H PHE 281  ? C PHE 296 
1178 1 Y 1 H GLU 282  ? C GLU 297 
1179 1 Y 1 H LYS 283  ? C LYS 298 
1180 1 Y 1 L ARG -147 ? D ARG 1   
1181 1 Y 1 L SER -146 ? D SER 2   
1182 1 Y 1 L GLN -145 ? D GLN 3   
1183 1 Y 1 L VAL -144 ? D VAL 4   
1184 1 Y 1 L GLN -143 ? D GLN 5   
1185 1 Y 1 L LEU -142 ? D LEU 6   
1186 1 Y 1 L VAL -141 ? D VAL 7   
1187 1 Y 1 L GLU -140 ? D GLU 8   
1188 1 Y 1 L SER -139 ? D SER 9   
1189 1 Y 1 L GLY -138 ? D GLY 10  
1190 1 Y 1 L GLY -137 ? D GLY 11  
1191 1 Y 1 L GLY -136 ? D GLY 12  
1192 1 Y 1 L VAL -135 ? D VAL 13  
1193 1 Y 1 L VAL -134 ? D VAL 14  
1194 1 Y 1 L GLN -133 ? D GLN 15  
1195 1 Y 1 L PRO -132 ? D PRO 16  
1196 1 Y 1 L GLY -131 ? D GLY 17  
1197 1 Y 1 L ARG -130 ? D ARG 18  
1198 1 Y 1 L SER -129 ? D SER 19  
1199 1 Y 1 L LEU -128 ? D LEU 20  
1200 1 Y 1 L ARG -127 ? D ARG 21  
1201 1 Y 1 L LEU -126 ? D LEU 22  
1202 1 Y 1 L SER -125 ? D SER 23  
1203 1 Y 1 L CYS -124 ? D CYS 24  
1204 1 Y 1 L ALA -123 ? D ALA 25  
1205 1 Y 1 L ALA -122 ? D ALA 26  
1206 1 Y 1 L SER -121 ? D SER 27  
1207 1 Y 1 L GLY -120 ? D GLY 28  
1208 1 Y 1 L PHE -119 ? D PHE 29  
1209 1 Y 1 L THR -118 ? D THR 30  
1210 1 Y 1 L PHE -117 ? D PHE 31  
1211 1 Y 1 L SER -116 ? D SER 32  
1212 1 Y 1 L SER -115 ? D SER 33  
1213 1 Y 1 L TYR -114 ? D TYR 34  
1214 1 Y 1 L ALA -113 ? D ALA 35  
1215 1 Y 1 L MET -112 ? D MET 36  
1216 1 Y 1 L HIS -111 ? D HIS 37  
1217 1 Y 1 L TRP -110 ? D TRP 38  
1218 1 Y 1 L VAL -109 ? D VAL 39  
1219 1 Y 1 L ARG -108 ? D ARG 40  
1220 1 Y 1 L GLN -107 ? D GLN 41  
1221 1 Y 1 L ALA -106 ? D ALA 42  
1222 1 Y 1 L PRO -105 ? D PRO 43  
1223 1 Y 1 L GLY -104 ? D GLY 44  
1224 1 Y 1 L LYS -103 ? D LYS 45  
1225 1 Y 1 L GLY -102 ? D GLY 46  
1226 1 Y 1 L LEU -101 ? D LEU 47  
1227 1 Y 1 L GLU -100 ? D GLU 48  
1228 1 Y 1 L TRP -99  ? D TRP 49  
1229 1 Y 1 L VAL -98  ? D VAL 50  
1230 1 Y 1 L ALA -97  ? D ALA 51  
1231 1 Y 1 L VAL -96  ? D VAL 52  
1232 1 Y 1 L THR -95  ? D THR 53  
1233 1 Y 1 L TRP -94  ? D TRP 54  
1234 1 Y 1 L PHE -93  ? D PHE 55  
1235 1 Y 1 L ASP -92  ? D ASP 56  
1236 1 Y 1 L VAL -91  ? D VAL 57  
1237 1 Y 1 L SER -90  ? D SER 58  
1238 1 Y 1 L LYS -89  ? D LYS 59  
1239 1 Y 1 L LYS -88  ? D LYS 60  
1240 1 Y 1 L ASP -87  ? D ASP 61  
1241 1 Y 1 L TYR -86  ? D TYR 62  
1242 1 Y 1 L ALA -85  ? D ALA 63  
1243 1 Y 1 L ASP -84  ? D ASP 64  
1244 1 Y 1 L SER -83  ? D SER 65  
1245 1 Y 1 L VAL -82  ? D VAL 66  
1246 1 Y 1 L LYS -81  ? D LYS 67  
1247 1 Y 1 L GLY -80  ? D GLY 68  
1248 1 Y 1 L ARG -79  ? D ARG 69  
1249 1 Y 1 L PHE -78  ? D PHE 70  
1250 1 Y 1 L THR -77  ? D THR 71  
1251 1 Y 1 L ILE -76  ? D ILE 72  
1252 1 Y 1 L SER -75  ? D SER 73  
1253 1 Y 1 L ARG -74  ? D ARG 74  
1254 1 Y 1 L ASP -73  ? D ASP 75  
1255 1 Y 1 L ASN -72  ? D ASN 76  
1256 1 Y 1 L SER -71  ? D SER 77  
1257 1 Y 1 L LYS -70  ? D LYS 78  
1258 1 Y 1 L ASN -69  ? D ASN 79  
1259 1 Y 1 L THR -68  ? D THR 80  
1260 1 Y 1 L LEU -67  ? D LEU 81  
1261 1 Y 1 L TYR -66  ? D TYR 82  
1262 1 Y 1 L LEU -65  ? D LEU 83  
1263 1 Y 1 L GLN -64  ? D GLN 84  
1264 1 Y 1 L MET -63  ? D MET 85  
1265 1 Y 1 L ASN -62  ? D ASN 86  
1266 1 Y 1 L SER -61  ? D SER 87  
1267 1 Y 1 L LEU -60  ? D LEU 88  
1268 1 Y 1 L ARG -59  ? D ARG 89  
1269 1 Y 1 L ALA -58  ? D ALA 90  
1270 1 Y 1 L GLU -57  ? D GLU 91  
1271 1 Y 1 L ASP -56  ? D ASP 92  
1272 1 Y 1 L THR -55  ? D THR 93  
1273 1 Y 1 L ALA -54  ? D ALA 94  
1274 1 Y 1 L VAL -53  ? D VAL 95  
1275 1 Y 1 L TYR -52  ? D TYR 96  
1276 1 Y 1 L TYR -51  ? D TYR 97  
1277 1 Y 1 L CYS -50  ? D CYS 98  
1278 1 Y 1 L ALA -49  ? D ALA 99  
1279 1 Y 1 L ARG -48  ? D ARG 100 
1280 1 Y 1 L ASN -47  ? D ASN 101 
1281 1 Y 1 L LEU -46  ? D LEU 102 
1282 1 Y 1 L ILE -45  ? D ILE 103 
1283 1 Y 1 L ARG -44  ? D ARG 104 
1284 1 Y 1 L TYR -43  ? D TYR 105 
1285 1 Y 1 L SER -42  ? D SER 106 
1286 1 Y 1 L GLY -41  ? D GLY 107 
1287 1 Y 1 L SER -40  ? D SER 108 
1288 1 Y 1 L TYR -39  ? D TYR 109 
1289 1 Y 1 L PHE -38  ? D PHE 110 
1290 1 Y 1 L PRO -37  ? D PRO 111 
1291 1 Y 1 L VAL -36  ? D VAL 112 
1292 1 Y 1 L HIS -35  ? D HIS 113 
1293 1 Y 1 L GLY -34  ? D GLY 114 
1294 1 Y 1 L MET -33  ? D MET 115 
1295 1 Y 1 L ASP -32  ? D ASP 116 
1296 1 Y 1 L VAL -31  ? D VAL 117 
1297 1 Y 1 L TRP -30  ? D TRP 118 
1298 1 Y 1 L GLY -29  ? D GLY 119 
1299 1 Y 1 L GLN -28  ? D GLN 120 
1300 1 Y 1 L GLY -27  ? D GLY 121 
1301 1 Y 1 L THR -26  ? D THR 122 
1302 1 Y 1 L THR -25  ? D THR 123 
1303 1 Y 1 L VAL -24  ? D VAL 124 
1304 1 Y 1 L THR -23  ? D THR 125 
1305 1 Y 1 L VAL -22  ? D VAL 126 
1306 1 Y 1 L SER -21  ? D SER 127 
1307 1 Y 1 L SER -20  ? D SER 128 
1308 1 Y 1 L GLY -19  ? D GLY 129 
1309 1 Y 1 L THR -18  ? D THR 130 
1310 1 Y 1 L GLY -17  ? D GLY 131 
1311 1 Y 1 L GLY -16  ? D GLY 132 
1312 1 Y 1 L SER -15  ? D SER 133 
1313 1 Y 1 L GLY -14  ? D GLY 134 
1314 1 Y 1 L GLY -13  ? D GLY 135 
1315 1 Y 1 L GLY -12  ? D GLY 136 
1316 1 Y 1 L GLY -11  ? D GLY 137 
1317 1 Y 1 L SER -10  ? D SER 138 
1318 1 Y 1 L GLY -9   ? D GLY 139 
1319 1 Y 1 L GLY -8   ? D GLY 140 
1320 1 Y 1 L GLY -7   ? D GLY 141 
1321 1 Y 1 L GLY -6   ? D GLY 142 
1322 1 Y 1 L SER -5   ? D SER 143 
1323 1 Y 1 L GLY -4   ? D GLY 144 
1324 1 Y 1 L GLY -3   ? D GLY 145 
1325 1 Y 1 L GLY -2   ? D GLY 146 
1326 1 Y 1 L ALA -1   ? D ALA 147 
1327 1 Y 1 L SER 0    ? D SER 148 
1328 1 Y 1 L ILE 105  ? D ILE 258 
1329 1 Y 1 L LYS 106  ? D LYS 259 
1330 1 Y 1 L GLY 107  ? D GLY 260 
1331 1 Y 1 L PRO 108  ? D PRO 261 
1332 1 Y 1 L PHE 109  ? D PHE 262 
1333 1 Y 1 L GLU 110  ? D GLU 263 
1334 1 Y 1 L ASP 111  ? D ASP 264 
1335 1 Y 1 L ASP 112  ? D ASP 265 
1336 1 Y 1 L ASP 113  ? D ASP 266 
1337 1 Y 1 L ASP 114  ? D ASP 267 
1338 1 Y 1 L LYS 115  ? D LYS 268 
1339 1 Y 1 L ALA 116  ? D ALA 269 
1340 1 Y 1 L GLY 117  ? D GLY 270 
1341 1 Y 1 L TRP 118  ? D TRP 271 
1342 1 Y 1 L SER 119  ? D SER 272 
1343 1 Y 1 L HIS 120  ? D HIS 273 
1344 1 Y 1 L PRO 121  ? D PRO 274 
1345 1 Y 1 L GLN 122  ? D GLN 275 
1346 1 Y 1 L PHE 123  ? D PHE 276 
1347 1 Y 1 L GLU 124  ? D GLU 277 
1348 1 Y 1 L LYS 125  ? D LYS 278 
1349 1 Y 1 L GLY 126  ? D GLY 279 
1350 1 Y 1 L GLY 127  ? D GLY 280 
1351 1 Y 1 L GLY 128  ? D GLY 281 
1352 1 Y 1 L SER 129  ? D SER 282 
1353 1 Y 1 L GLY 130  ? D GLY 283 
1354 1 Y 1 L GLY 131  ? D GLY 284 
1355 1 Y 1 L GLY 132  ? D GLY 285 
1356 1 Y 1 L SER 133  ? D SER 286 
1357 1 Y 1 L GLY 134  ? D GLY 287 
1358 1 Y 1 L GLY 135  ? D GLY 288 
1359 1 Y 1 L GLY 136  ? D GLY 289 
1360 1 Y 1 L SER 137  ? D SER 290 
1361 1 Y 1 L TRP 138  ? D TRP 291 
1362 1 Y 1 L SER 139  ? D SER 292 
1363 1 Y 1 L HIS 140  ? D HIS 293 
1364 1 Y 1 L PRO 141  ? D PRO 294 
1365 1 Y 1 L GLN 142  ? D GLN 295 
1366 1 Y 1 L PHE 143  ? D PHE 296 
1367 1 Y 1 L GLU 144  ? D GLU 297 
1368 1 Y 1 L LYS 145  ? D LYS 298 
# 
_pdbx_audit_support.funding_organization   'Agence Nationale de la Recherche (ANR)' 
_pdbx_audit_support.country                France 
_pdbx_audit_support.grant_number           ANR-18-CE11-0011 
_pdbx_audit_support.ordinal                1 
# 
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 
E 3 NAG 1 C NAG 1 A NAG 382  n 
E 3 NAG 2 C NAG 2 A NAG 383  n 
E 3 BMA 3 C BMA 3 A BMA 384  n 
E 3 MAN 4 C MAN 4 A MAN 385  n 
E 3 MAN 5 C MAN 5 A MAN 386  n 
E 3 MAN 6 C MAN 6 A MAN 389  n 
F 4 NAG 1 D NAG 1 A NAG 387  n 
F 4 NAG 2 D NAG 2 A NAG 388  n 
G 4 NAG 1 E NAG 1 B NAG 1095 n 
G 4 NAG 2 E NAG 2 B NAG 1096 n 
# 
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                            
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_entity_branch.entity_id 
_pdbx_entity_branch.type 
3 oligosaccharide 
4 oligosaccharide 
# 
loop_
_pdbx_entity_branch_descriptor.ordinal 
_pdbx_entity_branch_descriptor.entity_id 
_pdbx_entity_branch_descriptor.descriptor 
_pdbx_entity_branch_descriptor.type 
_pdbx_entity_branch_descriptor.program 
_pdbx_entity_branch_descriptor.program_version 
1 3 'DManpa1-2DManpa1-3[DManpa1-6]DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROH'                                                          
'Glycam Condensed Sequence' GMML       1.0   
2 3 'WURCS=2.0/3,6,5/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3-3-3/a4-b1_b4-c1_c3-d1_c6-f1_d2-e1'         
WURCS                       PDB2Glycan 1.1.0 
3 3 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{[(2+1)][a-D-Manp]{}}[(6+1)][a-D-Manp]{}}}}' 
LINUCS                      PDB-CARE   ?     
4 4 DGlcpNAcb1-4DGlcpNAcb1-ROH                                                                                                  
'Glycam Condensed Sequence' GMML       1.0   
5 4 'WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1'                                                                       
WURCS                       PDB2Glycan 1.1.0 
6 4 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}'                                                                             
LINUCS                      PDB-CARE   ?     
# 
loop_
_pdbx_entity_branch_link.link_id 
_pdbx_entity_branch_link.entity_id 
_pdbx_entity_branch_link.entity_branch_list_num_1 
_pdbx_entity_branch_link.comp_id_1 
_pdbx_entity_branch_link.atom_id_1 
_pdbx_entity_branch_link.leaving_atom_id_1 
_pdbx_entity_branch_link.entity_branch_list_num_2 
_pdbx_entity_branch_link.comp_id_2 
_pdbx_entity_branch_link.atom_id_2 
_pdbx_entity_branch_link.leaving_atom_id_2 
_pdbx_entity_branch_link.value_order 
_pdbx_entity_branch_link.details 
1 3 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
2 3 3 BMA C1 O1 2 NAG O4 HO4 sing ? 
3 3 4 MAN C1 O1 3 BMA O3 HO3 sing ? 
4 3 5 MAN C1 O1 4 MAN O2 HO2 sing ? 
5 3 6 MAN C1 O1 3 BMA O6 HO6 sing ? 
6 4 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
# 
loop_
_pdbx_entity_branch_list.entity_id 
_pdbx_entity_branch_list.comp_id 
_pdbx_entity_branch_list.num 
_pdbx_entity_branch_list.hetero 
3 NAG 1 n 
3 NAG 2 n 
3 BMA 3 n 
3 MAN 4 n 
3 MAN 5 n 
3 MAN 6 n 
4 NAG 1 n 
4 NAG 2 n 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
5 GLYCEROL GOL 
6 water    HOH 
# 
_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                ? 
# 
