data_5EBE
# 
_entry.id   5EBE 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.279 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   5EBE         
WWPDB D_1000214646 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        . 
_pdbx_database_related.db_id          5EBB 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        5EBE 
_pdbx_database_status.recvd_initial_deposition_date   2015-10-19 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Lim, S.M.'      1 
'Yeung, K.'      2 
'Tresaugues, L.' 3 
'Teo, H.L.'      4 
'Nordlund, P.'   5 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Febs J.' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1742-464X 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            283 
_citation.language                  ? 
_citation.page_first                1107 
_citation.page_last                 1123 
_citation.title                     
;The structure and catalytic mechanism of human sphingomyelin phosphodiesterase like 3a - an acid sphingomyelinase homologue with a novel nucleotide hydrolase activity.
;
_citation.year                      2016 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1111/febs.13655 
_citation.pdbx_database_id_PubMed   26783088 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Lim, S.M.'      1 
primary 'Yeung, K.'      2 
primary 'Tresaugues, L.' 3 
primary 'Ling, T.H.'     4 
primary 'Nordlund, P.'   5 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     5EBE 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     147.654 
_cell.length_a_esd                 ? 
_cell.length_b                     147.654 
_cell.length_b_esd                 ? 
_cell.length_c                     142.298 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        12 
_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                         5EBE 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                154 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 32 2 1' 
_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 'Acid sphingomyelinase-like phosphodiesterase 3a' 47597.648 1   3.1.4.- ? ? ? 
2  polymer     man 'Acid sphingomyelinase-like phosphodiesterase 3a' 47192.141 2   3.1.4.- ? ? ? 
3  non-polymer man N-ACETYL-D-GLUCOSAMINE                            221.208   13  ?       ? ? ? 
4  non-polymer syn 'ZINC ION'                                        65.409    6   ?       ? ? ? 
5  non-polymer syn "CYTIDINE-5'-MONOPHOSPHATE"                       323.197   2   ?       ? ? ? 
6  non-polymer syn GLYCEROL                                          92.094    2   ?       ? ? ? 
7  non-polymer syn 'MALONATE ION'                                    102.046   1   ?       ? ? ? 
8  non-polymer syn 5-O-phosphono-beta-D-ribofuranose                 230.110   1   ?       ? ? ? 
9  non-polymer syn 'THIOCYANATE ION'                                 58.082    2   ?       ? ? ? 
10 water       nat water                                             18.015    130 ?       ? ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'ASM-like phosphodiesterase 3a' 
2 'ASM-like phosphodiesterase 3a' 
# 
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 
;PPPAIGQFWHVTDLHLDPTYHITDDHTKVCASSKGANASNPGPFGDVLCDSPYQLILSAFDFIKNSGQEASFMIWTGDSP
PHVPVPELSTDTVINVITNMTTTIQSLFPNLQVFPALGNHDYWPQDQLPVVTSKVYNAVANLWKPWLDEEAISTLRKGGF
YSQKVTTNPNLRIISLNTNLYYGPNIMTLNKTDPANQFEWLESTLNNSQQNKEKVYIIAHVPVGYLPSSQNITAMREYYN
EKLIDIFQKYSDVIAGQFYGHTHRDSIMVLSDKKGSPVNSLFVAPAVTPVKSVLEKQTNNPGIRLFQYDPRDYKLLDMLQ
YYLNLTEANLKGESIWKLEYILTQTYDIEDLQPESLYGLAKQFTILDSKQFIKYYNYFFVSYDSSVTCDKTCKAFQICAI
MNLDNISYADCLKQLYIK
;
;PPPAIGQFWHVTDLHLDPTYHITDDHTKVCASSKGANASNPGPFGDVLCDSPYQLILSAFDFIKNSGQEASFMIWTGDSP
PHVPVPELSTDTVINVITNMTTTIQSLFPNLQVFPALGNHDYWPQDQLPVVTSKVYNAVANLWKPWLDEEAISTLRKGGF
YSQKVTTNPNLRIISLNTNLYYGPNIMTLNKTDPANQFEWLESTLNNSQQNKEKVYIIAHVPVGYLPSSQNITAMREYYN
EKLIDIFQKYSDVIAGQFYGHTHRDSIMVLSDKKGSPVNSLFVAPAVTPVKSVLEKQTNNPGIRLFQYDPRDYKLLDMLQ
YYLNLTEANLKGESIWKLEYILTQTYDIEDLQPESLYGLAKQFTILDSKQFIKYYNYFFVSYDSSVTCDKTCKAFQICAI
MNLDNISYADCLKQLYIK
;
A   ? 
2 'polypeptide(L)' no no 
;PPPAIGQFWHVTDLHLDPTYHITDDHTKVCASSKGANASNPGPFGDVLCDSPYQLILSAFDFIKNSGQEASFMIWTGDSP
PHVPVPELSTDTVINVITNMTTTIQSLFPNLQVFPALGNHDYWPQDQLPVVTSKVYNAVANLWKPWLDEEAISTLRKGGF
YSQKVTTNPNLRIISLNTNLYYGPNIMTLNKTDPANQFEWLESTLNNSQQNKEKVYIIAHVPVGYLPSSQNITAMREYYN
EKLIDIFQKYSDVIAGQFYGHTHRDSIMVLSDKKGSPVNSLFVAPAVTPVKSVLEKQTNNPGIRLFQYDPRDYKLLDMLQ
YYLNLTEANLKGESIWKLEYILTQTYDIEDLQPESLYGLAKQFTILDSKQFIKYYNYFFVSYDSSVTCDKTCKAFQICAI
MNLDNISYADCLKQL
;
;PPPAIGQFWHVTDLHLDPTYHITDDHTKVCASSKGANASNPGPFGDVLCDSPYQLILSAFDFIKNSGQEASFMIWTGDSP
PHVPVPELSTDTVINVITNMTTTIQSLFPNLQVFPALGNHDYWPQDQLPVVTSKVYNAVANLWKPWLDEEAISTLRKGGF
YSQKVTTNPNLRIISLNTNLYYGPNIMTLNKTDPANQFEWLESTLNNSQQNKEKVYIIAHVPVGYLPSSQNITAMREYYN
EKLIDIFQKYSDVIAGQFYGHTHRDSIMVLSDKKGSPVNSLFVAPAVTPVKSVLEKQTNNPGIRLFQYDPRDYKLLDMLQ
YYLNLTEANLKGESIWKLEYILTQTYDIEDLQPESLYGLAKQFTILDSKQFIKYYNYFFVSYDSSVTCDKTCKAFQICAI
MNLDNISYADCLKQL
;
B,C ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   PRO n 
1 2   PRO n 
1 3   PRO n 
1 4   ALA n 
1 5   ILE n 
1 6   GLY n 
1 7   GLN n 
1 8   PHE n 
1 9   TRP n 
1 10  HIS n 
1 11  VAL n 
1 12  THR n 
1 13  ASP n 
1 14  LEU n 
1 15  HIS n 
1 16  LEU n 
1 17  ASP n 
1 18  PRO n 
1 19  THR n 
1 20  TYR n 
1 21  HIS n 
1 22  ILE n 
1 23  THR n 
1 24  ASP n 
1 25  ASP n 
1 26  HIS n 
1 27  THR n 
1 28  LYS n 
1 29  VAL n 
1 30  CYS n 
1 31  ALA n 
1 32  SER n 
1 33  SER n 
1 34  LYS n 
1 35  GLY n 
1 36  ALA n 
1 37  ASN n 
1 38  ALA n 
1 39  SER n 
1 40  ASN n 
1 41  PRO n 
1 42  GLY n 
1 43  PRO n 
1 44  PHE n 
1 45  GLY n 
1 46  ASP n 
1 47  VAL n 
1 48  LEU n 
1 49  CYS n 
1 50  ASP n 
1 51  SER n 
1 52  PRO n 
1 53  TYR n 
1 54  GLN n 
1 55  LEU n 
1 56  ILE n 
1 57  LEU n 
1 58  SER n 
1 59  ALA n 
1 60  PHE n 
1 61  ASP n 
1 62  PHE n 
1 63  ILE n 
1 64  LYS n 
1 65  ASN n 
1 66  SER n 
1 67  GLY n 
1 68  GLN n 
1 69  GLU n 
1 70  ALA n 
1 71  SER n 
1 72  PHE n 
1 73  MET n 
1 74  ILE n 
1 75  TRP n 
1 76  THR n 
1 77  GLY n 
1 78  ASP n 
1 79  SER n 
1 80  PRO n 
1 81  PRO n 
1 82  HIS n 
1 83  VAL n 
1 84  PRO n 
1 85  VAL n 
1 86  PRO n 
1 87  GLU n 
1 88  LEU n 
1 89  SER n 
1 90  THR n 
1 91  ASP n 
1 92  THR n 
1 93  VAL n 
1 94  ILE n 
1 95  ASN n 
1 96  VAL n 
1 97  ILE n 
1 98  THR n 
1 99  ASN n 
1 100 MET n 
1 101 THR n 
1 102 THR n 
1 103 THR n 
1 104 ILE n 
1 105 GLN n 
1 106 SER n 
1 107 LEU n 
1 108 PHE n 
1 109 PRO n 
1 110 ASN n 
1 111 LEU n 
1 112 GLN n 
1 113 VAL n 
1 114 PHE n 
1 115 PRO n 
1 116 ALA n 
1 117 LEU n 
1 118 GLY n 
1 119 ASN n 
1 120 HIS n 
1 121 ASP n 
1 122 TYR n 
1 123 TRP n 
1 124 PRO n 
1 125 GLN n 
1 126 ASP n 
1 127 GLN n 
1 128 LEU n 
1 129 PRO n 
1 130 VAL n 
1 131 VAL n 
1 132 THR n 
1 133 SER n 
1 134 LYS n 
1 135 VAL n 
1 136 TYR n 
1 137 ASN n 
1 138 ALA n 
1 139 VAL n 
1 140 ALA n 
1 141 ASN n 
1 142 LEU n 
1 143 TRP n 
1 144 LYS n 
1 145 PRO n 
1 146 TRP n 
1 147 LEU n 
1 148 ASP n 
1 149 GLU n 
1 150 GLU n 
1 151 ALA n 
1 152 ILE n 
1 153 SER n 
1 154 THR n 
1 155 LEU n 
1 156 ARG n 
1 157 LYS n 
1 158 GLY n 
1 159 GLY n 
1 160 PHE n 
1 161 TYR n 
1 162 SER n 
1 163 GLN n 
1 164 LYS n 
1 165 VAL n 
1 166 THR n 
1 167 THR n 
1 168 ASN n 
1 169 PRO n 
1 170 ASN n 
1 171 LEU n 
1 172 ARG n 
1 173 ILE n 
1 174 ILE n 
1 175 SER n 
1 176 LEU n 
1 177 ASN n 
1 178 THR n 
1 179 ASN n 
1 180 LEU n 
1 181 TYR n 
1 182 TYR n 
1 183 GLY n 
1 184 PRO n 
1 185 ASN n 
1 186 ILE n 
1 187 MET n 
1 188 THR n 
1 189 LEU n 
1 190 ASN n 
1 191 LYS n 
1 192 THR n 
1 193 ASP n 
1 194 PRO n 
1 195 ALA n 
1 196 ASN n 
1 197 GLN n 
1 198 PHE n 
1 199 GLU n 
1 200 TRP n 
1 201 LEU n 
1 202 GLU n 
1 203 SER n 
1 204 THR n 
1 205 LEU n 
1 206 ASN n 
1 207 ASN n 
1 208 SER n 
1 209 GLN n 
1 210 GLN n 
1 211 ASN n 
1 212 LYS n 
1 213 GLU n 
1 214 LYS n 
1 215 VAL n 
1 216 TYR n 
1 217 ILE n 
1 218 ILE n 
1 219 ALA n 
1 220 HIS n 
1 221 VAL n 
1 222 PRO n 
1 223 VAL n 
1 224 GLY n 
1 225 TYR n 
1 226 LEU n 
1 227 PRO n 
1 228 SER n 
1 229 SER n 
1 230 GLN n 
1 231 ASN n 
1 232 ILE n 
1 233 THR n 
1 234 ALA n 
1 235 MET n 
1 236 ARG n 
1 237 GLU n 
1 238 TYR n 
1 239 TYR n 
1 240 ASN n 
1 241 GLU n 
1 242 LYS n 
1 243 LEU n 
1 244 ILE n 
1 245 ASP n 
1 246 ILE n 
1 247 PHE n 
1 248 GLN n 
1 249 LYS n 
1 250 TYR n 
1 251 SER n 
1 252 ASP n 
1 253 VAL n 
1 254 ILE n 
1 255 ALA n 
1 256 GLY n 
1 257 GLN n 
1 258 PHE n 
1 259 TYR n 
1 260 GLY n 
1 261 HIS n 
1 262 THR n 
1 263 HIS n 
1 264 ARG n 
1 265 ASP n 
1 266 SER n 
1 267 ILE n 
1 268 MET n 
1 269 VAL n 
1 270 LEU n 
1 271 SER n 
1 272 ASP n 
1 273 LYS n 
1 274 LYS n 
1 275 GLY n 
1 276 SER n 
1 277 PRO n 
1 278 VAL n 
1 279 ASN n 
1 280 SER n 
1 281 LEU n 
1 282 PHE n 
1 283 VAL n 
1 284 ALA n 
1 285 PRO n 
1 286 ALA n 
1 287 VAL n 
1 288 THR n 
1 289 PRO n 
1 290 VAL n 
1 291 LYS n 
1 292 SER n 
1 293 VAL n 
1 294 LEU n 
1 295 GLU n 
1 296 LYS n 
1 297 GLN n 
1 298 THR n 
1 299 ASN n 
1 300 ASN n 
1 301 PRO n 
1 302 GLY n 
1 303 ILE n 
1 304 ARG n 
1 305 LEU n 
1 306 PHE n 
1 307 GLN n 
1 308 TYR n 
1 309 ASP n 
1 310 PRO n 
1 311 ARG n 
1 312 ASP n 
1 313 TYR n 
1 314 LYS n 
1 315 LEU n 
1 316 LEU n 
1 317 ASP n 
1 318 MET n 
1 319 LEU n 
1 320 GLN n 
1 321 TYR n 
1 322 TYR n 
1 323 LEU n 
1 324 ASN n 
1 325 LEU n 
1 326 THR n 
1 327 GLU n 
1 328 ALA n 
1 329 ASN n 
1 330 LEU n 
1 331 LYS n 
1 332 GLY n 
1 333 GLU n 
1 334 SER n 
1 335 ILE n 
1 336 TRP n 
1 337 LYS n 
1 338 LEU n 
1 339 GLU n 
1 340 TYR n 
1 341 ILE n 
1 342 LEU n 
1 343 THR n 
1 344 GLN n 
1 345 THR n 
1 346 TYR n 
1 347 ASP n 
1 348 ILE n 
1 349 GLU n 
1 350 ASP n 
1 351 LEU n 
1 352 GLN n 
1 353 PRO n 
1 354 GLU n 
1 355 SER n 
1 356 LEU n 
1 357 TYR n 
1 358 GLY n 
1 359 LEU n 
1 360 ALA n 
1 361 LYS n 
1 362 GLN n 
1 363 PHE n 
1 364 THR n 
1 365 ILE n 
1 366 LEU n 
1 367 ASP n 
1 368 SER n 
1 369 LYS n 
1 370 GLN n 
1 371 PHE n 
1 372 ILE n 
1 373 LYS n 
1 374 TYR n 
1 375 TYR n 
1 376 ASN n 
1 377 TYR n 
1 378 PHE n 
1 379 PHE n 
1 380 VAL n 
1 381 SER n 
1 382 TYR n 
1 383 ASP n 
1 384 SER n 
1 385 SER n 
1 386 VAL n 
1 387 THR n 
1 388 CYS n 
1 389 ASP n 
1 390 LYS n 
1 391 THR n 
1 392 CYS n 
1 393 LYS n 
1 394 ALA n 
1 395 PHE n 
1 396 GLN n 
1 397 ILE n 
1 398 CYS n 
1 399 ALA n 
1 400 ILE n 
1 401 MET n 
1 402 ASN n 
1 403 LEU n 
1 404 ASP n 
1 405 ASN n 
1 406 ILE n 
1 407 SER n 
1 408 TYR n 
1 409 ALA n 
1 410 ASP n 
1 411 CYS n 
1 412 LEU n 
1 413 LYS n 
1 414 GLN n 
1 415 LEU n 
1 416 TYR n 
1 417 ILE n 
1 418 LYS n 
2 1   PRO n 
2 2   PRO n 
2 3   PRO n 
2 4   ALA n 
2 5   ILE n 
2 6   GLY n 
2 7   GLN n 
2 8   PHE n 
2 9   TRP n 
2 10  HIS n 
2 11  VAL n 
2 12  THR n 
2 13  ASP n 
2 14  LEU n 
2 15  HIS n 
2 16  LEU n 
2 17  ASP n 
2 18  PRO n 
2 19  THR n 
2 20  TYR n 
2 21  HIS n 
2 22  ILE n 
2 23  THR n 
2 24  ASP n 
2 25  ASP n 
2 26  HIS n 
2 27  THR n 
2 28  LYS n 
2 29  VAL n 
2 30  CYS n 
2 31  ALA n 
2 32  SER n 
2 33  SER n 
2 34  LYS n 
2 35  GLY n 
2 36  ALA n 
2 37  ASN n 
2 38  ALA n 
2 39  SER n 
2 40  ASN n 
2 41  PRO n 
2 42  GLY n 
2 43  PRO n 
2 44  PHE n 
2 45  GLY n 
2 46  ASP n 
2 47  VAL n 
2 48  LEU n 
2 49  CYS n 
2 50  ASP n 
2 51  SER n 
2 52  PRO n 
2 53  TYR n 
2 54  GLN n 
2 55  LEU n 
2 56  ILE n 
2 57  LEU n 
2 58  SER n 
2 59  ALA n 
2 60  PHE n 
2 61  ASP n 
2 62  PHE n 
2 63  ILE n 
2 64  LYS n 
2 65  ASN n 
2 66  SER n 
2 67  GLY n 
2 68  GLN n 
2 69  GLU n 
2 70  ALA n 
2 71  SER n 
2 72  PHE n 
2 73  MET n 
2 74  ILE n 
2 75  TRP n 
2 76  THR n 
2 77  GLY n 
2 78  ASP n 
2 79  SER n 
2 80  PRO n 
2 81  PRO n 
2 82  HIS n 
2 83  VAL n 
2 84  PRO n 
2 85  VAL n 
2 86  PRO n 
2 87  GLU n 
2 88  LEU n 
2 89  SER n 
2 90  THR n 
2 91  ASP n 
2 92  THR n 
2 93  VAL n 
2 94  ILE n 
2 95  ASN n 
2 96  VAL n 
2 97  ILE n 
2 98  THR n 
2 99  ASN n 
2 100 MET n 
2 101 THR n 
2 102 THR n 
2 103 THR n 
2 104 ILE n 
2 105 GLN n 
2 106 SER n 
2 107 LEU n 
2 108 PHE n 
2 109 PRO n 
2 110 ASN n 
2 111 LEU n 
2 112 GLN n 
2 113 VAL n 
2 114 PHE n 
2 115 PRO n 
2 116 ALA n 
2 117 LEU n 
2 118 GLY n 
2 119 ASN n 
2 120 HIS n 
2 121 ASP n 
2 122 TYR n 
2 123 TRP n 
2 124 PRO n 
2 125 GLN n 
2 126 ASP n 
2 127 GLN n 
2 128 LEU n 
2 129 PRO n 
2 130 VAL n 
2 131 VAL n 
2 132 THR n 
2 133 SER n 
2 134 LYS n 
2 135 VAL n 
2 136 TYR n 
2 137 ASN n 
2 138 ALA n 
2 139 VAL n 
2 140 ALA n 
2 141 ASN n 
2 142 LEU n 
2 143 TRP n 
2 144 LYS n 
2 145 PRO n 
2 146 TRP n 
2 147 LEU n 
2 148 ASP n 
2 149 GLU n 
2 150 GLU n 
2 151 ALA n 
2 152 ILE n 
2 153 SER n 
2 154 THR n 
2 155 LEU n 
2 156 ARG n 
2 157 LYS n 
2 158 GLY n 
2 159 GLY n 
2 160 PHE n 
2 161 TYR n 
2 162 SER n 
2 163 GLN n 
2 164 LYS n 
2 165 VAL n 
2 166 THR n 
2 167 THR n 
2 168 ASN n 
2 169 PRO n 
2 170 ASN n 
2 171 LEU n 
2 172 ARG n 
2 173 ILE n 
2 174 ILE n 
2 175 SER n 
2 176 LEU n 
2 177 ASN n 
2 178 THR n 
2 179 ASN n 
2 180 LEU n 
2 181 TYR n 
2 182 TYR n 
2 183 GLY n 
2 184 PRO n 
2 185 ASN n 
2 186 ILE n 
2 187 MET n 
2 188 THR n 
2 189 LEU n 
2 190 ASN n 
2 191 LYS n 
2 192 THR n 
2 193 ASP n 
2 194 PRO n 
2 195 ALA n 
2 196 ASN n 
2 197 GLN n 
2 198 PHE n 
2 199 GLU n 
2 200 TRP n 
2 201 LEU n 
2 202 GLU n 
2 203 SER n 
2 204 THR n 
2 205 LEU n 
2 206 ASN n 
2 207 ASN n 
2 208 SER n 
2 209 GLN n 
2 210 GLN n 
2 211 ASN n 
2 212 LYS n 
2 213 GLU n 
2 214 LYS n 
2 215 VAL n 
2 216 TYR n 
2 217 ILE n 
2 218 ILE n 
2 219 ALA n 
2 220 HIS n 
2 221 VAL n 
2 222 PRO n 
2 223 VAL n 
2 224 GLY n 
2 225 TYR n 
2 226 LEU n 
2 227 PRO n 
2 228 SER n 
2 229 SER n 
2 230 GLN n 
2 231 ASN n 
2 232 ILE n 
2 233 THR n 
2 234 ALA n 
2 235 MET n 
2 236 ARG n 
2 237 GLU n 
2 238 TYR n 
2 239 TYR n 
2 240 ASN n 
2 241 GLU n 
2 242 LYS n 
2 243 LEU n 
2 244 ILE n 
2 245 ASP n 
2 246 ILE n 
2 247 PHE n 
2 248 GLN n 
2 249 LYS n 
2 250 TYR n 
2 251 SER n 
2 252 ASP n 
2 253 VAL n 
2 254 ILE n 
2 255 ALA n 
2 256 GLY n 
2 257 GLN n 
2 258 PHE n 
2 259 TYR n 
2 260 GLY n 
2 261 HIS n 
2 262 THR n 
2 263 HIS n 
2 264 ARG n 
2 265 ASP n 
2 266 SER n 
2 267 ILE n 
2 268 MET n 
2 269 VAL n 
2 270 LEU n 
2 271 SER n 
2 272 ASP n 
2 273 LYS n 
2 274 LYS n 
2 275 GLY n 
2 276 SER n 
2 277 PRO n 
2 278 VAL n 
2 279 ASN n 
2 280 SER n 
2 281 LEU n 
2 282 PHE n 
2 283 VAL n 
2 284 ALA n 
2 285 PRO n 
2 286 ALA n 
2 287 VAL n 
2 288 THR n 
2 289 PRO n 
2 290 VAL n 
2 291 LYS n 
2 292 SER n 
2 293 VAL n 
2 294 LEU n 
2 295 GLU n 
2 296 LYS n 
2 297 GLN n 
2 298 THR n 
2 299 ASN n 
2 300 ASN n 
2 301 PRO n 
2 302 GLY n 
2 303 ILE n 
2 304 ARG n 
2 305 LEU n 
2 306 PHE n 
2 307 GLN n 
2 308 TYR n 
2 309 ASP n 
2 310 PRO n 
2 311 ARG n 
2 312 ASP n 
2 313 TYR n 
2 314 LYS n 
2 315 LEU n 
2 316 LEU n 
2 317 ASP n 
2 318 MET n 
2 319 LEU n 
2 320 GLN n 
2 321 TYR n 
2 322 TYR n 
2 323 LEU n 
2 324 ASN n 
2 325 LEU n 
2 326 THR n 
2 327 GLU n 
2 328 ALA n 
2 329 ASN n 
2 330 LEU n 
2 331 LYS n 
2 332 GLY n 
2 333 GLU n 
2 334 SER n 
2 335 ILE n 
2 336 TRP n 
2 337 LYS n 
2 338 LEU n 
2 339 GLU n 
2 340 TYR n 
2 341 ILE n 
2 342 LEU n 
2 343 THR n 
2 344 GLN n 
2 345 THR n 
2 346 TYR n 
2 347 ASP n 
2 348 ILE n 
2 349 GLU n 
2 350 ASP n 
2 351 LEU n 
2 352 GLN n 
2 353 PRO n 
2 354 GLU n 
2 355 SER n 
2 356 LEU n 
2 357 TYR n 
2 358 GLY n 
2 359 LEU n 
2 360 ALA n 
2 361 LYS n 
2 362 GLN n 
2 363 PHE n 
2 364 THR n 
2 365 ILE n 
2 366 LEU n 
2 367 ASP n 
2 368 SER n 
2 369 LYS n 
2 370 GLN n 
2 371 PHE n 
2 372 ILE n 
2 373 LYS n 
2 374 TYR n 
2 375 TYR n 
2 376 ASN n 
2 377 TYR n 
2 378 PHE n 
2 379 PHE n 
2 380 VAL n 
2 381 SER n 
2 382 TYR n 
2 383 ASP n 
2 384 SER n 
2 385 SER n 
2 386 VAL n 
2 387 THR n 
2 388 CYS n 
2 389 ASP n 
2 390 LYS n 
2 391 THR n 
2 392 CYS n 
2 393 LYS n 
2 394 ALA n 
2 395 PHE n 
2 396 GLN n 
2 397 ILE n 
2 398 CYS n 
2 399 ALA n 
2 400 ILE n 
2 401 MET n 
2 402 ASN n 
2 403 LEU n 
2 404 ASP n 
2 405 ASN n 
2 406 ILE n 
2 407 SER n 
2 408 TYR n 
2 409 ALA n 
2 410 ASP n 
2 411 CYS n 
2 412 LEU n 
2 413 LYS n 
2 414 GLN n 
2 415 LEU 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' 1 418 Human ? 'SMPDL3A, ASML3A' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? 'fall armyworm' 
'Spodoptera frugiperda' 7108 ? ? ? ? ? ? Sf9 ? ? ? ? ? ? ? ? ? ? ? pFB-Sec-NH ? ? 
2 1 sample 'Biological sequence' 1 415 Human ? 'SMPDL3A, ASML3A' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? 'fall armyworm' 
'Spodoptera frugiperda' 7108 ? ? ? ? ? ? ?   ? ? ? ? ? ? ? ? ? ? ? pFB-SEC-NH ? ? 
# 
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 ASM3A_HUMAN Q92484 ? 1 
;PPPAIGQFWHVTDLHLDPTYHITDDHTKVCASSKGANASNPGPFGDVLCDSPYQLILSAFDFIKNSGQEASFMIWTGDSP
PHVPVPELSTDTVINVITNMTTTIQSLFPNLQVFPALGNHDYWPQDQLPVVTSKVYNAVANLWKPWLDEEAISTLRKGGF
YSQKVTTNPNLRIISLNTNLYYGPNIMTLNKTDPANQFEWLESTLNNSQQNKEKVYIIAHVPVGYLPSSQNITAMREYYN
EKLIDIFQKYSDVIAGQFYGHTHRDSIMVLSDKKGSPVNSLFVAPAVTPVKSVLEKQTNNPGIRLFQYDPRDYKLLDMLQ
YYLNLTEANLKGESIWKLEYILTQTYDIEDLQPESLYGLAKQFTILDSKQFIKYYNYFFVSYDSSVTCDKTCKAFQICAI
MNLDNISYADCLKQLYIK
;
33 
2 UNP ASM3A_HUMAN Q92484 ? 2 
;PPPAIGQFWHVTDLHLDPTYHITDDHTKVCASSKGANASNPGPFGDVLCDSPYQLILSAFDFIKNSGQEASFMIWTGDSP
PHVPVPELSTDTVINVITNMTTTIQSLFPNLQVFPALGNHDYWPQDQLPVVTSKVYNAVANLWKPWLDEEAISTLRKGGF
YSQKVTTNPNLRIISLNTNLYYGPNIMTLNKTDPANQFEWLESTLNNSQQNKEKVYIIAHVPVGYLPSSQNITAMREYYN
EKLIDIFQKYSDVIAGQFYGHTHRDSIMVLSDKKGSPVNSLFVAPAVTPVKSVLEKQTNNPGIRLFQYDPRDYKLLDMLQ
YYLNLTEANLKGESIWKLEYILTQTYDIEDLQPESLYGLAKQFTILDSKQFIKYYNYFFVSYDSSVTCDKTCKAFQICAI
MNLDNISYADCLKQL
;
33 
# 
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 5EBE A 1 ? 418 ? Q92484 33 ? 450 ? 33 450 
2 2 5EBE B 1 ? 415 ? Q92484 33 ? 447 ? 33 447 
3 2 5EBE C 1 ? 415 ? Q92484 33 ? 447 ? 33 447 
# 
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 
C5P non-polymer         . "CYTIDINE-5'-MONOPHOSPHATE"       ? 'C9 H14 N3 O8 P' 323.197 
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 
MET 'L-peptide linking' y METHIONINE                        ? 'C5 H11 N O2 S'  149.211 
MLI non-polymer         . 'MALONATE ION'                    ? 'C3 H2 O4 -2'    102.046 
NAG D-saccharide        . 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 
RP5 non-polymer         . 5-O-phosphono-beta-D-ribofuranose 
'[(2R,3S,4S,5R)-3,4,5-TRIHYDROXYTETRAHYDROFURAN-2-YL]METHYL DIHYDROGEN PHOSPHATE' 'C5 H11 O8 P'    230.110 
SCN non-polymer         . 'THIOCYANATE ION'                 ? 'C N S -1'       58.082  
SER 'L-peptide linking' y SERINE                            ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE                         ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                        ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                          ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                            ? 'C5 H11 N O2'    117.146 
ZN  non-polymer         . 'ZINC ION'                        ? 'Zn 2'           65.409  
# 
_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                   5EBE 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                      ? 
_exptl_crystal.density_diffrn              ? 
_exptl_crystal.density_Matthews            3.15 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         57.39 
_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              7.2 
_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    
;Crystal grew in 2.08 M disodium malonate pH 7.2, 0.23 M sodium thiocyanate and 0.01 M TCEP. But soaked at 2.08M disodium malonate pH 5
;
_exptl_crystal_grow.pdbx_pH_range   5-7.2 
# 
_diffrn.ambient_environment    ? 
_diffrn.ambient_temp           80 
_diffrn.ambient_temp_details   ? 
_diffrn.ambient_temp_esd       ? 
_diffrn.crystal_id             1 
_diffrn.crystal_support        ? 
_diffrn.crystal_treatment      ? 
_diffrn.details                ? 
_diffrn.id                     1 
_diffrn.ambient_pressure       ? 
_diffrn.ambient_pressure_esd   ? 
_diffrn.ambient_pressure_gt    ? 
_diffrn.ambient_pressure_lt    ? 
_diffrn.ambient_temp_gt        ? 
_diffrn.ambient_temp_lt        ? 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'ADSC QUANTUM 315r' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2015-07-17 
# 
_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   0.9537 
_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                        'AUSTRALIAN SYNCHROTRON BEAMLINE MX2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9537 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   MX2 
_diffrn_source.pdbx_synchrotron_site       'Australian Synchrotron' 
# 
_reflns.B_iso_Wilson_estimate            ? 
_reflns.entry_id                         5EBE 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                3.0 
_reflns.d_resolution_low                 47.56 
_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                       40035 
_reflns.number_obs                       36234 
_reflns.observed_criterion               ? 
_reflns.observed_criterion_F_max         ? 
_reflns.observed_criterion_F_min         ? 
_reflns.observed_criterion_I_max         ? 
_reflns.observed_criterion_I_min         ? 
_reflns.observed_criterion_sigma_F       ? 
_reflns.observed_criterion_sigma_I       ? 
_reflns.percent_possible_obs             99.7 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  3.7 
_reflns.pdbx_Rmerge_I_obs                0.156 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  ? 
_reflns.pdbx_netI_over_av_sigmaI         ? 
_reflns.pdbx_netI_over_sigmaI            6.3 
_reflns.pdbx_res_netI_over_av_sigmaI_2   ? 
_reflns.pdbx_res_netI_over_sigmaI_2      ? 
_reflns.pdbx_chi_squared                 ? 
_reflns.pdbx_scaling_rejects             ? 
_reflns.pdbx_d_res_high_opt              ? 
_reflns.pdbx_d_res_low_opt               ? 
_reflns.pdbx_d_res_opt_method            ? 
_reflns.phase_calculation_details        ? 
_reflns.pdbx_Rrim_I_all                  ? 
_reflns.pdbx_Rpim_I_all                  ? 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         ? 
_reflns.pdbx_diffrn_id                   1 
_reflns.pdbx_ordinal                     1 
_reflns.pdbx_CC_half                     ? 
_reflns.pdbx_R_split                     ? 
# 
_reflns_shell.d_res_high                  3.0 
_reflns_shell.d_res_low                   3.13 
_reflns_shell.meanI_over_sigI_all         ? 
_reflns_shell.meanI_over_sigI_obs         1.9 
_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        99.9 
_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                0.60 
_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             3.7 
_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                1 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_CC_half                ? 
_reflns_shell.pdbx_R_split                ? 
# 
_refine.aniso_B[1][1]                            0.50 
_refine.aniso_B[1][2]                            0.25 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            0.50 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            -1.61 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               40.035 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.945 
_refine.correlation_coeff_Fo_to_Fc_free          0.908 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_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                                 5EBE 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            3.00 
_refine.ls_d_res_low                             47.56 
_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                     34411 
_refine.ls_number_reflns_R_free                  1790 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.63 
_refine.ls_percent_reflns_R_free                 4.9 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.25361 
_refine.ls_R_factor_R_free                       0.29481 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.25145 
_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                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_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                      5ebb 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.424 
_refine.pdbx_overall_ESU_R_Free                  0.497 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_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                            0.000 
_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                         1 
_refine_hist.pdbx_number_atoms_protein        10016 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         268 
_refine_hist.number_atoms_solvent             130 
_refine_hist.number_atoms_total               10414 
_refine_hist.d_res_high                       3.00 
_refine_hist.d_res_low                        47.56 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       3.000 
_refine_ls_shell.d_res_low                        3.078 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             121 
_refine_ls_shell.number_reflns_R_work             2566 
_refine_ls_shell.percent_reflns_obs               99.93 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free                  0.387 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.361 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
# 
_struct.entry_id                     5EBE 
_struct.title                        
;Structure of human sphingomyelinase phosphodiesterase like 3A (SMPDL3A) with 5' CMP
;
_struct.pdbx_descriptor              'Acid sphingomyelinase-like phosphodiesterase 3a (E.C.3.1.4.-)' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               ? 
# 
_struct_keywords.entry_id        5EBE 
_struct_keywords.text            
'calcineurin like phosphodiesterase, binuclear metallophosphodiesterase, acid sphingomyelinase like, hydrolase' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A  N N 1  ? 
B  N N 2  ? 
C  N N 2  ? 
D  N N 3  ? 
E  N N 3  ? 
F  N N 3  ? 
G  N N 3  ? 
H  N N 4  ? 
I  N N 4  ? 
J  N N 5  ? 
K  N N 3  ? 
L  N N 3  ? 
M  N N 3  ? 
N  N N 3  ? 
O  N N 3  ? 
P  N N 4  ? 
Q  N N 4  ? 
R  N N 6  ? 
S  N N 6  ? 
T  N N 7  ? 
U  N N 8  ? 
V  N N 3  ? 
W  N N 3  ? 
X  N N 3  ? 
Y  N N 3  ? 
Z  N N 4  ? 
AA N N 4  ? 
BA N N 5  ? 
CA N N 9  ? 
DA N N 9  ? 
EA N N 10 ? 
FA N N 10 ? 
GA N N 10 ? 
# 
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 CYS A 30  ? LYS A 34  ? CYS A 62  LYS A 66  5 ? 5  
HELX_P HELX_P2  AA2 PRO A 52  ? ASN A 65  ? PRO A 84  ASN A 97  1 ? 14 
HELX_P HELX_P3  AA3 PRO A 84  ? LEU A 88  ? PRO A 116 LEU A 120 5 ? 5  
HELX_P HELX_P4  AA4 SER A 89  ? PHE A 108 ? SER A 121 PHE A 140 1 ? 20 
HELX_P HELX_P5  AA5 SER A 133 ? LYS A 144 ? SER A 165 LYS A 176 1 ? 12 
HELX_P HELX_P6  AA6 PRO A 145 ? LEU A 147 ? PRO A 177 LEU A 179 5 ? 3  
HELX_P HELX_P7  AA7 ASP A 148 ? GLY A 159 ? ASP A 180 GLY A 191 1 ? 12 
HELX_P HELX_P8  AA8 ASN A 177 ? TYR A 182 ? ASN A 209 TYR A 214 5 ? 6  
HELX_P HELX_P9  AA9 ASN A 185 ? LEU A 189 ? ASN A 217 LEU A 221 5 ? 5  
HELX_P HELX_P10 AB1 ASP A 193 ? ALA A 195 ? ASP A 225 ALA A 227 5 ? 3  
HELX_P HELX_P11 AB2 ASN A 196 ? ASN A 211 ? ASN A 228 ASN A 243 1 ? 16 
HELX_P HELX_P12 AB3 ARG A 236 ? TYR A 250 ? ARG A 268 TYR A 282 1 ? 15 
HELX_P HELX_P13 AB4 ASN A 324 ? GLY A 332 ? ASN A 356 GLY A 364 1 ? 9  
HELX_P HELX_P14 AB5 LEU A 342 ? ASP A 347 ? LEU A 374 ASP A 379 1 ? 6  
HELX_P HELX_P15 AB6 GLN A 352 ? ILE A 365 ? GLN A 384 ILE A 397 1 ? 14 
HELX_P HELX_P16 AB7 SER A 368 ? PHE A 379 ? SER A 400 PHE A 411 1 ? 12 
HELX_P HELX_P17 AB8 ASP A 389 ? ASN A 402 ? ASP A 421 ASN A 434 1 ? 14 
HELX_P HELX_P18 AB9 ASP A 404 ? GLN A 414 ? ASP A 436 GLN A 446 1 ? 11 
HELX_P HELX_P19 AC1 CYS B 30  ? LYS B 34  ? CYS B 62  LYS B 66  5 ? 5  
HELX_P HELX_P20 AC2 PRO B 52  ? ASN B 65  ? PRO B 84  ASN B 97  1 ? 14 
HELX_P HELX_P21 AC3 PRO B 84  ? LEU B 88  ? PRO B 116 LEU B 120 5 ? 5  
HELX_P HELX_P22 AC4 SER B 89  ? PHE B 108 ? SER B 121 PHE B 140 1 ? 20 
HELX_P HELX_P23 AC5 SER B 133 ? LYS B 144 ? SER B 165 LYS B 176 1 ? 12 
HELX_P HELX_P24 AC6 ASP B 148 ? GLY B 158 ? ASP B 180 GLY B 190 1 ? 11 
HELX_P HELX_P25 AC7 ASN B 177 ? TYR B 182 ? ASN B 209 TYR B 214 5 ? 6  
HELX_P HELX_P26 AC8 ASP B 193 ? ALA B 195 ? ASP B 225 ALA B 227 5 ? 3  
HELX_P HELX_P27 AC9 ASN B 196 ? ASN B 211 ? ASN B 228 ASN B 243 1 ? 16 
HELX_P HELX_P28 AD1 ARG B 236 ? TYR B 250 ? ARG B 268 TYR B 282 1 ? 15 
HELX_P HELX_P29 AD2 ASN B 324 ? GLY B 332 ? ASN B 356 GLY B 364 1 ? 9  
HELX_P HELX_P30 AD3 LEU B 342 ? ASP B 347 ? LEU B 374 ASP B 379 1 ? 6  
HELX_P HELX_P31 AD4 GLN B 352 ? THR B 364 ? GLN B 384 THR B 396 1 ? 13 
HELX_P HELX_P32 AD5 SER B 368 ? PHE B 379 ? SER B 400 PHE B 411 1 ? 12 
HELX_P HELX_P33 AD6 ASP B 389 ? MET B 401 ? ASP B 421 MET B 433 1 ? 13 
HELX_P HELX_P34 AD7 ASP B 404 ? CYS B 411 ? ASP B 436 CYS B 443 1 ? 8  
HELX_P HELX_P35 AD8 CYS C 30  ? LYS C 34  ? CYS C 62  LYS C 66  5 ? 5  
HELX_P HELX_P36 AD9 PRO C 52  ? ASN C 65  ? PRO C 84  ASN C 97  1 ? 14 
HELX_P HELX_P37 AE1 PRO C 84  ? LEU C 88  ? PRO C 116 LEU C 120 5 ? 5  
HELX_P HELX_P38 AE2 SER C 89  ? PHE C 108 ? SER C 121 PHE C 140 1 ? 20 
HELX_P HELX_P39 AE3 SER C 133 ? TRP C 143 ? SER C 165 TRP C 175 1 ? 11 
HELX_P HELX_P40 AE4 LYS C 144 ? LEU C 147 ? LYS C 176 LEU C 179 5 ? 4  
HELX_P HELX_P41 AE5 ASP C 148 ? GLY C 159 ? ASP C 180 GLY C 191 1 ? 12 
HELX_P HELX_P42 AE6 ASN C 177 ? TYR C 181 ? ASN C 209 TYR C 213 5 ? 5  
HELX_P HELX_P43 AE7 ASN C 185 ? LEU C 189 ? ASN C 217 LEU C 221 5 ? 5  
HELX_P HELX_P44 AE8 ASP C 193 ? ALA C 195 ? ASP C 225 ALA C 227 5 ? 3  
HELX_P HELX_P45 AE9 ASN C 196 ? ASN C 211 ? ASN C 228 ASN C 243 1 ? 16 
HELX_P HELX_P46 AF1 ARG C 236 ? TYR C 250 ? ARG C 268 TYR C 282 1 ? 15 
HELX_P HELX_P47 AF2 ASN C 324 ? GLY C 332 ? ASN C 356 GLY C 364 1 ? 9  
HELX_P HELX_P48 AF3 LEU C 342 ? TYR C 346 ? LEU C 374 TYR C 378 1 ? 5  
HELX_P HELX_P49 AF4 GLN C 352 ? ILE C 365 ? GLN C 384 ILE C 397 1 ? 14 
HELX_P HELX_P50 AF5 SER C 368 ? TYR C 377 ? SER C 400 TYR C 409 1 ? 10 
HELX_P HELX_P51 AF6 ASP C 389 ? ASN C 402 ? ASP C 421 ASN C 434 1 ? 14 
HELX_P HELX_P52 AF7 ASP C 404 ? LEU C 412 ? ASP C 436 LEU C 444 1 ? 9  
# 
_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 
disulf1  disulf ?    ? A CYS 30  SG  ? ? ? 1_555 A  CYS 49  SG  ? ? A CYS 62  A CYS 81  1_555 ? ? ? ? ? ? ? 2.064 ? 
disulf2  disulf ?    ? A CYS 398 SG  ? ? ? 1_555 A  CYS 411 SG  ? ? A CYS 430 A CYS 443 1_555 ? ? ? ? ? ? ? 2.063 ? 
disulf3  disulf ?    ? B CYS 30  SG  ? ? ? 1_555 B  CYS 49  SG  ? ? B CYS 62  B CYS 81  1_555 ? ? ? ? ? ? ? 2.048 ? 
disulf4  disulf ?    ? C CYS 30  SG  ? ? ? 1_555 C  CYS 49  SG  ? ? C CYS 62  C CYS 81  1_555 ? ? ? ? ? ? ? 2.069 ? 
disulf5  disulf ?    ? C CYS 398 SG  ? ? ? 1_555 C  CYS 411 SG  ? ? C CYS 430 C CYS 443 1_555 ? ? ? ? ? ? ? 2.045 ? 
metalc1  metalc ?    ? A ASP 13  OD2 ? ? ? 1_555 I  ZN  .   ZN  ? ? A ASP 45  A ZN  606 1_555 ? ? ? ? ? ? ? 2.399 ? 
metalc2  metalc ?    ? A HIS 15  NE2 ? ? ? 1_555 I  ZN  .   ZN  ? ? A HIS 47  A ZN  606 1_555 ? ? ? ? ? ? ? 2.102 ? 
covale1  covale one  ? A ASN 37  ND2 ? ? ? 1_555 D  NAG .   C1  ? ? A ASN 69  A NAG 601 1_555 ? ? ? ? ? ? ? 1.307 ? 
metalc3  metalc ?    ? A ASP 78  OD2 ? ? ? 1_555 H  ZN  .   ZN  ? ? A ASP 110 A ZN  605 1_555 ? ? ? ? ? ? ? 2.228 ? 
metalc4  metalc ?    ? A ASP 78  OD2 ? ? ? 1_555 I  ZN  .   ZN  ? ? A ASP 110 A ZN  606 1_555 ? ? ? ? ? ? ? 2.374 ? 
covale2  covale one  ? A ASN 99  ND2 ? ? ? 1_555 E  NAG .   C1  ? ? A ASN 131 A NAG 602 1_555 ? ? ? ? ? ? ? 1.312 ? 
metalc5  metalc ?    ? A ASN 119 OD1 ? ? ? 1_555 H  ZN  .   ZN  ? ? A ASN 151 A ZN  605 1_555 ? ? ? ? ? ? ? 2.235 ? 
metalc6  metalc ?    ? A HIS 220 NE2 ? ? ? 1_555 H  ZN  .   ZN  ? ? A HIS 252 A ZN  605 1_555 ? ? ? ? ? ? ? 2.072 ? 
covale3  covale one  ? A ASN 231 ND2 ? ? ? 1_555 F  NAG .   C1  ? ? A ASN 263 A NAG 603 1_555 ? ? ? ? ? ? ? 1.301 ? 
metalc7  metalc ?    ? A HIS 261 ND1 ? ? ? 1_555 H  ZN  .   ZN  ? ? A HIS 293 A ZN  605 1_555 ? ? ? ? ? ? ? 2.331 ? 
metalc8  metalc ?    ? A HIS 263 NE2 ? ? ? 1_555 I  ZN  .   ZN  ? ? A HIS 295 A ZN  606 1_555 ? ? ? ? ? ? ? 2.303 ? 
metalc9  metalc ?    ? B ASP 13  OD2 ? ? ? 1_555 P  ZN  .   ZN  ? ? B ASP 45  B ZN  606 1_555 ? ? ? ? ? ? ? 2.296 ? 
metalc10 metalc ?    ? B HIS 15  NE2 ? ? ? 1_555 P  ZN  .   ZN  ? ? B HIS 47  B ZN  606 1_555 ? ? ? ? ? ? ? 2.395 ? 
covale4  covale one  ? B ASN 37  ND2 ? ? ? 1_555 K  NAG .   C1  ? ? B ASN 69  B NAG 601 1_555 ? ? ? ? ? ? ? 1.304 ? 
metalc11 metalc ?    ? B ASP 78  OD2 ? ? ? 1_555 P  ZN  .   ZN  ? ? B ASP 110 B ZN  606 1_555 ? ? ? ? ? ? ? 2.302 ? 
metalc12 metalc ?    ? B ASP 78  OD2 ? ? ? 1_555 Q  ZN  .   ZN  ? ? B ASP 110 B ZN  607 1_555 ? ? ? ? ? ? ? 2.382 ? 
covale5  covale one  ? B ASN 99  ND2 ? ? ? 1_555 L  NAG .   C1  ? ? B ASN 131 B NAG 602 1_555 ? ? ? ? ? ? ? 1.311 ? 
metalc13 metalc ?    ? B ASN 119 OD1 ? ? ? 1_555 Q  ZN  .   ZN  ? ? B ASN 151 B ZN  607 1_555 ? ? ? ? ? ? ? 2.491 ? 
metalc14 metalc ?    ? B HIS 220 NE2 ? ? ? 1_555 Q  ZN  .   ZN  ? ? B HIS 252 B ZN  607 1_555 ? ? ? ? ? ? ? 2.215 ? 
covale6  covale one  ? B ASN 231 ND2 ? ? ? 1_555 N  NAG .   C1  ? ? B ASN 263 B NAG 604 1_555 ? ? ? ? ? ? ? 1.275 ? 
metalc15 metalc ?    ? B HIS 261 ND1 ? ? ? 1_555 Q  ZN  .   ZN  ? ? B HIS 293 B ZN  607 1_555 ? ? ? ? ? ? ? 2.698 ? 
metalc16 metalc ?    ? B HIS 263 NE2 ? ? ? 1_555 P  ZN  .   ZN  ? ? B HIS 295 B ZN  606 1_555 ? ? ? ? ? ? ? 2.406 ? 
covale7  covale one  ? B ASN 324 ND2 ? ? ? 1_555 O  NAG .   C1  ? ? B ASN 356 B NAG 605 1_555 ? ? ? ? ? ? ? 1.322 ? 
metalc17 metalc ?    ? C ASP 13  OD2 ? ? ? 1_555 AA ZN  .   ZN  ? ? C ASP 45  C ZN  606 1_555 ? ? ? ? ? ? ? 2.144 ? 
metalc18 metalc ?    ? C HIS 15  NE2 ? ? ? 1_555 AA ZN  .   ZN  ? ? C HIS 47  C ZN  606 1_555 ? ? ? ? ? ? ? 2.330 ? 
covale8  covale one  ? C ASN 37  ND2 ? ? ? 1_555 V  NAG .   C1  ? ? C ASN 69  C NAG 601 1_555 ? ? ? ? ? ? ? 1.563 ? 
metalc19 metalc ?    ? C ASP 78  OD2 ? ? ? 1_555 AA ZN  .   ZN  ? ? C ASP 110 C ZN  606 1_555 ? ? ? ? ? ? ? 2.591 ? 
metalc20 metalc ?    ? C ASP 78  OD2 ? ? ? 1_555 Z  ZN  .   ZN  ? ? C ASP 110 C ZN  605 1_555 ? ? ? ? ? ? ? 2.406 ? 
covale9  covale one  ? C ASN 99  ND2 ? ? ? 1_555 W  NAG .   C1  ? ? C ASN 131 C NAG 602 1_555 ? ? ? ? ? ? ? 1.303 ? 
metalc21 metalc ?    ? C ASN 119 OD1 ? ? ? 1_555 Z  ZN  .   ZN  ? ? C ASN 151 C ZN  605 1_555 ? ? ? ? ? ? ? 2.274 ? 
metalc22 metalc ?    ? C HIS 220 NE2 ? ? ? 1_555 Z  ZN  .   ZN  ? ? C HIS 252 C ZN  605 1_555 ? ? ? ? ? ? ? 1.895 ? 
covale10 covale one  ? C ASN 231 ND2 ? ? ? 1_555 X  NAG .   C1  ? ? C ASN 263 C NAG 603 1_555 ? ? ? ? ? ? ? 1.298 ? 
metalc23 metalc ?    ? C HIS 261 ND1 ? ? ? 1_555 Z  ZN  .   ZN  ? ? C HIS 293 C ZN  605 1_555 ? ? ? ? ? ? ? 2.510 ? 
metalc24 metalc ?    ? C HIS 263 NE2 ? ? ? 1_555 AA ZN  .   ZN  ? ? C HIS 295 C ZN  606 1_555 ? ? ? ? ? ? ? 2.423 ? 
covale11 covale one  ? C ASN 324 ND2 ? ? ? 1_555 Y  NAG .   C1  ? ? C ASN 356 C NAG 604 1_555 ? ? ? ? ? ? ? 1.340 ? 
metalc25 metalc ?    ? H ZN  .   ZN  ? ? ? 1_555 J  C5P .   O1P ? ? A ZN  605 A C5P 607 1_555 ? ? ? ? ? ? ? 2.036 ? 
metalc26 metalc ?    ? I ZN  .   ZN  ? ? ? 1_555 J  C5P .   O2P ? ? A ZN  606 A C5P 607 1_555 ? ? ? ? ? ? ? 1.715 ? 
covale12 covale both ? L NAG .   O4  ? ? ? 1_555 M  NAG .   C1  ? ? B NAG 602 B NAG 603 1_555 ? ? ? ? ? ? ? 1.349 ? 
metalc27 metalc ?    ? P ZN  .   ZN  ? ? ? 1_555 U  RP5 .   O3X ? ? B ZN  606 B RP5 611 1_555 ? ? ? ? ? ? ? 2.277 ? 
metalc28 metalc ?    ? Z ZN  .   ZN  ? ? ? 1_555 BA C5P .   O2P ? ? C ZN  605 C C5P 607 1_555 ? ? ? ? ? ? ? 1.941 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
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 TRP 123 A . ? TRP 155 A PRO 124 A ? PRO 156 A 1 -2.78 
2 LEU 415 A . ? LEU 447 A TYR 416 A ? TYR 448 A 1 -3.55 
3 TRP 123 B . ? TRP 155 B PRO 124 B ? PRO 156 B 1 -6.57 
4 TRP 123 C . ? TRP 155 C PRO 124 C ? PRO 156 C 1 2.14  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 6 ? 
AA3 ? 6 ? 
AA4 ? 6 ? 
AA5 ? 6 ? 
AA6 ? 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 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA2 5 6 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? parallel      
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? parallel      
AA4 3 4 ? parallel      
AA4 4 5 ? parallel      
AA4 5 6 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? parallel      
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA5 5 6 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? parallel      
AA6 3 4 ? parallel      
AA6 4 5 ? parallel      
AA6 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 GLN A 112 ? PRO A 115 ? GLN A 144 PRO A 147 
AA1 2 PHE A 72  ? TRP A 75  ? PHE A 104 TRP A 107 
AA1 3 GLY A 6   ? VAL A 11  ? GLY A 38  VAL A 43  
AA1 4 GLY A 302 ? ASP A 309 ? GLY A 334 ASP A 341 
AA1 5 LYS A 314 ? LEU A 323 ? LYS A 346 LEU A 355 
AA1 6 TRP A 336 ? ILE A 341 ? TRP A 368 ILE A 373 
AA2 1 TYR A 161 ? VAL A 165 ? TYR A 193 VAL A 197 
AA2 2 ASN A 168 ? LEU A 176 ? ASN A 200 LEU A 208 
AA2 3 LYS A 214 ? ALA A 219 ? LYS A 246 ALA A 251 
AA2 4 ILE A 254 ? TYR A 259 ? ILE A 286 TYR A 291 
AA2 5 PRO A 277 ? VAL A 283 ? PRO A 309 VAL A 315 
AA2 6 SER A 266 ? SER A 271 ? SER A 298 SER A 303 
AA3 1 GLN B 112 ? ALA B 116 ? GLN B 144 ALA B 148 
AA3 2 PHE B 72  ? THR B 76  ? PHE B 104 THR B 108 
AA3 3 GLY B 6   ? VAL B 11  ? GLY B 38  VAL B 43  
AA3 4 GLY B 302 ? TYR B 308 ? GLY B 334 TYR B 340 
AA3 5 LEU B 315 ? LEU B 323 ? LEU B 347 LEU B 355 
AA3 6 TRP B 336 ? ILE B 341 ? TRP B 368 ILE B 373 
AA4 1 TYR B 161 ? VAL B 165 ? TYR B 193 VAL B 197 
AA4 2 ASN B 168 ? SER B 175 ? ASN B 200 SER B 207 
AA4 3 LYS B 214 ? ILE B 218 ? LYS B 246 ILE B 250 
AA4 4 ILE B 254 ? TYR B 259 ? ILE B 286 TYR B 291 
AA4 5 PRO B 277 ? VAL B 283 ? PRO B 309 VAL B 315 
AA4 6 SER B 266 ? SER B 271 ? SER B 298 SER B 303 
AA5 1 VAL C 113 ? PRO C 115 ? VAL C 145 PRO C 147 
AA5 2 PHE C 72  ? TRP C 75  ? PHE C 104 TRP C 107 
AA5 3 GLY C 6   ? VAL C 11  ? GLY C 38  VAL C 43  
AA5 4 GLY C 302 ? TYR C 308 ? GLY C 334 TYR C 340 
AA5 5 LEU C 315 ? TYR C 322 ? LEU C 347 TYR C 354 
AA5 6 LYS C 337 ? ILE C 341 ? LYS C 369 ILE C 373 
AA6 1 TYR C 161 ? VAL C 165 ? TYR C 193 VAL C 197 
AA6 2 ASN C 168 ? LEU C 176 ? ASN C 200 LEU C 208 
AA6 3 LYS C 214 ? ALA C 219 ? LYS C 246 ALA C 251 
AA6 4 ILE C 254 ? TYR C 259 ? ILE C 286 TYR C 291 
AA6 5 PRO C 277 ? VAL C 283 ? PRO C 309 VAL C 315 
AA6 6 SER C 266 ? SER C 271 ? SER C 298 SER C 303 
# 
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 O PHE A 114 ? O PHE A 146 N TRP A 75  ? N TRP A 107 
AA1 2 3 O ILE A 74  ? O ILE A 106 N VAL A 11  ? N VAL A 43  
AA1 3 4 N PHE A 8   ? N PHE A 40  O PHE A 306 ? O PHE A 338 
AA1 4 5 N ILE A 303 ? N ILE A 335 O TYR A 321 ? O TYR A 353 
AA1 5 6 N GLN A 320 ? N GLN A 352 O GLU A 339 ? O GLU A 371 
AA2 1 2 N GLN A 163 ? N GLN A 195 O ILE A 173 ? O ILE A 205 
AA2 2 3 N ARG A 172 ? N ARG A 204 O LYS A 214 ? O LYS A 246 
AA2 3 4 N VAL A 215 ? N VAL A 247 O ALA A 255 ? O ALA A 287 
AA2 4 5 N TYR A 259 ? N TYR A 291 O PHE A 282 ? O PHE A 314 
AA2 5 6 O VAL A 278 ? O VAL A 310 N LEU A 270 ? N LEU A 302 
AA3 1 2 O ALA B 116 ? O ALA B 148 N TRP B 75  ? N TRP B 107 
AA3 2 3 O ILE B 74  ? O ILE B 106 N TRP B 9   ? N TRP B 41  
AA3 3 4 N PHE B 8   ? N PHE B 40  O PHE B 306 ? O PHE B 338 
AA3 4 5 N LEU B 305 ? N LEU B 337 O LEU B 319 ? O LEU B 351 
AA3 5 6 N GLN B 320 ? N GLN B 352 O GLU B 339 ? O GLU B 371 
AA4 1 2 N VAL B 165 ? N VAL B 197 O LEU B 171 ? O LEU B 203 
AA4 2 3 N ARG B 172 ? N ARG B 204 O LYS B 214 ? O LYS B 246 
AA4 3 4 N ILE B 217 ? N ILE B 249 O PHE B 258 ? O PHE B 290 
AA4 4 5 N GLN B 257 ? N GLN B 289 O SER B 280 ? O SER B 312 
AA4 5 6 O VAL B 278 ? O VAL B 310 N LEU B 270 ? N LEU B 302 
AA5 1 2 O PHE C 114 ? O PHE C 146 N MET C 73  ? N MET C 105 
AA5 2 3 O ILE C 74  ? O ILE C 106 N VAL C 11  ? N VAL C 43  
AA5 3 4 N GLY C 6   ? N GLY C 38  O TYR C 308 ? O TYR C 340 
AA5 4 5 N GLN C 307 ? N GLN C 339 O ASP C 317 ? O ASP C 349 
AA5 5 6 N TYR C 322 ? N TYR C 354 O LYS C 337 ? O LYS C 369 
AA6 1 2 N GLN C 163 ? N GLN C 195 O ILE C 173 ? O ILE C 205 
AA6 2 3 N LEU C 176 ? N LEU C 208 O ILE C 218 ? O ILE C 250 
AA6 3 4 N VAL C 215 ? N VAL C 247 O ALA C 255 ? O ALA C 287 
AA6 4 5 N TYR C 259 ? N TYR C 291 O PHE C 282 ? O PHE C 314 
AA6 5 6 O VAL C 278 ? O VAL C 310 N LEU C 270 ? N LEU C 302 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A NAG 604 ? 3  'binding site for residue NAG A 604'                                                       
AC2 Software A ZN  605 ? 6  'binding site for residue ZN A 605'                                                        
AC3 Software A ZN  606 ? 6  'binding site for residue ZN A 606'                                                        
AC4 Software A C5P 607 ? 15 'binding site for residue C5P A 607'                                                       
AC5 Software B ZN  606 ? 6  'binding site for residue ZN B 606'                                                        
AC6 Software B ZN  607 ? 6  'binding site for residue ZN B 607'                                                        
AC7 Software B GOL 609 ? 2  'binding site for residue GOL B 609'                                                       
AC8 Software B MLI 610 ? 4  'binding site for residue MLI B 610'                                                       
AC9 Software B RP5 611 ? 9  'binding site for residue RP5 B 611'                                                       
AD1 Software C ZN  605 ? 5  'binding site for residue ZN C 605'                                                        
AD2 Software C ZN  606 ? 5  'binding site for residue ZN C 606'                                                        
AD3 Software C C5P 607 ? 14 'binding site for residue C5P C 607'                                                       
AD4 Software A NAG 601 ? 2  'binding site for Mono-Saccharide NAG A 601 bound to ASN A 69'                             
AD5 Software A NAG 602 ? 2  'binding site for Mono-Saccharide NAG A 602 bound to ASN A 131'                            
AD6 Software A NAG 603 ? 1  'binding site for Mono-Saccharide NAG A 603 bound to ASN A 263'                            
AD7 Software B NAG 601 ? 4  'binding site for Mono-Saccharide NAG B 601 bound to ASN B 69'                             
AD8 Software B ASN 131 ? 4  'binding site for Poly-Saccharide residues NAG B 602 through NAG B 603 bound to ASN B 131' 
AD9 Software B NAG 604 ? 1  'binding site for Mono-Saccharide NAG B 604 bound to ASN B 263'                            
AE1 Software B NAG 605 ? 4  'binding site for Mono-Saccharide NAG B 605 bound to ASN B 356'                            
AE2 Software C NAG 601 ? 2  'binding site for Mono-Saccharide NAG C 601 bound to ASN C 69'                             
AE3 Software C NAG 602 ? 1  'binding site for Mono-Saccharide NAG C 602 bound to ASN C 131'                            
AE4 Software C NAG 603 ? 1  'binding site for Mono-Saccharide NAG C 603 bound to ASN C 263'                            
AE5 Software C NAG 604 ? 4  'binding site for Mono-Saccharide NAG C 604 bound to ASN C 356'                            
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1   AC1 3  TYR A  322 ? TYR A 354 . ? 1_555 ? 
2   AC1 3  ASN A  324 ? ASN A 356 . ? 1_555 ? 
3   AC1 3  LYS A  337 ? LYS A 369 . ? 1_555 ? 
4   AC2 6  ASP A  78  ? ASP A 110 . ? 1_555 ? 
5   AC2 6  ASN A  119 ? ASN A 151 . ? 1_555 ? 
6   AC2 6  HIS A  220 ? HIS A 252 . ? 1_555 ? 
7   AC2 6  HIS A  261 ? HIS A 293 . ? 1_555 ? 
8   AC2 6  ZN  I  .   ? ZN  A 606 . ? 1_555 ? 
9   AC2 6  C5P J  .   ? C5P A 607 . ? 1_555 ? 
10  AC3 6  ASP A  13  ? ASP A 45  . ? 1_555 ? 
11  AC3 6  HIS A  15  ? HIS A 47  . ? 1_555 ? 
12  AC3 6  ASP A  78  ? ASP A 110 . ? 1_555 ? 
13  AC3 6  HIS A  263 ? HIS A 295 . ? 1_555 ? 
14  AC3 6  ZN  H  .   ? ZN  A 605 . ? 1_555 ? 
15  AC3 6  C5P J  .   ? C5P A 607 . ? 1_555 ? 
16  AC4 15 HIS A  15  ? HIS A 47  . ? 1_555 ? 
17  AC4 15 ASP A  78  ? ASP A 110 . ? 1_555 ? 
18  AC4 15 HIS A  82  ? HIS A 114 . ? 1_555 ? 
19  AC4 15 ASN A  119 ? ASN A 151 . ? 1_555 ? 
20  AC4 15 HIS A  120 ? HIS A 152 . ? 1_555 ? 
21  AC4 15 HIS A  261 ? HIS A 293 . ? 1_555 ? 
22  AC4 15 THR A  262 ? THR A 294 . ? 1_555 ? 
23  AC4 15 HIS A  263 ? HIS A 295 . ? 1_555 ? 
24  AC4 15 ARG A  264 ? ARG A 296 . ? 1_555 ? 
25  AC4 15 VAL A  290 ? VAL A 322 . ? 1_555 ? 
26  AC4 15 LYS A  291 ? LYS A 323 . ? 1_555 ? 
27  AC4 15 GLU A  295 ? GLU A 327 . ? 1_555 ? 
28  AC4 15 ZN  H  .   ? ZN  A 605 . ? 1_555 ? 
29  AC4 15 ZN  I  .   ? ZN  A 606 . ? 1_555 ? 
30  AC4 15 HOH EA .   ? HOH A 716 . ? 1_555 ? 
31  AC5 6  ASP B  13  ? ASP B 45  . ? 1_555 ? 
32  AC5 6  HIS B  15  ? HIS B 47  . ? 1_555 ? 
33  AC5 6  ASP B  78  ? ASP B 110 . ? 1_555 ? 
34  AC5 6  HIS B  263 ? HIS B 295 . ? 1_555 ? 
35  AC5 6  ZN  Q  .   ? ZN  B 607 . ? 1_555 ? 
36  AC5 6  RP5 U  .   ? RP5 B 611 . ? 1_555 ? 
37  AC6 6  ASP B  78  ? ASP B 110 . ? 1_555 ? 
38  AC6 6  ASN B  119 ? ASN B 151 . ? 1_555 ? 
39  AC6 6  HIS B  220 ? HIS B 252 . ? 1_555 ? 
40  AC6 6  HIS B  261 ? HIS B 293 . ? 1_555 ? 
41  AC6 6  ZN  P  .   ? ZN  B 606 . ? 1_555 ? 
42  AC6 6  RP5 U  .   ? RP5 B 611 . ? 1_555 ? 
43  AC7 2  ARG B  156 ? ARG B 188 . ? 1_555 ? 
44  AC7 2  HOH FA .   ? HOH B 730 . ? 1_555 ? 
45  AC8 4  SER B  133 ? SER B 165 . ? 1_555 ? 
46  AC8 4  LYS B  134 ? LYS B 166 . ? 1_555 ? 
47  AC8 4  ASN B  137 ? ASN B 169 . ? 1_555 ? 
48  AC8 4  LYS C  191 ? LYS C 223 . ? 6_654 ? 
49  AC9 9  HIS B  15  ? HIS B 47  . ? 1_555 ? 
50  AC9 9  ASP B  78  ? ASP B 110 . ? 1_555 ? 
51  AC9 9  HIS B  82  ? HIS B 114 . ? 1_555 ? 
52  AC9 9  ASN B  119 ? ASN B 151 . ? 1_555 ? 
53  AC9 9  HIS B  120 ? HIS B 152 . ? 1_555 ? 
54  AC9 9  HIS B  261 ? HIS B 293 . ? 1_555 ? 
55  AC9 9  HIS B  263 ? HIS B 295 . ? 1_555 ? 
56  AC9 9  ZN  P  .   ? ZN  B 606 . ? 1_555 ? 
57  AC9 9  ZN  Q  .   ? ZN  B 607 . ? 1_555 ? 
58  AD1 5  ASP C  78  ? ASP C 110 . ? 1_555 ? 
59  AD1 5  ASN C  119 ? ASN C 151 . ? 1_555 ? 
60  AD1 5  HIS C  220 ? HIS C 252 . ? 1_555 ? 
61  AD1 5  HIS C  261 ? HIS C 293 . ? 1_555 ? 
62  AD1 5  C5P BA .   ? C5P C 607 . ? 1_555 ? 
63  AD2 5  ASP C  13  ? ASP C 45  . ? 1_555 ? 
64  AD2 5  HIS C  15  ? HIS C 47  . ? 1_555 ? 
65  AD2 5  ASP C  78  ? ASP C 110 . ? 1_555 ? 
66  AD2 5  HIS C  263 ? HIS C 295 . ? 1_555 ? 
67  AD2 5  C5P BA .   ? C5P C 607 . ? 1_555 ? 
68  AD3 14 HIS C  15  ? HIS C 47  . ? 1_555 ? 
69  AD3 14 LYS C  34  ? LYS C 66  . ? 1_555 ? 
70  AD3 14 ASP C  78  ? ASP C 110 . ? 1_555 ? 
71  AD3 14 HIS C  82  ? HIS C 114 . ? 1_555 ? 
72  AD3 14 ASN C  119 ? ASN C 151 . ? 1_555 ? 
73  AD3 14 HIS C  120 ? HIS C 152 . ? 1_555 ? 
74  AD3 14 HIS C  220 ? HIS C 252 . ? 1_555 ? 
75  AD3 14 HIS C  261 ? HIS C 293 . ? 1_555 ? 
76  AD3 14 THR C  262 ? THR C 294 . ? 1_555 ? 
77  AD3 14 HIS C  263 ? HIS C 295 . ? 1_555 ? 
78  AD3 14 GLU C  295 ? GLU C 327 . ? 1_555 ? 
79  AD3 14 ZN  Z  .   ? ZN  C 605 . ? 1_555 ? 
80  AD3 14 ZN  AA .   ? ZN  C 606 . ? 1_555 ? 
81  AD3 14 HOH GA .   ? HOH C 725 . ? 1_555 ? 
82  AD4 2  ASN A  37  ? ASN A 69  . ? 1_555 ? 
83  AD4 2  THR A  387 ? THR A 419 . ? 4_555 ? 
84  AD5 2  ASN A  99  ? ASN A 131 . ? 1_555 ? 
85  AD5 2  HOH EA .   ? HOH A 707 . ? 1_555 ? 
86  AD6 1  ASN A  231 ? ASN A 263 . ? 1_555 ? 
87  AD7 4  THR B  27  ? THR B 59  . ? 1_555 ? 
88  AD7 4  ASN B  37  ? ASN B 69  . ? 1_555 ? 
89  AD7 4  ILE C  372 ? ILE C 404 . ? 4_545 ? 
90  AD7 4  THR C  387 ? THR C 419 . ? 4_545 ? 
91  AD8 4  PRO B  18  ? PRO B 50  . ? 1_555 ? 
92  AD8 4  TYR B  53  ? TYR B 85  . ? 1_555 ? 
93  AD8 4  ASN B  99  ? ASN B 131 . ? 1_555 ? 
94  AD8 4  HOH FA .   ? HOH B 709 . ? 1_555 ? 
95  AD9 1  ASN B  231 ? ASN B 263 . ? 1_555 ? 
96  AE1 4  LYS A  212 ? LYS A 244 . ? 1_555 ? 
97  AE1 4  TYR B  322 ? TYR B 354 . ? 1_555 ? 
98  AE1 4  ASN B  324 ? ASN B 356 . ? 1_555 ? 
99  AE1 4  SER B  381 ? SER B 413 . ? 1_555 ? 
100 AE2 2  THR B  387 ? THR B 419 . ? 4_655 ? 
101 AE2 2  ASN C  37  ? ASN C 69  . ? 1_555 ? 
102 AE3 1  ASN C  99  ? ASN C 131 . ? 1_555 ? 
103 AE4 1  ASN C  231 ? ASN C 263 . ? 1_555 ? 
104 AE5 4  ASN C  324 ? ASN C 356 . ? 1_555 ? 
105 AE5 4  SER C  381 ? SER C 413 . ? 1_555 ? 
106 AE5 4  TYR C  382 ? TYR C 414 . ? 1_555 ? 
107 AE5 4  SER C  384 ? SER C 416 . ? 1_555 ? 
# 
_atom_sites.entry_id                    5EBE 
_atom_sites.fract_transf_matrix[1][1]   0.006773 
_atom_sites.fract_transf_matrix[1][2]   0.003910 
_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]   0.007820 
_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]   0.007028 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
P  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N  N     . PRO A  1  1   ? 45.214 -10.179 12.927  1.00 89.75  ?  33  PRO A N     1 
ATOM   2     C  CA    . PRO A  1  1   ? 45.531 -9.226  11.856  1.00 86.61  ?  33  PRO A CA    1 
ATOM   3     C  C     . PRO A  1  1   ? 45.820 -9.907  10.494  1.00 82.06  ?  33  PRO A C     1 
ATOM   4     O  O     . PRO A  1  1   ? 46.472 -10.966 10.471  1.00 76.84  ?  33  PRO A O     1 
ATOM   5     C  CB    . PRO A  1  1   ? 46.756 -8.494  12.414  1.00 86.47  ?  33  PRO A CB    1 
ATOM   6     C  CG    . PRO A  1  1   ? 46.543 -8.512  13.912  1.00 88.12  ?  33  PRO A CG    1 
ATOM   7     C  CD    . PRO A  1  1   ? 45.630 -9.673  14.252  1.00 87.44  ?  33  PRO A CD    1 
ATOM   8     N  N     . PRO A  1  2   ? 45.318 -9.320  9.373   1.00 76.97  ?  34  PRO A N     1 
ATOM   9     C  CA    . PRO A  1  2   ? 45.398 -9.944  8.041   1.00 69.89  ?  34  PRO A CA    1 
ATOM   10    C  C     . PRO A  1  2   ? 46.470 -9.326  7.156   1.00 62.92  ?  34  PRO A C     1 
ATOM   11    O  O     . PRO A  1  2   ? 46.610 -8.107  7.145   1.00 64.11  ?  34  PRO A O     1 
ATOM   12    C  CB    . PRO A  1  2   ? 44.024 -9.643  7.452   1.00 70.14  ?  34  PRO A CB    1 
ATOM   13    C  CG    . PRO A  1  2   ? 43.677 -8.301  8.047   1.00 75.24  ?  34  PRO A CG    1 
ATOM   14    C  CD    . PRO A  1  2   ? 44.507 -8.089  9.301   1.00 75.26  ?  34  PRO A CD    1 
ATOM   15    N  N     . PRO A  1  3   ? 47.211 -10.155 6.401   1.00 57.92  ?  35  PRO A N     1 
ATOM   16    C  CA    . PRO A  1  3   ? 48.456 -9.683  5.750   1.00 53.80  ?  35  PRO A CA    1 
ATOM   17    C  C     . PRO A  1  3   ? 48.281 -8.906  4.425   1.00 47.77  ?  35  PRO A C     1 
ATOM   18    O  O     . PRO A  1  3   ? 49.157 -8.136  4.027   1.00 41.55  ?  35  PRO A O     1 
ATOM   19    C  CB    . PRO A  1  3   ? 49.269 -10.979 5.553   1.00 54.61  ?  35  PRO A CB    1 
ATOM   20    C  CG    . PRO A  1  3   ? 48.331 -12.119 5.814   1.00 56.78  ?  35  PRO A CG    1 
ATOM   21    C  CD    . PRO A  1  3   ? 46.959 -11.579 6.116   1.00 58.46  ?  35  PRO A CD    1 
ATOM   22    N  N     . ALA A  1  4   ? 47.164 -9.131  3.747   1.00 47.08  ?  36  ALA A N     1 
ATOM   23    C  CA    . ALA A  1  4   ? 46.744 -8.282  2.641   1.00 45.80  ?  36  ALA A CA    1 
ATOM   24    C  C     . ALA A  1  4   ? 45.214 -8.256  2.599   1.00 45.01  ?  36  ALA A C     1 
ATOM   25    O  O     . ALA A  1  4   ? 44.539 -9.202  3.025   1.00 43.21  ?  36  ALA A O     1 
ATOM   26    C  CB    . ALA A  1  4   ? 47.324 -8.769  1.316   1.00 44.42  ?  36  ALA A CB    1 
ATOM   27    N  N     . ILE A  1  5   ? 44.696 -7.144  2.089   1.00 44.28  ?  37  ILE A N     1 
ATOM   28    C  CA    . ILE A  1  5   ? 43.265 -6.851  2.018   1.00 40.56  ?  37  ILE A CA    1 
ATOM   29    C  C     . ILE A  1  5   ? 42.715 -7.125  0.613   1.00 37.66  ?  37  ILE A C     1 
ATOM   30    O  O     . ILE A  1  5   ? 43.168 -6.534  -0.377  1.00 33.72  ?  37  ILE A O     1 
ATOM   31    C  CB    . ILE A  1  5   ? 43.019 -5.353  2.342   1.00 38.66  ?  37  ILE A CB    1 
ATOM   32    C  CG1   . ILE A  1  5   ? 43.553 -5.002  3.737   1.00 37.20  ?  37  ILE A CG1   1 
ATOM   33    C  CG2   . ILE A  1  5   ? 41.547 -5.002  2.203   1.00 38.87  ?  37  ILE A CG2   1 
ATOM   34    C  CD1   . ILE A  1  5   ? 43.070 -5.919  4.838   1.00 36.31  ?  37  ILE A CD1   1 
ATOM   35    N  N     . GLY A  1  6   ? 41.728 -8.011  0.539   1.00 36.85  ?  38  GLY A N     1 
ATOM   36    C  CA    . GLY A  1  6   ? 40.935 -8.187  -0.685  1.00 35.20  ?  38  GLY A CA    1 
ATOM   37    C  C     . GLY A  1  6   ? 39.870 -7.109  -0.790  1.00 32.50  ?  38  GLY A C     1 
ATOM   38    O  O     . GLY A  1  6   ? 39.293 -6.717  0.222   1.00 31.27  ?  38  GLY A O     1 
ATOM   39    N  N     . GLN A  1  7   ? 39.607 -6.630  -2.003  1.00 30.41  ?  39  GLN A N     1 
ATOM   40    C  CA    . GLN A  1  7   ? 38.615 -5.575  -2.213  1.00 28.58  ?  39  GLN A CA    1 
ATOM   41    C  C     . GLN A  1  7   ? 37.794 -5.874  -3.447  1.00 28.65  ?  39  GLN A C     1 
ATOM   42    O  O     . GLN A  1  7   ? 38.337 -6.323  -4.456  1.00 29.99  ?  39  GLN A O     1 
ATOM   43    C  CB    . GLN A  1  7   ? 39.295 -4.224  -2.388  1.00 27.84  ?  39  GLN A CB    1 
ATOM   44    C  CG    . GLN A  1  7   ? 39.900 -3.672  -1.106  1.00 28.57  ?  39  GLN A CG    1 
ATOM   45    C  CD    . GLN A  1  7   ? 40.383 -2.222  -1.209  1.00 28.15  ?  39  GLN A CD    1 
ATOM   46    O  OE1   . GLN A  1  7   ? 40.611 -1.707  -2.293  1.00 29.13  ?  39  GLN A OE1   1 
ATOM   47    N  NE2   . GLN A  1  7   ? 40.540 -1.567  -0.070  1.00 27.20  ?  39  GLN A NE2   1 
ATOM   48    N  N     . PHE A  1  8   ? 36.484 -5.644  -3.371  1.00 27.00  ?  40  PHE A N     1 
ATOM   49    C  CA    . PHE A  1  8   ? 35.632 -5.711  -4.555  1.00 23.78  ?  40  PHE A CA    1 
ATOM   50    C  C     . PHE A  1  8   ? 34.530 -4.693  -4.497  1.00 20.63  ?  40  PHE A C     1 
ATOM   51    O  O     . PHE A  1  8   ? 34.115 -4.294  -3.433  1.00 19.12  ?  40  PHE A O     1 
ATOM   52    C  CB    . PHE A  1  8   ? 35.061 -7.103  -4.757  1.00 24.07  ?  40  PHE A CB    1 
ATOM   53    C  CG    . PHE A  1  8   ? 34.155 -7.551  -3.677  1.00 24.91  ?  40  PHE A CG    1 
ATOM   54    C  CD1   . PHE A  1  8   ? 34.637 -8.324  -2.647  1.00 25.87  ?  40  PHE A CD1   1 
ATOM   55    C  CD2   . PHE A  1  8   ? 32.803 -7.247  -3.718  1.00 26.28  ?  40  PHE A CD2   1 
ATOM   56    C  CE1   . PHE A  1  8   ? 33.792 -8.783  -1.648  1.00 27.45  ?  40  PHE A CE1   1 
ATOM   57    C  CE2   . PHE A  1  8   ? 31.940 -7.697  -2.727  1.00 27.52  ?  40  PHE A CE2   1 
ATOM   58    C  CZ    . PHE A  1  8   ? 32.438 -8.465  -1.681  1.00 28.43  ?  40  PHE A CZ    1 
ATOM   59    N  N     . TRP A  1  9   ? 34.070 -4.285  -5.671  1.00 19.17  ?  41  TRP A N     1 
ATOM   60    C  CA    . TRP A  1  9   ? 33.077 -3.232  -5.786  1.00 17.93  ?  41  TRP A CA    1 
ATOM   61    C  C     . TRP A  1  9   ? 31.735 -3.866  -5.884  1.00 16.64  ?  41  TRP A C     1 
ATOM   62    O  O     . TRP A  1  9   ? 31.634 -5.027  -6.313  1.00 16.14  ?  41  TRP A O     1 
ATOM   63    C  CB    . TRP A  1  9   ? 33.285 -2.430  -7.048  1.00 18.33  ?  41  TRP A CB    1 
ATOM   64    C  CG    . TRP A  1  9   ? 34.479 -1.591  -7.027  1.00 18.35  ?  41  TRP A CG    1 
ATOM   65    C  CD1   . TRP A  1  9   ? 35.695 -1.875  -7.575  1.00 18.39  ?  41  TRP A CD1   1 
ATOM   66    C  CD2   . TRP A  1  9   ? 34.582 -0.300  -6.449  1.00 18.14  ?  41  TRP A CD2   1 
ATOM   67    N  NE1   . TRP A  1  9   ? 36.562 -0.832  -7.352  1.00 18.59  ?  41  TRP A NE1   1 
ATOM   68    C  CE2   . TRP A  1  9   ? 35.903 0.148   -6.661  1.00 18.21  ?  41  TRP A CE2   1 
ATOM   69    C  CE3   . TRP A  1  9   ? 33.691 0.519   -5.772  1.00 17.89  ?  41  TRP A CE3   1 
ATOM   70    C  CZ2   . TRP A  1  9   ? 36.349 1.373   -6.223  1.00 18.40  ?  41  TRP A CZ2   1 
ATOM   71    C  CZ3   . TRP A  1  9   ? 34.135 1.739   -5.331  1.00 18.49  ?  41  TRP A CZ3   1 
ATOM   72    C  CH2   . TRP A  1  9   ? 35.452 2.161   -5.559  1.00 18.70  ?  41  TRP A CH2   1 
ATOM   73    N  N     . HIS A  1  10  ? 30.712 -3.103  -5.485  1.00 15.31  ?  42  HIS A N     1 
ATOM   74    C  CA    . HIS A  1  10  ? 29.316 -3.516  -5.668  1.00 14.32  ?  42  HIS A CA    1 
ATOM   75    C  C     . HIS A  1  10  ? 28.575 -2.357  -6.244  1.00 13.60  ?  42  HIS A C     1 
ATOM   76    O  O     . HIS A  1  10  ? 28.465 -1.311  -5.596  1.00 13.50  ?  42  HIS A O     1 
ATOM   77    C  CB    . HIS A  1  10  ? 28.668 -3.910  -4.354  1.00 13.86  ?  42  HIS A CB    1 
ATOM   78    C  CG    . HIS A  1  10  ? 27.258 -4.391  -4.483  1.00 13.60  ?  42  HIS A CG    1 
ATOM   79    N  ND1   . HIS A  1  10  ? 26.593 -4.994  -3.442  1.00 13.77  ?  42  HIS A ND1   1 
ATOM   80    C  CD2   . HIS A  1  10  ? 26.385 -4.367  -5.511  1.00 13.73  ?  42  HIS A CD2   1 
ATOM   81    C  CE1   . HIS A  1  10  ? 25.368 -5.313  -3.817  1.00 13.60  ?  42  HIS A CE1   1 
ATOM   82    N  NE2   . HIS A  1  10  ? 25.213 -4.937  -5.068  1.00 13.54  ?  42  HIS A NE2   1 
ATOM   83    N  N     . VAL A  1  11  ? 28.075 -2.550  -7.461  1.00 12.77  ?  43  VAL A N     1 
ATOM   84    C  CA    . VAL A  1  11  ? 27.271 -1.545  -8.130  1.00 12.45  ?  43  VAL A CA    1 
ATOM   85    C  C     . VAL A  1  11  ? 25.902 -2.149  -8.391  1.00 12.59  ?  43  VAL A C     1 
ATOM   86    O  O     . VAL A  1  11  ? 25.781 -3.355  -8.689  1.00 12.91  ?  43  VAL A O     1 
ATOM   87    C  CB    . VAL A  1  11  ? 27.880 -1.104  -9.456  1.00 12.33  ?  43  VAL A CB    1 
ATOM   88    C  CG1   . VAL A  1  11  ? 29.258 -0.505  -9.248  1.00 12.39  ?  43  VAL A CG1   1 
ATOM   89    C  CG2   . VAL A  1  11  ? 27.951 -2.284  -10.418 1.00 12.63  ?  43  VAL A CG2   1 
ATOM   90    N  N     . THR A  1  12  ? 24.860 -1.328  -8.279  1.00 12.17  ?  44  THR A N     1 
ATOM   91    C  CA    . THR A  1  12  ? 23.542 -1.837  -8.525  1.00 11.81  ?  44  THR A CA    1 
ATOM   92    C  C     . THR A  1  12  ? 22.519 -0.817  -8.992  1.00 11.65  ?  44  THR A C     1 
ATOM   93    O  O     . THR A  1  12  ? 22.699 0.405   -8.832  1.00 11.40  ?  44  THR A O     1 
ATOM   94    C  CB    . THR A  1  12  ? 23.006 -2.523  -7.288  1.00 11.95  ?  44  THR A CB    1 
ATOM   95    O  OG1   . THR A  1  12  ? 21.861 -3.281  -7.676  1.00 12.78  ?  44  THR A OG1   1 
ATOM   96    C  CG2   . THR A  1  12  ? 22.617 -1.506  -6.200  1.00 11.96  ?  44  THR A CG2   1 
ATOM   97    N  N     . ASP A  1  13  ? 21.431 -1.364  -9.546  1.00 11.61  ?  45  ASP A N     1 
ATOM   98    C  CA    . ASP A  1  13  ? 20.293 -0.596  -10.061 1.00 11.85  ?  45  ASP A CA    1 
ATOM   99    C  C     . ASP A  1  13  ? 20.773 0.672   -10.794 1.00 12.30  ?  45  ASP A C     1 
ATOM   100   O  O     . ASP A  1  13  ? 20.573 1.817   -10.353 1.00 11.89  ?  45  ASP A O     1 
ATOM   101   C  CB    . ASP A  1  13  ? 19.270 -0.314  -8.944  1.00 11.60  ?  45  ASP A CB    1 
ATOM   102   C  CG    . ASP A  1  13  ? 18.846 -1.597  -8.186  1.00 11.39  ?  45  ASP A CG    1 
ATOM   103   O  OD1   . ASP A  1  13  ? 19.494 -1.964  -7.175  1.00 11.04  ?  45  ASP A OD1   1 
ATOM   104   O  OD2   . ASP A  1  13  ? 17.843 -2.228  -8.578  1.00 11.14  -1 45  ASP A OD2   1 
ATOM   105   N  N     . LEU A  1  14  ? 21.427 0.422   -11.931 1.00 13.06  ?  46  LEU A N     1 
ATOM   106   C  CA    . LEU A  1  14  ? 21.967 1.491   -12.764 1.00 13.48  ?  46  LEU A CA    1 
ATOM   107   C  C     . LEU A  1  14  ? 20.811 2.265   -13.379 1.00 13.60  ?  46  LEU A C     1 
ATOM   108   O  O     . LEU A  1  14  ? 20.827 3.487   -13.351 1.00 14.18  ?  46  LEU A O     1 
ATOM   109   C  CB    . LEU A  1  14  ? 22.925 0.923   -13.820 1.00 13.96  ?  46  LEU A CB    1 
ATOM   110   C  CG    . LEU A  1  14  ? 24.193 0.188   -13.298 1.00 14.47  ?  46  LEU A CG    1 
ATOM   111   C  CD1   . LEU A  1  14  ? 25.001 -0.544  -14.355 1.00 14.54  ?  46  LEU A CD1   1 
ATOM   112   C  CD2   . LEU A  1  14  ? 25.113 1.182   -12.612 1.00 14.57  ?  46  LEU A CD2   1 
ATOM   113   N  N     . HIS A  1  15  ? 19.780 1.560   -13.853 1.00 13.57  ?  47  HIS A N     1 
ATOM   114   C  CA    . HIS A  1  15  ? 18.563 2.190   -14.365 1.00 13.98  ?  47  HIS A CA    1 
ATOM   115   C  C     . HIS A  1  15  ? 18.906 3.398   -15.266 1.00 14.93  ?  47  HIS A C     1 
ATOM   116   O  O     . HIS A  1  15  ? 18.693 4.587   -14.897 1.00 13.54  ?  47  HIS A O     1 
ATOM   117   C  CB    . HIS A  1  15  ? 17.620 2.603   -13.220 1.00 14.01  ?  47  HIS A CB    1 
ATOM   118   C  CG    . HIS A  1  15  ? 16.962 1.450   -12.505 1.00 13.93  ?  47  HIS A CG    1 
ATOM   119   N  ND1   . HIS A  1  15  ? 16.196 0.511   -13.157 1.00 13.89  ?  47  HIS A ND1   1 
ATOM   120   C  CD2   . HIS A  1  15  ? 16.934 1.101   -11.195 1.00 13.75  ?  47  HIS A CD2   1 
ATOM   121   C  CE1   . HIS A  1  15  ? 15.740 -0.373  -12.290 1.00 13.46  ?  47  HIS A CE1   1 
ATOM   122   N  NE2   . HIS A  1  15  ? 16.173 -0.036  -11.093 1.00 13.36  ?  47  HIS A NE2   1 
ATOM   123   N  N     . LEU A  1  16  ? 19.471 3.059   -16.435 1.00 16.20  ?  48  LEU A N     1 
ATOM   124   C  CA    . LEU A  1  16  ? 19.807 4.037   -17.478 1.00 17.04  ?  48  LEU A CA    1 
ATOM   125   C  C     . LEU A  1  16  ? 18.562 4.500   -18.197 1.00 17.32  ?  48  LEU A C     1 
ATOM   126   O  O     . LEU A  1  16  ? 17.745 3.668   -18.601 1.00 17.06  ?  48  LEU A O     1 
ATOM   127   C  CB    . LEU A  1  16  ? 20.737 3.435   -18.549 1.00 17.23  ?  48  LEU A CB    1 
ATOM   128   C  CG    . LEU A  1  16  ? 20.951 4.321   -19.808 1.00 17.13  ?  48  LEU A CG    1 
ATOM   129   C  CD1   . LEU A  1  16  ? 21.858 5.510   -19.550 1.00 17.25  ?  48  LEU A CD1   1 
ATOM   130   C  CD2   . LEU A  1  16  ? 21.536 3.522   -20.945 1.00 17.41  ?  48  LEU A CD2   1 
ATOM   131   N  N     . ASP A  1  17  ? 18.444 5.792   -18.420 1.00 17.78  ?  49  ASP A N     1 
ATOM   132   C  CA    . ASP A  1  17  ? 17.361 6.372   -19.155 1.00 19.92  ?  49  ASP A CA    1 
ATOM   133   C  C     . ASP A  1  17  ? 18.040 6.947   -20.345 1.00 19.70  ?  49  ASP A C     1 
ATOM   134   O  O     . ASP A  1  17  ? 18.640 7.973   -20.260 1.00 18.18  ?  49  ASP A O     1 
ATOM   135   C  CB    . ASP A  1  17  ? 16.722 7.486   -18.375 1.00 21.95  ?  49  ASP A CB    1 
ATOM   136   C  CG    . ASP A  1  17  ? 15.378 7.884   -18.895 1.00 23.18  ?  49  ASP A CG    1 
ATOM   137   O  OD1   . ASP A  1  17  ? 15.028 7.604   -20.020 1.00 22.78  ?  49  ASP A OD1   1 
ATOM   138   O  OD2   . ASP A  1  17  ? 14.669 8.546   -18.177 1.00 24.09  -1 49  ASP A OD2   1 
ATOM   139   N  N     . PRO A  1  18  ? 17.938 6.215   -21.514 1.00 20.36  ?  50  PRO A N     1 
ATOM   140   C  CA    . PRO A  1  18  ? 18.632 6.764   -22.670 1.00 20.11  ?  50  PRO A CA    1 
ATOM   141   C  C     . PRO A  1  18  ? 18.058 8.017   -23.264 1.00 20.40  ?  50  PRO A C     1 
ATOM   142   O  O     . PRO A  1  18  ? 18.635 8.574   -24.142 1.00 21.81  ?  50  PRO A O     1 
ATOM   143   C  CB    . PRO A  1  18  ? 18.495 5.659   -23.687 1.00 19.88  ?  50  PRO A CB    1 
ATOM   144   C  CG    . PRO A  1  18  ? 18.298 4.444   -22.922 1.00 19.90  ?  50  PRO A CG    1 
ATOM   145   C  CD    . PRO A  1  18  ? 17.315 4.915   -21.986 1.00 20.21  ?  50  PRO A CD    1 
ATOM   146   N  N     . THR A  1  19  ? 16.935 8.442   -22.731 1.00 19.88  ?  51  THR A N     1 
ATOM   147   C  CA    . THR A  1  19  ? 16.199 9.598   -23.157 1.00 19.47  ?  51  THR A CA    1 
ATOM   148   C  C     . THR A  1  19  ? 16.645 10.887  -22.586 1.00 19.88  ?  51  THR A C     1 
ATOM   149   O  O     . THR A  1  19  ? 16.394 11.921  -23.121 1.00 19.74  ?  51  THR A O     1 
ATOM   150   C  CB    . THR A  1  19  ? 14.803 9.443   -22.616 1.00 19.69  ?  51  THR A CB    1 
ATOM   151   O  OG1   . THR A  1  19  ? 14.290 8.224   -23.088 1.00 19.17  ?  51  THR A OG1   1 
ATOM   152   C  CG2   . THR A  1  19  ? 13.901 10.494  -23.097 1.00 21.25  ?  51  THR A CG2   1 
ATOM   153   N  N     . TYR A  1  20  ? 17.252 10.811  -21.445 1.00 21.19  ?  52  TYR A N     1 
ATOM   154   C  CA    . TYR A  1  20  ? 17.619 11.956  -20.728 1.00 21.43  ?  52  TYR A CA    1 
ATOM   155   C  C     . TYR A  1  20  ? 18.313 12.949  -21.547 1.00 22.51  ?  52  TYR A C     1 
ATOM   156   O  O     . TYR A  1  20  ? 19.032 12.628  -22.432 1.00 21.16  ?  52  TYR A O     1 
ATOM   157   C  CB    . TYR A  1  20  ? 18.449 11.549  -19.553 1.00 21.14  ?  52  TYR A CB    1 
ATOM   158   C  CG    . TYR A  1  20  ? 18.505 12.600  -18.537 1.00 20.50  ?  52  TYR A CG    1 
ATOM   159   C  CD1   . TYR A  1  20  ? 19.382 13.606  -18.642 1.00 20.34  ?  52  TYR A CD1   1 
ATOM   160   C  CD2   . TYR A  1  20  ? 17.679 12.590  -17.481 1.00 20.57  ?  52  TYR A CD2   1 
ATOM   161   C  CE1   . TYR A  1  20  ? 19.429 14.575  -17.715 1.00 20.45  ?  52  TYR A CE1   1 
ATOM   162   C  CE2   . TYR A  1  20  ? 17.721 13.576  -16.565 1.00 20.54  ?  52  TYR A CE2   1 
ATOM   163   C  CZ    . TYR A  1  20  ? 18.602 14.550  -16.708 1.00 20.60  ?  52  TYR A CZ    1 
ATOM   164   O  OH    . TYR A  1  20  ? 18.658 15.512  -15.798 1.00 21.42  ?  52  TYR A OH    1 
ATOM   165   N  N     . HIS A  1  21  ? 18.047 14.187  -21.222 1.00 25.85  ?  53  HIS A N     1 
ATOM   166   C  CA    . HIS A  1  21  ? 18.691 15.307  -21.802 1.00 30.90  ?  53  HIS A CA    1 
ATOM   167   C  C     . HIS A  1  21  ? 18.036 16.450  -21.166 1.00 29.95  ?  53  HIS A C     1 
ATOM   168   O  O     . HIS A  1  21  ? 16.939 16.371  -20.799 1.00 29.72  ?  53  HIS A O     1 
ATOM   169   C  CB    . HIS A  1  21  ? 18.822 15.180  -23.292 1.00 37.09  ?  53  HIS A CB    1 
ATOM   170   C  CG    . HIS A  1  21  ? 17.589 15.530  -24.045 1.00 44.26  ?  53  HIS A CG    1 
ATOM   171   N  ND1   . HIS A  1  21  ? 16.341 15.194  -23.600 1.00 48.45  ?  53  HIS A ND1   1 
ATOM   172   C  CD2   . HIS A  1  21  ? 17.413 16.193  -25.201 1.00 49.01  ?  53  HIS A CD2   1 
ATOM   173   C  CE1   . HIS A  1  21  ? 15.446 15.603  -24.471 1.00 51.37  ?  53  HIS A CE1   1 
ATOM   174   N  NE2   . HIS A  1  21  ? 16.072 16.230  -25.441 1.00 54.12  ?  53  HIS A NE2   1 
ATOM   175   N  N     . ILE A  1  22  ? 18.777 17.519  -21.063 1.00 30.87  ?  54  ILE A N     1 
ATOM   176   C  CA    . ILE A  1  22  ? 18.365 18.861  -20.661 1.00 31.34  ?  54  ILE A CA    1 
ATOM   177   C  C     . ILE A  1  22  ? 17.646 19.595  -21.793 1.00 32.88  ?  54  ILE A C     1 
ATOM   178   O  O     . ILE A  1  22  ? 18.162 19.731  -22.902 1.00 31.96  ?  54  ILE A O     1 
ATOM   179   C  CB    . ILE A  1  22  ? 19.586 19.701  -20.227 1.00 30.82  ?  54  ILE A CB    1 
ATOM   180   C  CG1   . ILE A  1  22  ? 20.322 18.996  -19.085 1.00 30.86  ?  54  ILE A CG1   1 
ATOM   181   C  CG2   . ILE A  1  22  ? 19.176 21.118  -19.840 1.00 30.78  ?  54  ILE A CG2   1 
ATOM   182   C  CD1   . ILE A  1  22  ? 19.419 18.563  -17.953 1.00 31.17  ?  54  ILE A CD1   1 
ATOM   183   N  N     . THR A  1  23  ? 16.446 20.066  -21.495 1.00 35.42  ?  55  THR A N     1 
ATOM   184   C  CA    . THR A  1  23  ? 15.680 20.885  -22.429 1.00 38.25  ?  55  THR A CA    1 
ATOM   185   C  C     . THR A  1  23  ? 14.761 21.779  -21.584 1.00 38.84  ?  55  THR A C     1 
ATOM   186   O  O     . THR A  1  23  ? 14.589 21.538  -20.382 1.00 40.07  ?  55  THR A O     1 
ATOM   187   C  CB    . THR A  1  23  ? 14.929 19.998  -23.464 1.00 39.52  ?  55  THR A CB    1 
ATOM   188   O  OG1   . THR A  1  23  ? 14.572 20.768  -24.617 1.00 40.05  ?  55  THR A OG1   1 
ATOM   189   C  CG2   . THR A  1  23  ? 13.675 19.361  -22.862 1.00 40.69  ?  55  THR A CG2   1 
ATOM   190   N  N     . ASP A  1  24  ? 14.198 22.821  -22.181 1.00 39.50  ?  56  ASP A N     1 
ATOM   191   C  CA    . ASP A  1  24  ? 13.448 23.812  -21.392 1.00 40.60  ?  56  ASP A CA    1 
ATOM   192   C  C     . ASP A  1  24  ? 12.064 23.350  -20.919 1.00 37.91  ?  56  ASP A C     1 
ATOM   193   O  O     . ASP A  1  24  ? 11.568 23.857  -19.927 1.00 39.65  ?  56  ASP A O     1 
ATOM   194   C  CB    . ASP A  1  24  ? 13.354 25.136  -22.151 1.00 42.10  ?  56  ASP A CB    1 
ATOM   195   C  CG    . ASP A  1  24  ? 14.713 25.762  -22.360 1.00 43.58  ?  56  ASP A CG    1 
ATOM   196   O  OD1   . ASP A  1  24  ? 15.406 26.042  -21.350 1.00 40.81  ?  56  ASP A OD1   1 
ATOM   197   O  OD2   . ASP A  1  24  ? 15.095 25.933  -23.540 1.00 45.67  -1 56  ASP A OD2   1 
ATOM   198   N  N     . ASP A  1  25  ? 11.457 22.401  -21.626 1.00 35.18  ?  57  ASP A N     1 
ATOM   199   C  CA    . ASP A  1  25  ? 10.219 21.745  -21.193 1.00 33.62  ?  57  ASP A CA    1 
ATOM   200   C  C     . ASP A  1  25  ? 10.602 20.560  -20.304 1.00 32.41  ?  57  ASP A C     1 
ATOM   201   O  O     . ASP A  1  25  ? 11.011 19.484  -20.782 1.00 30.83  ?  57  ASP A O     1 
ATOM   202   C  CB    . ASP A  1  25  ? 9.426  21.266  -22.420 1.00 35.35  ?  57  ASP A CB    1 
ATOM   203   C  CG    . ASP A  1  25  ? 8.045  20.710  -22.081 1.00 35.80  ?  57  ASP A CG    1 
ATOM   204   O  OD1   . ASP A  1  25  ? 7.708  20.537  -20.896 1.00 34.54  ?  57  ASP A OD1   1 
ATOM   205   O  OD2   . ASP A  1  25  ? 7.276  20.452  -23.034 1.00 39.28  -1 57  ASP A OD2   1 
ATOM   206   N  N     . HIS A  1  26  ? 10.454 20.763  -19.000 1.00 31.47  ?  58  HIS A N     1 
ATOM   207   C  CA    . HIS A  1  26  ? 10.863 19.769  -18.010 1.00 30.72  ?  58  HIS A CA    1 
ATOM   208   C  C     . HIS A  1  26  ? 10.009 18.488  -18.007 1.00 28.95  ?  58  HIS A C     1 
ATOM   209   O  O     . HIS A  1  26  ? 10.401 17.487  -17.412 1.00 31.15  ?  58  HIS A O     1 
ATOM   210   C  CB    . HIS A  1  26  ? 10.933 20.406  -16.603 1.00 31.04  ?  58  HIS A CB    1 
ATOM   211   C  CG    . HIS A  1  26  ? 12.117 21.310  -16.395 1.00 30.85  ?  58  HIS A CG    1 
ATOM   212   N  ND1   . HIS A  1  26  ? 13.125 21.467  -17.332 1.00 30.46  ?  58  HIS A ND1   1 
ATOM   213   C  CD2   . HIS A  1  26  ? 12.472 22.068  -15.328 1.00 29.68  ?  58  HIS A CD2   1 
ATOM   214   C  CE1   . HIS A  1  26  ? 14.034 22.298  -16.860 1.00 30.23  ?  58  HIS A CE1   1 
ATOM   215   N  NE2   . HIS A  1  26  ? 13.666 22.669  -15.644 1.00 30.74  ?  58  HIS A NE2   1 
ATOM   216   N  N     . THR A  1  27  ? 8.876  18.490  -18.688 1.00 26.84  ?  59  THR A N     1 
ATOM   217   C  CA    . THR A  1  27  ? 8.130  17.260  -18.857 1.00 27.23  ?  59  THR A CA    1 
ATOM   218   C  C     . THR A  1  27  ? 8.802  16.353  -19.880 1.00 29.23  ?  59  THR A C     1 
ATOM   219   O  O     . THR A  1  27  ? 8.507  15.161  -19.923 1.00 30.05  ?  59  THR A O     1 
ATOM   220   C  CB    . THR A  1  27  ? 6.721  17.511  -19.351 1.00 26.05  ?  59  THR A CB    1 
ATOM   221   O  OG1   . THR A  1  27  ? 6.791  17.906  -20.721 1.00 25.96  ?  59  THR A OG1   1 
ATOM   222   C  CG2   . THR A  1  27  ? 6.014  18.587  -18.490 1.00 25.93  ?  59  THR A CG2   1 
ATOM   223   N  N     . LYS A  1  28  ? 9.708  16.911  -20.684 1.00 31.69  ?  60  LYS A N     1 
ATOM   224   C  CA    . LYS A  1  28  ? 10.328 16.186  -21.796 1.00 33.81  ?  60  LYS A CA    1 
ATOM   225   C  C     . LYS A  1  28  ? 11.762 15.736  -21.534 1.00 32.45  ?  60  LYS A C     1 
ATOM   226   O  O     . LYS A  1  28  ? 12.323 14.924  -22.307 1.00 34.87  ?  60  LYS A O     1 
ATOM   227   C  CB    . LYS A  1  28  ? 10.289 17.046  -23.075 1.00 37.29  ?  60  LYS A CB    1 
ATOM   228   C  CG    . LYS A  1  28  ? 8.899  17.299  -23.658 1.00 38.67  ?  60  LYS A CG    1 
ATOM   229   C  CD    . LYS A  1  28  ? 8.179  15.993  -23.963 1.00 41.05  ?  60  LYS A CD    1 
ATOM   230   C  CE    . LYS A  1  28  ? 6.749  16.234  -24.387 1.00 42.24  ?  60  LYS A CE    1 
ATOM   231   N  NZ    . LYS A  1  28  ? 6.724  16.922  -25.705 1.00 42.35  1  60  LYS A NZ    1 
ATOM   232   N  N     . VAL A  1  29  ? 12.345 16.241  -20.449 1.00 29.06  ?  61  VAL A N     1 
ATOM   233   C  CA    . VAL A  1  29  ? 13.725 15.891  -20.061 1.00 26.48  ?  61  VAL A CA    1 
ATOM   234   C  C     . VAL A  1  29  ? 14.012 14.371  -20.034 1.00 25.20  ?  61  VAL A C     1 
ATOM   235   O  O     . VAL A  1  29  ? 15.068 13.910  -20.495 1.00 25.09  ?  61  VAL A O     1 
ATOM   236   C  CB    . VAL A  1  29  ? 14.064 16.507  -18.697 1.00 25.17  ?  61  VAL A CB    1 
ATOM   237   C  CG1   . VAL A  1  29  ? 15.256 15.818  -18.052 1.00 25.32  ?  61  VAL A CG1   1 
ATOM   238   C  CG2   . VAL A  1  29  ? 14.310 17.986  -18.854 1.00 24.90  ?  61  VAL A CG2   1 
ATOM   239   N  N     . CYS A  1  30  ? 13.088 13.588  -19.505 1.00 23.23  ?  62  CYS A N     1 
ATOM   240   C  CA    . CYS A  1  30  ? 13.338 12.166  -19.428 1.00 22.55  ?  62  CYS A CA    1 
ATOM   241   C  C     . CYS A  1  30  ? 12.046 11.406  -19.361 1.00 20.70  ?  62  CYS A C     1 
ATOM   242   O  O     . CYS A  1  30  ? 11.131 11.770  -18.616 1.00 20.58  ?  62  CYS A O     1 
ATOM   243   C  CB    . CYS A  1  30  ? 14.178 11.842  -18.190 1.00 23.57  ?  62  CYS A CB    1 
ATOM   244   S  SG    . CYS A  1  30  ? 13.199 11.757  -16.671 1.00 24.48  ?  62  CYS A SG    1 
ATOM   245   N  N     . ALA A  1  31  ? 11.999 10.318  -20.107 1.00 18.72  ?  63  ALA A N     1 
ATOM   246   C  CA    . ALA A  1  31  ? 10.793 9.542   -20.196 1.00 18.51  ?  63  ALA A CA    1 
ATOM   247   C  C     . ALA A  1  31  ? 10.418 8.892   -18.845 1.00 18.35  ?  63  ALA A C     1 
ATOM   248   O  O     . ALA A  1  31  ? 9.230  8.679   -18.563 1.00 18.69  ?  63  ALA A O     1 
ATOM   249   C  CB    . ALA A  1  31  ? 10.941 8.487   -21.269 1.00 18.23  ?  63  ALA A CB    1 
ATOM   250   N  N     . SER A  1  32  ? 11.409 8.587   -18.009 1.00 17.64  ?  64  SER A N     1 
ATOM   251   C  CA    . SER A  1  32  ? 11.141 7.938   -16.720 1.00 17.15  ?  64  SER A CA    1 
ATOM   252   C  C     . SER A  1  32  ? 10.267 8.802   -15.823 1.00 15.85  ?  64  SER A C     1 
ATOM   253   O  O     . SER A  1  32  ? 9.462  8.263   -15.081 1.00 15.38  ?  64  SER A O     1 
ATOM   254   C  CB    . SER A  1  32  ? 12.432 7.570   -15.998 1.00 17.84  ?  64  SER A CB    1 
ATOM   255   O  OG    . SER A  1  32  ? 13.349 8.661   -16.022 1.00 18.84  ?  64  SER A OG    1 
ATOM   256   N  N     . SER A  1  33  ? 10.388 10.130  -15.930 1.00 14.66  ?  65  SER A N     1 
ATOM   257   C  CA    . SER A  1  33  ? 9.552  11.027  -15.139 1.00 13.71  ?  65  SER A CA    1 
ATOM   258   C  C     . SER A  1  33  ? 8.076  10.879  -15.539 1.00 13.41  ?  65  SER A C     1 
ATOM   259   O  O     . SER A  1  33  ? 7.186  11.375  -14.851 1.00 13.09  ?  65  SER A O     1 
ATOM   260   C  CB    . SER A  1  33  ? 9.991  12.467  -15.288 1.00 13.32  ?  65  SER A CB    1 
ATOM   261   O  OG    . SER A  1  33  ? 9.031  13.171  -16.046 1.00 13.90  ?  65  SER A OG    1 
ATOM   262   N  N     . LYS A  1  34  ? 7.831  10.216  -16.662 1.00 13.11  ?  66  LYS A N     1 
ATOM   263   C  CA    . LYS A  1  34  ? 6.492  9.917   -17.116 1.00 13.68  ?  66  LYS A CA    1 
ATOM   264   C  C     . LYS A  1  34  ? 5.591  11.155  -17.255 1.00 14.01  ?  66  LYS A C     1 
ATOM   265   O  O     . LYS A  1  34  ? 4.388  11.120  -17.033 1.00 13.67  ?  66  LYS A O     1 
ATOM   266   C  CB    . LYS A  1  34  ? 5.848  8.865   -16.223 1.00 13.89  ?  66  LYS A CB    1 
ATOM   267   C  CG    . LYS A  1  34  ? 6.602  7.544   -16.200 1.00 14.19  ?  66  LYS A CG    1 
ATOM   268   C  CD    . LYS A  1  34  ? 6.322  6.813   -14.894 1.00 14.41  ?  66  LYS A CD    1 
ATOM   269   C  CE    . LYS A  1  34  ? 7.316  5.701   -14.628 1.00 14.68  ?  66  LYS A CE    1 
ATOM   270   N  NZ    . LYS A  1  34  ? 8.267  6.024   -13.529 1.00 14.95  1  66  LYS A NZ    1 
ATOM   271   N  N     . GLY A  1  35  ? 6.166  12.257  -17.669 1.00 14.56  ?  67  GLY A N     1 
ATOM   272   C  CA    . GLY A  1  35  ? 5.323  13.353  -17.998 1.00 15.75  ?  67  GLY A CA    1 
ATOM   273   C  C     . GLY A  1  35  ? 5.343  14.420  -16.953 1.00 17.06  ?  67  GLY A C     1 
ATOM   274   O  O     . GLY A  1  35  ? 4.939  15.565  -17.229 1.00 17.69  ?  67  GLY A O     1 
ATOM   275   N  N     . ALA A  1  36  ? 5.824  14.081  -15.760 1.00 18.17  ?  68  ALA A N     1 
ATOM   276   C  CA    . ALA A  1  36  ? 5.955  15.099  -14.705 1.00 18.59  ?  68  ALA A CA    1 
ATOM   277   C  C     . ALA A  1  36  ? 7.126  16.020  -15.003 1.00 17.96  ?  68  ALA A C     1 
ATOM   278   O  O     . ALA A  1  36  ? 8.056  15.634  -15.692 1.00 17.00  ?  68  ALA A O     1 
ATOM   279   C  CB    . ALA A  1  36  ? 6.121  14.453  -13.342 1.00 18.90  ?  68  ALA A CB    1 
ATOM   280   N  N     . ASN A  1  37  ? 7.040  17.248  -14.508 1.00 18.45  ?  69  ASN A N     1 
ATOM   281   C  CA    . ASN A  1  37  ? 8.145  18.183  -14.608 1.00 19.44  ?  69  ASN A CA    1 
ATOM   282   C  C     . ASN A  1  37  ? 9.258  17.640  -13.761 1.00 19.51  ?  69  ASN A C     1 
ATOM   283   O  O     . ASN A  1  37  ? 9.065  17.354  -12.577 1.00 19.17  ?  69  ASN A O     1 
ATOM   284   C  CB    . ASN A  1  37  ? 7.760  19.604  -14.145 1.00 20.12  ?  69  ASN A CB    1 
ATOM   285   C  CG    . ASN A  1  37  ? 7.303  20.501  -15.290 1.00 20.95  ?  69  ASN A CG    1 
ATOM   286   O  OD1   . ASN A  1  37  ? 7.750  20.339  -16.415 1.00 22.11  ?  69  ASN A OD1   1 
ATOM   287   N  ND2   . ASN A  1  37  ? 6.433  21.468  -14.998 1.00 22.25  ?  69  ASN A ND2   1 
ATOM   288   N  N     . ALA A  1  38  ? 10.409 17.456  -14.390 1.00 20.23  ?  70  ALA A N     1 
ATOM   289   C  CA    . ALA A  1  38  ? 11.602 17.032  -13.685 1.00 21.53  ?  70  ALA A CA    1 
ATOM   290   C  C     . ALA A  1  38  ? 11.910 18.137  -12.695 1.00 22.56  ?  70  ALA A C     1 
ATOM   291   O  O     . ALA A  1  38  ? 11.844 19.314  -13.050 1.00 23.76  ?  70  ALA A O     1 
ATOM   292   C  CB    . ALA A  1  38  ? 12.758 16.822  -14.644 1.00 21.35  ?  70  ALA A CB    1 
ATOM   293   N  N     . SER A  1  39  ? 12.193 17.769  -11.451 1.00 22.79  ?  71  SER A N     1 
ATOM   294   C  CA    . SER A  1  39  ? 12.193 18.753  -10.392 1.00 23.13  ?  71  SER A CA    1 
ATOM   295   C  C     . SER A  1  39  ? 13.170 19.871  -10.649 1.00 22.78  ?  71  SER A C     1 
ATOM   296   O  O     . SER A  1  39  ? 12.810 21.036  -10.568 1.00 22.30  ?  71  SER A O     1 
ATOM   297   C  CB    . SER A  1  39  ? 12.529 18.141  -9.044  1.00 23.43  ?  71  SER A CB    1 
ATOM   298   O  OG    . SER A  1  39  ? 12.423 19.176  -8.088  1.00 23.16  ?  71  SER A OG    1 
ATOM   299   N  N     . ASN A  1  40  ? 14.418 19.505  -10.914 1.00 22.96  ?  72  ASN A N     1 
ATOM   300   C  CA    . ASN A  1  40  ? 15.468 20.485  -11.108 1.00 22.77  ?  72  ASN A CA    1 
ATOM   301   C  C     . ASN A  1  40  ? 16.669 19.878  -11.802 1.00 21.01  ?  72  ASN A C     1 
ATOM   302   O  O     . ASN A  1  40  ? 17.694 19.657  -11.186 1.00 19.92  ?  72  ASN A O     1 
ATOM   303   C  CB    . ASN A  1  40  ? 15.904 21.065  -9.791  1.00 23.97  ?  72  ASN A CB    1 
ATOM   304   C  CG    . ASN A  1  40  ? 17.084 21.963  -9.960  1.00 26.72  ?  72  ASN A CG    1 
ATOM   305   O  OD1   . ASN A  1  40  ? 17.293 22.541  -11.038 1.00 28.47  ?  72  ASN A OD1   1 
ATOM   306   N  ND2   . ASN A  1  40  ? 17.895 22.066  -8.926  1.00 29.54  ?  72  ASN A ND2   1 
ATOM   307   N  N     . PRO A  1  41  ? 16.543 19.649  -13.108 1.00 19.73  ?  73  PRO A N     1 
ATOM   308   C  CA    . PRO A  1  41  ? 17.393 18.684  -13.749 1.00 19.40  ?  73  PRO A CA    1 
ATOM   309   C  C     . PRO A  1  41  ? 18.753 19.236  -14.049 1.00 18.73  ?  73  PRO A C     1 
ATOM   310   O  O     . PRO A  1  41  ? 18.879 20.413  -14.271 1.00 18.90  ?  73  PRO A O     1 
ATOM   311   C  CB    . PRO A  1  41  ? 16.638 18.372  -15.052 1.00 19.11  ?  73  PRO A CB    1 
ATOM   312   C  CG    . PRO A  1  41  ? 15.808 19.569  -15.326 1.00 18.69  ?  73  PRO A CG    1 
ATOM   313   C  CD    . PRO A  1  41  ? 15.693 20.370  -14.069 1.00 18.91  ?  73  PRO A CD    1 
ATOM   314   N  N     . GLY A  1  42  ? 19.749 18.366  -14.064 1.00 18.55  ?  74  GLY A N     1 
ATOM   315   C  CA    . GLY A  1  42  ? 21.088 18.733  -14.457 1.00 18.89  ?  74  GLY A CA    1 
ATOM   316   C  C     . GLY A  1  42  ? 21.764 17.648  -15.281 1.00 19.36  ?  74  GLY A C     1 
ATOM   317   O  O     . GLY A  1  42  ? 21.142 16.631  -15.640 1.00 17.93  ?  74  GLY A O     1 
ATOM   318   N  N     . PRO A  1  43  ? 23.053 17.862  -15.594 1.00 20.51  ?  75  PRO A N     1 
ATOM   319   C  CA    . PRO A  1  43  ? 23.820 16.931  -16.428 1.00 21.49  ?  75  PRO A CA    1 
ATOM   320   C  C     . PRO A  1  43  ? 23.996 15.546  -15.805 1.00 23.36  ?  75  PRO A C     1 
ATOM   321   O  O     . PRO A  1  43  ? 24.203 14.571  -16.541 1.00 24.46  ?  75  PRO A O     1 
ATOM   322   C  CB    . PRO A  1  43  ? 25.178 17.616  -16.588 1.00 21.12  ?  75  PRO A CB    1 
ATOM   323   C  CG    . PRO A  1  43  ? 25.237 18.679  -15.544 1.00 21.07  ?  75  PRO A CG    1 
ATOM   324   C  CD    . PRO A  1  43  ? 23.831 19.054  -15.209 1.00 20.55  ?  75  PRO A CD    1 
ATOM   325   N  N     . PHE A  1  44  ? 23.921 15.450  -14.472 1.00 24.83  ?  76  PHE A N     1 
ATOM   326   C  CA    . PHE A  1  44  ? 24.028 14.141  -13.793 1.00 24.84  ?  76  PHE A CA    1 
ATOM   327   C  C     . PHE A  1  44  ? 22.717 13.573  -13.278 1.00 23.17  ?  76  PHE A C     1 
ATOM   328   O  O     . PHE A  1  44  ? 22.719 12.482  -12.690 1.00 22.35  ?  76  PHE A O     1 
ATOM   329   C  CB    . PHE A  1  44  ? 25.024 14.233  -12.671 1.00 25.63  ?  76  PHE A CB    1 
ATOM   330   C  CG    . PHE A  1  44  ? 26.298 14.841  -13.100 1.00 27.19  ?  76  PHE A CG    1 
ATOM   331   C  CD1   . PHE A  1  44  ? 27.146 14.140  -13.921 1.00 28.27  ?  76  PHE A CD1   1 
ATOM   332   C  CD2   . PHE A  1  44  ? 26.627 16.134  -12.735 1.00 29.04  ?  76  PHE A CD2   1 
ATOM   333   C  CE1   . PHE A  1  44  ? 28.333 14.700  -14.346 1.00 29.24  ?  76  PHE A CE1   1 
ATOM   334   C  CE2   . PHE A  1  44  ? 27.818 16.700  -13.156 1.00 29.59  ?  76  PHE A CE2   1 
ATOM   335   C  CZ    . PHE A  1  44  ? 28.675 15.981  -13.957 1.00 29.03  ?  76  PHE A CZ    1 
ATOM   336   N  N     . GLY A  1  45  ? 21.628 14.318  -13.483 1.00 21.24  ?  77  GLY A N     1 
ATOM   337   C  CA    . GLY A  1  45  ? 20.294 13.766  -13.406 1.00 20.28  ?  77  GLY A CA    1 
ATOM   338   C  C     . GLY A  1  45  ? 19.308 14.574  -12.598 1.00 19.65  ?  77  GLY A C     1 
ATOM   339   O  O     . GLY A  1  45  ? 19.542 15.723  -12.282 1.00 19.38  ?  77  GLY A O     1 
ATOM   340   N  N     . ASP A  1  46  ? 18.194 13.941  -12.267 1.00 19.50  ?  78  ASP A N     1 
ATOM   341   C  CA    . ASP A  1  46  ? 17.139 14.572  -11.504 1.00 20.00  ?  78  ASP A CA    1 
ATOM   342   C  C     . ASP A  1  46  ? 16.427 13.544  -10.642 1.00 19.72  ?  78  ASP A C     1 
ATOM   343   O  O     . ASP A  1  46  ? 16.296 12.386  -11.026 1.00 20.08  ?  78  ASP A O     1 
ATOM   344   C  CB    . ASP A  1  46  ? 16.136 15.197  -12.440 1.00 20.41  ?  78  ASP A CB    1 
ATOM   345   C  CG    . ASP A  1  46  ? 15.144 16.020  -11.714 1.00 21.25  ?  78  ASP A CG    1 
ATOM   346   O  OD1   . ASP A  1  46  ? 15.561 16.965  -11.006 1.00 21.50  ?  78  ASP A OD1   1 
ATOM   347   O  OD2   . ASP A  1  46  ? 13.952 15.698  -11.827 1.00 22.26  -1 78  ASP A OD2   1 
ATOM   348   N  N     . VAL A  1  47  ? 15.954 13.953  -9.474  1.00 19.17  ?  79  VAL A N     1 
ATOM   349   C  CA    . VAL A  1  47  ? 15.358 12.976  -8.547  1.00 18.90  ?  79  VAL A CA    1 
ATOM   350   C  C     . VAL A  1  47  ? 14.157 12.233  -9.148  1.00 18.47  ?  79  VAL A C     1 
ATOM   351   O  O     . VAL A  1  47  ? 13.837 11.132  -8.723  1.00 17.84  ?  79  VAL A O     1 
ATOM   352   C  CB    . VAL A  1  47  ? 14.944 13.604  -7.188  1.00 18.83  ?  79  VAL A CB    1 
ATOM   353   C  CG1   . VAL A  1  47  ? 16.144 13.746  -6.279  1.00 18.96  ?  79  VAL A CG1   1 
ATOM   354   C  CG2   . VAL A  1  47  ? 14.261 14.953  -7.363  1.00 19.32  ?  79  VAL A CG2   1 
ATOM   355   N  N     . LEU A  1  48  ? 13.515 12.847  -10.136 1.00 18.55  ?  80  LEU A N     1 
ATOM   356   C  CA    . LEU A  1  48  ? 12.315 12.305  -10.768 1.00 18.92  ?  80  LEU A CA    1 
ATOM   357   C  C     . LEU A  1  48  ? 12.643 11.494  -12.034 1.00 19.16  ?  80  LEU A C     1 
ATOM   358   O  O     . LEU A  1  48  ? 11.772 10.891  -12.648 1.00 18.34  ?  80  LEU A O     1 
ATOM   359   C  CB    . LEU A  1  48  ? 11.392 13.474  -11.111 1.00 18.80  ?  80  LEU A CB    1 
ATOM   360   C  CG    . LEU A  1  48  ? 10.158 13.793  -10.258 1.00 18.48  ?  80  LEU A CG    1 
ATOM   361   C  CD1   . LEU A  1  48  ? 10.208 13.153  -8.905  1.00 18.62  ?  80  LEU A CD1   1 
ATOM   362   C  CD2   . LEU A  1  48  ? 9.979  15.295  -10.136 1.00 18.58  ?  80  LEU A CD2   1 
ATOM   363   N  N     . CYS A  1  49  ? 13.920 11.478  -12.387 1.00 19.87  ?  81  CYS A N     1 
ATOM   364   C  CA    . CYS A  1  49  ? 14.407 10.863  -13.599 1.00 20.22  ?  81  CYS A CA    1 
ATOM   365   C  C     . CYS A  1  49  ? 15.380 9.770   -13.244 1.00 20.17  ?  81  CYS A C     1 
ATOM   366   O  O     . CYS A  1  49  ? 16.194 9.928   -12.340 1.00 21.01  ?  81  CYS A O     1 
ATOM   367   C  CB    . CYS A  1  49  ? 15.166 11.897  -14.427 1.00 20.98  ?  81  CYS A CB    1 
ATOM   368   S  SG    . CYS A  1  49  ? 14.118 13.041  -15.341 1.00 22.73  ?  81  CYS A SG    1 
ATOM   369   N  N     . ASP A  1  50  ? 15.305 8.661   -13.960 1.00 19.34  ?  82  ASP A N     1 
ATOM   370   C  CA    . ASP A  1  50  ? 16.353 7.683   -13.927 1.00 18.66  ?  82  ASP A CA    1 
ATOM   371   C  C     . ASP A  1  50  ? 17.711 8.209   -14.434 1.00 18.38  ?  82  ASP A C     1 
ATOM   372   O  O     . ASP A  1  50  ? 17.847 9.371   -14.798 1.00 17.27  ?  82  ASP A O     1 
ATOM   373   C  CB    . ASP A  1  50  ? 15.908 6.504   -14.744 1.00 19.43  ?  82  ASP A CB    1 
ATOM   374   C  CG    . ASP A  1  50  ? 15.304 5.423   -13.888 1.00 20.94  ?  82  ASP A CG    1 
ATOM   375   O  OD1   . ASP A  1  50  ? 15.867 5.108   -12.814 1.00 22.44  ?  82  ASP A OD1   1 
ATOM   376   O  OD2   . ASP A  1  50  ? 14.282 4.840   -14.294 1.00 21.91  -1 82  ASP A OD2   1 
ATOM   377   N  N     . SER A  1  51  ? 18.734 7.361   -14.415 1.00 19.05  ?  83  SER A N     1 
ATOM   378   C  CA    . SER A  1  51  ? 20.117 7.819   -14.626 1.00 19.29  ?  83  SER A CA    1 
ATOM   379   C  C     . SER A  1  51  ? 20.382 8.243   -16.063 1.00 19.96  ?  83  SER A C     1 
ATOM   380   O  O     . SER A  1  51  ? 20.147 7.448   -16.972 1.00 20.62  ?  83  SER A O     1 
ATOM   381   C  CB    . SER A  1  51  ? 21.099 6.680   -14.307 1.00 18.92  ?  83  SER A CB    1 
ATOM   382   O  OG    . SER A  1  51  ? 20.964 6.177   -12.991 1.00 17.79  ?  83  SER A OG    1 
ATOM   383   N  N     . PRO A  1  52  ? 20.873 9.477   -16.284 1.00 20.55  ?  84  PRO A N     1 
ATOM   384   C  CA    . PRO A  1  52  ? 21.415 9.836   -17.608 1.00 20.66  ?  84  PRO A CA    1 
ATOM   385   C  C     . PRO A  1  52  ? 22.709 9.154   -17.773 1.00 21.21  ?  84  PRO A C     1 
ATOM   386   O  O     . PRO A  1  52  ? 23.375 8.945   -16.782 1.00 21.96  ?  84  PRO A O     1 
ATOM   387   C  CB    . PRO A  1  52  ? 21.689 11.327  -17.509 1.00 20.69  ?  84  PRO A CB    1 
ATOM   388   C  CG    . PRO A  1  52  ? 21.755 11.629  -16.050 1.00 21.22  ?  84  PRO A CG    1 
ATOM   389   C  CD    . PRO A  1  52  ? 20.866 10.623  -15.361 1.00 21.14  ?  84  PRO A CD    1 
ATOM   390   N  N     . TYR A  1  53  ? 23.095 8.839   -18.996 1.00 22.31  ?  85  TYR A N     1 
ATOM   391   C  CA    . TYR A  1  53  ? 24.312 8.058   -19.219 1.00 23.40  ?  85  TYR A CA    1 
ATOM   392   C  C     . TYR A  1  53  ? 25.551 8.593   -18.523 1.00 23.80  ?  85  TYR A C     1 
ATOM   393   O  O     . TYR A  1  53  ? 26.420 7.846   -18.126 1.00 24.18  ?  85  TYR A O     1 
ATOM   394   C  CB    . TYR A  1  53  ? 24.610 7.985   -20.696 1.00 24.40  ?  85  TYR A CB    1 
ATOM   395   C  CG    . TYR A  1  53  ? 25.764 7.090   -21.008 1.00 25.83  ?  85  TYR A CG    1 
ATOM   396   C  CD1   . TYR A  1  53  ? 25.680 5.732   -20.755 1.00 26.55  ?  85  TYR A CD1   1 
ATOM   397   C  CD2   . TYR A  1  53  ? 26.947 7.593   -21.555 1.00 26.33  ?  85  TYR A CD2   1 
ATOM   398   C  CE1   . TYR A  1  53  ? 26.731 4.887   -21.045 1.00 27.50  ?  85  TYR A CE1   1 
ATOM   399   C  CE2   . TYR A  1  53  ? 28.010 6.754   -21.843 1.00 27.21  ?  85  TYR A CE2   1 
ATOM   400   C  CZ    . TYR A  1  53  ? 27.890 5.397   -21.585 1.00 27.90  ?  85  TYR A CZ    1 
ATOM   401   O  OH    . TYR A  1  53  ? 28.912 4.524   -21.860 1.00 29.58  ?  85  TYR A OH    1 
ATOM   402   N  N     . GLN A  1  54  ? 25.629 9.892   -18.372 1.00 25.52  ?  86  GLN A N     1 
ATOM   403   C  CA    . GLN A  1  54  ? 26.824 10.508  -17.861 1.00 29.20  ?  86  GLN A CA    1 
ATOM   404   C  C     . GLN A  1  54  ? 27.011 10.340  -16.354 1.00 27.90  ?  86  GLN A C     1 
ATOM   405   O  O     . GLN A  1  54  ? 28.112 10.494  -15.816 1.00 28.31  ?  86  GLN A O     1 
ATOM   406   C  CB    . GLN A  1  54  ? 26.733 11.971  -18.191 1.00 34.29  ?  86  GLN A CB    1 
ATOM   407   C  CG    . GLN A  1  54  ? 28.020 12.744  -18.071 1.00 39.88  ?  86  GLN A CG    1 
ATOM   408   C  CD    . GLN A  1  54  ? 27.735 14.213  -18.301 1.00 48.17  ?  86  GLN A CD    1 
ATOM   409   O  OE1   . GLN A  1  54  ? 28.603 15.079  -18.118 1.00 56.46  ?  86  GLN A OE1   1 
ATOM   410   N  NE2   . GLN A  1  54  ? 26.490 14.513  -18.701 1.00 49.41  ?  86  GLN A NE2   1 
ATOM   411   N  N     . LEU A  1  55  ? 25.914 10.083  -15.662 1.00 27.04  ?  87  LEU A N     1 
ATOM   412   C  CA    . LEU A  1  55  ? 25.952 9.804   -14.231 1.00 25.04  ?  87  LEU A CA    1 
ATOM   413   C  C     . LEU A  1  55  ? 26.566 8.432   -14.106 1.00 23.97  ?  87  LEU A C     1 
ATOM   414   O  O     . LEU A  1  55  ? 27.556 8.259   -13.423 1.00 23.31  ?  87  LEU A O     1 
ATOM   415   C  CB    . LEU A  1  55  ? 24.538 9.810   -13.653 1.00 24.48  ?  87  LEU A CB    1 
ATOM   416   C  CG    . LEU A  1  55  ? 24.354 9.212   -12.271 1.00 24.12  ?  87  LEU A CG    1 
ATOM   417   C  CD1   . LEU A  1  55  ? 24.898 10.199  -11.278 1.00 24.69  ?  87  LEU A CD1   1 
ATOM   418   C  CD2   . LEU A  1  55  ? 22.901 8.933   -11.971 1.00 24.44  ?  87  LEU A CD2   1 
ATOM   419   N  N     . ILE A  1  56  ? 25.984 7.473   -14.815 1.00 23.69  ?  88  ILE A N     1 
ATOM   420   C  CA    . ILE A  1  56  ? 26.469 6.111   -14.810 1.00 24.41  ?  88  ILE A CA    1 
ATOM   421   C  C     . ILE A  1  56  ? 27.935 6.098   -15.168 1.00 24.96  ?  88  ILE A C     1 
ATOM   422   O  O     . ILE A  1  56  ? 28.729 5.296   -14.656 1.00 26.33  ?  88  ILE A O     1 
ATOM   423   C  CB    . ILE A  1  56  ? 25.811 5.257   -15.890 1.00 25.81  ?  88  ILE A CB    1 
ATOM   424   C  CG1   . ILE A  1  56  ? 24.282 5.293   -15.808 1.00 27.02  ?  88  ILE A CG1   1 
ATOM   425   C  CG2   . ILE A  1  56  ? 26.319 3.825   -15.783 1.00 26.72  ?  88  ILE A CG2   1 
ATOM   426   C  CD1   . ILE A  1  56  ? 23.719 4.791   -14.502 1.00 28.00  ?  88  ILE A CD1   1 
ATOM   427   N  N     . LEU A  1  57  ? 28.288 6.970   -16.096 1.00 24.14  ?  89  LEU A N     1 
ATOM   428   C  CA    . LEU A  1  57  ? 29.642 7.016   -16.567 1.00 23.98  ?  89  LEU A CA    1 
ATOM   429   C  C     . LEU A  1  57  ? 30.582 7.517   -15.489 1.00 23.09  ?  89  LEU A C     1 
ATOM   430   O  O     . LEU A  1  57  ? 31.620 6.921   -15.249 1.00 23.32  ?  89  LEU A O     1 
ATOM   431   C  CB    . LEU A  1  57  ? 29.725 7.917   -17.783 1.00 24.53  ?  89  LEU A CB    1 
ATOM   432   C  CG    . LEU A  1  57  ? 30.904 7.671   -18.709 1.00 24.69  ?  89  LEU A CG    1 
ATOM   433   C  CD1   . LEU A  1  57  ? 30.936 6.213   -19.188 1.00 24.35  ?  89  LEU A CD1   1 
ATOM   434   C  CD2   . LEU A  1  57  ? 30.762 8.645   -19.869 1.00 24.81  ?  89  LEU A CD2   1 
ATOM   435   N  N     . SER A  1  58  ? 30.203 8.610   -14.843 1.00 22.07  ?  90  SER A N     1 
ATOM   436   C  CA    . SER A  1  58  ? 31.026 9.203   -13.815 1.00 21.89  ?  90  SER A CA    1 
ATOM   437   C  C     . SER A  1  58  ? 31.197 8.263   -12.646 1.00 22.69  ?  90  SER A C     1 
ATOM   438   O  O     . SER A  1  58  ? 32.216 8.275   -11.970 1.00 24.43  ?  90  SER A O     1 
ATOM   439   C  CB    . SER A  1  58  ? 30.397 10.468  -13.302 1.00 21.21  ?  90  SER A CB    1 
ATOM   440   O  OG    . SER A  1  58  ? 29.333 10.137  -12.460 1.00 21.08  ?  90  SER A OG    1 
ATOM   441   N  N     . ALA A  1  59  ? 30.204 7.441   -12.392 1.00 22.75  ?  91  ALA A N     1 
ATOM   442   C  CA    . ALA A  1  59  ? 30.358 6.479   -11.333 1.00 24.06  ?  91  ALA A CA    1 
ATOM   443   C  C     . ALA A  1  59  ? 31.478 5.501   -11.661 1.00 23.98  ?  91  ALA A C     1 
ATOM   444   O  O     . ALA A  1  59  ? 32.371 5.279   -10.832 1.00 24.03  ?  91  ALA A O     1 
ATOM   445   C  CB    . ALA A  1  59  ? 29.056 5.746   -11.072 1.00 24.68  ?  91  ALA A CB    1 
ATOM   446   N  N     . PHE A  1  60  ? 31.440 4.917   -12.852 1.00 24.34  ?  92  PHE A N     1 
ATOM   447   C  CA    . PHE A  1  60  ? 32.543 4.030   -13.265 1.00 26.14  ?  92  PHE A CA    1 
ATOM   448   C  C     . PHE A  1  60  ? 33.897 4.753   -13.448 1.00 28.28  ?  92  PHE A C     1 
ATOM   449   O  O     . PHE A  1  60  ? 34.957 4.128   -13.308 1.00 28.74  ?  92  PHE A O     1 
ATOM   450   C  CB    . PHE A  1  60  ? 32.215 3.296   -14.557 1.00 24.70  ?  92  PHE A CB    1 
ATOM   451   C  CG    . PHE A  1  60  ? 31.198 2.224   -14.399 1.00 24.01  ?  92  PHE A CG    1 
ATOM   452   C  CD1   . PHE A  1  60  ? 31.419 1.168   -13.550 1.00 24.00  ?  92  PHE A CD1   1 
ATOM   453   C  CD2   . PHE A  1  60  ? 30.031 2.257   -15.123 1.00 24.15  ?  92  PHE A CD2   1 
ATOM   454   C  CE1   . PHE A  1  60  ? 30.486 0.159   -13.408 1.00 24.16  ?  92  PHE A CE1   1 
ATOM   455   C  CE2   . PHE A  1  60  ? 29.099 1.252   -14.999 1.00 24.12  ?  92  PHE A CE2   1 
ATOM   456   C  CZ    . PHE A  1  60  ? 29.325 0.197   -14.142 1.00 24.15  ?  92  PHE A CZ    1 
ATOM   457   N  N     . ASP A  1  61  ? 33.862 6.042   -13.788 1.00 28.90  ?  93  ASP A N     1 
ATOM   458   C  CA    . ASP A  1  61  ? 35.082 6.781   -13.982 1.00 30.37  ?  93  ASP A CA    1 
ATOM   459   C  C     . ASP A  1  61  ? 35.711 6.972   -12.636 1.00 32.26  ?  93  ASP A C     1 
ATOM   460   O  O     . ASP A  1  61  ? 36.913 6.788   -12.500 1.00 37.70  ?  93  ASP A O     1 
ATOM   461   C  CB    . ASP A  1  61  ? 34.841 8.133   -14.645 1.00 31.51  ?  93  ASP A CB    1 
ATOM   462   C  CG    . ASP A  1  61  ? 34.663 8.029   -16.140 1.00 32.11  ?  93  ASP A CG    1 
ATOM   463   O  OD1   . ASP A  1  61  ? 35.243 7.090   -16.743 1.00 32.24  ?  93  ASP A OD1   1 
ATOM   464   O  OD2   . ASP A  1  61  ? 33.948 8.897   -16.700 1.00 32.49  -1 93  ASP A OD2   1 
ATOM   465   N  N     . PHE A  1  62  ? 34.915 7.334   -11.634 1.00 32.03  ?  94  PHE A N     1 
ATOM   466   C  CA    . PHE A  1  62  ? 35.435 7.424   -10.276 1.00 30.57  ?  94  PHE A CA    1 
ATOM   467   C  C     . PHE A  1  62  ? 36.069 6.102   -9.850  1.00 28.91  ?  94  PHE A C     1 
ATOM   468   O  O     . PHE A  1  62  ? 37.110 6.105   -9.231  1.00 29.44  ?  94  PHE A O     1 
ATOM   469   C  CB    . PHE A  1  62  ? 34.350 7.817   -9.292  1.00 30.54  ?  94  PHE A CB    1 
ATOM   470   C  CG    . PHE A  1  62  ? 34.767 7.695   -7.857  1.00 32.44  ?  94  PHE A CG    1 
ATOM   471   C  CD1   . PHE A  1  62  ? 35.480 8.715   -7.229  1.00 34.19  ?  94  PHE A CD1   1 
ATOM   472   C  CD2   . PHE A  1  62  ? 34.455 6.559   -7.120  1.00 34.06  ?  94  PHE A CD2   1 
ATOM   473   C  CE1   . PHE A  1  62  ? 35.858 8.608   -5.890  1.00 34.27  ?  94  PHE A CE1   1 
ATOM   474   C  CE2   . PHE A  1  62  ? 34.835 6.437   -5.781  1.00 34.49  ?  94  PHE A CE2   1 
ATOM   475   C  CZ    . PHE A  1  62  ? 35.532 7.468   -5.165  1.00 34.60  ?  94  PHE A CZ    1 
ATOM   476   N  N     . ILE A  1  63  ? 35.466 4.971   -10.169 1.00 27.75  ?  95  ILE A N     1 
ATOM   477   C  CA    . ILE A  1  63  ? 36.075 3.734   -9.755  1.00 29.65  ?  95  ILE A CA    1 
ATOM   478   C  C     . ILE A  1  63  ? 37.451 3.609   -10.374 1.00 33.57  ?  95  ILE A C     1 
ATOM   479   O  O     . ILE A  1  63  ? 38.423 3.385   -9.674  1.00 36.35  ?  95  ILE A O     1 
ATOM   480   C  CB    . ILE A  1  63  ? 35.236 2.503   -10.092 1.00 28.79  ?  95  ILE A CB    1 
ATOM   481   C  CG1   . ILE A  1  63  ? 34.062 2.402   -9.102  1.00 29.03  ?  95  ILE A CG1   1 
ATOM   482   C  CG2   . ILE A  1  63  ? 36.112 1.255   -10.015 1.00 27.77  ?  95  ILE A CG2   1 
ATOM   483   C  CD1   . ILE A  1  63  ? 32.975 1.397   -9.448  1.00 27.94  ?  95  ILE A CD1   1 
ATOM   484   N  N     . LYS A  1  64  ? 37.535 3.757   -11.686 1.00 39.22  ?  96  LYS A N     1 
ATOM   485   C  CA    . LYS A  1  64  ? 38.814 3.653   -12.412 1.00 41.69  ?  96  LYS A CA    1 
ATOM   486   C  C     . LYS A  1  64  ? 39.849 4.659   -11.852 1.00 39.63  ?  96  LYS A C     1 
ATOM   487   O  O     . LYS A  1  64  ? 40.946 4.284   -11.513 1.00 36.00  ?  96  LYS A O     1 
ATOM   488   C  CB    . LYS A  1  64  ? 38.541 3.815   -13.920 1.00 46.76  ?  96  LYS A CB    1 
ATOM   489   C  CG    . LYS A  1  64  ? 39.714 4.176   -14.824 1.00 53.43  ?  96  LYS A CG    1 
ATOM   490   C  CD    . LYS A  1  64  ? 39.423 5.464   -15.618 1.00 57.34  ?  96  LYS A CD    1 
ATOM   491   C  CE    . LYS A  1  64  ? 38.672 5.226   -16.925 1.00 58.03  ?  96  LYS A CE    1 
ATOM   492   N  NZ    . LYS A  1  64  ? 39.519 5.402   -18.138 1.00 57.60  1  96  LYS A NZ    1 
ATOM   493   N  N     . ASN A  1  65  ? 39.471 5.915   -11.688 1.00 42.34  ?  97  ASN A N     1 
ATOM   494   C  CA    . ASN A  1  65  ? 40.332 6.922   -11.043 1.00 47.04  ?  97  ASN A CA    1 
ATOM   495   C  C     . ASN A  1  65  ? 40.400 6.838   -9.516  1.00 48.66  ?  97  ASN A C     1 
ATOM   496   O  O     . ASN A  1  65  ? 40.936 7.749   -8.880  1.00 52.10  ?  97  ASN A O     1 
ATOM   497   C  CB    . ASN A  1  65  ? 39.822 8.340   -11.361 1.00 50.22  ?  97  ASN A CB    1 
ATOM   498   C  CG    . ASN A  1  65  ? 40.121 8.787   -12.777 1.00 52.78  ?  97  ASN A CG    1 
ATOM   499   O  OD1   . ASN A  1  65  ? 40.177 9.991   -13.033 1.00 54.70  ?  97  ASN A OD1   1 
ATOM   500   N  ND2   . ASN A  1  65  ? 40.294 7.843   -13.707 1.00 54.36  ?  97  ASN A ND2   1 
ATOM   501   N  N     . SER A  1  66  ? 39.849 5.786   -8.915  1.00 48.30  ?  98  SER A N     1 
ATOM   502   C  CA    . SER A  1  66  ? 39.633 5.785   -7.464  1.00 45.48  ?  98  SER A CA    1 
ATOM   503   C  C     . SER A  1  66  ? 40.941 5.778   -6.709  1.00 44.06  ?  98  SER A C     1 
ATOM   504   O  O     . SER A  1  66  ? 41.108 6.492   -5.729  1.00 47.80  ?  98  SER A O     1 
ATOM   505   C  CB    . SER A  1  66  ? 38.806 4.574   -7.016  1.00 43.28  ?  98  SER A CB    1 
ATOM   506   O  OG    . SER A  1  66  ? 39.576 3.385   -7.009  1.00 42.08  ?  98  SER A OG    1 
ATOM   507   N  N     . GLY A  1  67  ? 41.869 4.966   -7.177  1.00 42.19  ?  99  GLY A N     1 
ATOM   508   C  CA    . GLY A  1  67  ? 43.072 4.696   -6.424  1.00 43.04  ?  99  GLY A CA    1 
ATOM   509   C  C     . GLY A  1  67  ? 42.809 3.620   -5.402  1.00 41.09  ?  99  GLY A C     1 
ATOM   510   O  O     . GLY A  1  67  ? 43.336 3.672   -4.297  1.00 47.84  ?  99  GLY A O     1 
ATOM   511   N  N     . GLN A  1  68  ? 41.957 2.675   -5.772  1.00 38.39  ?  100 GLN A N     1 
ATOM   512   C  CA    . GLN A  1  68  ? 41.704 1.479   -5.000  1.00 36.81  ?  100 GLN A CA    1 
ATOM   513   C  C     . GLN A  1  68  ? 41.931 0.381   -5.992  1.00 36.98  ?  100 GLN A C     1 
ATOM   514   O  O     . GLN A  1  68  ? 41.682 0.584   -7.158  1.00 37.55  ?  100 GLN A O     1 
ATOM   515   C  CB    . GLN A  1  68  ? 40.247 1.436   -4.526  1.00 35.97  ?  100 GLN A CB    1 
ATOM   516   C  CG    . GLN A  1  68  ? 39.825 2.564   -3.577  1.00 35.12  ?  100 GLN A CG    1 
ATOM   517   C  CD    . GLN A  1  68  ? 40.053 2.264   -2.087  1.00 33.54  ?  100 GLN A CD    1 
ATOM   518   O  OE1   . GLN A  1  68  ? 40.595 1.212   -1.714  1.00 30.61  ?  100 GLN A OE1   1 
ATOM   519   N  NE2   . GLN A  1  68  ? 39.625 3.200   -1.225  1.00 32.08  ?  100 GLN A NE2   1 
ATOM   520   N  N     . GLU A  1  69  ? 42.411 -0.766  -5.552  1.00 39.58  ?  101 GLU A N     1 
ATOM   521   C  CA    . GLU A  1  69  ? 42.545 -1.912  -6.437  1.00 45.94  ?  101 GLU A CA    1 
ATOM   522   C  C     . GLU A  1  69  ? 41.473 -2.930  -6.062  1.00 41.39  ?  101 GLU A C     1 
ATOM   523   O  O     . GLU A  1  69  ? 41.058 -2.984  -4.914  1.00 43.22  ?  101 GLU A O     1 
ATOM   524   C  CB    . GLU A  1  69  ? 43.961 -2.510  -6.330  1.00 57.84  ?  101 GLU A CB    1 
ATOM   525   C  CG    . GLU A  1  69  ? 44.144 -3.725  -5.395  1.00 70.71  ?  101 GLU A CG    1 
ATOM   526   C  CD    . GLU A  1  69  ? 43.982 -3.424  -3.899  1.00 80.95  ?  101 GLU A CD    1 
ATOM   527   O  OE1   . GLU A  1  69  ? 44.230 -2.264  -3.481  1.00 86.07  ?  101 GLU A OE1   1 
ATOM   528   O  OE2   . GLU A  1  69  ? 43.614 -4.361  -3.135  1.00 86.74  -1 101 GLU A OE2   1 
ATOM   529   N  N     . ALA A  1  70  ? 41.021 -3.751  -6.996  1.00 35.39  ?  102 ALA A N     1 
ATOM   530   C  CA    . ALA A  1  70  ? 39.976 -4.695  -6.640  1.00 33.30  ?  102 ALA A CA    1 
ATOM   531   C  C     . ALA A  1  70  ? 40.071 -5.991  -7.405  1.00 31.30  ?  102 ALA A C     1 
ATOM   532   O  O     . ALA A  1  70  ? 40.259 -5.995  -8.598  1.00 32.92  ?  102 ALA A O     1 
ATOM   533   C  CB    . ALA A  1  70  ? 38.603 -4.063  -6.846  1.00 32.65  ?  102 ALA A CB    1 
ATOM   534   N  N     . SER A  1  71  ? 39.903 -7.099  -6.712  1.00 29.42  ?  103 SER A N     1 
ATOM   535   C  CA    . SER A  1  71  ? 39.927 -8.390  -7.350  1.00 28.31  ?  103 SER A CA    1 
ATOM   536   C  C     . SER A  1  71  ? 38.725 -8.632  -8.232  1.00 27.29  ?  103 SER A C     1 
ATOM   537   O  O     . SER A  1  71  ? 38.850 -9.313  -9.235  1.00 29.17  ?  103 SER A O     1 
ATOM   538   C  CB    . SER A  1  71  ? 40.016 -9.456  -6.290  1.00 29.31  ?  103 SER A CB    1 
ATOM   539   O  OG    . SER A  1  71  ? 41.137 -9.158  -5.476  1.00 31.47  ?  103 SER A OG    1 
ATOM   540   N  N     . PHE A  1  72  ? 37.564 -8.088  -7.870  1.00 26.18  ?  104 PHE A N     1 
ATOM   541   C  CA    . PHE A  1  72  ? 36.379 -8.172  -8.741  1.00 24.32  ?  104 PHE A CA    1 
ATOM   542   C  C     . PHE A  1  72  ? 35.311 -7.103  -8.517  1.00 23.13  ?  104 PHE A C     1 
ATOM   543   O  O     . PHE A  1  72  ? 35.560 -6.055  -7.911  1.00 22.34  ?  104 PHE A O     1 
ATOM   544   C  CB    . PHE A  1  72  ? 35.765 -9.561  -8.670  1.00 23.75  ?  104 PHE A CB    1 
ATOM   545   C  CG    . PHE A  1  72  ? 35.322 -9.949  -7.323  1.00 23.82  ?  104 PHE A CG    1 
ATOM   546   C  CD1   . PHE A  1  72  ? 36.228 -10.434 -6.409  1.00 24.02  ?  104 PHE A CD1   1 
ATOM   547   C  CD2   . PHE A  1  72  ? 33.998 -9.865  -6.969  1.00 24.71  ?  104 PHE A CD2   1 
ATOM   548   C  CE1   . PHE A  1  72  ? 35.823 -10.818 -5.144  1.00 23.72  ?  104 PHE A CE1   1 
ATOM   549   C  CE2   . PHE A  1  72  ? 33.581 -10.257 -5.706  1.00 24.63  ?  104 PHE A CE2   1 
ATOM   550   C  CZ    . PHE A  1  72  ? 34.499 -10.728 -4.792  1.00 23.87  ?  104 PHE A CZ    1 
ATOM   551   N  N     . MET A  1  73  ? 34.147 -7.349  -9.106  1.00 22.66  ?  105 MET A N     1 
ATOM   552   C  CA    . MET A  1  73  ? 32.999 -6.467  -8.994  1.00 22.28  ?  105 MET A CA    1 
ATOM   553   C  C     . MET A  1  73  ? 31.750 -7.309  -9.061  1.00 20.67  ?  105 MET A C     1 
ATOM   554   O  O     . MET A  1  73  ? 31.685 -8.306  -9.762  1.00 20.23  ?  105 MET A O     1 
ATOM   555   C  CB    . MET A  1  73  ? 32.985 -5.422  -10.116 1.00 22.84  ?  105 MET A CB    1 
ATOM   556   C  CG    . MET A  1  73  ? 31.803 -4.451  -10.112 1.00 23.67  ?  105 MET A CG    1 
ATOM   557   S  SD    . MET A  1  73  ? 31.820 -3.294  -11.513 1.00 25.70  ?  105 MET A SD    1 
ATOM   558   C  CE    . MET A  1  73  ? 32.974 -2.048  -10.962 1.00 25.93  ?  105 MET A CE    1 
ATOM   559   N  N     . ILE A  1  74  ? 30.774 -6.889  -8.284  1.00 19.96  ?  106 ILE A N     1 
ATOM   560   C  CA    A ILE A  1  74  ? 29.471 -7.511  -8.202  0.50 19.98  ?  106 ILE A CA    1 
ATOM   561   C  CA    B ILE A  1  74  ? 29.483 -7.547  -8.288  0.50 19.66  ?  106 ILE A CA    1 
ATOM   562   C  C     . ILE A  1  74  ? 28.466 -6.546  -8.823  1.00 20.07  ?  106 ILE A C     1 
ATOM   563   O  O     . ILE A  1  74  ? 28.470 -5.356  -8.464  1.00 20.17  ?  106 ILE A O     1 
ATOM   564   C  CB    A ILE A  1  74  ? 29.133 -7.725  -6.717  0.50 19.92  ?  106 ILE A CB    1 
ATOM   565   C  CB    B ILE A  1  74  ? 29.086 -8.113  -6.902  0.50 19.15  ?  106 ILE A CB    1 
ATOM   566   C  CG1   A ILE A  1  74  ? 29.959 -8.871  -6.172  0.50 19.70  ?  106 ILE A CG1   1 
ATOM   567   C  CG1   B ILE A  1  74  ? 29.154 -7.055  -5.798  0.50 19.01  ?  106 ILE A CG1   1 
ATOM   568   C  CG2   A ILE A  1  74  ? 27.657 -7.994  -6.511  0.50 20.10  ?  106 ILE A CG2   1 
ATOM   569   C  CG2   B ILE A  1  74  ? 29.993 -9.261  -6.519  0.50 18.93  ?  106 ILE A CG2   1 
ATOM   570   C  CD1   A ILE A  1  74  ? 30.072 -9.989  -7.170  0.50 19.91  ?  106 ILE A CD1   1 
ATOM   571   C  CD1   B ILE A  1  74  ? 28.387 -7.450  -4.558  0.50 18.88  ?  106 ILE A CD1   1 
ATOM   572   N  N     . TRP A  1  75  ? 27.605 -7.020  -9.716  1.00 20.09  ?  107 TRP A N     1 
ATOM   573   C  CA    . TRP A  1  75  ? 26.665 -6.123  -10.361 1.00 21.36  ?  107 TRP A CA    1 
ATOM   574   C  C     . TRP A  1  75  ? 25.260 -6.676  -10.295 1.00 20.75  ?  107 TRP A C     1 
ATOM   575   O  O     . TRP A  1  75  ? 24.922 -7.579  -11.035 1.00 21.18  ?  107 TRP A O     1 
ATOM   576   C  CB    . TRP A  1  75  ? 27.103 -5.938  -11.791 1.00 23.15  ?  107 TRP A CB    1 
ATOM   577   C  CG    . TRP A  1  75  ? 26.219 -5.095  -12.608 1.00 25.71  ?  107 TRP A CG    1 
ATOM   578   C  CD1   . TRP A  1  75  ? 25.399 -4.101  -12.175 1.00 27.04  ?  107 TRP A CD1   1 
ATOM   579   C  CD2   . TRP A  1  75  ? 26.112 -5.115  -14.040 1.00 27.41  ?  107 TRP A CD2   1 
ATOM   580   N  NE1   . TRP A  1  75  ? 24.752 -3.516  -13.251 1.00 28.52  ?  107 TRP A NE1   1 
ATOM   581   C  CE2   . TRP A  1  75  ? 25.183 -4.118  -14.407 1.00 27.78  ?  107 TRP A CE2   1 
ATOM   582   C  CE3   . TRP A  1  75  ? 26.716 -5.877  -15.047 1.00 27.98  ?  107 TRP A CE3   1 
ATOM   583   C  CZ2   . TRP A  1  75  ? 24.836 -3.869  -15.741 1.00 27.35  ?  107 TRP A CZ2   1 
ATOM   584   C  CZ3   . TRP A  1  75  ? 26.359 -5.632  -16.371 1.00 28.32  ?  107 TRP A CZ3   1 
ATOM   585   C  CH2   . TRP A  1  75  ? 25.429 -4.631  -16.701 1.00 27.45  ?  107 TRP A CH2   1 
ATOM   586   N  N     . THR A  1  76  ? 24.416 -6.124  -9.432  1.00 20.40  ?  108 THR A N     1 
ATOM   587   C  CA    . THR A  1  76  ? 23.141 -6.796  -9.135  1.00 20.40  ?  108 THR A CA    1 
ATOM   588   C  C     . THR A  1  76  ? 21.917 -6.340  -9.946  1.00 20.38  ?  108 THR A C     1 
ATOM   589   O  O     . THR A  1  76  ? 20.788 -6.534  -9.504  1.00 21.25  ?  108 THR A O     1 
ATOM   590   C  CB    . THR A  1  76  ? 22.804 -6.718  -7.637  1.00 19.82  ?  108 THR A CB    1 
ATOM   591   O  OG1   . THR A  1  76  ? 22.888 -5.366  -7.214  1.00 19.16  ?  108 THR A OG1   1 
ATOM   592   C  CG2   . THR A  1  76  ? 23.773 -7.535  -6.846  1.00 19.80  ?  108 THR A CG2   1 
ATOM   593   N  N     . GLY A  1  77  ? 22.134 -5.756  -11.121 1.00 19.84  ?  109 GLY A N     1 
ATOM   594   C  CA    . GLY A  1  77  ? 21.099 -5.692  -12.142 1.00 19.20  ?  109 GLY A CA    1 
ATOM   595   C  C     . GLY A  1  77  ? 20.301 -4.410  -12.187 1.00 18.39  ?  109 GLY A C     1 
ATOM   596   O  O     . GLY A  1  77  ? 20.799 -3.361  -11.781 1.00 18.74  ?  109 GLY A O     1 
ATOM   597   N  N     . ASP A  1  78  ? 19.061 -4.526  -12.699 1.00 17.33  ?  110 ASP A N     1 
ATOM   598   C  CA    . ASP A  1  78  ? 18.124 -3.398  -12.962 1.00 16.41  ?  110 ASP A CA    1 
ATOM   599   C  C     . ASP A  1  78  ? 18.738 -2.277  -13.795 1.00 15.64  ?  110 ASP A C     1 
ATOM   600   O  O     . ASP A  1  78  ? 19.078 -1.209  -13.265 1.00 14.97  ?  110 ASP A O     1 
ATOM   601   C  CB    . ASP A  1  78  ? 17.546 -2.827  -11.649 1.00 16.45  ?  110 ASP A CB    1 
ATOM   602   C  CG    . ASP A  1  78  ? 16.234 -3.504  -11.215 1.00 15.91  ?  110 ASP A CG    1 
ATOM   603   O  OD1   . ASP A  1  78  ? 15.879 -4.572  -11.763 1.00 15.17  ?  110 ASP A OD1   1 
ATOM   604   O  OD2   . ASP A  1  78  ? 15.587 -2.968  -10.288 1.00 15.43  -1 110 ASP A OD2   1 
ATOM   605   N  N     . SER A  1  79  ? 18.880 -2.537  -15.094 1.00 15.28  ?  111 SER A N     1 
ATOM   606   C  CA    . SER A  1  79  ? 19.556 -1.601  -16.000 1.00 15.37  ?  111 SER A CA    1 
ATOM   607   C  C     . SER A  1  79  ? 18.634 -0.741  -16.846 1.00 14.96  ?  111 SER A C     1 
ATOM   608   O  O     . SER A  1  79  ? 18.914 0.448   -17.053 1.00 15.21  ?  111 SER A O     1 
ATOM   609   C  CB    . SER A  1  79  ? 20.549 -2.347  -16.878 1.00 15.72  ?  111 SER A CB    1 
ATOM   610   O  OG    . SER A  1  79  ? 21.583 -2.891  -16.080 1.00 16.74  ?  111 SER A OG    1 
ATOM   611   N  N     . PRO A  1  80  ? 17.539 -1.328  -17.354 1.00 14.82  ?  112 PRO A N     1 
ATOM   612   C  CA    . PRO A  1  80  ? 16.525 -0.513  -18.018 1.00 14.68  ?  112 PRO A CA    1 
ATOM   613   C  C     . PRO A  1  80  ? 15.792 0.423   -17.066 1.00 14.61  ?  112 PRO A C     1 
ATOM   614   O  O     . PRO A  1  80  ? 15.587 0.078   -15.909 1.00 14.37  ?  112 PRO A O     1 
ATOM   615   C  CB    . PRO A  1  80  ? 15.531 -1.548  -18.519 1.00 14.67  ?  112 PRO A CB    1 
ATOM   616   C  CG    . PRO A  1  80  ? 16.336 -2.777  -18.665 1.00 14.84  ?  112 PRO A CG    1 
ATOM   617   C  CD    . PRO A  1  80  ? 17.225 -2.760  -17.478 1.00 14.89  ?  112 PRO A CD    1 
ATOM   618   N  N     . PRO A  1  81  ? 15.325 1.564   -17.574 1.00 14.53  ?  113 PRO A N     1 
ATOM   619   C  CA    . PRO A  1  81  ? 14.648 2.545   -16.749 1.00 14.46  ?  113 PRO A CA    1 
ATOM   620   C  C     . PRO A  1  81  ? 13.183 2.213   -16.430 1.00 14.59  ?  113 PRO A C     1 
ATOM   621   O  O     . PRO A  1  81  ? 12.610 1.220   -16.922 1.00 14.53  ?  113 PRO A O     1 
ATOM   622   C  CB    . PRO A  1  81  ? 14.697 3.797   -17.615 1.00 14.63  ?  113 PRO A CB    1 
ATOM   623   C  CG    . PRO A  1  81  ? 14.667 3.269   -19.019 1.00 14.77  ?  113 PRO A CG    1 
ATOM   624   C  CD    . PRO A  1  81  ? 15.121 1.834   -19.006 1.00 14.44  ?  113 PRO A CD    1 
ATOM   625   N  N     . HIS A  1  82  ? 12.612 3.074   -15.592 1.00 14.60  ?  114 HIS A N     1 
ATOM   626   C  CA    . HIS A  1  82  ? 11.242 2.980   -15.122 1.00 14.57  ?  114 HIS A CA    1 
ATOM   627   C  C     . HIS A  1  82  ? 10.358 3.794   -16.057 1.00 14.66  ?  114 HIS A C     1 
ATOM   628   O  O     . HIS A  1  82  ? 10.178 5.018   -15.910 1.00 13.50  ?  114 HIS A O     1 
ATOM   629   C  CB    . HIS A  1  82  ? 11.113 3.531   -13.694 1.00 14.95  ?  114 HIS A CB    1 
ATOM   630   C  CG    . HIS A  1  82  ? 11.901 2.780   -12.677 1.00 14.90  ?  114 HIS A CG    1 
ATOM   631   N  ND1   . HIS A  1  82  ? 13.242 3.006   -12.465 1.00 15.35  ?  114 HIS A ND1   1 
ATOM   632   C  CD2   . HIS A  1  82  ? 11.541 1.794   -11.818 1.00 15.16  ?  114 HIS A CD2   1 
ATOM   633   C  CE1   . HIS A  1  82  ? 13.679 2.182   -11.525 1.00 15.72  ?  114 HIS A CE1   1 
ATOM   634   N  NE2   . HIS A  1  82  ? 12.661 1.444   -11.108 1.00 15.38  ?  114 HIS A NE2   1 
ATOM   635   N  N     . VAL A  1  83  ? 9.833  3.081   -17.041 1.00 15.47  ?  115 VAL A N     1 
ATOM   636   C  CA    . VAL A  1  83  ? 8.818  3.586   -17.940 1.00 15.93  ?  115 VAL A CA    1 
ATOM   637   C  C     . VAL A  1  83  ? 7.843  2.429   -18.171 1.00 17.11  ?  115 VAL A C     1 
ATOM   638   O  O     . VAL A  1  83  ? 8.187  1.246   -17.964 1.00 17.23  ?  115 VAL A O     1 
ATOM   639   C  CB    . VAL A  1  83  ? 9.435  4.074   -19.266 1.00 15.47  ?  115 VAL A CB    1 
ATOM   640   C  CG1   . VAL A  1  83  ? 10.478 5.168   -19.040 1.00 15.20  ?  115 VAL A CG1   1 
ATOM   641   C  CG2   . VAL A  1  83  ? 10.103 2.932   -19.959 1.00 15.77  ?  115 VAL A CG2   1 
ATOM   642   N  N     . PRO A  1  84  ? 6.621  2.746   -18.587 1.00 18.93  ?  116 PRO A N     1 
ATOM   643   C  CA    . PRO A  1  84  ? 5.601  1.709   -18.753 1.00 19.71  ?  116 PRO A CA    1 
ATOM   644   C  C     . PRO A  1  84  ? 5.922  0.751   -19.875 1.00 20.95  ?  116 PRO A C     1 
ATOM   645   O  O     . PRO A  1  84  ? 6.596  1.136   -20.856 1.00 19.77  ?  116 PRO A O     1 
ATOM   646   C  CB    . PRO A  1  84  ? 4.351  2.487   -19.115 1.00 19.86  ?  116 PRO A CB    1 
ATOM   647   C  CG    . PRO A  1  84  ? 4.656  3.925   -18.838 1.00 20.10  ?  116 PRO A CG    1 
ATOM   648   C  CD    . PRO A  1  84  ? 6.135  4.073   -18.980 1.00 19.71  ?  116 PRO A CD    1 
ATOM   649   N  N     . VAL A  1  85  ? 5.412  -0.474  -19.713 1.00 22.94  ?  117 VAL A N     1 
ATOM   650   C  CA    . VAL A  1  85  ? 5.723  -1.620  -20.590 1.00 24.75  ?  117 VAL A CA    1 
ATOM   651   C  C     . VAL A  1  85  ? 5.624  -1.329  -22.081 1.00 25.94  ?  117 VAL A C     1 
ATOM   652   O  O     . VAL A  1  85  ? 6.590  -1.561  -22.806 1.00 25.05  ?  117 VAL A O     1 
ATOM   653   C  CB    . VAL A  1  85  ? 4.821  -2.829  -20.317 1.00 25.70  ?  117 VAL A CB    1 
ATOM   654   C  CG1   . VAL A  1  85  ? 5.159  -3.945  -21.291 1.00 26.77  ?  117 VAL A CG1   1 
ATOM   655   C  CG2   . VAL A  1  85  ? 4.980  -3.314  -18.884 1.00 26.77  ?  117 VAL A CG2   1 
ATOM   656   N  N     . PRO A  1  86  ? 4.462  -0.821  -22.544 1.00 28.78  ?  118 PRO A N     1 
ATOM   657   C  CA    . PRO A  1  86  ? 4.306  -0.502  -23.973 1.00 29.60  ?  118 PRO A CA    1 
ATOM   658   C  C     . PRO A  1  86  ? 5.392  0.401   -24.501 1.00 29.63  ?  118 PRO A C     1 
ATOM   659   O  O     . PRO A  1  86  ? 5.837  0.217   -25.607 1.00 29.69  ?  118 PRO A O     1 
ATOM   660   C  CB    . PRO A  1  86  ? 2.965  0.227   -24.048 1.00 30.43  ?  118 PRO A CB    1 
ATOM   661   C  CG    . PRO A  1  86  ? 2.270  -0.020  -22.743 1.00 30.22  ?  118 PRO A CG    1 
ATOM   662   C  CD    . PRO A  1  86  ? 3.327  -0.324  -21.738 1.00 29.89  ?  118 PRO A CD    1 
ATOM   663   N  N     . GLU A  1  87  ? 5.838  1.362   -23.710 1.00 32.38  ?  119 GLU A N     1 
ATOM   664   C  CA    . GLU A  1  87  ? 6.981  2.181   -24.123 1.00 33.72  ?  119 GLU A CA    1 
ATOM   665   C  C     . GLU A  1  87  ? 8.298  1.421   -24.295 1.00 29.66  ?  119 GLU A C     1 
ATOM   666   O  O     . GLU A  1  87  ? 9.238  1.964   -24.841 1.00 27.84  ?  119 GLU A O     1 
ATOM   667   C  CB    . GLU A  1  87  ? 7.192  3.349   -23.163 1.00 38.03  ?  119 GLU A CB    1 
ATOM   668   C  CG    . GLU A  1  87  ? 6.659  4.659   -23.710 1.00 43.55  ?  119 GLU A CG    1 
ATOM   669   C  CD    . GLU A  1  87  ? 7.260  5.854   -22.992 1.00 48.33  ?  119 GLU A CD    1 
ATOM   670   O  OE1   . GLU A  1  87  ? 8.124  6.550   -23.616 1.00 52.17  ?  119 GLU A OE1   1 
ATOM   671   O  OE2   . GLU A  1  87  ? 6.876  6.071   -21.808 1.00 45.22  -1 119 GLU A OE2   1 
ATOM   672   N  N     . LEU A  1  88  ? 8.372  0.178   -23.850 1.00 27.54  ?  120 LEU A N     1 
ATOM   673   C  CA    . LEU A  1  88  ? 9.613  -0.584  -23.949 1.00 27.98  ?  120 LEU A CA    1 
ATOM   674   C  C     . LEU A  1  88  ? 9.506  -1.900  -24.731 1.00 26.06  ?  120 LEU A C     1 
ATOM   675   O  O     . LEU A  1  88  ? 8.428  -2.302  -25.120 1.00 27.67  ?  120 LEU A O     1 
ATOM   676   C  CB    . LEU A  1  88  ? 10.067 -0.926  -22.541 1.00 29.33  ?  120 LEU A CB    1 
ATOM   677   C  CG    . LEU A  1  88  ? 10.743 0.152   -21.728 1.00 28.64  ?  120 LEU A CG    1 
ATOM   678   C  CD1   . LEU A  1  88  ? 11.085 -0.500  -20.399 1.00 29.36  ?  120 LEU A CD1   1 
ATOM   679   C  CD2   . LEU A  1  88  ? 11.988 0.702   -22.423 1.00 28.67  ?  120 LEU A CD2   1 
ATOM   680   N  N     . SER A  1  89  ? 10.615 -2.599  -24.901 1.00 23.41  ?  121 SER A N     1 
ATOM   681   C  CA    . SER A  1  89  ? 10.567 -3.893  -25.522 1.00 23.50  ?  121 SER A CA    1 
ATOM   682   C  C     . SER A  1  89  ? 11.754 -4.737  -25.128 1.00 23.92  ?  121 SER A C     1 
ATOM   683   O  O     . SER A  1  89  ? 12.774 -4.205  -24.667 1.00 24.27  ?  121 SER A O     1 
ATOM   684   C  CB    . SER A  1  89  ? 10.614 -3.719  -27.026 1.00 23.91  ?  121 SER A CB    1 
ATOM   685   O  OG    . SER A  1  89  ? 11.943 -3.505  -27.477 1.00 23.19  ?  121 SER A OG    1 
ATOM   686   N  N     . THR A  1  90  ? 11.644 -6.041  -25.383 1.00 22.94  ?  122 THR A N     1 
ATOM   687   C  CA    . THR A  1  90  ? 12.774 -6.963  -25.240 1.00 22.22  ?  122 THR A CA    1 
ATOM   688   C  C     . THR A  1  90  ? 14.047 -6.453  -25.920 1.00 25.10  ?  122 THR A C     1 
ATOM   689   O  O     . THR A  1  90  ? 15.148 -6.562  -25.383 1.00 27.94  ?  122 THR A O     1 
ATOM   690   C  CB    . THR A  1  90  ? 12.425 -8.333  -25.816 1.00 20.53  ?  122 THR A CB    1 
ATOM   691   O  OG1   . THR A  1  90  ? 11.388 -8.906  -25.034 1.00 20.01  ?  122 THR A OG1   1 
ATOM   692   C  CG2   . THR A  1  90  ? 13.585 -9.260  -25.786 1.00 20.07  ?  122 THR A CG2   1 
ATOM   693   N  N     . ASP A  1  91  ? 13.923 -5.885  -27.103 1.00 28.01  ?  123 ASP A N     1 
ATOM   694   C  CA    . ASP A  1  91  ? 15.129 -5.466  -27.810 1.00 29.82  ?  123 ASP A CA    1 
ATOM   695   C  C     . ASP A  1  91  ? 15.740 -4.238  -27.148 1.00 28.32  ?  123 ASP A C     1 
ATOM   696   O  O     . ASP A  1  91  ? 16.950 -4.122  -27.107 1.00 28.28  ?  123 ASP A O     1 
ATOM   697   C  CB    . ASP A  1  91  ? 14.867 -5.266  -29.319 1.00 32.23  ?  123 ASP A CB    1 
ATOM   698   C  CG    . ASP A  1  91  ? 14.806 -6.614  -30.111 1.00 33.06  ?  123 ASP A CG    1 
ATOM   699   O  OD1   . ASP A  1  91  ? 14.272 -7.668  -29.638 1.00 32.71  ?  123 ASP A OD1   1 
ATOM   700   O  OD2   . ASP A  1  91  ? 15.300 -6.600  -31.250 1.00 34.65  -1 123 ASP A OD2   1 
ATOM   701   N  N     . THR A  1  92  ? 14.920 -3.354  -26.591 1.00 27.71  ?  124 THR A N     1 
ATOM   702   C  CA    . THR A  1  92  ? 15.451 -2.182  -25.899 1.00 29.17  ?  124 THR A CA    1 
ATOM   703   C  C     . THR A  1  92  ? 16.138 -2.601  -24.604 1.00 29.92  ?  124 THR A C     1 
ATOM   704   O  O     . THR A  1  92  ? 17.227 -2.097  -24.248 1.00 30.45  ?  124 THR A O     1 
ATOM   705   C  CB    . THR A  1  92  ? 14.354 -1.202  -25.490 1.00 29.51  ?  124 THR A CB    1 
ATOM   706   O  OG1   . THR A  1  92  ? 13.196 -1.437  -26.278 1.00 32.50  ?  124 THR A OG1   1 
ATOM   707   C  CG2   . THR A  1  92  ? 14.811 0.213   -25.687 1.00 30.06  ?  124 THR A CG2   1 
ATOM   708   N  N     . VAL A  1  93  ? 15.480 -3.498  -23.879 1.00 28.02  ?  125 VAL A N     1 
ATOM   709   C  CA    . VAL A  1  93  ? 16.062 -4.040  -22.676 1.00 26.67  ?  125 VAL A CA    1 
ATOM   710   C  C     . VAL A  1  93  ? 17.495 -4.496  -23.009 1.00 27.26  ?  125 VAL A C     1 
ATOM   711   O  O     . VAL A  1  93  ? 18.471 -4.066  -22.358 1.00 28.05  ?  125 VAL A O     1 
ATOM   712   C  CB    . VAL A  1  93  ? 15.184 -5.173  -22.119 1.00 26.36  ?  125 VAL A CB    1 
ATOM   713   C  CG1   . VAL A  1  93  ? 15.996 -6.187  -21.329 1.00 27.55  ?  125 VAL A CG1   1 
ATOM   714   C  CG2   . VAL A  1  93  ? 14.076 -4.602  -21.253 1.00 25.96  ?  125 VAL A CG2   1 
ATOM   715   N  N     . ILE A  1  94  ? 17.623 -5.309  -24.056 1.00 25.45  ?  126 ILE A N     1 
ATOM   716   C  CA    . ILE A  1  94  ? 18.906 -5.894  -24.409 1.00 24.25  ?  126 ILE A CA    1 
ATOM   717   C  C     . ILE A  1  94  ? 19.916 -4.835  -24.853 1.00 23.75  ?  126 ILE A C     1 
ATOM   718   O  O     . ILE A  1  94  ? 21.087 -4.895  -24.495 1.00 21.68  ?  126 ILE A O     1 
ATOM   719   C  CB    . ILE A  1  94  ? 18.708 -7.004  -25.453 1.00 24.30  ?  126 ILE A CB    1 
ATOM   720   C  CG1   . ILE A  1  94  ? 17.906 -8.119  -24.797 1.00 25.91  ?  126 ILE A CG1   1 
ATOM   721   C  CG2   . ILE A  1  94  ? 20.035 -7.562  -25.956 1.00 23.43  ?  126 ILE A CG2   1 
ATOM   722   C  CD1   . ILE A  1  94  ? 17.531 -9.271  -25.703 1.00 26.64  ?  126 ILE A CD1   1 
ATOM   723   N  N     . ASN A  1  95  ? 19.470 -3.840  -25.597 1.00 25.23  ?  127 ASN A N     1 
ATOM   724   C  CA    . ASN A  1  95  ? 20.394 -2.790  -25.990 1.00 28.08  ?  127 ASN A CA    1 
ATOM   725   C  C     . ASN A  1  95  ? 20.929 -2.100  -24.757 1.00 28.52  ?  127 ASN A C     1 
ATOM   726   O  O     . ASN A  1  95  ? 22.137 -1.857  -24.660 1.00 29.78  ?  127 ASN A O     1 
ATOM   727   C  CB    . ASN A  1  95  ? 19.744 -1.762  -26.894 1.00 30.81  ?  127 ASN A CB    1 
ATOM   728   C  CG    . ASN A  1  95  ? 19.170 -2.373  -28.151 1.00 33.81  ?  127 ASN A CG    1 
ATOM   729   O  OD1   . ASN A  1  95  ? 19.694 -3.358  -28.692 1.00 35.38  ?  127 ASN A OD1   1 
ATOM   730   N  ND2   . ASN A  1  95  ? 18.053 -1.809  -28.611 1.00 37.39  ?  127 ASN A ND2   1 
ATOM   731   N  N     . VAL A  1  96  ? 20.045 -1.821  -23.798 1.00 27.36  ?  128 VAL A N     1 
ATOM   732   C  CA    . VAL A  1  96  ? 20.484 -1.239  -22.518 1.00 26.10  ?  128 VAL A CA    1 
ATOM   733   C  C     . VAL A  1  96  ? 21.416 -2.117  -21.683 1.00 23.49  ?  128 VAL A C     1 
ATOM   734   O  O     . VAL A  1  96  ? 22.432 -1.656  -21.207 1.00 21.97  ?  128 VAL A O     1 
ATOM   735   C  CB    . VAL A  1  96  ? 19.301 -0.807  -21.663 1.00 26.96  ?  128 VAL A CB    1 
ATOM   736   C  CG1   . VAL A  1  96  ? 19.754 -0.416  -20.265 1.00 27.31  ?  128 VAL A CG1   1 
ATOM   737   C  CG2   . VAL A  1  96  ? 18.633 0.381   -22.332 1.00 28.31  ?  128 VAL A CG2   1 
ATOM   738   N  N     . ILE A  1  97  ? 21.093 -3.380  -21.502 1.00 22.43  ?  129 ILE A N     1 
ATOM   739   C  CA    . ILE A  1  97  ? 22.039 -4.235  -20.812 1.00 22.36  ?  129 ILE A CA    1 
ATOM   740   C  C     . ILE A  1  97  ? 23.364 -4.252  -21.583 1.00 23.84  ?  129 ILE A C     1 
ATOM   741   O  O     . ILE A  1  97  ? 24.456 -4.176  -20.985 1.00 23.51  ?  129 ILE A O     1 
ATOM   742   C  CB    . ILE A  1  97  ? 21.496 -5.656  -20.648 1.00 21.50  ?  129 ILE A CB    1 
ATOM   743   C  CG1   . ILE A  1  97  ? 20.250 -5.634  -19.753 1.00 21.42  ?  129 ILE A CG1   1 
ATOM   744   C  CG2   . ILE A  1  97  ? 22.564 -6.557  -20.048 1.00 21.03  ?  129 ILE A CG2   1 
ATOM   745   C  CD1   . ILE A  1  97  ? 19.590 -6.987  -19.553 1.00 21.53  ?  129 ILE A CD1   1 
ATOM   746   N  N     . THR A  1  98  ? 23.269 -4.336  -22.911 1.00 24.84  ?  130 THR A N     1 
ATOM   747   C  CA    . THR A  1  98  ? 24.460 -4.434  -23.746 1.00 26.08  ?  130 THR A CA    1 
ATOM   748   C  C     . THR A  1  98  ? 25.359 -3.209  -23.523 1.00 25.54  ?  130 THR A C     1 
ATOM   749   O  O     . THR A  1  98  ? 26.566 -3.355  -23.333 1.00 24.46  ?  130 THR A O     1 
ATOM   750   C  CB    . THR A  1  98  ? 24.097 -4.598  -25.253 1.00 27.40  ?  130 THR A CB    1 
ATOM   751   O  OG1   . THR A  1  98  ? 23.270 -5.757  -25.438 1.00 27.93  ?  130 THR A OG1   1 
ATOM   752   C  CG2   . THR A  1  98  ? 25.357 -4.745  -26.133 1.00 26.73  ?  130 THR A CG2   1 
ATOM   753   N  N     . ASN A  1  99  ? 24.770 -2.011  -23.523 1.00 25.49  ?  131 ASN A N     1 
ATOM   754   C  CA    . ASN A  1  99  ? 25.547 -0.774  -23.347 1.00 25.90  ?  131 ASN A CA    1 
ATOM   755   C  C     . ASN A  1  99  ? 26.312 -0.832  -22.026 1.00 25.50  ?  131 ASN A C     1 
ATOM   756   O  O     . ASN A  1  99  ? 27.536 -0.738  -22.008 1.00 26.59  ?  131 ASN A O     1 
ATOM   757   C  CB    . ASN A  1  99  ? 24.650 0.475   -23.435 1.00 27.15  ?  131 ASN A CB    1 
ATOM   758   C  CG    . ASN A  1  99  ? 25.442 1.781   -23.380 1.00 30.34  ?  131 ASN A CG    1 
ATOM   759   O  OD1   . ASN A  1  99  ? 26.264 1.956   -22.481 1.00 32.51  ?  131 ASN A OD1   1 
ATOM   760   N  ND2   . ASN A  1  99  ? 25.178 2.729   -24.325 1.00 33.36  ?  131 ASN A ND2   1 
ATOM   761   N  N     . MET A  1  100 ? 25.590 -1.028  -20.926 1.00 25.02  ?  132 MET A N     1 
ATOM   762   C  CA    . MET A  1  100 ? 26.205 -1.227  -19.607 1.00 23.92  ?  132 MET A CA    1 
ATOM   763   C  C     . MET A  1  100 ? 27.331 -2.275  -19.691 1.00 23.11  ?  132 MET A C     1 
ATOM   764   O  O     . MET A  1  100 ? 28.506 -1.948  -19.470 1.00 21.96  ?  132 MET A O     1 
ATOM   765   C  CB    . MET A  1  100 ? 25.151 -1.650  -18.571 1.00 23.39  ?  132 MET A CB    1 
ATOM   766   C  CG    . MET A  1  100 ? 24.031 -0.646  -18.356 1.00 23.12  ?  132 MET A CG    1 
ATOM   767   S  SD    . MET A  1  100 ? 24.575 0.944   -17.689 1.00 24.37  ?  132 MET A SD    1 
ATOM   768   C  CE    . MET A  1  100 ? 24.732 2.016   -19.100 1.00 24.39  ?  132 MET A CE    1 
ATOM   769   N  N     . THR A  1  101 ? 26.983 -3.508  -20.059 1.00 21.97  ?  133 THR A N     1 
ATOM   770   C  CA    . THR A  1  101 ? 27.978 -4.556  -20.128 1.00 22.01  ?  133 THR A CA    1 
ATOM   771   C  C     . THR A  1  101 ? 29.177 -4.147  -20.955 1.00 23.55  ?  133 THR A C     1 
ATOM   772   O  O     . THR A  1  101 ? 30.300 -4.336  -20.543 1.00 24.95  ?  133 THR A O     1 
ATOM   773   C  CB    . THR A  1  101 ? 27.455 -5.837  -20.745 1.00 21.51  ?  133 THR A CB    1 
ATOM   774   O  OG1   . THR A  1  101 ? 26.279 -6.284  -20.056 1.00 21.12  ?  133 THR A OG1   1 
ATOM   775   C  CG2   . THR A  1  101 ? 28.534 -6.888  -20.653 1.00 21.27  ?  133 THR A CG2   1 
ATOM   776   N  N     . THR A  1  102 ? 28.961 -3.591  -22.130 1.00 25.92  ?  134 THR A N     1 
ATOM   777   C  CA    . THR A  1  102 ? 30.087 -3.078  -22.894 1.00 28.53  ?  134 THR A CA    1 
ATOM   778   C  C     . THR A  1  102 ? 30.849 -1.977  -22.144 1.00 30.16  ?  134 THR A C     1 
ATOM   779   O  O     . THR A  1  102 ? 32.053 -2.132  -21.912 1.00 33.09  ?  134 THR A O     1 
ATOM   780   C  CB    . THR A  1  102 ? 29.651 -2.549  -24.253 1.00 29.11  ?  134 THR A CB    1 
ATOM   781   O  OG1   . THR A  1  102 ? 28.946 -3.594  -24.916 1.00 27.93  ?  134 THR A OG1   1 
ATOM   782   C  CG2   . THR A  1  102 ? 30.871 -2.110  -25.084 1.00 29.30  ?  134 THR A CG2   1 
ATOM   783   N  N     . THR A  1  103 ? 30.160 -0.898  -21.757 1.00 29.10  ?  135 THR A N     1 
ATOM   784   C  CA    . THR A  1  103 ? 30.796 0.226   -21.046 1.00 29.08  ?  135 THR A CA    1 
ATOM   785   C  C     . THR A  1  103 ? 31.746 -0.199  -19.914 1.00 29.13  ?  135 THR A C     1 
ATOM   786   O  O     . THR A  1  103 ? 32.879 0.314   -19.806 1.00 27.61  ?  135 THR A O     1 
ATOM   787   C  CB    . THR A  1  103 ? 29.755 1.168   -20.432 1.00 28.62  ?  135 THR A CB    1 
ATOM   788   O  OG1   . THR A  1  103 ? 28.851 1.614   -21.446 1.00 28.96  ?  135 THR A OG1   1 
ATOM   789   C  CG2   . THR A  1  103 ? 30.444 2.376   -19.818 1.00 28.43  ?  135 THR A CG2   1 
ATOM   790   N  N     . ILE A  1  104 ? 31.270 -1.124  -19.080 1.00 28.87  ?  136 ILE A N     1 
ATOM   791   C  CA    . ILE A  1  104 ? 32.087 -1.718  -18.019 1.00 29.30  ?  136 ILE A CA    1 
ATOM   792   C  C     . ILE A  1  104 ? 33.300 -2.437  -18.604 1.00 28.97  ?  136 ILE A C     1 
ATOM   793   O  O     . ILE A  1  104 ? 34.432 -2.253  -18.142 1.00 26.84  ?  136 ILE A O     1 
ATOM   794   C  CB    . ILE A  1  104 ? 31.273 -2.736  -17.189 1.00 28.99  ?  136 ILE A CB    1 
ATOM   795   C  CG1   . ILE A  1  104 ? 30.231 -2.006  -16.338 1.00 28.56  ?  136 ILE A CG1   1 
ATOM   796   C  CG2   . ILE A  1  104 ? 32.189 -3.593  -16.314 1.00 29.03  ?  136 ILE A CG2   1 
ATOM   797   C  CD1   . ILE A  1  104 ? 29.080 -2.903  -15.908 1.00 28.57  ?  136 ILE A CD1   1 
ATOM   798   N  N     . GLN A  1  105 ? 33.046 -3.272  -19.610 1.00 29.23  ?  137 GLN A N     1 
ATOM   799   C  CA    . GLN A  1  105 ? 34.099 -4.096  -20.180 1.00 30.01  ?  137 GLN A CA    1 
ATOM   800   C  C     . GLN A  1  105 ? 35.179 -3.233  -20.806 1.00 31.20  ?  137 GLN A C     1 
ATOM   801   O  O     . GLN A  1  105 ? 36.342 -3.548  -20.685 1.00 33.25  ?  137 GLN A O     1 
ATOM   802   C  CB    . GLN A  1  105 ? 33.545 -5.118  -21.175 1.00 28.93  ?  137 GLN A CB    1 
ATOM   803   C  CG    . GLN A  1  105 ? 32.913 -6.319  -20.497 1.00 29.03  ?  137 GLN A CG    1 
ATOM   804   C  CD    . GLN A  1  105 ? 32.258 -7.293  -21.469 1.00 31.05  ?  137 GLN A CD    1 
ATOM   805   O  OE1   . GLN A  1  105 ? 32.466 -7.217  -22.682 1.00 33.06  ?  137 GLN A OE1   1 
ATOM   806   N  NE2   . GLN A  1  105 ? 31.454 -8.219  -20.938 1.00 31.45  ?  137 GLN A NE2   1 
ATOM   807   N  N     . SER A  1  106 ? 34.801 -2.133  -21.439 1.00 33.26  ?  138 SER A N     1 
ATOM   808   C  CA    . SER A  1  106 ? 35.777 -1.194  -22.001 1.00 35.46  ?  138 SER A CA    1 
ATOM   809   C  C     . SER A  1  106 ? 36.657 -0.567  -20.948 1.00 34.67  ?  138 SER A C     1 
ATOM   810   O  O     . SER A  1  106 ? 37.873 -0.554  -21.101 1.00 36.26  ?  138 SER A O     1 
ATOM   811   C  CB    . SER A  1  106 ? 35.073 -0.067  -22.748 1.00 38.17  ?  138 SER A CB    1 
ATOM   812   O  OG    . SER A  1  106 ? 34.049 -0.606  -23.572 1.00 44.83  ?  138 SER A OG    1 
ATOM   813   N  N     . LEU A  1  107 ? 36.039 -0.026  -19.900 1.00 33.66  ?  139 LEU A N     1 
ATOM   814   C  CA    . LEU A  1  107 ? 36.777 0.645   -18.837 1.00 31.47  ?  139 LEU A CA    1 
ATOM   815   C  C     . LEU A  1  107 ? 37.499 -0.333  -17.944 1.00 30.13  ?  139 LEU A C     1 
ATOM   816   O  O     . LEU A  1  107 ? 38.497 0.025   -17.358 1.00 30.54  ?  139 LEU A O     1 
ATOM   817   C  CB    . LEU A  1  107 ? 35.842 1.468   -17.976 1.00 32.34  ?  139 LEU A CB    1 
ATOM   818   C  CG    . LEU A  1  107 ? 35.273 2.726   -18.619 1.00 34.42  ?  139 LEU A CG    1 
ATOM   819   C  CD1   . LEU A  1  107 ? 33.985 3.120   -17.926 1.00 35.15  ?  139 LEU A CD1   1 
ATOM   820   C  CD2   . LEU A  1  107 ? 36.259 3.882   -18.556 1.00 35.68  ?  139 LEU A CD2   1 
ATOM   821   N  N     . PHE A  1  108 ? 36.985 -1.551  -17.826 1.00 29.35  ?  140 PHE A N     1 
ATOM   822   C  CA    . PHE A  1  108 ? 37.527 -2.531  -16.889 1.00 30.79  ?  140 PHE A CA    1 
ATOM   823   C  C     . PHE A  1  108 ? 37.812 -3.838  -17.631 1.00 33.44  ?  140 PHE A C     1 
ATOM   824   O  O     . PHE A  1  108 ? 37.230 -4.907  -17.338 1.00 31.06  ?  140 PHE A O     1 
ATOM   825   C  CB    . PHE A  1  108 ? 36.600 -2.731  -15.664 1.00 30.33  ?  140 PHE A CB    1 
ATOM   826   C  CG    . PHE A  1  108 ? 36.317 -1.451  -14.893 1.00 29.00  ?  140 PHE A CG    1 
ATOM   827   C  CD1   . PHE A  1  108 ? 37.333 -0.769  -14.243 1.00 27.95  ?  140 PHE A CD1   1 
ATOM   828   C  CD2   . PHE A  1  108 ? 35.042 -0.923  -14.834 1.00 28.39  ?  140 PHE A CD2   1 
ATOM   829   C  CE1   . PHE A  1  108 ? 37.083 0.418   -13.563 1.00 27.39  ?  140 PHE A CE1   1 
ATOM   830   C  CE2   . PHE A  1  108 ? 34.793 0.252   -14.143 1.00 27.93  ?  140 PHE A CE2   1 
ATOM   831   C  CZ    . PHE A  1  108 ? 35.811 0.927   -13.510 1.00 26.87  ?  140 PHE A CZ    1 
ATOM   832   N  N     . PRO A  1  109 ? 38.746 -3.756  -18.595 1.00 37.88  ?  141 PRO A N     1 
ATOM   833   C  CA    . PRO A  1  109 ? 39.116 -4.881  -19.480 1.00 39.67  ?  141 PRO A CA    1 
ATOM   834   C  C     . PRO A  1  109 ? 39.608 -6.116  -18.733 1.00 42.49  ?  141 PRO A C     1 
ATOM   835   O  O     . PRO A  1  109 ? 39.272 -7.248  -19.111 1.00 41.82  ?  141 PRO A O     1 
ATOM   836   C  CB    . PRO A  1  109 ? 40.246 -4.298  -20.334 1.00 39.29  ?  141 PRO A CB    1 
ATOM   837   C  CG    . PRO A  1  109 ? 40.769 -3.113  -19.572 1.00 38.87  ?  141 PRO A CG    1 
ATOM   838   C  CD    . PRO A  1  109 ? 39.595 -2.564  -18.827 1.00 37.89  ?  141 PRO A CD    1 
ATOM   839   N  N     . ASN A  1  110 ? 40.389 -5.881  -17.678 1.00 45.77  ?  142 ASN A N     1 
ATOM   840   C  CA    . ASN A  1  110 ? 40.967 -6.956  -16.876 1.00 48.11  ?  142 ASN A CA    1 
ATOM   841   C  C     . ASN A  1  110 ? 40.144 -7.369  -15.662 1.00 42.83  ?  142 ASN A C     1 
ATOM   842   O  O     . ASN A  1  110 ? 40.457 -8.364  -15.008 1.00 41.58  ?  142 ASN A O     1 
ATOM   843   C  CB    . ASN A  1  110 ? 42.354 -6.544  -16.410 1.00 53.76  ?  142 ASN A CB    1 
ATOM   844   C  CG    . ASN A  1  110 ? 43.281 -6.256  -17.563 1.00 58.36  ?  142 ASN A CG    1 
ATOM   845   O  OD1   . ASN A  1  110 ? 43.788 -5.140  -17.707 1.00 66.07  ?  142 ASN A OD1   1 
ATOM   846   N  ND2   . ASN A  1  110 ? 43.491 -7.257  -18.414 1.00 59.36  ?  142 ASN A ND2   1 
ATOM   847   N  N     . LEU A  1  111 ? 39.097 -6.616  -15.361 1.00 38.62  ?  143 LEU A N     1 
ATOM   848   C  CA    . LEU A  1  111 ? 38.307 -6.868  -14.170 1.00 35.35  ?  143 LEU A CA    1 
ATOM   849   C  C     . LEU A  1  111 ? 37.199 -7.896  -14.397 1.00 33.04  ?  143 LEU A C     1 
ATOM   850   O  O     . LEU A  1  111 ? 36.421 -7.782  -15.348 1.00 35.28  ?  143 LEU A O     1 
ATOM   851   C  CB    . LEU A  1  111 ? 37.685 -5.573  -13.696 1.00 35.26  ?  143 LEU A CB    1 
ATOM   852   C  CG    . LEU A  1  111 ? 36.897 -5.685  -12.404 1.00 35.72  ?  143 LEU A CG    1 
ATOM   853   C  CD1   . LEU A  1  111 ? 37.754 -6.238  -11.282 1.00 36.39  ?  143 LEU A CD1   1 
ATOM   854   C  CD2   . LEU A  1  111 ? 36.381 -4.304  -12.064 1.00 36.43  ?  143 LEU A CD2   1 
ATOM   855   N  N     . GLN A  1  112 ? 37.130 -8.893  -13.517 1.00 28.72  ?  144 GLN A N     1 
ATOM   856   C  CA    . GLN A  1  112 ? 36.042 -9.846  -13.533 1.00 24.73  ?  144 GLN A CA    1 
ATOM   857   C  C     . GLN A  1  112 ? 34.851 -9.185  -12.839 1.00 23.43  ?  144 GLN A C     1 
ATOM   858   O  O     . GLN A  1  112 ? 35.013 -8.369  -11.921 1.00 22.34  ?  144 GLN A O     1 
ATOM   859   C  CB    . GLN A  1  112 ? 36.434 -11.133 -12.826 1.00 23.50  ?  144 GLN A CB    1 
ATOM   860   C  CG    . GLN A  1  112 ? 35.418 -12.235 -13.023 1.00 23.44  ?  144 GLN A CG    1 
ATOM   861   C  CD    . GLN A  1  112 ? 35.825 -13.586 -12.443 1.00 23.65  ?  144 GLN A CD    1 
ATOM   862   O  OE1   . GLN A  1  112 ? 36.735 -13.715 -11.603 1.00 23.40  ?  144 GLN A OE1   1 
ATOM   863   N  NE2   . GLN A  1  112 ? 35.111 -14.608 -12.866 1.00 23.44  ?  144 GLN A NE2   1 
ATOM   864   N  N     . VAL A  1  113 ? 33.663 -9.532  -13.314 1.00 21.28  ?  145 VAL A N     1 
ATOM   865   C  CA    . VAL A  1  113 ? 32.429 -8.964  -12.851 1.00 19.84  ?  145 VAL A CA    1 
ATOM   866   C  C     . VAL A  1  113 ? 31.426 -10.084 -12.799 1.00 19.98  ?  145 VAL A C     1 
ATOM   867   O  O     . VAL A  1  113 ? 31.382 -10.920 -13.679 1.00 19.32  ?  145 VAL A O     1 
ATOM   868   C  CB    . VAL A  1  113 ? 31.896 -7.927  -13.843 1.00 19.47  ?  145 VAL A CB    1 
ATOM   869   C  CG1   . VAL A  1  113 ? 30.687 -7.212  -13.270 1.00 19.68  ?  145 VAL A CG1   1 
ATOM   870   C  CG2   . VAL A  1  113 ? 32.973 -6.931  -14.218 1.00 19.24  ?  145 VAL A CG2   1 
ATOM   871   N  N     . PHE A  1  114 ? 30.595 -10.091 -11.778 1.00 21.29  ?  146 PHE A N     1 
ATOM   872   C  CA    . PHE A  1  114 ? 29.572 -11.116 -11.658 1.00 22.46  ?  146 PHE A CA    1 
ATOM   873   C  C     . PHE A  1  114 ? 28.206 -10.452 -11.609 1.00 22.50  ?  146 PHE A C     1 
ATOM   874   O  O     . PHE A  1  114 ? 27.813 -9.900  -10.576 1.00 23.65  ?  146 PHE A O     1 
ATOM   875   C  CB    . PHE A  1  114 ? 29.772 -11.924 -10.396 1.00 23.20  ?  146 PHE A CB    1 
ATOM   876   C  CG    . PHE A  1  114 ? 31.142 -12.475 -10.249 1.00 24.01  ?  146 PHE A CG    1 
ATOM   877   C  CD1   . PHE A  1  114 ? 32.199 -11.644 -9.922  1.00 24.24  ?  146 PHE A CD1   1 
ATOM   878   C  CD2   . PHE A  1  114 ? 31.366 -13.838 -10.402 1.00 24.60  ?  146 PHE A CD2   1 
ATOM   879   C  CE1   . PHE A  1  114 ? 33.463 -12.165 -9.764  1.00 25.29  ?  146 PHE A CE1   1 
ATOM   880   C  CE2   . PHE A  1  114 ? 32.624 -14.363 -10.246 1.00 24.80  ?  146 PHE A CE2   1 
ATOM   881   C  CZ    . PHE A  1  114 ? 33.676 -13.526 -9.927  1.00 25.66  ?  146 PHE A CZ    1 
ATOM   882   N  N     . PRO A  1  115 ? 27.488 -10.474 -12.736 1.00 21.12  ?  147 PRO A N     1 
ATOM   883   C  CA    . PRO A  1  115 ? 26.167 -9.904  -12.765 1.00 19.54  ?  147 PRO A CA    1 
ATOM   884   C  C     . PRO A  1  115 ? 25.162 -10.804 -12.155 1.00 18.23  ?  147 PRO A C     1 
ATOM   885   O  O     . PRO A  1  115 ? 25.394 -11.985 -12.040 1.00 18.34  ?  147 PRO A O     1 
ATOM   886   C  CB    . PRO A  1  115 ? 25.871 -9.780  -14.248 1.00 20.07  ?  147 PRO A CB    1 
ATOM   887   C  CG    . PRO A  1  115 ? 27.204 -9.667  -14.874 1.00 20.67  ?  147 PRO A CG    1 
ATOM   888   C  CD    . PRO A  1  115 ? 28.017 -10.653 -14.093 1.00 21.20  ?  147 PRO A CD    1 
ATOM   889   N  N     . ALA A  1  116 ? 24.065 -10.210 -11.727 1.00 17.78  ?  148 ALA A N     1 
ATOM   890   C  CA    . ALA A  1  116 ? 22.856 -10.926 -11.460 1.00 17.42  ?  148 ALA A CA    1 
ATOM   891   C  C     . ALA A  1  116 ? 21.775 -10.168 -12.213 1.00 17.45  ?  148 ALA A C     1 
ATOM   892   O  O     . ALA A  1  116 ? 21.955 -8.979  -12.569 1.00 17.03  ?  148 ALA A O     1 
ATOM   893   C  CB    . ALA A  1  116 ? 22.570 -10.957 -9.978  1.00 17.15  ?  148 ALA A CB    1 
ATOM   894   N  N     . LEU A  1  117 ? 20.671 -10.863 -12.473 1.00 17.27  ?  149 LEU A N     1 
ATOM   895   C  CA    . LEU A  1  117 ? 19.542 -10.251 -13.149 1.00 17.83  ?  149 LEU A CA    1 
ATOM   896   C  C     . LEU A  1  117 ? 18.628 -9.590  -12.146 1.00 18.34  ?  149 LEU A C     1 
ATOM   897   O  O     . LEU A  1  117 ? 18.370 -10.139 -11.070 1.00 19.46  ?  149 LEU A O     1 
ATOM   898   C  CB    . LEU A  1  117 ? 18.755 -11.287 -13.956 1.00 17.55  ?  149 LEU A CB    1 
ATOM   899   C  CG    . LEU A  1  117 ? 19.506 -11.829 -15.162 1.00 17.55  ?  149 LEU A CG    1 
ATOM   900   C  CD1   . LEU A  1  117 ? 18.681 -12.901 -15.846 1.00 17.63  ?  149 LEU A CD1   1 
ATOM   901   C  CD2   . LEU A  1  117 ? 19.853 -10.714 -16.133 1.00 17.64  ?  149 LEU A CD2   1 
ATOM   902   N  N     . GLY A  1  118 ? 18.147 -8.410  -12.502 1.00 18.36  ?  150 GLY A N     1 
ATOM   903   C  CA    . GLY A  1  118 ? 17.098 -7.769  -11.744 1.00 18.97  ?  150 GLY A CA    1 
ATOM   904   C  C     . GLY A  1  118 ? 15.788 -7.823  -12.505 1.00 19.28  ?  150 GLY A C     1 
ATOM   905   O  O     . GLY A  1  118 ? 15.719 -8.334  -13.603 1.00 18.69  ?  150 GLY A O     1 
ATOM   906   N  N     . ASN A  1  119 ? 14.750 -7.245  -11.927 1.00 19.93  ?  151 ASN A N     1 
ATOM   907   C  CA    . ASN A  1  119 ? 13.414 -7.453  -12.422 1.00 20.64  ?  151 ASN A CA    1 
ATOM   908   C  C     . ASN A  1  119 ? 13.060 -6.579  -13.602 1.00 20.94  ?  151 ASN A C     1 
ATOM   909   O  O     . ASN A  1  119 ? 12.181 -6.920  -14.371 1.00 22.05  ?  151 ASN A O     1 
ATOM   910   C  CB    . ASN A  1  119 ? 12.385 -7.306  -11.302 1.00 21.49  ?  151 ASN A CB    1 
ATOM   911   C  CG    . ASN A  1  119 ? 12.565 -6.035  -10.494 1.00 22.42  ?  151 ASN A CG    1 
ATOM   912   O  OD1   . ASN A  1  119 ? 13.573 -5.845  -9.793  1.00 23.46  ?  151 ASN A OD1   1 
ATOM   913   N  ND2   . ASN A  1  119 ? 11.566 -5.174  -10.544 1.00 22.81  ?  151 ASN A ND2   1 
ATOM   914   N  N     . HIS A  1  120 ? 13.736 -5.463  -13.775 1.00 20.78  ?  152 HIS A N     1 
ATOM   915   C  CA    . HIS A  1  120 ? 13.584 -4.736  -15.020 1.00 20.81  ?  152 HIS A CA    1 
ATOM   916   C  C     . HIS A  1  120 ? 14.526 -5.207  -16.116 1.00 21.12  ?  152 HIS A C     1 
ATOM   917   O  O     . HIS A  1  120 ? 14.538 -4.626  -17.181 1.00 20.16  ?  152 HIS A O     1 
ATOM   918   C  CB    . HIS A  1  120 ? 13.848 -3.275  -14.800 1.00 20.53  ?  152 HIS A CB    1 
ATOM   919   C  CG    . HIS A  1  120 ? 12.829 -2.621  -13.956 1.00 20.58  ?  152 HIS A CG    1 
ATOM   920   N  ND1   . HIS A  1  120 ? 12.008 -1.632  -14.433 1.00 21.03  ?  152 HIS A ND1   1 
ATOM   921   C  CD2   . HIS A  1  120 ? 12.509 -2.791  -12.654 1.00 20.80  ?  152 HIS A CD2   1 
ATOM   922   C  CE1   . HIS A  1  120 ? 11.224 -1.213  -13.453 1.00 21.46  ?  152 HIS A CE1   1 
ATOM   923   N  NE2   . HIS A  1  120 ? 11.512 -1.897  -12.362 1.00 20.48  ?  152 HIS A NE2   1 
ATOM   924   N  N     . ASP A  1  121 ? 15.359 -6.208  -15.870 1.00 22.24  ?  153 ASP A N     1 
ATOM   925   C  CA    . ASP A  1  121 ? 16.221 -6.700  -16.944 1.00 23.65  ?  153 ASP A CA    1 
ATOM   926   C  C     . ASP A  1  121 ? 15.444 -7.778  -17.736 1.00 25.96  ?  153 ASP A C     1 
ATOM   927   O  O     . ASP A  1  121 ? 15.931 -8.884  -17.974 1.00 25.90  ?  153 ASP A O     1 
ATOM   928   C  CB    . ASP A  1  121 ? 17.541 -7.236  -16.393 1.00 22.89  ?  153 ASP A CB    1 
ATOM   929   C  CG    . ASP A  1  121 ? 18.342 -6.181  -15.647 1.00 22.04  ?  153 ASP A CG    1 
ATOM   930   O  OD1   . ASP A  1  121 ? 18.455 -5.023  -16.140 1.00 19.80  ?  153 ASP A OD1   1 
ATOM   931   O  OD2   . ASP A  1  121 ? 18.873 -6.547  -14.566 1.00 21.55  -1 153 ASP A OD2   1 
ATOM   932   N  N     . TYR A  1  122 ? 14.215 -7.417  -18.112 1.00 27.92  ?  154 TYR A N     1 
ATOM   933   C  CA    . TYR A  1  122 ? 13.318 -8.249  -18.888 1.00 27.82  ?  154 TYR A CA    1 
ATOM   934   C  C     . TYR A  1  122 ? 12.213 -7.359  -19.465 1.00 29.54  ?  154 TYR A C     1 
ATOM   935   O  O     . TYR A  1  122 ? 11.946 -6.242  -18.963 1.00 30.66  ?  154 TYR A O     1 
ATOM   936   C  CB    . TYR A  1  122 ? 12.704 -9.338  -18.019 1.00 27.26  ?  154 TYR A CB    1 
ATOM   937   C  CG    . TYR A  1  122 ? 12.361 -10.558 -18.805 1.00 27.91  ?  154 TYR A CG    1 
ATOM   938   C  CD1   . TYR A  1  122 ? 13.343 -11.497 -19.118 1.00 28.39  ?  154 TYR A CD1   1 
ATOM   939   C  CD2   . TYR A  1  122 ? 11.067 -10.778 -19.268 1.00 28.11  ?  154 TYR A CD2   1 
ATOM   940   C  CE1   . TYR A  1  122 ? 13.048 -12.627 -19.864 1.00 28.52  ?  154 TYR A CE1   1 
ATOM   941   C  CE2   . TYR A  1  122 ? 10.759 -11.916 -20.009 1.00 28.75  ?  154 TYR A CE2   1 
ATOM   942   C  CZ    . TYR A  1  122 ? 11.755 -12.838 -20.317 1.00 28.47  ?  154 TYR A CZ    1 
ATOM   943   O  OH    . TYR A  1  122 ? 11.472 -13.981 -21.054 1.00 26.70  ?  154 TYR A OH    1 
ATOM   944   N  N     . TRP A  1  123 ? 11.595 -7.844  -20.537 1.00 30.08  ?  155 TRP A N     1 
ATOM   945   C  CA    . TRP A  1  123 ? 10.388 -7.234  -21.084 1.00 29.55  ?  155 TRP A CA    1 
ATOM   946   C  C     . TRP A  1  123 ? 9.331  -8.329  -21.287 1.00 30.43  ?  155 TRP A C     1 
ATOM   947   O  O     . TRP A  1  123 ? 9.595  -9.307  -21.968 1.00 31.23  ?  155 TRP A O     1 
ATOM   948   C  CB    . TRP A  1  123 ? 10.667 -6.517  -22.398 1.00 28.50  ?  155 TRP A CB    1 
ATOM   949   C  CG    . TRP A  1  123 ? 9.513  -5.705  -22.796 1.00 29.23  ?  155 TRP A CG    1 
ATOM   950   C  CD1   . TRP A  1  123 ? 9.325  -4.372  -22.568 1.00 29.25  ?  155 TRP A CD1   1 
ATOM   951   C  CD2   . TRP A  1  123 ? 8.323  -6.174  -23.440 1.00 30.86  ?  155 TRP A CD2   1 
ATOM   952   N  NE1   . TRP A  1  123 ? 8.094  -3.977  -23.037 1.00 29.19  ?  155 TRP A NE1   1 
ATOM   953   C  CE2   . TRP A  1  123 ? 7.462  -5.063  -23.585 1.00 30.07  ?  155 TRP A CE2   1 
ATOM   954   C  CE3   . TRP A  1  123 ? 7.902  -7.429  -23.924 1.00 29.71  ?  155 TRP A CE3   1 
ATOM   955   C  CZ2   . TRP A  1  123 ? 6.220  -5.165  -24.203 1.00 29.71  ?  155 TRP A CZ2   1 
ATOM   956   C  CZ3   . TRP A  1  123 ? 6.669  -7.525  -24.525 1.00 28.50  ?  155 TRP A CZ3   1 
ATOM   957   C  CH2   . TRP A  1  123 ? 5.844  -6.402  -24.668 1.00 29.24  ?  155 TRP A CH2   1 
ATOM   958   N  N     . PRO A  1  124 ? 8.145  -8.190  -20.699 1.00 30.61  ?  156 PRO A N     1 
ATOM   959   C  CA    . PRO A  1  124 ? 7.775  -7.067  -19.798 1.00 31.13  ?  156 PRO A CA    1 
ATOM   960   C  C     . PRO A  1  124 ? 8.417  -7.191  -18.409 1.00 29.48  ?  156 PRO A C     1 
ATOM   961   O  O     . PRO A  1  124 ? 8.709  -8.301  -17.958 1.00 29.91  ?  156 PRO A O     1 
ATOM   962   C  CB    . PRO A  1  124 ? 6.246  -7.175  -19.699 1.00 30.80  ?  156 PRO A CB    1 
ATOM   963   C  CG    . PRO A  1  124 ? 5.925  -8.569  -20.126 1.00 30.35  ?  156 PRO A CG    1 
ATOM   964   C  CD    . PRO A  1  124 ? 7.040  -9.122  -20.953 1.00 29.39  ?  156 PRO A CD    1 
ATOM   965   N  N     . GLN A  1  125 ? 8.637  -6.077  -17.732 1.00 26.50  ?  157 GLN A N     1 
ATOM   966   C  CA    . GLN A  1  125 ? 9.287  -6.165  -16.445 1.00 26.01  ?  157 GLN A CA    1 
ATOM   967   C  C     . GLN A  1  125 ? 8.700  -7.242  -15.545 1.00 25.05  ?  157 GLN A C     1 
ATOM   968   O  O     . GLN A  1  125 ? 7.552  -7.596  -15.675 1.00 22.95  ?  157 GLN A O     1 
ATOM   969   C  CB    . GLN A  1  125 ? 9.298  -4.813  -15.731 1.00 26.82  ?  157 GLN A CB    1 
ATOM   970   C  CG    . GLN A  1  125 ? 7.962  -4.187  -15.371 1.00 26.69  ?  157 GLN A CG    1 
ATOM   971   C  CD    . GLN A  1  125 ? 8.152  -2.735  -14.965 1.00 27.13  ?  157 GLN A CD    1 
ATOM   972   O  OE1   . GLN A  1  125 ? 8.305  -1.839  -15.815 1.00 28.75  ?  157 GLN A OE1   1 
ATOM   973   N  NE2   . GLN A  1  125 ? 8.196  -2.495  -13.665 1.00 27.05  ?  157 GLN A NE2   1 
ATOM   974   N  N     . ASP A  1  126 ? 9.549  -7.795  -14.683 1.00 26.65  ?  158 ASP A N     1 
ATOM   975   C  CA    . ASP A  1  126 ? 9.177  -8.758  -13.629 1.00 29.01  ?  158 ASP A CA    1 
ATOM   976   C  C     . ASP A  1  126 ? 8.824  -10.185 -14.075 1.00 28.08  ?  158 ASP A C     1 
ATOM   977   O  O     . ASP A  1  126 ? 8.688  -11.090 -13.254 1.00 25.74  ?  158 ASP A O     1 
ATOM   978   C  CB    . ASP A  1  126 ? 8.024  -8.214  -12.778 1.00 32.43  ?  158 ASP A CB    1 
ATOM   979   C  CG    . ASP A  1  126 ? 8.223  -6.775  -12.365 1.00 34.55  ?  158 ASP A CG    1 
ATOM   980   O  OD1   . ASP A  1  126 ? 9.328  -6.253  -12.596 1.00 34.86  ?  158 ASP A OD1   1 
ATOM   981   O  OD2   . ASP A  1  126 ? 7.263  -6.176  -11.822 1.00 38.09  -1 158 ASP A OD2   1 
ATOM   982   N  N     . GLN A  1  127 ? 8.707  -10.400 -15.368 1.00 29.01  ?  159 GLN A N     1 
ATOM   983   C  CA    . GLN A  1  127 ? 8.160  -11.637 -15.869 1.00 30.65  ?  159 GLN A CA    1 
ATOM   984   C  C     . GLN A  1  127 ? 9.290  -12.557 -16.272 1.00 32.34  ?  159 GLN A C     1 
ATOM   985   O  O     . GLN A  1  127 ? 9.290  -13.129 -17.356 1.00 35.81  ?  159 GLN A O     1 
ATOM   986   C  CB    . GLN A  1  127 ? 7.248  -11.324 -17.047 1.00 30.24  ?  159 GLN A CB    1 
ATOM   987   C  CG    . GLN A  1  127 ? 6.241  -10.236 -16.719 1.00 30.29  ?  159 GLN A CG    1 
ATOM   988   C  CD    . GLN A  1  127 ? 5.365  -10.615 -15.537 1.00 30.24  ?  159 GLN A CD    1 
ATOM   989   O  OE1   . GLN A  1  127 ? 4.773  -11.690 -15.537 1.00 32.72  ?  159 GLN A OE1   1 
ATOM   990   N  NE2   . GLN A  1  127 ? 5.281  -9.749  -14.530 1.00 28.47  ?  159 GLN A NE2   1 
ATOM   991   N  N     . LEU A  1  128 ? 10.267 -12.694 -15.394 1.00 32.89  ?  160 LEU A N     1 
ATOM   992   C  CA    . LEU A  1  128 ? 11.422 -13.503 -15.707 1.00 33.31  ?  160 LEU A CA    1 
ATOM   993   C  C     . LEU A  1  128 ? 10.949 -14.956 -15.649 1.00 34.44  ?  160 LEU A C     1 
ATOM   994   O  O     . LEU A  1  128 ? 10.295 -15.334 -14.683 1.00 35.39  ?  160 LEU A O     1 
ATOM   995   C  CB    . LEU A  1  128 ? 12.568 -13.191 -14.738 1.00 32.24  ?  160 LEU A CB    1 
ATOM   996   C  CG    . LEU A  1  128 ? 13.323 -11.887 -15.089 1.00 31.57  ?  160 LEU A CG    1 
ATOM   997   C  CD1   . LEU A  1  128 ? 12.566 -10.629 -14.683 1.00 30.89  ?  160 LEU A CD1   1 
ATOM   998   C  CD2   . LEU A  1  128 ? 14.711 -11.886 -14.472 1.00 31.47  ?  160 LEU A CD2   1 
ATOM   999   N  N     . PRO A  1  129 ? 11.204 -15.747 -16.716 1.00 35.01  ?  161 PRO A N     1 
ATOM   1000  C  CA    . PRO A  1  129 ? 10.699 -17.121 -16.809 1.00 34.57  ?  161 PRO A CA    1 
ATOM   1001  C  C     . PRO A  1  129 ? 11.607 -18.225 -16.260 1.00 33.14  ?  161 PRO A C     1 
ATOM   1002  O  O     . PRO A  1  129 ? 12.759 -17.977 -15.879 1.00 31.54  ?  161 PRO A O     1 
ATOM   1003  C  CB    . PRO A  1  129 ? 10.536 -17.313 -18.317 1.00 34.56  ?  161 PRO A CB    1 
ATOM   1004  C  CG    . PRO A  1  129 ? 11.672 -16.542 -18.876 1.00 34.73  ?  161 PRO A CG    1 
ATOM   1005  C  CD    . PRO A  1  129 ? 11.701 -15.290 -18.030 1.00 35.11  ?  161 PRO A CD    1 
ATOM   1006  N  N     . VAL A  1  130 ? 11.036 -19.432 -16.270 1.00 32.48  ?  162 VAL A N     1 
ATOM   1007  C  CA    . VAL A  1  130 ? 11.602 -20.679 -15.728 1.00 32.21  ?  162 VAL A CA    1 
ATOM   1008  C  C     . VAL A  1  130 ? 12.522 -21.384 -16.723 1.00 31.21  ?  162 VAL A C     1 
ATOM   1009  O  O     . VAL A  1  130 ? 13.447 -22.128 -16.369 1.00 30.74  ?  162 VAL A O     1 
ATOM   1010  C  CB    . VAL A  1  130 ? 10.440 -21.661 -15.441 1.00 33.52  ?  162 VAL A CB    1 
ATOM   1011  C  CG1   . VAL A  1  130 ? 10.934 -23.093 -15.156 1.00 33.62  ?  162 VAL A CG1   1 
ATOM   1012  C  CG2   . VAL A  1  130 ? 9.535  -21.110 -14.336 1.00 33.90  ?  162 VAL A CG2   1 
ATOM   1013  N  N     . VAL A  1  131 ? 12.227 -21.164 -17.986 1.00 30.58  ?  163 VAL A N     1 
ATOM   1014  C  CA    . VAL A  1  131 ? 12.877 -21.874 -19.056 1.00 30.83  ?  163 VAL A CA    1 
ATOM   1015  C  C     . VAL A  1  131 ? 13.615 -20.838 -19.867 1.00 31.61  ?  163 VAL A C     1 
ATOM   1016  O  O     . VAL A  1  131 ? 13.334 -19.635 -19.747 1.00 35.89  ?  163 VAL A O     1 
ATOM   1017  C  CB    . VAL A  1  131 ? 11.833 -22.582 -19.936 1.00 30.43  ?  163 VAL A CB    1 
ATOM   1018  C  CG1   . VAL A  1  131 ? 10.881 -23.413 -19.073 1.00 29.41  ?  163 VAL A CG1   1 
ATOM   1019  C  CG2   . VAL A  1  131 ? 11.058 -21.568 -20.781 1.00 30.73  ?  163 VAL A CG2   1 
ATOM   1020  N  N     . THR A  1  132 ? 14.538 -21.287 -20.704 1.00 29.82  ?  164 THR A N     1 
ATOM   1021  C  CA    . THR A  1  132 ? 15.315 -20.360 -21.519 1.00 28.68  ?  164 THR A CA    1 
ATOM   1022  C  C     . THR A  1  132 ? 14.447 -19.322 -22.301 1.00 27.93  ?  164 THR A C     1 
ATOM   1023  O  O     . THR A  1  132 ? 13.196 -19.442 -22.378 1.00 26.86  ?  164 THR A O     1 
ATOM   1024  C  CB    . THR A  1  132 ? 16.257 -21.126 -22.461 1.00 28.00  ?  164 THR A CB    1 
ATOM   1025  O  OG1   . THR A  1  132 ? 17.129 -20.194 -23.122 1.00 25.77  ?  164 THR A OG1   1 
ATOM   1026  C  CG2   . THR A  1  132 ? 15.437 -21.961 -23.481 1.00 28.23  ?  164 THR A CG2   1 
ATOM   1027  N  N     . SER A  1  133 ? 15.127 -18.314 -22.860 1.00 26.39  ?  165 SER A N     1 
ATOM   1028  C  CA    . SER A  1  133 ? 14.472 -17.116 -23.375 1.00 26.69  ?  165 SER A CA    1 
ATOM   1029  C  C     . SER A  1  133 ? 15.457 -16.204 -24.069 1.00 26.93  ?  165 SER A C     1 
ATOM   1030  O  O     . SER A  1  133 ? 16.654 -16.247 -23.820 1.00 26.36  ?  165 SER A O     1 
ATOM   1031  C  CB    . SER A  1  133 ? 13.835 -16.308 -22.234 1.00 27.45  ?  165 SER A CB    1 
ATOM   1032  O  OG    . SER A  1  133 ? 14.823 -15.510 -21.577 1.00 27.69  ?  165 SER A OG    1 
ATOM   1033  N  N     . LYS A  1  134 ? 14.925 -15.313 -24.888 1.00 29.33  ?  166 LYS A N     1 
ATOM   1034  C  CA    . LYS A  1  134 ? 15.747 -14.405 -25.670 1.00 30.69  ?  166 LYS A CA    1 
ATOM   1035  C  C     . LYS A  1  134 ? 16.688 -13.583 -24.790 1.00 30.56  ?  166 LYS A C     1 
ATOM   1036  O  O     . LYS A  1  134 ? 17.847 -13.404 -25.131 1.00 31.08  ?  166 LYS A O     1 
ATOM   1037  C  CB    . LYS A  1  134 ? 14.863 -13.499 -26.530 1.00 32.12  ?  166 LYS A CB    1 
ATOM   1038  C  CG    . LYS A  1  134 ? 15.653 -12.505 -27.359 1.00 35.41  ?  166 LYS A CG    1 
ATOM   1039  C  CD    . LYS A  1  134 ? 14.800 -11.759 -28.377 1.00 38.20  ?  166 LYS A CD    1 
ATOM   1040  C  CE    . LYS A  1  134 ? 15.274 -12.005 -29.797 1.00 41.06  ?  166 LYS A CE    1 
ATOM   1041  N  NZ    . LYS A  1  134 ? 14.581 -11.073 -30.727 1.00 43.50  1  166 LYS A NZ    1 
ATOM   1042  N  N     . VAL A  1  135 ? 16.197 -13.109 -23.651 1.00 31.13  ?  167 VAL A N     1 
ATOM   1043  C  CA    . VAL A  1  135 ? 16.999 -12.271 -22.740 1.00 30.63  ?  167 VAL A CA    1 
ATOM   1044  C  C     . VAL A  1  135 ? 18.070 -13.094 -22.014 1.00 29.22  ?  167 VAL A C     1 
ATOM   1045  O  O     . VAL A  1  135 ? 19.248 -12.699 -21.941 1.00 27.47  ?  167 VAL A O     1 
ATOM   1046  C  CB    . VAL A  1  135 ? 16.106 -11.584 -21.684 1.00 30.97  ?  167 VAL A CB    1 
ATOM   1047  C  CG1   . VAL A  1  135 ? 16.939 -10.744 -20.733 1.00 30.79  ?  167 VAL A CG1   1 
ATOM   1048  C  CG2   . VAL A  1  135 ? 15.057 -10.724 -22.369 1.00 31.83  ?  167 VAL A CG2   1 
ATOM   1049  N  N     . TYR A  1  136 ? 17.659 -14.237 -21.480 1.00 27.72  ?  168 TYR A N     1 
ATOM   1050  C  CA    . TYR A  1  136 ? 18.596 -15.105 -20.796 1.00 27.69  ?  168 TYR A CA    1 
ATOM   1051  C  C     . TYR A  1  136 ? 19.763 -15.450 -21.728 1.00 27.97  ?  168 TYR A C     1 
ATOM   1052  O  O     . TYR A  1  136 ? 20.924 -15.484 -21.305 1.00 26.34  ?  168 TYR A O     1 
ATOM   1053  C  CB    . TYR A  1  136 ? 17.898 -16.373 -20.295 1.00 27.57  ?  168 TYR A CB    1 
ATOM   1054  C  CG    . TYR A  1  136 ? 16.919 -16.208 -19.122 1.00 27.95  ?  168 TYR A CG    1 
ATOM   1055  C  CD1   . TYR A  1  136 ? 16.799 -15.004 -18.383 1.00 27.98  ?  168 TYR A CD1   1 
ATOM   1056  C  CD2   . TYR A  1  136 ? 16.140 -17.286 -18.713 1.00 28.04  ?  168 TYR A CD2   1 
ATOM   1057  C  CE1   . TYR A  1  136 ? 15.905 -14.894 -17.305 1.00 26.64  ?  168 TYR A CE1   1 
ATOM   1058  C  CE2   . TYR A  1  136 ? 15.254 -17.183 -17.641 1.00 27.90  ?  168 TYR A CE2   1 
ATOM   1059  C  CZ    . TYR A  1  136 ? 15.138 -15.998 -16.935 1.00 26.78  ?  168 TYR A CZ    1 
ATOM   1060  O  OH    . TYR A  1  136 ? 14.232 -15.956 -15.893 1.00 24.60  ?  168 TYR A OH    1 
ATOM   1061  N  N     . ASN A  1  137 ? 19.456 -15.673 -23.004 1.00 28.98  ?  169 ASN A N     1 
ATOM   1062  C  CA    . ASN A  1  137 ? 20.491 -16.074 -23.956 1.00 30.85  ?  169 ASN A CA    1 
ATOM   1063  C  C     . ASN A  1  137 ? 21.318 -14.910 -24.404 1.00 31.63  ?  169 ASN A C     1 
ATOM   1064  O  O     . ASN A  1  137 ? 22.493 -15.081 -24.756 1.00 32.18  ?  169 ASN A O     1 
ATOM   1065  C  CB    . ASN A  1  137 ? 19.892 -16.764 -25.164 1.00 31.24  ?  169 ASN A CB    1 
ATOM   1066  C  CG    . ASN A  1  137 ? 19.484 -18.181 -24.858 1.00 33.00  ?  169 ASN A CG    1 
ATOM   1067  O  OD1   . ASN A  1  137 ? 18.305 -18.469 -24.683 1.00 37.29  ?  169 ASN A OD1   1 
ATOM   1068  N  ND2   . ASN A  1  137 ? 20.457 -19.073 -24.754 1.00 33.10  ?  169 ASN A ND2   1 
ATOM   1069  N  N     . ALA A  1  138 ? 20.687 -13.738 -24.407 1.00 31.48  ?  170 ALA A N     1 
ATOM   1070  C  CA    . ALA A  1  138 ? 21.342 -12.496 -24.780 1.00 32.14  ?  170 ALA A CA    1 
ATOM   1071  C  C     . ALA A  1  138 ? 22.435 -12.183 -23.766 1.00 35.08  ?  170 ALA A C     1 
ATOM   1072  O  O     . ALA A  1  138 ? 23.592 -11.890 -24.125 1.00 34.45  ?  170 ALA A O     1 
ATOM   1073  C  CB    . ALA A  1  138 ? 20.327 -11.355 -24.851 1.00 30.97  ?  170 ALA A CB    1 
ATOM   1074  N  N     . VAL A  1  139 ? 22.069 -12.261 -22.489 1.00 36.57  ?  171 VAL A N     1 
ATOM   1075  C  CA    . VAL A  1  139 ? 23.026 -11.951 -21.439 1.00 36.42  ?  171 VAL A CA    1 
ATOM   1076  C  C     . VAL A  1  139 ? 24.112 -13.001 -21.377 1.00 36.73  ?  171 VAL A C     1 
ATOM   1077  O  O     . VAL A  1  139 ? 25.265 -12.666 -21.134 1.00 37.82  ?  171 VAL A O     1 
ATOM   1078  C  CB    . VAL A  1  139 ? 22.379 -11.781 -20.054 1.00 35.39  ?  171 VAL A CB    1 
ATOM   1079  C  CG1   . VAL A  1  139 ? 21.462 -10.575 -20.051 1.00 34.61  ?  171 VAL A CG1   1 
ATOM   1080  C  CG2   . VAL A  1  139 ? 21.636 -13.030 -19.629 1.00 36.03  ?  171 VAL A CG2   1 
ATOM   1081  N  N     . ALA A  1  140 ? 23.772 -14.264 -21.611 1.00 37.02  ?  172 ALA A N     1 
ATOM   1082  C  CA    . ALA A  1  140 ? 24.807 -15.291 -21.590 1.00 39.35  ?  172 ALA A CA    1 
ATOM   1083  C  C     . ALA A  1  140 ? 25.919 -14.945 -22.606 1.00 40.41  ?  172 ALA A C     1 
ATOM   1084  O  O     . ALA A  1  140 ? 27.111 -15.059 -22.295 1.00 40.40  ?  172 ALA A O     1 
ATOM   1085  C  CB    . ALA A  1  140 ? 24.223 -16.678 -21.830 1.00 39.09  ?  172 ALA A CB    1 
ATOM   1086  N  N     . ASN A  1  141 ? 25.540 -14.464 -23.785 1.00 40.13  ?  173 ASN A N     1 
ATOM   1087  C  CA    . ASN A  1  141 ? 26.549 -14.048 -24.759 1.00 44.54  ?  173 ASN A CA    1 
ATOM   1088  C  C     . ASN A  1  141 ? 27.359 -12.868 -24.246 1.00 42.25  ?  173 ASN A C     1 
ATOM   1089  O  O     . ASN A  1  141 ? 28.573 -12.893 -24.279 1.00 43.93  ?  173 ASN A O     1 
ATOM   1090  C  CB    . ASN A  1  141 ? 25.925 -13.686 -26.113 1.00 49.62  ?  173 ASN A CB    1 
ATOM   1091  C  CG    . ASN A  1  141 ? 25.148 -14.846 -26.740 1.00 53.68  ?  173 ASN A CG    1 
ATOM   1092  O  OD1   . ASN A  1  141 ? 25.449 -16.028 -26.503 1.00 53.55  ?  173 ASN A OD1   1 
ATOM   1093  N  ND2   . ASN A  1  141 ? 24.135 -14.508 -27.549 1.00 54.65  ?  173 ASN A ND2   1 
ATOM   1094  N  N     . LEU A  1  142 ? 26.669 -11.843 -23.761 1.00 40.31  ?  174 LEU A N     1 
ATOM   1095  C  CA    . LEU A  1  142 ? 27.299 -10.623 -23.251 1.00 36.19  ?  174 LEU A CA    1 
ATOM   1096  C  C     . LEU A  1  142 ? 28.248 -10.850 -22.080 1.00 33.89  ?  174 LEU A C     1 
ATOM   1097  O  O     . LEU A  1  142 ? 29.187 -10.079 -21.887 1.00 31.08  ?  174 LEU A O     1 
ATOM   1098  C  CB    . LEU A  1  142 ? 26.214 -9.682  -22.774 1.00 37.13  ?  174 LEU A CB    1 
ATOM   1099  C  CG    . LEU A  1  142 ? 25.302 -9.118  -23.854 1.00 37.89  ?  174 LEU A CG    1 
ATOM   1100  C  CD1   . LEU A  1  142 ? 23.936 -8.763  -23.284 1.00 37.28  ?  174 LEU A CD1   1 
ATOM   1101  C  CD2   . LEU A  1  142 ? 25.955 -7.892  -24.476 1.00 38.06  ?  174 LEU A CD2   1 
ATOM   1102  N  N     . TRP A  1  143 ? 27.980 -11.883 -21.282 1.00 33.15  ?  175 TRP A N     1 
ATOM   1103  C  CA    . TRP A  1  143 ? 28.741 -12.118 -20.053 1.00 33.70  ?  175 TRP A CA    1 
ATOM   1104  C  C     . TRP A  1  143 ? 29.670 -13.310 -20.126 1.00 36.04  ?  175 TRP A C     1 
ATOM   1105  O  O     . TRP A  1  143 ? 30.349 -13.605 -19.152 1.00 38.02  ?  175 TRP A O     1 
ATOM   1106  C  CB    . TRP A  1  143 ? 27.808 -12.232 -18.834 1.00 31.12  ?  175 TRP A CB    1 
ATOM   1107  C  CG    . TRP A  1  143 ? 27.007 -10.995 -18.621 1.00 28.85  ?  175 TRP A CG    1 
ATOM   1108  C  CD1   . TRP A  1  143 ? 27.295 -9.738  -19.083 1.00 28.92  ?  175 TRP A CD1   1 
ATOM   1109  C  CD2   . TRP A  1  143 ? 25.791 -10.883 -17.899 1.00 27.20  ?  175 TRP A CD2   1 
ATOM   1110  N  NE1   . TRP A  1  143 ? 26.319 -8.853  -18.701 1.00 28.89  ?  175 TRP A NE1   1 
ATOM   1111  C  CE2   . TRP A  1  143 ? 25.386 -9.533  -17.963 1.00 27.94  ?  175 TRP A CE2   1 
ATOM   1112  C  CE3   . TRP A  1  143 ? 24.995 -11.790 -17.207 1.00 27.31  ?  175 TRP A CE3   1 
ATOM   1113  C  CZ2   . TRP A  1  143 ? 24.225 -9.072  -17.347 1.00 27.27  ?  175 TRP A CZ2   1 
ATOM   1114  C  CZ3   . TRP A  1  143 ? 23.829 -11.331 -16.603 1.00 27.15  ?  175 TRP A CZ3   1 
ATOM   1115  C  CH2   . TRP A  1  143 ? 23.461 -9.986  -16.673 1.00 26.99  ?  175 TRP A CH2   1 
ATOM   1116  N  N     . LYS A  1  144 ? 29.716 -13.983 -21.274 1.00 39.00  ?  176 LYS A N     1 
ATOM   1117  C  CA    . LYS A  1  144 ? 30.771 -14.959 -21.561 1.00 39.31  ?  176 LYS A CA    1 
ATOM   1118  C  C     . LYS A  1  144 ? 32.137 -14.489 -21.064 1.00 34.30  ?  176 LYS A C     1 
ATOM   1119  O  O     . LYS A  1  144 ? 32.815 -15.227 -20.343 1.00 36.36  ?  176 LYS A O     1 
ATOM   1120  C  CB    . LYS A  1  144 ? 30.881 -15.225 -23.074 1.00 46.65  ?  176 LYS A CB    1 
ATOM   1121  C  CG    . LYS A  1  144 ? 29.990 -16.343 -23.652 1.00 53.05  ?  176 LYS A CG    1 
ATOM   1122  C  CD    . LYS A  1  144 ? 29.994 -16.374 -25.196 1.00 57.68  ?  176 LYS A CD    1 
ATOM   1123  C  CE    . LYS A  1  144 ? 31.399 -16.157 -25.795 1.00 62.28  ?  176 LYS A CE    1 
ATOM   1124  N  NZ    . LYS A  1  144 ? 31.438 -15.910 -27.267 1.00 63.88  1  176 LYS A NZ    1 
ATOM   1125  N  N     . PRO A  1  145 ? 32.548 -13.260 -21.416 1.00 28.74  ?  177 PRO A N     1 
ATOM   1126  C  CA    . PRO A  1  145 ? 33.933 -12.922 -21.123 1.00 28.44  ?  177 PRO A CA    1 
ATOM   1127  C  C     . PRO A  1  145 ? 34.276 -12.912 -19.642 1.00 30.22  ?  177 PRO A C     1 
ATOM   1128  O  O     . PRO A  1  145 ? 35.430 -12.673 -19.301 1.00 32.40  ?  177 PRO A O     1 
ATOM   1129  C  CB    . PRO A  1  145 ? 34.090 -11.503 -21.677 1.00 27.77  ?  177 PRO A CB    1 
ATOM   1130  C  CG    . PRO A  1  145 ? 32.860 -11.212 -22.433 1.00 28.13  ?  177 PRO A CG    1 
ATOM   1131  C  CD    . PRO A  1  145 ? 31.793 -12.095 -21.876 1.00 28.28  ?  177 PRO A CD    1 
ATOM   1132  N  N     . TRP A  1  146 ? 33.276 -13.121 -18.777 1.00 31.85  ?  178 TRP A N     1 
ATOM   1133  C  CA    . TRP A  1  146 ? 33.449 -13.202 -17.317 1.00 30.42  ?  178 TRP A CA    1 
ATOM   1134  C  C     . TRP A  1  146 ? 33.110 -14.563 -16.712 1.00 33.25  ?  178 TRP A C     1 
ATOM   1135  O  O     . TRP A  1  146 ? 33.354 -14.750 -15.543 1.00 35.82  ?  178 TRP A O     1 
ATOM   1136  C  CB    . TRP A  1  146 ? 32.561 -12.171 -16.610 1.00 27.85  ?  178 TRP A CB    1 
ATOM   1137  C  CG    . TRP A  1  146 ? 32.837 -10.747 -16.930 1.00 25.65  ?  178 TRP A CG    1 
ATOM   1138  C  CD1   . TRP A  1  146 ? 34.047 -10.179 -17.133 1.00 25.80  ?  178 TRP A CD1   1 
ATOM   1139  C  CD2   . TRP A  1  146 ? 31.874 -9.696  -17.046 1.00 24.31  ?  178 TRP A CD2   1 
ATOM   1140  N  NE1   . TRP A  1  146 ? 33.910 -8.835  -17.383 1.00 25.40  ?  178 TRP A NE1   1 
ATOM   1141  C  CE2   . TRP A  1  146 ? 32.582 -8.512  -17.334 1.00 24.87  ?  178 TRP A CE2   1 
ATOM   1142  C  CE3   . TRP A  1  146 ? 30.482 -9.643  -16.951 1.00 23.47  ?  178 TRP A CE3   1 
ATOM   1143  C  CZ2   . TRP A  1  146 ? 31.947 -7.278  -17.509 1.00 24.60  ?  178 TRP A CZ2   1 
ATOM   1144  C  CZ3   . TRP A  1  146 ? 29.850 -8.429  -17.136 1.00 23.48  ?  178 TRP A CZ3   1 
ATOM   1145  C  CH2   . TRP A  1  146 ? 30.585 -7.256  -17.405 1.00 24.09  ?  178 TRP A CH2   1 
ATOM   1146  N  N     . LEU A  1  147 ? 32.560 -15.514 -17.455 1.00 36.94  ?  179 LEU A N     1 
ATOM   1147  C  CA    . LEU A  1  147 ? 32.066 -16.724 -16.814 1.00 42.78  ?  179 LEU A CA    1 
ATOM   1148  C  C     . LEU A  1  147 ? 32.486 -18.047 -17.476 1.00 47.62  ?  179 LEU A C     1 
ATOM   1149  O  O     . LEU A  1  147 ? 32.961 -18.076 -18.610 1.00 51.25  ?  179 LEU A O     1 
ATOM   1150  C  CB    . LEU A  1  147 ? 30.537 -16.644 -16.719 1.00 45.35  ?  179 LEU A CB    1 
ATOM   1151  C  CG    . LEU A  1  147 ? 29.899 -15.372 -16.101 1.00 47.90  ?  179 LEU A CG    1 
ATOM   1152  C  CD1   . LEU A  1  147 ? 28.375 -15.504 -16.090 1.00 49.20  ?  179 LEU A CD1   1 
ATOM   1153  C  CD2   . LEU A  1  147 ? 30.369 -15.046 -14.684 1.00 46.77  ?  179 LEU A CD2   1 
ATOM   1154  N  N     . ASP A  1  148 ? 32.304 -19.133 -16.722 1.00 50.61  ?  180 ASP A N     1 
ATOM   1155  C  CA    . ASP A  1  148 ? 32.458 -20.519 -17.186 1.00 51.71  ?  180 ASP A CA    1 
ATOM   1156  C  C     . ASP A  1  148 ? 31.495 -20.863 -18.278 1.00 54.14  ?  180 ASP A C     1 
ATOM   1157  O  O     . ASP A  1  148 ? 30.505 -20.183 -18.442 1.00 56.64  ?  180 ASP A O     1 
ATOM   1158  C  CB    . ASP A  1  148 ? 32.049 -21.480 -16.073 1.00 52.75  ?  180 ASP A CB    1 
ATOM   1159  C  CG    . ASP A  1  148 ? 33.112 -21.723 -15.066 1.00 53.60  ?  180 ASP A CG    1 
ATOM   1160  O  OD1   . ASP A  1  148 ? 34.305 -21.456 -15.326 1.00 52.31  ?  180 ASP A OD1   1 
ATOM   1161  O  OD2   . ASP A  1  148 ? 32.719 -22.213 -13.990 1.00 56.42  -1 180 ASP A OD2   1 
ATOM   1162  N  N     . GLU A  1  149 ? 31.742 -21.979 -18.956 1.00 57.68  ?  181 GLU A N     1 
ATOM   1163  C  CA    . GLU A  1  149 ? 30.714 -22.614 -19.783 1.00 60.39  ?  181 GLU A CA    1 
ATOM   1164  C  C     . GLU A  1  149 ? 29.632 -23.212 -18.872 1.00 58.78  ?  181 GLU A C     1 
ATOM   1165  O  O     . GLU A  1  149 ? 28.471 -23.330 -19.266 1.00 59.77  ?  181 GLU A O     1 
ATOM   1166  C  CB    . GLU A  1  149 ? 31.281 -23.765 -20.617 1.00 65.89  ?  181 GLU A CB    1 
ATOM   1167  C  CG    . GLU A  1  149 ? 32.523 -23.479 -21.457 1.00 70.65  ?  181 GLU A CG    1 
ATOM   1168  C  CD    . GLU A  1  149 ? 33.311 -24.751 -21.793 1.00 74.60  ?  181 GLU A CD    1 
ATOM   1169  O  OE1   . GLU A  1  149 ? 32.883 -25.875 -21.417 1.00 72.73  ?  181 GLU A OE1   1 
ATOM   1170  O  OE2   . GLU A  1  149 ? 34.375 -24.625 -22.436 1.00 73.80  -1 181 GLU A OE2   1 
ATOM   1171  N  N     . GLU A  1  150 ? 30.043 -23.639 -17.680 1.00 54.83  ?  182 GLU A N     1 
ATOM   1172  C  CA    . GLU A  1  150 ? 29.155 -24.273 -16.705 1.00 54.80  ?  182 GLU A CA    1 
ATOM   1173  C  C     . GLU A  1  150 ? 28.185 -23.237 -16.157 1.00 50.65  ?  182 GLU A C     1 
ATOM   1174  O  O     . GLU A  1  150 ? 26.974 -23.477 -16.025 1.00 44.65  ?  182 GLU A O     1 
ATOM   1175  C  CB    . GLU A  1  150 ? 29.970 -24.861 -15.540 1.00 59.19  ?  182 GLU A CB    1 
ATOM   1176  C  CG    . GLU A  1  150 ? 30.939 -25.989 -15.906 1.00 62.96  ?  182 GLU A CG    1 
ATOM   1177  C  CD    . GLU A  1  150 ? 32.242 -25.498 -16.543 1.00 66.15  ?  182 GLU A CD    1 
ATOM   1178  O  OE1   . GLU A  1  150 ? 33.191 -25.110 -15.820 1.00 62.83  ?  182 GLU A OE1   1 
ATOM   1179  O  OE2   . GLU A  1  150 ? 32.322 -25.502 -17.789 1.00 71.22  -1 182 GLU A OE2   1 
ATOM   1180  N  N     . ALA A  1  151 ? 28.761 -22.093 -15.807 1.00 45.57  ?  183 ALA A N     1 
ATOM   1181  C  CA    . ALA A  1  151 ? 28.007 -20.935 -15.393 1.00 42.32  ?  183 ALA A CA    1 
ATOM   1182  C  C     . ALA A  1  151 ? 27.041 -20.600 -16.505 1.00 39.36  ?  183 ALA A C     1 
ATOM   1183  O  O     . ALA A  1  151 ? 25.832 -20.805 -16.385 1.00 38.84  ?  183 ALA A O     1 
ATOM   1184  C  CB    . ALA A  1  151 ? 28.951 -19.760 -15.136 1.00 42.65  ?  183 ALA A CB    1 
ATOM   1185  N  N     . ILE A  1  152 ? 27.610 -20.132 -17.609 1.00 37.26  ?  184 ILE A N     1 
ATOM   1186  C  CA    . ILE A  1  152 ? 26.865 -19.704 -18.779 1.00 35.93  ?  184 ILE A CA    1 
ATOM   1187  C  C     . ILE A  1  152 ? 25.731 -20.651 -19.117 1.00 35.18  ?  184 ILE A C     1 
ATOM   1188  O  O     . ILE A  1  152 ? 24.618 -20.232 -19.438 1.00 33.89  ?  184 ILE A O     1 
ATOM   1189  C  CB    . ILE A  1  152 ? 27.814 -19.606 -19.974 1.00 36.58  ?  184 ILE A CB    1 
ATOM   1190  C  CG1   . ILE A  1  152 ? 28.599 -18.282 -19.902 1.00 39.01  ?  184 ILE A CG1   1 
ATOM   1191  C  CG2   . ILE A  1  152 ? 27.077 -19.748 -21.297 1.00 38.34  ?  184 ILE A CG2   1 
ATOM   1192  C  CD1   . ILE A  1  152 ? 27.802 -17.016 -20.177 1.00 39.51  ?  184 ILE A CD1   1 
ATOM   1193  N  N     . SER A  1  153 ? 26.029 -21.935 -19.057 1.00 35.30  ?  185 SER A N     1 
ATOM   1194  C  CA    . SER A  1  153 ? 25.024 -22.935 -19.263 1.00 35.34  ?  185 SER A CA    1 
ATOM   1195  C  C     . SER A  1  153 ? 23.751 -22.579 -18.514 1.00 34.47  ?  185 SER A C     1 
ATOM   1196  O  O     . SER A  1  153 ? 22.727 -22.369 -19.163 1.00 34.31  ?  185 SER A O     1 
ATOM   1197  C  CB    . SER A  1  153 ? 25.526 -24.292 -18.807 1.00 36.93  ?  185 SER A CB    1 
ATOM   1198  O  OG    . SER A  1  153 ? 24.425 -25.139 -18.544 1.00 39.86  ?  185 SER A OG    1 
ATOM   1199  N  N     . THR A  1  154 ? 23.818 -22.506 -17.171 1.00 33.52  ?  186 THR A N     1 
ATOM   1200  C  CA    . THR A  1  154 ? 22.602 -22.303 -16.333 1.00 31.72  ?  186 THR A CA    1 
ATOM   1201  C  C     . THR A  1  154 ? 22.054 -20.910 -16.495 1.00 29.66  ?  186 THR A C     1 
ATOM   1202  O  O     . THR A  1  154 ? 20.843 -20.699 -16.385 1.00 27.97  ?  186 THR A O     1 
ATOM   1203  C  CB    . THR A  1  154 ? 22.775 -22.558 -14.797 1.00 31.49  ?  186 THR A CB    1 
ATOM   1204  O  OG1   . THR A  1  154 ? 24.144 -22.419 -14.393 1.00 32.47  ?  186 THR A OG1   1 
ATOM   1205  C  CG2   . THR A  1  154 ? 22.269 -23.930 -14.409 1.00 31.35  ?  186 THR A CG2   1 
ATOM   1206  N  N     . LEU A  1  155 ? 22.945 -19.960 -16.744 1.00 28.62  ?  187 LEU A N     1 
ATOM   1207  C  CA    . LEU A  1  155 ? 22.519 -18.603 -17.016 1.00 30.00  ?  187 LEU A CA    1 
ATOM   1208  C  C     . LEU A  1  155 ? 21.375 -18.528 -18.047 1.00 31.90  ?  187 LEU A C     1 
ATOM   1209  O  O     . LEU A  1  155 ? 20.351 -17.933 -17.765 1.00 32.58  ?  187 LEU A O     1 
ATOM   1210  C  CB    . LEU A  1  155 ? 23.713 -17.784 -17.465 1.00 29.97  ?  187 LEU A CB    1 
ATOM   1211  C  CG    . LEU A  1  155 ? 23.490 -16.280 -17.561 1.00 30.46  ?  187 LEU A CG    1 
ATOM   1212  C  CD1   . LEU A  1  155 ? 22.617 -15.738 -16.444 1.00 30.37  ?  187 LEU A CD1   1 
ATOM   1213  C  CD2   . LEU A  1  155 ? 24.837 -15.574 -17.586 1.00 30.63  ?  187 LEU A CD2   1 
ATOM   1214  N  N     . ARG A  1  156 ? 21.530 -19.177 -19.204 1.00 34.18  ?  188 ARG A N     1 
ATOM   1215  C  CA    . ARG A  1  156 ? 20.469 -19.262 -20.235 1.00 35.64  ?  188 ARG A CA    1 
ATOM   1216  C  C     . ARG A  1  156 ? 19.258 -20.105 -19.849 1.00 35.60  ?  188 ARG A C     1 
ATOM   1217  O  O     . ARG A  1  156 ? 18.198 -19.951 -20.435 1.00 36.20  ?  188 ARG A O     1 
ATOM   1218  C  CB    . ARG A  1  156 ? 20.966 -19.929 -21.515 1.00 38.98  ?  188 ARG A CB    1 
ATOM   1219  C  CG    . ARG A  1  156 ? 22.365 -19.569 -22.007 1.00 41.85  ?  188 ARG A CG    1 
ATOM   1220  C  CD    . ARG A  1  156 ? 22.838 -20.582 -23.055 1.00 41.16  ?  188 ARG A CD    1 
ATOM   1221  N  NE    . ARG A  1  156 ? 24.201 -20.346 -23.512 1.00 38.98  ?  188 ARG A NE    1 
ATOM   1222  C  CZ    . ARG A  1  156 ? 24.598 -19.302 -24.237 1.00 38.31  ?  188 ARG A CZ    1 
ATOM   1223  N  NH1   . ARG A  1  156 ? 23.762 -18.331 -24.616 1.00 37.13  1  188 ARG A NH1   1 
ATOM   1224  N  NH2   . ARG A  1  156 ? 25.867 -19.223 -24.580 1.00 40.00  ?  188 ARG A NH2   1 
ATOM   1225  N  N     . LYS A  1  157 ? 19.439 -21.063 -18.949 1.00 35.49  ?  189 LYS A N     1 
ATOM   1226  C  CA    . LYS A  1  157 ? 18.340 -21.925 -18.507 1.00 37.20  ?  189 LYS A CA    1 
ATOM   1227  C  C     . LYS A  1  157 ? 17.287 -21.165 -17.647 1.00 37.50  ?  189 LYS A C     1 
ATOM   1228  O  O     . LYS A  1  157 ? 16.069 -21.307 -17.869 1.00 34.59  ?  189 LYS A O     1 
ATOM   1229  C  CB    . LYS A  1  157 ? 18.887 -23.131 -17.711 1.00 40.29  ?  189 LYS A CB    1 
ATOM   1230  C  CG    . LYS A  1  157 ? 19.141 -24.439 -18.468 1.00 41.24  ?  189 LYS A CG    1 
ATOM   1231  C  CD    . LYS A  1  157 ? 20.323 -24.376 -19.424 1.00 44.61  ?  189 LYS A CD    1 
ATOM   1232  C  CE    . LYS A  1  157 ? 19.865 -24.186 -20.885 1.00 48.38  ?  189 LYS A CE    1 
ATOM   1233  N  NZ    . LYS A  1  157 ? 20.891 -23.640 -21.836 1.00 47.95  1  189 LYS A NZ    1 
ATOM   1234  N  N     . GLY A  1  158 ? 17.759 -20.386 -16.659 1.00 37.57  ?  190 GLY A N     1 
ATOM   1235  C  CA    . GLY A  1  158 ? 16.863 -19.694 -15.703 1.00 34.95  ?  190 GLY A CA    1 
ATOM   1236  C  C     . GLY A  1  158 ? 17.351 -18.413 -15.040 1.00 33.25  ?  190 GLY A C     1 
ATOM   1237  O  O     . GLY A  1  158 ? 16.834 -18.025 -14.008 1.00 31.55  ?  190 GLY A O     1 
ATOM   1238  N  N     . GLY A  1  159 ? 18.332 -17.739 -15.627 1.00 32.82  ?  191 GLY A N     1 
ATOM   1239  C  CA    . GLY A  1  159 ? 18.832 -16.472 -15.076 1.00 32.08  ?  191 GLY A CA    1 
ATOM   1240  C  C     . GLY A  1  159 ? 19.850 -16.542 -13.936 1.00 31.60  ?  191 GLY A C     1 
ATOM   1241  O  O     . GLY A  1  159 ? 20.058 -15.551 -13.223 1.00 30.23  ?  191 GLY A O     1 
ATOM   1242  N  N     . PHE A  1  160 ? 20.515 -17.684 -13.768 1.00 30.65  ?  192 PHE A N     1 
ATOM   1243  C  CA    . PHE A  1  160 ? 21.469 -17.829 -12.681 1.00 28.80  ?  192 PHE A CA    1 
ATOM   1244  C  C     . PHE A  1  160 ? 22.686 -18.690 -12.980 1.00 29.32  ?  192 PHE A C     1 
ATOM   1245  O  O     . PHE A  1  160 ? 22.700 -19.462 -13.925 1.00 31.54  ?  192 PHE A O     1 
ATOM   1246  C  CB    . PHE A  1  160 ? 20.750 -18.361 -11.467 1.00 27.26  ?  192 PHE A CB    1 
ATOM   1247  C  CG    . PHE A  1  160 ? 20.107 -19.697 -11.658 1.00 26.87  ?  192 PHE A CG    1 
ATOM   1248  C  CD1   . PHE A  1  160 ? 20.839 -20.861 -11.504 1.00 27.21  ?  192 PHE A CD1   1 
ATOM   1249  C  CD2   . PHE A  1  160 ? 18.744 -19.798 -11.893 1.00 26.83  ?  192 PHE A CD2   1 
ATOM   1250  C  CE1   . PHE A  1  160 ? 20.222 -22.102 -11.611 1.00 26.97  ?  192 PHE A CE1   1 
ATOM   1251  C  CE2   . PHE A  1  160 ? 18.124 -21.032 -11.997 1.00 26.42  ?  192 PHE A CE2   1 
ATOM   1252  C  CZ    . PHE A  1  160 ? 18.862 -22.185 -11.860 1.00 26.43  ?  192 PHE A CZ    1 
ATOM   1253  N  N     . TYR A  1  161 ? 23.711 -18.548 -12.150 1.00 29.19  ?  193 TYR A N     1 
ATOM   1254  C  CA    . TYR A  1  161 ? 24.957 -19.280 -12.316 1.00 29.43  ?  193 TYR A CA    1 
ATOM   1255  C  C     . TYR A  1  161 ? 25.739 -19.191 -11.033 1.00 29.75  ?  193 TYR A C     1 
ATOM   1256  O  O     . TYR A  1  161 ? 25.347 -18.477 -10.134 1.00 30.03  ?  193 TYR A O     1 
ATOM   1257  C  CB    . TYR A  1  161 ? 25.794 -18.651 -13.424 1.00 29.73  ?  193 TYR A CB    1 
ATOM   1258  C  CG    . TYR A  1  161 ? 26.272 -17.251 -13.092 1.00 29.56  ?  193 TYR A CG    1 
ATOM   1259  C  CD1   . TYR A  1  161 ? 25.465 -16.146 -13.317 1.00 29.19  ?  193 TYR A CD1   1 
ATOM   1260  C  CD2   . TYR A  1  161 ? 27.512 -17.035 -12.539 1.00 30.05  ?  193 TYR A CD2   1 
ATOM   1261  C  CE1   . TYR A  1  161 ? 25.886 -14.866 -13.018 1.00 27.86  ?  193 TYR A CE1   1 
ATOM   1262  C  CE2   . TYR A  1  161 ? 27.936 -15.751 -12.230 1.00 30.23  ?  193 TYR A CE2   1 
ATOM   1263  C  CZ    . TYR A  1  161 ? 27.113 -14.671 -12.470 1.00 28.52  ?  193 TYR A CZ    1 
ATOM   1264  O  OH    . TYR A  1  161 ? 27.539 -13.402 -12.161 1.00 27.93  ?  193 TYR A OH    1 
ATOM   1265  N  N     . SER A  1  162 ? 26.858 -19.898 -10.967 1.00 30.55  ?  194 SER A N     1 
ATOM   1266  C  CA    . SER A  1  162 ? 27.781 -19.794 -9.838  1.00 31.21  ?  194 SER A CA    1 
ATOM   1267  C  C     . SER A  1  162 ? 29.171 -19.914 -10.379 1.00 31.27  ?  194 SER A C     1 
ATOM   1268  O  O     . SER A  1  162 ? 29.381 -20.554 -11.394 1.00 32.08  ?  194 SER A O     1 
ATOM   1269  C  CB    . SER A  1  162 ? 27.582 -20.925 -8.842  1.00 31.87  ?  194 SER A CB    1 
ATOM   1270  O  OG    . SER A  1  162 ? 28.427 -22.015 -9.178  1.00 31.47  ?  194 SER A OG    1 
ATOM   1271  N  N     . GLN A  1  163 ? 30.145 -19.363 -9.685  1.00 31.84  ?  195 GLN A N     1 
ATOM   1272  C  CA    . GLN A  1  163 ? 31.409 -19.150 -10.339 1.00 33.17  ?  195 GLN A CA    1 
ATOM   1273  C  C     . GLN A  1  163 ? 32.534 -18.919 -9.359  1.00 33.29  ?  195 GLN A C     1 
ATOM   1274  O  O     . GLN A  1  163 ? 32.447 -18.041 -8.515  1.00 35.22  ?  195 GLN A O     1 
ATOM   1275  C  CB    . GLN A  1  163 ? 31.252 -17.929 -11.252 1.00 34.41  ?  195 GLN A CB    1 
ATOM   1276  C  CG    . GLN A  1  163 ? 32.488 -17.527 -12.038 1.00 36.04  ?  195 GLN A CG    1 
ATOM   1277  C  CD    . GLN A  1  163 ? 32.906 -18.564 -13.051 1.00 36.31  ?  195 GLN A CD    1 
ATOM   1278  O  OE1   . GLN A  1  163 ? 32.061 -19.248 -13.652 1.00 37.42  ?  195 GLN A OE1   1 
ATOM   1279  N  NE2   . GLN A  1  163 ? 34.211 -18.683 -13.259 1.00 35.97  ?  195 GLN A NE2   1 
ATOM   1280  N  N     . LYS A  1  164 ? 33.601 -19.693 -9.496  1.00 33.15  ?  196 LYS A N     1 
ATOM   1281  C  CA    . LYS A  1  164 ? 34.802 -19.468 -8.723  1.00 33.21  ?  196 LYS A CA    1 
ATOM   1282  C  C     . LYS A  1  164 ? 35.354 -18.166 -9.195  1.00 31.19  ?  196 LYS A C     1 
ATOM   1283  O  O     . LYS A  1  164 ? 35.214 -17.837 -10.349 1.00 29.82  ?  196 LYS A O     1 
ATOM   1284  C  CB    . LYS A  1  164 ? 35.823 -20.583 -8.961  1.00 37.09  ?  196 LYS A CB    1 
ATOM   1285  C  CG    . LYS A  1  164 ? 35.385 -21.941 -8.399  1.00 41.54  ?  196 LYS A CG    1 
ATOM   1286  C  CD    . LYS A  1  164 ? 36.247 -23.133 -8.855  1.00 43.26  ?  196 LYS A CD    1 
ATOM   1287  C  CE    . LYS A  1  164 ? 35.756 -23.771 -10.154 1.00 43.37  ?  196 LYS A CE    1 
ATOM   1288  N  NZ    . LYS A  1  164 ? 35.824 -25.250 -10.036 1.00 43.01  1  196 LYS A NZ    1 
ATOM   1289  N  N     . VAL A  1  165 ? 35.965 -17.412 -8.303  1.00 32.47  ?  197 VAL A N     1 
ATOM   1290  C  CA    . VAL A  1  165 ? 36.554 -16.150 -8.691  1.00 34.81  ?  197 VAL A CA    1 
ATOM   1291  C  C     . VAL A  1  165 ? 37.936 -16.433 -9.234  1.00 36.50  ?  197 VAL A C     1 
ATOM   1292  O  O     . VAL A  1  165 ? 38.750 -17.085 -8.569  1.00 34.97  ?  197 VAL A O     1 
ATOM   1293  C  CB    . VAL A  1  165 ? 36.706 -15.194 -7.498  1.00 36.40  ?  197 VAL A CB    1 
ATOM   1294  C  CG1   . VAL A  1  165 ? 37.336 -13.879 -7.940  1.00 37.47  ?  197 VAL A CG1   1 
ATOM   1295  C  CG2   . VAL A  1  165 ? 35.366 -14.931 -6.848  1.00 37.16  ?  197 VAL A CG2   1 
ATOM   1296  N  N     . THR A  1  166 ? 38.207 -15.928 -10.433 1.00 39.02  ?  198 THR A N     1 
ATOM   1297  C  CA    . THR A  1  166 ? 39.532 -16.065 -11.040 1.00 39.58  ?  198 THR A CA    1 
ATOM   1298  C  C     . THR A  1  166 ? 40.593 -15.823 -9.975  1.00 38.69  ?  198 THR A C     1 
ATOM   1299  O  O     . THR A  1  166 ? 41.314 -16.732 -9.638  1.00 41.29  ?  198 THR A O     1 
ATOM   1300  C  CB    . THR A  1  166 ? 39.726 -15.101 -12.242 1.00 39.04  ?  198 THR A CB    1 
ATOM   1301  O  OG1   . THR A  1  166 ? 39.062 -15.645 -13.386 1.00 34.35  ?  198 THR A OG1   1 
ATOM   1302  C  CG2   . THR A  1  166 ? 41.231 -14.848 -12.570 1.00 38.11  ?  198 THR A CG2   1 
ATOM   1303  N  N     . THR A  1  167 ? 40.646 -14.627 -9.408  1.00 37.38  ?  199 THR A N     1 
ATOM   1304  C  CA    . THR A  1  167 ? 41.759 -14.267 -8.522  1.00 38.23  ?  199 THR A CA    1 
ATOM   1305  C  C     . THR A  1  167 ? 41.707 -14.854 -7.109  1.00 34.45  ?  199 THR A C     1 
ATOM   1306  O  O     . THR A  1  167 ? 42.547 -14.498 -6.293  1.00 29.87  ?  199 THR A O     1 
ATOM   1307  C  CB    . THR A  1  167 ? 41.901 -12.728 -8.379  1.00 41.07  ?  199 THR A CB    1 
ATOM   1308  O  OG1   . THR A  1  167 ? 40.739 -12.176 -7.738  1.00 44.25  ?  199 THR A OG1   1 
ATOM   1309  C  CG2   . THR A  1  167 ? 42.075 -12.085 -9.739  1.00 40.70  ?  199 THR A CG2   1 
ATOM   1310  N  N     . ASN A  1  168 ? 40.747 -15.696 -6.819  1.00 32.97  ?  200 ASN A N     1 
ATOM   1311  C  CA    . ASN A  1  168 ? 40.607 -16.294 -5.518  1.00 35.77  ?  200 ASN A CA    1 
ATOM   1312  C  C     . ASN A  1  168 ? 39.746 -17.426 -5.921  1.00 40.50  ?  200 ASN A C     1 
ATOM   1313  O  O     . ASN A  1  168 ? 38.560 -17.303 -5.993  1.00 44.48  ?  200 ASN A O     1 
ATOM   1314  C  CB    . ASN A  1  168 ? 39.821 -15.388 -4.594  1.00 35.39  ?  200 ASN A CB    1 
ATOM   1315  C  CG    . ASN A  1  168 ? 40.466 -14.060 -4.367  1.00 35.34  ?  200 ASN A CG    1 
ATOM   1316  O  OD1   . ASN A  1  168 ? 41.253 -13.886 -3.461  1.00 36.30  ?  200 ASN A OD1   1 
ATOM   1317  N  ND2   . ASN A  1  168 ? 40.077 -13.103 -5.141  1.00 34.64  ?  200 ASN A ND2   1 
ATOM   1318  N  N     . PRO A  1  169 ? 40.307 -18.557 -6.230  1.00 42.84  ?  201 PRO A N     1 
ATOM   1319  C  CA    . PRO A  1  169 ? 39.431 -19.597 -6.787  1.00 42.41  ?  201 PRO A CA    1 
ATOM   1320  C  C     . PRO A  1  169 ? 38.788 -20.578 -5.810  1.00 41.34  ?  201 PRO A C     1 
ATOM   1321  O  O     . PRO A  1  169 ? 38.177 -21.549 -6.264  1.00 42.20  ?  201 PRO A O     1 
ATOM   1322  C  CB    . PRO A  1  169 ? 40.344 -20.338 -7.763  1.00 44.35  ?  201 PRO A CB    1 
ATOM   1323  C  CG    . PRO A  1  169 ? 41.628 -19.548 -7.805  1.00 45.11  ?  201 PRO A CG    1 
ATOM   1324  C  CD    . PRO A  1  169 ? 41.719 -18.795 -6.522  1.00 43.87  ?  201 PRO A CD    1 
ATOM   1325  N  N     . ASN A  1  170 ? 38.928 -20.358 -4.502  1.00 40.92  ?  202 ASN A N     1 
ATOM   1326  C  CA    . ASN A  1  170 ? 38.113 -21.093 -3.510  1.00 41.69  ?  202 ASN A CA    1 
ATOM   1327  C  C     . ASN A  1  170 ? 37.017 -20.199 -2.924  1.00 41.84  ?  202 ASN A C     1 
ATOM   1328  O  O     . ASN A  1  170 ? 36.330 -20.561 -1.965  1.00 44.08  ?  202 ASN A O     1 
ATOM   1329  C  CB    . ASN A  1  170 ? 38.977 -21.697 -2.407  1.00 41.18  ?  202 ASN A CB    1 
ATOM   1330  C  CG    . ASN A  1  170 ? 39.879 -20.680 -1.763  1.00 41.18  ?  202 ASN A CG    1 
ATOM   1331  O  OD1   . ASN A  1  170 ? 40.311 -19.720 -2.411  1.00 38.92  ?  202 ASN A OD1   1 
ATOM   1332  N  ND2   . ASN A  1  170 ? 40.177 -20.883 -0.484  1.00 41.90  ?  202 ASN A ND2   1 
ATOM   1333  N  N     . LEU A  1  171 ? 36.869 -19.026 -3.529  1.00 40.30  ?  203 LEU A N     1 
ATOM   1334  C  CA    . LEU A  1  171 ? 35.717 -18.178 -3.345  1.00 37.75  ?  203 LEU A CA    1 
ATOM   1335  C  C     . LEU A  1  171 ? 34.783 -18.409 -4.520  1.00 36.47  ?  203 LEU A C     1 
ATOM   1336  O  O     . LEU A  1  171 ? 35.177 -18.187 -5.662  1.00 36.12  ?  203 LEU A O     1 
ATOM   1337  C  CB    . LEU A  1  171 ? 36.168 -16.721 -3.350  1.00 36.71  ?  203 LEU A CB    1 
ATOM   1338  C  CG    . LEU A  1  171 ? 35.071 -15.714 -3.064  1.00 36.35  ?  203 LEU A CG    1 
ATOM   1339  C  CD1   . LEU A  1  171 ? 34.428 -16.064 -1.734  1.00 36.47  ?  203 LEU A CD1   1 
ATOM   1340  C  CD2   . LEU A  1  171 ? 35.620 -14.297 -3.066  1.00 35.39  ?  203 LEU A CD2   1 
ATOM   1341  N  N     . ARG A  1  172 ? 33.557 -18.845 -4.256  1.00 34.89  ?  204 ARG A N     1 
ATOM   1342  C  CA    . ARG A  1  172 ? 32.559 -18.973 -5.325  1.00 33.91  ?  204 ARG A CA    1 
ATOM   1343  C  C     . ARG A  1  172 ? 31.398 -17.992 -5.190  1.00 29.93  ?  204 ARG A C     1 
ATOM   1344  O  O     . ARG A  1  172 ? 30.636 -18.048 -4.238  1.00 29.32  ?  204 ARG A O     1 
ATOM   1345  C  CB    . ARG A  1  172 ? 31.986 -20.390 -5.374  1.00 36.82  ?  204 ARG A CB    1 
ATOM   1346  C  CG    . ARG A  1  172 ? 30.774 -20.557 -6.305  1.00 39.31  ?  204 ARG A CG    1 
ATOM   1347  C  CD    . ARG A  1  172 ? 30.085 -21.902 -6.078  1.00 41.55  ?  204 ARG A CD    1 
ATOM   1348  N  NE    . ARG A  1  172 ? 31.028 -23.025 -6.085  1.00 42.45  ?  204 ARG A NE    1 
ATOM   1349  C  CZ    . ARG A  1  172 ? 31.564 -23.558 -7.182  1.00 42.71  ?  204 ARG A CZ    1 
ATOM   1350  N  NH1   . ARG A  1  172 ? 31.269 -23.093 -8.393  1.00 44.09  1  204 ARG A NH1   1 
ATOM   1351  N  NH2   . ARG A  1  172 ? 32.416 -24.558 -7.067  1.00 42.91  ?  204 ARG A NH2   1 
ATOM   1352  N  N     . ILE A  1  173 ? 31.236 -17.137 -6.184  1.00 26.30  ?  205 ILE A N     1 
ATOM   1353  C  CA    . ILE A  1  173 ? 30.107 -16.259 -6.230  1.00 25.29  ?  205 ILE A CA    1 
ATOM   1354  C  C     . ILE A  1  173 ? 28.940 -17.071 -6.724  1.00 24.73  ?  205 ILE A C     1 
ATOM   1355  O  O     . ILE A  1  173 ? 29.040 -17.696 -7.768  1.00 24.96  ?  205 ILE A O     1 
ATOM   1356  C  CB    . ILE A  1  173 ? 30.320 -15.107 -7.225  1.00 26.08  ?  205 ILE A CB    1 
ATOM   1357  C  CG1   . ILE A  1  173 ? 31.607 -14.308 -6.918  1.00 26.53  ?  205 ILE A CG1   1 
ATOM   1358  C  CG2   . ILE A  1  173 ? 29.110 -14.187 -7.223  1.00 26.16  ?  205 ILE A CG2   1 
ATOM   1359  C  CD1   . ILE A  1  173 ? 31.727 -13.756 -5.500  1.00 26.13  ?  205 ILE A CD1   1 
ATOM   1360  N  N     . ILE A  1  174 ? 27.845 -17.068 -5.968  1.00 24.35  ?  206 ILE A N     1 
ATOM   1361  C  CA    . ILE A  1  174 ? 26.549 -17.617 -6.418  1.00 23.60  ?  206 ILE A CA    1 
ATOM   1362  C  C     . ILE A  1  174 ? 25.590 -16.474 -6.800  1.00 22.80  ?  206 ILE A C     1 
ATOM   1363  O  O     . ILE A  1  174 ? 25.025 -15.830 -5.929  1.00 22.93  ?  206 ILE A O     1 
ATOM   1364  C  CB    . ILE A  1  174 ? 25.864 -18.465 -5.312  1.00 23.11  ?  206 ILE A CB    1 
ATOM   1365  C  CG1   . ILE A  1  174 ? 26.700 -19.690 -4.953  1.00 22.76  ?  206 ILE A CG1   1 
ATOM   1366  C  CG2   . ILE A  1  174 ? 24.458 -18.895 -5.727  1.00 23.03  ?  206 ILE A CG2   1 
ATOM   1367  C  CD1   . ILE A  1  174 ? 26.080 -20.535 -3.853  1.00 22.15  ?  206 ILE A CD1   1 
ATOM   1368  N  N     . SER A  1  175 ? 25.399 -16.234 -8.095  1.00 22.48  ?  207 SER A N     1 
ATOM   1369  C  CA    . SER A  1  175 ? 24.443 -15.230 -8.564  1.00 22.13  ?  207 SER A CA    1 
ATOM   1370  C  C     . SER A  1  175 ? 23.058 -15.836 -8.746  1.00 22.32  ?  207 SER A C     1 
ATOM   1371  O  O     . SER A  1  175 ? 22.867 -16.698 -9.584  1.00 21.35  ?  207 SER A O     1 
ATOM   1372  C  CB    . SER A  1  175 ? 24.896 -14.594 -9.884  1.00 22.02  ?  207 SER A CB    1 
ATOM   1373  O  OG    . SER A  1  175 ? 23.894 -13.714 -10.398 1.00 21.57  ?  207 SER A OG    1 
ATOM   1374  N  N     . LEU A  1  176 ? 22.094 -15.348 -7.967  1.00 23.95  ?  208 LEU A N     1 
ATOM   1375  C  CA    . LEU A  1  176 ? 20.717 -15.830 -8.009  1.00 24.23  ?  208 LEU A CA    1 
ATOM   1376  C  C     . LEU A  1  176 ? 19.773 -14.890 -8.716  1.00 24.08  ?  208 LEU A C     1 
ATOM   1377  O  O     . LEU A  1  176 ? 19.890 -13.641 -8.689  1.00 23.76  ?  208 LEU A O     1 
ATOM   1378  C  CB    . LEU A  1  176 ? 20.162 -16.041 -6.607  1.00 25.23  ?  208 LEU A CB    1 
ATOM   1379  C  CG    . LEU A  1  176 ? 20.757 -17.154 -5.734  1.00 26.80  ?  208 LEU A CG    1 
ATOM   1380  C  CD1   . LEU A  1  176 ? 20.330 -16.891 -4.295  1.00 27.26  ?  208 LEU A CD1   1 
ATOM   1381  C  CD2   . LEU A  1  176 ? 20.340 -18.561 -6.165  1.00 26.43  ?  208 LEU A CD2   1 
ATOM   1382  N  N     . ASN A  1  177 ? 18.801 -15.523 -9.344  1.00 24.17  ?  209 ASN A N     1 
ATOM   1383  C  CA    . ASN A  1  177 ? 17.706 -14.804 -9.911  1.00 24.39  ?  209 ASN A CA    1 
ATOM   1384  C  C     . ASN A  1  177 ? 16.586 -14.926 -8.934  1.00 22.83  ?  209 ASN A C     1 
ATOM   1385  O  O     . ASN A  1  177 ? 15.822 -15.892 -8.966  1.00 22.14  ?  209 ASN A O     1 
ATOM   1386  C  CB    . ASN A  1  177 ? 17.298 -15.377 -11.247 1.00 25.52  ?  209 ASN A CB    1 
ATOM   1387  C  CG    . ASN A  1  177 ? 16.118 -14.654 -11.832 1.00 26.46  ?  209 ASN A CG    1 
ATOM   1388  O  OD1   . ASN A  1  177 ? 15.546 -13.762 -11.209 1.00 27.17  ?  209 ASN A OD1   1 
ATOM   1389  N  ND2   . ASN A  1  177 ? 15.737 -15.041 -13.027 1.00 27.73  ?  209 ASN A ND2   1 
ATOM   1390  N  N     . THR A  1  178 ? 16.511 -13.930 -8.060  1.00 21.44  ?  210 THR A N     1 
ATOM   1391  C  CA    . THR A  1  178 ? 15.487 -13.880 -7.056  1.00 20.47  ?  210 THR A CA    1 
ATOM   1392  C  C     . THR A  1  178 ? 14.281 -13.164 -7.623  1.00 21.27  ?  210 THR A C     1 
ATOM   1393  O  O     . THR A  1  178 ? 13.227 -13.143 -6.985  1.00 23.67  ?  210 THR A O     1 
ATOM   1394  C  CB    . THR A  1  178 ? 15.993 -13.208 -5.779  1.00 19.65  ?  210 THR A CB    1 
ATOM   1395  O  OG1   . THR A  1  178 ? 16.764 -12.038 -6.102  1.00 19.18  ?  210 THR A OG1   1 
ATOM   1396  C  CG2   . THR A  1  178 ? 16.870 -14.187 -5.035  1.00 19.53  ?  210 THR A CG2   1 
ATOM   1397  N  N     . ASN A  1  179 ? 14.404 -12.621 -8.835  1.00 19.80  ?  211 ASN A N     1 
ATOM   1398  C  CA    . ASN A  1  179 ? 13.250 -12.067 -9.502  1.00 19.36  ?  211 ASN A CA    1 
ATOM   1399  C  C     . ASN A  1  179 ? 12.202 -13.144 -9.743  1.00 19.84  ?  211 ASN A C     1 
ATOM   1400  O  O     . ASN A  1  179 ? 11.013 -12.847 -9.921  1.00 19.44  ?  211 ASN A O     1 
ATOM   1401  C  CB    . ASN A  1  179 ? 13.648 -11.438 -10.819 1.00 19.22  ?  211 ASN A CB    1 
ATOM   1402  C  CG    . ASN A  1  179 ? 14.783 -10.453 -10.676 1.00 18.93  ?  211 ASN A CG    1 
ATOM   1403  O  OD1   . ASN A  1  179 ? 15.847 -10.615 -11.251 1.00 18.87  ?  211 ASN A OD1   1 
ATOM   1404  N  ND2   . ASN A  1  179 ? 14.553 -9.421  -9.917  1.00 18.94  ?  211 ASN A ND2   1 
ATOM   1405  N  N     . LEU A  1  180 ? 12.651 -14.393 -9.745  1.00 20.94  ?  212 LEU A N     1 
ATOM   1406  C  CA    . LEU A  1  180 ? 11.749 -15.547 -9.841  1.00 23.08  ?  212 LEU A CA    1 
ATOM   1407  C  C     . LEU A  1  180 ? 10.771 -15.559 -8.665  1.00 24.09  ?  212 LEU A C     1 
ATOM   1408  O  O     . LEU A  1  180 ? 9.658  -16.113 -8.785  1.00 26.87  ?  212 LEU A O     1 
ATOM   1409  C  CB    . LEU A  1  180 ? 12.532 -16.886 -9.901  1.00 23.21  ?  212 LEU A CB    1 
ATOM   1410  C  CG    . LEU A  1  180 ? 13.540 -16.958 -11.073 1.00 23.59  ?  212 LEU A CG    1 
ATOM   1411  C  CD1   . LEU A  1  180 ? 14.499 -18.132 -10.993 1.00 23.34  ?  212 LEU A CD1   1 
ATOM   1412  C  CD2   . LEU A  1  180 ? 12.823 -16.950 -12.419 1.00 23.59  ?  212 LEU A CD2   1 
ATOM   1413  N  N     . TYR A  1  181 ? 11.179 -14.937 -7.550  1.00 22.16  ?  213 TYR A N     1 
ATOM   1414  C  CA    . TYR A  1  181 ? 10.426 -14.954 -6.319  1.00 20.31  ?  213 TYR A CA    1 
ATOM   1415  C  C     . TYR A  1  181 ? 9.701  -13.678 -6.047  1.00 17.70  ?  213 TYR A C     1 
ATOM   1416  O  O     . TYR A  1  181 ? 9.023  -13.560 -5.062  1.00 16.08  ?  213 TYR A O     1 
ATOM   1417  C  CB    . TYR A  1  181 ? 11.387 -15.244 -5.193  1.00 22.43  ?  213 TYR A CB    1 
ATOM   1418  C  CG    . TYR A  1  181 ? 12.208 -16.489 -5.453  1.00 25.15  ?  213 TYR A CG    1 
ATOM   1419  C  CD1   . TYR A  1  181 ? 11.595 -17.679 -5.861  1.00 25.89  ?  213 TYR A CD1   1 
ATOM   1420  C  CD2   . TYR A  1  181 ? 13.592 -16.481 -5.297  1.00 26.22  ?  213 TYR A CD2   1 
ATOM   1421  C  CE1   . TYR A  1  181 ? 12.339 -18.810 -6.102  1.00 27.65  ?  213 TYR A CE1   1 
ATOM   1422  C  CE2   . TYR A  1  181 ? 14.345 -17.621 -5.531  1.00 27.42  ?  213 TYR A CE2   1 
ATOM   1423  C  CZ    . TYR A  1  181 ? 13.712 -18.776 -5.936  1.00 28.56  ?  213 TYR A CZ    1 
ATOM   1424  O  OH    . TYR A  1  181 ? 14.437 -19.909 -6.189  1.00 30.59  ?  213 TYR A OH    1 
ATOM   1425  N  N     . TYR A  1  182 ? 9.826  -12.723 -6.946  1.00 17.01  ?  214 TYR A N     1 
ATOM   1426  C  CA    . TYR A  1  182 ? 9.213  -11.419 -6.773  1.00 17.05  ?  214 TYR A CA    1 
ATOM   1427  C  C     . TYR A  1  182 ? 7.727  -11.475 -7.007  1.00 17.47  ?  214 TYR A C     1 
ATOM   1428  O  O     . TYR A  1  182 ? 7.271  -12.144 -7.920  1.00 17.48  ?  214 TYR A O     1 
ATOM   1429  C  CB    . TYR A  1  182 ? 9.838  -10.463 -7.759  1.00 17.21  ?  214 TYR A CB    1 
ATOM   1430  C  CG    . TYR A  1  182 ? 9.526  -8.993  -7.592  1.00 17.42  ?  214 TYR A CG    1 
ATOM   1431  C  CD1   . TYR A  1  182 ? 9.382  -8.418  -6.349  1.00 16.93  ?  214 TYR A CD1   1 
ATOM   1432  C  CD2   . TYR A  1  182 ? 9.460  -8.161  -8.727  1.00 18.22  ?  214 TYR A CD2   1 
ATOM   1433  C  CE1   . TYR A  1  182 ? 9.130  -7.076  -6.232  1.00 17.51  ?  214 TYR A CE1   1 
ATOM   1434  C  CE2   . TYR A  1  182 ? 9.200  -6.816  -8.622  1.00 17.90  ?  214 TYR A CE2   1 
ATOM   1435  C  CZ    . TYR A  1  182 ? 9.039  -6.283  -7.368  1.00 18.00  ?  214 TYR A CZ    1 
ATOM   1436  O  OH    . TYR A  1  182 ? 8.798  -4.939  -7.251  1.00 19.18  ?  214 TYR A OH    1 
ATOM   1437  N  N     . GLY A  1  183 ? 6.978  -10.771 -6.167  1.00 18.61  ?  215 GLY A N     1 
ATOM   1438  C  CA    . GLY A  1  183 ? 5.500  -10.751 -6.206  1.00 18.87  ?  215 GLY A CA    1 
ATOM   1439  C  C     . GLY A  1  183 ? 4.905  -10.613 -7.590  1.00 19.21  ?  215 GLY A C     1 
ATOM   1440  O  O     . GLY A  1  183 ? 4.326  -11.570 -8.097  1.00 19.31  ?  215 GLY A O     1 
ATOM   1441  N  N     . PRO A  1  184 ? 5.092  -9.449  -8.240  1.00 20.00  ?  216 PRO A N     1 
ATOM   1442  C  CA    . PRO A  1  184 ? 4.540  -9.193  -9.592  1.00 20.77  ?  216 PRO A CA    1 
ATOM   1443  C  C     . PRO A  1  184 ? 4.874  -10.196 -10.702 1.00 21.78  ?  216 PRO A C     1 
ATOM   1444  O  O     . PRO A  1  184 ? 4.428  -9.987  -11.840 1.00 22.50  ?  216 PRO A O     1 
ATOM   1445  C  CB    . PRO A  1  184 ? 5.146  -7.842  -9.979  1.00 20.08  ?  216 PRO A CB    1 
ATOM   1446  C  CG    . PRO A  1  184 ? 5.488  -7.202  -8.684  1.00 19.97  ?  216 PRO A CG    1 
ATOM   1447  C  CD    . PRO A  1  184 ? 5.859  -8.297  -7.736  1.00 19.73  ?  216 PRO A CD    1 
ATOM   1448  N  N     . ASN A  1  185 ? 5.636  -11.247 -10.407 1.00 22.86  ?  217 ASN A N     1 
ATOM   1449  C  CA    . ASN A  1  185 ? 6.091  -12.153 -11.453 1.00 25.62  ?  217 ASN A CA    1 
ATOM   1450  C  C     . ASN A  1  185 ? 5.088  -13.251 -11.745 1.00 27.97  ?  217 ASN A C     1 
ATOM   1451  O  O     . ASN A  1  185 ? 5.090  -14.319 -11.096 1.00 28.33  ?  217 ASN A O     1 
ATOM   1452  C  CB    . ASN A  1  185 ? 7.439  -12.772 -11.105 1.00 26.86  ?  217 ASN A CB    1 
ATOM   1453  C  CG    . ASN A  1  185 ? 8.032  -13.554 -12.257 1.00 27.37  ?  217 ASN A CG    1 
ATOM   1454  O  OD1   . ASN A  1  185 ? 7.477  -13.584 -13.344 1.00 28.21  ?  217 ASN A OD1   1 
ATOM   1455  N  ND2   . ASN A  1  185 ? 9.178  -14.176 -12.025 1.00 28.48  ?  217 ASN A ND2   1 
ATOM   1456  N  N     . ILE A  1  186 ? 4.272  -12.995 -12.770 1.00 29.26  ?  218 ILE A N     1 
ATOM   1457  C  CA    . ILE A  1  186 ? 3.147  -13.854 -13.118 1.00 29.71  ?  218 ILE A CA    1 
ATOM   1458  C  C     . ILE A  1  186 ? 3.597  -15.241 -13.577 1.00 30.51  ?  218 ILE A C     1 
ATOM   1459  O  O     . ILE A  1  186 ? 2.878  -16.223 -13.377 1.00 29.77  ?  218 ILE A O     1 
ATOM   1460  C  CB    . ILE A  1  186 ? 2.287  -13.224 -14.220 1.00 29.86  ?  218 ILE A CB    1 
ATOM   1461  C  CG1   . ILE A  1  186 ? 1.785  -11.835 -13.804 1.00 31.47  ?  218 ILE A CG1   1 
ATOM   1462  C  CG2   . ILE A  1  186 ? 1.121  -14.132 -14.569 1.00 30.33  ?  218 ILE A CG2   1 
ATOM   1463  C  CD1   . ILE A  1  186 ? 0.671  -11.815 -12.771 1.00 33.38  ?  218 ILE A CD1   1 
ATOM   1464  N  N     . MET A  1  187 ? 4.786  -15.321 -14.172 1.00 31.88  ?  219 MET A N     1 
ATOM   1465  C  CA    . MET A  1  187 ? 5.344  -16.605 -14.623 1.00 34.52  ?  219 MET A CA    1 
ATOM   1466  C  C     . MET A  1  187 ? 5.388  -17.655 -13.517 1.00 34.52  ?  219 MET A C     1 
ATOM   1467  O  O     . MET A  1  187 ? 5.077  -18.811 -13.761 1.00 34.10  ?  219 MET A O     1 
ATOM   1468  C  CB    . MET A  1  187 ? 6.756  -16.417 -15.192 1.00 36.85  ?  219 MET A CB    1 
ATOM   1469  C  CG    . MET A  1  187 ? 6.840  -15.487 -16.399 1.00 39.80  ?  219 MET A CG    1 
ATOM   1470  S  SD    . MET A  1  187 ? 5.705  -15.973 -17.720 1.00 44.07  ?  219 MET A SD    1 
ATOM   1471  C  CE    . MET A  1  187 ? 4.218  -14.994 -17.390 1.00 43.75  ?  219 MET A CE    1 
ATOM   1472  N  N     . THR A  1  188 ? 5.731  -17.238 -12.299 1.00 35.19  ?  220 THR A N     1 
ATOM   1473  C  CA    . THR A  1  188 ? 6.056  -18.167 -11.229 1.00 34.62  ?  220 THR A CA    1 
ATOM   1474  C  C     . THR A  1  188 ? 4.956  -18.400 -10.200 1.00 33.55  ?  220 THR A C     1 
ATOM   1475  O  O     . THR A  1  188 ? 5.196  -19.056 -9.199  1.00 33.61  ?  220 THR A O     1 
ATOM   1476  C  CB    . THR A  1  188 ? 7.320  -17.692 -10.469 1.00 36.41  ?  220 THR A CB    1 
ATOM   1477  O  OG1   . THR A  1  188 ? 7.065  -16.427 -9.845  1.00 36.26  ?  220 THR A OG1   1 
ATOM   1478  C  CG2   . THR A  1  188 ? 8.519  -17.571 -11.421 1.00 36.88  ?  220 THR A CG2   1 
ATOM   1479  N  N     . LEU A  1  189 ? 3.755  -17.883 -10.410 1.00 34.22  ?  221 LEU A N     1 
ATOM   1480  C  CA    . LEU A  1  189 ? 2.672  -18.169 -9.451  1.00 34.92  ?  221 LEU A CA    1 
ATOM   1481  C  C     . LEU A  1  189 ? 2.495  -19.654 -9.223  1.00 39.01  ?  221 LEU A C     1 
ATOM   1482  O  O     . LEU A  1  189 ? 2.656  -20.463 -10.136 1.00 42.33  ?  221 LEU A O     1 
ATOM   1483  C  CB    . LEU A  1  189 ? 1.345  -17.589 -9.910  1.00 32.50  ?  221 LEU A CB    1 
ATOM   1484  C  CG    . LEU A  1  189 ? 1.234  -16.154 -9.411  1.00 32.17  ?  221 LEU A CG    1 
ATOM   1485  C  CD1   . LEU A  1  189 ? 0.525  -15.244 -10.402 1.00 32.64  ?  221 LEU A CD1   1 
ATOM   1486  C  CD2   . LEU A  1  189 ? 0.542  -16.142 -8.068  1.00 31.32  ?  221 LEU A CD2   1 
ATOM   1487  N  N     . ASN A  1  190 ? 2.190  -20.008 -7.982  1.00 41.20  ?  222 ASN A N     1 
ATOM   1488  C  CA    . ASN A  1  190 ? 1.860  -21.378 -7.615  1.00 42.22  ?  222 ASN A CA    1 
ATOM   1489  C  C     . ASN A  1  190 ? 2.943  -22.435 -7.902  1.00 39.97  ?  222 ASN A C     1 
ATOM   1490  O  O     . ASN A  1  190 ? 2.657  -23.623 -7.840  1.00 38.97  ?  222 ASN A O     1 
ATOM   1491  C  CB    . ASN A  1  190 ? 0.510  -21.782 -8.251  1.00 44.77  ?  222 ASN A CB    1 
ATOM   1492  C  CG    . ASN A  1  190 ? -0.383 -22.558 -7.283  1.00 49.91  ?  222 ASN A CG    1 
ATOM   1493  O  OD1   . ASN A  1  190 ? -0.621 -22.115 -6.148  1.00 53.06  ?  222 ASN A OD1   1 
ATOM   1494  N  ND2   . ASN A  1  190 ? -0.876 -23.721 -7.716  1.00 51.89  ?  222 ASN A ND2   1 
ATOM   1495  N  N     . LYS A  1  191 ? 4.179  -22.015 -8.169  1.00 40.77  ?  223 LYS A N     1 
ATOM   1496  C  CA    . LYS A  1  191 ? 5.279  -22.960 -8.393  1.00 43.48  ?  223 LYS A CA    1 
ATOM   1497  C  C     . LYS A  1  191 ? 6.086  -23.246 -7.137  1.00 43.88  ?  223 LYS A C     1 
ATOM   1498  O  O     . LYS A  1  191 ? 6.765  -22.378 -6.598  1.00 40.08  ?  223 LYS A O     1 
ATOM   1499  C  CB    . LYS A  1  191 ? 6.238  -22.455 -9.458  1.00 45.42  ?  223 LYS A CB    1 
ATOM   1500  C  CG    . LYS A  1  191 ? 5.648  -22.409 -10.847 1.00 47.19  ?  223 LYS A CG    1 
ATOM   1501  C  CD    . LYS A  1  191 ? 6.694  -22.759 -11.892 1.00 48.64  ?  223 LYS A CD    1 
ATOM   1502  C  CE    . LYS A  1  191 ? 6.209  -22.385 -13.282 1.00 49.66  ?  223 LYS A CE    1 
ATOM   1503  N  NZ    . LYS A  1  191 ? 6.709  -23.328 -14.315 1.00 51.57  1  223 LYS A NZ    1 
ATOM   1504  N  N     . THR A  1  192 ? 5.993  -24.489 -6.692  1.00 48.72  ?  224 THR A N     1 
ATOM   1505  C  CA    . THR A  1  192 ? 6.861  -25.052 -5.657  1.00 49.49  ?  224 THR A CA    1 
ATOM   1506  C  C     . THR A  1  192 ? 8.327  -24.583 -5.717  1.00 47.15  ?  224 THR A C     1 
ATOM   1507  O  O     . THR A  1  192 ? 8.885  -24.202 -4.698  1.00 43.31  ?  224 THR A O     1 
ATOM   1508  C  CB    . THR A  1  192 ? 6.860  -26.602 -5.737  1.00 52.63  ?  224 THR A CB    1 
ATOM   1509  O  OG1   . THR A  1  192 ? 7.860  -27.114 -4.858  1.00 55.30  ?  224 THR A OG1   1 
ATOM   1510  C  CG2   . THR A  1  192 ? 7.150  -27.145 -7.195  1.00 53.33  ?  224 THR A CG2   1 
ATOM   1511  N  N     . ASP A  1  193 ? 8.943  -24.635 -6.902  1.00 45.44  ?  225 ASP A N     1 
ATOM   1512  C  CA    . ASP A  1  193 ? 10.356 -24.288 -7.068  1.00 43.78  ?  225 ASP A CA    1 
ATOM   1513  C  C     . ASP A  1  193 ? 10.607 -23.862 -8.499  1.00 42.15  ?  225 ASP A C     1 
ATOM   1514  O  O     . ASP A  1  193 ? 10.876 -24.693 -9.361  1.00 43.62  ?  225 ASP A O     1 
ATOM   1515  C  CB    . ASP A  1  193 ? 11.299 -25.449 -6.712  1.00 43.69  ?  225 ASP A CB    1 
ATOM   1516  C  CG    . ASP A  1  193 ? 12.786 -25.072 -6.871  1.00 44.88  ?  225 ASP A CG    1 
ATOM   1517  O  OD1   . ASP A  1  193 ? 13.095 -23.898 -7.213  1.00 46.29  ?  225 ASP A OD1   1 
ATOM   1518  O  OD2   . ASP A  1  193 ? 13.650 -25.945 -6.642  1.00 43.98  -1 225 ASP A OD2   1 
ATOM   1519  N  N     . PRO A  1  194 ? 10.525 -22.554 -8.756  1.00 39.55  ?  226 PRO A N     1 
ATOM   1520  C  CA    . PRO A  1  194 ? 10.769 -22.041 -10.096 1.00 37.24  ?  226 PRO A CA    1 
ATOM   1521  C  C     . PRO A  1  194 ? 12.189 -22.314 -10.542 1.00 33.00  ?  226 PRO A C     1 
ATOM   1522  O  O     . PRO A  1  194 ? 13.112 -22.130 -9.765  1.00 33.17  ?  226 PRO A O     1 
ATOM   1523  C  CB    . PRO A  1  194 ? 10.529 -20.535 -9.965  1.00 38.05  ?  226 PRO A CB    1 
ATOM   1524  C  CG    . PRO A  1  194 ? 9.714  -20.371 -8.743  1.00 38.53  ?  226 PRO A CG    1 
ATOM   1525  C  CD    . PRO A  1  194 ? 10.009 -21.526 -7.844  1.00 38.61  ?  226 PRO A CD    1 
ATOM   1526  N  N     . ALA A  1  195 ? 12.310 -22.771 -11.782 1.00 29.67  ?  227 ALA A N     1 
ATOM   1527  C  CA    . ALA A  1  195 ? 13.565 -23.098 -12.451 1.00 27.85  ?  227 ALA A CA    1 
ATOM   1528  C  C     . ALA A  1  195 ? 14.497 -23.961 -11.629 1.00 27.58  ?  227 ALA A C     1 
ATOM   1529  O  O     . ALA A  1  195 ? 15.720 -23.954 -11.856 1.00 24.28  ?  227 ALA A O     1 
ATOM   1530  C  CB    . ALA A  1  195 ? 14.255 -21.841 -12.901 1.00 27.38  ?  227 ALA A CB    1 
ATOM   1531  N  N     . ASN A  1  196 ? 13.908 -24.722 -10.701 1.00 28.57  ?  228 ASN A N     1 
ATOM   1532  C  CA    . ASN A  1  196 ? 14.676 -25.564 -9.802  1.00 32.18  ?  228 ASN A CA    1 
ATOM   1533  C  C     . ASN A  1  196 ? 15.877 -24.826 -9.196  1.00 33.16  ?  228 ASN A C     1 
ATOM   1534  O  O     . ASN A  1  196 ? 17.017 -25.303 -9.197  1.00 33.85  ?  228 ASN A O     1 
ATOM   1535  C  CB    . ASN A  1  196 ? 15.169 -26.788 -10.561 1.00 34.85  ?  228 ASN A CB    1 
ATOM   1536  C  CG    . ASN A  1  196 ? 14.080 -27.454 -11.333 1.00 35.59  ?  228 ASN A CG    1 
ATOM   1537  O  OD1   . ASN A  1  196 ? 14.002 -27.303 -12.550 1.00 40.32  ?  228 ASN A OD1   1 
ATOM   1538  N  ND2   . ASN A  1  196 ? 13.211 -28.173 -10.634 1.00 36.03  ?  228 ASN A ND2   1 
ATOM   1539  N  N     . GLN A  1  197 ? 15.626 -23.637 -8.693  1.00 34.26  ?  229 GLN A N     1 
ATOM   1540  C  CA    . GLN A  1  197 ? 16.707 -22.823 -8.207  1.00 33.86  ?  229 GLN A CA    1 
ATOM   1541  C  C     . GLN A  1  197 ? 17.070 -23.247 -6.799  1.00 35.46  ?  229 GLN A C     1 
ATOM   1542  O  O     . GLN A  1  197 ? 18.252 -23.248 -6.435  1.00 34.97  ?  229 GLN A O     1 
ATOM   1543  C  CB    . GLN A  1  197 ? 16.323 -21.360 -8.243  1.00 32.47  ?  229 GLN A CB    1 
ATOM   1544  C  CG    . GLN A  1  197 ? 17.428 -20.470 -7.732  1.00 31.80  ?  229 GLN A CG    1 
ATOM   1545  C  CD    . GLN A  1  197 ? 17.279 -19.055 -8.204  1.00 31.40  ?  229 GLN A CD    1 
ATOM   1546  O  OE1   . GLN A  1  197 ? 16.419 -18.314 -7.724  1.00 32.46  ?  229 GLN A OE1   1 
ATOM   1547  N  NE2   . GLN A  1  197 ? 18.108 -18.668 -9.150  1.00 30.04  ?  229 GLN A NE2   1 
ATOM   1548  N  N     . PHE A  1  198 ? 16.053 -23.606 -6.016  1.00 37.30  ?  230 PHE A N     1 
ATOM   1549  C  CA    . PHE A  1  198 ? 16.277 -24.087 -4.670  1.00 39.10  ?  230 PHE A CA    1 
ATOM   1550  C  C     . PHE A  1  198 ? 17.073 -25.375 -4.738  1.00 41.80  ?  230 PHE A C     1 
ATOM   1551  O  O     . PHE A  1  198 ? 18.056 -25.538 -4.006  1.00 45.78  ?  230 PHE A O     1 
ATOM   1552  C  CB    . PHE A  1  198 ? 14.960 -24.315 -3.942  1.00 39.98  ?  230 PHE A CB    1 
ATOM   1553  C  CG    . PHE A  1  198 ? 14.109 -23.083 -3.841  1.00 42.19  ?  230 PHE A CG    1 
ATOM   1554  C  CD1   . PHE A  1  198 ? 14.651 -21.882 -3.392  1.00 43.53  ?  230 PHE A CD1   1 
ATOM   1555  C  CD2   . PHE A  1  198 ? 12.767 -23.114 -4.189  1.00 42.77  ?  230 PHE A CD2   1 
ATOM   1556  C  CE1   . PHE A  1  198 ? 13.877 -20.734 -3.306  1.00 43.22  ?  230 PHE A CE1   1 
ATOM   1557  C  CE2   . PHE A  1  198 ? 11.986 -21.972 -4.099  1.00 42.91  ?  230 PHE A CE2   1 
ATOM   1558  C  CZ    . PHE A  1  198 ? 12.541 -20.780 -3.655  1.00 43.25  ?  230 PHE A CZ    1 
ATOM   1559  N  N     . GLU A  1  199 ? 16.675 -26.268 -5.639  1.00 40.80  ?  231 GLU A N     1 
ATOM   1560  C  CA    . GLU A  1  199 ? 17.341 -27.553 -5.774  1.00 41.74  ?  231 GLU A CA    1 
ATOM   1561  C  C     . GLU A  1  199 ? 18.809 -27.338 -6.107  1.00 36.52  ?  231 GLU A C     1 
ATOM   1562  O  O     . GLU A  1  199 ? 19.701 -27.884 -5.465  1.00 33.68  ?  231 GLU A O     1 
ATOM   1563  C  CB    . GLU A  1  199 ? 16.655 -28.370 -6.864  1.00 51.40  ?  231 GLU A CB    1 
ATOM   1564  C  CG    . GLU A  1  199 ? 16.843 -29.880 -6.751  1.00 60.19  ?  231 GLU A CG    1 
ATOM   1565  C  CD    . GLU A  1  199 ? 16.468 -30.629 -8.033  1.00 63.52  ?  231 GLU A CD    1 
ATOM   1566  O  OE1   . GLU A  1  199 ? 15.669 -30.107 -8.853  1.00 62.21  ?  231 GLU A OE1   1 
ATOM   1567  O  OE2   . GLU A  1  199 ? 16.985 -31.753 -8.218  1.00 65.93  -1 231 GLU A OE2   1 
ATOM   1568  N  N     . TRP A  1  200 ? 19.043 -26.511 -7.111  1.00 34.84  ?  232 TRP A N     1 
ATOM   1569  C  CA    . TRP A  1  200 ? 20.388 -26.144 -7.536  1.00 34.66  ?  232 TRP A CA    1 
ATOM   1570  C  C     . TRP A  1  200 ? 21.184 -25.412 -6.453  1.00 34.89  ?  232 TRP A C     1 
ATOM   1571  O  O     . TRP A  1  200 ? 22.393 -25.605 -6.338  1.00 34.68  ?  232 TRP A O     1 
ATOM   1572  C  CB    . TRP A  1  200 ? 20.286 -25.256 -8.774  1.00 34.64  ?  232 TRP A CB    1 
ATOM   1573  C  CG    . TRP A  1  200 ? 21.580 -24.769 -9.305  1.00 34.40  ?  232 TRP A CG    1 
ATOM   1574  C  CD1   . TRP A  1  200 ? 22.378 -25.405 -10.176 1.00 35.02  ?  232 TRP A CD1   1 
ATOM   1575  C  CD2   . TRP A  1  200 ? 22.208 -23.526 -9.017  1.00 35.51  ?  232 TRP A CD2   1 
ATOM   1576  N  NE1   . TRP A  1  200 ? 23.480 -24.645 -10.465 1.00 35.87  ?  232 TRP A NE1   1 
ATOM   1577  C  CE2   . TRP A  1  200 ? 23.408 -23.485 -9.755  1.00 36.34  ?  232 TRP A CE2   1 
ATOM   1578  C  CE3   . TRP A  1  200 ? 21.879 -22.446 -8.210  1.00 36.51  ?  232 TRP A CE3   1 
ATOM   1579  C  CZ2   . TRP A  1  200 ? 24.290 -22.405 -9.712  1.00 38.03  ?  232 TRP A CZ2   1 
ATOM   1580  C  CZ3   . TRP A  1  200 ? 22.747 -21.360 -8.180  1.00 39.11  ?  232 TRP A CZ3   1 
ATOM   1581  C  CH2   . TRP A  1  200 ? 23.943 -21.350 -8.931  1.00 38.11  ?  232 TRP A CH2   1 
ATOM   1582  N  N     . LEU A  1  201 ? 20.519 -24.553 -5.683  1.00 34.69  ?  233 LEU A N     1 
ATOM   1583  C  CA    . LEU A  1  201 ? 21.166 -23.848 -4.581  1.00 34.41  ?  233 LEU A CA    1 
ATOM   1584  C  C     . LEU A  1  201 ? 21.610 -24.832 -3.522  1.00 34.96  ?  233 LEU A C     1 
ATOM   1585  O  O     . LEU A  1  201 ? 22.809 -24.946 -3.248  1.00 35.80  ?  233 LEU A O     1 
ATOM   1586  C  CB    . LEU A  1  201 ? 20.224 -22.818 -3.956  1.00 34.55  ?  233 LEU A CB    1 
ATOM   1587  C  CG    . LEU A  1  201 ? 20.797 -21.912 -2.861  1.00 33.19  ?  233 LEU A CG    1 
ATOM   1588  C  CD1   . LEU A  1  201 ? 21.996 -21.131 -3.365  1.00 33.33  ?  233 LEU A CD1   1 
ATOM   1589  C  CD2   . LEU A  1  201 ? 19.709 -20.963 -2.411  1.00 32.85  ?  233 LEU A CD2   1 
ATOM   1590  N  N     . GLU A  1  202 ? 20.643 -25.541 -2.937  1.00 35.22  ?  234 GLU A N     1 
ATOM   1591  C  CA    . GLU A  1  202 ? 20.937 -26.605 -1.978  1.00 36.38  ?  234 GLU A CA    1 
ATOM   1592  C  C     . GLU A  1  202 ? 22.064 -27.467 -2.486  1.00 36.43  ?  234 GLU A C     1 
ATOM   1593  O  O     . GLU A  1  202 ? 23.034 -27.716 -1.765  1.00 37.60  ?  234 GLU A O     1 
ATOM   1594  C  CB    . GLU A  1  202 ? 19.717 -27.480 -1.738  1.00 37.67  ?  234 GLU A CB    1 
ATOM   1595  C  CG    . GLU A  1  202 ? 18.951 -27.115 -0.487  1.00 41.16  ?  234 GLU A CG    1 
ATOM   1596  C  CD    . GLU A  1  202 ? 17.457 -27.362 -0.601  1.00 44.61  ?  234 GLU A CD    1 
ATOM   1597  O  OE1   . GLU A  1  202 ? 16.952 -27.405 -1.753  1.00 41.83  ?  234 GLU A OE1   1 
ATOM   1598  O  OE2   . GLU A  1  202 ? 16.793 -27.486 0.474   1.00 48.35  -1 234 GLU A OE2   1 
ATOM   1599  N  N     . SER A  1  203 ? 21.932 -27.908 -3.735  1.00 35.95  ?  235 SER A N     1 
ATOM   1600  C  CA    . SER A  1  203 ? 23.001 -28.636 -4.396  1.00 36.71  ?  235 SER A CA    1 
ATOM   1601  C  C     . SER A  1  203 ? 24.335 -27.845 -4.438  1.00 37.61  ?  235 SER A C     1 
ATOM   1602  O  O     . SER A  1  203 ? 25.335 -28.319 -3.892  1.00 39.10  ?  235 SER A O     1 
ATOM   1603  C  CB    . SER A  1  203 ? 22.574 -29.061 -5.793  1.00 35.40  ?  235 SER A CB    1 
ATOM   1604  O  OG    . SER A  1  203 ? 23.594 -29.818 -6.398  1.00 34.09  ?  235 SER A OG    1 
ATOM   1605  N  N     . THR A  1  204 ? 24.354 -26.655 -5.046  1.00 36.98  ?  236 THR A N     1 
ATOM   1606  C  CA    . THR A  1  204 ? 25.601 -25.897 -5.181  1.00 38.02  ?  236 THR A CA    1 
ATOM   1607  C  C     . THR A  1  204 ? 26.264 -25.602 -3.820  1.00 40.67  ?  236 THR A C     1 
ATOM   1608  O  O     . THR A  1  204 ? 27.505 -25.558 -3.722  1.00 42.41  ?  236 THR A O     1 
ATOM   1609  C  CB    . THR A  1  204 ? 25.419 -24.568 -5.949  1.00 38.05  ?  236 THR A CB    1 
ATOM   1610  O  OG1   . THR A  1  204 ? 24.755 -24.794 -7.204  1.00 37.97  ?  236 THR A OG1   1 
ATOM   1611  C  CG2   . THR A  1  204 ? 26.778 -23.916 -6.220  1.00 37.42  ?  236 THR A CG2   1 
ATOM   1612  N  N     . LEU A  1  205 ? 25.459 -25.400 -2.776  1.00 40.72  ?  237 LEU A N     1 
ATOM   1613  C  CA    . LEU A  1  205 ? 26.020 -25.085 -1.459  1.00 41.33  ?  237 LEU A CA    1 
ATOM   1614  C  C     . LEU A  1  205 ? 26.685 -26.311 -0.877  1.00 43.14  ?  237 LEU A C     1 
ATOM   1615  O  O     . LEU A  1  205 ? 27.883 -26.276 -0.587  1.00 44.45  ?  237 LEU A O     1 
ATOM   1616  C  CB    . LEU A  1  205 ? 24.956 -24.535 -0.499  1.00 39.70  ?  237 LEU A CB    1 
ATOM   1617  C  CG    . LEU A  1  205 ? 24.511 -23.101 -0.806  1.00 37.67  ?  237 LEU A CG    1 
ATOM   1618  C  CD1   . LEU A  1  205 ? 23.244 -22.794 -0.029  1.00 37.80  ?  237 LEU A CD1   1 
ATOM   1619  C  CD2   . LEU A  1  205 ? 25.600 -22.069 -0.522  1.00 36.45  ?  237 LEU A CD2   1 
ATOM   1620  N  N     . ASN A  1  206 ? 25.901 -27.385 -0.741  1.00 44.65  ?  238 ASN A N     1 
ATOM   1621  C  CA    . ASN A  1  206 ? 26.381 -28.691 -0.270  1.00 45.17  ?  238 ASN A CA    1 
ATOM   1622  C  C     . ASN A  1  206 ? 27.720 -29.053 -0.898  1.00 45.45  ?  238 ASN A C     1 
ATOM   1623  O  O     . ASN A  1  206 ? 28.679 -29.445 -0.211  1.00 47.13  ?  238 ASN A O     1 
ATOM   1624  C  CB    . ASN A  1  206 ? 25.334 -29.768 -0.573  1.00 44.47  ?  238 ASN A CB    1 
ATOM   1625  C  CG    . ASN A  1  206 ? 25.600 -31.098 0.130   1.00 46.96  ?  238 ASN A CG    1 
ATOM   1626  O  OD1   . ASN A  1  206 ? 25.163 -32.138 -0.364  1.00 54.32  ?  238 ASN A OD1   1 
ATOM   1627  N  ND2   . ASN A  1  206 ? 26.269 -31.084 1.285   1.00 45.73  ?  238 ASN A ND2   1 
ATOM   1628  N  N     . ASN A  1  207 ? 27.790 -28.871 -2.207  1.00 44.39  ?  239 ASN A N     1 
ATOM   1629  C  CA    . ASN A  1  207 ? 29.032 -29.045 -2.931  1.00 45.17  ?  239 ASN A CA    1 
ATOM   1630  C  C     . ASN A  1  207 ? 30.186 -28.131 -2.408  1.00 43.41  ?  239 ASN A C     1 
ATOM   1631  O  O     . ASN A  1  207 ? 31.277 -28.607 -2.152  1.00 43.90  ?  239 ASN A O     1 
ATOM   1632  C  CB    . ASN A  1  207 ? 28.752 -28.939 -4.439  1.00 46.59  ?  239 ASN A CB    1 
ATOM   1633  C  CG    . ASN A  1  207 ? 29.984 -28.637 -5.256  1.00 51.72  ?  239 ASN A CG    1 
ATOM   1634  O  OD1   . ASN A  1  207 ? 30.012 -27.650 -5.987  1.00 61.98  ?  239 ASN A OD1   1 
ATOM   1635  N  ND2   . ASN A  1  207 ? 31.005 -29.480 -5.152  1.00 53.16  ?  239 ASN A ND2   1 
ATOM   1636  N  N     . SER A  1  208 ? 29.958 -26.847 -2.191  1.00 44.63  ?  240 SER A N     1 
ATOM   1637  C  CA    . SER A  1  208 ? 31.042 -25.986 -1.689  1.00 45.23  ?  240 SER A CA    1 
ATOM   1638  C  C     . SER A  1  208 ? 31.427 -26.368 -0.261  1.00 47.02  ?  240 SER A C     1 
ATOM   1639  O  O     . SER A  1  208 ? 32.593 -26.195 0.159   1.00 44.16  ?  240 SER A O     1 
ATOM   1640  C  CB    . SER A  1  208 ? 30.636 -24.510 -1.742  1.00 44.47  ?  240 SER A CB    1 
ATOM   1641  O  OG    . SER A  1  208 ? 30.518 -24.054 -3.077  1.00 42.79  ?  240 SER A OG    1 
ATOM   1642  N  N     . GLN A  1  209 ? 30.432 -26.878 0.472   1.00 51.05  ?  241 GLN A N     1 
ATOM   1643  C  CA    . GLN A  1  209 ? 30.580 -27.240 1.881   1.00 54.56  ?  241 GLN A CA    1 
ATOM   1644  C  C     . GLN A  1  209 ? 31.744 -28.155 2.006   1.00 56.67  ?  241 GLN A C     1 
ATOM   1645  O  O     . GLN A  1  209 ? 32.630 -27.929 2.820   1.00 57.30  ?  241 GLN A O     1 
ATOM   1646  C  CB    . GLN A  1  209 ? 29.334 -27.943 2.421   1.00 54.92  ?  241 GLN A CB    1 
ATOM   1647  C  CG    . GLN A  1  209 ? 29.379 -28.218 3.914   1.00 57.23  ?  241 GLN A CG    1 
ATOM   1648  C  CD    . GLN A  1  209 ? 28.062 -27.875 4.608   1.00 60.38  ?  241 GLN A CD    1 
ATOM   1649  O  OE1   . GLN A  1  209 ? 27.719 -26.704 4.741   1.00 58.66  ?  241 GLN A OE1   1 
ATOM   1650  N  NE2   . GLN A  1  209 ? 27.324 -28.894 5.062   1.00 61.10  ?  241 GLN A NE2   1 
ATOM   1651  N  N     . GLN A  1  210 ? 31.753 -29.168 1.151   1.00 60.60  ?  242 GLN A N     1 
ATOM   1652  C  CA    . GLN A  1  210 ? 32.778 -30.187 1.207   1.00 63.44  ?  242 GLN A CA    1 
ATOM   1653  C  C     . GLN A  1  210 ? 34.137 -29.773 0.678   1.00 63.09  ?  242 GLN A C     1 
ATOM   1654  O  O     . GLN A  1  210 ? 35.148 -30.210 1.207   1.00 78.57  ?  242 GLN A O     1 
ATOM   1655  C  CB    . GLN A  1  210 ? 32.295 -31.422 0.485   1.00 62.78  ?  242 GLN A CB    1 
ATOM   1656  C  CG    . GLN A  1  210 ? 31.219 -32.119 1.283   1.00 65.45  ?  242 GLN A CG    1 
ATOM   1657  C  CD    . GLN A  1  210 ? 30.066 -32.535 0.424   1.00 68.72  ?  242 GLN A CD    1 
ATOM   1658  O  OE1   . GLN A  1  210 ? 30.201 -32.637 -0.790  1.00 67.72  ?  242 GLN A OE1   1 
ATOM   1659  N  NE2   . GLN A  1  210 ? 28.917 -32.778 1.046   1.00 73.77  ?  242 GLN A NE2   1 
ATOM   1660  N  N     . ASN A  1  211 ? 34.184 -28.911 -0.325  1.00 57.80  ?  243 ASN A N     1 
ATOM   1661  C  CA    . ASN A  1  211 ? 35.447 -28.641 -1.003  1.00 57.22  ?  243 ASN A CA    1 
ATOM   1662  C  C     . ASN A  1  211 ? 36.228 -27.462 -0.401  1.00 61.89  ?  243 ASN A C     1 
ATOM   1663  O  O     . ASN A  1  211 ? 37.013 -26.799 -1.109  1.00 57.12  ?  243 ASN A O     1 
ATOM   1664  C  CB    . ASN A  1  211 ? 35.189 -28.449 -2.500  1.00 55.21  ?  243 ASN A CB    1 
ATOM   1665  C  CG    . ASN A  1  211 ? 34.175 -29.440 -3.031  1.00 50.10  ?  243 ASN A CG    1 
ATOM   1666  O  OD1   . ASN A  1  211 ? 33.560 -30.166 -2.253  1.00 47.93  ?  243 ASN A OD1   1 
ATOM   1667  N  ND2   . ASN A  1  211 ? 33.996 -29.482 -4.343  1.00 46.79  ?  243 ASN A ND2   1 
ATOM   1668  N  N     . LYS A  1  212 ? 36.049 -27.243 0.910   1.00 66.69  ?  244 LYS A N     1 
ATOM   1669  C  CA    . LYS A  1  212 ? 36.666 -26.119 1.610   1.00 72.25  ?  244 LYS A CA    1 
ATOM   1670  C  C     . LYS A  1  212 ? 36.477 -24.862 0.768   1.00 69.46  ?  244 LYS A C     1 
ATOM   1671  O  O     . LYS A  1  212 ? 37.451 -24.210 0.375   1.00 68.31  ?  244 LYS A O     1 
ATOM   1672  C  CB    . LYS A  1  212 ? 38.165 -26.358 1.865   1.00 79.08  ?  244 LYS A CB    1 
ATOM   1673  C  CG    . LYS A  1  212 ? 38.527 -27.599 2.678   1.00 86.91  ?  244 LYS A CG    1 
ATOM   1674  C  CD    . LYS A  1  212 ? 39.884 -27.412 3.369   1.00 97.14  ?  244 LYS A CD    1 
ATOM   1675  C  CE    . LYS A  1  212 ? 40.557 -28.720 3.787   1.00 101.06 ?  244 LYS A CE    1 
ATOM   1676  N  NZ    . LYS A  1  212 ? 41.481 -29.256 2.741   1.00 103.76 1  244 LYS A NZ    1 
ATOM   1677  N  N     . GLU A  1  213 ? 35.224 -24.553 0.445   1.00 64.22  ?  245 GLU A N     1 
ATOM   1678  C  CA    . GLU A  1  213 ? 34.938 -23.377 -0.368  1.00 60.33  ?  245 GLU A CA    1 
ATOM   1679  C  C     . GLU A  1  213 ? 34.041 -22.378 0.354   1.00 54.39  ?  245 GLU A C     1 
ATOM   1680  O  O     . GLU A  1  213 ? 33.076 -22.764 1.014   1.00 49.29  ?  245 GLU A O     1 
ATOM   1681  C  CB    . GLU A  1  213 ? 34.334 -23.782 -1.717  1.00 61.37  ?  245 GLU A CB    1 
ATOM   1682  C  CG    . GLU A  1  213 ? 35.378 -23.831 -2.828  1.00 63.86  ?  245 GLU A CG    1 
ATOM   1683  C  CD    . GLU A  1  213 ? 34.790 -23.722 -4.225  1.00 63.72  ?  245 GLU A CD    1 
ATOM   1684  O  OE1   . GLU A  1  213 ? 33.662 -24.228 -4.446  1.00 59.37  ?  245 GLU A OE1   1 
ATOM   1685  O  OE2   . GLU A  1  213 ? 35.471 -23.131 -5.096  1.00 62.37  -1 245 GLU A OE2   1 
ATOM   1686  N  N     . LYS A  1  214 ? 34.384 -21.094 0.228   1.00 47.98  ?  246 LYS A N     1 
ATOM   1687  C  CA    . LYS A  1  214 ? 33.524 -20.022 0.710   1.00 45.13  ?  246 LYS A CA    1 
ATOM   1688  C  C     . LYS A  1  214 ? 32.680 -19.386 -0.414  1.00 40.99  ?  246 LYS A C     1 
ATOM   1689  O  O     . LYS A  1  214 ? 33.122 -19.195 -1.566  1.00 36.00  ?  246 LYS A O     1 
ATOM   1690  C  CB    . LYS A  1  214 ? 34.334 -18.958 1.446   1.00 46.40  ?  246 LYS A CB    1 
ATOM   1691  C  CG    . LYS A  1  214 ? 35.183 -19.504 2.578   1.00 48.68  ?  246 LYS A CG    1 
ATOM   1692  C  CD    . LYS A  1  214 ? 34.357 -20.073 3.729   1.00 49.60  ?  246 LYS A CD    1 
ATOM   1693  C  CE    . LYS A  1  214 ? 34.142 -19.040 4.819   1.00 51.57  ?  246 LYS A CE    1 
ATOM   1694  N  NZ    . LYS A  1  214 ? 33.178 -19.513 5.849   1.00 52.13  1  246 LYS A NZ    1 
ATOM   1695  N  N     . VAL A  1  215 ? 31.451 -19.064 -0.026  1.00 37.88  ?  247 VAL A N     1 
ATOM   1696  C  CA    . VAL A  1  215 ? 30.445 -18.551 -0.916  1.00 35.48  ?  247 VAL A CA    1 
ATOM   1697  C  C     . VAL A  1  215 ? 30.020 -17.159 -0.499  1.00 31.92  ?  247 VAL A C     1 
ATOM   1698  O  O     . VAL A  1  215 ? 29.769 -16.897 0.673   1.00 31.35  ?  247 VAL A O     1 
ATOM   1699  C  CB    . VAL A  1  215 ? 29.192 -19.441 -0.895  1.00 36.86  ?  247 VAL A CB    1 
ATOM   1700  C  CG1   . VAL A  1  215 ? 27.953 -18.674 -1.368  1.00 37.54  ?  247 VAL A CG1   1 
ATOM   1701  C  CG2   . VAL A  1  215 ? 29.418 -20.669 -1.756  1.00 37.35  ?  247 VAL A CG2   1 
ATOM   1702  N  N     . TYR A  1  216 ? 29.924 -16.294 -1.503  1.00 28.33  ?  248 TYR A N     1 
ATOM   1703  C  CA    . TYR A  1  216 ? 29.239 -15.007 -1.428  1.00 25.04  ?  248 TYR A CA    1 
ATOM   1704  C  C     . TYR A  1  216 ? 27.953 -15.062 -2.249  1.00 23.15  ?  248 TYR A C     1 
ATOM   1705  O  O     . TYR A  1  216 ? 28.020 -15.276 -3.457  1.00 24.94  ?  248 TYR A O     1 
ATOM   1706  C  CB    . TYR A  1  216 ? 30.130 -13.930 -2.041  1.00 23.29  ?  248 TYR A CB    1 
ATOM   1707  C  CG    . TYR A  1  216 ? 31.284 -13.480 -1.203  1.00 22.13  ?  248 TYR A CG    1 
ATOM   1708  C  CD1   . TYR A  1  216 ? 31.437 -13.886 0.124   1.00 21.49  ?  248 TYR A CD1   1 
ATOM   1709  C  CD2   . TYR A  1  216 ? 32.200 -12.587 -1.728  1.00 21.79  ?  248 TYR A CD2   1 
ATOM   1710  C  CE1   . TYR A  1  216 ? 32.498 -13.427 0.876   1.00 21.72  ?  248 TYR A CE1   1 
ATOM   1711  C  CE2   . TYR A  1  216 ? 33.254 -12.109 -0.978  1.00 21.79  ?  248 TYR A CE2   1 
ATOM   1712  C  CZ    . TYR A  1  216 ? 33.398 -12.535 0.316   1.00 21.94  ?  248 TYR A CZ    1 
ATOM   1713  O  OH    . TYR A  1  216 ? 34.448 -12.054 1.048   1.00 23.23  ?  248 TYR A OH    1 
ATOM   1714  N  N     . ILE A  1  217 ? 26.794 -14.845 -1.640  1.00 20.40  ?  249 ILE A N     1 
ATOM   1715  C  CA    . ILE A  1  217 ? 25.576 -14.761 -2.433  1.00 18.92  ?  249 ILE A CA    1 
ATOM   1716  C  C     . ILE A  1  217 ? 25.374 -13.388 -3.045  1.00 18.44  ?  249 ILE A C     1 
ATOM   1717  O  O     . ILE A  1  217 ? 25.489 -12.373 -2.363  1.00 18.90  ?  249 ILE A O     1 
ATOM   1718  C  CB    . ILE A  1  217 ? 24.329 -14.991 -1.623  1.00 18.85  ?  249 ILE A CB    1 
ATOM   1719  C  CG1   . ILE A  1  217 ? 24.407 -16.276 -0.808  1.00 19.22  ?  249 ILE A CG1   1 
ATOM   1720  C  CG2   . ILE A  1  217 ? 23.154 -14.994 -2.556  1.00 19.27  ?  249 ILE A CG2   1 
ATOM   1721  C  CD1   . ILE A  1  217 ? 24.754 -17.504 -1.585  1.00 19.68  ?  249 ILE A CD1   1 
ATOM   1722  N  N     . ILE A  1  218 ? 25.037 -13.376 -4.327  1.00 17.43  ?  250 ILE A N     1 
ATOM   1723  C  CA    . ILE A  1  218 ? 24.743 -12.172 -5.090  1.00 17.02  ?  250 ILE A CA    1 
ATOM   1724  C  C     . ILE A  1  218 ? 23.306 -12.351 -5.575  1.00 16.98  ?  250 ILE A C     1 
ATOM   1725  O  O     . ILE A  1  218 ? 22.892 -13.457 -5.906  1.00 17.11  ?  250 ILE A O     1 
ATOM   1726  C  CB    . ILE A  1  218 ? 25.773 -12.054 -6.236  1.00 17.19  ?  250 ILE A CB    1 
ATOM   1727  C  CG1   . ILE A  1  218 ? 26.799 -11.032 -5.872  1.00 17.94  ?  250 ILE A CG1   1 
ATOM   1728  C  CG2   . ILE A  1  218 ? 25.206 -11.620 -7.568  1.00 17.09  ?  250 ILE A CG2   1 
ATOM   1729  C  CD1   . ILE A  1  218 ? 27.494 -11.353 -4.579  1.00 18.57  ?  250 ILE A CD1   1 
ATOM   1730  N  N     . ALA A  1  219 ? 22.518 -11.292 -5.568  1.00 16.51  ?  251 ALA A N     1 
ATOM   1731  C  CA    . ALA A  1  219 ? 21.158 -11.366 -6.104  1.00 16.24  ?  251 ALA A CA    1 
ATOM   1732  C  C     . ALA A  1  219 ? 20.552 -9.982  -6.091  1.00 16.31  ?  251 ALA A C     1 
ATOM   1733  O  O     . ALA A  1  219 ? 21.094 -9.063  -5.469  1.00 16.86  ?  251 ALA A O     1 
ATOM   1734  C  CB    . ALA A  1  219 ? 20.291 -12.324 -5.298  1.00 16.01  ?  251 ALA A CB    1 
ATOM   1735  N  N     . HIS A  1  220 ? 19.413 -9.837  -6.753  1.00 15.94  ?  252 HIS A N     1 
ATOM   1736  C  CA    . HIS A  1  220 ? 18.781 -8.531  -6.884  1.00 15.34  ?  252 HIS A CA    1 
ATOM   1737  C  C     . HIS A  1  220 ? 17.757 -8.266  -5.782  1.00 15.15  ?  252 HIS A C     1 
ATOM   1738  O  O     . HIS A  1  220 ? 17.925 -7.334  -4.978  1.00 15.09  ?  252 HIS A O     1 
ATOM   1739  C  CB    . HIS A  1  220 ? 18.112 -8.419  -8.238  1.00 15.04  ?  252 HIS A CB    1 
ATOM   1740  C  CG    . HIS A  1  220 ? 17.420 -7.124  -8.447  1.00 14.73  ?  252 HIS A CG    1 
ATOM   1741  N  ND1   . HIS A  1  220 ? 18.111 -5.960  -8.664  1.00 14.72  ?  252 HIS A ND1   1 
ATOM   1742  C  CD2   . HIS A  1  220 ? 16.109 -6.795  -8.451  1.00 14.65  ?  252 HIS A CD2   1 
ATOM   1743  C  CE1   . HIS A  1  220 ? 17.256 -4.968  -8.819  1.00 14.58  ?  252 HIS A CE1   1 
ATOM   1744  N  NE2   . HIS A  1  220 ? 16.035 -5.450  -8.697  1.00 14.61  ?  252 HIS A NE2   1 
ATOM   1745  N  N     . VAL A  1  221 ? 16.694 -9.068  -5.759  1.00 14.50  ?  253 VAL A N     1 
ATOM   1746  C  CA    . VAL A  1  221 ? 15.643 -8.864  -4.782  1.00 14.54  ?  253 VAL A CA    1 
ATOM   1747  C  C     . VAL A  1  221 ? 16.160 -9.492  -3.515  1.00 14.47  ?  253 VAL A C     1 
ATOM   1748  O  O     . VAL A  1  221 ? 16.437 -10.686 -3.500  1.00 15.31  ?  253 VAL A O     1 
ATOM   1749  C  CB    . VAL A  1  221 ? 14.317 -9.555  -5.174  1.00 14.62  ?  253 VAL A CB    1 
ATOM   1750  C  CG1   . VAL A  1  221 ? 13.218 -9.289  -4.147  1.00 14.43  ?  253 VAL A CG1   1 
ATOM   1751  C  CG2   . VAL A  1  221 ? 13.857 -9.075  -6.532  1.00 14.86  ?  253 VAL A CG2   1 
ATOM   1752  N  N     . PRO A  1  222 ? 16.288 -8.712  -2.446  1.00 13.96  ?  254 PRO A N     1 
ATOM   1753  C  CA    . PRO A  1  222 ? 16.722 -9.331  -1.231  1.00 14.19  ?  254 PRO A CA    1 
ATOM   1754  C  C     . PRO A  1  222 ? 15.650 -10.216 -0.561  1.00 14.55  ?  254 PRO A C     1 
ATOM   1755  O  O     . PRO A  1  222 ? 14.453 -10.128 -0.842  1.00 13.64  ?  254 PRO A O     1 
ATOM   1756  C  CB    . PRO A  1  222 ? 17.028 -8.135  -0.352  1.00 14.14  ?  254 PRO A CB    1 
ATOM   1757  C  CG    . PRO A  1  222 ? 16.008 -7.136  -0.751  1.00 14.00  ?  254 PRO A CG    1 
ATOM   1758  C  CD    . PRO A  1  222 ? 15.821 -7.341  -2.219  1.00 13.96  ?  254 PRO A CD    1 
ATOM   1759  N  N     . VAL A  1  223 ? 16.138 -11.076 0.317   1.00 15.29  ?  255 VAL A N     1 
ATOM   1760  C  CA    . VAL A  1  223 ? 15.316 -11.765 1.278   1.00 16.01  ?  255 VAL A CA    1 
ATOM   1761  C  C     . VAL A  1  223 ? 14.942 -10.793 2.376   1.00 16.95  ?  255 VAL A C     1 
ATOM   1762  O  O     . VAL A  1  223 ? 15.519 -9.703  2.498   1.00 17.19  ?  255 VAL A O     1 
ATOM   1763  C  CB    . VAL A  1  223 ? 16.074 -12.931 1.934   1.00 16.14  ?  255 VAL A CB    1 
ATOM   1764  C  CG1   . VAL A  1  223 ? 16.547 -13.900 0.864   1.00 16.47  ?  255 VAL A CG1   1 
ATOM   1765  C  CG2   . VAL A  1  223 ? 17.252 -12.437 2.779   1.00 15.72  ?  255 VAL A CG2   1 
ATOM   1766  N  N     . GLY A  1  224 ? 13.986 -11.215 3.193   1.00 17.87  ?  256 GLY A N     1 
ATOM   1767  C  CA    . GLY A  1  224 ? 13.582 -10.451 4.365   1.00 17.87  ?  256 GLY A CA    1 
ATOM   1768  C  C     . GLY A  1  224 ? 12.473 -9.449  4.137   1.00 17.55  ?  256 GLY A C     1 
ATOM   1769  O  O     . GLY A  1  224 ? 11.812 -9.407  3.086   1.00 17.45  ?  256 GLY A O     1 
ATOM   1770  N  N     . TYR A  1  225 ? 12.287 -8.631  5.156   1.00 16.83  ?  257 TYR A N     1 
ATOM   1771  C  CA    . TYR A  1  225 ? 11.238 -7.663  5.159   1.00 16.27  ?  257 TYR A CA    1 
ATOM   1772  C  C     . TYR A  1  225 ? 11.725 -6.307  4.672   1.00 15.80  ?  257 TYR A C     1 
ATOM   1773  O  O     . TYR A  1  225 ? 12.837 -5.869  4.982   1.00 15.78  ?  257 TYR A O     1 
ATOM   1774  C  CB    . TYR A  1  225 ? 10.655 -7.611  6.561   1.00 16.70  ?  257 TYR A CB    1 
ATOM   1775  C  CG    . TYR A  1  225 ? 9.780  -8.811  6.813   1.00 17.04  ?  257 TYR A CG    1 
ATOM   1776  C  CD1   . TYR A  1  225 ? 10.309 -10.016 7.255   1.00 17.09  ?  257 TYR A CD1   1 
ATOM   1777  C  CD2   . TYR A  1  225 ? 8.425  -8.740  6.546   1.00 17.76  ?  257 TYR A CD2   1 
ATOM   1778  C  CE1   . TYR A  1  225 ? 9.497  -11.109 7.451   1.00 17.77  ?  257 TYR A CE1   1 
ATOM   1779  C  CE2   . TYR A  1  225 ? 7.610  -9.820  6.719   1.00 18.42  ?  257 TYR A CE2   1 
ATOM   1780  C  CZ    . TYR A  1  225 ? 8.146  -10.993 7.165   1.00 18.85  ?  257 TYR A CZ    1 
ATOM   1781  O  OH    . TYR A  1  225 ? 7.251  -12.016 7.293   1.00 21.84  ?  257 TYR A OH    1 
ATOM   1782  N  N     . LEU A  1  226 ? 10.890 -5.650  3.882   1.00 15.49  ?  258 LEU A N     1 
ATOM   1783  C  CA    . LEU A  1  226 ? 11.184 -4.301  3.450   1.00 15.44  ?  258 LEU A CA    1 
ATOM   1784  C  C     . LEU A  1  226 ? 11.133 -3.393  4.649   1.00 16.12  ?  258 LEU A C     1 
ATOM   1785  O  O     . LEU A  1  226 ? 10.118 -3.345  5.342   1.00 16.87  ?  258 LEU A O     1 
ATOM   1786  C  CB    . LEU A  1  226 ? 10.166 -3.838  2.441   1.00 14.89  ?  258 LEU A CB    1 
ATOM   1787  C  CG    . LEU A  1  226 ? 10.168 -4.614  1.134   1.00 14.31  ?  258 LEU A CG    1 
ATOM   1788  C  CD1   . LEU A  1  226 ? 8.921  -4.182  0.391   1.00 14.16  ?  258 LEU A CD1   1 
ATOM   1789  C  CD2   . LEU A  1  226 ? 11.427 -4.361  0.318   1.00 14.12  ?  258 LEU A CD2   1 
ATOM   1790  N  N     . PRO A  1  227 ? 12.216 -2.654  4.903   1.00 16.78  ?  259 PRO A N     1 
ATOM   1791  C  CA    . PRO A  1  227 ? 12.282 -1.965  6.184   1.00 17.47  ?  259 PRO A CA    1 
ATOM   1792  C  C     . PRO A  1  227 ? 11.353 -0.732  6.331   1.00 18.22  ?  259 PRO A C     1 
ATOM   1793  O  O     . PRO A  1  227 ? 11.030 -0.339  7.458   1.00 18.47  ?  259 PRO A O     1 
ATOM   1794  C  CB    . PRO A  1  227 ? 13.766 -1.569  6.281   1.00 17.05  ?  259 PRO A CB    1 
ATOM   1795  C  CG    . PRO A  1  227 ? 14.284 -1.559  4.892   1.00 16.89  ?  259 PRO A CG    1 
ATOM   1796  C  CD    . PRO A  1  227 ? 13.251 -2.169  3.978   1.00 17.05  ?  259 PRO A CD    1 
ATOM   1797  N  N     A SER A  1  228 ? 10.947 -0.100  5.231   0.50 18.46  ?  260 SER A N     1 
ATOM   1798  N  N     B SER A  1  228 ? 10.914 -0.192  5.194   0.50 18.57  ?  260 SER A N     1 
ATOM   1799  C  CA    A SER A  1  228 ? 10.097 1.086   5.353   0.50 18.77  ?  260 SER A CA    1 
ATOM   1800  C  CA    B SER A  1  228 ? 10.118 1.022   5.121   0.50 18.93  ?  260 SER A CA    1 
ATOM   1801  C  C     A SER A  1  228 ? 8.601  0.771   5.256   0.50 19.75  ?  260 SER A C     1 
ATOM   1802  C  C     B SER A  1  228 ? 8.608  0.769   5.264   0.50 19.87  ?  260 SER A C     1 
ATOM   1803  O  O     A SER A  1  228 ? 7.804  1.646   4.915   0.50 19.60  ?  260 SER A O     1 
ATOM   1804  O  O     B SER A  1  228 ? 7.807  1.689   5.083   0.50 19.68  ?  260 SER A O     1 
ATOM   1805  C  CB    A SER A  1  228 ? 10.514 2.180   4.375   0.50 18.06  ?  260 SER A CB    1 
ATOM   1806  C  CB    B SER A  1  228 ? 10.394 1.675   3.776   0.50 18.45  ?  260 SER A CB    1 
ATOM   1807  O  OG    A SER A  1  228 ? 11.421 3.060   5.024   0.50 17.68  ?  260 SER A OG    1 
ATOM   1808  O  OG    B SER A  1  228 ? 10.660 0.663   2.807   0.50 18.36  ?  260 SER A OG    1 
ATOM   1809  N  N     . SER A  1  229 ? 8.220  -0.460  5.597   1.00 20.54  ?  261 SER A N     1 
ATOM   1810  C  CA    . SER A  1  229 ? 6.814  -0.816  5.686   1.00 22.10  ?  261 SER A CA    1 
ATOM   1811  C  C     . SER A  1  229 ? 6.591  -2.105  6.483   1.00 23.99  ?  261 SER A C     1 
ATOM   1812  O  O     . SER A  1  229 ? 7.541  -2.819  6.811   1.00 24.49  ?  261 SER A O     1 
ATOM   1813  C  CB    . SER A  1  229 ? 6.155  -0.878  4.285   1.00 22.02  ?  261 SER A CB    1 
ATOM   1814  O  OG    . SER A  1  229 ? 6.917  -1.594  3.338   1.00 21.53  ?  261 SER A OG    1 
ATOM   1815  N  N     . GLN A  1  230 ? 5.316  -2.371  6.772   1.00 25.72  ?  262 GLN A N     1 
ATOM   1816  C  CA    . GLN A  1  230 ? 4.901  -3.324  7.777   1.00 27.18  ?  262 GLN A CA    1 
ATOM   1817  C  C     . GLN A  1  230 ? 4.538  -4.712  7.227   1.00 25.87  ?  262 GLN A C     1 
ATOM   1818  O  O     . GLN A  1  230 ? 3.681  -4.850  6.361   1.00 26.34  ?  262 GLN A O     1 
ATOM   1819  C  CB    . GLN A  1  230 ? 3.715  -2.722  8.544   1.00 30.72  ?  262 GLN A CB    1 
ATOM   1820  C  CG    . GLN A  1  230 ? 2.968  -3.714  9.448   1.00 34.50  ?  262 GLN A CG    1 
ATOM   1821  C  CD    . GLN A  1  230 ? 2.085  -3.064  10.513  1.00 35.17  ?  262 GLN A CD    1 
ATOM   1822  O  OE1   . GLN A  1  230 ? 1.740  -3.717  11.520  1.00 36.23  ?  262 GLN A OE1   1 
ATOM   1823  N  NE2   . GLN A  1  230 ? 1.706  -1.790  10.299  1.00 32.93  ?  262 GLN A NE2   1 
ATOM   1824  N  N     . ASN A  1  231 ? 5.201  -5.730  7.763   1.00 24.97  ?  263 ASN A N     1 
ATOM   1825  C  CA    . ASN A  1  231 ? 4.928  -7.140  7.480   1.00 24.94  ?  263 ASN A CA    1 
ATOM   1826  C  C     . ASN A  1  231 ? 4.918  -7.492  5.981   1.00 24.05  ?  263 ASN A C     1 
ATOM   1827  O  O     . ASN A  1  231 ? 4.223  -8.412  5.572   1.00 25.08  ?  263 ASN A O     1 
ATOM   1828  C  CB    . ASN A  1  231 ? 3.641  -7.589  8.194   1.00 26.10  ?  263 ASN A CB    1 
ATOM   1829  C  CG    . ASN A  1  231 ? 3.436  -9.108  8.174   1.00 29.02  ?  263 ASN A CG    1 
ATOM   1830  O  OD1   . ASN A  1  231 ? 4.382  -9.889  8.287   1.00 28.73  ?  263 ASN A OD1   1 
ATOM   1831  N  ND2   . ASN A  1  231 ? 2.180  -9.530  7.973   1.00 34.38  ?  263 ASN A ND2   1 
ATOM   1832  N  N     . ILE A  1  232 ? 5.724  -6.796  5.173   1.00 22.00  ?  264 ILE A N     1 
ATOM   1833  C  CA    . ILE A  1  232 ? 5.848  -7.103  3.741   1.00 20.00  ?  264 ILE A CA    1 
ATOM   1834  C  C     . ILE A  1  232 ? 7.238  -7.555  3.375   1.00 18.71  ?  264 ILE A C     1 
ATOM   1835  O  O     . ILE A  1  232 ? 8.157  -6.748  3.317   1.00 17.94  ?  264 ILE A O     1 
ATOM   1836  C  CB    . ILE A  1  232 ? 5.577  -5.880  2.875   1.00 19.75  ?  264 ILE A CB    1 
ATOM   1837  C  CG1   . ILE A  1  232 ? 4.179  -5.357  3.161   1.00 20.44  ?  264 ILE A CG1   1 
ATOM   1838  C  CG2   . ILE A  1  232 ? 5.760  -6.211  1.397   1.00 19.07  ?  264 ILE A CG2   1 
ATOM   1839  C  CD1   . ILE A  1  232 ? 4.073  -3.859  2.956   1.00 21.18  ?  264 ILE A CD1   1 
ATOM   1840  N  N     . THR A  1  233 ? 7.365  -8.843  3.092   1.00 18.05  ?  265 THR A N     1 
ATOM   1841  C  CA    . THR A  1  233 ? 8.589  -9.400  2.572   1.00 18.27  ?  265 THR A CA    1 
ATOM   1842  C  C     . THR A  1  233 ? 8.756  -8.867  1.178   1.00 18.18  ?  265 THR A C     1 
ATOM   1843  O  O     . THR A  1  233 ? 7.770  -8.535  0.547   1.00 18.18  ?  265 THR A O     1 
ATOM   1844  C  CB    . THR A  1  233 ? 8.487  -10.915 2.483   1.00 18.91  ?  265 THR A CB    1 
ATOM   1845  O  OG1   . THR A  1  233 ? 7.301  -11.245 1.754   1.00 19.09  ?  265 THR A OG1   1 
ATOM   1846  C  CG2   . THR A  1  233 ? 8.412  -11.535 3.887   1.00 19.57  ?  265 THR A CG2   1 
ATOM   1847  N  N     . ALA A  1  234 ? 9.989  -8.792  0.694   1.00 18.41  ?  266 ALA A N     1 
ATOM   1848  C  CA    . ALA A  1  234 ? 10.264 -8.207  -0.614  1.00 19.03  ?  266 ALA A CA    1 
ATOM   1849  C  C     . ALA A  1  234 ? 9.919  -9.188  -1.725  1.00 20.41  ?  266 ALA A C     1 
ATOM   1850  O  O     . ALA A  1  234 ? 9.258  -8.839  -2.715  1.00 21.66  ?  266 ALA A O     1 
ATOM   1851  C  CB    . ALA A  1  234 ? 11.723 -7.814  -0.693  1.00 19.24  ?  266 ALA A CB    1 
ATOM   1852  N  N     . MET A  1  235 ? 10.408 -10.412 -1.554  1.00 21.61  ?  267 MET A N     1 
ATOM   1853  C  CA    . MET A  1  235 ? 9.945  -11.594 -2.284  1.00 22.13  ?  267 MET A CA    1 
ATOM   1854  C  C     . MET A  1  235 ? 8.601  -12.033 -1.752  1.00 22.77  ?  267 MET A C     1 
ATOM   1855  O  O     . MET A  1  235 ? 8.115  -11.508 -0.755  1.00 22.45  ?  267 MET A O     1 
ATOM   1856  C  CB    . MET A  1  235 ? 10.877 -12.776 -2.014  1.00 22.52  ?  267 MET A CB    1 
ATOM   1857  C  CG    . MET A  1  235 ? 12.250 -12.664 -2.639  1.00 23.26  ?  267 MET A CG    1 
ATOM   1858  S  SD    . MET A  1  235 ? 13.438 -13.762 -1.855  1.00 23.13  ?  267 MET A SD    1 
ATOM   1859  C  CE    . MET A  1  235 ? 12.387 -15.178 -1.607  1.00 23.00  ?  267 MET A CE    1 
ATOM   1860  N  N     . ARG A  1  236 ? 8.031  -13.044 -2.394  1.00 24.30  ?  268 ARG A N     1 
ATOM   1861  C  CA    . ARG A  1  236 ? 6.868  -13.736 -1.842  1.00 25.29  ?  268 ARG A CA    1 
ATOM   1862  C  C     . ARG A  1  236 ? 7.252  -14.509 -0.582  1.00 26.84  ?  268 ARG A C     1 
ATOM   1863  O  O     . ARG A  1  236 ? 8.169  -15.350 -0.582  1.00 24.55  ?  268 ARG A O     1 
ATOM   1864  C  CB    . ARG A  1  236 ? 6.196  -14.651 -2.878  1.00 24.72  ?  268 ARG A CB    1 
ATOM   1865  C  CG    . ARG A  1  236 ? 5.241  -13.919 -3.816  1.00 23.75  ?  268 ARG A CG    1 
ATOM   1866  C  CD    . ARG A  1  236 ? 4.484  -14.862 -4.746  1.00 22.87  ?  268 ARG A CD    1 
ATOM   1867  N  NE    . ARG A  1  236 ? 4.384  -14.306 -6.101  1.00 22.04  ?  268 ARG A NE    1 
ATOM   1868  C  CZ    . ARG A  1  236 ? 4.782  -14.915 -7.218  1.00 22.02  ?  268 ARG A CZ    1 
ATOM   1869  N  NH1   . ARG A  1  236 ? 5.292  -16.159 -7.198  1.00 21.94  1  268 ARG A NH1   1 
ATOM   1870  N  NH2   . ARG A  1  236 ? 4.642  -14.276 -8.377  1.00 21.82  ?  268 ARG A NH2   1 
ATOM   1871  N  N     . GLU A  1  237 ? 6.534  -14.175 0.486   1.00 30.10  ?  269 GLU A N     1 
ATOM   1872  C  CA    . GLU A  1  237 ? 6.709  -14.779 1.788   1.00 34.54  ?  269 GLU A CA    1 
ATOM   1873  C  C     . GLU A  1  237 ? 7.165  -16.203 1.628   1.00 35.95  ?  269 GLU A C     1 
ATOM   1874  O  O     . GLU A  1  237 ? 8.160  -16.639 2.227   1.00 35.03  ?  269 GLU A O     1 
ATOM   1875  C  CB    . GLU A  1  237 ? 5.368  -14.779 2.510   1.00 37.11  ?  269 GLU A CB    1 
ATOM   1876  C  CG    . GLU A  1  237 ? 5.192  -15.862 3.574   1.00 40.07  ?  269 GLU A CG    1 
ATOM   1877  C  CD    . GLU A  1  237 ? 5.177  -15.299 4.967   1.00 44.36  ?  269 GLU A CD    1 
ATOM   1878  O  OE1   . GLU A  1  237 ? 4.905  -14.084 5.113   1.00 50.70  ?  269 GLU A OE1   1 
ATOM   1879  O  OE2   . GLU A  1  237 ? 5.421  -16.076 5.913   1.00 48.24  -1 269 GLU A OE2   1 
ATOM   1880  N  N     . TYR A  1  238 ? 6.405  -16.924 0.812   1.00 37.33  ?  270 TYR A N     1 
ATOM   1881  C  CA    . TYR A  1  238 ? 6.590  -18.353 0.692   1.00 38.82  ?  270 TYR A CA    1 
ATOM   1882  C  C     . TYR A  1  238 ? 8.026  -18.670 0.328   1.00 34.84  ?  270 TYR A C     1 
ATOM   1883  O  O     . TYR A  1  238 ? 8.632  -19.568 0.904   1.00 33.81  ?  270 TYR A O     1 
ATOM   1884  C  CB    . TYR A  1  238 ? 5.616  -18.956 -0.330  1.00 41.18  ?  270 TYR A CB    1 
ATOM   1885  C  CG    . TYR A  1  238 ? 5.981  -20.368 -0.670  1.00 42.70  ?  270 TYR A CG    1 
ATOM   1886  C  CD1   . TYR A  1  238 ? 5.684  -21.416 0.200   1.00 44.14  ?  270 TYR A CD1   1 
ATOM   1887  C  CD2   . TYR A  1  238 ? 6.680  -20.648 -1.835  1.00 45.07  ?  270 TYR A CD2   1 
ATOM   1888  C  CE1   . TYR A  1  238 ? 6.047  -22.721 -0.106  1.00 47.55  ?  270 TYR A CE1   1 
ATOM   1889  C  CE2   . TYR A  1  238 ? 7.053  -21.943 -2.154  1.00 48.87  ?  270 TYR A CE2   1 
ATOM   1890  C  CZ    . TYR A  1  238 ? 6.742  -22.985 -1.292  1.00 49.01  ?  270 TYR A CZ    1 
ATOM   1891  O  OH    . TYR A  1  238 ? 7.144  -24.267 -1.634  1.00 48.27  ?  270 TYR A OH    1 
ATOM   1892  N  N     . TYR A  1  239 ? 8.567  -17.922 -0.620  1.00 32.78  ?  271 TYR A N     1 
ATOM   1893  C  CA    . TYR A  1  239 ? 9.924  -18.169 -1.053  1.00 32.78  ?  271 TYR A CA    1 
ATOM   1894  C  C     . TYR A  1  239 ? 10.888 -17.650 -0.019  1.00 31.67  ?  271 TYR A C     1 
ATOM   1895  O  O     . TYR A  1  239 ? 11.938 -18.268 0.214   1.00 30.54  ?  271 TYR A O     1 
ATOM   1896  C  CB    . TYR A  1  239 ? 10.210 -17.505 -2.392  1.00 33.27  ?  271 TYR A CB    1 
ATOM   1897  C  CG    . TYR A  1  239 ? 9.370  -18.030 -3.520  1.00 34.37  ?  271 TYR A CG    1 
ATOM   1898  C  CD1   . TYR A  1  239 ? 9.336  -19.389 -3.821  1.00 34.85  ?  271 TYR A CD1   1 
ATOM   1899  C  CD2   . TYR A  1  239 ? 8.605  -17.168 -4.291  1.00 34.47  ?  271 TYR A CD2   1 
ATOM   1900  C  CE1   . TYR A  1  239 ? 8.551  -19.872 -4.857  1.00 35.04  ?  271 TYR A CE1   1 
ATOM   1901  C  CE2   . TYR A  1  239 ? 7.835  -17.637 -5.338  1.00 35.68  ?  271 TYR A CE2   1 
ATOM   1902  C  CZ    . TYR A  1  239 ? 7.807  -18.987 -5.618  1.00 35.32  ?  271 TYR A CZ    1 
ATOM   1903  O  OH    . TYR A  1  239 ? 7.031  -19.439 -6.659  1.00 34.83  ?  271 TYR A OH    1 
ATOM   1904  N  N     . ASN A  1  240 ? 10.549 -16.515 0.597   1.00 30.13  ?  272 ASN A N     1 
ATOM   1905  C  CA    . ASN A  1  240 ? 11.462 -15.928 1.565   1.00 28.42  ?  272 ASN A CA    1 
ATOM   1906  C  C     . ASN A  1  240 ? 11.726 -16.926 2.648   1.00 29.02  ?  272 ASN A C     1 
ATOM   1907  O  O     . ASN A  1  240 ? 12.877 -17.161 2.982   1.00 29.54  ?  272 ASN A O     1 
ATOM   1908  C  CB    . ASN A  1  240 ? 10.957 -14.619 2.155   1.00 26.83  ?  272 ASN A CB    1 
ATOM   1909  C  CG    . ASN A  1  240 ? 11.846 -14.121 3.268   1.00 24.91  ?  272 ASN A CG    1 
ATOM   1910  O  OD1   . ASN A  1  240 ? 13.002 -13.763 3.051   1.00 22.40  ?  272 ASN A OD1   1 
ATOM   1911  N  ND2   . ASN A  1  240 ? 11.323 -14.142 4.476   1.00 25.32  ?  272 ASN A ND2   1 
ATOM   1912  N  N     . GLU A  1  241 ? 10.667 -17.554 3.150   1.00 30.48  ?  273 GLU A N     1 
ATOM   1913  C  CA    . GLU A  1  241 ? 10.807 -18.568 4.198   1.00 32.17  ?  273 GLU A CA    1 
ATOM   1914  C  C     . GLU A  1  241 ? 11.689 -19.726 3.744   1.00 32.89  ?  273 GLU A C     1 
ATOM   1915  O  O     . GLU A  1  241 ? 12.552 -20.207 4.482   1.00 34.75  ?  273 GLU A O     1 
ATOM   1916  C  CB    . GLU A  1  241 ? 9.446  -19.105 4.598   1.00 32.52  ?  273 GLU A CB    1 
ATOM   1917  C  CG    . GLU A  1  241 ? 8.565  -18.090 5.298   1.00 34.64  ?  273 GLU A CG    1 
ATOM   1918  C  CD    . GLU A  1  241 ? 9.073  -17.677 6.671   1.00 37.28  ?  273 GLU A CD    1 
ATOM   1919  O  OE1   . GLU A  1  241 ? 9.678  -18.511 7.386   1.00 37.28  ?  273 GLU A OE1   1 
ATOM   1920  O  OE2   . GLU A  1  241 ? 8.847  -16.498 7.037   1.00 42.44  -1 273 GLU A OE2   1 
ATOM   1921  N  N     . LYS A  1  242 ? 11.462 -20.149 2.513   1.00 32.02  ?  274 LYS A N     1 
ATOM   1922  C  CA    . LYS A  1  242 ? 12.185 -21.250 1.925   1.00 32.34  ?  274 LYS A CA    1 
ATOM   1923  C  C     . LYS A  1  242 ? 13.676 -20.924 1.809   1.00 29.47  ?  274 LYS A C     1 
ATOM   1924  O  O     . LYS A  1  242 ? 14.524 -21.727 2.156   1.00 28.53  ?  274 LYS A O     1 
ATOM   1925  C  CB    . LYS A  1  242 ? 11.581 -21.521 0.555   1.00 36.01  ?  274 LYS A CB    1 
ATOM   1926  C  CG    . LYS A  1  242 ? 11.589 -22.966 0.097   1.00 40.21  ?  274 LYS A CG    1 
ATOM   1927  C  CD    . LYS A  1  242 ? 10.363 -23.238 -0.778  1.00 43.42  ?  274 LYS A CD    1 
ATOM   1928  C  CE    . LYS A  1  242 ? 10.538 -24.451 -1.685  1.00 45.84  ?  274 LYS A CE    1 
ATOM   1929  N  NZ    . LYS A  1  242 ? 10.655 -25.722 -0.922  1.00 48.97  1  274 LYS A NZ    1 
ATOM   1930  N  N     . LEU A  1  243 ? 13.988 -19.731 1.330   1.00 28.15  ?  275 LEU A N     1 
ATOM   1931  C  CA    . LEU A  1  243 ? 15.381 -19.306 1.164   1.00 27.24  ?  275 LEU A CA    1 
ATOM   1932  C  C     . LEU A  1  243 ? 16.132 -19.143 2.469   1.00 28.41  ?  275 LEU A C     1 
ATOM   1933  O  O     . LEU A  1  243 ? 17.346 -19.409 2.528   1.00 26.37  ?  275 LEU A O     1 
ATOM   1934  C  CB    . LEU A  1  243 ? 15.444 -17.955 0.472   1.00 26.15  ?  275 LEU A CB    1 
ATOM   1935  C  CG    . LEU A  1  243 ? 15.577 -17.905 -1.030  1.00 25.23  ?  275 LEU A CG    1 
ATOM   1936  C  CD1   . LEU A  1  243 ? 15.737 -16.451 -1.475  1.00 25.21  ?  275 LEU A CD1   1 
ATOM   1937  C  CD2   . LEU A  1  243 ? 16.781 -18.717 -1.442  1.00 24.73  ?  275 LEU A CD2   1 
ATOM   1938  N  N     . ILE A  1  244 ? 15.415 -18.639 3.481   1.00 29.83  ?  276 ILE A N     1 
ATOM   1939  C  CA    . ILE A  1  244 ? 16.000 -18.327 4.781   1.00 30.50  ?  276 ILE A CA    1 
ATOM   1940  C  C     . ILE A  1  244 ? 16.479 -19.628 5.378   1.00 32.99  ?  276 ILE A C     1 
ATOM   1941  O  O     . ILE A  1  244 ? 17.614 -19.702 5.872   1.00 32.12  ?  276 ILE A O     1 
ATOM   1942  C  CB    . ILE A  1  244 ? 14.986 -17.641 5.722   1.00 29.99  ?  276 ILE A CB    1 
ATOM   1943  C  CG1   . ILE A  1  244 ? 14.746 -16.192 5.312   1.00 30.46  ?  276 ILE A CG1   1 
ATOM   1944  C  CG2   . ILE A  1  244 ? 15.471 -17.650 7.157   1.00 30.34  ?  276 ILE A CG2   1 
ATOM   1945  C  CD1   . ILE A  1  244 ? 16.011 -15.418 5.010   1.00 30.95  ?  276 ILE A CD1   1 
ATOM   1946  N  N     . ASP A  1  245 ? 15.622 -20.652 5.297   1.00 35.50  ?  277 ASP A N     1 
ATOM   1947  C  CA    . ASP A  1  245 ? 15.971 -21.980 5.783   1.00 38.00  ?  277 ASP A CA    1 
ATOM   1948  C  C     . ASP A  1  245 ? 17.223 -22.461 5.131   1.00 36.28  ?  277 ASP A C     1 
ATOM   1949  O  O     . ASP A  1  245 ? 18.156 -22.877 5.812   1.00 37.14  ?  277 ASP A O     1 
ATOM   1950  C  CB    . ASP A  1  245 ? 14.866 -22.973 5.527   1.00 42.88  ?  277 ASP A CB    1 
ATOM   1951  C  CG    . ASP A  1  245 ? 13.846 -22.969 6.627   1.00 51.31  ?  277 ASP A CG    1 
ATOM   1952  O  OD1   . ASP A  1  245 ? 13.118 -21.952 6.767   1.00 61.69  ?  277 ASP A OD1   1 
ATOM   1953  O  OD2   . ASP A  1  245 ? 13.791 -23.975 7.371   1.00 56.37  -1 277 ASP A OD2   1 
ATOM   1954  N  N     . ILE A  1  246 ? 17.261 -22.372 3.810   1.00 33.17  ?  278 ILE A N     1 
ATOM   1955  C  CA    . ILE A  1  246 ? 18.453 -22.765 3.090   1.00 31.91  ?  278 ILE A CA    1 
ATOM   1956  C  C     . ILE A  1  246 ? 19.683 -22.025 3.630   1.00 31.49  ?  278 ILE A C     1 
ATOM   1957  O  O     . ILE A  1  246 ? 20.722 -22.640 3.827   1.00 30.80  ?  278 ILE A O     1 
ATOM   1958  C  CB    . ILE A  1  246 ? 18.320 -22.564 1.555   1.00 30.82  ?  278 ILE A CB    1 
ATOM   1959  C  CG1   . ILE A  1  246 ? 17.295 -23.539 0.966   1.00 29.39  ?  278 ILE A CG1   1 
ATOM   1960  C  CG2   . ILE A  1  246 ? 19.668 -22.770 0.857   1.00 30.21  ?  278 ILE A CG2   1 
ATOM   1961  C  CD1   . ILE A  1  246 ? 16.800 -23.156 -0.414  1.00 28.55  ?  278 ILE A CD1   1 
ATOM   1962  N  N     . PHE A  1  247 ? 19.569 -20.720 3.860   1.00 32.50  ?  279 PHE A N     1 
ATOM   1963  C  CA    . PHE A  1  247 ? 20.732 -19.930 4.282   1.00 33.14  ?  279 PHE A CA    1 
ATOM   1964  C  C     . PHE A  1  247 ? 21.091 -20.274 5.707   1.00 32.23  ?  279 PHE A C     1 
ATOM   1965  O  O     . PHE A  1  247 ? 22.270 -20.325 6.064   1.00 29.20  ?  279 PHE A O     1 
ATOM   1966  C  CB    . PHE A  1  247 ? 20.475 -18.415 4.174   1.00 35.08  ?  279 PHE A CB    1 
ATOM   1967  C  CG    . PHE A  1  247 ? 20.343 -17.886 2.748   1.00 36.11  ?  279 PHE A CG    1 
ATOM   1968  C  CD1   . PHE A  1  247 ? 21.046 -18.452 1.679   1.00 36.74  ?  279 PHE A CD1   1 
ATOM   1969  C  CD2   . PHE A  1  247 ? 19.537 -16.783 2.490   1.00 36.46  ?  279 PHE A CD2   1 
ATOM   1970  C  CE1   . PHE A  1  247 ? 20.928 -17.943 0.390   1.00 36.88  ?  279 PHE A CE1   1 
ATOM   1971  C  CE2   . PHE A  1  247 ? 19.412 -16.275 1.208   1.00 37.35  ?  279 PHE A CE2   1 
ATOM   1972  C  CZ    . PHE A  1  247 ? 20.111 -16.853 0.157   1.00 37.89  ?  279 PHE A CZ    1 
ATOM   1973  N  N     . GLN A  1  248 ? 20.065 -20.502 6.521   1.00 33.56  ?  280 GLN A N     1 
ATOM   1974  C  CA    . GLN A  1  248 ? 20.270 -21.006 7.863   1.00 35.19  ?  280 GLN A CA    1 
ATOM   1975  C  C     . GLN A  1  248 ? 21.125 -22.266 7.806   1.00 37.41  ?  280 GLN A C     1 
ATOM   1976  O  O     . GLN A  1  248 ? 22.225 -22.283 8.365   1.00 39.61  ?  280 GLN A O     1 
ATOM   1977  C  CB    . GLN A  1  248 ? 18.940 -21.296 8.553   1.00 36.00  ?  280 GLN A CB    1 
ATOM   1978  C  CG    . GLN A  1  248 ? 18.470 -20.167 9.452   1.00 37.60  ?  280 GLN A CG    1 
ATOM   1979  C  CD    . GLN A  1  248 ? 16.970 -20.182 9.749   1.00 40.24  ?  280 GLN A CD    1 
ATOM   1980  O  OE1   . GLN A  1  248 ? 16.189 -20.944 9.170   1.00 41.08  ?  280 GLN A OE1   1 
ATOM   1981  N  NE2   . GLN A  1  248 ? 16.559 -19.308 10.653  1.00 42.91  ?  280 GLN A NE2   1 
ATOM   1982  N  N     . LYS A  1  249 ? 20.638 -23.292 7.100   1.00 37.05  ?  281 LYS A N     1 
ATOM   1983  C  CA    . LYS A  1  249 ? 21.320 -24.594 7.027   1.00 37.25  ?  281 LYS A CA    1 
ATOM   1984  C  C     . LYS A  1  249 ? 22.810 -24.488 6.648   1.00 37.15  ?  281 LYS A C     1 
ATOM   1985  O  O     . LYS A  1  249 ? 23.661 -25.080 7.298   1.00 37.08  ?  281 LYS A O     1 
ATOM   1986  C  CB    . LYS A  1  249 ? 20.573 -25.563 6.084   1.00 39.91  ?  281 LYS A CB    1 
ATOM   1987  C  CG    . LYS A  1  249 ? 19.100 -25.848 6.492   1.00 43.87  ?  281 LYS A CG    1 
ATOM   1988  C  CD    . LYS A  1  249 ? 18.525 -27.240 6.122   1.00 44.26  ?  281 LYS A CD    1 
ATOM   1989  C  CE    . LYS A  1  249 ? 18.522 -27.576 4.616   1.00 46.16  ?  281 LYS A CE    1 
ATOM   1990  N  NZ    . LYS A  1  249 ? 17.402 -27.010 3.790   1.00 45.04  1  281 LYS A NZ    1 
ATOM   1991  N  N     . TYR A  1  250 ? 23.131 -23.689 5.638   1.00 38.67  ?  282 TYR A N     1 
ATOM   1992  C  CA    . TYR A  1  250 ? 24.497 -23.588 5.129   1.00 37.97  ?  282 TYR A CA    1 
ATOM   1993  C  C     . TYR A  1  250 ? 25.227 -22.290 5.488   1.00 36.76  ?  282 TYR A C     1 
ATOM   1994  O  O     . TYR A  1  250 ? 26.097 -21.855 4.733   1.00 37.19  ?  282 TYR A O     1 
ATOM   1995  C  CB    . TYR A  1  250 ? 24.451 -23.711 3.612   1.00 39.39  ?  282 TYR A CB    1 
ATOM   1996  C  CG    . TYR A  1  250 ? 23.983 -25.059 3.109   1.00 42.63  ?  282 TYR A CG    1 
ATOM   1997  C  CD1   . TYR A  1  250 ? 24.917 -26.041 2.731   1.00 43.17  ?  282 TYR A CD1   1 
ATOM   1998  C  CD2   . TYR A  1  250 ? 22.613 -25.358 2.982   1.00 43.57  ?  282 TYR A CD2   1 
ATOM   1999  C  CE1   . TYR A  1  250 ? 24.509 -27.275 2.261   1.00 42.67  ?  282 TYR A CE1   1 
ATOM   2000  C  CE2   . TYR A  1  250 ? 22.194 -26.601 2.509   1.00 44.48  ?  282 TYR A CE2   1 
ATOM   2001  C  CZ    . TYR A  1  250 ? 23.153 -27.552 2.152   1.00 44.20  ?  282 TYR A CZ    1 
ATOM   2002  O  OH    . TYR A  1  250 ? 22.779 -28.779 1.674   1.00 43.41  ?  282 TYR A OH    1 
ATOM   2003  N  N     . SER A  1  251 ? 24.904 -21.678 6.623   1.00 35.06  ?  283 SER A N     1 
ATOM   2004  C  CA    . SER A  1  251 ? 25.470 -20.362 6.962   1.00 35.29  ?  283 SER A CA    1 
ATOM   2005  C  C     . SER A  1  251 ? 26.969 -20.393 7.222   1.00 35.11  ?  283 SER A C     1 
ATOM   2006  O  O     . SER A  1  251 ? 27.679 -19.397 7.056   1.00 32.66  ?  283 SER A O     1 
ATOM   2007  C  CB    . SER A  1  251 ? 24.778 -19.770 8.184   1.00 36.90  ?  283 SER A CB    1 
ATOM   2008  O  OG    . SER A  1  251 ? 25.112 -20.481 9.362   1.00 39.78  ?  283 SER A OG    1 
ATOM   2009  N  N     . ASP A  1  252 ? 27.434 -21.547 7.666   1.00 37.40  ?  284 ASP A N     1 
ATOM   2010  C  CA    . ASP A  1  252 ? 28.861 -21.808 7.842   1.00 38.34  ?  284 ASP A CA    1 
ATOM   2011  C  C     . ASP A  1  252 ? 29.624 -21.569 6.536   1.00 31.80  ?  284 ASP A C     1 
ATOM   2012  O  O     . ASP A  1  252 ? 30.747 -21.109 6.573   1.00 29.80  ?  284 ASP A O     1 
ATOM   2013  C  CB    . ASP A  1  252 ? 29.051 -23.236 8.359   1.00 43.89  ?  284 ASP A CB    1 
ATOM   2014  C  CG    . ASP A  1  252 ? 27.936 -24.182 7.861   1.00 51.76  ?  284 ASP A CG    1 
ATOM   2015  O  OD1   . ASP A  1  252 ? 26.774 -24.058 8.333   1.00 51.67  ?  284 ASP A OD1   1 
ATOM   2016  O  OD2   . ASP A  1  252 ? 28.207 -25.017 6.964   1.00 58.96  -1 284 ASP A OD2   1 
ATOM   2017  N  N     . VAL A  1  253 ? 28.997 -21.833 5.389   1.00 28.95  ?  285 VAL A N     1 
ATOM   2018  C  CA    . VAL A  1  253 ? 29.658 -21.643 4.069   1.00 27.83  ?  285 VAL A CA    1 
ATOM   2019  C  C     . VAL A  1  253 ? 29.587 -20.227 3.504   1.00 25.46  ?  285 VAL A C     1 
ATOM   2020  O  O     . VAL A  1  253 ? 30.516 -19.776 2.836   1.00 24.29  ?  285 VAL A O     1 
ATOM   2021  C  CB    . VAL A  1  253 ? 29.060 -22.524 2.947   1.00 27.98  ?  285 VAL A CB    1 
ATOM   2022  C  CG1   . VAL A  1  253 ? 30.095 -22.710 1.847   1.00 27.55  ?  285 VAL A CG1   1 
ATOM   2023  C  CG2   . VAL A  1  253 ? 28.607 -23.876 3.473   1.00 29.13  ?  285 VAL A CG2   1 
ATOM   2024  N  N     . ILE A  1  254 ? 28.465 -19.560 3.745   1.00 23.32  ?  286 ILE A N     1 
ATOM   2025  C  CA    . ILE A  1  254 ? 28.204 -18.271 3.174   1.00 22.69  ?  286 ILE A CA    1 
ATOM   2026  C  C     . ILE A  1  254 ? 28.916 -17.236 4.005   1.00 23.37  ?  286 ILE A C     1 
ATOM   2027  O  O     . ILE A  1  254 ? 28.653 -17.090 5.191   1.00 25.30  ?  286 ILE A O     1 
ATOM   2028  C  CB    . ILE A  1  254 ? 26.718 -17.943 3.217   1.00 22.87  ?  286 ILE A CB    1 
ATOM   2029  C  CG1   . ILE A  1  254 ? 25.913 -19.078 2.576   1.00 23.09  ?  286 ILE A CG1   1 
ATOM   2030  C  CG2   . ILE A  1  254 ? 26.466 -16.590 2.553   1.00 22.58  ?  286 ILE A CG2   1 
ATOM   2031  C  CD1   . ILE A  1  254 ? 24.419 -18.957 2.782   1.00 23.29  ?  286 ILE A CD1   1 
ATOM   2032  N  N     . ALA A  1  255 ? 29.816 -16.505 3.377   1.00 23.63  ?  287 ALA A N     1 
ATOM   2033  C  CA    . ALA A  1  255 ? 30.660 -15.557 4.078   1.00 23.16  ?  287 ALA A CA    1 
ATOM   2034  C  C     . ALA A  1  255 ? 30.168 -14.148 3.875   1.00 22.54  ?  287 ALA A C     1 
ATOM   2035  O  O     . ALA A  1  255 ? 30.811 -13.199 4.317   1.00 22.75  ?  287 ALA A O     1 
ATOM   2036  C  CB    . ALA A  1  255 ? 32.097 -15.691 3.588   1.00 23.64  ?  287 ALA A CB    1 
ATOM   2037  N  N     . GLY A  1  256 ? 29.034 -14.014 3.196   1.00 23.11  ?  288 GLY A N     1 
ATOM   2038  C  CA    . GLY A  1  256 ? 28.405 -12.706 2.968   1.00 23.49  ?  288 GLY A CA    1 
ATOM   2039  C  C     . GLY A  1  256 ? 27.351 -12.733 1.868   1.00 22.20  ?  288 GLY A C     1 
ATOM   2040  O  O     . GLY A  1  256 ? 27.438 -13.537 0.940   1.00 22.29  ?  288 GLY A O     1 
ATOM   2041  N  N     . GLN A  1  257 ? 26.353 -11.861 1.986   1.00 20.32  ?  289 GLN A N     1 
ATOM   2042  C  CA    . GLN A  1  257 ? 25.308 -11.750 0.993   1.00 18.91  ?  289 GLN A CA    1 
ATOM   2043  C  C     . GLN A  1  257 ? 25.123 -10.312 0.603   1.00 19.32  ?  289 GLN A C     1 
ATOM   2044  O  O     . GLN A  1  257 ? 25.403 -9.397  1.379   1.00 18.75  ?  289 GLN A O     1 
ATOM   2045  C  CB    . GLN A  1  257 ? 24.008 -12.281 1.512   1.00 17.77  ?  289 GLN A CB    1 
ATOM   2046  C  CG    . GLN A  1  257 ? 24.109 -13.688 2.006   1.00 17.43  ?  289 GLN A CG    1 
ATOM   2047  C  CD    . GLN A  1  257 ? 22.785 -14.170 2.536   1.00 17.58  ?  289 GLN A CD    1 
ATOM   2048  O  OE1   . GLN A  1  257 ? 21.772 -14.078 1.857   1.00 17.81  ?  289 GLN A OE1   1 
ATOM   2049  N  NE2   . GLN A  1  257 ? 22.780 -14.674 3.758   1.00 17.62  ?  289 GLN A NE2   1 
ATOM   2050  N  N     . PHE A  1  258 ? 24.631 -10.139 -0.620  1.00 19.72  ?  290 PHE A N     1 
ATOM   2051  C  CA    . PHE A  1  258 ? 24.659 -8.855  -1.306  1.00 19.92  ?  290 PHE A CA    1 
ATOM   2052  C  C     . PHE A  1  258 ? 23.447 -8.714  -2.223  1.00 19.13  ?  290 PHE A C     1 
ATOM   2053  O  O     . PHE A  1  258 ? 23.174 -9.575  -3.058  1.00 19.91  ?  290 PHE A O     1 
ATOM   2054  C  CB    . PHE A  1  258 ? 25.974 -8.721  -2.096  1.00 20.01  ?  290 PHE A CB    1 
ATOM   2055  C  CG    . PHE A  1  258 ? 27.187 -9.027  -1.274  1.00 20.37  ?  290 PHE A CG    1 
ATOM   2056  C  CD1   . PHE A  1  258 ? 27.832 -8.024  -0.571  1.00 21.14  ?  290 PHE A CD1   1 
ATOM   2057  C  CD2   . PHE A  1  258 ? 27.650 -10.326 -1.156  1.00 20.26  ?  290 PHE A CD2   1 
ATOM   2058  C  CE1   . PHE A  1  258 ? 28.947 -8.309  0.206   1.00 21.66  ?  290 PHE A CE1   1 
ATOM   2059  C  CE2   . PHE A  1  258 ? 28.743 -10.618 -0.377  1.00 20.64  ?  290 PHE A CE2   1 
ATOM   2060  C  CZ    . PHE A  1  258 ? 29.397 -9.613  0.305   1.00 21.13  ?  290 PHE A CZ    1 
ATOM   2061  N  N     . TYR A  1  259 ? 22.726 -7.619  -2.070  1.00 17.67  ?  291 TYR A N     1 
ATOM   2062  C  CA    . TYR A  1  259 ? 21.535 -7.415  -2.834  1.00 16.80  ?  291 TYR A CA    1 
ATOM   2063  C  C     . TYR A  1  259 ? 21.402 -5.965  -3.232  1.00 16.64  ?  291 TYR A C     1 
ATOM   2064  O  O     . TYR A  1  259 ? 22.196 -5.113  -2.815  1.00 16.96  ?  291 TYR A O     1 
ATOM   2065  C  CB    . TYR A  1  259 ? 20.351 -7.771  -1.975  1.00 17.02  ?  291 TYR A CB    1 
ATOM   2066  C  CG    . TYR A  1  259 ? 20.358 -9.154  -1.411  1.00 16.73  ?  291 TYR A CG    1 
ATOM   2067  C  CD1   . TYR A  1  259 ? 19.910 -10.206 -2.157  1.00 16.86  ?  291 TYR A CD1   1 
ATOM   2068  C  CD2   . TYR A  1  259 ? 20.775 -9.399  -0.123  1.00 16.75  ?  291 TYR A CD2   1 
ATOM   2069  C  CE1   . TYR A  1  259 ? 19.879 -11.487 -1.648  1.00 17.11  ?  291 TYR A CE1   1 
ATOM   2070  C  CE2   . TYR A  1  259 ? 20.744 -10.677 0.405   1.00 17.09  ?  291 TYR A CE2   1 
ATOM   2071  C  CZ    . TYR A  1  259 ? 20.296 -11.726 -0.373  1.00 17.26  ?  291 TYR A CZ    1 
ATOM   2072  O  OH    . TYR A  1  259 ? 20.263 -13.025 0.089   1.00 17.12  ?  291 TYR A OH    1 
ATOM   2073  N  N     . GLY A  1  260 ? 20.375 -5.691  -4.038  1.00 16.15  ?  292 GLY A N     1 
ATOM   2074  C  CA    . GLY A  1  260 ? 20.011 -4.331  -4.437  1.00 15.31  ?  292 GLY A CA    1 
ATOM   2075  C  C     . GLY A  1  260 ? 18.517 -4.182  -4.333  1.00 14.81  ?  292 GLY A C     1 
ATOM   2076  O  O     . GLY A  1  260 ? 17.932 -4.467  -3.301  1.00 13.99  ?  292 GLY A O     1 
ATOM   2077  N  N     . HIS A  1  261 ? 17.910 -3.736  -5.421  1.00 15.09  ?  293 HIS A N     1 
ATOM   2078  C  CA    . HIS A  1  261 ? 16.462 -3.705  -5.606  1.00 14.85  ?  293 HIS A CA    1 
ATOM   2079  C  C     . HIS A  1  261 ? 15.809 -2.601  -4.797  1.00 14.38  ?  293 HIS A C     1 
ATOM   2080  O  O     . HIS A  1  261 ? 15.145 -1.797  -5.374  1.00 14.94  ?  293 HIS A O     1 
ATOM   2081  C  CB    . HIS A  1  261 ? 15.819 -5.067  -5.346  1.00 15.13  ?  293 HIS A CB    1 
ATOM   2082  C  CG    . HIS A  1  261 ? 14.332 -5.055  -5.463  1.00 16.07  ?  293 HIS A CG    1 
ATOM   2083  N  ND1   . HIS A  1  261 ? 13.673 -4.729  -6.629  1.00 16.56  ?  293 HIS A ND1   1 
ATOM   2084  C  CD2   . HIS A  1  261 ? 13.366 -5.343  -4.557  1.00 16.77  ?  293 HIS A CD2   1 
ATOM   2085  C  CE1   . HIS A  1  261 ? 12.367 -4.797  -6.434  1.00 16.84  ?  293 HIS A CE1   1 
ATOM   2086  N  NE2   . HIS A  1  261 ? 12.152 -5.168  -5.183  1.00 17.10  ?  293 HIS A NE2   1 
ATOM   2087  N  N     . THR A  1  262 ? 16.037 -2.506  -3.492  1.00 13.88  ?  294 THR A N     1 
ATOM   2088  C  CA    . THR A  1  262 ? 15.406 -1.438  -2.677  1.00 13.28  ?  294 THR A CA    1 
ATOM   2089  C  C     . THR A  1  262 ? 15.906 -0.030  -2.934  1.00 12.93  ?  294 THR A C     1 
ATOM   2090  O  O     . THR A  1  262 ? 15.272 0.920   -2.496  1.00 12.52  ?  294 THR A O     1 
ATOM   2091  C  CB    . THR A  1  262 ? 15.638 -1.636  -1.171  1.00 13.36  ?  294 THR A CB    1 
ATOM   2092  O  OG1   . THR A  1  262 ? 17.010 -1.329  -0.850  1.00 13.43  ?  294 THR A OG1   1 
ATOM   2093  C  CG2   . THR A  1  262 ? 15.258 -3.063  -0.734  1.00 13.38  ?  294 THR A CG2   1 
ATOM   2094  N  N     . HIS A  1  263 ? 17.063 0.099   -3.581  1.00 13.08  ?  295 HIS A N     1 
ATOM   2095  C  CA    . HIS A  1  263 ? 17.704 1.397   -3.808  1.00 13.21  ?  295 HIS A CA    1 
ATOM   2096  C  C     . HIS A  1  263 ? 18.148 2.083   -2.494  1.00 13.05  ?  295 HIS A C     1 
ATOM   2097  O  O     . HIS A  1  263 ? 18.390 3.294   -2.444  1.00 12.77  ?  295 HIS A O     1 
ATOM   2098  C  CB    . HIS A  1  263 ? 16.757 2.335   -4.562  1.00 13.62  ?  295 HIS A CB    1 
ATOM   2099  C  CG    . HIS A  1  263 ? 16.531 1.966   -5.988  1.00 13.67  ?  295 HIS A CG    1 
ATOM   2100  N  ND1   . HIS A  1  263 ? 16.196 2.907   -6.945  1.00 14.03  ?  295 HIS A ND1   1 
ATOM   2101  C  CD2   . HIS A  1  263 ? 16.606 0.777   -6.628  1.00 13.44  ?  295 HIS A CD2   1 
ATOM   2102  C  CE1   . HIS A  1  263 ? 16.059 2.299   -8.113  1.00 13.93  ?  295 HIS A CE1   1 
ATOM   2103  N  NE2   . HIS A  1  263 ? 16.311 1.011   -7.949  1.00 13.49  ?  295 HIS A NE2   1 
ATOM   2104  N  N     . ARG A  1  264 ? 18.276 1.318   -1.426  1.00 12.89  ?  296 ARG A N     1 
ATOM   2105  C  CA    . ARG A  1  264 ? 18.573 1.916   -0.140  1.00 12.77  ?  296 ARG A CA    1 
ATOM   2106  C  C     . ARG A  1  264 ? 19.712 1.181   0.525   1.00 12.78  ?  296 ARG A C     1 
ATOM   2107  O  O     . ARG A  1  264 ? 19.941 -0.001  0.254   1.00 12.93  ?  296 ARG A O     1 
ATOM   2108  C  CB    . ARG A  1  264 ? 17.335 1.848   0.750   1.00 12.66  ?  296 ARG A CB    1 
ATOM   2109  C  CG    . ARG A  1  264 ? 16.099 2.499   0.154   1.00 12.40  ?  296 ARG A CG    1 
ATOM   2110  C  CD    . ARG A  1  264 ? 16.061 3.966   0.465   1.00 12.58  ?  296 ARG A CD    1 
ATOM   2111  N  NE    . ARG A  1  264 ? 15.048 4.642   -0.337  1.00 12.95  ?  296 ARG A NE    1 
ATOM   2112  C  CZ    . ARG A  1  264 ? 15.237 5.089   -1.578  1.00 13.21  ?  296 ARG A CZ    1 
ATOM   2113  N  NH1   . ARG A  1  264 ? 16.396 4.937   -2.188  1.00 13.53  1  296 ARG A NH1   1 
ATOM   2114  N  NH2   . ARG A  1  264 ? 14.258 5.693   -2.226  1.00 13.65  ?  296 ARG A NH2   1 
ATOM   2115  N  N     . ASP A  1  265 ? 20.414 1.881   1.404   1.00 12.83  ?  297 ASP A N     1 
ATOM   2116  C  CA    . ASP A  1  265 ? 21.516 1.286   2.155   1.00 12.95  ?  297 ASP A CA    1 
ATOM   2117  C  C     . ASP A  1  265 ? 20.987 0.567   3.394   1.00 12.98  ?  297 ASP A C     1 
ATOM   2118  O  O     . ASP A  1  265 ? 20.552 1.216   4.342   1.00 12.87  ?  297 ASP A O     1 
ATOM   2119  C  CB    . ASP A  1  265 ? 22.488 2.379   2.585   1.00 12.77  ?  297 ASP A CB    1 
ATOM   2120  C  CG    . ASP A  1  265 ? 23.742 1.821   3.172   1.00 12.75  ?  297 ASP A CG    1 
ATOM   2121  O  OD1   . ASP A  1  265 ? 23.672 0.732   3.804   1.00 13.04  ?  297 ASP A OD1   1 
ATOM   2122  O  OD2   . ASP A  1  265 ? 24.801 2.454   2.983   1.00 12.51  -1 297 ASP A OD2   1 
ATOM   2123  N  N     . SER A  1  266 ? 21.033 -0.754  3.397   1.00 12.97  ?  298 SER A N     1 
ATOM   2124  C  CA    . SER A  1  266 ? 20.474 -1.508  4.508   1.00 13.84  ?  298 SER A CA    1 
ATOM   2125  C  C     . SER A  1  266 ? 21.376 -2.646  4.960   1.00 14.66  ?  298 SER A C     1 
ATOM   2126  O  O     . SER A  1  266 ? 22.088 -3.224  4.140   1.00 15.80  ?  298 SER A O     1 
ATOM   2127  C  CB    . SER A  1  266 ? 19.105 -2.069  4.126   1.00 13.90  ?  298 SER A CB    1 
ATOM   2128  O  OG    . SER A  1  266 ? 18.058 -1.204  4.534   1.00 14.54  ?  298 SER A OG    1 
ATOM   2129  N  N     . ILE A  1  267 ? 21.380 -2.963  6.256   1.00 15.10  ?  299 ILE A N     1 
ATOM   2130  C  CA    . ILE A  1  267 ? 21.965 -4.236  6.676   1.00 16.00  ?  299 ILE A CA    1 
ATOM   2131  C  C     . ILE A  1  267 ? 20.887 -5.173  7.199   1.00 16.18  ?  299 ILE A C     1 
ATOM   2132  O  O     . ILE A  1  267 ? 19.786 -4.770  7.568   1.00 16.24  ?  299 ILE A O     1 
ATOM   2133  C  CB    . ILE A  1  267 ? 23.068 -4.125  7.748   1.00 16.73  ?  299 ILE A CB    1 
ATOM   2134  C  CG1   . ILE A  1  267 ? 22.491 -3.599  9.039   1.00 18.05  ?  299 ILE A CG1   1 
ATOM   2135  C  CG2   . ILE A  1  267 ? 24.212 -3.218  7.328   1.00 16.69  ?  299 ILE A CG2   1 
ATOM   2136  C  CD1   . ILE A  1  267 ? 23.476 -3.685  10.183  1.00 19.09  ?  299 ILE A CD1   1 
ATOM   2137  N  N     . MET A  1  268 ? 21.221 -6.444  7.212   1.00 16.73  ?  300 MET A N     1 
ATOM   2138  C  CA    . MET A  1  268 ? 20.367 -7.452  7.818   1.00 17.28  ?  300 MET A CA    1 
ATOM   2139  C  C     . MET A  1  268 ? 21.255 -8.516  8.412   1.00 16.81  ?  300 MET A C     1 
ATOM   2140  O  O     . MET A  1  268 ? 22.406 -8.683  7.984   1.00 16.71  ?  300 MET A O     1 
ATOM   2141  C  CB    . MET A  1  268 ? 19.428 -8.087  6.796   1.00 17.49  ?  300 MET A CB    1 
ATOM   2142  C  CG    . MET A  1  268 ? 18.120 -7.355  6.634   1.00 17.52  ?  300 MET A CG    1 
ATOM   2143  S  SD    . MET A  1  268 ? 17.156 -8.175  5.356   1.00 18.30  ?  300 MET A SD    1 
ATOM   2144  C  CE    . MET A  1  268 ? 18.023 -7.747  3.852   1.00 18.45  ?  300 MET A CE    1 
ATOM   2145  N  N     . VAL A  1  269 ? 20.704 -9.224  9.391   1.00 16.20  ?  301 VAL A N     1 
ATOM   2146  C  CA    . VAL A  1  269 ? 21.445 -10.216 10.115  1.00 16.25  ?  301 VAL A CA    1 
ATOM   2147  C  C     . VAL A  1  269 ? 20.589 -11.432 10.231  1.00 17.00  ?  301 VAL A C     1 
ATOM   2148  O  O     . VAL A  1  269 ? 19.541 -11.409 10.866  1.00 17.21  ?  301 VAL A O     1 
ATOM   2149  C  CB    . VAL A  1  269 ? 21.814 -9.733  11.512  1.00 16.14  ?  301 VAL A CB    1 
ATOM   2150  C  CG1   . VAL A  1  269 ? 22.685 -10.776 12.187  1.00 16.13  ?  301 VAL A CG1   1 
ATOM   2151  C  CG2   . VAL A  1  269 ? 22.555 -8.405  11.420  1.00 16.34  ?  301 VAL A CG2   1 
ATOM   2152  N  N     . LEU A  1  270 ? 21.036 -12.497 9.597   1.00 18.22  ?  302 LEU A N     1 
ATOM   2153  C  CA    . LEU A  1  270 ? 20.317 -13.751 9.633   1.00 19.27  ?  302 LEU A CA    1 
ATOM   2154  C  C     . LEU A  1  270 ? 20.653 -14.400 10.955  1.00 20.44  ?  302 LEU A C     1 
ATOM   2155  O  O     . LEU A  1  270 ? 21.821 -14.399 11.357  1.00 20.61  ?  302 LEU A O     1 
ATOM   2156  C  CB    . LEU A  1  270 ? 20.782 -14.621 8.474   1.00 19.11  ?  302 LEU A CB    1 
ATOM   2157  C  CG    . LEU A  1  270 ? 20.221 -16.032 8.416   1.00 19.58  ?  302 LEU A CG    1 
ATOM   2158  C  CD1   . LEU A  1  270 ? 18.701 -16.008 8.441   1.00 19.35  ?  302 LEU A CD1   1 
ATOM   2159  C  CD2   . LEU A  1  270 ? 20.752 -16.741 7.163   1.00 20.01  ?  302 LEU A CD2   1 
ATOM   2160  N  N     . SER A  1  271 ? 19.654 -14.911 11.658  1.00 22.39  ?  303 SER A N     1 
ATOM   2161  C  CA    . SER A  1  271 ? 19.936 -15.693 12.870  1.00 25.29  ?  303 SER A CA    1 
ATOM   2162  C  C     . SER A  1  271 ? 19.627 -17.173 12.658  1.00 28.26  ?  303 SER A C     1 
ATOM   2163  O  O     . SER A  1  271 ? 18.896 -17.538 11.751  1.00 28.79  ?  303 SER A O     1 
ATOM   2164  C  CB    . SER A  1  271 ? 19.177 -15.138 14.075  1.00 25.08  ?  303 SER A CB    1 
ATOM   2165  O  OG    . SER A  1  271 ? 19.582 -13.803 14.347  1.00 24.96  ?  303 SER A OG    1 
ATOM   2166  N  N     . ASP A  1  272 ? 20.211 -18.040 13.469  1.00 32.94  ?  304 ASP A N     1 
ATOM   2167  C  CA    . ASP A  1  272 ? 19.918 -19.463 13.332  1.00 36.37  ?  304 ASP A CA    1 
ATOM   2168  C  C     . ASP A  1  272 ? 18.541 -19.712 13.960  1.00 38.67  ?  304 ASP A C     1 
ATOM   2169  O  O     . ASP A  1  272 ? 17.968 -18.827 14.601  1.00 36.98  ?  304 ASP A O     1 
ATOM   2170  C  CB    . ASP A  1  272 ? 21.058 -20.363 13.897  1.00 37.64  ?  304 ASP A CB    1 
ATOM   2171  C  CG    . ASP A  1  272 ? 21.206 -20.294 15.431  1.00 38.78  ?  304 ASP A CG    1 
ATOM   2172  O  OD1   . ASP A  1  272 ? 20.495 -19.499 16.083  1.00 40.26  ?  304 ASP A OD1   1 
ATOM   2173  O  OD2   . ASP A  1  272 ? 22.042 -21.048 15.992  1.00 39.54  -1 304 ASP A OD2   1 
ATOM   2174  N  N     . LYS A  1  273 ? 18.000 -20.900 13.748  1.00 43.06  ?  305 LYS A N     1 
ATOM   2175  C  CA    . LYS A  1  273 ? 16.701 -21.252 14.296  1.00 47.61  ?  305 LYS A CA    1 
ATOM   2176  C  C     . LYS A  1  273 ? 16.671 -21.038 15.801  1.00 46.72  ?  305 LYS A C     1 
ATOM   2177  O  O     . LYS A  1  273 ? 15.632 -20.744 16.366  1.00 47.12  ?  305 LYS A O     1 
ATOM   2178  C  CB    . LYS A  1  273 ? 16.384 -22.709 13.962  1.00 54.73  ?  305 LYS A CB    1 
ATOM   2179  C  CG    . LYS A  1  273 ? 15.985 -22.946 12.506  1.00 60.56  ?  305 LYS A CG    1 
ATOM   2180  C  CD    . LYS A  1  273 ? 14.463 -22.903 12.355  1.00 67.55  ?  305 LYS A CD    1 
ATOM   2181  C  CE    . LYS A  1  273 ? 13.998 -22.722 10.913  1.00 72.71  ?  305 LYS A CE    1 
ATOM   2182  N  NZ    . LYS A  1  273 ? 14.554 -23.765 10.006  1.00 73.92  1  305 LYS A NZ    1 
ATOM   2183  N  N     . LYS A  1  274 ? 17.825 -21.185 16.438  1.00 48.31  ?  306 LYS A N     1 
ATOM   2184  C  CA    . LYS A  1  274 ? 17.973 -20.969 17.880  1.00 51.20  ?  306 LYS A CA    1 
ATOM   2185  C  C     . LYS A  1  274 ? 17.861 -19.491 18.304  1.00 45.68  ?  306 LYS A C     1 
ATOM   2186  O  O     . LYS A  1  274 ? 17.539 -19.209 19.447  1.00 44.88  ?  306 LYS A O     1 
ATOM   2187  C  CB    . LYS A  1  274 ? 19.329 -21.544 18.357  1.00 57.72  ?  306 LYS A CB    1 
ATOM   2188  C  CG    . LYS A  1  274 ? 19.337 -22.166 19.758  1.00 62.10  ?  306 LYS A CG    1 
ATOM   2189  C  CD    . LYS A  1  274 ? 19.250 -23.697 19.737  1.00 65.70  ?  306 LYS A CD    1 
ATOM   2190  C  CE    . LYS A  1  274 ? 17.819 -24.220 19.658  1.00 67.49  ?  306 LYS A CE    1 
ATOM   2191  N  NZ    . LYS A  1  274 ? 17.084 -23.999 20.938  1.00 70.60  1  306 LYS A NZ    1 
ATOM   2192  N  N     . GLY A  1  275 ? 18.144 -18.563 17.395  1.00 41.74  ?  307 GLY A N     1 
ATOM   2193  C  CA    . GLY A  1  275 ? 18.089 -17.125 17.688  1.00 39.43  ?  307 GLY A CA    1 
ATOM   2194  C  C     . GLY A  1  275 ? 19.445 -16.439 17.797  1.00 38.11  ?  307 GLY A C     1 
ATOM   2195  O  O     . GLY A  1  275 ? 19.535 -15.341 18.328  1.00 38.74  ?  307 GLY A O     1 
ATOM   2196  N  N     . SER A  1  276 ? 20.491 -17.069 17.263  1.00 36.31  ?  308 SER A N     1 
ATOM   2197  C  CA    . SER A  1  276 ? 21.877 -16.583 17.358  1.00 33.35  ?  308 SER A CA    1 
ATOM   2198  C  C     . SER A  1  276 ? 22.357 -16.080 15.989  1.00 29.93  ?  308 SER A C     1 
ATOM   2199  O  O     . SER A  1  276 ? 22.255 -16.813 15.015  1.00 29.77  ?  308 SER A O     1 
ATOM   2200  C  CB    . SER A  1  276 ? 22.767 -17.746 17.791  1.00 33.90  ?  308 SER A CB    1 
ATOM   2201  O  OG    . SER A  1  276 ? 23.568 -17.391 18.887  1.00 36.94  ?  308 SER A OG    1 
ATOM   2202  N  N     . PRO A  1  277 ? 22.887 -14.846 15.899  1.00 26.14  ?  309 PRO A N     1 
ATOM   2203  C  CA    . PRO A  1  277 ? 23.268 -14.309 14.593  1.00 24.55  ?  309 PRO A CA    1 
ATOM   2204  C  C     . PRO A  1  277 ? 24.282 -15.177 13.892  1.00 23.38  ?  309 PRO A C     1 
ATOM   2205  O  O     . PRO A  1  277 ? 25.197 -15.652 14.533  1.00 23.29  ?  309 PRO A O     1 
ATOM   2206  C  CB    . PRO A  1  277 ? 23.906 -12.966 14.932  1.00 24.86  ?  309 PRO A CB    1 
ATOM   2207  C  CG    . PRO A  1  277 ? 24.319 -13.070 16.350  1.00 25.52  ?  309 PRO A CG    1 
ATOM   2208  C  CD    . PRO A  1  277 ? 23.266 -13.933 16.982  1.00 26.03  ?  309 PRO A CD    1 
ATOM   2209  N  N     . VAL A  1  278 ? 24.111 -15.388 12.592  1.00 23.08  ?  310 VAL A N     1 
ATOM   2210  C  CA    . VAL A  1  278 ? 24.977 -16.312 11.840  1.00 22.63  ?  310 VAL A CA    1 
ATOM   2211  C  C     . VAL A  1  278 ? 25.305 -15.901 10.420  1.00 20.99  ?  310 VAL A C     1 
ATOM   2212  O  O     . VAL A  1  278 ? 26.081 -16.564 9.789   1.00 21.10  ?  310 VAL A O     1 
ATOM   2213  C  CB    . VAL A  1  278 ? 24.376 -17.753 11.746  1.00 23.92  ?  310 VAL A CB    1 
ATOM   2214  C  CG1   . VAL A  1  278 ? 24.255 -18.396 13.122  1.00 23.92  ?  310 VAL A CG1   1 
ATOM   2215  C  CG2   . VAL A  1  278 ? 23.019 -17.770 11.031  1.00 24.25  ?  310 VAL A CG2   1 
ATOM   2216  N  N     . ASN A  1  279 ? 24.712 -14.855 9.877   1.00 20.14  ?  311 ASN A N     1 
ATOM   2217  C  CA    . ASN A  1  279 ? 25.101 -14.442 8.524   1.00 19.81  ?  311 ASN A CA    1 
ATOM   2218  C  C     . ASN A  1  279 ? 24.775 -12.976 8.371   1.00 18.39  ?  311 ASN A C     1 
ATOM   2219  O  O     . ASN A  1  279 ? 23.728 -12.531 8.848   1.00 18.22  ?  311 ASN A O     1 
ATOM   2220  C  CB    . ASN A  1  279 ? 24.372 -15.281 7.450   1.00 20.58  ?  311 ASN A CB    1 
ATOM   2221  C  CG    . ASN A  1  279 ? 25.263 -15.626 6.258   1.00 20.97  ?  311 ASN A CG    1 
ATOM   2222  O  OD1   . ASN A  1  279 ? 25.520 -14.799 5.379   1.00 22.67  ?  311 ASN A OD1   1 
ATOM   2223  N  ND2   . ASN A  1  279 ? 25.734 -16.846 6.230   1.00 20.48  ?  311 ASN A ND2   1 
ATOM   2224  N  N     . SER A  1  280 ? 25.681 -12.232 7.744   1.00 16.80  ?  312 SER A N     1 
ATOM   2225  C  CA    . SER A  1  280 ? 25.472 -10.818 7.497   1.00 15.78  ?  312 SER A CA    1 
ATOM   2226  C  C     . SER A  1  280 ? 25.083 -10.606 6.059   1.00 15.38  ?  312 SER A C     1 
ATOM   2227  O  O     . SER A  1  280 ? 25.689 -11.209 5.147   1.00 15.52  ?  312 SER A O     1 
ATOM   2228  C  CB    . SER A  1  280 ? 26.746 -10.053 7.749   1.00 15.80  ?  312 SER A CB    1 
ATOM   2229  O  OG    . SER A  1  280 ? 27.120 -10.192 9.084   1.00 16.10  ?  312 SER A OG    1 
ATOM   2230  N  N     . LEU A  1  281 ? 24.096 -9.728  5.879   1.00 14.52  ?  313 LEU A N     1 
ATOM   2231  C  CA    . LEU A  1  281 ? 23.532 -9.391  4.588   1.00 14.21  ?  313 LEU A CA    1 
ATOM   2232  C  C     . LEU A  1  281 ? 23.679 -7.898  4.333   1.00 13.79  ?  313 LEU A C     1 
ATOM   2233  O  O     . LEU A  1  281 ? 23.619 -7.090  5.250   1.00 13.83  ?  313 LEU A O     1 
ATOM   2234  C  CB    . LEU A  1  281 ? 22.064 -9.763  4.583   1.00 14.51  ?  313 LEU A CB    1 
ATOM   2235  C  CG    . LEU A  1  281 ? 21.821 -11.276 4.599   1.00 15.12  ?  313 LEU A CG    1 
ATOM   2236  C  CD1   . LEU A  1  281 ? 22.005 -11.879 5.973   1.00 15.62  ?  313 LEU A CD1   1 
ATOM   2237  C  CD2   . LEU A  1  281 ? 20.433 -11.648 4.120   1.00 15.45  ?  313 LEU A CD2   1 
ATOM   2238  N  N     . PHE A  1  282 ? 23.875 -7.527  3.080   1.00 13.39  ?  314 PHE A N     1 
ATOM   2239  C  CA    . PHE A  1  282 ? 24.173 -6.138  2.739   1.00 13.16  ?  314 PHE A CA    1 
ATOM   2240  C  C     . PHE A  1  282 ? 23.429 -5.724  1.504   1.00 12.80  ?  314 PHE A C     1 
ATOM   2241  O  O     . PHE A  1  282 ? 23.672 -6.262  0.424   1.00 13.03  ?  314 PHE A O     1 
ATOM   2242  C  CB    . PHE A  1  282 ? 25.657 -5.990  2.497   1.00 13.20  ?  314 PHE A CB    1 
ATOM   2243  C  CG    . PHE A  1  282 ? 26.460 -6.343  3.693   1.00 13.66  ?  314 PHE A CG    1 
ATOM   2244  C  CD1   . PHE A  1  282 ? 26.847 -5.349  4.594   1.00 13.67  ?  314 PHE A CD1   1 
ATOM   2245  C  CD2   . PHE A  1  282 ? 26.766 -7.682  3.973   1.00 13.62  ?  314 PHE A CD2   1 
ATOM   2246  C  CE1   . PHE A  1  282 ? 27.570 -5.674  5.725   1.00 13.70  ?  314 PHE A CE1   1 
ATOM   2247  C  CE2   . PHE A  1  282 ? 27.482 -8.013  5.102   1.00 13.70  ?  314 PHE A CE2   1 
ATOM   2248  C  CZ    . PHE A  1  282 ? 27.893 -7.005  5.980   1.00 13.88  ?  314 PHE A CZ    1 
ATOM   2249  N  N     . VAL A  1  283 ? 22.510 -4.781  1.676   1.00 12.07  ?  315 VAL A N     1 
ATOM   2250  C  CA    . VAL A  1  283 ? 21.773 -4.229  0.572   1.00 11.63  ?  315 VAL A CA    1 
ATOM   2251  C  C     . VAL A  1  283 ? 22.336 -2.867  0.222   1.00 11.57  ?  315 VAL A C     1 
ATOM   2252  O  O     . VAL A  1  283 ? 22.290 -1.923  1.010   1.00 11.72  ?  315 VAL A O     1 
ATOM   2253  C  CB    . VAL A  1  283 ? 20.294 -4.091  0.892   1.00 11.49  ?  315 VAL A CB    1 
ATOM   2254  C  CG1   . VAL A  1  283 ? 19.569 -3.499  -0.315  1.00 11.41  ?  315 VAL A CG1   1 
ATOM   2255  C  CG2   . VAL A  1  283 ? 19.708 -5.442  1.326   1.00 11.33  ?  315 VAL A CG2   1 
ATOM   2256  N  N     . ALA A  1  284 ? 22.838 -2.774  -0.994  1.00 11.46  ?  316 ALA A N     1 
ATOM   2257  C  CA    . ALA A  1  284 ? 23.505 -1.595  -1.470  1.00 11.42  ?  316 ALA A CA    1 
ATOM   2258  C  C     . ALA A  1  284 ? 22.526 -0.681  -2.143  1.00 11.38  ?  316 ALA A C     1 
ATOM   2259  O  O     . ALA A  1  284 ? 21.675 -1.139  -2.896  1.00 11.43  ?  316 ALA A O     1 
ATOM   2260  C  CB    . ALA A  1  284 ? 24.552 -2.014  -2.478  1.00 11.79  ?  316 ALA A CB    1 
ATOM   2261  N  N     . PRO A  1  285 ? 22.668 0.625   -1.936  1.00 11.59  ?  317 PRO A N     1 
ATOM   2262  C  CA    . PRO A  1  285 ? 21.732 1.511   -2.603  1.00 11.94  ?  317 PRO A CA    1 
ATOM   2263  C  C     . PRO A  1  285 ? 22.091 1.691   -4.080  1.00 12.08  ?  317 PRO A C     1 
ATOM   2264  O  O     . PRO A  1  285 ? 23.154 1.276   -4.522  1.00 12.94  ?  317 PRO A O     1 
ATOM   2265  C  CB    . PRO A  1  285 ? 21.888 2.829   -1.829  1.00 11.70  ?  317 PRO A CB    1 
ATOM   2266  C  CG    . PRO A  1  285 ? 23.331 2.826   -1.445  1.00 11.81  ?  317 PRO A CG    1 
ATOM   2267  C  CD    . PRO A  1  285 ? 23.784 1.378   -1.352  1.00 11.79  ?  317 PRO A CD    1 
ATOM   2268  N  N     . ALA A  1  286 ? 21.206 2.358   -4.800  1.00 12.00  ?  318 ALA A N     1 
ATOM   2269  C  CA    . ALA A  1  286 ? 21.233 2.437   -6.250  1.00 11.56  ?  318 ALA A CA    1 
ATOM   2270  C  C     . ALA A  1  286 ? 22.117 3.555   -6.749  1.00 10.84  ?  318 ALA A C     1 
ATOM   2271  O  O     . ALA A  1  286 ? 22.450 4.471   -5.989  1.00 10.14  ?  318 ALA A O     1 
ATOM   2272  C  CB    . ALA A  1  286 ? 19.801 2.657   -6.757  1.00 11.76  ?  318 ALA A CB    1 
ATOM   2273  N  N     . VAL A  1  287 ? 22.470 3.457   -8.038  1.00 10.48  ?  319 VAL A N     1 
ATOM   2274  C  CA    . VAL A  1  287 ? 23.113 4.561   -8.758  1.00 10.38  ?  319 VAL A CA    1 
ATOM   2275  C  C     . VAL A  1  287 ? 22.067 5.586   -9.187  1.00 10.30  ?  319 VAL A C     1 
ATOM   2276  O  O     . VAL A  1  287 ? 22.302 6.811   -9.081  1.00 10.62  ?  319 VAL A O     1 
ATOM   2277  C  CB    . VAL A  1  287 ? 23.933 4.106   -9.994  1.00 10.28  ?  319 VAL A CB    1 
ATOM   2278  C  CG1   . VAL A  1  287 ? 24.498 5.316   -10.734 1.00 10.14  ?  319 VAL A CG1   1 
ATOM   2279  C  CG2   . VAL A  1  287 ? 25.085 3.201   -9.577  1.00 10.37  ?  319 VAL A CG2   1 
ATOM   2280  N  N     . THR A  1  288 ? 20.932 5.109   -9.694  1.00 9.87   ?  320 THR A N     1 
ATOM   2281  C  CA    . THR A  1  288 ? 19.867 6.030   -10.036 1.00 9.69   ?  320 THR A CA    1 
ATOM   2282  C  C     . THR A  1  288 ? 19.339 6.695   -8.778  1.00 9.70   ?  320 THR A C     1 
ATOM   2283  O  O     . THR A  1  288 ? 19.181 6.051   -7.763  1.00 9.83   ?  320 THR A O     1 
ATOM   2284  C  CB    . THR A  1  288 ? 18.685 5.359   -10.753 1.00 9.61   ?  320 THR A CB    1 
ATOM   2285  O  OG1   . THR A  1  288 ? 17.655 6.343   -10.975 1.00 9.48   ?  320 THR A OG1   1 
ATOM   2286  C  CG2   . THR A  1  288 ? 18.114 4.218   -9.939  1.00 9.55   ?  320 THR A CG2   1 
ATOM   2287  N  N     . PRO A  1  289 ? 19.036 7.977   -8.853  1.00 9.66   ?  321 PRO A N     1 
ATOM   2288  C  CA    . PRO A  1  289 ? 18.380 8.710   -7.806  1.00 10.10  ?  321 PRO A CA    1 
ATOM   2289  C  C     . PRO A  1  289 ? 16.839 8.763   -7.909  1.00 10.99  ?  321 PRO A C     1 
ATOM   2290  O  O     . PRO A  1  289 ? 16.177 9.545   -7.176  1.00 10.82  ?  321 PRO A O     1 
ATOM   2291  C  CB    . PRO A  1  289 ? 18.898 10.115  -8.044  1.00 9.95   ?  321 PRO A CB    1 
ATOM   2292  C  CG    . PRO A  1  289 ? 18.980 10.203  -9.512  1.00 9.79   ?  321 PRO A CG    1 
ATOM   2293  C  CD    . PRO A  1  289 ? 19.319 8.827   -10.006 1.00 9.67   ?  321 PRO A CD    1 
ATOM   2294  N  N     . VAL A  1  290 ? 16.271 7.971   -8.810  1.00 11.87  ?  322 VAL A N     1 
ATOM   2295  C  CA    . VAL A  1  290 ? 14.898 8.198   -9.243  1.00 12.78  ?  322 VAL A CA    1 
ATOM   2296  C  C     . VAL A  1  290 ? 13.905 7.997   -8.082  1.00 13.14  ?  322 VAL A C     1 
ATOM   2297  O  O     . VAL A  1  290 ? 14.178 7.218   -7.161  1.00 14.17  ?  322 VAL A O     1 
ATOM   2298  C  CB    . VAL A  1  290 ? 14.549 7.308   -10.483 1.00 13.32  ?  322 VAL A CB    1 
ATOM   2299  C  CG1   . VAL A  1  290 ? 14.375 5.844   -10.090 1.00 13.48  ?  322 VAL A CG1   1 
ATOM   2300  C  CG2   . VAL A  1  290 ? 13.305 7.819   -11.215 1.00 13.48  ?  322 VAL A CG2   1 
ATOM   2301  N  N     . LYS A  1  291 ? 12.791 8.729   -8.116  1.00 12.86  ?  323 LYS A N     1 
ATOM   2302  C  CA    . LYS A  1  291 ? 11.699 8.557   -7.170  1.00 13.03  ?  323 LYS A CA    1 
ATOM   2303  C  C     . LYS A  1  291 ? 10.369 9.086   -7.683  1.00 13.74  ?  323 LYS A C     1 
ATOM   2304  O  O     . LYS A  1  291 ? 10.305 9.786   -8.725  1.00 13.79  ?  323 LYS A O     1 
ATOM   2305  C  CB    . LYS A  1  291 ? 11.999 9.256   -5.878  1.00 12.59  ?  323 LYS A CB    1 
ATOM   2306  C  CG    . LYS A  1  291 ? 12.114 10.746  -6.040  1.00 12.24  ?  323 LYS A CG    1 
ATOM   2307  C  CD    . LYS A  1  291 ? 11.471 11.460  -4.879  1.00 11.98  ?  323 LYS A CD    1 
ATOM   2308  C  CE    . LYS A  1  291 ? 11.531 12.952  -5.079  1.00 11.84  ?  323 LYS A CE    1 
ATOM   2309  N  NZ    . LYS A  1  291 ? 10.289 13.558  -4.549  1.00 12.07  1  323 LYS A NZ    1 
ATOM   2310  N  N     . SER A  1  292 ? 9.312  8.708   -6.957  1.00 14.07  ?  324 SER A N     1 
ATOM   2311  C  CA    A SER A  1  292 ? 7.970  9.182   -7.255  0.50 14.59  ?  324 SER A CA    1 
ATOM   2312  C  CA    B SER A  1  292 ? 7.968  9.180   -7.252  0.50 14.43  ?  324 SER A CA    1 
ATOM   2313  C  C     . SER A  1  292 ? 7.860  10.660  -6.898  1.00 15.06  ?  324 SER A C     1 
ATOM   2314  O  O     . SER A  1  292 ? 8.671  11.205  -6.120  1.00 15.13  ?  324 SER A O     1 
ATOM   2315  C  CB    A SER A  1  292 ? 6.915  8.417   -6.455  0.50 14.74  ?  324 SER A CB    1 
ATOM   2316  C  CB    B SER A  1  292 ? 6.911  8.368   -6.483  0.50 14.40  ?  324 SER A CB    1 
ATOM   2317  O  OG    A SER A  1  292 ? 6.879  7.046   -6.789  0.50 15.02  ?  324 SER A OG    1 
ATOM   2318  O  OG    B SER A  1  292 ? 5.964  9.200   -5.816  0.50 14.24  ?  324 SER A OG    1 
ATOM   2319  N  N     . VAL A  1  293 ? 6.849  11.303  -7.452  1.00 15.55  ?  325 VAL A N     1 
ATOM   2320  C  CA    . VAL A  1  293 ? 6.577  12.669  -7.131  1.00 15.87  ?  325 VAL A CA    1 
ATOM   2321  C  C     . VAL A  1  293 ? 6.096  12.788  -5.687  1.00 16.47  ?  325 VAL A C     1 
ATOM   2322  O  O     . VAL A  1  293 ? 6.473  13.713  -4.988  1.00 17.30  ?  325 VAL A O     1 
ATOM   2323  C  CB    . VAL A  1  293 ? 5.546  13.207  -8.102  1.00 16.15  ?  325 VAL A CB    1 
ATOM   2324  C  CG1   . VAL A  1  293 ? 4.959  14.519  -7.590  1.00 16.93  ?  325 VAL A CG1   1 
ATOM   2325  C  CG2   . VAL A  1  293 ? 6.206  13.372  -9.464  1.00 16.23  ?  325 VAL A CG2   1 
ATOM   2326  N  N     . LEU A  1  294 ? 5.302  11.835  -5.220  1.00 16.76  ?  326 LEU A N     1 
ATOM   2327  C  CA    . LEU A  1  294 ? 4.722  11.935  -3.891  1.00 17.32  ?  326 LEU A CA    1 
ATOM   2328  C  C     . LEU A  1  294 ? 5.712  11.617  -2.770  1.00 18.59  ?  326 LEU A C     1 
ATOM   2329  O  O     . LEU A  1  294 ? 5.454  11.912  -1.604  1.00 18.46  ?  326 LEU A O     1 
ATOM   2330  C  CB    . LEU A  1  294 ? 3.502  11.022  -3.803  1.00 17.26  ?  326 LEU A CB    1 
ATOM   2331  C  CG    . LEU A  1  294 ? 2.389  11.380  -4.811  1.00 17.54  ?  326 LEU A CG    1 
ATOM   2332  C  CD1   . LEU A  1  294 ? 1.086  10.642  -4.590  1.00 17.43  ?  326 LEU A CD1   1 
ATOM   2333  C  CD2   . LEU A  1  294 ? 2.095  12.870  -4.779  1.00 18.09  ?  326 LEU A CD2   1 
ATOM   2334  N  N     . GLU A  1  295 ? 6.852  11.036  -3.123  1.00 20.17  ?  327 GLU A N     1 
ATOM   2335  C  CA    . GLU A  1  295 ? 7.840  10.634  -2.134  1.00 21.22  ?  327 GLU A CA    1 
ATOM   2336  C  C     . GLU A  1  295 ? 8.724  11.813  -1.701  1.00 21.42  ?  327 GLU A C     1 
ATOM   2337  O  O     . GLU A  1  295 ? 9.308  12.499  -2.517  1.00 21.37  ?  327 GLU A O     1 
ATOM   2338  C  CB    . GLU A  1  295 ? 8.677  9.490   -2.703  1.00 22.15  ?  327 GLU A CB    1 
ATOM   2339  C  CG    . GLU A  1  295 ? 7.914  8.184   -2.832  1.00 23.53  ?  327 GLU A CG    1 
ATOM   2340  C  CD    . GLU A  1  295 ? 8.640  7.128   -3.665  1.00 26.38  ?  327 GLU A CD    1 
ATOM   2341  O  OE1   . GLU A  1  295 ? 8.025  6.083   -3.999  1.00 29.16  ?  327 GLU A OE1   1 
ATOM   2342  O  OE2   . GLU A  1  295 ? 9.827  7.326   -4.003  1.00 28.64  -1 327 GLU A OE2   1 
ATOM   2343  N  N     . LYS A  1  296 ? 8.805  12.056  -0.404  1.00 22.58  ?  328 LYS A N     1 
ATOM   2344  C  CA    . LYS A  1  296 ? 9.669  13.105  0.131   1.00 24.01  ?  328 LYS A CA    1 
ATOM   2345  C  C     . LYS A  1  296 ? 11.123 12.825  -0.156  1.00 22.18  ?  328 LYS A C     1 
ATOM   2346  O  O     . LYS A  1  296 ? 11.865 13.694  -0.581  1.00 22.25  ?  328 LYS A O     1 
ATOM   2347  C  CB    . LYS A  1  296 ? 9.494  13.178  1.646   1.00 26.93  ?  328 LYS A CB    1 
ATOM   2348  C  CG    . LYS A  1  296 ? 10.330 14.238  2.342   1.00 30.48  ?  328 LYS A CG    1 
ATOM   2349  C  CD    . LYS A  1  296 ? 9.927  15.658  1.931   1.00 34.56  ?  328 LYS A CD    1 
ATOM   2350  C  CE    . LYS A  1  296 ? 10.690 16.746  2.693   1.00 37.72  ?  328 LYS A CE    1 
ATOM   2351  N  NZ    . LYS A  1  296 ? 12.176 16.514  2.692   1.00 40.57  1  328 LYS A NZ    1 
ATOM   2352  N  N     . GLN A  1  297 ? 11.498 11.582  0.082   1.00 20.82  ?  329 GLN A N     1 
ATOM   2353  C  CA    . GLN A  1  297 ? 12.861 11.139  0.101   1.00 19.68  ?  329 GLN A CA    1 
ATOM   2354  C  C     . GLN A  1  297 ? 13.239 10.350  -1.142  1.00 17.96  ?  329 GLN A C     1 
ATOM   2355  O  O     . GLN A  1  297 ? 12.397 9.788   -1.823  1.00 17.28  ?  329 GLN A O     1 
ATOM   2356  C  CB    . GLN A  1  297 ? 13.003 10.208  1.292   1.00 21.28  ?  329 GLN A CB    1 
ATOM   2357  C  CG    . GLN A  1  297 ? 12.850 10.921  2.609   1.00 22.98  ?  329 GLN A CG    1 
ATOM   2358  C  CD    . GLN A  1  297 ? 13.894 12.002  2.744   1.00 25.44  ?  329 GLN A CD    1 
ATOM   2359  O  OE1   . GLN A  1  297 ? 13.596 13.181  2.968   1.00 27.77  ?  329 GLN A OE1   1 
ATOM   2360  N  NE2   . GLN A  1  297 ? 15.141 11.608  2.588   1.00 27.34  ?  329 GLN A NE2   1 
ATOM   2361  N  N     . THR A  1  298 ? 14.533 10.306  -1.415  1.00 16.53  ?  330 THR A N     1 
ATOM   2362  C  CA    . THR A  1  298 ? 15.124 9.301   -2.295  1.00 15.24  ?  330 THR A CA    1 
ATOM   2363  C  C     . THR A  1  298 ? 16.586 9.081   -1.865  1.00 14.41  ?  330 THR A C     1 
ATOM   2364  O  O     . THR A  1  298 ? 17.049 9.650   -0.867  1.00 13.79  ?  330 THR A O     1 
ATOM   2365  C  CB    . THR A  1  298 ? 14.983 9.689   -3.799  1.00 14.79  ?  330 THR A CB    1 
ATOM   2366  O  OG1   . THR A  1  298 ? 15.330 8.577   -4.647  1.00 14.34  ?  330 THR A OG1   1 
ATOM   2367  C  CG2   . THR A  1  298 ? 15.841 10.873  -4.138  1.00 14.79  ?  330 THR A CG2   1 
ATOM   2368  N  N     . ASN A  1  299 ? 17.300 8.240   -2.609  1.00 13.94  ?  331 ASN A N     1 
ATOM   2369  C  CA    . ASN A  1  299 ? 18.744 8.088   -2.419  1.00 13.68  ?  331 ASN A CA    1 
ATOM   2370  C  C     . ASN A  1  299 ? 19.535 9.106   -3.243  1.00 13.93  ?  331 ASN A C     1 
ATOM   2371  O  O     . ASN A  1  299 ? 19.009 9.718   -4.159  1.00 14.82  ?  331 ASN A O     1 
ATOM   2372  C  CB    . ASN A  1  299 ? 19.179 6.692   -2.778  1.00 13.28  ?  331 ASN A CB    1 
ATOM   2373  C  CG    . ASN A  1  299 ? 18.852 6.333   -4.204  1.00 13.36  ?  331 ASN A CG    1 
ATOM   2374  O  OD1   . ASN A  1  299 ? 17.686 6.120   -4.586  1.00 13.60  ?  331 ASN A OD1   1 
ATOM   2375  N  ND2   . ASN A  1  299 ? 19.886 6.238   -5.009  1.00 13.72  ?  331 ASN A ND2   1 
ATOM   2376  N  N     . ASN A  1  300 ? 20.772 9.375   -2.844  1.00 13.69  ?  332 ASN A N     1 
ATOM   2377  C  CA    . ASN A  1  300 ? 21.755 9.953   -3.748  1.00 12.97  ?  332 ASN A CA    1 
ATOM   2378  C  C     . ASN A  1  300 ? 22.371 8.736   -4.402  1.00 12.87  ?  332 ASN A C     1 
ATOM   2379  O  O     . ASN A  1  300 ? 22.330 7.638   -3.832  1.00 12.31  ?  332 ASN A O     1 
ATOM   2380  C  CB    . ASN A  1  300 ? 22.876 10.708  -3.020  1.00 12.58  ?  332 ASN A CB    1 
ATOM   2381  C  CG    . ASN A  1  300 ? 22.500 12.114  -2.595  1.00 12.13  ?  332 ASN A CG    1 
ATOM   2382  O  OD1   . ASN A  1  300 ? 22.667 12.472  -1.420  1.00 11.79  ?  332 ASN A OD1   1 
ATOM   2383  N  ND2   . ASN A  1  300 ? 22.052 12.935  -3.541  1.00 11.93  ?  332 ASN A ND2   1 
ATOM   2384  N  N     . PRO A  1  301 ? 22.973 8.923   -5.579  1.00 13.02  ?  333 PRO A N     1 
ATOM   2385  C  CA    . PRO A  1  301 ? 23.626 7.809   -6.237  1.00 13.17  ?  333 PRO A CA    1 
ATOM   2386  C  C     . PRO A  1  301 ? 24.722 7.278   -5.348  1.00 13.49  ?  333 PRO A C     1 
ATOM   2387  O  O     . PRO A  1  301 ? 25.311 8.035   -4.590  1.00 13.21  ?  333 PRO A O     1 
ATOM   2388  C  CB    . PRO A  1  301 ? 24.206 8.443   -7.495  1.00 13.12  ?  333 PRO A CB    1 
ATOM   2389  C  CG    . PRO A  1  301 ? 23.313 9.596   -7.767  1.00 13.16  ?  333 PRO A CG    1 
ATOM   2390  C  CD    . PRO A  1  301 ? 23.014 10.139  -6.403  1.00 13.07  ?  333 PRO A CD    1 
ATOM   2391  N  N     . GLY A  1  302 ? 24.975 5.983   -5.437  1.00 14.14  ?  334 GLY A N     1 
ATOM   2392  C  CA    . GLY A  1  302 ? 25.931 5.352   -4.571  1.00 14.85  ?  334 GLY A CA    1 
ATOM   2393  C  C     . GLY A  1  302 ? 26.591 4.141   -5.192  1.00 15.67  ?  334 GLY A C     1 
ATOM   2394  O  O     . GLY A  1  302 ? 26.039 3.475   -6.076  1.00 15.36  ?  334 GLY A O     1 
ATOM   2395  N  N     . ILE A  1  303 ? 27.763 3.859   -4.641  1.00 16.46  ?  335 ILE A N     1 
ATOM   2396  C  CA    . ILE A  1  303 ? 28.756 2.964   -5.175  1.00 17.14  ?  335 ILE A CA    1 
ATOM   2397  C  C     . ILE A  1  303 ? 29.457 2.525   -3.917  1.00 16.97  ?  335 ILE A C     1 
ATOM   2398  O  O     . ILE A  1  303 ? 29.655 3.346   -3.017  1.00 16.87  ?  335 ILE A O     1 
ATOM   2399  C  CB    . ILE A  1  303 ? 29.676 3.793   -6.113  1.00 18.60  ?  335 ILE A CB    1 
ATOM   2400  C  CG1   . ILE A  1  303 ? 29.037 3.877   -7.486  1.00 20.22  ?  335 ILE A CG1   1 
ATOM   2401  C  CG2   . ILE A  1  303 ? 31.087 3.253   -6.273  1.00 18.64  ?  335 ILE A CG2   1 
ATOM   2402  C  CD1   . ILE A  1  303 ? 28.530 2.530   -8.009  1.00 20.75  ?  335 ILE A CD1   1 
ATOM   2403  N  N     . ARG A  1  304 ? 29.784 1.249   -3.800  1.00 16.76  ?  336 ARG A N     1 
ATOM   2404  C  CA    . ARG A  1  304 ? 30.427 0.801   -2.597  1.00 17.14  ?  336 ARG A CA    1 
ATOM   2405  C  C     . ARG A  1  304 ? 31.468 -0.249  -2.867  1.00 18.94  ?  336 ARG A C     1 
ATOM   2406  O  O     . ARG A  1  304 ? 31.394 -0.999  -3.853  1.00 20.34  ?  336 ARG A O     1 
ATOM   2407  C  CB    . ARG A  1  304 ? 29.400 0.297   -1.582  1.00 16.60  ?  336 ARG A CB    1 
ATOM   2408  C  CG    . ARG A  1  304 ? 28.656 -0.955  -1.996  1.00 16.50  ?  336 ARG A CG    1 
ATOM   2409  C  CD    . ARG A  1  304 ? 27.909 -1.635  -0.843  1.00 16.28  ?  336 ARG A CD    1 
ATOM   2410  N  NE    . ARG A  1  304 ? 27.053 -0.709  -0.103  1.00 16.17  ?  336 ARG A NE    1 
ATOM   2411  C  CZ    . ARG A  1  304 ? 26.087 -1.062  0.746   1.00 16.51  ?  336 ARG A CZ    1 
ATOM   2412  N  NH1   . ARG A  1  304 ? 25.785 -2.336  0.980   1.00 17.29  1  336 ARG A NH1   1 
ATOM   2413  N  NH2   . ARG A  1  304 ? 25.394 -0.122  1.367   1.00 16.39  ?  336 ARG A NH2   1 
ATOM   2414  N  N     . LEU A  1  305 ? 32.413 -0.308  -1.936  1.00 20.27  ?  337 LEU A N     1 
ATOM   2415  C  CA    . LEU A  1  305 ? 33.564 -1.164  -1.993  1.00 21.03  ?  337 LEU A CA    1 
ATOM   2416  C  C     . LEU A  1  305 ? 33.661 -1.950  -0.692  1.00 21.38  ?  337 LEU A C     1 
ATOM   2417  O  O     . LEU A  1  305 ? 33.677 -1.363  0.410   1.00 21.48  ?  337 LEU A O     1 
ATOM   2418  C  CB    . LEU A  1  305 ? 34.775 -0.271  -2.128  1.00 23.19  ?  337 LEU A CB    1 
ATOM   2419  C  CG    . LEU A  1  305 ? 36.145 -0.913  -1.953  1.00 25.41  ?  337 LEU A CG    1 
ATOM   2420  C  CD1   . LEU A  1  305 ? 36.314 -1.997  -3.014  1.00 26.92  ?  337 LEU A CD1   1 
ATOM   2421  C  CD2   . LEU A  1  305 ? 37.243 0.143   -2.043  1.00 25.59  ?  337 LEU A CD2   1 
ATOM   2422  N  N     . PHE A  1  306 ? 33.725 -3.274  -0.822  1.00 21.66  ?  338 PHE A N     1 
ATOM   2423  C  CA    . PHE A  1  306 ? 33.960 -4.184  0.312   1.00 21.83  ?  338 PHE A CA    1 
ATOM   2424  C  C     . PHE A  1  306 ? 35.423 -4.615  0.486   1.00 24.10  ?  338 PHE A C     1 
ATOM   2425  O  O     . PHE A  1  306 ? 36.232 -4.579  -0.462  1.00 25.31  ?  338 PHE A O     1 
ATOM   2426  C  CB    . PHE A  1  306 ? 33.130 -5.435  0.150   1.00 20.51  ?  338 PHE A CB    1 
ATOM   2427  C  CG    . PHE A  1  306 ? 31.713 -5.240  0.513   1.00 19.97  ?  338 PHE A CG    1 
ATOM   2428  C  CD1   . PHE A  1  306 ? 31.341 -5.189  1.835   1.00 19.75  ?  338 PHE A CD1   1 
ATOM   2429  C  CD2   . PHE A  1  306 ? 30.748 -5.101  -0.458  1.00 19.67  ?  338 PHE A CD2   1 
ATOM   2430  C  CE1   . PHE A  1  306 ? 30.017 -5.026  2.188   1.00 19.45  ?  338 PHE A CE1   1 
ATOM   2431  C  CE2   . PHE A  1  306 ? 29.429 -4.928  -0.119  1.00 19.23  ?  338 PHE A CE2   1 
ATOM   2432  C  CZ    . PHE A  1  306 ? 29.065 -4.891  1.208   1.00 19.62  ?  338 PHE A CZ    1 
ATOM   2433  N  N     . GLN A  1  307 ? 35.742 -5.039  1.712   1.00 24.80  ?  339 GLN A N     1 
ATOM   2434  C  CA    . GLN A  1  307 ? 37.070 -5.517  2.062   1.00 24.02  ?  339 GLN A CA    1 
ATOM   2435  C  C     . GLN A  1  307 ? 36.985 -6.892  2.677   1.00 25.78  ?  339 GLN A C     1 
ATOM   2436  O  O     . GLN A  1  307 ? 36.133 -7.157  3.521   1.00 27.15  ?  339 GLN A O     1 
ATOM   2437  C  CB    . GLN A  1  307 ? 37.712 -4.557  3.037   1.00 23.05  ?  339 GLN A CB    1 
ATOM   2438  C  CG    . GLN A  1  307 ? 38.067 -3.233  2.387   1.00 23.01  ?  339 GLN A CG    1 
ATOM   2439  C  CD    . GLN A  1  307 ? 38.817 -2.329  3.318   1.00 22.76  ?  339 GLN A CD    1 
ATOM   2440  O  OE1   . GLN A  1  307 ? 38.887 -2.591  4.501   1.00 23.95  ?  339 GLN A OE1   1 
ATOM   2441  N  NE2   . GLN A  1  307 ? 39.363 -1.251  2.798   1.00 22.65  ?  339 GLN A NE2   1 
ATOM   2442  N  N     . TYR A  1  308 ? 37.875 -7.778  2.273   1.00 27.97  ?  340 TYR A N     1 
ATOM   2443  C  CA    . TYR A  1  308 ? 37.883 -9.100  2.857   1.00 29.03  ?  340 TYR A CA    1 
ATOM   2444  C  C     . TYR A  1  308 ? 39.270 -9.607  3.213   1.00 29.30  ?  340 TYR A C     1 
ATOM   2445  O  O     . TYR A  1  308 ? 40.296 -9.028  2.845   1.00 27.59  ?  340 TYR A O     1 
ATOM   2446  C  CB    . TYR A  1  308 ? 37.182 -10.077 1.937   1.00 30.08  ?  340 TYR A CB    1 
ATOM   2447  C  CG    . TYR A  1  308 ? 37.784 -10.200 0.561   1.00 31.76  ?  340 TYR A CG    1 
ATOM   2448  C  CD1   . TYR A  1  308 ? 37.581 -9.221  -0.392  1.00 33.22  ?  340 TYR A CD1   1 
ATOM   2449  C  CD2   . TYR A  1  308 ? 38.522 -11.317 0.200   1.00 33.75  ?  340 TYR A CD2   1 
ATOM   2450  C  CE1   . TYR A  1  308 ? 38.103 -9.334  -1.670  1.00 34.11  ?  340 TYR A CE1   1 
ATOM   2451  C  CE2   . TYR A  1  308 ? 39.046 -11.448 -1.075  1.00 34.79  ?  340 TYR A CE2   1 
ATOM   2452  C  CZ    . TYR A  1  308 ? 38.834 -10.448 -2.014  1.00 35.03  ?  340 TYR A CZ    1 
ATOM   2453  O  OH    . TYR A  1  308 ? 39.342 -10.555 -3.298  1.00 34.51  ?  340 TYR A OH    1 
ATOM   2454  N  N     . ASP A  1  309 ? 39.255 -10.682 3.986   1.00 30.78  ?  341 ASP A N     1 
ATOM   2455  C  CA    . ASP A  1  309 ? 40.438 -11.401 4.366   1.00 33.26  ?  341 ASP A CA    1 
ATOM   2456  C  C     . ASP A  1  309 ? 40.559 -12.516 3.357   1.00 31.51  ?  341 ASP A C     1 
ATOM   2457  O  O     . ASP A  1  309 ? 39.664 -13.375 3.287   1.00 32.97  ?  341 ASP A O     1 
ATOM   2458  C  CB    . ASP A  1  309 ? 40.271 -11.981 5.771   1.00 37.81  ?  341 ASP A CB    1 
ATOM   2459  C  CG    . ASP A  1  309 ? 41.595 -12.359 6.425   1.00 42.31  ?  341 ASP A CG    1 
ATOM   2460  O  OD1   . ASP A  1  309 ? 42.664 -11.994 5.881   1.00 48.90  ?  341 ASP A OD1   1 
ATOM   2461  O  OD2   . ASP A  1  309 ? 41.564 -13.000 7.504   1.00 44.81  -1 341 ASP A OD2   1 
ATOM   2462  N  N     . PRO A  1  310 ? 41.645 -12.515 2.562   1.00 28.81  ?  342 PRO A N     1 
ATOM   2463  C  CA    . PRO A  1  310 ? 41.845 -13.500 1.500   1.00 29.21  ?  342 PRO A CA    1 
ATOM   2464  C  C     . PRO A  1  310 ? 41.924 -14.969 1.928   1.00 29.58  ?  342 PRO A C     1 
ATOM   2465  O  O     . PRO A  1  310 ? 41.807 -15.867 1.088   1.00 29.92  ?  342 PRO A O     1 
ATOM   2466  C  CB    . PRO A  1  310 ? 43.155 -13.050 0.868   1.00 28.60  ?  342 PRO A CB    1 
ATOM   2467  C  CG    . PRO A  1  310 ? 43.166 -11.581 1.071   1.00 28.27  ?  342 PRO A CG    1 
ATOM   2468  C  CD    . PRO A  1  310 ? 42.624 -11.425 2.453   1.00 28.81  ?  342 PRO A CD    1 
ATOM   2469  N  N     . ARG A  1  311 ? 42.093 -15.203 3.218   1.00 31.04  ?  343 ARG A N     1 
ATOM   2470  C  CA    . ARG A  1  311 ? 42.197 -16.542 3.753   1.00 31.78  ?  343 ARG A CA    1 
ATOM   2471  C  C     . ARG A  1  311 ? 40.831 -17.202 3.855   1.00 31.92  ?  343 ARG A C     1 
ATOM   2472  O  O     . ARG A  1  311 ? 40.628 -18.244 3.262   1.00 33.26  ?  343 ARG A O     1 
ATOM   2473  C  CB    . ARG A  1  311 ? 42.888 -16.486 5.109   1.00 33.43  ?  343 ARG A CB    1 
ATOM   2474  C  CG    . ARG A  1  311 ? 44.291 -15.899 5.011   1.00 36.70  ?  343 ARG A CG    1 
ATOM   2475  C  CD    . ARG A  1  311 ? 44.956 -15.722 6.367   1.00 39.67  ?  343 ARG A CD    1 
ATOM   2476  N  NE    . ARG A  1  311 ? 44.651 -14.430 6.974   1.00 41.53  ?  343 ARG A NE    1 
ATOM   2477  C  CZ    . ARG A  1  311 ? 44.836 -14.128 8.258   1.00 43.06  ?  343 ARG A CZ    1 
ATOM   2478  N  NH1   . ARG A  1  311 ? 45.334 -15.028 9.102   1.00 46.10  1  343 ARG A NH1   1 
ATOM   2479  N  NH2   . ARG A  1  311 ? 44.510 -12.918 8.701   1.00 42.30  ?  343 ARG A NH2   1 
ATOM   2480  N  N     . ASP A  1  312 ? 39.897 -16.587 4.582   1.00 32.38  ?  344 ASP A N     1 
ATOM   2481  C  CA    . ASP A  1  312 ? 38.554 -17.163 4.832   1.00 31.56  ?  344 ASP A CA    1 
ATOM   2482  C  C     . ASP A  1  312 ? 37.432 -16.354 4.179   1.00 30.06  ?  344 ASP A C     1 
ATOM   2483  O  O     . ASP A  1  312 ? 36.251 -16.694 4.329   1.00 27.54  ?  344 ASP A O     1 
ATOM   2484  C  CB    . ASP A  1  312 ? 38.271 -17.347 6.346   1.00 32.47  ?  344 ASP A CB    1 
ATOM   2485  C  CG    . ASP A  1  312 ? 38.827 -16.191 7.235   1.00 34.78  ?  344 ASP A CG    1 
ATOM   2486  O  OD1   . ASP A  1  312 ? 39.372 -15.185 6.707   1.00 36.06  ?  344 ASP A OD1   1 
ATOM   2487  O  OD2   . ASP A  1  312 ? 38.740 -16.301 8.484   1.00 36.03  -1 344 ASP A OD2   1 
ATOM   2488  N  N     . TYR A  1  313 ? 37.807 -15.298 3.451   1.00 29.77  ?  345 TYR A N     1 
ATOM   2489  C  CA    . TYR A  1  313 ? 36.829 -14.400 2.795   1.00 31.89  ?  345 TYR A CA    1 
ATOM   2490  C  C     . TYR A  1  313 ? 35.860 -13.782 3.796   1.00 31.42  ?  345 TYR A C     1 
ATOM   2491  O  O     . TYR A  1  313 ? 34.706 -13.503 3.489   1.00 29.16  ?  345 TYR A O     1 
ATOM   2492  C  CB    . TYR A  1  313 ? 36.108 -15.135 1.638   1.00 32.52  ?  345 TYR A CB    1 
ATOM   2493  C  CG    . TYR A  1  313 ? 37.145 -15.700 0.717   1.00 32.28  ?  345 TYR A CG    1 
ATOM   2494  C  CD1   . TYR A  1  313 ? 37.940 -14.847 -0.051  1.00 31.85  ?  345 TYR A CD1   1 
ATOM   2495  C  CD2   . TYR A  1  313 ? 37.414 -17.060 0.698   1.00 32.45  ?  345 TYR A CD2   1 
ATOM   2496  C  CE1   . TYR A  1  313 ? 38.945 -15.336 -0.846  1.00 32.68  ?  345 TYR A CE1   1 
ATOM   2497  C  CE2   . TYR A  1  313 ? 38.419 -17.569 -0.098  1.00 33.28  ?  345 TYR A CE2   1 
ATOM   2498  C  CZ    . TYR A  1  313 ? 39.183 -16.701 -0.859  1.00 34.65  ?  345 TYR A CZ    1 
ATOM   2499  O  OH    . TYR A  1  313 ? 40.187 -17.205 -1.650  1.00 39.81  ?  345 TYR A OH    1 
ATOM   2500  N  N     . LYS A  1  314 ? 36.381 -13.577 4.998   1.00 32.19  ?  346 LYS A N     1 
ATOM   2501  C  CA    . LYS A  1  314 ? 35.689 -12.922 6.086   1.00 33.24  ?  346 LYS A CA    1 
ATOM   2502  C  C     . LYS A  1  314 ? 35.622 -11.448 5.725   1.00 30.26  ?  346 LYS A C     1 
ATOM   2503  O  O     . LYS A  1  314 ? 36.547 -10.919 5.114   1.00 29.24  ?  346 LYS A O     1 
ATOM   2504  C  CB    . LYS A  1  314 ? 36.483 -13.168 7.378   1.00 37.47  ?  346 LYS A CB    1 
ATOM   2505  C  CG    . LYS A  1  314 ? 36.121 -12.343 8.603   1.00 42.87  ?  346 LYS A CG    1 
ATOM   2506  C  CD    . LYS A  1  314 ? 36.767 -12.951 9.860   1.00 46.62  ?  346 LYS A CD    1 
ATOM   2507  C  CE    . LYS A  1  314 ? 36.526 -12.105 11.111  1.00 49.01  ?  346 LYS A CE    1 
ATOM   2508  N  NZ    . LYS A  1  314 ? 37.458 -10.943 11.189  1.00 51.29  1  346 LYS A NZ    1 
ATOM   2509  N  N     . LEU A  1  315 ? 34.514 -10.801 6.067   1.00 28.03  ?  347 LEU A N     1 
ATOM   2510  C  CA    . LEU A  1  315 ? 34.266 -9.417  5.646   1.00 26.41  ?  347 LEU A CA    1 
ATOM   2511  C  C     . LEU A  1  315 ? 34.837 -8.392  6.611   1.00 25.49  ?  347 LEU A C     1 
ATOM   2512  O  O     . LEU A  1  315 ? 34.413 -8.284  7.741   1.00 26.87  ?  347 LEU A O     1 
ATOM   2513  C  CB    . LEU A  1  315 ? 32.764 -9.202  5.460   1.00 24.93  ?  347 LEU A CB    1 
ATOM   2514  C  CG    . LEU A  1  315 ? 32.291 -9.779  4.141   1.00 24.10  ?  347 LEU A CG    1 
ATOM   2515  C  CD1   . LEU A  1  315 ? 30.776 -9.773  4.068   1.00 24.08  ?  347 LEU A CD1   1 
ATOM   2516  C  CD2   . LEU A  1  315 ? 32.909 -8.999  2.986   1.00 23.70  ?  347 LEU A CD2   1 
ATOM   2517  N  N     . LEU A  1  316 ? 35.799 -7.620  6.174   1.00 25.00  ?  348 LEU A N     1 
ATOM   2518  C  CA    . LEU A  1  316 ? 36.474 -6.773  7.122   1.00 26.48  ?  348 LEU A CA    1 
ATOM   2519  C  C     . LEU A  1  316 ? 35.803 -5.457  7.255   1.00 25.87  ?  348 LEU A C     1 
ATOM   2520  O  O     . LEU A  1  316 ? 35.773 -4.910  8.344   1.00 28.07  ?  348 LEU A O     1 
ATOM   2521  C  CB    . LEU A  1  316 ? 37.935 -6.578  6.734   1.00 27.98  ?  348 LEU A CB    1 
ATOM   2522  C  CG    . LEU A  1  316 ? 38.649 -7.934  6.805   1.00 29.92  ?  348 LEU A CG    1 
ATOM   2523  C  CD1   . LEU A  1  316 ? 40.076 -7.824  6.298   1.00 30.69  ?  348 LEU A CD1   1 
ATOM   2524  C  CD2   . LEU A  1  316 ? 38.595 -8.535  8.214   1.00 30.43  ?  348 LEU A CD2   1 
ATOM   2525  N  N     . ASP A  1  317 ? 35.286 -4.929  6.154   1.00 24.48  ?  349 ASP A N     1 
ATOM   2526  C  CA    . ASP A  1  317 ? 34.702 -3.596  6.162   1.00 22.73  ?  349 ASP A CA    1 
ATOM   2527  C  C     . ASP A  1  317 ? 33.989 -3.243  4.848   1.00 21.86  ?  349 ASP A C     1 
ATOM   2528  O  O     . ASP A  1  317 ? 34.046 -3.996  3.864   1.00 22.48  ?  349 ASP A O     1 
ATOM   2529  C  CB    . ASP A  1  317 ? 35.798 -2.571  6.440   1.00 21.92  ?  349 ASP A CB    1 
ATOM   2530  C  CG    . ASP A  1  317 ? 35.302 -1.411  7.253   1.00 21.83  ?  349 ASP A CG    1 
ATOM   2531  O  OD1   . ASP A  1  317 ? 34.201 -0.902  6.987   1.00 21.57  ?  349 ASP A OD1   1 
ATOM   2532  O  OD2   . ASP A  1  317 ? 36.017 -0.983  8.165   1.00 22.60  -1 349 ASP A OD2   1 
ATOM   2533  N  N     . MET A  1  318 ? 33.320 -2.096  4.846   1.00 20.38  ?  350 MET A N     1 
ATOM   2534  C  CA    . MET A  1  318 ? 32.700 -1.565  3.653   1.00 20.20  ?  350 MET A CA    1 
ATOM   2535  C  C     . MET A  1  318 ? 32.782 -0.052  3.612   1.00 19.71  ?  350 MET A C     1 
ATOM   2536  O  O     . MET A  1  318 ? 32.572 0.639   4.614   1.00 18.57  ?  350 MET A O     1 
ATOM   2537  C  CB    . MET A  1  318 ? 31.250 -1.989  3.610   1.00 21.72  ?  350 MET A CB    1 
ATOM   2538  C  CG    . MET A  1  318 ? 30.533 -1.549  2.347   1.00 23.12  ?  350 MET A CG    1 
ATOM   2539  S  SD    . MET A  1  318 ? 29.415 -0.196  2.684   1.00 24.48  ?  350 MET A SD    1 
ATOM   2540  C  CE    . MET A  1  318 ? 28.040 -1.173  3.272   1.00 24.24  ?  350 MET A CE    1 
ATOM   2541  N  N     . LEU A  1  319 ? 33.109 0.469   2.440   1.00 19.71  ?  351 LEU A N     1 
ATOM   2542  C  CA    . LEU A  1  319 ? 33.227 1.913   2.269   1.00 19.55  ?  351 LEU A CA    1 
ATOM   2543  C  C     . LEU A  1  319 ? 32.129 2.265   1.306   1.00 19.48  ?  351 LEU A C     1 
ATOM   2544  O  O     . LEU A  1  319 ? 31.945 1.572   0.306   1.00 20.20  ?  351 LEU A O     1 
ATOM   2545  C  CB    . LEU A  1  319 ? 34.580 2.302   1.684   1.00 19.76  ?  351 LEU A CB    1 
ATOM   2546  C  CG    . LEU A  1  319 ? 35.836 1.885   2.464   1.00 20.31  ?  351 LEU A CG    1 
ATOM   2547  C  CD1   . LEU A  1  319 ? 36.262 0.431   2.187   1.00 20.02  ?  351 LEU A CD1   1 
ATOM   2548  C  CD2   . LEU A  1  319 ? 36.955 2.859   2.112   1.00 20.40  ?  351 LEU A CD2   1 
ATOM   2549  N  N     . GLN A  1  320 ? 31.381 3.316   1.613   1.00 18.64  ?  352 GLN A N     1 
ATOM   2550  C  CA    . GLN A  1  320 ? 30.242 3.673   0.814   1.00 17.95  ?  352 GLN A CA    1 
ATOM   2551  C  C     . GLN A  1  320 ? 30.543 4.983   0.228   1.00 16.57  ?  352 GLN A C     1 
ATOM   2552  O  O     . GLN A  1  320 ? 30.737 5.938   0.952   1.00 15.99  ?  352 GLN A O     1 
ATOM   2553  C  CB    . GLN A  1  320 ? 28.988 3.801   1.664   1.00 19.23  ?  352 GLN A CB    1 
ATOM   2554  C  CG    . GLN A  1  320 ? 27.755 4.185   0.852   1.00 20.35  ?  352 GLN A CG    1 
ATOM   2555  C  CD    . GLN A  1  320 ? 27.250 3.052   -0.024  1.00 21.38  ?  352 GLN A CD    1 
ATOM   2556  O  OE1   . GLN A  1  320 ? 27.039 1.939   0.467   1.00 22.75  ?  352 GLN A OE1   1 
ATOM   2557  N  NE2   . GLN A  1  320 ? 27.041 3.321   -1.319  1.00 21.81  ?  352 GLN A NE2   1 
ATOM   2558  N  N     . TYR A  1  321 ? 30.561 5.025   -1.094  1.00 16.37  ?  353 TYR A N     1 
ATOM   2559  C  CA    . TYR A  1  321 ? 30.786 6.257   -1.832  1.00 15.89  ?  353 TYR A CA    1 
ATOM   2560  C  C     . TYR A  1  321 ? 29.468 6.735   -2.376  1.00 15.77  ?  353 TYR A C     1 
ATOM   2561  O  O     . TYR A  1  321 ? 28.533 5.940   -2.533  1.00 15.21  ?  353 TYR A O     1 
ATOM   2562  C  CB    . TYR A  1  321 ? 31.753 6.010   -2.977  1.00 15.41  ?  353 TYR A CB    1 
ATOM   2563  C  CG    . TYR A  1  321 ? 33.116 5.570   -2.535  1.00 15.43  ?  353 TYR A CG    1 
ATOM   2564  C  CD1   . TYR A  1  321 ? 34.067 6.492   -2.140  1.00 15.46  ?  353 TYR A CD1   1 
ATOM   2565  C  CD2   . TYR A  1  321 ? 33.453 4.220   -2.515  1.00 15.77  ?  353 TYR A CD2   1 
ATOM   2566  C  CE1   . TYR A  1  321 ? 35.333 6.083   -1.745  1.00 15.87  ?  353 TYR A CE1   1 
ATOM   2567  C  CE2   . TYR A  1  321 ? 34.715 3.794   -2.130  1.00 16.26  ?  353 TYR A CE2   1 
ATOM   2568  C  CZ    . TYR A  1  321 ? 35.659 4.728   -1.739  1.00 16.38  ?  353 TYR A CZ    1 
ATOM   2569  O  OH    . TYR A  1  321 ? 36.915 4.295   -1.333  1.00 16.82  ?  353 TYR A OH    1 
ATOM   2570  N  N     . TYR A  1  322 ? 29.403 8.032   -2.677  1.00 16.28  ?  354 TYR A N     1 
ATOM   2571  C  CA    . TYR A  1  322 ? 28.169 8.654   -3.179  1.00 16.46  ?  354 TYR A CA    1 
ATOM   2572  C  C     . TYR A  1  322 ? 28.364 9.936   -3.950  1.00 16.48  ?  354 TYR A C     1 
ATOM   2573  O  O     . TYR A  1  322 ? 29.452 10.483  -3.959  1.00 16.16  ?  354 TYR A O     1 
ATOM   2574  C  CB    . TYR A  1  322 ? 27.238 8.944   -2.015  1.00 16.67  ?  354 TYR A CB    1 
ATOM   2575  C  CG    . TYR A  1  322 ? 27.479 10.231  -1.255  1.00 16.90  ?  354 TYR A CG    1 
ATOM   2576  C  CD1   . TYR A  1  322 ? 28.537 10.362  -0.373  1.00 17.58  ?  354 TYR A CD1   1 
ATOM   2577  C  CD2   . TYR A  1  322 ? 26.599 11.291  -1.369  1.00 17.12  ?  354 TYR A CD2   1 
ATOM   2578  C  CE1   . TYR A  1  322 ? 28.709 11.532  0.349   1.00 17.97  ?  354 TYR A CE1   1 
ATOM   2579  C  CE2   . TYR A  1  322 ? 26.767 12.458  -0.655  1.00 17.07  ?  354 TYR A CE2   1 
ATOM   2580  C  CZ    . TYR A  1  322 ? 27.818 12.576  0.193   1.00 17.47  ?  354 TYR A CZ    1 
ATOM   2581  O  OH    . TYR A  1  322 ? 27.984 13.741  0.878   1.00 18.05  ?  354 TYR A OH    1 
ATOM   2582  N  N     . LEU A  1  323 ? 27.284 10.413  -4.570  1.00 17.19  ?  355 LEU A N     1 
ATOM   2583  C  CA    . LEU A  1  323 ? 27.283 11.671  -5.320  1.00 18.03  ?  355 LEU A CA    1 
ATOM   2584  C  C     . LEU A  1  323 ? 26.265 12.619  -4.704  1.00 18.68  ?  355 LEU A C     1 
ATOM   2585  O  O     . LEU A  1  323 ? 25.108 12.238  -4.613  1.00 18.29  ?  355 LEU A O     1 
ATOM   2586  C  CB    . LEU A  1  323 ? 26.927 11.402  -6.784  1.00 18.20  ?  355 LEU A CB    1 
ATOM   2587  C  CG    . LEU A  1  323 ? 27.041 12.596  -7.747  1.00 18.74  ?  355 LEU A CG    1 
ATOM   2588  C  CD1   . LEU A  1  323 ? 28.490 12.980  -7.929  1.00 19.14  ?  355 LEU A CD1   1 
ATOM   2589  C  CD2   . LEU A  1  323 ? 26.491 12.272  -9.124  1.00 18.88  ?  355 LEU A CD2   1 
ATOM   2590  N  N     . ASN A  1  324 ? 26.647 13.827  -4.293  1.00 20.19  ?  356 ASN A N     1 
ATOM   2591  C  CA    . ASN A  1  324 ? 25.711 14.811  -3.784  1.00 20.70  ?  356 ASN A CA    1 
ATOM   2592  C  C     . ASN A  1  324 ? 25.242 15.401  -5.061  1.00 20.90  ?  356 ASN A C     1 
ATOM   2593  O  O     . ASN A  1  324 ? 25.836 16.295  -5.581  1.00 20.82  ?  356 ASN A O     1 
ATOM   2594  C  CB    . ASN A  1  324 ? 26.365 15.862  -2.910  1.00 21.49  ?  356 ASN A CB    1 
ATOM   2595  C  CG    . ASN A  1  324 ? 25.403 16.900  -2.468  1.00 23.31  ?  356 ASN A CG    1 
ATOM   2596  O  OD1   . ASN A  1  324 ? 24.461 17.116  -3.133  1.00 24.91  ?  356 ASN A OD1   1 
ATOM   2597  N  ND2   . ASN A  1  324 ? 25.616 17.513  -1.341  1.00 25.76  ?  356 ASN A ND2   1 
ATOM   2598  N  N     . LEU A  1  325 ? 24.152 14.869  -5.562  1.00 20.97  ?  357 LEU A N     1 
ATOM   2599  C  CA    . LEU A  1  325 ? 23.570 15.174  -6.872  1.00 20.42  ?  357 LEU A CA    1 
ATOM   2600  C  C     . LEU A  1  325 ? 23.281 16.635  -7.030  1.00 19.60  ?  357 LEU A C     1 
ATOM   2601  O  O     . LEU A  1  325 ? 23.661 17.236  -7.999  1.00 18.61  ?  357 LEU A O     1 
ATOM   2602  C  CB    . LEU A  1  325 ? 22.261 14.398  -7.050  1.00 21.16  ?  357 LEU A CB    1 
ATOM   2603  C  CG    . LEU A  1  325 ? 21.526 14.507  -8.393  1.00 21.34  ?  357 LEU A CG    1 
ATOM   2604  C  CD1   . LEU A  1  325 ? 22.448 14.115  -9.530  1.00 21.71  ?  357 LEU A CD1   1 
ATOM   2605  C  CD2   . LEU A  1  325 ? 20.284 13.629  -8.400  1.00 21.03  ?  357 LEU A CD2   1 
ATOM   2606  N  N     . THR A  1  326 ? 22.600 17.210  -6.062  1.00 20.14  ?  358 THR A N     1 
ATOM   2607  C  CA    . THR A  1  326 ? 22.359 18.611  -6.127  1.00 21.27  ?  358 THR A CA    1 
ATOM   2608  C  C     . THR A  1  326 ? 23.611 19.390  -6.339  1.00 23.30  ?  358 THR A C     1 
ATOM   2609  O  O     . THR A  1  326 ? 23.620 20.286  -7.155  1.00 23.23  ?  358 THR A O     1 
ATOM   2610  C  CB    . THR A  1  326 ? 21.735 19.112  -4.862  1.00 20.96  ?  358 THR A CB    1 
ATOM   2611  O  OG1   . THR A  1  326 ? 20.367 18.757  -4.920  1.00 20.76  ?  358 THR A OG1   1 
ATOM   2612  C  CG2   . THR A  1  326 ? 21.848 20.624  -4.780  1.00 21.10  ?  358 THR A CG2   1 
ATOM   2613  N  N     . GLU A  1  327 ? 24.642 19.086  -5.566  1.00 27.29  ?  359 GLU A N     1 
ATOM   2614  C  CA    . GLU A  1  327 ? 25.901 19.812  -5.655  1.00 32.33  ?  359 GLU A CA    1 
ATOM   2615  C  C     . GLU A  1  327 ? 26.470 19.527  -7.019  1.00 30.61  ?  359 GLU A C     1 
ATOM   2616  O  O     . GLU A  1  327 ? 26.795 20.441  -7.770  1.00 30.84  ?  359 GLU A O     1 
ATOM   2617  C  CB    . GLU A  1  327 ? 26.886 19.367  -4.559  1.00 38.73  ?  359 GLU A CB    1 
ATOM   2618  C  CG    . GLU A  1  327 ? 28.250 20.053  -4.591  1.00 43.39  ?  359 GLU A CG    1 
ATOM   2619  C  CD    . GLU A  1  327 ? 29.279 19.388  -3.671  1.00 50.63  ?  359 GLU A CD    1 
ATOM   2620  O  OE1   . GLU A  1  327 ? 29.653 18.208  -3.895  1.00 52.76  ?  359 GLU A OE1   1 
ATOM   2621  O  OE2   . GLU A  1  327 ? 29.737 20.057  -2.717  1.00 55.71  -1 359 GLU A OE2   1 
ATOM   2622  N  N     . ALA A  1  328 ? 26.557 18.245  -7.340  1.00 28.73  ?  360 ALA A N     1 
ATOM   2623  C  CA    . ALA A  1  328 ? 27.094 17.809  -8.617  1.00 28.32  ?  360 ALA A CA    1 
ATOM   2624  C  C     . ALA A  1  328 ? 26.442 18.504  -9.781  1.00 27.69  ?  360 ALA A C     1 
ATOM   2625  O  O     . ALA A  1  328 ? 27.091 18.756  -10.762 1.00 27.65  ?  360 ALA A O     1 
ATOM   2626  C  CB    . ALA A  1  328 ? 26.936 16.308  -8.770  1.00 29.24  ?  360 ALA A CB    1 
ATOM   2627  N  N     . ASN A  1  329 ? 25.154 18.800  -9.688  1.00 28.44  ?  361 ASN A N     1 
ATOM   2628  C  CA    . ASN A  1  329 ? 24.517 19.600  -10.722 1.00 28.84  ?  361 ASN A CA    1 
ATOM   2629  C  C     . ASN A  1  329 ? 24.854 21.088  -10.595 1.00 30.84  ?  361 ASN A C     1 
ATOM   2630  O  O     . ASN A  1  329 ? 25.215 21.688  -11.576 1.00 33.57  ?  361 ASN A O     1 
ATOM   2631  C  CB    . ASN A  1  329 ? 23.016 19.326  -10.814 1.00 27.68  ?  361 ASN A CB    1 
ATOM   2632  C  CG    . ASN A  1  329 ? 22.706 17.979  -11.478 1.00 28.06  ?  361 ASN A CG    1 
ATOM   2633  O  OD1   . ASN A  1  329 ? 23.528 17.388  -12.206 1.00 26.27  ?  361 ASN A OD1   1 
ATOM   2634  N  ND2   . ASN A  1  329 ? 21.510 17.485  -11.228 1.00 28.42  ?  361 ASN A ND2   1 
ATOM   2635  N  N     . LEU A  1  330 ? 24.823 21.675  -9.404  1.00 34.35  ?  362 LEU A N     1 
ATOM   2636  C  CA    . LEU A  1  330 ? 25.264 23.084  -9.216  1.00 35.50  ?  362 LEU A CA    1 
ATOM   2637  C  C     . LEU A  1  330 ? 26.636 23.378  -9.789  1.00 37.13  ?  362 LEU A C     1 
ATOM   2638  O  O     . LEU A  1  330 ? 26.853 24.393  -10.437 1.00 39.16  ?  362 LEU A O     1 
ATOM   2639  C  CB    . LEU A  1  330 ? 25.302 23.460  -7.730  1.00 35.59  ?  362 LEU A CB    1 
ATOM   2640  C  CG    . LEU A  1  330 ? 23.941 23.847  -7.146  1.00 36.77  ?  362 LEU A CG    1 
ATOM   2641  C  CD1   . LEU A  1  330 ? 24.030 24.145  -5.653  1.00 36.98  ?  362 LEU A CD1   1 
ATOM   2642  C  CD2   . LEU A  1  330 ? 23.379 25.038  -7.906  1.00 36.93  ?  362 LEU A CD2   1 
ATOM   2643  N  N     . LYS A  1  331 ? 27.585 22.506  -9.515  1.00 39.36  ?  363 LYS A N     1 
ATOM   2644  C  CA    . LYS A  1  331 ? 28.941 22.728  -9.995  1.00 41.45  ?  363 LYS A CA    1 
ATOM   2645  C  C     . LYS A  1  331 ? 29.043 22.239  -11.429 1.00 38.33  ?  363 LYS A C     1 
ATOM   2646  O  O     . LYS A  1  331 ? 29.866 22.703  -12.215 1.00 37.00  ?  363 LYS A O     1 
ATOM   2647  C  CB    . LYS A  1  331 ? 29.956 22.022  -9.075  1.00 43.81  ?  363 LYS A CB    1 
ATOM   2648  C  CG    . LYS A  1  331 ? 30.024 22.677  -7.701  1.00 46.38  ?  363 LYS A CG    1 
ATOM   2649  C  CD    . LYS A  1  331 ? 30.542 21.749  -6.616  1.00 51.32  ?  363 LYS A CD    1 
ATOM   2650  C  CE    . LYS A  1  331 ? 32.060 21.738  -6.525  1.00 55.82  ?  363 LYS A CE    1 
ATOM   2651  N  NZ    . LYS A  1  331 ? 32.501 21.401  -5.139  1.00 58.76  1  363 LYS A NZ    1 
ATOM   2652  N  N     . GLY A  1  332 ? 28.178 21.305  -11.771 1.00 35.75  ?  364 GLY A N     1 
ATOM   2653  C  CA    . GLY A  1  332 ? 28.324 20.613  -13.013 1.00 35.75  ?  364 GLY A CA    1 
ATOM   2654  C  C     . GLY A  1  332 ? 29.665 19.925  -12.992 1.00 36.58  ?  364 GLY A C     1 
ATOM   2655  O  O     . GLY A  1  332 ? 30.435 20.080  -13.919 1.00 38.02  ?  364 GLY A O     1 
ATOM   2656  N  N     . GLU A  1  333 ? 29.946 19.188  -11.915 1.00 39.00  ?  365 GLU A N     1 
ATOM   2657  C  CA    . GLU A  1  333 ? 31.036 18.214  -11.884 1.00 39.73  ?  365 GLU A CA    1 
ATOM   2658  C  C     . GLU A  1  333 ? 30.669 16.946  -11.088 1.00 35.69  ?  365 GLU A C     1 
ATOM   2659  O  O     . GLU A  1  333 ? 29.899 17.013  -10.142 1.00 32.21  ?  365 GLU A O     1 
ATOM   2660  C  CB    . GLU A  1  333 ? 32.273 18.861  -11.270 1.00 45.94  ?  365 GLU A CB    1 
ATOM   2661  C  CG    . GLU A  1  333 ? 32.894 20.012  -12.068 1.00 51.32  ?  365 GLU A CG    1 
ATOM   2662  C  CD    . GLU A  1  333 ? 33.549 19.604  -13.401 1.00 55.51  ?  365 GLU A CD    1 
ATOM   2663  O  OE1   . GLU A  1  333 ? 33.703 18.384  -13.692 1.00 55.17  ?  365 GLU A OE1   1 
ATOM   2664  O  OE2   . GLU A  1  333 ? 33.929 20.537  -14.161 1.00 60.98  -1 365 GLU A OE2   1 
ATOM   2665  N  N     . SER A  1  334 ? 31.250 15.806  -11.469 1.00 34.91  ?  366 SER A N     1 
ATOM   2666  C  CA    . SER A  1  334 ? 31.091 14.524  -10.745 1.00 34.20  ?  366 SER A CA    1 
ATOM   2667  C  C     . SER A  1  334 ? 31.958 14.374  -9.520  1.00 33.25  ?  366 SER A C     1 
ATOM   2668  O  O     . SER A  1  334 ? 32.932 13.619  -9.543  1.00 35.59  ?  366 SER A O     1 
ATOM   2669  C  CB    . SER A  1  334 ? 31.482 13.355  -11.633 1.00 34.85  ?  366 SER A CB    1 
ATOM   2670  O  OG    . SER A  1  334 ? 30.588 13.259  -12.697 1.00 39.09  ?  366 SER A OG    1 
ATOM   2671  N  N     A ILE A  1  335 ? 31.628 15.072  -8.442  0.50 32.22  ?  367 ILE A N     1 
ATOM   2672  N  N     B ILE A  1  335 ? 31.581 15.060  -8.453  0.50 31.89  ?  367 ILE A N     1 
ATOM   2673  C  CA    A ILE A  1  335 ? 32.389 14.928  -7.208  0.50 32.43  ?  367 ILE A CA    1 
ATOM   2674  C  CA    B ILE A  1  335 ? 32.267 14.970  -7.181  0.50 31.78  ?  367 ILE A CA    1 
ATOM   2675  C  C     A ILE A  1  335 ? 31.907 13.715  -6.412  0.50 30.97  ?  367 ILE A C     1 
ATOM   2676  C  C     B ILE A  1  335 ? 31.864 13.703  -6.407  0.50 30.58  ?  367 ILE A C     1 
ATOM   2677  O  O     A ILE A  1  335 ? 31.130 13.838  -5.463  0.50 31.34  ?  367 ILE A O     1 
ATOM   2678  O  O     B ILE A  1  335 ? 31.091 13.781  -5.450  0.50 30.86  ?  367 ILE A O     1 
ATOM   2679  C  CB    A ILE A  1  335 ? 32.281 16.191  -6.347  0.50 33.96  ?  367 ILE A CB    1 
ATOM   2680  C  CB    B ILE A  1  335 ? 31.909 16.208  -6.341  0.50 32.74  ?  367 ILE A CB    1 
ATOM   2681  C  CG1   A ILE A  1  335 ? 32.293 17.422  -7.253  0.50 34.85  ?  367 ILE A CG1   1 
ATOM   2682  C  CG1   B ILE A  1  335 ? 30.385 16.379  -6.285  0.50 31.63  ?  367 ILE A CG1   1 
ATOM   2683  C  CG2   A ILE A  1  335 ? 33.419 16.239  -5.335  0.50 33.35  ?  367 ILE A CG2   1 
ATOM   2684  C  CG2   B ILE A  1  335 ? 32.537 17.459  -6.941  0.50 33.76  ?  367 ILE A CG2   1 
ATOM   2685  C  CD1   A ILE A  1  335 ? 33.478 17.444  -8.195  0.50 34.62  ?  367 ILE A CD1   1 
ATOM   2686  C  CD1   B ILE A  1  335 ? 29.915 17.783  -6.575  0.50 30.87  ?  367 ILE A CD1   1 
ATOM   2687  N  N     . TRP A  1  336 ? 32.366 12.540  -6.816  1.00 29.42  ?  368 TRP A N     1 
ATOM   2688  C  CA    . TRP A  1  336 ? 32.062 11.310  -6.099  1.00 29.39  ?  368 TRP A CA    1 
ATOM   2689  C  C     . TRP A  1  336 ? 32.871 11.315  -4.813  1.00 30.06  ?  368 TRP A C     1 
ATOM   2690  O  O     . TRP A  1  336 ? 34.081 11.159  -4.849  1.00 31.72  ?  368 TRP A O     1 
ATOM   2691  C  CB    . TRP A  1  336 ? 32.382 10.047  -6.921  1.00 29.16  ?  368 TRP A CB    1 
ATOM   2692  C  CG    . TRP A  1  336 ? 31.271 9.623   -7.833  1.00 29.03  ?  368 TRP A CG    1 
ATOM   2693  C  CD1   . TRP A  1  336 ? 31.119 9.945   -9.161  1.00 29.95  ?  368 TRP A CD1   1 
ATOM   2694  C  CD2   . TRP A  1  336 ? 30.148 8.812   -7.489  1.00 28.41  ?  368 TRP A CD2   1 
ATOM   2695  N  NE1   . TRP A  1  336 ? 29.968 9.375   -9.660  1.00 29.34  ?  368 TRP A NE1   1 
ATOM   2696  C  CE2   . TRP A  1  336 ? 29.346 8.688   -8.652  1.00 28.26  ?  368 TRP A CE2   1 
ATOM   2697  C  CE3   . TRP A  1  336 ? 29.730 8.190   -6.309  1.00 27.97  ?  368 TRP A CE3   1 
ATOM   2698  C  CZ2   . TRP A  1  336 ? 28.169 7.963   -8.669  1.00 26.77  ?  368 TRP A CZ2   1 
ATOM   2699  C  CZ3   . TRP A  1  336 ? 28.554 7.475   -6.327  1.00 27.78  ?  368 TRP A CZ3   1 
ATOM   2700  C  CH2   . TRP A  1  336 ? 27.787 7.366   -7.506  1.00 27.78  ?  368 TRP A CH2   1 
ATOM   2701  N  N     . LYS A  1  337 ? 32.194 11.520  -3.687  1.00 30.55  ?  369 LYS A N     1 
ATOM   2702  C  CA    . LYS A  1  337 ? 32.822 11.512  -2.375  1.00 29.86  ?  369 LYS A CA    1 
ATOM   2703  C  C     . LYS A  1  337 ? 32.640 10.153  -1.685  1.00 28.65  ?  369 LYS A C     1 
ATOM   2704  O  O     . LYS A  1  337 ? 31.973 9.249   -2.185  1.00 28.59  ?  369 LYS A O     1 
ATOM   2705  C  CB    . LYS A  1  337 ? 32.227 12.601  -1.471  1.00 31.81  ?  369 LYS A CB    1 
ATOM   2706  C  CG    . LYS A  1  337 ? 32.180 14.020  -2.020  1.00 34.11  ?  369 LYS A CG    1 
ATOM   2707  C  CD    . LYS A  1  337 ? 31.409 14.919  -1.047  1.00 38.43  ?  369 LYS A CD    1 
ATOM   2708  C  CE    . LYS A  1  337 ? 30.800 16.156  -1.714  1.00 43.38  ?  369 LYS A CE    1 
ATOM   2709  N  NZ    . LYS A  1  337 ? 29.475 16.554  -1.118  1.00 45.25  1  369 LYS A NZ    1 
ATOM   2710  N  N     . LEU A  1  338 ? 33.277 10.040  -0.527  1.00 27.21  ?  370 LEU A N     1 
ATOM   2711  C  CA    . LEU A  1  338 ? 33.110 8.933   0.386   1.00 24.96  ?  370 LEU A CA    1 
ATOM   2712  C  C     . LEU A  1  338 ? 32.068 9.354   1.390   1.00 22.21  ?  370 LEU A C     1 
ATOM   2713  O  O     . LEU A  1  338 ? 32.188 10.419  1.975   1.00 21.41  ?  370 LEU A O     1 
ATOM   2714  C  CB    . LEU A  1  338 ? 34.412 8.722   1.126   1.00 26.38  ?  370 LEU A CB    1 
ATOM   2715  C  CG    . LEU A  1  338 ? 34.403 7.716   2.269   1.00 28.28  ?  370 LEU A CG    1 
ATOM   2716  C  CD1   . LEU A  1  338 ? 34.183 6.295   1.773   1.00 28.46  ?  370 LEU A CD1   1 
ATOM   2717  C  CD2   . LEU A  1  338 ? 35.722 7.831   3.021   1.00 28.76  ?  370 LEU A CD2   1 
ATOM   2718  N  N     . GLU A  1  339 ? 31.064 8.516   1.604   1.00 19.67  ?  371 GLU A N     1 
ATOM   2719  C  CA    . GLU A  1  339 ? 30.035 8.791   2.584   1.00 17.73  ?  371 GLU A CA    1 
ATOM   2720  C  C     . GLU A  1  339 ? 30.491 8.366   3.952   1.00 16.34  ?  371 GLU A C     1 
ATOM   2721  O  O     . GLU A  1  339 ? 30.364 9.126   4.925   1.00 15.93  ?  371 GLU A O     1 
ATOM   2722  C  CB    . GLU A  1  339 ? 28.772 8.020   2.248   1.00 18.10  ?  371 GLU A CB    1 
ATOM   2723  C  CG    . GLU A  1  339 ? 27.524 8.567   2.923   1.00 18.80  ?  371 GLU A CG    1 
ATOM   2724  C  CD    . GLU A  1  339 ? 26.301 7.680   2.704   1.00 19.77  ?  371 GLU A CD    1 
ATOM   2725  O  OE1   . GLU A  1  339 ? 26.474 6.493   2.359   1.00 19.94  ?  371 GLU A OE1   1 
ATOM   2726  O  OE2   . GLU A  1  339 ? 25.159 8.162   2.886   1.00 20.51  -1 371 GLU A OE2   1 
ATOM   2727  N  N     . TYR A  1  340 ? 30.987 7.132   4.033   1.00 15.16  ?  372 TYR A N     1 
ATOM   2728  C  CA    . TYR A  1  340 ? 31.339 6.526   5.315   1.00 14.71  ?  372 TYR A CA    1 
ATOM   2729  C  C     . TYR A  1  340 ? 32.062 5.198   5.175   1.00 14.92  ?  372 TYR A C     1 
ATOM   2730  O  O     . TYR A  1  340 ? 31.914 4.495   4.188   1.00 14.23  ?  372 TYR A O     1 
ATOM   2731  C  CB    . TYR A  1  340 ? 30.109 6.323   6.224   1.00 14.05  ?  372 TYR A CB    1 
ATOM   2732  C  CG    . TYR A  1  340 ? 29.256 5.135   5.865   1.00 13.70  ?  372 TYR A CG    1 
ATOM   2733  C  CD1   . TYR A  1  340 ? 29.558 3.869   6.332   1.00 13.59  ?  372 TYR A CD1   1 
ATOM   2734  C  CD2   . TYR A  1  340 ? 28.123 5.284   5.081   1.00 13.65  ?  372 TYR A CD2   1 
ATOM   2735  C  CE1   . TYR A  1  340 ? 28.767 2.775   6.015   1.00 13.50  ?  372 TYR A CE1   1 
ATOM   2736  C  CE2   . TYR A  1  340 ? 27.320 4.204   4.763   1.00 13.59  ?  372 TYR A CE2   1 
ATOM   2737  C  CZ    . TYR A  1  340 ? 27.650 2.950   5.222   1.00 13.53  ?  372 TYR A CZ    1 
ATOM   2738  O  OH    . TYR A  1  340 ? 26.862 1.870   4.874   1.00 13.62  ?  372 TYR A OH    1 
ATOM   2739  N  N     . ILE A  1  341 ? 32.831 4.878   6.214   1.00 15.93  ?  373 ILE A N     1 
ATOM   2740  C  CA    . ILE A  1  341 ? 33.483 3.585   6.365   1.00 17.01  ?  373 ILE A CA    1 
ATOM   2741  C  C     . ILE A  1  341 ? 32.822 2.823   7.501   1.00 16.88  ?  373 ILE A C     1 
ATOM   2742  O  O     . ILE A  1  341 ? 32.789 3.315   8.630   1.00 17.69  ?  373 ILE A O     1 
ATOM   2743  C  CB    . ILE A  1  341 ? 34.968 3.747   6.708   1.00 17.68  ?  373 ILE A CB    1 
ATOM   2744  C  CG1   . ILE A  1  341 ? 35.654 4.557   5.611   1.00 18.09  ?  373 ILE A CG1   1 
ATOM   2745  C  CG2   . ILE A  1  341 ? 35.622 2.367   6.897   1.00 17.90  ?  373 ILE A CG2   1 
ATOM   2746  C  CD1   . ILE A  1  341 ? 37.035 5.023   6.003   1.00 18.70  ?  373 ILE A CD1   1 
ATOM   2747  N  N     . LEU A  1  342 ? 32.322 1.623   7.223   1.00 16.13  ?  374 LEU A N     1 
ATOM   2748  C  CA    . LEU A  1  342 ? 31.317 1.058   8.097   1.00 15.79  ?  374 LEU A CA    1 
ATOM   2749  C  C     . LEU A  1  342 ? 31.821 0.886   9.529   1.00 16.29  ?  374 LEU A C     1 
ATOM   2750  O  O     . LEU A  1  342 ? 31.174 1.366   10.473  1.00 16.99  ?  374 LEU A O     1 
ATOM   2751  C  CB    . LEU A  1  342 ? 30.760 -0.232  7.536   1.00 15.41  ?  374 LEU A CB    1 
ATOM   2752  C  CG    . LEU A  1  342 ? 29.438 -0.666  8.148   1.00 15.26  ?  374 LEU A CG    1 
ATOM   2753  C  CD1   . LEU A  1  342 ? 28.746 -1.621  7.203   1.00 15.10  ?  374 LEU A CD1   1 
ATOM   2754  C  CD2   . LEU A  1  342 ? 29.641 -1.336  9.503   1.00 15.65  ?  374 LEU A CD2   1 
ATOM   2755  N  N     . THR A  1  343 ? 32.976 0.262   9.712   1.00 16.35  ?  375 THR A N     1 
ATOM   2756  C  CA    . THR A  1  343 ? 33.443 0.004   11.072  1.00 16.64  ?  375 THR A CA    1 
ATOM   2757  C  C     . THR A  1  343 ? 33.833 1.291   11.775  1.00 18.57  ?  375 THR A C     1 
ATOM   2758  O  O     . THR A  1  343 ? 33.735 1.375   12.990  1.00 18.56  ?  375 THR A O     1 
ATOM   2759  C  CB    . THR A  1  343 ? 34.637 -0.937  11.127  1.00 15.83  ?  375 THR A CB    1 
ATOM   2760  O  OG1   . THR A  1  343 ? 35.749 -0.334  10.478  1.00 15.64  ?  375 THR A OG1   1 
ATOM   2761  C  CG2   . THR A  1  343 ? 34.321 -2.262  10.494  1.00 15.61  ?  375 THR A CG2   1 
ATOM   2762  N  N     . GLN A  1  344 ? 34.260 2.292   11.012  1.00 21.36  ?  376 GLN A N     1 
ATOM   2763  C  CA    . GLN A  1  344 ? 34.570 3.595   11.567  1.00 24.07  ?  376 GLN A CA    1 
ATOM   2764  C  C     . GLN A  1  344 ? 33.385 4.314   12.132  1.00 21.59  ?  376 GLN A C     1 
ATOM   2765  O  O     . GLN A  1  344 ? 33.464 4.779   13.254  1.00 22.11  ?  376 GLN A O     1 
ATOM   2766  C  CB    . GLN A  1  344 ? 35.159 4.507   10.517  1.00 30.53  ?  376 GLN A CB    1 
ATOM   2767  C  CG    . GLN A  1  344 ? 36.624 4.270   10.236  1.00 37.81  ?  376 GLN A CG    1 
ATOM   2768  C  CD    . GLN A  1  344 ? 37.502 4.869   11.315  1.00 48.32  ?  376 GLN A CD    1 
ATOM   2769  O  OE1   . GLN A  1  344 ? 37.010 5.580   12.210  1.00 56.84  ?  376 GLN A OE1   1 
ATOM   2770  N  NE2   . GLN A  1  344 ? 38.816 4.587   11.247  1.00 55.05  ?  376 GLN A NE2   1 
ATOM   2771  N  N     . THR A  1  345 ? 32.301 4.459   11.372  1.00 20.08  ?  377 THR A N     1 
ATOM   2772  C  CA    . THR A  1  345 ? 31.209 5.340   11.837  1.00 19.25  ?  377 THR A CA    1 
ATOM   2773  C  C     . THR A  1  345 ? 30.423 4.719   12.920  1.00 19.78  ?  377 THR A C     1 
ATOM   2774  O  O     . THR A  1  345 ? 29.827 5.430   13.713  1.00 19.79  ?  377 THR A O     1 
ATOM   2775  C  CB    . THR A  1  345 ? 30.172 5.719   10.784  1.00 18.15  ?  377 THR A CB    1 
ATOM   2776  O  OG1   . THR A  1  345 ? 30.011 4.640   9.865   1.00 17.11  ?  377 THR A OG1   1 
ATOM   2777  C  CG2   . THR A  1  345 ? 30.593 6.962   10.089  1.00 18.44  ?  377 THR A CG2   1 
ATOM   2778  N  N     . TYR A  1  346 ? 30.384 3.397   12.938  1.00 20.51  ?  378 TYR A N     1 
ATOM   2779  C  CA    . TYR A  1  346 ? 29.619 2.702   13.946  1.00 21.58  ?  378 TYR A CA    1 
ATOM   2780  C  C     . TYR A  1  346 ? 30.468 2.190   15.079  1.00 22.53  ?  378 TYR A C     1 
ATOM   2781  O  O     . TYR A  1  346 ? 29.957 1.695   16.097  1.00 22.02  ?  378 TYR A O     1 
ATOM   2782  C  CB    . TYR A  1  346 ? 28.891 1.562   13.296  1.00 21.89  ?  378 TYR A CB    1 
ATOM   2783  C  CG    . TYR A  1  346 ? 27.831 2.033   12.360  1.00 21.96  ?  378 TYR A CG    1 
ATOM   2784  C  CD1   . TYR A  1  346 ? 26.770 2.790   12.820  1.00 22.27  ?  378 TYR A CD1   1 
ATOM   2785  C  CD2   . TYR A  1  346 ? 27.876 1.703   11.010  1.00 22.25  ?  378 TYR A CD2   1 
ATOM   2786  C  CE1   . TYR A  1  346 ? 25.775 3.216   11.950  1.00 23.76  ?  378 TYR A CE1   1 
ATOM   2787  C  CE2   . TYR A  1  346 ? 26.887 2.116   10.132  1.00 22.57  ?  378 TYR A CE2   1 
ATOM   2788  C  CZ    . TYR A  1  346 ? 25.836 2.877   10.598  1.00 23.05  ?  378 TYR A CZ    1 
ATOM   2789  O  OH    . TYR A  1  346 ? 24.843 3.287   9.738   1.00 22.25  ?  378 TYR A OH    1 
ATOM   2790  N  N     . ASP A  1  347 ? 31.769 2.314   14.896  1.00 24.63  ?  379 ASP A N     1 
ATOM   2791  C  CA    . ASP A  1  347 ? 32.701 1.907   15.905  1.00 28.03  ?  379 ASP A CA    1 
ATOM   2792  C  C     . ASP A  1  347 ? 32.450 0.466   16.286  1.00 27.89  ?  379 ASP A C     1 
ATOM   2793  O  O     . ASP A  1  347 ? 32.084 0.182   17.413  1.00 28.84  ?  379 ASP A O     1 
ATOM   2794  C  CB    . ASP A  1  347 ? 32.583 2.816   17.115  1.00 30.41  ?  379 ASP A CB    1 
ATOM   2795  C  CG    . ASP A  1  347 ? 33.895 3.008   17.798  1.00 34.14  ?  379 ASP A CG    1 
ATOM   2796  O  OD1   . ASP A  1  347 ? 34.347 2.018   18.426  1.00 37.47  ?  379 ASP A OD1   1 
ATOM   2797  O  OD2   . ASP A  1  347 ? 34.474 4.130   17.678  1.00 36.90  -1 379 ASP A OD2   1 
ATOM   2798  N  N     . ILE A  1  348 ? 32.610 -0.421  15.309  1.00 27.27  ?  380 ILE A N     1 
ATOM   2799  C  CA    . ILE A  1  348 ? 32.525 -1.837  15.531  1.00 27.83  ?  380 ILE A CA    1 
ATOM   2800  C  C     . ILE A  1  348 ? 33.739 -2.489  14.885  1.00 29.11  ?  380 ILE A C     1 
ATOM   2801  O  O     . ILE A  1  348 ? 34.423 -1.872  14.101  1.00 27.21  ?  380 ILE A O     1 
ATOM   2802  C  CB    . ILE A  1  348 ? 31.207 -2.415  15.000  1.00 28.67  ?  380 ILE A CB    1 
ATOM   2803  C  CG1   . ILE A  1  348 ? 31.036 -2.112  13.519  1.00 30.75  ?  380 ILE A CG1   1 
ATOM   2804  C  CG2   . ILE A  1  348 ? 30.027 -1.818  15.750  1.00 28.82  ?  380 ILE A CG2   1 
ATOM   2805  C  CD1   . ILE A  1  348 ? 29.899 -2.886  12.878  1.00 31.56  ?  380 ILE A CD1   1 
ATOM   2806  N  N     . GLU A  1  349 ? 33.998 -3.736  15.251  1.00 33.25  ?  381 GLU A N     1 
ATOM   2807  C  CA    . GLU A  1  349 ? 35.211 -4.452  14.874  1.00 35.88  ?  381 GLU A CA    1 
ATOM   2808  C  C     . GLU A  1  349 ? 35.330 -4.770  13.393  1.00 33.47  ?  381 GLU A C     1 
ATOM   2809  O  O     . GLU A  1  349 ? 36.346 -4.487  12.785  1.00 33.42  ?  381 GLU A O     1 
ATOM   2810  C  CB    . GLU A  1  349 ? 35.269 -5.774  15.645  1.00 42.69  ?  381 GLU A CB    1 
ATOM   2811  C  CG    . GLU A  1  349 ? 35.810 -5.648  17.055  1.00 50.08  ?  381 GLU A CG    1 
ATOM   2812  C  CD    . GLU A  1  349 ? 37.264 -5.196  17.056  1.00 59.25  ?  381 GLU A CD    1 
ATOM   2813  O  OE1   . GLU A  1  349 ? 38.130 -5.954  16.542  1.00 64.27  ?  381 GLU A OE1   1 
ATOM   2814  O  OE2   . GLU A  1  349 ? 37.536 -4.072  17.551  1.00 64.12  -1 381 GLU A OE2   1 
ATOM   2815  N  N     . ASP A  1  350 ? 34.292 -5.387  12.833  1.00 31.00  ?  382 ASP A N     1 
ATOM   2816  C  CA    . ASP A  1  350 ? 34.331 -5.961  11.491  1.00 29.08  ?  382 ASP A CA    1 
ATOM   2817  C  C     . ASP A  1  350 ? 32.892 -6.128  10.960  1.00 27.84  ?  382 ASP A C     1 
ATOM   2818  O  O     . ASP A  1  350 ? 31.989 -5.441  11.432  1.00 29.93  ?  382 ASP A O     1 
ATOM   2819  C  CB    . ASP A  1  350 ? 35.057 -7.297  11.558  1.00 29.97  ?  382 ASP A CB    1 
ATOM   2820  C  CG    . ASP A  1  350 ? 34.409 -8.258  12.530  1.00 30.92  ?  382 ASP A CG    1 
ATOM   2821  O  OD1   . ASP A  1  350 ? 33.198 -8.130  12.764  1.00 30.87  ?  382 ASP A OD1   1 
ATOM   2822  O  OD2   . ASP A  1  350 ? 35.102 -9.144  13.066  1.00 33.24  -1 382 ASP A OD2   1 
ATOM   2823  N  N     . LEU A  1  351 ? 32.658 -7.006  9.987   1.00 24.69  ?  383 LEU A N     1 
ATOM   2824  C  CA    . LEU A  1  351 ? 31.329 -7.153  9.425   1.00 22.83  ?  383 LEU A CA    1 
ATOM   2825  C  C     . LEU A  1  351 ? 30.807 -8.534  9.715   1.00 23.39  ?  383 LEU A C     1 
ATOM   2826  O  O     . LEU A  1  351 ? 29.958 -9.066  9.008   1.00 23.13  ?  383 LEU A O     1 
ATOM   2827  C  CB    . LEU A  1  351 ? 31.360 -6.849  7.925   1.00 22.10  ?  383 LEU A CB    1 
ATOM   2828  C  CG    . LEU A  1  351 ? 31.012 -5.417  7.474   1.00 21.54  ?  383 LEU A CG    1 
ATOM   2829  C  CD1   . LEU A  1  351 ? 31.599 -4.349  8.377   1.00 21.35  ?  383 LEU A CD1   1 
ATOM   2830  C  CD2   . LEU A  1  351 ? 31.454 -5.181  6.043   1.00 21.30  ?  383 LEU A CD2   1 
ATOM   2831  N  N     . GLN A  1  352 ? 31.312 -9.123  10.785  1.00 25.27  ?  384 GLN A N     1 
ATOM   2832  C  CA    . GLN A  1  352 ? 30.864 -10.444 11.210  1.00 26.64  ?  384 GLN A CA    1 
ATOM   2833  C  C     . GLN A  1  352 ? 29.431 -10.334 11.658  1.00 25.53  ?  384 GLN A C     1 
ATOM   2834  O  O     . GLN A  1  352 ? 28.977 -9.244  11.950  1.00 26.77  ?  384 GLN A O     1 
ATOM   2835  C  CB    . GLN A  1  352 ? 31.705 -10.932 12.383  1.00 28.97  ?  384 GLN A CB    1 
ATOM   2836  C  CG    . GLN A  1  352 ? 33.081 -11.428 11.986  1.00 30.18  ?  384 GLN A CG    1 
ATOM   2837  C  CD    . GLN A  1  352 ? 33.017 -12.835 11.432  1.00 31.37  ?  384 GLN A CD    1 
ATOM   2838  O  OE1   . GLN A  1  352 ? 33.392 -13.064 10.288  1.00 32.91  ?  384 GLN A OE1   1 
ATOM   2839  N  NE2   . GLN A  1  352 ? 32.502 -13.781 12.229  1.00 31.25  ?  384 GLN A NE2   1 
ATOM   2840  N  N     . PRO A  1  353 ? 28.712 -11.450 11.728  1.00 24.68  ?  385 PRO A N     1 
ATOM   2841  C  CA    . PRO A  1  353 ? 27.301 -11.341 12.119  1.00 25.10  ?  385 PRO A CA    1 
ATOM   2842  C  C     . PRO A  1  353 ? 27.072 -10.850 13.548  1.00 25.75  ?  385 PRO A C     1 
ATOM   2843  O  O     . PRO A  1  353 ? 26.137 -10.089 13.787  1.00 25.74  ?  385 PRO A O     1 
ATOM   2844  C  CB    . PRO A  1  353 ? 26.774 -12.767 11.937  1.00 24.73  ?  385 PRO A CB    1 
ATOM   2845  C  CG    . PRO A  1  353 ? 27.667 -13.353 10.894  1.00 24.87  ?  385 PRO A CG    1 
ATOM   2846  C  CD    . PRO A  1  353 ? 29.027 -12.767 11.165  1.00 24.70  ?  385 PRO A CD    1 
ATOM   2847  N  N     . GLU A  1  354 ? 27.929 -11.272 14.468  1.00 26.49  ?  386 GLU A N     1 
ATOM   2848  C  CA    . GLU A  1  354 ? 27.829 -10.875 15.859  1.00 27.88  ?  386 GLU A CA    1 
ATOM   2849  C  C     . GLU A  1  354 ? 28.104 -9.363  15.916  1.00 25.53  ?  386 GLU A C     1 
ATOM   2850  O  O     . GLU A  1  354 ? 27.356 -8.602  16.549  1.00 25.40  ?  386 GLU A O     1 
ATOM   2851  C  CB    . GLU A  1  354 ? 28.819 -11.654 16.753  1.00 33.52  ?  386 GLU A CB    1 
ATOM   2852  C  CG    . GLU A  1  354 ? 29.106 -13.127 16.364  1.00 40.54  ?  386 GLU A CG    1 
ATOM   2853  C  CD    . GLU A  1  354 ? 30.232 -13.317 15.281  1.00 46.89  ?  386 GLU A CD    1 
ATOM   2854  O  OE1   . GLU A  1  354 ? 31.429 -12.939 15.539  1.00 50.69  ?  386 GLU A OE1   1 
ATOM   2855  O  OE2   . GLU A  1  354 ? 29.921 -13.857 14.170  1.00 42.15  -1 386 GLU A OE2   1 
ATOM   2856  N  N     . SER A  1  355 ? 29.147 -8.908  15.221  1.00 22.95  ?  387 SER A N     1 
ATOM   2857  C  CA    . SER A  1  355 ? 29.436 -7.456  15.142  1.00 21.15  ?  387 SER A CA    1 
ATOM   2858  C  C     . SER A  1  355 ? 28.230 -6.604  14.773  1.00 19.69  ?  387 SER A C     1 
ATOM   2859  O  O     . SER A  1  355 ? 27.996 -5.578  15.378  1.00 20.97  ?  387 SER A O     1 
ATOM   2860  C  CB    . SER A  1  355 ? 30.539 -7.157  14.134  1.00 20.53  ?  387 SER A CB    1 
ATOM   2861  O  OG    . SER A  1  355 ? 31.795 -7.465  14.676  1.00 20.55  ?  387 SER A OG    1 
ATOM   2862  N  N     . LEU A  1  356 ? 27.491 -7.027  13.763  1.00 17.99  ?  388 LEU A N     1 
ATOM   2863  C  CA    . LEU A  1  356 ? 26.375 -6.258  13.246  1.00 17.29  ?  388 LEU A CA    1 
ATOM   2864  C  C     . LEU A  1  356 ? 25.121 -6.419  14.087  1.00 17.65  ?  388 LEU A C     1 
ATOM   2865  O  O     . LEU A  1  356 ? 24.334 -5.469  14.225  1.00 17.82  ?  388 LEU A O     1 
ATOM   2866  C  CB    . LEU A  1  356 ? 26.069 -6.679  11.805  1.00 16.50  ?  388 LEU A CB    1 
ATOM   2867  C  CG    . LEU A  1  356 ? 27.151 -6.320  10.815  1.00 15.76  ?  388 LEU A CG    1 
ATOM   2868  C  CD1   . LEU A  1  356 ? 26.777 -6.817  9.442   1.00 15.71  ?  388 LEU A CD1   1 
ATOM   2869  C  CD2   . LEU A  1  356 ? 27.337 -4.820  10.792  1.00 15.82  ?  388 LEU A CD2   1 
ATOM   2870  N  N     . TYR A  1  357 ? 24.903 -7.625  14.603  1.00 17.55  ?  389 TYR A N     1 
ATOM   2871  C  CA    . TYR A  1  357 ? 23.809 -7.844  15.519  1.00 17.95  ?  389 TYR A CA    1 
ATOM   2872  C  C     . TYR A  1  357 ? 23.945 -6.910  16.709  1.00 17.23  ?  389 TYR A C     1 
ATOM   2873  O  O     . TYR A  1  357 ? 22.959 -6.332  17.193  1.00 16.76  ?  389 TYR A O     1 
ATOM   2874  C  CB    . TYR A  1  357 ? 23.823 -9.253  16.026  1.00 19.24  ?  389 TYR A CB    1 
ATOM   2875  C  CG    . TYR A  1  357 ? 22.563 -9.635  16.753  1.00 20.80  ?  389 TYR A CG    1 
ATOM   2876  C  CD1   . TYR A  1  357 ? 21.345 -9.737  16.061  1.00 21.68  ?  389 TYR A CD1   1 
ATOM   2877  C  CD2   . TYR A  1  357 ? 22.587 -9.930  18.110  1.00 21.22  ?  389 TYR A CD2   1 
ATOM   2878  C  CE1   . TYR A  1  357 ? 20.187 -10.106 16.702  1.00 22.47  ?  389 TYR A CE1   1 
ATOM   2879  C  CE2   . TYR A  1  357 ? 21.436 -10.311 18.761  1.00 22.51  ?  389 TYR A CE2   1 
ATOM   2880  C  CZ    . TYR A  1  357 ? 20.247 -10.395 18.046  1.00 23.66  ?  389 TYR A CZ    1 
ATOM   2881  O  OH    . TYR A  1  357 ? 19.105 -10.762 18.704  1.00 27.92  ?  389 TYR A OH    1 
ATOM   2882  N  N     . GLY A  1  358 ? 25.180 -6.747  17.169  1.00 16.01  ?  390 GLY A N     1 
ATOM   2883  C  CA    . GLY A  1  358 ? 25.444 -5.824  18.262  1.00 15.61  ?  390 GLY A CA    1 
ATOM   2884  C  C     . GLY A  1  358 ? 25.132 -4.375  17.965  1.00 14.99  ?  390 GLY A C     1 
ATOM   2885  O  O     . GLY A  1  358 ? 24.678 -3.640  18.848  1.00 15.10  ?  390 GLY A O     1 
ATOM   2886  N  N     . LEU A  1  359 ? 25.413 -3.956  16.733  1.00 14.29  ?  391 LEU A N     1 
ATOM   2887  C  CA    . LEU A  1  359 ? 25.087 -2.615  16.294  1.00 13.84  ?  391 LEU A CA    1 
ATOM   2888  C  C     . LEU A  1  359 ? 23.573 -2.478  16.262  1.00 14.08  ?  391 LEU A C     1 
ATOM   2889  O  O     . LEU A  1  359 ? 23.015 -1.467  16.670  1.00 13.76  ?  391 LEU A O     1 
ATOM   2890  C  CB    . LEU A  1  359 ? 25.701 -2.344  14.926  1.00 13.40  ?  391 LEU A CB    1 
ATOM   2891  C  CG    . LEU A  1  359 ? 25.510 -0.962  14.302  1.00 13.11  ?  391 LEU A CG    1 
ATOM   2892  C  CD1   . LEU A  1  359 ? 26.012 0.150   15.183  1.00 13.01  ?  391 LEU A CD1   1 
ATOM   2893  C  CD2   . LEU A  1  359 ? 26.244 -0.892  12.978  1.00 13.14  ?  391 LEU A CD2   1 
ATOM   2894  N  N     . ALA A  1  360 ? 22.900 -3.522  15.807  1.00 14.67  ?  392 ALA A N     1 
ATOM   2895  C  CA    . ALA A  1  360 ? 21.455 -3.477  15.721  1.00 15.33  ?  392 ALA A CA    1 
ATOM   2896  C  C     . ALA A  1  360 ? 20.846 -3.207  17.091  1.00 16.23  ?  392 ALA A C     1 
ATOM   2897  O  O     . ALA A  1  360 ? 19.936 -2.393  17.223  1.00 16.03  ?  392 ALA A O     1 
ATOM   2898  C  CB    . ALA A  1  360 ? 20.918 -4.764  15.128  1.00 15.09  ?  392 ALA A CB    1 
ATOM   2899  N  N     . LYS A  1  361 ? 21.376 -3.868  18.113  1.00 17.49  ?  393 LYS A N     1 
ATOM   2900  C  CA    . LYS A  1  361 ? 20.877 -3.698  19.465  1.00 18.02  ?  393 LYS A CA    1 
ATOM   2901  C  C     . LYS A  1  361 ? 21.081 -2.277  19.888  1.00 18.32  ?  393 LYS A C     1 
ATOM   2902  O  O     . LYS A  1  361 ? 20.179 -1.666  20.430  1.00 18.51  ?  393 LYS A O     1 
ATOM   2903  C  CB    . LYS A  1  361 ? 21.611 -4.616  20.409  1.00 19.11  ?  393 LYS A CB    1 
ATOM   2904  C  CG    . LYS A  1  361 ? 21.269 -6.094  20.247  1.00 20.57  ?  393 LYS A CG    1 
ATOM   2905  C  CD    . LYS A  1  361 ? 19.905 -6.409  20.846  1.00 22.35  ?  393 LYS A CD    1 
ATOM   2906  C  CE    . LYS A  1  361 ? 19.703 -7.902  21.081  1.00 24.44  ?  393 LYS A CE    1 
ATOM   2907  N  NZ    . LYS A  1  361 ? 18.393 -8.205  21.741  1.00 25.52  1  393 LYS A NZ    1 
ATOM   2908  N  N     . GLN A  1  362 ? 22.250 -1.724  19.595  1.00 19.47  ?  394 GLN A N     1 
ATOM   2909  C  CA    . GLN A  1  362 ? 22.521 -0.326  19.930  1.00 20.97  ?  394 GLN A CA    1 
ATOM   2910  C  C     . GLN A  1  362 ? 21.487 0.606   19.307  1.00 19.76  ?  394 GLN A C     1 
ATOM   2911  O  O     . GLN A  1  362 ? 21.165 1.628   19.859  1.00 18.96  ?  394 GLN A O     1 
ATOM   2912  C  CB    . GLN A  1  362 ? 23.906 0.111   19.444  1.00 24.02  ?  394 GLN A CB    1 
ATOM   2913  C  CG    . GLN A  1  362 ? 25.141 -0.529  20.085  1.00 26.09  ?  394 GLN A CG    1 
ATOM   2914  C  CD    . GLN A  1  362 ? 26.419 0.204   19.629  1.00 30.32  ?  394 GLN A CD    1 
ATOM   2915  O  OE1   . GLN A  1  362 ? 27.327 -0.368  18.984  1.00 30.29  ?  394 GLN A OE1   1 
ATOM   2916  N  NE2   . GLN A  1  362 ? 26.476 1.509   19.939  1.00 34.15  ?  394 GLN A NE2   1 
ATOM   2917  N  N     . PHE A  1  363 ? 20.991 0.265   18.131  1.00 20.01  ?  395 PHE A N     1 
ATOM   2918  C  CA    . PHE A  1  363 ? 19.965 1.063   17.494  1.00 20.07  ?  395 PHE A CA    1 
ATOM   2919  C  C     . PHE A  1  363 ? 18.697 1.155   18.312  1.00 21.17  ?  395 PHE A C     1 
ATOM   2920  O  O     . PHE A  1  363 ? 18.010 2.168   18.251  1.00 22.13  ?  395 PHE A O     1 
ATOM   2921  C  CB    . PHE A  1  363 ? 19.585 0.478   16.141  1.00 19.66  ?  395 PHE A CB    1 
ATOM   2922  C  CG    . PHE A  1  363 ? 20.638 0.594   15.100  1.00 19.50  ?  395 PHE A CG    1 
ATOM   2923  C  CD1   . PHE A  1  363 ? 21.788 1.365   15.288  1.00 19.78  ?  395 PHE A CD1   1 
ATOM   2924  C  CD2   . PHE A  1  363 ? 20.449 -0.026  13.889  1.00 19.63  ?  395 PHE A CD2   1 
ATOM   2925  C  CE1   . PHE A  1  363 ? 22.740 1.474   14.290  1.00 19.67  ?  395 PHE A CE1   1 
ATOM   2926  C  CE2   . PHE A  1  363 ? 21.397 0.080   12.887  1.00 19.88  ?  395 PHE A CE2   1 
ATOM   2927  C  CZ    . PHE A  1  363 ? 22.543 0.833   13.088  1.00 19.69  ?  395 PHE A CZ    1 
ATOM   2928  N  N     . THR A  1  364 ? 18.382 0.094   19.056  1.00 22.02  ?  396 THR A N     1 
ATOM   2929  C  CA    . THR A  1  364 ? 17.133 0.001   19.827  1.00 22.29  ?  396 THR A CA    1 
ATOM   2930  C  C     . THR A  1  364 ? 17.056 0.969   21.042  1.00 22.56  ?  396 THR A C     1 
ATOM   2931  O  O     . THR A  1  364 ? 15.975 1.387   21.461  1.00 24.43  ?  396 THR A O     1 
ATOM   2932  C  CB    . THR A  1  364 ? 16.900 -1.455  20.274  1.00 22.69  ?  396 THR A CB    1 
ATOM   2933  O  OG1   . THR A  1  364 ? 17.893 -1.844  21.227  1.00 22.33  ?  396 THR A OG1   1 
ATOM   2934  C  CG2   . THR A  1  364 ? 16.978 -2.395  19.083  1.00 22.92  ?  396 THR A CG2   1 
ATOM   2935  N  N     . ILE A  1  365 ? 18.199 1.334   21.594  1.00 22.05  ?  397 ILE A N     1 
ATOM   2936  C  CA    . ILE A  1  365 ? 18.267 2.399   22.581  1.00 22.12  ?  397 ILE A CA    1 
ATOM   2937  C  C     . ILE A  1  365 ? 17.370 3.580   22.217  1.00 24.74  ?  397 ILE A C     1 
ATOM   2938  O  O     . ILE A  1  365 ? 17.419 4.057   21.085  1.00 23.84  ?  397 ILE A O     1 
ATOM   2939  C  CB    . ILE A  1  365 ? 19.703 2.939   22.656  1.00 20.89  ?  397 ILE A CB    1 
ATOM   2940  C  CG1   . ILE A  1  365 ? 20.627 1.883   23.255  1.00 20.26  ?  397 ILE A CG1   1 
ATOM   2941  C  CG2   . ILE A  1  365 ? 19.771 4.235   23.457  1.00 20.83  ?  397 ILE A CG2   1 
ATOM   2942  C  CD1   . ILE A  1  365 ? 22.091 2.237   23.185  1.00 20.22  ?  397 ILE A CD1   1 
ATOM   2943  N  N     . LEU A  1  366 ? 16.577 4.067   23.178  1.00 28.35  ?  398 LEU A N     1 
ATOM   2944  C  CA    . LEU A  1  366 ? 15.816 5.312   22.983  1.00 31.71  ?  398 LEU A CA    1 
ATOM   2945  C  C     . LEU A  1  366 ? 16.710 6.382   22.377  1.00 31.83  ?  398 LEU A C     1 
ATOM   2946  O  O     . LEU A  1  366 ? 17.783 6.669   22.890  1.00 32.13  ?  398 LEU A O     1 
ATOM   2947  C  CB    . LEU A  1  366 ? 15.279 5.856   24.314  1.00 36.16  ?  398 LEU A CB    1 
ATOM   2948  C  CG    . LEU A  1  366 ? 13.874 5.544   24.884  1.00 39.06  ?  398 LEU A CG    1 
ATOM   2949  C  CD1   . LEU A  1  366 ? 13.239 4.264   24.322  1.00 40.59  ?  398 LEU A CD1   1 
ATOM   2950  C  CD2   . LEU A  1  366 ? 13.945 5.504   26.422  1.00 38.42  ?  398 LEU A CD2   1 
ATOM   2951  N  N     . ASP A  1  367 ? 16.260 6.981   21.291  1.00 33.45  ?  399 ASP A N     1 
ATOM   2952  C  CA    . ASP A  1  367 ? 16.989 8.087   20.650  1.00 35.15  ?  399 ASP A CA    1 
ATOM   2953  C  C     . ASP A  1  367 ? 18.421 7.758   20.266  1.00 32.07  ?  399 ASP A C     1 
ATOM   2954  O  O     . ASP A  1  367 ? 19.276 8.638   20.266  1.00 30.63  ?  399 ASP A O     1 
ATOM   2955  C  CB    . ASP A  1  367 ? 16.959 9.347   21.524  1.00 38.64  ?  399 ASP A CB    1 
ATOM   2956  C  CG    . ASP A  1  367 ? 15.542 9.844   21.771  1.00 43.91  ?  399 ASP A CG    1 
ATOM   2957  O  OD1   . ASP A  1  367 ? 14.811 9.210   22.602  1.00 44.53  ?  399 ASP A OD1   1 
ATOM   2958  O  OD2   . ASP A  1  367 ? 15.171 10.857  21.110  1.00 44.89  -1 399 ASP A OD2   1 
ATOM   2959  N  N     . SER A  1  368 ? 18.662 6.500   19.896  1.00 29.58  ?  400 SER A N     1 
ATOM   2960  C  CA    . SER A  1  368 ? 19.994 6.057   19.486  1.00 27.49  ?  400 SER A CA    1 
ATOM   2961  C  C     . SER A  1  368 ? 20.581 6.998   18.449  1.00 26.75  ?  400 SER A C     1 
ATOM   2962  O  O     . SER A  1  368 ? 20.051 7.119   17.364  1.00 26.57  ?  400 SER A O     1 
ATOM   2963  C  CB    . SER A  1  368 ? 19.951 4.630   18.917  1.00 25.84  ?  400 SER A CB    1 
ATOM   2964  O  OG    . SER A  1  368 ? 21.250 4.178   18.610  1.00 24.08  ?  400 SER A OG    1 
ATOM   2965  N  N     . LYS A  1  369 ? 21.667 7.668   18.808  1.00 27.20  ?  401 LYS A N     1 
ATOM   2966  C  CA    . LYS A  1  369 ? 22.466 8.428   17.849  1.00 27.73  ?  401 LYS A CA    1 
ATOM   2967  C  C     . LYS A  1  369 ? 22.943 7.504   16.727  1.00 24.36  ?  401 LYS A C     1 
ATOM   2968  O  O     . LYS A  1  369 ? 23.177 7.966   15.625  1.00 24.41  ?  401 LYS A O     1 
ATOM   2969  C  CB    . LYS A  1  369 ? 23.685 9.098   18.542  1.00 32.17  ?  401 LYS A CB    1 
ATOM   2970  C  CG    . LYS A  1  369 ? 23.506 10.537  19.076  1.00 38.03  ?  401 LYS A CG    1 
ATOM   2971  C  CD    . LYS A  1  369 ? 22.376 10.725  20.108  1.00 45.07  ?  401 LYS A CD    1 
ATOM   2972  C  CE    . LYS A  1  369 ? 21.318 11.791  19.671  1.00 50.53  ?  401 LYS A CE    1 
ATOM   2973  N  NZ    . LYS A  1  369 ? 19.884 11.564  20.120  1.00 49.31  1  401 LYS A NZ    1 
ATOM   2974  N  N     . GLN A  1  370 ? 23.096 6.207   17.008  1.00 22.23  ?  402 GLN A N     1 
ATOM   2975  C  CA    . GLN A  1  370 ? 23.592 5.235   16.015  1.00 20.92  ?  402 GLN A CA    1 
ATOM   2976  C  C     . GLN A  1  370 ? 22.584 5.001   14.941  1.00 19.92  ?  402 GLN A C     1 
ATOM   2977  O  O     . GLN A  1  370 ? 22.885 5.151   13.775  1.00 20.44  ?  402 GLN A O     1 
ATOM   2978  C  CB    . GLN A  1  370 ? 23.898 3.875   16.639  1.00 20.99  ?  402 GLN A CB    1 
ATOM   2979  C  CG    . GLN A  1  370 ? 25.128 3.824   17.522  1.00 20.99  ?  402 GLN A CG    1 
ATOM   2980  C  CD    . GLN A  1  370 ? 26.407 4.013   16.734  1.00 20.88  ?  402 GLN A CD    1 
ATOM   2981  O  OE1   . GLN A  1  370 ? 26.638 5.083   16.114  1.00 21.34  ?  402 GLN A OE1   1 
ATOM   2982  N  NE2   . GLN A  1  370 ? 27.263 2.981   16.756  1.00 20.20  ?  402 GLN A NE2   1 
ATOM   2983  N  N     . PHE A  1  371 ? 21.382 4.622   15.335  1.00 18.93  ?  403 PHE A N     1 
ATOM   2984  C  CA    . PHE A  1  371 ? 20.288 4.537   14.392  1.00 18.57  ?  403 PHE A CA    1 
ATOM   2985  C  C     . PHE A  1  371 ? 20.099 5.835   13.603  1.00 18.66  ?  403 PHE A C     1 
ATOM   2986  O  O     . PHE A  1  371 ? 19.842 5.777   12.404  1.00 20.06  ?  403 PHE A O     1 
ATOM   2987  C  CB    . PHE A  1  371 ? 18.976 4.186   15.089  1.00 18.50  ?  403 PHE A CB    1 
ATOM   2988  C  CG    . PHE A  1  371 ? 17.815 4.108   14.155  1.00 18.20  ?  403 PHE A CG    1 
ATOM   2989  C  CD1   . PHE A  1  371 ? 17.585 2.961   13.421  1.00 18.35  ?  403 PHE A CD1   1 
ATOM   2990  C  CD2   . PHE A  1  371 ? 16.979 5.193   13.976  1.00 17.93  ?  403 PHE A CD2   1 
ATOM   2991  C  CE1   . PHE A  1  371 ? 16.526 2.902   12.538  1.00 18.35  ?  403 PHE A CE1   1 
ATOM   2992  C  CE2   . PHE A  1  371 ? 15.911 5.141   13.104  1.00 17.64  ?  403 PHE A CE2   1 
ATOM   2993  C  CZ    . PHE A  1  371 ? 15.686 3.997   12.385  1.00 18.23  ?  403 PHE A CZ    1 
ATOM   2994  N  N     . ILE A  1  372 ? 20.223 6.999   14.233  1.00 18.06  ?  404 ILE A N     1 
ATOM   2995  C  CA    . ILE A  1  372 ? 20.015 8.219   13.462  1.00 18.75  ?  404 ILE A CA    1 
ATOM   2996  C  C     . ILE A  1  372 ? 20.953 8.192   12.276  1.00 18.30  ?  404 ILE A C     1 
ATOM   2997  O  O     . ILE A  1  372 ? 20.517 8.444   11.171  1.00 18.85  ?  404 ILE A O     1 
ATOM   2998  C  CB    . ILE A  1  372 ? 20.258 9.579   14.187  1.00 19.81  ?  404 ILE A CB    1 
ATOM   2999  C  CG1   . ILE A  1  372 ? 19.669 9.659   15.601  1.00 20.82  ?  404 ILE A CG1   1 
ATOM   3000  C  CG2   . ILE A  1  372 ? 19.653 10.705  13.362  1.00 19.98  ?  404 ILE A CG2   1 
ATOM   3001  C  CD1   . ILE A  1  372 ? 18.201 9.292   15.735  1.00 21.34  ?  404 ILE A CD1   1 
ATOM   3002  N  N     . LYS A  1  373 ? 22.235 7.915   12.506  1.00 18.08  ?  405 LYS A N     1 
ATOM   3003  C  CA    . LYS A  1  373 ? 23.191 7.821   11.407  1.00 18.22  ?  405 LYS A CA    1 
ATOM   3004  C  C     . LYS A  1  373 ? 22.643 6.876   10.348  1.00 16.20  ?  405 LYS A C     1 
ATOM   3005  O  O     . LYS A  1  373 ? 22.538 7.224   9.182   1.00 14.78  ?  405 LYS A O     1 
ATOM   3006  C  CB    . LYS A  1  373 ? 24.524 7.233   11.880  1.00 20.51  ?  405 LYS A CB    1 
ATOM   3007  C  CG    . LYS A  1  373 ? 25.609 8.200   12.291  1.00 22.71  ?  405 LYS A CG    1 
ATOM   3008  C  CD    . LYS A  1  373 ? 26.922 7.430   12.471  1.00 25.56  ?  405 LYS A CD    1 
ATOM   3009  C  CE    . LYS A  1  373 ? 27.776 7.926   13.659  1.00 28.60  ?  405 LYS A CE    1 
ATOM   3010  N  NZ    . LYS A  1  373 ? 29.218 8.127   13.262  1.00 29.86  1  405 LYS A NZ    1 
ATOM   3011  N  N     . TYR A  1  374 ? 22.309 5.669   10.783  1.00 14.68  ?  406 TYR A N     1 
ATOM   3012  C  CA    . TYR A  1  374 ? 21.915 4.637   9.876   1.00 14.38  ?  406 TYR A CA    1 
ATOM   3013  C  C     . TYR A  1  374 ? 20.771 5.084   9.007   1.00 15.54  ?  406 TYR A C     1 
ATOM   3014  O  O     . TYR A  1  374 ? 20.664 4.643   7.860   1.00 16.53  ?  406 TYR A O     1 
ATOM   3015  C  CB    . TYR A  1  374 ? 21.527 3.374   10.628  1.00 13.50  ?  406 TYR A CB    1 
ATOM   3016  C  CG    . TYR A  1  374 ? 21.011 2.217   9.779   1.00 12.48  ?  406 TYR A CG    1 
ATOM   3017  C  CD1   . TYR A  1  374 ? 21.861 1.245   9.275   1.00 12.13  ?  406 TYR A CD1   1 
ATOM   3018  C  CD2   . TYR A  1  374 ? 19.672 2.089   9.513   1.00 12.23  ?  406 TYR A CD2   1 
ATOM   3019  C  CE1   . TYR A  1  374 ? 21.372 0.167   8.531   1.00 11.92  ?  406 TYR A CE1   1 
ATOM   3020  C  CE2   . TYR A  1  374 ? 19.176 1.022   8.769   1.00 12.08  ?  406 TYR A CE2   1 
ATOM   3021  C  CZ    . TYR A  1  374 ? 20.022 0.059   8.286   1.00 11.76  ?  406 TYR A CZ    1 
ATOM   3022  O  OH    . TYR A  1  374 ? 19.481 -0.979  7.568   1.00 11.20  ?  406 TYR A OH    1 
ATOM   3023  N  N     . TYR A  1  375 ? 19.911 5.952   9.518   1.00 16.40  ?  407 TYR A N     1 
ATOM   3024  C  CA    . TYR A  1  375 ? 18.801 6.439   8.707   1.00 17.01  ?  407 TYR A CA    1 
ATOM   3025  C  C     . TYR A  1  375 ? 19.189 7.571   7.721   1.00 19.40  ?  407 TYR A C     1 
ATOM   3026  O  O     . TYR A  1  375 ? 18.604 7.651   6.647   1.00 19.74  ?  407 TYR A O     1 
ATOM   3027  C  CB    . TYR A  1  375 ? 17.653 6.810   9.614   1.00 16.08  ?  407 TYR A CB    1 
ATOM   3028  C  CG    . TYR A  1  375 ? 16.304 6.778   8.967   1.00 15.63  ?  407 TYR A CG    1 
ATOM   3029  C  CD1   . TYR A  1  375 ? 15.666 5.596   8.674   1.00 15.48  ?  407 TYR A CD1   1 
ATOM   3030  C  CD2   . TYR A  1  375 ? 15.651 7.940   8.692   1.00 16.02  ?  407 TYR A CD2   1 
ATOM   3031  C  CE1   . TYR A  1  375 ? 14.424 5.591   8.074   1.00 15.59  ?  407 TYR A CE1   1 
ATOM   3032  C  CE2   . TYR A  1  375 ? 14.402 7.944   8.118   1.00 16.24  ?  407 TYR A CE2   1 
ATOM   3033  C  CZ    . TYR A  1  375 ? 13.801 6.780   7.804   1.00 15.93  ?  407 TYR A CZ    1 
ATOM   3034  O  OH    . TYR A  1  375 ? 12.564 6.888   7.239   1.00 16.76  ?  407 TYR A OH    1 
ATOM   3035  N  N     . ASN A  1  376 ? 20.169 8.418   8.048   1.00 22.38  ?  408 ASN A N     1 
ATOM   3036  C  CA    . ASN A  1  376 ? 20.768 9.287   7.036   1.00 26.12  ?  408 ASN A CA    1 
ATOM   3037  C  C     . ASN A  1  376 ? 21.377 8.448   5.967   1.00 24.99  ?  408 ASN A C     1 
ATOM   3038  O  O     . ASN A  1  376 ? 21.196 8.717   4.804   1.00 28.06  ?  408 ASN A O     1 
ATOM   3039  C  CB    . ASN A  1  376 ? 21.900 10.155  7.574   1.00 32.38  ?  408 ASN A CB    1 
ATOM   3040  C  CG    . ASN A  1  376 ? 21.404 11.265  8.465   1.00 39.74  ?  408 ASN A CG    1 
ATOM   3041  O  OD1   . ASN A  1  376 ? 20.476 11.978  8.087   1.00 48.85  ?  408 ASN A OD1   1 
ATOM   3042  N  ND2   . ASN A  1  376 ? 22.011 11.422  9.664   1.00 42.78  ?  408 ASN A ND2   1 
ATOM   3043  N  N     . TYR A  1  377 ? 22.128 7.435   6.356   1.00 23.39  ?  409 TYR A N     1 
ATOM   3044  C  CA    . TYR A  1  377 ? 22.836 6.637   5.387   1.00 22.91  ?  409 TYR A CA    1 
ATOM   3045  C  C     . TYR A  1  377 ? 21.878 5.784   4.596   1.00 21.44  ?  409 TYR A C     1 
ATOM   3046  O  O     . TYR A  1  377 ? 22.165 5.427   3.460   1.00 22.12  ?  409 TYR A O     1 
ATOM   3047  C  CB    . TYR A  1  377 ? 23.865 5.747   6.070   1.00 24.90  ?  409 TYR A CB    1 
ATOM   3048  C  CG    . TYR A  1  377 ? 25.041 6.488   6.680   1.00 27.46  ?  409 TYR A CG    1 
ATOM   3049  C  CD1   . TYR A  1  377 ? 25.368 7.789   6.285   1.00 28.88  ?  409 TYR A CD1   1 
ATOM   3050  C  CD2   . TYR A  1  377 ? 25.850 5.880   7.641   1.00 29.04  ?  409 TYR A CD2   1 
ATOM   3051  C  CE1   . TYR A  1  377 ? 26.439 8.462   6.841   1.00 29.00  ?  409 TYR A CE1   1 
ATOM   3052  C  CE2   . TYR A  1  377 ? 26.931 6.552   8.196   1.00 29.58  ?  409 TYR A CE2   1 
ATOM   3053  C  CZ    . TYR A  1  377 ? 27.217 7.838   7.778   1.00 29.48  ?  409 TYR A CZ    1 
ATOM   3054  O  OH    . TYR A  1  377 ? 28.291 8.520   8.284   1.00 32.28  ?  409 TYR A OH    1 
ATOM   3055  N  N     . PHE A  1  378 ? 20.737 5.456   5.185   1.00 19.33  ?  410 PHE A N     1 
ATOM   3056  C  CA    . PHE A  1  378 ? 19.701 4.678   4.496   1.00 17.44  ?  410 PHE A CA    1 
ATOM   3057  C  C     . PHE A  1  378 ? 19.230 5.287   3.171   1.00 16.37  ?  410 PHE A C     1 
ATOM   3058  O  O     . PHE A  1  378 ? 18.997 4.551   2.227   1.00 15.87  ?  410 PHE A O     1 
ATOM   3059  C  CB    . PHE A  1  378 ? 18.512 4.524   5.420   1.00 16.78  ?  410 PHE A CB    1 
ATOM   3060  C  CG    . PHE A  1  378 ? 17.364 3.783   4.817   1.00 16.32  ?  410 PHE A CG    1 
ATOM   3061  C  CD1   . PHE A  1  378 ? 17.436 2.423   4.607   1.00 16.24  ?  410 PHE A CD1   1 
ATOM   3062  C  CD2   . PHE A  1  378 ? 16.199 4.448   4.478   1.00 16.33  ?  410 PHE A CD2   1 
ATOM   3063  C  CE1   . PHE A  1  378 ? 16.361 1.733   4.078   1.00 16.17  ?  410 PHE A CE1   1 
ATOM   3064  C  CE2   . PHE A  1  378 ? 15.123 3.765   3.943   1.00 16.19  ?  410 PHE A CE2   1 
ATOM   3065  C  CZ    . PHE A  1  378 ? 15.204 2.406   3.747   1.00 15.97  ?  410 PHE A CZ    1 
ATOM   3066  N  N     . PHE A  1  379 ? 19.067 6.611   3.119   1.00 15.35  ?  411 PHE A N     1 
ATOM   3067  C  CA    . PHE A  1  379 ? 18.779 7.329   1.868   1.00 14.70  ?  411 PHE A CA    1 
ATOM   3068  C  C     . PHE A  1  379 ? 20.022 7.953   1.286   1.00 13.61  ?  411 PHE A C     1 
ATOM   3069  O  O     . PHE A  1  379 ? 19.939 8.980   0.624   1.00 13.01  ?  411 PHE A O     1 
ATOM   3070  C  CB    . PHE A  1  379 ? 17.812 8.479   2.100   1.00 15.30  ?  411 PHE A CB    1 
ATOM   3071  C  CG    . PHE A  1  379 ? 16.526 8.073   2.704   1.00 16.11  ?  411 PHE A CG    1 
ATOM   3072  C  CD1   . PHE A  1  379 ? 15.520 7.533   1.916   1.00 16.26  ?  411 PHE A CD1   1 
ATOM   3073  C  CD2   . PHE A  1  379 ? 16.304 8.248   4.067   1.00 16.80  ?  411 PHE A CD2   1 
ATOM   3074  C  CE1   . PHE A  1  379 ? 14.310 7.155   2.479   1.00 16.71  ?  411 PHE A CE1   1 
ATOM   3075  C  CE2   . PHE A  1  379 ? 15.088 7.876   4.633   1.00 17.19  ?  411 PHE A CE2   1 
ATOM   3076  C  CZ    . PHE A  1  379 ? 14.087 7.333   3.836   1.00 16.82  ?  411 PHE A CZ    1 
ATOM   3077  N  N     . VAL A  1  380 ? 21.168 7.340   1.549   1.00 12.90  ?  412 VAL A N     1 
ATOM   3078  C  CA    . VAL A  1  380 ? 22.467 7.804   1.058   1.00 12.46  ?  412 VAL A CA    1 
ATOM   3079  C  C     . VAL A  1  380 ? 22.712 9.319   1.213   1.00 12.64  ?  412 VAL A C     1 
ATOM   3080  O  O     . VAL A  1  380 ? 23.082 10.028  0.271   1.00 12.04  ?  412 VAL A O     1 
ATOM   3081  C  CB    . VAL A  1  380 ? 22.699 7.368   -0.377  1.00 11.82  ?  412 VAL A CB    1 
ATOM   3082  C  CG1   . VAL A  1  380 ? 24.166 7.525   -0.699  1.00 11.88  ?  412 VAL A CG1   1 
ATOM   3083  C  CG2   . VAL A  1  380 ? 22.270 5.934   -0.553  1.00 11.59  ?  412 VAL A CG2   1 
ATOM   3084  N  N     . SER A  1  381 ? 22.512 9.769   2.444   1.00 13.13  ?  413 SER A N     1 
ATOM   3085  C  CA    . SER A  1  381 ? 22.777 11.132  2.881   1.00 14.06  ?  413 SER A CA    1 
ATOM   3086  C  C     . SER A  1  381 ? 21.937 12.178  2.119   1.00 15.47  ?  413 SER A C     1 
ATOM   3087  O  O     . SER A  1  381 ? 22.278 13.348  2.081   1.00 15.39  ?  413 SER A O     1 
ATOM   3088  C  CB    . SER A  1  381 ? 24.291 11.434  2.826   1.00 13.76  ?  413 SER A CB    1 
ATOM   3089  O  OG    . SER A  1  381 ? 25.074 10.671  3.755   1.00 13.14  ?  413 SER A OG    1 
ATOM   3090  N  N     . TYR A  1  382 ? 20.799 11.760  1.587   1.00 17.56  ?  414 TYR A N     1 
ATOM   3091  C  CA    . TYR A  1  382 ? 20.041 12.584  0.654   1.00 20.42  ?  414 TYR A CA    1 
ATOM   3092  C  C     . TYR A  1  382 ? 19.453 13.879  1.234   1.00 24.61  ?  414 TYR A C     1 
ATOM   3093  O  O     . TYR A  1  382 ? 19.656 14.956  0.684   1.00 26.33  ?  414 TYR A O     1 
ATOM   3094  C  CB    . TYR A  1  382 ? 18.927 11.758  -0.032  1.00 19.81  ?  414 TYR A CB    1 
ATOM   3095  C  CG    . TYR A  1  382 ? 17.965 12.619  -0.823  1.00 18.43  ?  414 TYR A CG    1 
ATOM   3096  C  CD1   . TYR A  1  382 ? 18.324 13.142  -2.052  1.00 17.64  ?  414 TYR A CD1   1 
ATOM   3097  C  CD2   . TYR A  1  382 ? 16.721 12.930  -0.311  1.00 17.67  ?  414 TYR A CD2   1 
ATOM   3098  C  CE1   . TYR A  1  382 ? 17.456 13.938  -2.750  1.00 17.49  ?  414 TYR A CE1   1 
ATOM   3099  C  CE2   . TYR A  1  382 ? 15.850 13.718  -1.000  1.00 17.49  ?  414 TYR A CE2   1 
ATOM   3100  C  CZ    . TYR A  1  382 ? 16.222 14.223  -2.215  1.00 17.26  ?  414 TYR A CZ    1 
ATOM   3101  O  OH    . TYR A  1  382 ? 15.329 15.007  -2.882  1.00 16.86  ?  414 TYR A OH    1 
ATOM   3102  N  N     . ASP A  1  383 ? 18.660 13.775  2.283   1.00 30.41  ?  415 ASP A N     1 
ATOM   3103  C  CA    . ASP A  1  383 ? 18.399 14.934  3.108   1.00 37.08  ?  415 ASP A CA    1 
ATOM   3104  C  C     . ASP A  1  383 ? 19.017 14.483  4.388   1.00 40.93  ?  415 ASP A C     1 
ATOM   3105  O  O     . ASP A  1  383 ? 18.970 13.264  4.705   1.00 44.19  ?  415 ASP A O     1 
ATOM   3106  C  CB    . ASP A  1  383 ? 16.909 15.209  3.303   1.00 43.09  ?  415 ASP A CB    1 
ATOM   3107  C  CG    . ASP A  1  383 ? 16.650 16.398  4.240   1.00 45.92  ?  415 ASP A CG    1 
ATOM   3108  O  OD1   . ASP A  1  383 ? 17.536 17.294  4.299   1.00 44.76  ?  415 ASP A OD1   1 
ATOM   3109  O  OD2   . ASP A  1  383 ? 15.573 16.426  4.907   1.00 45.25  -1 415 ASP A OD2   1 
ATOM   3110  N  N     . SER A  1  384 ? 19.651 15.423  5.087   1.00 41.34  ?  416 SER A N     1 
ATOM   3111  C  CA    . SER A  1  384 ? 20.300 15.077  6.332   1.00 45.80  ?  416 SER A CA    1 
ATOM   3112  C  C     . SER A  1  384 ? 19.705 15.826  7.502   1.00 45.50  ?  416 SER A C     1 
ATOM   3113  O  O     . SER A  1  384 ? 20.093 15.619  8.646   1.00 48.79  ?  416 SER A O     1 
ATOM   3114  C  CB    . SER A  1  384 ? 21.833 15.177  6.213   1.00 49.42  ?  416 SER A CB    1 
ATOM   3115  O  OG    . SER A  1  384 ? 22.381 13.913  5.771   1.00 50.07  ?  416 SER A OG    1 
ATOM   3116  N  N     . SER A  1  385 ? 18.713 16.654  7.211   1.00 45.16  ?  417 SER A N     1 
ATOM   3117  C  CA    . SER A  1  385 ? 17.771 17.110  8.226   1.00 44.97  ?  417 SER A CA    1 
ATOM   3118  C  C     . SER A  1  385 ? 16.533 16.203  8.236   1.00 43.97  ?  417 SER A C     1 
ATOM   3119  O  O     . SER A  1  385 ? 15.411 16.664  8.497   1.00 42.12  ?  417 SER A O     1 
ATOM   3120  C  CB    . SER A  1  385 ? 17.337 18.538  7.920   1.00 45.87  ?  417 SER A CB    1 
ATOM   3121  O  OG    . SER A  1  385 ? 16.347 18.539  6.905   1.00 46.54  ?  417 SER A OG    1 
ATOM   3122  N  N     . VAL A  1  386 ? 16.732 14.923  7.937   1.00 42.87  ?  418 VAL A N     1 
ATOM   3123  C  CA    . VAL A  1  386 ? 15.620 13.990  7.828   1.00 41.03  ?  418 VAL A CA    1 
ATOM   3124  C  C     . VAL A  1  386 ? 15.466 13.306  9.170   1.00 36.51  ?  418 VAL A C     1 
ATOM   3125  O  O     . VAL A  1  386 ? 16.413 13.220  9.913   1.00 39.03  ?  418 VAL A O     1 
ATOM   3126  C  CB    . VAL A  1  386 ? 15.851 12.959  6.705   1.00 42.36  ?  418 VAL A CB    1 
ATOM   3127  C  CG1   . VAL A  1  386 ? 16.869 11.895  7.117   1.00 41.82  ?  418 VAL A CG1   1 
ATOM   3128  C  CG2   . VAL A  1  386 ? 14.525 12.317  6.313   1.00 44.36  ?  418 VAL A CG2   1 
ATOM   3129  N  N     . THR A  1  387 ? 14.276 12.836  9.486   1.00 32.31  ?  419 THR A N     1 
ATOM   3130  C  CA    . THR A  1  387 ? 14.005 12.304  10.805  1.00 29.60  ?  419 THR A CA    1 
ATOM   3131  C  C     . THR A  1  387 ? 13.132 11.089  10.652  1.00 27.10  ?  419 THR A C     1 
ATOM   3132  O  O     . THR A  1  387 ? 12.910 10.630  9.548   1.00 27.09  ?  419 THR A O     1 
ATOM   3133  C  CB    . THR A  1  387 ? 13.337 13.371  11.702  1.00 30.21  ?  419 THR A CB    1 
ATOM   3134  O  OG1   . THR A  1  387 ? 13.003 12.795  12.965  1.00 30.61  ?  419 THR A OG1   1 
ATOM   3135  C  CG2   . THR A  1  387 ? 12.065 13.934  11.067  1.00 30.58  ?  419 THR A CG2   1 
ATOM   3136  N  N     . CYS A  1  388 ? 12.615 10.572  11.752  1.00 26.23  ?  420 CYS A N     1 
ATOM   3137  C  CA    . CYS A  1  388 ? 11.997 9.250   11.737  1.00 26.69  ?  420 CYS A CA    1 
ATOM   3138  C  C     . CYS A  1  388 ? 11.230 9.001   13.022  1.00 25.26  ?  420 CYS A C     1 
ATOM   3139  O  O     . CYS A  1  388 ? 11.799 9.134   14.075  1.00 26.64  ?  420 CYS A O     1 
ATOM   3140  C  CB    . CYS A  1  388 ? 13.087 8.183   11.594  1.00 26.52  ?  420 CYS A CB    1 
ATOM   3141  S  SG    . CYS A  1  388 ? 12.422 6.520   11.525  1.00 28.62  ?  420 CYS A SG    1 
ATOM   3142  N  N     . ASP A  1  389 ? 9.957  8.641   12.951  1.00 23.73  ?  421 ASP A N     1 
ATOM   3143  C  CA    . ASP A  1  389 ? 9.169  8.476   14.173  1.00 23.63  ?  421 ASP A CA    1 
ATOM   3144  C  C     . ASP A  1  389 ? 9.319  7.055   14.738  1.00 23.10  ?  421 ASP A C     1 
ATOM   3145  O  O     . ASP A  1  389 ? 9.984  6.235   14.132  1.00 21.74  ?  421 ASP A O     1 
ATOM   3146  C  CB    . ASP A  1  389 ? 7.712  8.800   13.891  1.00 23.57  ?  421 ASP A CB    1 
ATOM   3147  C  CG    . ASP A  1  389 ? 7.064  7.750   13.092  1.00 23.88  ?  421 ASP A CG    1 
ATOM   3148  O  OD1   . ASP A  1  389 ? 7.789  7.147   12.291  1.00 25.75  ?  421 ASP A OD1   1 
ATOM   3149  O  OD2   . ASP A  1  389 ? 5.865  7.499   13.257  1.00 24.38  -1 421 ASP A OD2   1 
ATOM   3150  N  N     . LYS A  1  390 ? 8.698  6.781   15.886  1.00 24.43  ?  422 LYS A N     1 
ATOM   3151  C  CA    . LYS A  1  390 ? 8.888  5.510   16.599  1.00 27.26  ?  422 LYS A CA    1 
ATOM   3152  C  C     . LYS A  1  390 ? 8.523  4.316   15.733  1.00 26.37  ?  422 LYS A C     1 
ATOM   3153  O  O     . LYS A  1  390 ? 9.135  3.245   15.828  1.00 26.47  ?  422 LYS A O     1 
ATOM   3154  C  CB    . LYS A  1  390 ? 8.016  5.402   17.859  1.00 31.18  ?  422 LYS A CB    1 
ATOM   3155  C  CG    . LYS A  1  390 ? 8.215  6.463   18.935  1.00 36.99  ?  422 LYS A CG    1 
ATOM   3156  C  CD    . LYS A  1  390 ? 6.965  6.666   19.829  1.00 43.48  ?  422 LYS A CD    1 
ATOM   3157  C  CE    . LYS A  1  390 ? 5.648  6.794   19.023  1.00 46.37  ?  422 LYS A CE    1 
ATOM   3158  N  NZ    . LYS A  1  390 ? 4.457  7.382   19.714  1.00 46.57  1  422 LYS A NZ    1 
ATOM   3159  N  N     . THR A  1  391 ? 7.499  4.489   14.914  1.00 23.99  ?  423 THR A N     1 
ATOM   3160  C  CA    . THR A  1  391 ? 6.963  3.389   14.152  1.00 23.23  ?  423 THR A CA    1 
ATOM   3161  C  C     . THR A  1  391 ? 7.862  3.032   12.959  1.00 22.97  ?  423 THR A C     1 
ATOM   3162  O  O     . THR A  1  391 ? 8.235  1.866   12.765  1.00 21.64  ?  423 THR A O     1 
ATOM   3163  C  CB    . THR A  1  391 ? 5.561  3.768   13.700  1.00 23.44  ?  423 THR A CB    1 
ATOM   3164  O  OG1   . THR A  1  391 ? 4.879  4.330   14.823  1.00 23.26  ?  423 THR A OG1   1 
ATOM   3165  C  CG2   . THR A  1  391 ? 4.807  2.567   13.195  1.00 23.58  ?  423 THR A CG2   1 
ATOM   3166  N  N     . CYS A  1  392 ? 8.229  4.040   12.177  1.00 22.85  ?  424 CYS A N     1 
ATOM   3167  C  CA    . CYS A  1  392 ? 9.191  3.830   11.111  1.00 24.36  ?  424 CYS A CA    1 
ATOM   3168  C  C     . CYS A  1  392 ? 10.430 3.146   11.638  1.00 21.93  ?  424 CYS A C     1 
ATOM   3169  O  O     . CYS A  1  392 ? 10.869 2.149   11.065  1.00 22.24  ?  424 CYS A O     1 
ATOM   3170  C  CB    . CYS A  1  392 ? 9.552  5.139   10.407  1.00 27.11  ?  424 CYS A CB    1 
ATOM   3171  S  SG    . CYS A  1  392 ? 8.312  5.528   9.127   1.00 35.69  ?  424 CYS A SG    1 
ATOM   3172  N  N     . LYS A  1  393 ? 10.959 3.660   12.745  1.00 18.95  ?  425 LYS A N     1 
ATOM   3173  C  CA    . LYS A  1  393 ? 12.114 3.058   13.375  1.00 17.28  ?  425 LYS A CA    1 
ATOM   3174  C  C     . LYS A  1  393 ? 11.860 1.640   13.786  1.00 16.57  ?  425 LYS A C     1 
ATOM   3175  O  O     . LYS A  1  393 ? 12.746 0.816   13.699  1.00 16.76  ?  425 LYS A O     1 
ATOM   3176  C  CB    . LYS A  1  393 ? 12.555 3.835   14.605  1.00 16.67  ?  425 LYS A CB    1 
ATOM   3177  C  CG    . LYS A  1  393 ? 13.586 3.108   15.462  1.00 16.14  ?  425 LYS A CG    1 
ATOM   3178  C  CD    . LYS A  1  393 ? 14.426 4.065   16.271  1.00 15.80  ?  425 LYS A CD    1 
ATOM   3179  C  CE    . LYS A  1  393 ? 14.986 3.424   17.537  1.00 15.82  ?  425 LYS A CE    1 
ATOM   3180  N  NZ    . LYS A  1  393 ? 15.987 4.337   18.171  1.00 15.96  1  425 LYS A NZ    1 
ATOM   3181  N  N     . ALA A  1  394 ? 10.674 1.344   14.267  1.00 15.89  ?  426 ALA A N     1 
ATOM   3182  C  CA    . ALA A  1  394 ? 10.395 -0.016  14.650  1.00 16.15  ?  426 ALA A CA    1 
ATOM   3183  C  C     . ALA A  1  394 ? 10.435 -0.905  13.431  1.00 16.52  ?  426 ALA A C     1 
ATOM   3184  O  O     . ALA A  1  394 ? 10.946 -2.017  13.457  1.00 16.18  ?  426 ALA A O     1 
ATOM   3185  C  CB    . ALA A  1  394 ? 9.040  -0.096  15.289  1.00 16.45  ?  426 ALA A CB    1 
ATOM   3186  N  N     . PHE A  1  395 ? 9.880  -0.403  12.348  1.00 17.41  ?  427 PHE A N     1 
ATOM   3187  C  CA    . PHE A  1  395 ? 9.812  -1.187  11.143  1.00 18.48  ?  427 PHE A CA    1 
ATOM   3188  C  C     . PHE A  1  395 ? 11.181 -1.444  10.566  1.00 17.67  ?  427 PHE A C     1 
ATOM   3189  O  O     . PHE A  1  395 ? 11.359 -2.406  9.819   1.00 18.96  ?  427 PHE A O     1 
ATOM   3190  C  CB    . PHE A  1  395 ? 8.968  -0.477  10.076  1.00 19.98  ?  427 PHE A CB    1 
ATOM   3191  C  CG    . PHE A  1  395 ? 7.507  -0.415  10.387  1.00 20.48  ?  427 PHE A CG    1 
ATOM   3192  C  CD1   . PHE A  1  395 ? 6.906  -1.337  11.249  1.00 20.88  ?  427 PHE A CD1   1 
ATOM   3193  C  CD2   . PHE A  1  395 ? 6.725  0.562   9.782   1.00 20.94  ?  427 PHE A CD2   1 
ATOM   3194  C  CE1   . PHE A  1  395 ? 5.552  -1.265  11.513  1.00 21.73  ?  427 PHE A CE1   1 
ATOM   3195  C  CE2   . PHE A  1  395 ? 5.379  0.649   10.043  1.00 21.03  ?  427 PHE A CE2   1 
ATOM   3196  C  CZ    . PHE A  1  395 ? 4.789  -0.270  10.907  1.00 21.89  ?  427 PHE A CZ    1 
ATOM   3197  N  N     . GLN A  1  396 ? 12.114 -0.549  10.843  1.00 16.56  ?  428 GLN A N     1 
ATOM   3198  C  CA    . GLN A  1  396 ? 13.485 -0.715  10.401  1.00 16.29  ?  428 GLN A CA    1 
ATOM   3199  C  C     . GLN A  1  396 ? 14.152 -1.761  11.264  1.00 16.42  ?  428 GLN A C     1 
ATOM   3200  O  O     . GLN A  1  396 ? 14.716 -2.728  10.759  1.00 16.29  ?  428 GLN A O     1 
ATOM   3201  C  CB    . GLN A  1  396 ? 14.258 0.595   10.546  1.00 16.20  ?  428 GLN A CB    1 
ATOM   3202  C  CG    . GLN A  1  396 ? 13.996 1.632   9.471   1.00 15.83  ?  428 GLN A CG    1 
ATOM   3203  C  CD    . GLN A  1  396 ? 14.782 1.407   8.203   1.00 15.81  ?  428 GLN A CD    1 
ATOM   3204  O  OE1   . GLN A  1  396 ? 15.711 0.588   8.142   1.00 16.60  ?  428 GLN A OE1   1 
ATOM   3205  N  NE2   . GLN A  1  396 ? 14.413 2.132   7.167   1.00 15.96  ?  428 GLN A NE2   1 
ATOM   3206  N  N     . ILE A  1  397 ? 14.077 -1.563  12.575  1.00 16.84  ?  429 ILE A N     1 
ATOM   3207  C  CA    . ILE A  1  397 ? 14.761 -2.434  13.516  1.00 17.71  ?  429 ILE A CA    1 
ATOM   3208  C  C     . ILE A  1  397 ? 14.353 -3.867  13.283  1.00 17.90  ?  429 ILE A C     1 
ATOM   3209  O  O     . ILE A  1  397 ? 15.200 -4.709  13.035  1.00 18.16  ?  429 ILE A O     1 
ATOM   3210  C  CB    . ILE A  1  397 ? 14.450 -2.087  14.987  1.00 18.36  ?  429 ILE A CB    1 
ATOM   3211  C  CG1   . ILE A  1  397 ? 15.012 -0.713  15.351  1.00 18.54  ?  429 ILE A CG1   1 
ATOM   3212  C  CG2   . ILE A  1  397 ? 15.015 -3.146  15.941  1.00 18.47  ?  429 ILE A CG2   1 
ATOM   3213  C  CD1   . ILE A  1  397 ? 16.494 -0.558  15.122  1.00 18.53  ?  429 ILE A CD1   1 
ATOM   3214  N  N     . CYS A  1  398 ? 13.063 -4.146  13.355  1.00 17.92  ?  430 CYS A N     1 
ATOM   3215  C  CA    . CYS A  1  398 ? 12.618 -5.502  13.165  1.00 18.43  ?  430 CYS A CA    1 
ATOM   3216  C  C     . CYS A  1  398 ? 13.115 -6.093  11.853  1.00 17.11  ?  430 CYS A C     1 
ATOM   3217  O  O     . CYS A  1  398 ? 13.417 -7.280  11.802  1.00 16.56  ?  430 CYS A O     1 
ATOM   3218  C  CB    . CYS A  1  398 ? 11.103 -5.587  13.233  1.00 20.41  ?  430 CYS A CB    1 
ATOM   3219  S  SG    . CYS A  1  398 ? 10.454 -5.359  14.902  1.00 24.52  ?  430 CYS A SG    1 
ATOM   3220  N  N     . ALA A  1  399 ? 13.195 -5.277  10.801  1.00 15.83  ?  431 ALA A N     1 
ATOM   3221  C  CA    . ALA A  1  399 ? 13.613 -5.762  9.501   1.00 15.07  ?  431 ALA A CA    1 
ATOM   3222  C  C     . ALA A  1  399 ? 15.055 -6.175  9.564   1.00 15.12  ?  431 ALA A C     1 
ATOM   3223  O  O     . ALA A  1  399 ? 15.421 -7.245  9.097   1.00 15.35  ?  431 ALA A O     1 
ATOM   3224  C  CB    . ALA A  1  399 ? 13.437 -4.698  8.464   1.00 14.90  ?  431 ALA A CB    1 
ATOM   3225  N  N     . ILE A  1  400 ? 15.873 -5.341  10.179  1.00 15.16  ?  432 ILE A N     1 
ATOM   3226  C  CA    . ILE A  1  400 ? 17.298 -5.632  10.303  1.00 15.64  ?  432 ILE A CA    1 
ATOM   3227  C  C     . ILE A  1  400 ? 17.612 -6.909  11.073  1.00 16.28  ?  432 ILE A C     1 
ATOM   3228  O  O     . ILE A  1  400 ? 18.591 -7.572  10.788  1.00 16.08  ?  432 ILE A O     1 
ATOM   3229  C  CB    . ILE A  1  400 ? 18.025 -4.496  11.022  1.00 15.32  ?  432 ILE A CB    1 
ATOM   3230  C  CG1   . ILE A  1  400 ? 17.883 -3.213  10.218  1.00 15.31  ?  432 ILE A CG1   1 
ATOM   3231  C  CG2   . ILE A  1  400 ? 19.504 -4.822  11.179  1.00 15.30  ?  432 ILE A CG2   1 
ATOM   3232  C  CD1   . ILE A  1  400 ? 18.017 -1.968  11.049  1.00 15.37  ?  432 ILE A CD1   1 
ATOM   3233  N  N     . MET A  1  401 ? 16.788 -7.234  12.060  1.00 17.98  ?  433 MET A N     1 
ATOM   3234  C  CA    . MET A  1  401 ? 17.069 -8.326  12.987  1.00 18.93  ?  433 MET A CA    1 
ATOM   3235  C  C     . MET A  1  401 ? 16.226 -9.539  12.770  1.00 18.38  ?  433 MET A C     1 
ATOM   3236  O  O     . MET A  1  401 ? 16.530 -10.570 13.333  1.00 19.53  ?  433 MET A O     1 
ATOM   3237  C  CB    . MET A  1  401 ? 16.869 -7.868  14.425  1.00 20.54  ?  433 MET A CB    1 
ATOM   3238  C  CG    . MET A  1  401 ? 18.125 -7.299  15.054  1.00 22.39  ?  433 MET A CG    1 
ATOM   3239  S  SD    . MET A  1  401 ? 17.739 -6.046  16.297  1.00 27.39  ?  433 MET A SD    1 
ATOM   3240  C  CE    . MET A  1  401 ? 18.983 -6.532  17.502  1.00 27.90  ?  433 MET A CE    1 
ATOM   3241  N  N     . ASN A  1  402 ? 15.165 -9.436  11.986  1.00 18.00  ?  434 ASN A N     1 
ATOM   3242  C  CA    . ASN A  1  402 ? 14.296 -10.580 11.749  1.00 17.87  ?  434 ASN A CA    1 
ATOM   3243  C  C     . ASN A  1  402 ? 13.959 -10.755 10.273  1.00 18.85  ?  434 ASN A C     1 
ATOM   3244  O  O     . ASN A  1  402 ? 13.463 -9.839  9.587   1.00 18.92  ?  434 ASN A O     1 
ATOM   3245  C  CB    . ASN A  1  402 ? 13.062 -10.479 12.628  1.00 17.50  ?  434 ASN A CB    1 
ATOM   3246  C  CG    . ASN A  1  402 ? 13.421 -10.127 14.056  1.00 16.84  ?  434 ASN A CG    1 
ATOM   3247  O  OD1   . ASN A  1  402 ? 13.773 -10.990 14.853  1.00 16.95  ?  434 ASN A OD1   1 
ATOM   3248  N  ND2   . ASN A  1  402 ? 13.388 -8.849  14.366  1.00 16.56  ?  434 ASN A ND2   1 
ATOM   3249  N  N     . LEU A  1  403 ? 14.296 -11.945 9.790   1.00 20.22  ?  435 LEU A N     1 
ATOM   3250  C  CA    . LEU A  1  403 ? 14.260 -12.250 8.383   1.00 21.01  ?  435 LEU A CA    1 
ATOM   3251  C  C     . LEU A  1  403 ? 13.116 -13.144 8.019   1.00 22.95  ?  435 LEU A C     1 
ATOM   3252  O  O     . LEU A  1  403 ? 12.640 -13.054 6.908   1.00 23.28  ?  435 LEU A O     1 
ATOM   3253  C  CB    . LEU A  1  403 ? 15.564 -12.898 7.966   1.00 20.59  ?  435 LEU A CB    1 
ATOM   3254  C  CG    . LEU A  1  403 ? 16.526 -11.870 7.394   1.00 21.06  ?  435 LEU A CG    1 
ATOM   3255  C  CD1   . LEU A  1  403 ? 16.962 -10.875 8.447   1.00 21.35  ?  435 LEU A CD1   1 
ATOM   3256  C  CD2   . LEU A  1  403 ? 17.737 -12.558 6.802   1.00 21.65  ?  435 LEU A CD2   1 
ATOM   3257  N  N     . ASP A  1  404 ? 12.707 -14.031 8.932   1.00 26.42  ?  436 ASP A N     1 
ATOM   3258  C  CA    . ASP A  1  404 ? 11.596 -14.966 8.701   1.00 28.21  ?  436 ASP A CA    1 
ATOM   3259  C  C     . ASP A  1  404 ? 10.445 -14.451 9.514   1.00 28.30  ?  436 ASP A C     1 
ATOM   3260  O  O     . ASP A  1  404 ? 10.650 -13.609 10.366  1.00 29.65  ?  436 ASP A O     1 
ATOM   3261  C  CB    . ASP A  1  404 ? 11.972 -16.390 9.113   1.00 29.98  ?  436 ASP A CB    1 
ATOM   3262  C  CG    . ASP A  1  404 ? 12.200 -16.527 10.604  1.00 33.05  ?  436 ASP A CG    1 
ATOM   3263  O  OD1   . ASP A  1  404 ? 11.191 -16.452 11.366  1.00 35.99  ?  436 ASP A OD1   1 
ATOM   3264  O  OD2   . ASP A  1  404 ? 13.386 -16.706 11.010  1.00 33.97  -1 436 ASP A OD2   1 
ATOM   3265  N  N     . ASN A  1  405 ? 9.246  -14.956 9.288   1.00 29.63  ?  437 ASN A N     1 
ATOM   3266  C  CA    . ASN A  1  405 ? 8.071  -14.232 9.757   1.00 32.08  ?  437 ASN A CA    1 
ATOM   3267  C  C     . ASN A  1  405 ? 7.719  -14.462 11.199  1.00 31.09  ?  437 ASN A C     1 
ATOM   3268  O  O     . ASN A  1  405 ? 7.043  -13.623 11.800  1.00 30.51  ?  437 ASN A O     1 
ATOM   3269  C  CB    . ASN A  1  405 ? 6.836  -14.529 8.909   1.00 35.87  ?  437 ASN A CB    1 
ATOM   3270  C  CG    . ASN A  1  405 ? 5.918  -15.534 9.554   1.00 38.57  ?  437 ASN A CG    1 
ATOM   3271  O  OD1   . ASN A  1  405 ? 4.736  -15.242 9.805   1.00 38.17  ?  437 ASN A OD1   1 
ATOM   3272  N  ND2   . ASN A  1  405 ? 6.460  -16.729 9.852   1.00 40.65  ?  437 ASN A ND2   1 
ATOM   3273  N  N     . ILE A  1  406 ? 8.126  -15.603 11.742  1.00 29.89  ?  438 ILE A N     1 
ATOM   3274  C  CA    . ILE A  1  406 ? 7.887  -15.863 13.146  1.00 30.45  ?  438 ILE A CA    1 
ATOM   3275  C  C     . ILE A  1  406 ? 8.552  -14.715 13.898  1.00 28.44  ?  438 ILE A C     1 
ATOM   3276  O  O     . ILE A  1  406 ? 7.895  -13.868 14.521  1.00 26.59  ?  438 ILE A O     1 
ATOM   3277  C  CB    . ILE A  1  406 ? 8.476  -17.234 13.583  1.00 32.89  ?  438 ILE A CB    1 
ATOM   3278  C  CG1   . ILE A  1  406 ? 7.527  -18.378 13.206  1.00 33.72  ?  438 ILE A CG1   1 
ATOM   3279  C  CG2   . ILE A  1  406 ? 8.768  -17.292 15.082  1.00 33.67  ?  438 ILE A CG2   1 
ATOM   3280  C  CD1   . ILE A  1  406 ? 6.250  -18.452 14.027  1.00 34.23  ?  438 ILE A CD1   1 
ATOM   3281  N  N     . SER A  1  407 ? 9.868  -14.681 13.791  1.00 26.34  ?  439 SER A N     1 
ATOM   3282  C  CA    . SER A  1  407 ? 10.660 -13.728 14.527  1.00 25.62  ?  439 SER A CA    1 
ATOM   3283  C  C     . SER A  1  407 ? 10.354 -12.255 14.169  1.00 24.26  ?  439 SER A C     1 
ATOM   3284  O  O     . SER A  1  407 ? 10.548 -11.378 15.009  1.00 23.52  ?  439 SER A O     1 
ATOM   3285  C  CB    . SER A  1  407 ? 12.108 -14.058 14.277  1.00 25.58  ?  439 SER A CB    1 
ATOM   3286  O  OG    . SER A  1  407 ? 12.210 -14.455 12.924  1.00 27.26  ?  439 SER A OG    1 
ATOM   3287  N  N     . TYR A  1  408 ? 9.881  -11.987 12.950  1.00 22.66  ?  440 TYR A N     1 
ATOM   3288  C  CA    . TYR A  1  408 ? 9.493  -10.635 12.571  1.00 22.24  ?  440 TYR A CA    1 
ATOM   3289  C  C     . TYR A  1  408 ? 8.235  -10.184 13.243  1.00 23.43  ?  440 TYR A C     1 
ATOM   3290  O  O     . TYR A  1  408 ? 8.082  -9.016  13.502  1.00 23.53  ?  440 TYR A O     1 
ATOM   3291  C  CB    . TYR A  1  408 ? 9.236  -10.516 11.092  1.00 21.74  ?  440 TYR A CB    1 
ATOM   3292  C  CG    . TYR A  1  408 ? 8.920  -9.104  10.663  1.00 20.69  ?  440 TYR A CG    1 
ATOM   3293  C  CD1   . TYR A  1  408 ? 9.931  -8.186  10.489  1.00 20.18  ?  440 TYR A CD1   1 
ATOM   3294  C  CD2   . TYR A  1  408 ? 7.611  -8.684  10.434  1.00 20.24  ?  440 TYR A CD2   1 
ATOM   3295  C  CE1   . TYR A  1  408 ? 9.659  -6.887  10.086  1.00 20.12  ?  440 TYR A CE1   1 
ATOM   3296  C  CE2   . TYR A  1  408 ? 7.327  -7.375  10.037  1.00 19.61  ?  440 TYR A CE2   1 
ATOM   3297  C  CZ    . TYR A  1  408 ? 8.361  -6.477  9.861   1.00 19.40  ?  440 TYR A CZ    1 
ATOM   3298  O  OH    . TYR A  1  408 ? 8.169  -5.171  9.454   1.00 18.75  ?  440 TYR A OH    1 
ATOM   3299  N  N     . ALA A  1  409 ? 7.308  -11.094 13.475  1.00 26.04  ?  441 ALA A N     1 
ATOM   3300  C  CA    . ALA A  1  409 ? 6.083  -10.743 14.189  1.00 28.33  ?  441 ALA A CA    1 
ATOM   3301  C  C     . ALA A  1  409 ? 6.329  -10.627 15.696  1.00 30.94  ?  441 ALA A C     1 
ATOM   3302  O  O     . ALA A  1  409 ? 5.842  -9.703  16.323  1.00 30.76  ?  441 ALA A O     1 
ATOM   3303  C  CB    . ALA A  1  409 ? 4.996  -11.762 13.901  1.00 28.51  ?  441 ALA A CB    1 
ATOM   3304  N  N     . ASP A  1  410 ? 7.087  -11.558 16.275  1.00 34.75  ?  442 ASP A N     1 
ATOM   3305  C  CA    . ASP A  1  410 ? 7.466  -11.457 17.677  1.00 37.54  ?  442 ASP A CA    1 
ATOM   3306  C  C     . ASP A  1  410 ? 7.998  -10.034 17.924  1.00 35.17  ?  442 ASP A C     1 
ATOM   3307  O  O     . ASP A  1  410 ? 7.666  -9.376  18.921  1.00 33.39  ?  442 ASP A O     1 
ATOM   3308  C  CB    . ASP A  1  410 ? 8.522  -12.531 18.033  1.00 43.07  ?  442 ASP A CB    1 
ATOM   3309  C  CG    . ASP A  1  410 ? 8.670  -12.768 19.571  1.00 51.51  ?  442 ASP A CG    1 
ATOM   3310  O  OD1   . ASP A  1  410 ? 7.686  -12.642 20.353  1.00 55.88  ?  442 ASP A OD1   1 
ATOM   3311  O  OD2   . ASP A  1  410 ? 9.791  -13.103 20.007  1.00 54.42  -1 442 ASP A OD2   1 
ATOM   3312  N  N     . CYS A  1  411 ? 8.798  -9.552  16.981  1.00 33.61  ?  443 CYS A N     1 
ATOM   3313  C  CA    . CYS A  1  411 ? 9.500  -8.279  17.142  1.00 33.76  ?  443 CYS A CA    1 
ATOM   3314  C  C     . CYS A  1  411 ? 8.556  -7.102  17.021  1.00 36.89  ?  443 CYS A C     1 
ATOM   3315  O  O     . CYS A  1  411 ? 8.738  -6.047  17.640  1.00 39.09  ?  443 CYS A O     1 
ATOM   3316  C  CB    . CYS A  1  411 ? 10.606 -8.167  16.096  1.00 30.95  ?  443 CYS A CB    1 
ATOM   3317  S  SG    . CYS A  1  411 ? 11.532 -6.625  16.123  1.00 27.20  ?  443 CYS A SG    1 
ATOM   3318  N  N     . LEU A  1  412 ? 7.557  -7.299  16.191  1.00 41.27  ?  444 LEU A N     1 
ATOM   3319  C  CA    . LEU A  1  412 ? 6.530  -6.322  15.968  1.00 45.41  ?  444 LEU A CA    1 
ATOM   3320  C  C     . LEU A  1  412 ? 5.544  -6.276  17.135  1.00 49.63  ?  444 LEU A C     1 
ATOM   3321  O  O     . LEU A  1  412 ? 5.153  -5.197  17.568  1.00 50.55  ?  444 LEU A O     1 
ATOM   3322  C  CB    . LEU A  1  412 ? 5.796  -6.705  14.695  1.00 46.34  ?  444 LEU A CB    1 
ATOM   3323  C  CG    . LEU A  1  412 ? 5.490  -5.589  13.724  1.00 49.00  ?  444 LEU A CG    1 
ATOM   3324  C  CD1   . LEU A  1  412 ? 6.716  -4.718  13.468  1.00 48.60  ?  444 LEU A CD1   1 
ATOM   3325  C  CD2   . LEU A  1  412 ? 4.905  -6.218  12.457  1.00 51.00  ?  444 LEU A CD2   1 
ATOM   3326  N  N     . LYS A  1  413 ? 5.071  -7.425  17.553  1.00 55.02  ?  445 LYS A N     1 
ATOM   3327  C  CA    . LYS A  1  413 ? 4.086  -7.454  18.603  1.00 61.75  ?  445 LYS A CA    1 
ATOM   3328  C  C     . LYS A  1  413 ? 4.748  -7.021  19.847  1.00 60.47  ?  445 LYS A C     1 
ATOM   3329  O  O     . LYS A  1  413 ? 4.216  -6.266  20.621  1.00 66.42  ?  445 LYS A O     1 
ATOM   3330  C  CB    . LYS A  1  413 ? 3.431  -8.829  18.704  1.00 69.33  ?  445 LYS A CB    1 
ATOM   3331  C  CG    . LYS A  1  413 ? 3.779  -9.688  19.892  1.00 76.36  ?  445 LYS A CG    1 
ATOM   3332  C  CD    . LYS A  1  413 ? 3.004  -10.984 19.885  1.00 82.52  ?  445 LYS A CD    1 
ATOM   3333  C  CE    . LYS A  1  413 ? 3.028  -11.655 18.531  1.00 86.44  ?  445 LYS A CE    1 
ATOM   3334  N  NZ    . LYS A  1  413 ? 3.618  -13.016 18.596  1.00 89.13  1  445 LYS A NZ    1 
ATOM   3335  N  N     . GLN A  1  414 ? 5.921  -7.536  20.038  1.00 56.36  ?  446 GLN A N     1 
ATOM   3336  C  CA    . GLN A  1  414 ? 6.647  -7.189  21.188  1.00 55.74  ?  446 GLN A CA    1 
ATOM   3337  C  C     . GLN A  1  414 ? 6.451  -5.717  21.400  1.00 59.96  ?  446 GLN A C     1 
ATOM   3338  O  O     . GLN A  1  414 ? 6.384  -5.321  22.526  1.00 67.21  ?  446 GLN A O     1 
ATOM   3339  C  CB    . GLN A  1  414 ? 8.020  -7.834  21.096  1.00 53.65  ?  446 GLN A CB    1 
ATOM   3340  C  CG    . GLN A  1  414 ? 9.180  -7.070  21.682  1.00 54.17  ?  446 GLN A CG    1 
ATOM   3341  C  CD    . GLN A  1  414 ? 9.821  -7.763  22.843  1.00 56.70  ?  446 GLN A CD    1 
ATOM   3342  O  OE1   . GLN A  1  414 ? 10.210 -8.914  22.751  1.00 52.04  ?  446 GLN A OE1   1 
ATOM   3343  N  NE2   . GLN A  1  414 ? 9.967  -7.048  23.933  1.00 56.84  ?  446 GLN A NE2   1 
ATOM   3344  N  N     . LEU A  1  415 ? 6.335  -4.902  20.350  1.00 60.32  ?  447 LEU A N     1 
ATOM   3345  C  CA    . LEU A  1  415 ? 6.168  -3.442  20.524  1.00 59.12  ?  447 LEU A CA    1 
ATOM   3346  C  C     . LEU A  1  415 ? 5.658  -2.531  19.354  1.00 61.70  ?  447 LEU A C     1 
ATOM   3347  O  O     . LEU A  1  415 ? 6.460  -1.863  18.729  1.00 65.82  ?  447 LEU A O     1 
ATOM   3348  C  CB    . LEU A  1  415 ? 7.644  -3.064  20.775  1.00 57.09  ?  447 LEU A CB    1 
ATOM   3349  C  CG    . LEU A  1  415 ? 8.465  -3.457  19.550  1.00 52.72  ?  447 LEU A CG    1 
ATOM   3350  C  CD1   . LEU A  1  415 ? 9.123  -2.233  18.969  1.00 50.41  ?  447 LEU A CD1   1 
ATOM   3351  C  CD2   . LEU A  1  415 ? 9.466  -4.578  19.763  1.00 52.87  ?  447 LEU A CD2   1 
ATOM   3352  N  N     . TYR A  1  416 ? 4.385  -2.399  18.993  1.00 61.64  ?  448 TYR A N     1 
ATOM   3353  C  CA    . TYR A  1  416 ? 3.179  -3.021  19.442  1.00 63.20  ?  448 TYR A CA    1 
ATOM   3354  C  C     . TYR A  1  416 ? 2.394  -3.065  18.110  1.00 68.39  ?  448 TYR A C     1 
ATOM   3355  O  O     . TYR A  1  416 ? 2.832  -2.461  17.152  1.00 68.17  ?  448 TYR A O     1 
ATOM   3356  C  CB    . TYR A  1  416 ? 2.510  -2.107  20.409  1.00 63.75  ?  448 TYR A CB    1 
ATOM   3357  C  CG    . TYR A  1  416 ? 2.672  -2.515  21.837  1.00 66.88  ?  448 TYR A CG    1 
ATOM   3358  C  CD1   . TYR A  1  416 ? 2.203  -3.733  22.294  1.00 68.09  ?  448 TYR A CD1   1 
ATOM   3359  C  CD2   . TYR A  1  416 ? 3.281  -1.686  22.728  1.00 66.84  ?  448 TYR A CD2   1 
ATOM   3360  C  CE1   . TYR A  1  416 ? 2.349  -4.101  23.612  1.00 66.91  ?  448 TYR A CE1   1 
ATOM   3361  C  CE2   . TYR A  1  416 ? 3.430  -2.050  24.033  1.00 65.37  ?  448 TYR A CE2   1 
ATOM   3362  C  CZ    . TYR A  1  416 ? 2.957  -3.250  24.468  1.00 65.36  ?  448 TYR A CZ    1 
ATOM   3363  O  OH    . TYR A  1  416 ? 3.130  -3.568  25.779  1.00 60.95  ?  448 TYR A OH    1 
ATOM   3364  N  N     . ILE A  1  417 ? 1.257  -3.758  18.017  1.00 75.03  ?  449 ILE A N     1 
ATOM   3365  C  CA    . ILE A  1  417 ? 0.510  -3.913  16.703  1.00 74.73  ?  449 ILE A CA    1 
ATOM   3366  C  C     . ILE A  1  417 ? -1.039 -3.964  16.713  1.00 77.10  ?  449 ILE A C     1 
ATOM   3367  O  O     . ILE A  1  417 ? -1.648 -4.504  17.639  1.00 79.16  ?  449 ILE A O     1 
ATOM   3368  C  CB    . ILE A  1  417 ? 1.021  -5.165  15.930  1.00 69.35  ?  449 ILE A CB    1 
ATOM   3369  C  CG1   . ILE A  1  417 ? 2.523  -5.049  15.745  1.00 67.40  ?  449 ILE A CG1   1 
ATOM   3370  C  CG2   . ILE A  1  417 ? 0.336  -5.337  14.568  1.00 67.31  ?  449 ILE A CG2   1 
ATOM   3371  C  CD1   . ILE A  1  417 ? 2.970  -3.746  15.094  1.00 66.38  ?  449 ILE A CD1   1 
ATOM   3372  N  N     . LYS A  1  418 ? -1.652 -3.417  15.651  1.00 74.01  ?  450 LYS A N     1 
ATOM   3373  C  CA    . LYS A  1  418 ? -3.106 -3.451  15.451  1.00 69.79  ?  450 LYS A CA    1 
ATOM   3374  C  C     . LYS A  1  418 ? -3.740 -4.745  15.976  1.00 74.24  ?  450 LYS A C     1 
ATOM   3375  O  O     . LYS A  1  418 ? -4.091 -4.841  17.164  1.00 69.62  ?  450 LYS A O     1 
ATOM   3376  C  CB    . LYS A  1  418 ? -3.455 -3.237  13.966  1.00 63.17  ?  450 LYS A CB    1 
ATOM   3377  C  CG    . LYS A  1  418 ? -3.835 -1.798  13.649  1.00 58.31  ?  450 LYS A CG    1 
ATOM   3378  C  CD    . LYS A  1  418 ? -5.307 -1.510  13.962  1.00 54.78  ?  450 LYS A CD    1 
ATOM   3379  C  CE    . LYS A  1  418 ? -5.558 -0.089  14.484  1.00 51.29  ?  450 LYS A CE    1 
ATOM   3380  N  NZ    . LYS A  1  418 ? -6.683 0.623   13.795  1.00 48.32  1  450 LYS A NZ    1 
ATOM   3381  N  N     . PRO B  2  1   ? 60.418 2.716   15.954  1.00 121.00 ?  33  PRO B N     1 
ATOM   3382  C  CA    . PRO B  2  1   ? 59.397 1.915   15.264  1.00 119.93 ?  33  PRO B CA    1 
ATOM   3383  C  C     . PRO B  2  1   ? 59.601 1.966   13.741  1.00 119.47 ?  33  PRO B C     1 
ATOM   3384  O  O     . PRO B  2  1   ? 60.235 2.910   13.263  1.00 114.10 ?  33  PRO B O     1 
ATOM   3385  C  CB    . PRO B  2  1   ? 58.075 2.586   15.680  1.00 118.52 ?  33  PRO B CB    1 
ATOM   3386  C  CG    . PRO B  2  1   ? 58.404 3.399   16.897  1.00 118.67 ?  33  PRO B CG    1 
ATOM   3387  C  CD    . PRO B  2  1   ? 59.833 3.826   16.726  1.00 119.55 ?  33  PRO B CD    1 
ATOM   3388  N  N     . PRO B  2  2   ? 59.069 0.994   13.008  1.00 120.28 ?  34  PRO B N     1 
ATOM   3389  C  CA    . PRO B  2  2   ? 59.206 0.960   11.552  1.00 116.78 ?  34  PRO B CA    1 
ATOM   3390  C  C     . PRO B  2  2   ? 58.463 2.091   10.886  1.00 110.14 ?  34  PRO B C     1 
ATOM   3391  O  O     . PRO B  2  2   ? 57.416 2.481   11.387  1.00 110.34 ?  34  PRO B O     1 
ATOM   3392  C  CB    . PRO B  2  2   ? 58.537 -0.351  11.177  1.00 113.92 ?  34  PRO B CB    1 
ATOM   3393  C  CG    . PRO B  2  2   ? 57.615 -0.670  12.312  1.00 114.72 ?  34  PRO B CG    1 
ATOM   3394  C  CD    . PRO B  2  2   ? 57.877 0.269   13.452  1.00 116.93 ?  34  PRO B CD    1 
ATOM   3395  N  N     . PRO B  2  3   ? 58.961 2.614   9.774   1.00 102.21 ?  35  PRO B N     1 
ATOM   3396  C  CA    . PRO B  2  3   ? 58.275 3.723   9.100   1.00 94.53  ?  35  PRO B CA    1 
ATOM   3397  C  C     . PRO B  2  3   ? 57.669 3.402   7.743   1.00 88.24  ?  35  PRO B C     1 
ATOM   3398  O  O     . PRO B  2  3   ? 56.722 4.027   7.301   1.00 75.33  ?  35  PRO B O     1 
ATOM   3399  C  CB    . PRO B  2  3   ? 59.404 4.704   8.846   1.00 94.69  ?  35  PRO B CB    1 
ATOM   3400  C  CG    . PRO B  2  3   ? 60.608 3.854   8.774   1.00 98.45  ?  35  PRO B CG    1 
ATOM   3401  C  CD    . PRO B  2  3   ? 60.402 2.863   9.865   1.00 102.03 ?  35  PRO B CD    1 
ATOM   3402  N  N     . ALA B  2  4   ? 58.246 2.419   7.086   1.00 87.40  ?  36  ALA B N     1 
ATOM   3403  C  CA    . ALA B  2  4   ? 57.799 1.995   5.781   1.00 82.77  ?  36  ALA B CA    1 
ATOM   3404  C  C     . ALA B  2  4   ? 58.186 0.561   5.744   1.00 81.29  ?  36  ALA B C     1 
ATOM   3405  O  O     . ALA B  2  4   ? 59.225 0.207   6.244   1.00 80.70  ?  36  ALA B O     1 
ATOM   3406  C  CB    . ALA B  2  4   ? 58.492 2.737   4.667   1.00 81.23  ?  36  ALA B CB    1 
ATOM   3407  N  N     . ILE B  2  5   ? 57.362 -0.285  5.155   1.00 76.46  ?  37  ILE B N     1 
ATOM   3408  C  CA    . ILE B  2  5   ? 57.711 -1.718  5.128   1.00 66.94  ?  37  ILE B CA    1 
ATOM   3409  C  C     . ILE B  2  5   ? 58.256 -2.107  3.743   1.00 64.33  ?  37  ILE B C     1 
ATOM   3410  O  O     . ILE B  2  5   ? 57.553 -2.002  2.739   1.00 62.91  ?  37  ILE B O     1 
ATOM   3411  C  CB    . ILE B  2  5   ? 56.490 -2.612  5.475   1.00 58.26  ?  37  ILE B CB    1 
ATOM   3412  C  CG1   . ILE B  2  5   ? 56.004 -2.357  6.906   1.00 54.46  ?  37  ILE B CG1   1 
ATOM   3413  C  CG2   . ILE B  2  5   ? 56.828 -4.086  5.297   1.00 56.88  ?  37  ILE B CG2   1 
ATOM   3414  C  CD1   . ILE B  2  5   ? 56.999 -2.703  7.995   1.00 53.37  ?  37  ILE B CD1   1 
ATOM   3415  N  N     . GLY B  2  6   ? 59.509 -2.548  3.696   1.00 62.21  ?  38  GLY B N     1 
ATOM   3416  C  CA    . GLY B  2  6   ? 60.089 -3.104  2.464   1.00 61.28  ?  38  GLY B CA    1 
ATOM   3417  C  C     . GLY B  2  6   ? 59.686 -4.558  2.301   1.00 56.25  ?  38  GLY B C     1 
ATOM   3418  O  O     . GLY B  2  6   ? 59.438 -5.228  3.295   1.00 57.85  ?  38  GLY B O     1 
ATOM   3419  N  N     . GLN B  2  7   ? 59.618 -5.053  1.068   1.00 50.46  ?  39  GLN B N     1 
ATOM   3420  C  CA    . GLN B  2  7   ? 59.126 -6.413  0.824   1.00 48.52  ?  39  GLN B CA    1 
ATOM   3421  C  C     . GLN B  2  7   ? 59.845 -7.098  -0.329  1.00 49.78  ?  39  GLN B C     1 
ATOM   3422  O  O     . GLN B  2  7   ? 60.145 -6.466  -1.333  1.00 59.11  ?  39  GLN B O     1 
ATOM   3423  C  CB    . GLN B  2  7   ? 57.612 -6.391  0.545   1.00 45.16  ?  39  GLN B CB    1 
ATOM   3424  C  CG    . GLN B  2  7   ? 56.743 -6.104  1.772   1.00 42.48  ?  39  GLN B CG    1 
ATOM   3425  C  CD    . GLN B  2  7   ? 55.375 -6.759  1.716   1.00 38.79  ?  39  GLN B CD    1 
ATOM   3426  O  OE1   . GLN B  2  7   ? 54.844 -7.001  0.650   1.00 39.24  ?  39  GLN B OE1   1 
ATOM   3427  N  NE2   . GLN B  2  7   ? 54.805 -7.043  2.867   1.00 37.04  ?  39  GLN B NE2   1 
ATOM   3428  N  N     . PHE B  2  8   ? 60.133 -8.388  -0.209  1.00 46.91  ?  40  PHE B N     1 
ATOM   3429  C  CA    . PHE B  2  8   ? 60.612 -9.110  -1.385  1.00 42.68  ?  40  PHE B CA    1 
ATOM   3430  C  C     . PHE B  2  8   ? 60.254 -10.572 -1.358  1.00 37.91  ?  40  PHE B C     1 
ATOM   3431  O  O     . PHE B  2  8   ? 59.977 -11.136 -0.315  1.00 36.67  ?  40  PHE B O     1 
ATOM   3432  C  CB    . PHE B  2  8   ? 62.112 -8.886  -1.629  1.00 42.36  ?  40  PHE B CB    1 
ATOM   3433  C  CG    . PHE B  2  8   ? 63.003 -9.353  -0.518  1.00 42.41  ?  40  PHE B CG    1 
ATOM   3434  C  CD1   . PHE B  2  8   ? 63.431 -8.468  0.460   1.00 42.01  ?  40  PHE B CD1   1 
ATOM   3435  C  CD2   . PHE B  2  8   ? 63.458 -10.668 -0.481  1.00 42.43  ?  40  PHE B CD2   1 
ATOM   3436  C  CE1   . PHE B  2  8   ? 64.278 -8.890  1.472   1.00 43.35  ?  40  PHE B CE1   1 
ATOM   3437  C  CE2   . PHE B  2  8   ? 64.299 -11.105 0.535   1.00 44.03  ?  40  PHE B CE2   1 
ATOM   3438  C  CZ    . PHE B  2  8   ? 64.711 -10.213 1.517   1.00 44.76  ?  40  PHE B CZ    1 
ATOM   3439  N  N     . TRP B  2  9   ? 60.219 -11.159 -2.543  1.00 36.17  ?  41  TRP B N     1 
ATOM   3440  C  CA    . TRP B  2  9   ? 59.822 -12.542 -2.704  1.00 35.91  ?  41  TRP B CA    1 
ATOM   3441  C  C     . TRP B  2  9   ? 61.055 -13.358 -2.799  1.00 35.79  ?  41  TRP B C     1 
ATOM   3442  O  O     . TRP B  2  9   ? 62.097 -12.871 -3.290  1.00 36.58  ?  41  TRP B O     1 
ATOM   3443  C  CB    . TRP B  2  9   ? 59.052 -12.752 -4.001  1.00 36.46  ?  41  TRP B CB    1 
ATOM   3444  C  CG    . TRP B  2  9   ? 57.729 -12.145 -3.976  1.00 36.08  ?  41  TRP B CG    1 
ATOM   3445  C  CD1   . TRP B  2  9   ? 57.375 -10.905 -4.430  1.00 36.10  ?  41  TRP B CD1   1 
ATOM   3446  C  CD2   . TRP B  2  9   ? 56.560 -12.731 -3.446  1.00 34.32  ?  41  TRP B CD2   1 
ATOM   3447  N  NE1   . TRP B  2  9   ? 56.040 -10.689 -4.210  1.00 34.97  ?  41  TRP B NE1   1 
ATOM   3448  C  CE2   . TRP B  2  9   ? 55.513 -11.798 -3.612  1.00 33.89  ?  41  TRP B CE2   1 
ATOM   3449  C  CE3   . TRP B  2  9   ? 56.290 -13.956 -2.855  1.00 33.52  ?  41  TRP B CE3   1 
ATOM   3450  C  CZ2   . TRP B  2  9   ? 54.224 -12.053 -3.211  1.00 35.04  ?  41  TRP B CZ2   1 
ATOM   3451  C  CZ3   . TRP B  2  9   ? 55.007 -14.212 -2.449  1.00 35.80  ?  41  TRP B CZ3   1 
ATOM   3452  C  CH2   . TRP B  2  9   ? 53.982 -13.263 -2.625  1.00 36.19  ?  41  TRP B CH2   1 
ATOM   3453  N  N     . HIS B  2  10  ? 60.926 -14.608 -2.360  1.00 32.55  ?  42  HIS B N     1 
ATOM   3454  C  CA    . HIS B  2  10  ? 61.940 -15.623 -2.610  1.00 30.01  ?  42  HIS B CA    1 
ATOM   3455  C  C     . HIS B  2  10  ? 61.201 -16.717 -3.307  1.00 26.81  ?  42  HIS B C     1 
ATOM   3456  O  O     . HIS B  2  10  ? 60.162 -17.149 -2.832  1.00 25.88  ?  42  HIS B O     1 
ATOM   3457  C  CB    . HIS B  2  10  ? 62.549 -16.145 -1.310  1.00 31.28  ?  42  HIS B CB    1 
ATOM   3458  C  CG    . HIS B  2  10  ? 63.807 -16.938 -1.493  1.00 32.89  ?  42  HIS B CG    1 
ATOM   3459  N  ND1   . HIS B  2  10  ? 64.886 -16.824 -0.645  1.00 34.84  ?  42  HIS B ND1   1 
ATOM   3460  C  CD2   . HIS B  2  10  ? 64.162 -17.855 -2.422  1.00 34.49  ?  42  HIS B CD2   1 
ATOM   3461  C  CE1   . HIS B  2  10  ? 65.851 -17.635 -1.044  1.00 34.95  ?  42  HIS B CE1   1 
ATOM   3462  N  NE2   . HIS B  2  10  ? 65.438 -18.272 -2.120  1.00 33.76  ?  42  HIS B NE2   1 
ATOM   3463  N  N     . VAL B  2  11  ? 61.710 -17.110 -4.469  1.00 25.47  ?  43  VAL B N     1 
ATOM   3464  C  CA    . VAL B  2  11  ? 61.241 -18.300 -5.195  1.00 23.27  ?  43  VAL B CA    1 
ATOM   3465  C  C     . VAL B  2  11  ? 62.463 -19.145 -5.396  1.00 23.28  ?  43  VAL B C     1 
ATOM   3466  O  O     . VAL B  2  11  ? 63.523 -18.624 -5.775  1.00 23.20  ?  43  VAL B O     1 
ATOM   3467  C  CB    . VAL B  2  11  ? 60.591 -17.969 -6.556  1.00 21.26  ?  43  VAL B CB    1 
ATOM   3468  C  CG1   . VAL B  2  11  ? 59.400 -17.074 -6.368  1.00 21.52  ?  43  VAL B CG1   1 
ATOM   3469  C  CG2   . VAL B  2  11  ? 61.556 -17.285 -7.489  1.00 21.21  ?  43  VAL B CG2   1 
ATOM   3470  N  N     . THR B  2  12  ? 62.367 -20.436 -5.125  1.00 24.10  ?  44  THR B N     1 
ATOM   3471  C  CA    . THR B  2  12  ? 63.498 -21.272 -5.473  1.00 26.17  ?  44  THR B CA    1 
ATOM   3472  C  C     . THR B  2  12  ? 63.113 -22.609 -6.040  1.00 28.97  ?  44  THR B C     1 
ATOM   3473  O  O     . THR B  2  12  ? 61.983 -23.072 -5.840  1.00 30.44  ?  44  THR B O     1 
ATOM   3474  C  CB    . THR B  2  12  ? 64.459 -21.451 -4.298  1.00 25.66  ?  44  THR B CB    1 
ATOM   3475  O  OG1   . THR B  2  12  ? 65.694 -21.986 -4.799  1.00 26.77  ?  44  THR B OG1   1 
ATOM   3476  C  CG2   . THR B  2  12  ? 63.866 -22.344 -3.184  1.00 25.60  ?  44  THR B CG2   1 
ATOM   3477  N  N     . ASP B  2  13  ? 64.067 -23.210 -6.757  1.00 31.36  ?  45  ASP B N     1 
ATOM   3478  C  CA    . ASP B  2  13  ? 63.961 -24.592 -7.180  1.00 32.77  ?  45  ASP B CA    1 
ATOM   3479  C  C     . ASP B  2  13  ? 62.637 -24.758 -7.864  1.00 34.16  ?  45  ASP B C     1 
ATOM   3480  O  O     . ASP B  2  13  ? 61.701 -25.309 -7.300  1.00 37.17  ?  45  ASP B O     1 
ATOM   3481  C  CB    . ASP B  2  13  ? 64.056 -25.520 -5.977  1.00 33.20  ?  45  ASP B CB    1 
ATOM   3482  C  CG    . ASP B  2  13  ? 65.362 -25.380 -5.264  1.00 37.53  ?  45  ASP B CG    1 
ATOM   3483  O  OD1   . ASP B  2  13  ? 65.452 -24.614 -4.285  1.00 41.07  ?  45  ASP B OD1   1 
ATOM   3484  O  OD2   . ASP B  2  13  ? 66.329 -26.024 -5.694  1.00 42.65  -1 45  ASP B OD2   1 
ATOM   3485  N  N     . LEU B  2  14  ? 62.544 -24.249 -9.075  1.00 33.52  ?  46  LEU B N     1 
ATOM   3486  C  CA    . LEU B  2  14  ? 61.316 -24.351 -9.812  1.00 33.96  ?  46  LEU B CA    1 
ATOM   3487  C  C     . LEU B  2  14  ? 61.246 -25.694 -10.472 1.00 34.10  ?  46  LEU B C     1 
ATOM   3488  O  O     . LEU B  2  14  ? 60.165 -26.250 -10.639 1.00 35.67  ?  46  LEU B O     1 
ATOM   3489  C  CB    . LEU B  2  14  ? 61.276 -23.269 -10.852 1.00 37.86  ?  46  LEU B CB    1 
ATOM   3490  C  CG    . LEU B  2  14  ? 61.446 -21.890 -10.222 1.00 41.26  ?  46  LEU B CG    1 
ATOM   3491  C  CD1   . LEU B  2  14  ? 61.564 -20.851 -11.312 1.00 42.75  ?  46  LEU B CD1   1 
ATOM   3492  C  CD2   . LEU B  2  14  ? 60.279 -21.584 -9.288  1.00 41.41  ?  46  LEU B CD2   1 
ATOM   3493  N  N     . HIS B  2  15  ? 62.414 -26.209 -10.857 1.00 34.17  ?  47  HIS B N     1 
ATOM   3494  C  CA    . HIS B  2  15  ? 62.565 -27.573 -11.373 1.00 33.35  ?  47  HIS B CA    1 
ATOM   3495  C  C     . HIS B  2  15  ? 61.414 -27.931 -12.314 1.00 36.37  ?  47  HIS B C     1 
ATOM   3496  O  O     . HIS B  2  15  ? 60.547 -28.762 -11.977 1.00 36.24  ?  47  HIS B O     1 
ATOM   3497  C  CB    . HIS B  2  15  ? 62.695 -28.589 -10.222 1.00 29.82  ?  47  HIS B CB    1 
ATOM   3498  C  CG    . HIS B  2  15  ? 64.061 -28.642 -9.615  1.00 26.49  ?  47  HIS B CG    1 
ATOM   3499  N  ND1   . HIS B  2  15  ? 65.207 -28.678 -10.373 1.00 26.83  ?  47  HIS B ND1   1 
ATOM   3500  C  CD2   . HIS B  2  15  ? 64.470 -28.670 -8.331  1.00 24.77  ?  47  HIS B CD2   1 
ATOM   3501  C  CE1   . HIS B  2  15  ? 66.260 -28.720 -9.585  1.00 24.76  ?  47  HIS B CE1   1 
ATOM   3502  N  NE2   . HIS B  2  15  ? 65.838 -28.724 -8.340  1.00 23.87  ?  47  HIS B NE2   1 
ATOM   3503  N  N     . LEU B  2  16  ? 61.409 -27.266 -13.477 1.00 36.67  ?  48  LEU B N     1 
ATOM   3504  C  CA    . LEU B  2  16  ? 60.400 -27.501 -14.523 1.00 34.95  ?  48  LEU B CA    1 
ATOM   3505  C  C     . LEU B  2  16  ? 60.628 -28.817 -15.258 1.00 31.55  ?  48  LEU B C     1 
ATOM   3506  O  O     . LEU B  2  16  ? 61.732 -29.124 -15.684 1.00 28.36  ?  48  LEU B O     1 
ATOM   3507  C  CB    . LEU B  2  16  ? 60.390 -26.366 -15.560 1.00 34.93  ?  48  LEU B CB    1 
ATOM   3508  C  CG    . LEU B  2  16  ? 59.413 -26.582 -16.730 1.00 33.88  ?  48  LEU B CG    1 
ATOM   3509  C  CD1   . LEU B  2  16  ? 58.004 -26.156 -16.318 1.00 33.28  ?  48  LEU B CD1   1 
ATOM   3510  C  CD2   . LEU B  2  16  ? 59.898 -25.854 -17.982 1.00 34.00  ?  48  LEU B CD2   1 
ATOM   3511  N  N     . ASP B  2  17  ? 59.543 -29.553 -15.426 1.00 31.12  ?  49  ASP B N     1 
ATOM   3512  C  CA    . ASP B  2  17  ? 59.525 -30.761 -16.218 1.00 31.71  ?  49  ASP B CA    1 
ATOM   3513  C  C     . ASP B  2  17  ? 58.644 -30.468 -17.437 1.00 30.69  ?  49  ASP B C     1 
ATOM   3514  O  O     . ASP B  2  17  ? 57.410 -30.490 -17.300 1.00 27.60  ?  49  ASP B O     1 
ATOM   3515  C  CB    . ASP B  2  17  ? 58.947 -31.920 -15.381 1.00 31.76  ?  49  ASP B CB    1 
ATOM   3516  C  CG    . ASP B  2  17  ? 59.448 -33.283 -15.829 1.00 30.17  ?  49  ASP B CG    1 
ATOM   3517  O  OD1   . ASP B  2  17  ? 59.840 -33.438 -17.006 1.00 27.74  ?  49  ASP B OD1   1 
ATOM   3518  O  OD2   . ASP B  2  17  ? 59.420 -34.199 -14.986 1.00 28.38  -1 49  ASP B OD2   1 
ATOM   3519  N  N     . PRO B  2  18  ? 59.279 -30.138 -18.610 1.00 31.46  ?  50  PRO B N     1 
ATOM   3520  C  CA    . PRO B  2  18  ? 58.619 -29.964 -19.915 1.00 30.04  ?  50  PRO B CA    1 
ATOM   3521  C  C     . PRO B  2  18  ? 57.784 -31.166 -20.327 1.00 29.49  ?  50  PRO B C     1 
ATOM   3522  O  O     . PRO B  2  18  ? 56.789 -30.995 -21.013 1.00 30.32  ?  50  PRO B O     1 
ATOM   3523  C  CB    . PRO B  2  18  ? 59.791 -29.791 -20.877 1.00 29.08  ?  50  PRO B CB    1 
ATOM   3524  C  CG    . PRO B  2  18  ? 60.849 -29.138 -20.074 1.00 29.16  ?  50  PRO B CG    1 
ATOM   3525  C  CD    . PRO B  2  18  ? 60.710 -29.764 -18.709 1.00 31.20  ?  50  PRO B CD    1 
ATOM   3526  N  N     . THR B  2  19  ? 58.170 -32.355 -19.886 1.00 27.55  ?  51  THR B N     1 
ATOM   3527  C  CA    . THR B  2  19  ? 57.425 -33.555 -20.158 1.00 28.27  ?  51  THR B CA    1 
ATOM   3528  C  C     . THR B  2  19  ? 56.049 -33.698 -19.576 1.00 31.34  ?  51  THR B C     1 
ATOM   3529  O  O     . THR B  2  19  ? 55.222 -34.414 -20.139 1.00 33.28  ?  51  THR B O     1 
ATOM   3530  C  CB    . THR B  2  19  ? 58.124 -34.708 -19.505 1.00 28.64  ?  51  THR B CB    1 
ATOM   3531  O  OG1   . THR B  2  19  ? 59.497 -34.590 -19.824 1.00 28.95  ?  51  THR B OG1   1 
ATOM   3532  C  CG2   . THR B  2  19  ? 57.526 -36.086 -19.981 1.00 29.38  ?  51  THR B CG2   1 
ATOM   3533  N  N     . TYR B  2  20  ? 55.825 -33.130 -18.399 1.00 34.01  ?  52  TYR B N     1 
ATOM   3534  C  CA    . TYR B  2  20  ? 54.643 -33.494 -17.599 1.00 35.47  ?  52  TYR B CA    1 
ATOM   3535  C  C     . TYR B  2  20  ? 53.399 -33.410 -18.433 1.00 34.57  ?  52  TYR B C     1 
ATOM   3536  O  O     . TYR B  2  20  ? 53.234 -32.465 -19.175 1.00 31.68  ?  52  TYR B O     1 
ATOM   3537  C  CB    . TYR B  2  20  ? 54.481 -32.571 -16.363 1.00 38.11  ?  52  TYR B CB    1 
ATOM   3538  C  CG    . TYR B  2  20  ? 53.436 -33.035 -15.355 1.00 37.86  ?  52  TYR B CG    1 
ATOM   3539  C  CD1   . TYR B  2  20  ? 52.135 -32.574 -15.412 1.00 37.22  ?  52  TYR B CD1   1 
ATOM   3540  C  CD2   . TYR B  2  20  ? 53.762 -33.950 -14.356 1.00 40.76  ?  52  TYR B CD2   1 
ATOM   3541  C  CE1   . TYR B  2  20  ? 51.183 -33.000 -14.503 1.00 39.05  ?  52  TYR B CE1   1 
ATOM   3542  C  CE2   . TYR B  2  20  ? 52.815 -34.401 -13.447 1.00 40.76  ?  52  TYR B CE2   1 
ATOM   3543  C  CZ    . TYR B  2  20  ? 51.522 -33.921 -13.527 1.00 39.84  ?  52  TYR B CZ    1 
ATOM   3544  O  OH    . TYR B  2  20  ? 50.578 -34.346 -12.623 1.00 38.81  ?  52  TYR B OH    1 
ATOM   3545  N  N     . HIS B  2  21  ? 52.537 -34.400 -18.316 1.00 38.84  ?  53  HIS B N     1 
ATOM   3546  C  CA    . HIS B  2  21  ? 51.162 -34.258 -18.758 1.00 48.10  ?  53  HIS B CA    1 
ATOM   3547  C  C     . HIS B  2  21  ? 50.359 -35.469 -18.318 1.00 46.98  ?  53  HIS B C     1 
ATOM   3548  O  O     . HIS B  2  21  ? 50.869 -36.589 -18.252 1.00 43.30  ?  53  HIS B O     1 
ATOM   3549  C  CB    . HIS B  2  21  ? 51.051 -34.074 -20.289 1.00 58.83  ?  53  HIS B CB    1 
ATOM   3550  C  CG    . HIS B  2  21  ? 51.407 -35.297 -21.070 1.00 67.56  ?  53  HIS B CG    1 
ATOM   3551  N  ND1   . HIS B  2  21  ? 52.712 -35.690 -21.283 1.00 74.65  ?  53  HIS B ND1   1 
ATOM   3552  C  CD2   . HIS B  2  21  ? 50.629 -36.235 -21.658 1.00 72.71  ?  53  HIS B CD2   1 
ATOM   3553  C  CE1   . HIS B  2  21  ? 52.723 -36.813 -21.978 1.00 77.48  ?  53  HIS B CE1   1 
ATOM   3554  N  NE2   . HIS B  2  21  ? 51.472 -37.164 -22.218 1.00 79.27  ?  53  HIS B NE2   1 
ATOM   3555  N  N     . ILE B  2  22  ? 49.086 -35.244 -18.027 1.00 49.35  ?  54  ILE B N     1 
ATOM   3556  C  CA    . ILE B  2  22  ? 48.212 -36.341 -17.654 1.00 49.17  ?  54  ILE B CA    1 
ATOM   3557  C  C     . ILE B  2  22  ? 48.022 -37.264 -18.839 1.00 49.60  ?  54  ILE B C     1 
ATOM   3558  O  O     . ILE B  2  22  ? 47.781 -36.845 -19.982 1.00 44.24  ?  54  ILE B O     1 
ATOM   3559  C  CB    . ILE B  2  22  ? 46.825 -35.886 -17.158 1.00 49.24  ?  54  ILE B CB    1 
ATOM   3560  C  CG1   . ILE B  2  22  ? 46.969 -34.866 -16.025 1.00 47.64  ?  54  ILE B CG1   1 
ATOM   3561  C  CG2   . ILE B  2  22  ? 46.006 -37.098 -16.703 1.00 50.86  ?  54  ILE B CG2   1 
ATOM   3562  C  CD1   . ILE B  2  22  ? 47.827 -35.346 -14.882 1.00 47.98  ?  54  ILE B CD1   1 
ATOM   3563  N  N     . THR B  2  23  ? 48.169 -38.538 -18.527 1.00 53.19  ?  55  THR B N     1 
ATOM   3564  C  CA    . THR B  2  23  ? 47.813 -39.604 -19.430 1.00 55.61  ?  55  THR B CA    1 
ATOM   3565  C  C     . THR B  2  23  ? 47.519 -40.814 -18.524 1.00 55.88  ?  55  THR B C     1 
ATOM   3566  O  O     . THR B  2  23  ? 47.848 -40.824 -17.314 1.00 50.87  ?  55  THR B O     1 
ATOM   3567  C  CB    . THR B  2  23  ? 48.914 -39.849 -20.511 1.00 56.33  ?  55  THR B CB    1 
ATOM   3568  O  OG1   . THR B  2  23  ? 48.431 -40.728 -21.547 1.00 56.39  ?  55  THR B OG1   1 
ATOM   3569  C  CG2   . THR B  2  23  ? 50.188 -40.438 -19.889 1.00 58.17  ?  55  THR B CG2   1 
ATOM   3570  N  N     . ASP B  2  24  ? 46.867 -41.807 -19.117 1.00 57.11  ?  56  ASP B N     1 
ATOM   3571  C  CA    . ASP B  2  24  ? 46.389 -42.975 -18.386 1.00 58.91  ?  56  ASP B CA    1 
ATOM   3572  C  C     . ASP B  2  24  ? 47.508 -43.926 -17.958 1.00 57.80  ?  56  ASP B C     1 
ATOM   3573  O  O     . ASP B  2  24  ? 47.353 -44.660 -16.985 1.00 53.82  ?  56  ASP B O     1 
ATOM   3574  C  CB    . ASP B  2  24  ? 45.329 -43.688 -19.221 1.00 58.77  ?  56  ASP B CB    1 
ATOM   3575  C  CG    . ASP B  2  24  ? 44.090 -42.834 -19.396 1.00 61.00  ?  56  ASP B CG    1 
ATOM   3576  O  OD1   . ASP B  2  24  ? 43.423 -42.541 -18.379 1.00 58.22  ?  56  ASP B OD1   1 
ATOM   3577  O  OD2   . ASP B  2  24  ? 43.805 -42.420 -20.539 1.00 65.53  -1 56  ASP B OD2   1 
ATOM   3578  N  N     . ASP B  2  25  ? 48.619 -43.905 -18.696 1.00 58.91  ?  57  ASP B N     1 
ATOM   3579  C  CA    . ASP B  2  25  ? 49.848 -44.603 -18.318 1.00 56.61  ?  57  ASP B CA    1 
ATOM   3580  C  C     . ASP B  2  25  ? 50.646 -43.678 -17.372 1.00 56.14  ?  57  ASP B C     1 
ATOM   3581  O  O     . ASP B  2  25  ? 51.210 -42.632 -17.775 1.00 51.72  ?  57  ASP B O     1 
ATOM   3582  C  CB    . ASP B  2  25  ? 50.645 -44.980 -19.582 1.00 57.19  ?  57  ASP B CB    1 
ATOM   3583  C  CG    . ASP B  2  25  ? 51.709 -46.045 -19.336 1.00 56.91  ?  57  ASP B CG    1 
ATOM   3584  O  OD1   . ASP B  2  25  ? 51.878 -46.507 -18.182 1.00 52.57  ?  57  ASP B OD1   1 
ATOM   3585  O  OD2   . ASP B  2  25  ? 52.386 -46.415 -20.326 1.00 58.40  -1 57  ASP B OD2   1 
ATOM   3586  N  N     . HIS B  2  26  ? 50.667 -44.075 -16.100 1.00 54.81  ?  58  HIS B N     1 
ATOM   3587  C  CA    . HIS B  2  26  ? 51.273 -43.275 -15.037 1.00 52.72  ?  58  HIS B CA    1 
ATOM   3588  C  C     . HIS B  2  26  ? 52.791 -43.364 -15.021 1.00 48.22  ?  58  HIS B C     1 
ATOM   3589  O  O     . HIS B  2  26  ? 53.436 -42.552 -14.363 1.00 46.08  ?  58  HIS B O     1 
ATOM   3590  C  CB    . HIS B  2  26  ? 50.666 -43.651 -13.672 1.00 51.89  ?  58  HIS B CB    1 
ATOM   3591  C  CG    . HIS B  2  26  ? 49.342 -43.004 -13.408 1.00 50.31  ?  58  HIS B CG    1 
ATOM   3592  N  ND1   . HIS B  2  26  ? 48.646 -42.304 -14.376 1.00 49.55  ?  58  HIS B ND1   1 
ATOM   3593  C  CD2   . HIS B  2  26  ? 48.585 -42.953 -12.288 1.00 49.95  ?  58  HIS B CD2   1 
ATOM   3594  C  CE1   . HIS B  2  26  ? 47.520 -41.849 -13.861 1.00 50.79  ?  58  HIS B CE1   1 
ATOM   3595  N  NE2   . HIS B  2  26  ? 47.464 -42.221 -12.593 1.00 52.18  ?  58  HIS B NE2   1 
ATOM   3596  N  N     . THR B  2  27  ? 53.349 -44.336 -15.749 1.00 46.00  ?  59  THR B N     1 
ATOM   3597  C  CA    . THR B  2  27  ? 54.794 -44.383 -15.997 1.00 44.47  ?  59  THR B CA    1 
ATOM   3598  C  C     . THR B  2  27  ? 55.175 -43.301 -17.008 1.00 43.58  ?  59  THR B C     1 
ATOM   3599  O  O     . THR B  2  27  ? 56.353 -42.977 -17.129 1.00 44.07  ?  59  THR B O     1 
ATOM   3600  C  CB    . THR B  2  27  ? 55.310 -45.752 -16.534 1.00 43.79  ?  59  THR B CB    1 
ATOM   3601  O  OG1   . THR B  2  27  ? 55.093 -45.849 -17.951 1.00 43.25  ?  59  THR B OG1   1 
ATOM   3602  C  CG2   . THR B  2  27  ? 54.668 -46.960 -15.801 1.00 43.76  ?  59  THR B CG2   1 
ATOM   3603  N  N     . LYS B  2  28  ? 54.182 -42.740 -17.710 1.00 41.80  ?  60  LYS B N     1 
ATOM   3604  C  CA    . LYS B  2  28  ? 54.423 -41.868 -18.851 1.00 40.69  ?  60  LYS B CA    1 
ATOM   3605  C  C     . LYS B  2  28  ? 54.055 -40.401 -18.619 1.00 42.04  ?  60  LYS B C     1 
ATOM   3606  O  O     . LYS B  2  28  ? 54.354 -39.530 -19.449 1.00 43.94  ?  60  LYS B O     1 
ATOM   3607  C  CB    . LYS B  2  28  ? 53.690 -42.439 -20.071 1.00 40.24  ?  60  LYS B CB    1 
ATOM   3608  C  CG    . LYS B  2  28  ? 54.198 -43.801 -20.528 1.00 39.78  ?  60  LYS B CG    1 
ATOM   3609  C  CD    . LYS B  2  28  ? 55.674 -43.718 -20.871 1.00 42.60  ?  60  LYS B CD    1 
ATOM   3610  C  CE    . LYS B  2  28  ? 56.321 -45.076 -21.006 1.00 44.71  ?  60  LYS B CE    1 
ATOM   3611  N  NZ    . LYS B  2  28  ? 56.126 -45.545 -22.401 1.00 47.60  1  60  LYS B NZ    1 
ATOM   3612  N  N     . VAL B  2  29  ? 53.449 -40.120 -17.471 1.00 41.62  ?  61  VAL B N     1 
ATOM   3613  C  CA    . VAL B  2  29  ? 53.037 -38.751 -17.098 1.00 39.64  ?  61  VAL B CA    1 
ATOM   3614  C  C     . VAL B  2  29  ? 54.167 -37.674 -17.072 1.00 40.05  ?  61  VAL B C     1 
ATOM   3615  O  O     . VAL B  2  29  ? 53.932 -36.496 -17.360 1.00 44.27  ?  61  VAL B O     1 
ATOM   3616  C  CB    . VAL B  2  29  ? 52.288 -38.815 -15.747 1.00 37.11  ?  61  VAL B CB    1 
ATOM   3617  C  CG1   . VAL B  2  29  ? 52.262 -37.474 -15.015 1.00 36.85  ?  61  VAL B CG1   1 
ATOM   3618  C  CG2   . VAL B  2  29  ? 50.897 -39.358 -15.980 1.00 37.38  ?  61  VAL B CG2   1 
ATOM   3619  N  N     . CYS B  2  30  ? 55.383 -38.049 -16.728 1.00 36.15  ?  62  CYS B N     1 
ATOM   3620  C  CA    . CYS B  2  30  ? 56.417 -37.052 -16.597 1.00 34.91  ?  62  CYS B CA    1 
ATOM   3621  C  C     . CYS B  2  30  ? 57.695 -37.817 -16.478 1.00 34.47  ?  62  CYS B C     1 
ATOM   3622  O  O     . CYS B  2  30  ? 57.732 -38.850 -15.788 1.00 36.14  ?  62  CYS B O     1 
ATOM   3623  C  CB    . CYS B  2  30  ? 56.206 -36.247 -15.330 1.00 35.18  ?  62  CYS B CB    1 
ATOM   3624  S  SG    . CYS B  2  30  ? 56.962 -37.017 -13.868 1.00 38.64  ?  62  CYS B SG    1 
ATOM   3625  N  N     . ALA B  2  31  ? 58.747 -37.332 -17.125 1.00 31.56  ?  63  ALA B N     1 
ATOM   3626  C  CA    . ALA B  2  31  ? 60.012 -38.054 -17.117 1.00 30.36  ?  63  ALA B CA    1 
ATOM   3627  C  C     . ALA B  2  31  ? 60.731 -38.039 -15.748 1.00 29.38  ?  63  ALA B C     1 
ATOM   3628  O  O     . ALA B  2  31  ? 61.526 -38.939 -15.473 1.00 29.85  ?  63  ALA B O     1 
ATOM   3629  C  CB    . ALA B  2  31  ? 60.931 -37.515 -18.194 1.00 30.46  ?  63  ALA B CB    1 
ATOM   3630  N  N     . SER B  2  32  ? 60.453 -37.053 -14.888 1.00 27.17  ?  64  SER B N     1 
ATOM   3631  C  CA    . SER B  2  32  ? 61.229 -36.887 -13.653 1.00 25.21  ?  64  SER B CA    1 
ATOM   3632  C  C     . SER B  2  32  ? 61.125 -38.102 -12.769 1.00 23.87  ?  64  SER B C     1 
ATOM   3633  O  O     . SER B  2  32  ? 62.091 -38.455 -12.097 1.00 22.71  ?  64  SER B O     1 
ATOM   3634  C  CB    . SER B  2  32  ? 60.805 -35.636 -12.898 1.00 25.52  ?  64  SER B CB    1 
ATOM   3635  O  OG    . SER B  2  32  ? 59.450 -35.326 -13.161 1.00 25.67  ?  64  SER B OG    1 
ATOM   3636  N  N     . SER B  2  33  ? 59.973 -38.773 -12.827 1.00 23.90  ?  65  SER B N     1 
ATOM   3637  C  CA    . SER B  2  33  ? 59.699 -39.969 -12.006 1.00 23.38  ?  65  SER B CA    1 
ATOM   3638  C  C     . SER B  2  33  ? 60.551 -41.140 -12.414 1.00 22.45  ?  65  SER B C     1 
ATOM   3639  O  O     . SER B  2  33  ? 60.507 -42.203 -11.763 1.00 21.45  ?  65  SER B O     1 
ATOM   3640  C  CB    . SER B  2  33  ? 58.264 -40.421 -12.155 1.00 22.87  ?  65  SER B CB    1 
ATOM   3641  O  OG    . SER B  2  33  ? 58.264 -41.465 -13.111 1.00 23.34  ?  65  SER B OG    1 
ATOM   3642  N  N     . LYS B  2  34  ? 61.250 -40.956 -13.530 1.00 22.25  ?  66  LYS B N     1 
ATOM   3643  C  CA    . LYS B  2  34  ? 62.182 -41.935 -14.070 1.00 24.19  ?  66  LYS B CA    1 
ATOM   3644  C  C     . LYS B  2  34  ? 61.525 -43.335 -14.258 1.00 23.68  ?  66  LYS B C     1 
ATOM   3645  O  O     . LYS B  2  34  ? 62.103 -44.376 -13.984 1.00 23.12  ?  66  LYS B O     1 
ATOM   3646  C  CB    . LYS B  2  34  ? 63.463 -41.987 -13.207 1.00 25.21  ?  66  LYS B CB    1 
ATOM   3647  C  CG    . LYS B  2  34  ? 64.202 -40.664 -13.084 1.00 26.30  ?  66  LYS B CG    1 
ATOM   3648  C  CD    . LYS B  2  34  ? 65.025 -40.590 -11.804 1.00 28.59  ?  66  LYS B CD    1 
ATOM   3649  C  CE    . LYS B  2  34  ? 65.495 -39.168 -11.461 1.00 31.08  ?  66  LYS B CE    1 
ATOM   3650  N  NZ    . LYS B  2  34  ? 64.532 -38.416 -10.584 1.00 32.01  1  66  LYS B NZ    1 
ATOM   3651  N  N     . GLY B  2  35  ? 60.307 -43.354 -14.743 1.00 23.64  ?  67  GLY B N     1 
ATOM   3652  C  CA    . GLY B  2  35  ? 59.700 -44.610 -15.023 1.00 25.03  ?  67  GLY B CA    1 
ATOM   3653  C  C     . GLY B  2  35  ? 58.796 -45.056 -13.919 1.00 26.84  ?  67  GLY B C     1 
ATOM   3654  O  O     . GLY B  2  35  ? 58.038 -46.002 -14.106 1.00 28.58  ?  67  GLY B O     1 
ATOM   3655  N  N     . ALA B  2  36  ? 58.829 -44.387 -12.775 1.00 29.32  ?  68  ALA B N     1 
ATOM   3656  C  CA    . ALA B  2  36  ? 57.905 -44.763 -11.696 1.00 32.64  ?  68  ALA B CA    1 
ATOM   3657  C  C     . ALA B  2  36  ? 56.433 -44.383 -12.023 1.00 33.74  ?  68  ALA B C     1 
ATOM   3658  O  O     . ALA B  2  36  ? 56.202 -43.378 -12.669 1.00 33.03  ?  68  ALA B O     1 
ATOM   3659  C  CB    . ALA B  2  36  ? 58.363 -44.153 -10.379 1.00 32.34  ?  68  ALA B CB    1 
ATOM   3660  N  N     . ASN B  2  37  ? 55.458 -45.211 -11.624 1.00 36.63  ?  69  ASN B N     1 
ATOM   3661  C  CA    . ASN B  2  37  ? 54.033 -44.827 -11.676 1.00 37.62  ?  69  ASN B CA    1 
ATOM   3662  C  C     . ASN B  2  37  ? 53.886 -43.580 -10.815 1.00 38.12  ?  69  ASN B C     1 
ATOM   3663  O  O     . ASN B  2  37  ? 54.202 -43.610 -9.615  1.00 37.70  ?  69  ASN B O     1 
ATOM   3664  C  CB    . ASN B  2  37  ? 53.077 -45.948 -11.160 1.00 38.35  ?  69  ASN B CB    1 
ATOM   3665  C  CG    . ASN B  2  37  ? 52.474 -46.813 -12.283 1.00 39.55  ?  69  ASN B CG    1 
ATOM   3666  O  OD1   . ASN B  2  37  ? 52.464 -46.418 -13.453 1.00 41.42  ?  69  ASN B OD1   1 
ATOM   3667  N  ND2   . ASN B  2  37  ? 51.947 -47.999 -11.918 1.00 39.20  ?  69  ASN B ND2   1 
ATOM   3668  N  N     . ALA B  2  38  ? 53.460 -42.478 -11.434 1.00 38.85  ?  70  ALA B N     1 
ATOM   3669  C  CA    . ALA B  2  38  ? 53.224 -41.220 -10.717 1.00 39.08  ?  70  ALA B CA    1 
ATOM   3670  C  C     . ALA B  2  38  ? 52.103 -41.457 -9.718  1.00 38.23  ?  70  ALA B C     1 
ATOM   3671  O  O     . ALA B  2  38  ? 51.117 -42.112 -10.057 1.00 37.84  ?  70  ALA B O     1 
ATOM   3672  C  CB    . ALA B  2  38  ? 52.853 -40.121 -11.691 1.00 39.18  ?  70  ALA B CB    1 
ATOM   3673  N  N     . SER B  2  39  ? 52.258 -40.944 -8.497  1.00 38.17  ?  71  SER B N     1 
ATOM   3674  C  CA    . SER B  2  39  ? 51.432 -41.402 -7.359  1.00 38.89  ?  71  SER B CA    1 
ATOM   3675  C  C     . SER B  2  39  ? 49.922 -41.190 -7.556  1.00 38.31  ?  71  SER B C     1 
ATOM   3676  O  O     . SER B  2  39  ? 49.120 -42.113 -7.424  1.00 35.87  ?  71  SER B O     1 
ATOM   3677  C  CB    . SER B  2  39  ? 51.878 -40.742 -6.045  1.00 37.50  ?  71  SER B CB    1 
ATOM   3678  O  OG    . SER B  2  39  ? 51.044 -41.178 -4.984  1.00 34.75  ?  71  SER B OG    1 
ATOM   3679  N  N     . ASN B  2  40  ? 49.554 -39.953 -7.853  1.00 38.77  ?  72  ASN B N     1 
ATOM   3680  C  CA    . ASN B  2  40  ? 48.166 -39.578 -8.024  1.00 37.88  ?  72  ASN B CA    1 
ATOM   3681  C  C     . ASN B  2  40  ? 48.137 -38.227 -8.725  1.00 35.43  ?  72  ASN B C     1 
ATOM   3682  O  O     . ASN B  2  40  ? 47.848 -37.206 -8.114  1.00 31.98  ?  72  ASN B O     1 
ATOM   3683  C  CB    . ASN B  2  40  ? 47.461 -39.510 -6.679  1.00 38.80  ?  72  ASN B CB    1 
ATOM   3684  C  CG    . ASN B  2  40  ? 46.019 -39.133 -6.827  1.00 41.38  ?  72  ASN B CG    1 
ATOM   3685  O  OD1   . ASN B  2  40  ? 45.471 -39.171 -7.936  1.00 40.96  ?  72  ASN B OD1   1 
ATOM   3686  N  ND2   . ASN B  2  40  ? 45.390 -38.747 -5.723  1.00 44.66  ?  72  ASN B ND2   1 
ATOM   3687  N  N     . PRO B  2  41  ? 48.456 -38.229 -10.028 1.00 35.04  ?  73  PRO B N     1 
ATOM   3688  C  CA    . PRO B  2  41  ? 48.815 -36.988 -10.705 1.00 33.73  ?  73  PRO B CA    1 
ATOM   3689  C  C     . PRO B  2  41  ? 47.595 -36.135 -11.075 1.00 30.85  ?  73  PRO B C     1 
ATOM   3690  O  O     . PRO B  2  41  ? 46.551 -36.691 -11.395 1.00 29.25  ?  73  PRO B O     1 
ATOM   3691  C  CB    . PRO B  2  41  ? 49.567 -37.485 -11.961 1.00 32.81  ?  73  PRO B CB    1 
ATOM   3692  C  CG    . PRO B  2  41  ? 49.038 -38.843 -12.224 1.00 32.75  ?  73  PRO B CG    1 
ATOM   3693  C  CD    . PRO B  2  41  ? 48.408 -39.375 -10.960 1.00 33.60  ?  73  PRO B CD    1 
ATOM   3694  N  N     . GLY B  2  42  ? 47.763 -34.809 -11.027 1.00 28.30  ?  74  GLY B N     1 
ATOM   3695  C  CA    . GLY B  2  42  ? 46.749 -33.840 -11.441 1.00 26.93  ?  74  GLY B CA    1 
ATOM   3696  C  C     . GLY B  2  42  ? 47.340 -32.695 -12.255 1.00 26.89  ?  74  GLY B C     1 
ATOM   3697  O  O     . GLY B  2  42  ? 48.518 -32.717 -12.644 1.00 24.92  ?  74  GLY B O     1 
ATOM   3698  N  N     . PRO B  2  43  ? 46.524 -31.673 -12.531 1.00 27.53  ?  75  PRO B N     1 
ATOM   3699  C  CA    . PRO B  2  43  ? 47.028 -30.555 -13.351 1.00 29.07  ?  75  PRO B CA    1 
ATOM   3700  C  C     . PRO B  2  43  ? 48.252 -29.817 -12.753 1.00 31.51  ?  75  PRO B C     1 
ATOM   3701  O  O     . PRO B  2  43  ? 49.041 -29.240 -13.494 1.00 32.22  ?  75  PRO B O     1 
ATOM   3702  C  CB    . PRO B  2  43  ? 45.811 -29.621 -13.489 1.00 27.55  ?  75  PRO B CB    1 
ATOM   3703  C  CG    . PRO B  2  43  ? 44.787 -30.108 -12.512 1.00 26.84  ?  75  PRO B CG    1 
ATOM   3704  C  CD    . PRO B  2  43  ? 45.113 -31.521 -12.140 1.00 26.26  ?  75  PRO B CD    1 
ATOM   3705  N  N     . PHE B  2  44  ? 48.414 -29.858 -11.431 1.00 34.92  ?  76  PHE B N     1 
ATOM   3706  C  CA    . PHE B  2  44  ? 49.471 -29.112 -10.729 1.00 36.83  ?  76  PHE B CA    1 
ATOM   3707  C  C     . PHE B  2  44  ? 50.625 -29.946 -10.208 1.00 37.25  ?  76  PHE B C     1 
ATOM   3708  O  O     . PHE B  2  44  ? 51.561 -29.420 -9.553  1.00 36.25  ?  76  PHE B O     1 
ATOM   3709  C  CB    . PHE B  2  44  ? 48.853 -28.388 -9.570  1.00 38.33  ?  76  PHE B CB    1 
ATOM   3710  C  CG    . PHE B  2  44  ? 47.705 -27.584 -9.974  1.00 38.75  ?  76  PHE B CG    1 
ATOM   3711  C  CD1   . PHE B  2  44  ? 47.913 -26.418 -10.670 1.00 39.68  ?  76  PHE B CD1   1 
ATOM   3712  C  CD2   . PHE B  2  44  ? 46.420 -28.021 -9.720  1.00 39.44  ?  76  PHE B CD2   1 
ATOM   3713  C  CE1   . PHE B  2  44  ? 46.845 -25.666 -11.086 1.00 42.71  ?  76  PHE B CE1   1 
ATOM   3714  C  CE2   . PHE B  2  44  ? 45.341 -27.281 -10.135 1.00 41.87  ?  76  PHE B CE2   1 
ATOM   3715  C  CZ    . PHE B  2  44  ? 45.549 -26.096 -10.817 1.00 43.46  ?  76  PHE B CZ    1 
ATOM   3716  N  N     . GLY B  2  45  ? 50.693 -31.193 -10.588 1.00 36.07  ?  77  GLY B N     1 
ATOM   3717  C  CA    . GLY B  2  45  ? 51.859 -31.919 -10.207 1.00 35.91  ?  77  GLY B CA    1 
ATOM   3718  C  C     . GLY B  2  45  ? 51.674 -33.218 -9.539  1.00 35.92  ?  77  GLY B C     1 
ATOM   3719  O  O     . GLY B  2  45  ? 50.623 -33.783 -9.523  1.00 34.20  ?  77  GLY B O     1 
ATOM   3720  N  N     . ASP B  2  46  ? 52.757 -33.672 -8.958  1.00 35.84  ?  78  ASP B N     1 
ATOM   3721  C  CA    . ASP B  2  46  ? 52.740 -34.892 -8.256  1.00 34.86  ?  78  ASP B CA    1 
ATOM   3722  C  C     . ASP B  2  46  ? 54.018 -34.997 -7.526  1.00 35.49  ?  78  ASP B C     1 
ATOM   3723  O  O     . ASP B  2  46  ? 55.034 -34.636 -8.014  1.00 35.02  ?  78  ASP B O     1 
ATOM   3724  C  CB    . ASP B  2  46  ? 52.669 -36.042 -9.257  1.00 33.31  ?  78  ASP B CB    1 
ATOM   3725  C  CG    . ASP B  2  46  ? 52.254 -37.315 -8.645  1.00 34.57  ?  78  ASP B CG    1 
ATOM   3726  O  OD1   . ASP B  2  46  ? 51.380 -37.274 -7.800  1.00 34.93  ?  78  ASP B OD1   1 
ATOM   3727  O  OD2   . ASP B  2  46  ? 52.784 -38.363 -8.979  1.00 34.08  -1 78  ASP B OD2   1 
ATOM   3728  N  N     . VAL B  2  47  ? 53.944 -35.480 -6.318  1.00 37.66  ?  79  VAL B N     1 
ATOM   3729  C  CA    . VAL B  2  47  ? 55.152 -35.879 -5.573  1.00 39.25  ?  79  VAL B CA    1 
ATOM   3730  C  C     . VAL B  2  47  ? 55.742 -36.873 -6.570  1.00 41.06  ?  79  VAL B C     1 
ATOM   3731  O  O     . VAL B  2  47  ? 55.025 -37.255 -7.502  1.00 46.54  ?  79  VAL B O     1 
ATOM   3732  C  CB    . VAL B  2  47  ? 54.799 -36.501 -4.175  1.00 39.13  ?  79  VAL B CB    1 
ATOM   3733  C  CG1   . VAL B  2  47  ? 54.062 -35.496 -3.295  1.00 39.25  ?  79  VAL B CG1   1 
ATOM   3734  C  CG2   . VAL B  2  47  ? 53.944 -37.767 -4.277  1.00 38.87  ?  79  VAL B CG2   1 
ATOM   3735  N  N     . LEU B  2  48  ? 56.998 -37.290 -6.479  1.00 39.38  ?  80  LEU B N     1 
ATOM   3736  C  CA    . LEU B  2  48  ? 57.527 -38.222 -7.553  1.00 40.83  ?  80  LEU B CA    1 
ATOM   3737  C  C     . LEU B  2  48  ? 57.653 -37.663 -9.009  1.00 41.14  ?  80  LEU B C     1 
ATOM   3738  O  O     . LEU B  2  48  ? 58.134 -38.368 -9.898  1.00 40.92  ?  80  LEU B O     1 
ATOM   3739  C  CB    . LEU B  2  48  ? 56.637 -39.483 -7.688  1.00 36.52  ?  80  LEU B CB    1 
ATOM   3740  C  CG    . LEU B  2  48  ? 57.141 -40.787 -7.120  1.00 33.51  ?  80  LEU B CG    1 
ATOM   3741  C  CD1   . LEU B  2  48  ? 57.440 -40.630 -5.652  1.00 32.41  ?  80  LEU B CD1   1 
ATOM   3742  C  CD2   . LEU B  2  48  ? 56.076 -41.836 -7.362  1.00 32.93  ?  80  LEU B CD2   1 
ATOM   3743  N  N     . CYS B  2  49  ? 57.163 -36.444 -9.242  1.00 40.48  ?  81  CYS B N     1 
ATOM   3744  C  CA    . CYS B  2  49  ? 57.247 -35.756 -10.527 1.00 39.19  ?  81  CYS B CA    1 
ATOM   3745  C  C     . CYS B  2  49  ? 57.613 -34.311 -10.211 1.00 39.17  ?  81  CYS B C     1 
ATOM   3746  O  O     . CYS B  2  49  ? 56.978 -33.660 -9.360  1.00 38.59  ?  81  CYS B O     1 
ATOM   3747  C  CB    . CYS B  2  49  ? 55.903 -35.735 -11.303 1.00 39.51  ?  81  CYS B CB    1 
ATOM   3748  S  SG    . CYS B  2  49  ? 55.483 -37.083 -12.453 1.00 36.71  ?  81  CYS B SG    1 
ATOM   3749  N  N     . ASP B  2  50  ? 58.612 -33.802 -10.920 1.00 39.09  ?  82  ASP B N     1 
ATOM   3750  C  CA    . ASP B  2  50  ? 58.930 -32.391 -10.871 1.00 39.22  ?  82  ASP B CA    1 
ATOM   3751  C  C     . ASP B  2  50  ? 57.789 -31.474 -11.338 1.00 41.46  ?  82  ASP B C     1 
ATOM   3752  O  O     . ASP B  2  50  ? 56.700 -31.931 -11.702 1.00 43.33  ?  82  ASP B O     1 
ATOM   3753  C  CB    . ASP B  2  50  ? 60.135 -32.123 -11.742 1.00 38.55  ?  82  ASP B CB    1 
ATOM   3754  C  CG    . ASP B  2  50  ? 61.380 -32.074 -10.943 1.00 40.89  ?  82  ASP B CG    1 
ATOM   3755  O  OD1   . ASP B  2  50  ? 61.433 -31.283 -9.976  1.00 41.72  ?  82  ASP B OD1   1 
ATOM   3756  O  OD2   . ASP B  2  50  ? 62.303 -32.844 -11.254 1.00 44.64  -1 82  ASP B OD2   1 
ATOM   3757  N  N     . SER B  2  51  ? 58.029 -30.172 -11.279 1.00 42.71  ?  83  SER B N     1 
ATOM   3758  C  CA    . SER B  2  51  ? 57.017 -29.192 -11.641 1.00 42.89  ?  83  SER B CA    1 
ATOM   3759  C  C     . SER B  2  51  ? 56.473 -29.229 -13.083 1.00 44.65  ?  83  SER B C     1 
ATOM   3760  O  O     . SER B  2  51  ? 57.234 -29.132 -14.058 1.00 42.28  ?  83  SER B O     1 
ATOM   3761  C  CB    . SER B  2  51  ? 57.533 -27.785 -11.339 1.00 41.56  ?  83  SER B CB    1 
ATOM   3762  O  OG    . SER B  2  51  ? 57.855 -27.625 -9.979  1.00 38.67  ?  83  SER B OG    1 
ATOM   3763  N  N     . PRO B  2  52  ? 55.137 -29.358 -13.217 1.00 48.84  ?  84  PRO B N     1 
ATOM   3764  C  CA    . PRO B  2  52  ? 54.526 -29.065 -14.506 1.00 49.10  ?  84  PRO B CA    1 
ATOM   3765  C  C     . PRO B  2  52  ? 54.542 -27.585 -14.713 1.00 46.01  ?  84  PRO B C     1 
ATOM   3766  O  O     . PRO B  2  52  ? 54.600 -26.850 -13.742 1.00 46.52  ?  84  PRO B O     1 
ATOM   3767  C  CB    . PRO B  2  52  ? 53.079 -29.545 -14.342 1.00 50.80  ?  84  PRO B CB    1 
ATOM   3768  C  CG    . PRO B  2  52  ? 52.826 -29.594 -12.879 1.00 50.72  ?  84  PRO B CG    1 
ATOM   3769  C  CD    . PRO B  2  52  ? 54.150 -29.840 -12.226 1.00 50.61  ?  84  PRO B CD    1 
ATOM   3770  N  N     . TYR B  2  53  ? 54.466 -27.143 -15.955 1.00 45.13  ?  85  TYR B N     1 
ATOM   3771  C  CA    . TYR B  2  53  ? 54.447 -25.716 -16.224 1.00 45.31  ?  85  TYR B CA    1 
ATOM   3772  C  C     . TYR B  2  53  ? 53.331 -24.953 -15.466 1.00 44.15  ?  85  TYR B C     1 
ATOM   3773  O  O     . TYR B  2  53  ? 53.537 -23.810 -15.074 1.00 40.50  ?  85  TYR B O     1 
ATOM   3774  C  CB    . TYR B  2  53  ? 54.355 -25.465 -17.727 1.00 46.13  ?  85  TYR B CB    1 
ATOM   3775  C  CG    . TYR B  2  53  ? 54.553 -24.013 -18.095 1.00 49.00  ?  85  TYR B CG    1 
ATOM   3776  C  CD1   . TYR B  2  53  ? 55.736 -23.346 -17.755 1.00 49.30  ?  85  TYR B CD1   1 
ATOM   3777  C  CD2   . TYR B  2  53  ? 53.551 -23.290 -18.763 1.00 48.32  ?  85  TYR B CD2   1 
ATOM   3778  C  CE1   . TYR B  2  53  ? 55.917 -22.006 -18.076 1.00 50.15  ?  85  TYR B CE1   1 
ATOM   3779  C  CE2   . TYR B  2  53  ? 53.720 -21.950 -19.076 1.00 49.71  ?  85  TYR B CE2   1 
ATOM   3780  C  CZ    . TYR B  2  53  ? 54.912 -21.318 -18.736 1.00 49.89  ?  85  TYR B CZ    1 
ATOM   3781  O  OH    . TYR B  2  53  ? 55.115 -20.004 -19.048 1.00 49.51  ?  85  TYR B OH    1 
ATOM   3782  N  N     . GLN B  2  54  ? 52.174 -25.577 -15.233 1.00 47.12  ?  86  GLN B N     1 
ATOM   3783  C  CA    . GLN B  2  54  ? 51.031 -24.868 -14.611 1.00 51.59  ?  86  GLN B CA    1 
ATOM   3784  C  C     . GLN B  2  54  ? 51.069 -24.778 -13.076 1.00 50.73  ?  86  GLN B C     1 
ATOM   3785  O  O     . GLN B  2  54  ? 50.310 -24.012 -12.455 1.00 47.23  ?  86  GLN B O     1 
ATOM   3786  C  CB    . GLN B  2  54  ? 49.719 -25.502 -15.029 1.00 55.67  ?  86  GLN B CB    1 
ATOM   3787  C  CG    . GLN B  2  54  ? 48.573 -24.527 -14.879 1.00 62.88  ?  86  GLN B CG    1 
ATOM   3788  C  CD    . GLN B  2  54  ? 47.248 -25.112 -15.298 1.00 75.98  ?  86  GLN B CD    1 
ATOM   3789  O  OE1   . GLN B  2  54  ? 46.314 -24.374 -15.632 1.00 89.95  ?  86  GLN B OE1   1 
ATOM   3790  N  NE2   . GLN B  2  54  ? 47.148 -26.444 -15.283 1.00 80.60  ?  86  GLN B NE2   1 
ATOM   3791  N  N     . LEU B  2  55  ? 51.925 -25.608 -12.481 1.00 49.94  ?  87  LEU B N     1 
ATOM   3792  C  CA    . LEU B  2  55  ? 52.319 -25.485 -11.082 1.00 45.67  ?  87  LEU B CA    1 
ATOM   3793  C  C     . LEU B  2  55  ? 53.128 -24.204 -10.941 1.00 44.44  ?  87  LEU B C     1 
ATOM   3794  O  O     . LEU B  2  55  ? 52.681 -23.251 -10.301 1.00 46.73  ?  87  LEU B O     1 
ATOM   3795  C  CB    . LEU B  2  55  ? 53.160 -26.694 -10.671 1.00 43.92  ?  87  LEU B CB    1 
ATOM   3796  C  CG    . LEU B  2  55  ? 53.902 -26.643 -9.353  1.00 42.27  ?  87  LEU B CG    1 
ATOM   3797  C  CD1   . LEU B  2  55  ? 52.894 -26.452 -8.242  1.00 44.93  ?  87  LEU B CD1   1 
ATOM   3798  C  CD2   . LEU B  2  55  ? 54.666 -27.925 -9.162  1.00 40.68  ?  87  LEU B CD2   1 
ATOM   3799  N  N     . ILE B  2  56  ? 54.295 -24.175 -11.583 1.00 41.20  ?  88  ILE B N     1 
ATOM   3800  C  CA    . ILE B  2  56  ? 55.142 -23.000 -11.570 1.00 42.08  ?  88  ILE B CA    1 
ATOM   3801  C  C     . ILE B  2  56  ? 54.403 -21.751 -12.054 1.00 44.02  ?  88  ILE B C     1 
ATOM   3802  O  O     . ILE B  2  56  ? 54.686 -20.654 -11.560 1.00 51.85  ?  88  ILE B O     1 
ATOM   3803  C  CB    . ILE B  2  56  ? 56.364 -23.176 -12.468 1.00 44.94  ?  88  ILE B CB    1 
ATOM   3804  C  CG1   . ILE B  2  56  ? 57.218 -24.364 -11.991 1.00 48.18  ?  88  ILE B CG1   1 
ATOM   3805  C  CG2   . ILE B  2  56  ? 57.181 -21.883 -12.486 1.00 45.54  ?  88  ILE B CG2   1 
ATOM   3806  C  CD1   . ILE B  2  56  ? 58.306 -24.800 -12.972 1.00 49.43  ?  88  ILE B CD1   1 
ATOM   3807  N  N     . LEU B  2  57  ? 53.488 -21.904 -13.024 1.00 40.60  ?  89  LEU B N     1 
ATOM   3808  C  CA    . LEU B  2  57  ? 52.745 -20.771 -13.575 1.00 36.36  ?  89  LEU B CA    1 
ATOM   3809  C  C     . LEU B  2  57  ? 51.833 -20.228 -12.514 1.00 35.70  ?  89  LEU B C     1 
ATOM   3810  O  O     . LEU B  2  57  ? 51.775 -19.045 -12.332 1.00 37.90  ?  89  LEU B O     1 
ATOM   3811  C  CB    . LEU B  2  57  ? 51.928 -21.162 -14.807 1.00 36.33  ?  89  LEU B CB    1 
ATOM   3812  C  CG    . LEU B  2  57  ? 51.531 -20.084 -15.835 1.00 37.40  ?  89  LEU B CG    1 
ATOM   3813  C  CD1   . LEU B  2  57  ? 52.700 -19.287 -16.414 1.00 37.01  ?  89  LEU B CD1   1 
ATOM   3814  C  CD2   . LEU B  2  57  ? 50.799 -20.744 -16.993 1.00 38.89  ?  89  LEU B CD2   1 
ATOM   3815  N  N     . SER B  2  58  ? 51.140 -21.097 -11.792 1.00 35.68  ?  90  SER B N     1 
ATOM   3816  C  CA    . SER B  2  58  ? 50.228 -20.681 -10.718 1.00 34.37  ?  90  SER B CA    1 
ATOM   3817  C  C     . SER B  2  58  ? 50.899 -19.997 -9.531  1.00 35.81  ?  90  SER B C     1 
ATOM   3818  O  O     . SER B  2  58  ? 50.245 -19.237 -8.803  1.00 39.24  ?  90  SER B O     1 
ATOM   3819  C  CB    . SER B  2  58  ? 49.540 -21.900 -10.167 1.00 32.33  ?  90  SER B CB    1 
ATOM   3820  O  OG    . SER B  2  58  ? 50.509 -22.781 -9.661  1.00 31.05  ?  90  SER B OG    1 
ATOM   3821  N  N     . ALA B  2  59  ? 52.171 -20.315 -9.305  1.00 33.92  ?  91  ALA B N     1 
ATOM   3822  C  CA    . ALA B  2  59  ? 52.931 -19.723 -8.225  1.00 33.78  ?  91  ALA B CA    1 
ATOM   3823  C  C     . ALA B  2  59  ? 53.163 -18.272 -8.495  1.00 34.48  ?  91  ALA B C     1 
ATOM   3824  O  O     . ALA B  2  59  ? 53.023 -17.455 -7.616  1.00 35.04  ?  91  ALA B O     1 
ATOM   3825  C  CB    . ALA B  2  59  ? 54.262 -20.420 -8.068  1.00 33.69  ?  91  ALA B CB    1 
ATOM   3826  N  N     . PHE B  2  60  ? 53.554 -17.958 -9.716  1.00 38.97  ?  92  PHE B N     1 
ATOM   3827  C  CA    . PHE B  2  60  ? 53.795 -16.556 -10.126 1.00 44.25  ?  92  PHE B CA    1 
ATOM   3828  C  C     . PHE B  2  60  ? 52.506 -15.698 -10.283 1.00 46.23  ?  92  PHE B C     1 
ATOM   3829  O  O     . PHE B  2  60  ? 52.421 -14.613 -9.708  1.00 44.92  ?  92  PHE B O     1 
ATOM   3830  C  CB    . PHE B  2  60  ? 54.590 -16.519 -11.436 1.00 43.02  ?  92  PHE B CB    1 
ATOM   3831  C  CG    . PHE B  2  60  ? 56.017 -16.948 -11.297 1.00 41.92  ?  92  PHE B CG    1 
ATOM   3832  C  CD1   . PHE B  2  60  ? 56.874 -16.267 -10.429 1.00 44.32  ?  92  PHE B CD1   1 
ATOM   3833  C  CD2   . PHE B  2  60  ? 56.512 -17.992 -12.059 1.00 39.15  ?  92  PHE B CD2   1 
ATOM   3834  C  CE1   . PHE B  2  60  ? 58.201 -16.623 -10.317 1.00 45.07  ?  92  PHE B CE1   1 
ATOM   3835  C  CE2   . PHE B  2  60  ? 57.826 -18.357 -11.953 1.00 40.96  ?  92  PHE B CE2   1 
ATOM   3836  C  CZ    . PHE B  2  60  ? 58.679 -17.672 -11.087 1.00 44.82  ?  92  PHE B CZ    1 
ATOM   3837  N  N     . ASP B  2  61  ? 51.532 -16.182 -11.069 1.00 47.23  ?  93  ASP B N     1 
ATOM   3838  C  CA    . ASP B  2  61  ? 50.188 -15.594 -11.141 1.00 48.33  ?  93  ASP B CA    1 
ATOM   3839  C  C     . ASP B  2  61  ? 49.651 -15.307 -9.744  1.00 53.54  ?  93  ASP B C     1 
ATOM   3840  O  O     . ASP B  2  61  ? 48.913 -14.330 -9.577  1.00 63.66  ?  93  ASP B O     1 
ATOM   3841  C  CB    . ASP B  2  61  ? 49.158 -16.521 -11.820 1.00 47.17  ?  93  ASP B CB    1 
ATOM   3842  C  CG    . ASP B  2  61  ? 49.460 -16.794 -13.261 1.00 46.15  ?  93  ASP B CG    1 
ATOM   3843  O  OD1   . ASP B  2  61  ? 50.147 -15.958 -13.895 1.00 45.72  ?  93  ASP B OD1   1 
ATOM   3844  O  OD2   . ASP B  2  61  ? 49.010 -17.861 -13.744 1.00 44.02  -1 93  ASP B OD2   1 
ATOM   3845  N  N     . PHE B  2  62  ? 49.949 -16.174 -8.760  1.00 50.59  ?  94  PHE B N     1 
ATOM   3846  C  CA    . PHE B  2  62  ? 49.557 -15.875 -7.388  1.00 45.11  ?  94  PHE B CA    1 
ATOM   3847  C  C     . PHE B  2  62  ? 50.364 -14.659 -6.937  1.00 42.13  ?  94  PHE B C     1 
ATOM   3848  O  O     . PHE B  2  62  ? 49.803 -13.733 -6.378  1.00 45.56  ?  94  PHE B O     1 
ATOM   3849  C  CB    . PHE B  2  62  ? 49.736 -17.047 -6.417  1.00 43.85  ?  94  PHE B CB    1 
ATOM   3850  C  CG    . PHE B  2  62  ? 49.683 -16.621 -4.976  1.00 45.29  ?  94  PHE B CG    1 
ATOM   3851  C  CD1   . PHE B  2  62  ? 48.467 -16.532 -4.304  1.00 46.95  ?  94  PHE B CD1   1 
ATOM   3852  C  CD2   . PHE B  2  62  ? 50.838 -16.231 -4.307  1.00 46.60  ?  94  PHE B CD2   1 
ATOM   3853  C  CE1   . PHE B  2  62  ? 48.407 -16.112 -2.975  1.00 47.18  ?  94  PHE B CE1   1 
ATOM   3854  C  CE2   . PHE B  2  62  ? 50.787 -15.789 -2.985  1.00 49.17  ?  94  PHE B CE2   1 
ATOM   3855  C  CZ    . PHE B  2  62  ? 49.569 -15.736 -2.313  1.00 48.19  ?  94  PHE B CZ    1 
ATOM   3856  N  N     . ILE B  2  63  ? 51.662 -14.630 -7.197  1.00 37.67  ?  95  ILE B N     1 
ATOM   3857  C  CA    . ILE B  2  63  ? 52.440 -13.502 -6.749  1.00 39.27  ?  95  ILE B CA    1 
ATOM   3858  C  C     . ILE B  2  63  ? 51.870 -12.215 -7.336  1.00 43.41  ?  95  ILE B C     1 
ATOM   3859  O  O     . ILE B  2  63  ? 51.729 -11.229 -6.629  1.00 45.88  ?  95  ILE B O     1 
ATOM   3860  C  CB    . ILE B  2  63  ? 53.950 -13.667 -7.042  1.00 40.44  ?  95  ILE B CB    1 
ATOM   3861  C  CG1   . ILE B  2  63  ? 54.583 -14.627 -5.998  1.00 40.29  ?  95  ILE B CG1   1 
ATOM   3862  C  CG2   . ILE B  2  63  ? 54.647 -12.306 -7.007  1.00 41.93  ?  95  ILE B CG2   1 
ATOM   3863  C  CD1   . ILE B  2  63  ? 56.046 -15.014 -6.165  1.00 37.03  ?  95  ILE B CD1   1 
ATOM   3864  N  N     . LYS B  2  64  ? 51.513 -12.238 -8.617  1.00 50.56  ?  96  LYS B N     1 
ATOM   3865  C  CA    . LYS B  2  64  ? 50.993 -11.050 -9.335  1.00 53.05  ?  96  LYS B CA    1 
ATOM   3866  C  C     . LYS B  2  64  ? 49.682 -10.606 -8.705  1.00 49.75  ?  96  LYS B C     1 
ATOM   3867  O  O     . LYS B  2  64  ? 49.562 -9.476  -8.281  1.00 48.28  ?  96  LYS B O     1 
ATOM   3868  C  CB    . LYS B  2  64  ? 50.791 -11.377 -10.831 1.00 56.48  ?  96  LYS B CB    1 
ATOM   3869  C  CG    . LYS B  2  64  ? 50.727 -10.213 -11.816 1.00 58.85  ?  96  LYS B CG    1 
ATOM   3870  C  CD    . LYS B  2  64  ? 50.711 -10.766 -13.241 1.00 61.01  ?  96  LYS B CD    1 
ATOM   3871  C  CE    . LYS B  2  64  ? 50.300 -9.736  -14.275 1.00 63.09  ?  96  LYS B CE    1 
ATOM   3872  N  NZ    . LYS B  2  64  ? 48.872 -9.913  -14.658 1.00 62.73  1  96  LYS B NZ    1 
ATOM   3873  N  N     . ASN B  2  65  ? 48.732 -11.528 -8.604  1.00 51.16  ?  97  ASN B N     1 
ATOM   3874  C  CA    . ASN B  2  65  ? 47.403 -11.264 -8.041  1.00 54.40  ?  97  ASN B CA    1 
ATOM   3875  C  C     . ASN B  2  65  ? 47.379 -11.300 -6.513  1.00 54.72  ?  97  ASN B C     1 
ATOM   3876  O  O     . ASN B  2  65  ? 46.304 -11.417 -5.931  1.00 57.27  ?  97  ASN B O     1 
ATOM   3877  C  CB    . ASN B  2  65  ? 46.379 -12.322 -8.514  1.00 56.47  ?  97  ASN B CB    1 
ATOM   3878  C  CG    . ASN B  2  65  ? 46.203 -12.385 -10.026 1.00 56.31  ?  97  ASN B CG    1 
ATOM   3879  O  OD1   . ASN B  2  65  ? 45.238 -12.981 -10.498 1.00 59.28  ?  97  ASN B OD1   1 
ATOM   3880  N  ND2   . ASN B  2  65  ? 47.130 -11.808 -10.788 1.00 56.64  ?  97  ASN B ND2   1 
ATOM   3881  N  N     . SER B  2  66  ? 48.541 -11.216 -5.862  1.00 54.82  ?  98  SER B N     1 
ATOM   3882  C  CA    . SER B  2  66  ? 48.627 -11.402 -4.405  1.00 52.71  ?  98  SER B CA    1 
ATOM   3883  C  C     . SER B  2  66  ? 48.070 -10.238 -3.610  1.00 52.47  ?  98  SER B C     1 
ATOM   3884  O  O     . SER B  2  66  ? 47.602 -10.430 -2.498  1.00 54.68  ?  98  SER B O     1 
ATOM   3885  C  CB    . SER B  2  66  ? 50.077 -11.620 -3.958  1.00 51.60  ?  98  SER B CB    1 
ATOM   3886  O  OG    . SER B  2  66  ? 50.815 -10.408 -3.977  1.00 50.93  ?  98  SER B OG    1 
ATOM   3887  N  N     . GLY B  2  67  ? 48.142 -9.033  -4.165  1.00 53.70  ?  99  GLY B N     1 
ATOM   3888  C  CA    . GLY B  2  67  ? 47.840 -7.828  -3.399  1.00 56.39  ?  99  GLY B CA    1 
ATOM   3889  C  C     . GLY B  2  67  ? 48.986 -7.470  -2.458  1.00 56.12  ?  99  GLY B C     1 
ATOM   3890  O  O     . GLY B  2  67  ? 48.763 -6.804  -1.440  1.00 58.06  ?  99  GLY B O     1 
ATOM   3891  N  N     . GLN B  2  68  ? 50.196 -7.946  -2.789  1.00 56.14  ?  100 GLN B N     1 
ATOM   3892  C  CA    . GLN B  2  68  ? 51.450 -7.574  -2.115  1.00 53.04  ?  100 GLN B CA    1 
ATOM   3893  C  C     . GLN B  2  68  ? 52.266 -6.827  -3.147  1.00 54.53  ?  100 GLN B C     1 
ATOM   3894  O  O     . GLN B  2  68  ? 52.274 -7.217  -4.312  1.00 52.54  ?  100 GLN B O     1 
ATOM   3895  C  CB    . GLN B  2  68  ? 52.263 -8.805  -1.643  1.00 49.56  ?  100 GLN B CB    1 
ATOM   3896  C  CG    . GLN B  2  68  ? 51.641 -9.670  -0.531  1.00 46.46  ?  100 GLN B CG    1 
ATOM   3897  C  CD    . GLN B  2  68  ? 51.828 -9.124  0.905   1.00 44.26  ?  100 GLN B CD    1 
ATOM   3898  O  OE1   . GLN B  2  68  ? 52.484 -8.104  1.138   1.00 41.83  ?  100 GLN B OE1   1 
ATOM   3899  N  NE2   . GLN B  2  68  ? 51.248 -9.819  1.871   1.00 41.67  ?  100 GLN B NE2   1 
ATOM   3900  N  N     . GLU B  2  69  ? 52.934 -5.757  -2.730  1.00 59.82  ?  101 GLU B N     1 
ATOM   3901  C  CA    . GLU B  2  69  ? 53.923 -5.094  -3.576  1.00 68.19  ?  101 GLU B CA    1 
ATOM   3902  C  C     . GLU B  2  69  ? 55.322 -5.616  -3.195  1.00 66.44  ?  101 GLU B C     1 
ATOM   3903  O  O     . GLU B  2  69  ? 55.469 -6.345  -2.208  1.00 69.95  ?  101 GLU B O     1 
ATOM   3904  C  CB    . GLU B  2  69  ? 53.802 -3.559  -3.466  1.00 76.39  ?  101 GLU B CB    1 
ATOM   3905  C  CG    . GLU B  2  69  ? 54.741 -2.858  -2.478  1.00 86.15  ?  101 GLU B CG    1 
ATOM   3906  C  CD    . GLU B  2  69  ? 54.607 -3.343  -1.039  1.00 90.83  ?  101 GLU B CD    1 
ATOM   3907  O  OE1   . GLU B  2  69  ? 53.576 -3.966  -0.708  1.00 95.12  ?  101 GLU B OE1   1 
ATOM   3908  O  OE2   . GLU B  2  69  ? 55.540 -3.100  -0.235  1.00 92.46  -1 101 GLU B OE2   1 
ATOM   3909  N  N     . ALA B  2  70  ? 56.336 -5.285  -3.989  1.00 60.29  ?  102 ALA B N     1 
ATOM   3910  C  CA    . ALA B  2  70  ? 57.713 -5.610  -3.614  1.00 58.09  ?  102 ALA B CA    1 
ATOM   3911  C  C     . ALA B  2  70  ? 58.740 -4.747  -4.382  1.00 56.84  ?  102 ALA B C     1 
ATOM   3912  O  O     . ALA B  2  70  ? 58.504 -4.314  -5.508  1.00 60.86  ?  102 ALA B O     1 
ATOM   3913  C  CB    . ALA B  2  70  ? 57.993 -7.119  -3.770  1.00 53.13  ?  102 ALA B CB    1 
ATOM   3914  N  N     . SER B  2  71  ? 59.865 -4.468  -3.734  1.00 54.00  ?  103 SER B N     1 
ATOM   3915  C  CA    . SER B  2  71  ? 60.995 -3.826  -4.379  1.00 49.70  ?  103 SER B CA    1 
ATOM   3916  C  C     . SER B  2  71  ? 61.686 -4.807  -5.268  1.00 47.37  ?  103 SER B C     1 
ATOM   3917  O  O     . SER B  2  71  ? 62.133 -4.447  -6.349  1.00 45.95  ?  103 SER B O     1 
ATOM   3918  C  CB    . SER B  2  71  ? 61.987 -3.339  -3.346  1.00 49.08  ?  103 SER B CB    1 
ATOM   3919  O  OG    . SER B  2  71  ? 61.418 -2.249  -2.658  1.00 51.12  ?  103 SER B OG    1 
ATOM   3920  N  N     . PHE B  2  72  ? 61.774 -6.054  -4.810  1.00 46.12  ?  104 PHE B N     1 
ATOM   3921  C  CA    . PHE B  2  72  ? 62.396 -7.101  -5.621  1.00 44.67  ?  104 PHE B CA    1 
ATOM   3922  C  C     . PHE B  2  72  ? 61.836 -8.544  -5.436  1.00 41.23  ?  104 PHE B C     1 
ATOM   3923  O  O     . PHE B  2  72  ? 60.764 -8.750  -4.851  1.00 38.43  ?  104 PHE B O     1 
ATOM   3924  C  CB    . PHE B  2  72  ? 63.939 -7.009  -5.493  1.00 45.05  ?  104 PHE B CB    1 
ATOM   3925  C  CG    . PHE B  2  72  ? 64.475 -7.134  -4.074  1.00 47.04  ?  104 PHE B CG    1 
ATOM   3926  C  CD1   . PHE B  2  72  ? 64.401 -6.067  -3.174  1.00 47.08  ?  104 PHE B CD1   1 
ATOM   3927  C  CD2   . PHE B  2  72  ? 65.110 -8.308  -3.656  1.00 45.54  ?  104 PHE B CD2   1 
ATOM   3928  C  CE1   . PHE B  2  72  ? 64.921 -6.188  -1.889  1.00 45.53  ?  104 PHE B CE1   1 
ATOM   3929  C  CE2   . PHE B  2  72  ? 65.624 -8.430  -2.371  1.00 44.02  ?  104 PHE B CE2   1 
ATOM   3930  C  CZ    . PHE B  2  72  ? 65.532 -7.368  -1.490  1.00 44.24  ?  104 PHE B CZ    1 
ATOM   3931  N  N     . MET B  2  73  ? 62.537 -9.500  -6.056  1.00 39.43  ?  105 MET B N     1 
ATOM   3932  C  CA    . MET B  2  73  ? 62.304 -10.942 -5.951  1.00 37.43  ?  105 MET B CA    1 
ATOM   3933  C  C     . MET B  2  73  ? 63.676 -11.559 -6.087  1.00 35.44  ?  105 MET B C     1 
ATOM   3934  O  O     . MET B  2  73  ? 64.486 -11.069 -6.881  1.00 33.92  ?  105 MET B O     1 
ATOM   3935  C  CB    . MET B  2  73  ? 61.435 -11.436 -7.102  1.00 38.64  ?  105 MET B CB    1 
ATOM   3936  C  CG    . MET B  2  73  ? 61.274 -12.948 -7.234  1.00 39.51  ?  105 MET B CG    1 
ATOM   3937  S  SD    . MET B  2  73  ? 60.115 -13.421 -8.567  1.00 44.15  ?  105 MET B SD    1 
ATOM   3938  C  CE    . MET B  2  73  ? 58.514 -12.787 -8.041  1.00 41.16  ?  105 MET B CE    1 
ATOM   3939  N  N     . ILE B  2  74  ? 63.941 -12.586 -5.280  1.00 33.27  ?  106 ILE B N     1 
ATOM   3940  C  CA    A ILE B  2  74  ? 65.199 -13.328 -5.260  0.50 33.25  ?  106 ILE B CA    1 
ATOM   3941  C  CA    B ILE B  2  74  ? 65.220 -13.292 -5.364  0.50 32.14  ?  106 ILE B CA    1 
ATOM   3942  C  C     . ILE B  2  74  ? 64.911 -14.677 -5.880  1.00 31.33  ?  106 ILE B C     1 
ATOM   3943  O  O     . ILE B  2  74  ? 63.909 -15.259 -5.554  1.00 30.32  ?  106 ILE B O     1 
ATOM   3944  C  CB    A ILE B  2  74  ? 65.643 -13.558 -3.791  0.50 35.06  ?  106 ILE B CB    1 
ATOM   3945  C  CB    B ILE B  2  74  ? 66.044 -13.312 -4.034  0.50 32.36  ?  106 ILE B CB    1 
ATOM   3946  C  CG1   A ILE B  2  74  ? 66.202 -12.272 -3.177  0.50 35.36  ?  106 ILE B CG1   1 
ATOM   3947  C  CG1   B ILE B  2  74  ? 65.399 -14.168 -2.928  0.50 32.02  ?  106 ILE B CG1   1 
ATOM   3948  C  CG2   A ILE B  2  74  ? 66.665 -14.680 -3.673  0.50 35.44  ?  106 ILE B CG2   1 
ATOM   3949  C  CG2   B ILE B  2  74  ? 66.270 -11.899 -3.501  0.50 32.42  ?  106 ILE B CG2   1 
ATOM   3950  C  CD1   A ILE B  2  74  ? 67.195 -11.591 -4.075  0.50 35.79  ?  106 ILE B CD1   1 
ATOM   3951  C  CD1   B ILE B  2  74  ? 66.249 -14.257 -1.673  0.50 30.67  ?  106 ILE B CD1   1 
ATOM   3952  N  N     . TRP B  2  75  ? 65.785 -15.185 -6.731  1.00 32.18  ?  107 TRP B N     1 
ATOM   3953  C  CA    . TRP B  2  75  ? 65.561 -16.473 -7.386  1.00 34.89  ?  107 TRP B CA    1 
ATOM   3954  C  C     . TRP B  2  75  ? 66.790 -17.375 -7.190  1.00 35.15  ?  107 TRP B C     1 
ATOM   3955  O  O     . TRP B  2  75  ? 67.841 -17.123 -7.783  1.00 37.35  ?  107 TRP B O     1 
ATOM   3956  C  CB    . TRP B  2  75  ? 65.277 -16.211 -8.872  1.00 37.46  ?  107 TRP B CB    1 
ATOM   3957  C  CG    . TRP B  2  75  ? 65.058 -17.407 -9.700  1.00 42.27  ?  107 TRP B CG    1 
ATOM   3958  C  CD1   . TRP B  2  75  ? 64.804 -18.666 -9.260  1.00 46.93  ?  107 TRP B CD1   1 
ATOM   3959  C  CD2   . TRP B  2  75  ? 65.022 -17.462 -11.125 1.00 45.71  ?  107 TRP B CD2   1 
ATOM   3960  N  NE1   . TRP B  2  75  ? 64.634 -19.513 -10.322 1.00 50.25  ?  107 TRP B NE1   1 
ATOM   3961  C  CE2   . TRP B  2  75  ? 64.761 -18.799 -11.484 1.00 48.52  ?  107 TRP B CE2   1 
ATOM   3962  C  CE3   . TRP B  2  75  ? 65.182 -16.512 -12.136 1.00 50.29  ?  107 TRP B CE3   1 
ATOM   3963  C  CZ2   . TRP B  2  75  ? 64.658 -19.223 -12.828 1.00 49.72  ?  107 TRP B CZ2   1 
ATOM   3964  C  CZ3   . TRP B  2  75  ? 65.084 -16.930 -13.471 1.00 51.76  ?  107 TRP B CZ3   1 
ATOM   3965  C  CH2   . TRP B  2  75  ? 64.821 -18.281 -13.799 1.00 50.39  ?  107 TRP B CH2   1 
ATOM   3966  N  N     . THR B  2  76  ? 66.694 -18.418 -6.363  1.00 33.25  ?  108 THR B N     1 
ATOM   3967  C  CA    . THR B  2  76  ? 67.910 -19.212 -6.064  1.00 33.31  ?  108 THR B CA    1 
ATOM   3968  C  C     . THR B  2  76  ? 68.060 -20.571 -6.850  1.00 34.81  ?  108 THR B C     1 
ATOM   3969  O  O     . THR B  2  76  ? 68.154 -21.653 -6.234  1.00 35.18  ?  108 THR B O     1 
ATOM   3970  C  CB    . THR B  2  76  ? 68.084 -19.418 -4.549  1.00 30.00  ?  108 THR B CB    1 
ATOM   3971  O  OG1   . THR B  2  76  ? 66.952 -20.118 -4.067  1.00 29.17  ?  108 THR B OG1   1 
ATOM   3972  C  CG2   . THR B  2  76  ? 68.202 -18.080 -3.814  1.00 28.78  ?  108 THR B CG2   1 
ATOM   3973  N  N     . GLY B  2  77  ? 68.063 -20.486 -8.195  1.00 32.43  ?  109 GLY B N     1 
ATOM   3974  C  CA    . GLY B  2  77  ? 68.529 -21.560 -9.074  1.00 30.45  ?  109 GLY B CA    1 
ATOM   3975  C  C     . GLY B  2  77  ? 67.650 -22.788 -9.281  1.00 30.01  ?  109 GLY B C     1 
ATOM   3976  O  O     . GLY B  2  77  ? 66.443 -22.769 -8.989  1.00 31.06  ?  109 GLY B O     1 
ATOM   3977  N  N     . ASP B  2  78  ? 68.297 -23.853 -9.787  1.00 29.30  ?  110 ASP B N     1 
ATOM   3978  C  CA    . ASP B  2  78  ? 67.700 -25.197 -10.086 1.00 29.45  ?  110 ASP B CA    1 
ATOM   3979  C  C     . ASP B  2  78  ? 66.440 -25.157 -10.942 1.00 28.60  ?  110 ASP B C     1 
ATOM   3980  O  O     . ASP B  2  78  ? 65.339 -25.284 -10.419 1.00 29.02  ?  110 ASP B O     1 
ATOM   3981  C  CB    . ASP B  2  78  ? 67.402 -25.986 -8.793  1.00 29.19  ?  110 ASP B CB    1 
ATOM   3982  C  CG    . ASP B  2  78  ? 68.581 -26.831 -8.312  1.00 28.28  ?  110 ASP B CG    1 
ATOM   3983  O  OD1   . ASP B  2  78  ? 69.702 -26.631 -8.798  1.00 29.81  ?  110 ASP B OD1   1 
ATOM   3984  O  OD2   . ASP B  2  78  ? 68.393 -27.669 -7.415  1.00 25.29  -1 110 ASP B OD2   1 
ATOM   3985  N  N     . SER B  2  79  ? 66.605 -24.951 -12.246 1.00 27.78  ?  111 SER B N     1 
ATOM   3986  C  CA    . SER B  2  79  ? 65.470 -24.901 -13.173 1.00 27.11  ?  111 SER B CA    1 
ATOM   3987  C  C     . SER B  2  79  ? 65.211 -26.189 -13.998 1.00 26.43  ?  111 SER B C     1 
ATOM   3988  O  O     . SER B  2  79  ? 64.043 -26.604 -14.078 1.00 27.48  ?  111 SER B O     1 
ATOM   3989  C  CB    . SER B  2  79  ? 65.497 -23.619 -14.027 1.00 27.98  ?  111 SER B CB    1 
ATOM   3990  O  OG    . SER B  2  79  ? 65.100 -22.465 -13.269 1.00 28.47  ?  111 SER B OG    1 
ATOM   3991  N  N     A PRO B  2  80  ? 66.265 -26.823 -14.564 0.50 25.41  ?  112 PRO B N     1 
ATOM   3992  N  N     B PRO B  2  80  ? 66.254 -26.817 -14.597 0.50 25.32  ?  112 PRO B N     1 
ATOM   3993  C  CA    A PRO B  2  80  ? 66.104 -28.147 -15.147 0.50 25.87  ?  112 PRO B CA    1 
ATOM   3994  C  CA    B PRO B  2  80  ? 65.917 -28.083 -15.232 0.50 25.92  ?  112 PRO B CA    1 
ATOM   3995  C  C     A PRO B  2  80  ? 65.582 -29.172 -14.143 0.50 27.87  ?  112 PRO B C     1 
ATOM   3996  C  C     B PRO B  2  80  ? 65.595 -29.158 -14.202 0.50 27.92  ?  112 PRO B C     1 
ATOM   3997  O  O     A PRO B  2  80  ? 65.830 -29.047 -12.950 0.50 28.47  ?  112 PRO B O     1 
ATOM   3998  O  O     B PRO B  2  80  ? 66.004 -29.057 -13.050 0.50 28.67  ?  112 PRO B O     1 
ATOM   3999  C  CB    A PRO B  2  80  ? 67.522 -28.511 -15.548 0.50 24.72  ?  112 PRO B CB    1 
ATOM   4000  C  CB    B PRO B  2  80  ? 67.175 -28.444 -16.000 0.50 24.82  ?  112 PRO B CB    1 
ATOM   4001  C  CG    A PRO B  2  80  ? 68.119 -27.214 -15.888 0.50 24.94  ?  112 PRO B CG    1 
ATOM   4002  C  CG    B PRO B  2  80  ? 68.246 -27.823 -15.233 0.50 24.47  ?  112 PRO B CG    1 
ATOM   4003  C  CD    A PRO B  2  80  ? 67.624 -26.321 -14.800 0.50 24.90  ?  112 PRO B CD    1 
ATOM   4004  C  CD    B PRO B  2  80  ? 67.696 -26.553 -14.675 0.50 24.71  ?  112 PRO B CD    1 
ATOM   4005  N  N     . PRO B  2  81  ? 64.885 -30.202 -14.627 1.00 29.86  ?  113 PRO B N     1 
ATOM   4006  C  CA    . PRO B  2  81  ? 64.349 -31.237 -13.741 1.00 31.16  ?  113 PRO B CA    1 
ATOM   4007  C  C     . PRO B  2  81  ? 65.370 -32.299 -13.270 1.00 32.00  ?  113 PRO B C     1 
ATOM   4008  O  O     . PRO B  2  81  ? 66.568 -32.199 -13.553 1.00 31.57  ?  113 PRO B O     1 
ATOM   4009  C  CB    . PRO B  2  81  ? 63.292 -31.909 -14.628 1.00 32.89  ?  113 PRO B CB    1 
ATOM   4010  C  CG    . PRO B  2  81  ? 63.850 -31.786 -16.021 1.00 32.99  ?  113 PRO B CG    1 
ATOM   4011  C  CD    . PRO B  2  81  ? 64.707 -30.541 -16.057 1.00 31.43  ?  113 PRO B CD    1 
ATOM   4012  N  N     . HIS B  2  82  ? 64.871 -33.308 -12.555 1.00 32.30  ?  114 HIS B N     1 
ATOM   4013  C  CA    . HIS B  2  82  ? 65.678 -34.425 -12.091 1.00 32.25  ?  114 HIS B CA    1 
ATOM   4014  C  C     . HIS B  2  82  ? 65.442 -35.579 -13.023 1.00 31.53  ?  114 HIS B C     1 
ATOM   4015  O  O     . HIS B  2  82  ? 64.561 -36.411 -12.816 1.00 29.64  ?  114 HIS B O     1 
ATOM   4016  C  CB    . HIS B  2  82  ? 65.312 -34.821 -10.657 1.00 33.61  ?  114 HIS B CB    1 
ATOM   4017  C  CG    . HIS B  2  82  ? 65.492 -33.715 -9.675  1.00 34.48  ?  114 HIS B CG    1 
ATOM   4018  N  ND1   . HIS B  2  82  ? 64.584 -32.686 -9.545  1.00 36.65  ?  114 HIS B ND1   1 
ATOM   4019  C  CD2   . HIS B  2  82  ? 66.493 -33.448 -8.804  1.00 35.58  ?  114 HIS B CD2   1 
ATOM   4020  C  CE1   . HIS B  2  82  ? 65.018 -31.832 -8.632  1.00 36.84  ?  114 HIS B CE1   1 
ATOM   4021  N  NE2   . HIS B  2  82  ? 66.175 -32.271 -8.167  1.00 35.98  ?  114 HIS B NE2   1 
ATOM   4022  N  N     . VAL B  2  83  ? 66.229 -35.596 -14.079 1.00 32.75  ?  115 VAL B N     1 
ATOM   4023  C  CA    . VAL B  2  83  ? 66.311 -36.752 -14.944 1.00 35.59  ?  115 VAL B CA    1 
ATOM   4024  C  C     . VAL B  2  83  ? 67.796 -37.061 -15.200 1.00 37.26  ?  115 VAL B C     1 
ATOM   4025  O  O     . VAL B  2  83  ? 68.663 -36.183 -15.018 1.00 35.35  ?  115 VAL B O     1 
ATOM   4026  C  CB    . VAL B  2  83  ? 65.543 -36.528 -16.258 1.00 35.76  ?  115 VAL B CB    1 
ATOM   4027  C  CG1   . VAL B  2  83  ? 64.062 -36.298 -15.991 1.00 34.09  ?  115 VAL B CG1   1 
ATOM   4028  C  CG2   . VAL B  2  83  ? 66.135 -35.353 -17.016 1.00 37.23  ?  115 VAL B CG2   1 
ATOM   4029  N  N     . PRO B  2  84  ? 68.102 -38.313 -15.597 1.00 39.87  ?  116 PRO B N     1 
ATOM   4030  C  CA    . PRO B  2  84  ? 69.514 -38.703 -15.773 1.00 41.01  ?  116 PRO B CA    1 
ATOM   4031  C  C     . PRO B  2  84  ? 70.217 -37.888 -16.864 1.00 43.53  ?  116 PRO B C     1 
ATOM   4032  O  O     . PRO B  2  84  ? 69.572 -37.504 -17.850 1.00 43.30  ?  116 PRO B O     1 
ATOM   4033  C  CB    . PRO B  2  84  ? 69.432 -40.181 -16.159 1.00 40.47  ?  116 PRO B CB    1 
ATOM   4034  C  CG    . PRO B  2  84  ? 68.072 -40.633 -15.716 1.00 40.50  ?  116 PRO B CG    1 
ATOM   4035  C  CD    . PRO B  2  84  ? 67.178 -39.440 -15.827 1.00 39.26  ?  116 PRO B CD    1 
ATOM   4036  N  N     . VAL B  2  85  ? 71.515 -37.626 -16.669 1.00 45.35  ?  117 VAL B N     1 
ATOM   4037  C  CA    . VAL B  2  85  ? 72.308 -36.729 -17.537 1.00 45.75  ?  117 VAL B CA    1 
ATOM   4038  C  C     . VAL B  2  85  ? 72.215 -37.026 -19.043 1.00 47.55  ?  117 VAL B C     1 
ATOM   4039  O  O     . VAL B  2  85  ? 72.054 -36.090 -19.830 1.00 49.40  ?  117 VAL B O     1 
ATOM   4040  C  CB    . VAL B  2  85  ? 73.798 -36.723 -17.134 1.00 46.50  ?  117 VAL B CB    1 
ATOM   4041  C  CG1   . VAL B  2  85  ? 74.659 -36.046 -18.203 1.00 47.06  ?  117 VAL B CG1   1 
ATOM   4042  C  CG2   . VAL B  2  85  ? 73.982 -36.056 -15.778 1.00 46.11  ?  117 VAL B CG2   1 
ATOM   4043  N  N     . PRO B  2  86  ? 72.347 -38.313 -19.456 1.00 48.62  ?  118 PRO B N     1 
ATOM   4044  C  CA    . PRO B  2  86  ? 72.133 -38.679 -20.874 1.00 47.73  ?  118 PRO B CA    1 
ATOM   4045  C  C     . PRO B  2  86  ? 70.741 -38.369 -21.461 1.00 46.82  ?  118 PRO B C     1 
ATOM   4046  O  O     . PRO B  2  86  ? 70.580 -38.418 -22.680 1.00 49.75  ?  118 PRO B O     1 
ATOM   4047  C  CB    . PRO B  2  86  ? 72.385 -40.198 -20.900 1.00 47.53  ?  118 PRO B CB    1 
ATOM   4048  C  CG    . PRO B  2  86  ? 72.584 -40.628 -19.477 1.00 46.98  ?  118 PRO B CG    1 
ATOM   4049  C  CD    . PRO B  2  86  ? 73.002 -39.412 -18.719 1.00 48.23  ?  118 PRO B CD    1 
ATOM   4050  N  N     . GLU B  2  87  ? 69.751 -38.088 -20.615 1.00 47.50  ?  119 GLU B N     1 
ATOM   4051  C  CA    . GLU B  2  87  ? 68.422 -37.696 -21.083 1.00 47.36  ?  119 GLU B CA    1 
ATOM   4052  C  C     . GLU B  2  87  ? 68.334 -36.198 -21.324 1.00 47.10  ?  119 GLU B C     1 
ATOM   4053  O  O     . GLU B  2  87  ? 67.368 -35.747 -21.931 1.00 47.35  ?  119 GLU B O     1 
ATOM   4054  C  CB    . GLU B  2  87  ? 67.340 -38.125 -20.088 1.00 48.90  ?  119 GLU B CB    1 
ATOM   4055  C  CG    . GLU B  2  87  ? 66.099 -38.680 -20.772 1.00 53.30  ?  119 GLU B CG    1 
ATOM   4056  C  CD    . GLU B  2  87  ? 64.947 -39.006 -19.823 1.00 55.53  ?  119 GLU B CD    1 
ATOM   4057  O  OE1   . GLU B  2  87  ? 63.778 -38.839 -20.256 1.00 57.16  ?  119 GLU B OE1   1 
ATOM   4058  O  OE2   . GLU B  2  87  ? 65.195 -39.426 -18.665 1.00 51.08  -1 119 GLU B OE2   1 
ATOM   4059  N  N     . LEU B  2  88  ? 69.341 -35.446 -20.859 1.00 46.43  ?  120 LEU B N     1 
ATOM   4060  C  CA    . LEU B  2  88  ? 69.388 -33.972 -20.976 1.00 48.44  ?  120 LEU B CA    1 
ATOM   4061  C  C     . LEU B  2  88  ? 70.607 -33.431 -21.740 1.00 45.19  ?  120 LEU B C     1 
ATOM   4062  O  O     . LEU B  2  88  ? 71.517 -34.159 -22.073 1.00 45.98  ?  120 LEU B O     1 
ATOM   4063  C  CB    . LEU B  2  88  ? 69.421 -33.325 -19.577 1.00 50.98  ?  120 LEU B CB    1 
ATOM   4064  C  CG    . LEU B  2  88  ? 68.260 -33.439 -18.587 1.00 48.42  ?  120 LEU B CG    1 
ATOM   4065  C  CD1   . LEU B  2  88  ? 68.757 -32.819 -17.287 1.00 48.38  ?  120 LEU B CD1   1 
ATOM   4066  C  CD2   . LEU B  2  88  ? 66.966 -32.778 -19.072 1.00 47.57  ?  120 LEU B CD2   1 
ATOM   4067  N  N     . SER B  2  89  ? 70.621 -32.126 -21.964 1.00 43.85  ?  121 SER B N     1 
ATOM   4068  C  CA    . SER B  2  89  ? 71.786 -31.436 -22.488 1.00 44.77  ?  121 SER B CA    1 
ATOM   4069  C  C     . SER B  2  89  ? 71.855 -29.936 -22.038 1.00 47.95  ?  121 SER B C     1 
ATOM   4070  O  O     . SER B  2  89  ? 70.897 -29.365 -21.450 1.00 48.68  ?  121 SER B O     1 
ATOM   4071  C  CB    . SER B  2  89  ? 71.774 -31.535 -24.010 1.00 43.54  ?  121 SER B CB    1 
ATOM   4072  O  OG    . SER B  2  89  ? 70.925 -30.556 -24.587 1.00 40.32  ?  121 SER B OG    1 
ATOM   4073  N  N     . THR B  2  90  ? 73.010 -29.325 -22.316 1.00 44.32  ?  122 THR B N     1 
ATOM   4074  C  CA    . THR B  2  90  ? 73.221 -27.869 -22.243 1.00 40.83  ?  122 THR B CA    1 
ATOM   4075  C  C     . THR B  2  90  ? 72.118 -27.065 -22.931 1.00 42.80  ?  122 THR B C     1 
ATOM   4076  O  O     . THR B  2  90  ? 71.623 -26.046 -22.427 1.00 38.22  ?  122 THR B O     1 
ATOM   4077  C  CB    . THR B  2  90  ? 74.548 -27.532 -22.950 1.00 38.12  ?  122 THR B CB    1 
ATOM   4078  O  OG1   . THR B  2  90  ? 75.621 -27.856 -22.077 1.00 34.15  ?  122 THR B OG1   1 
ATOM   4079  C  CG2   . THR B  2  90  ? 74.652 -26.080 -23.340 1.00 37.41  ?  122 THR B CG2   1 
ATOM   4080  N  N     . ASP B  2  91  ? 71.776 -27.517 -24.124 1.00 47.32  ?  123 ASP B N     1 
ATOM   4081  C  CA    . ASP B  2  91  ? 70.696 -26.895 -24.866 1.00 50.30  ?  123 ASP B CA    1 
ATOM   4082  C  C     . ASP B  2  91  ? 69.369 -27.027 -24.124 1.00 48.40  ?  123 ASP B C     1 
ATOM   4083  O  O     . ASP B  2  91  ? 68.655 -26.044 -24.014 1.00 48.16  ?  123 ASP B O     1 
ATOM   4084  C  CB    . ASP B  2  91  ? 70.589 -27.445 -26.307 1.00 51.20  ?  123 ASP B CB    1 
ATOM   4085  C  CG    . ASP B  2  91  ? 71.388 -26.618 -27.314 1.00 48.06  ?  123 ASP B CG    1 
ATOM   4086  O  OD1   . ASP B  2  91  ? 72.599 -26.365 -27.053 1.00 46.27  ?  123 ASP B OD1   1 
ATOM   4087  O  OD2   . ASP B  2  91  ? 70.781 -26.229 -28.345 1.00 44.08  -1 123 ASP B OD2   1 
ATOM   4088  N  N     . THR B  2  92  ? 69.032 -28.205 -23.602 1.00 46.92  ?  124 THR B N     1 
ATOM   4089  C  CA    . THR B  2  92  ? 67.764 -28.315 -22.890 1.00 51.10  ?  124 THR B CA    1 
ATOM   4090  C  C     . THR B  2  92  ? 67.853 -27.458 -21.630 1.00 54.40  ?  124 THR B C     1 
ATOM   4091  O  O     . THR B  2  92  ? 66.926 -26.673 -21.350 1.00 56.39  ?  124 THR B O     1 
ATOM   4092  C  CB    . THR B  2  92  ? 67.365 -29.758 -22.528 1.00 52.48  ?  124 THR B CB    1 
ATOM   4093  O  OG1   . THR B  2  92  ? 68.033 -30.673 -23.393 1.00 54.46  ?  124 THR B OG1   1 
ATOM   4094  C  CG2   . THR B  2  92  ? 65.822 -29.956 -22.651 1.00 52.65  ?  124 THR B CG2   1 
ATOM   4095  N  N     . VAL B  2  93  ? 68.966 -27.591 -20.895 1.00 52.03  ?  125 VAL B N     1 
ATOM   4096  C  CA    . VAL B  2  93  ? 69.221 -26.792 -19.672 1.00 50.61  ?  125 VAL B CA    1 
ATOM   4097  C  C     . VAL B  2  93  ? 68.877 -25.284 -19.869 1.00 48.42  ?  125 VAL B C     1 
ATOM   4098  O  O     . VAL B  2  93  ? 68.101 -24.686 -19.088 1.00 44.77  ?  125 VAL B O     1 
ATOM   4099  C  CB    . VAL B  2  93  ? 70.692 -27.012 -19.194 1.00 51.48  ?  125 VAL B CB    1 
ATOM   4100  C  CG1   . VAL B  2  93  ? 71.248 -25.838 -18.391 1.00 53.79  ?  125 VAL B CG1   1 
ATOM   4101  C  CG2   . VAL B  2  93  ? 70.793 -28.286 -18.382 1.00 49.48  ?  125 VAL B CG2   1 
ATOM   4102  N  N     . ILE B  2  94  ? 69.435 -24.704 -20.934 1.00 43.02  ?  126 ILE B N     1 
ATOM   4103  C  CA    . ILE B  2  94  ? 69.266 -23.291 -21.243 1.00 39.81  ?  126 ILE B CA    1 
ATOM   4104  C  C     . ILE B  2  94  ? 67.879 -23.014 -21.822 1.00 38.34  ?  126 ILE B C     1 
ATOM   4105  O  O     . ILE B  2  94  ? 67.282 -21.969 -21.593 1.00 33.93  ?  126 ILE B O     1 
ATOM   4106  C  CB    . ILE B  2  94  ? 70.359 -22.831 -22.223 1.00 40.29  ?  126 ILE B CB    1 
ATOM   4107  C  CG1   . ILE B  2  94  ? 71.729 -22.943 -21.569 1.00 41.76  ?  126 ILE B CG1   1 
ATOM   4108  C  CG2   . ILE B  2  94  ? 70.155 -21.383 -22.656 1.00 40.04  ?  126 ILE B CG2   1 
ATOM   4109  C  CD1   . ILE B  2  94  ? 72.883 -22.783 -22.536 1.00 41.59  ?  126 ILE B CD1   1 
ATOM   4110  N  N     . ASN B  2  95  ? 67.360 -23.947 -22.598 1.00 41.40  ?  127 ASN B N     1 
ATOM   4111  C  CA    . ASN B  2  95  ? 65.979 -23.843 -23.004 1.00 44.01  ?  127 ASN B CA    1 
ATOM   4112  C  C     . ASN B  2  95  ? 65.197 -23.593 -21.760 1.00 43.55  ?  127 ASN B C     1 
ATOM   4113  O  O     . ASN B  2  95  ? 64.477 -22.604 -21.690 1.00 42.96  ?  127 ASN B O     1 
ATOM   4114  C  CB    . ASN B  2  95  ? 65.469 -25.130 -23.638 1.00 49.29  ?  127 ASN B CB    1 
ATOM   4115  C  CG    . ASN B  2  95  ? 66.102 -25.417 -24.984 1.00 53.29  ?  127 ASN B CG    1 
ATOM   4116  O  OD1   . ASN B  2  95  ? 66.432 -24.501 -25.766 1.00 56.88  ?  127 ASN B OD1   1 
ATOM   4117  N  ND2   . ASN B  2  95  ? 66.267 -26.707 -25.270 1.00 52.81  ?  127 ASN B ND2   1 
ATOM   4118  N  N     . VAL B  2  96  ? 65.381 -24.476 -20.768 1.00 43.74  ?  128 VAL B N     1 
ATOM   4119  C  CA    . VAL B  2  96  ? 64.650 -24.390 -19.495 1.00 42.94  ?  128 VAL B CA    1 
ATOM   4120  C  C     . VAL B  2  96  ? 64.895 -23.105 -18.671 1.00 43.42  ?  128 VAL B C     1 
ATOM   4121  O  O     . VAL B  2  96  ? 63.907 -22.516 -18.207 1.00 45.40  ?  128 VAL B O     1 
ATOM   4122  C  CB    . VAL B  2  96  ? 64.846 -25.632 -18.617 1.00 39.75  ?  128 VAL B CB    1 
ATOM   4123  C  CG1   . VAL B  2  96  ? 64.264 -25.388 -17.232 1.00 39.91  ?  128 VAL B CG1   1 
ATOM   4124  C  CG2   . VAL B  2  96  ? 64.155 -26.821 -19.261 1.00 39.84  ?  128 VAL B CG2   1 
ATOM   4125  N  N     . ILE B  2  97  ? 66.149 -22.659 -18.496 1.00 39.68  ?  129 ILE B N     1 
ATOM   4126  C  CA    . ILE B  2  97  ? 66.409 -21.376 -17.789 1.00 39.13  ?  129 ILE B CA    1 
ATOM   4127  C  C     . ILE B  2  97  ? 65.818 -20.142 -18.523 1.00 41.69  ?  129 ILE B C     1 
ATOM   4128  O  O     . ILE B  2  97  ? 65.349 -19.167 -17.898 1.00 41.48  ?  129 ILE B O     1 
ATOM   4129  C  CB    . ILE B  2  97  ? 67.912 -21.122 -17.558 1.00 38.21  ?  129 ILE B CB    1 
ATOM   4130  C  CG1   . ILE B  2  97  ? 68.520 -22.256 -16.757 1.00 39.89  ?  129 ILE B CG1   1 
ATOM   4131  C  CG2   . ILE B  2  97  ? 68.145 -19.801 -16.811 1.00 37.77  ?  129 ILE B CG2   1 
ATOM   4132  C  CD1   . ILE B  2  97  ? 70.005 -22.087 -16.480 1.00 42.04  ?  129 ILE B CD1   1 
ATOM   4133  N  N     . THR B  2  98  ? 65.870 -20.174 -19.852 1.00 43.15  ?  130 THR B N     1 
ATOM   4134  C  CA    . THR B  2  98  ? 65.321 -19.099 -20.669 1.00 41.60  ?  130 THR B CA    1 
ATOM   4135  C  C     . THR B  2  98  ? 63.826 -19.024 -20.434 1.00 39.40  ?  130 THR B C     1 
ATOM   4136  O  O     . THR B  2  98  ? 63.311 -17.936 -20.260 1.00 36.54  ?  130 THR B O     1 
ATOM   4137  C  CB    . THR B  2  98  ? 65.578 -19.332 -22.183 1.00 42.18  ?  130 THR B CB    1 
ATOM   4138  O  OG1   . THR B  2  98  ? 66.985 -19.505 -22.427 1.00 40.45  ?  130 THR B OG1   1 
ATOM   4139  C  CG2   . THR B  2  98  ? 65.022 -18.164 -23.023 1.00 39.79  ?  130 THR B CG2   1 
ATOM   4140  N  N     . ASN B  2  99  ? 63.150 -20.183 -20.423 1.00 39.54  ?  131 ASN B N     1 
ATOM   4141  C  CA    . ASN B  2  99  ? 61.689 -20.240 -20.260 1.00 41.45  ?  131 ASN B CA    1 
ATOM   4142  C  C     . ASN B  2  99  ? 61.286 -19.632 -18.929 1.00 42.35  ?  131 ASN B C     1 
ATOM   4143  O  O     . ASN B  2  99  ? 60.426 -18.745 -18.893 1.00 42.32  ?  131 ASN B O     1 
ATOM   4144  C  CB    . ASN B  2  99  ? 61.133 -21.672 -20.412 1.00 44.74  ?  131 ASN B CB    1 
ATOM   4145  C  CG    . ASN B  2  99  ? 59.597 -21.710 -20.467 1.00 50.38  ?  131 ASN B CG    1 
ATOM   4146  O  OD1   . ASN B  2  99  ? 58.959 -21.383 -19.469 1.00 57.17  ?  131 ASN B OD1   1 
ATOM   4147  N  ND2   . ASN B  2  99  ? 58.990 -22.107 -21.632 1.00 52.32  ?  131 ASN B ND2   1 
ATOM   4148  N  N     . MET B  2  100 ? 61.933 -20.086 -17.847 1.00 43.60  ?  132 MET B N     1 
ATOM   4149  C  CA    . MET B  2  100 ? 61.792 -19.480 -16.491 1.00 41.68  ?  132 MET B CA    1 
ATOM   4150  C  C     . MET B  2  100 ? 62.102 -17.979 -16.474 1.00 38.44  ?  132 MET B C     1 
ATOM   4151  O  O     . MET B  2  100 ? 61.364 -17.208 -15.847 1.00 36.00  ?  132 MET B O     1 
ATOM   4152  C  CB    . MET B  2  100 ? 62.671 -20.204 -15.435 1.00 40.63  ?  132 MET B CB    1 
ATOM   4153  C  CG    . MET B  2  100 ? 62.242 -21.638 -15.138 1.00 40.06  ?  132 MET B CG    1 
ATOM   4154  S  SD    . MET B  2  100 ? 60.537 -21.787 -14.525 1.00 40.66  ?  132 MET B SD    1 
ATOM   4155  C  CE    . MET B  2  100 ? 59.550 -22.212 -15.955 1.00 38.57  ?  132 MET B CE    1 
ATOM   4156  N  N     . THR B  2  101 ? 63.172 -17.577 -17.166 1.00 36.26  ?  133 THR B N     1 
ATOM   4157  C  CA    . THR B  2  101 ? 63.567 -16.174 -17.195 1.00 38.16  ?  133 THR B CA    1 
ATOM   4158  C  C     . THR B  2  101 ? 62.562 -15.263 -17.977 1.00 43.03  ?  133 THR B C     1 
ATOM   4159  O  O     . THR B  2  101 ? 62.172 -14.180 -17.499 1.00 42.07  ?  133 THR B O     1 
ATOM   4160  C  CB    . THR B  2  101 ? 65.005 -16.000 -17.709 1.00 36.89  ?  133 THR B CB    1 
ATOM   4161  O  OG1   . THR B  2  101 ? 65.918 -16.834 -16.969 1.00 34.85  ?  133 THR B OG1   1 
ATOM   4162  C  CG2   . THR B  2  101 ? 65.424 -14.557 -17.541 1.00 37.23  ?  133 THR B CG2   1 
ATOM   4163  N  N     . THR B  2  102 ? 62.124 -15.701 -19.157 1.00 49.67  ?  134 THR B N     1 
ATOM   4164  C  CA    . THR B  2  102 ? 61.070 -14.980 -19.896 1.00 51.49  ?  134 THR B CA    1 
ATOM   4165  C  C     . THR B  2  102 ? 59.773 -14.879 -19.073 1.00 55.76  ?  134 THR B C     1 
ATOM   4166  O  O     . THR B  2  102 ? 59.343 -13.773 -18.755 1.00 58.88  ?  134 THR B O     1 
ATOM   4167  C  CB    . THR B  2  102 ? 60.788 -15.607 -21.277 1.00 49.04  ?  134 THR B CB    1 
ATOM   4168  O  OG1   . THR B  2  102 ? 62.029 -15.760 -21.972 1.00 45.55  ?  134 THR B OG1   1 
ATOM   4169  C  CG2   . THR B  2  102 ? 59.831 -14.718 -22.107 1.00 47.34  ?  134 THR B CG2   1 
ATOM   4170  N  N     . THR B  2  103 ? 59.178 -16.016 -18.703 1.00 56.14  ?  135 THR B N     1 
ATOM   4171  C  CA    . THR B  2  103 ? 57.978 -16.025 -17.835 1.00 57.90  ?  135 THR B CA    1 
ATOM   4172  C  C     . THR B  2  103 ? 58.042 -15.043 -16.632 1.00 54.80  ?  135 THR B C     1 
ATOM   4173  O  O     . THR B  2  103 ? 57.054 -14.318 -16.358 1.00 47.70  ?  135 THR B O     1 
ATOM   4174  C  CB    . THR B  2  103 ? 57.679 -17.444 -17.293 1.00 60.09  ?  135 THR B CB    1 
ATOM   4175  O  OG1   . THR B  2  103 ? 57.863 -18.404 -18.337 1.00 65.29  ?  135 THR B OG1   1 
ATOM   4176  C  CG2   . THR B  2  103 ? 56.235 -17.551 -16.772 1.00 60.36  ?  135 THR B CG2   1 
ATOM   4177  N  N     . ILE B  2  104 ? 59.178 -15.026 -15.918 1.00 53.11  ?  136 ILE B N     1 
ATOM   4178  C  CA    . ILE B  2  104 ? 59.362 -14.065 -14.807 1.00 53.93  ?  136 ILE B CA    1 
ATOM   4179  C  C     . ILE B  2  104 ? 59.363 -12.658 -15.413 1.00 53.64  ?  136 ILE B C     1 
ATOM   4180  O  O     . ILE B  2  104 ? 58.653 -11.775 -14.903 1.00 54.99  ?  136 ILE B O     1 
ATOM   4181  C  CB    . ILE B  2  104 ? 60.621 -14.327 -13.892 1.00 50.88  ?  136 ILE B CB    1 
ATOM   4182  C  CG1   . ILE B  2  104 ? 60.470 -15.648 -13.116 1.00 48.48  ?  136 ILE B CG1   1 
ATOM   4183  C  CG2   . ILE B  2  104 ? 60.850 -13.178 -12.892 1.00 47.35  ?  136 ILE B CG2   1 
ATOM   4184  C  CD1   . ILE B  2  104 ? 61.771 -16.208 -12.580 1.00 47.65  ?  136 ILE B CD1   1 
ATOM   4185  N  N     . GLN B  2  105 ? 60.105 -12.469 -16.513 1.00 48.39  ?  137 GLN B N     1 
ATOM   4186  C  CA    . GLN B  2  105 ? 60.214 -11.139 -17.140 1.00 49.26  ?  137 GLN B CA    1 
ATOM   4187  C  C     . GLN B  2  105 ? 58.930 -10.584 -17.850 1.00 49.88  ?  137 GLN B C     1 
ATOM   4188  O  O     . GLN B  2  105 ? 58.763 -9.367  -17.913 1.00 49.26  ?  137 GLN B O     1 
ATOM   4189  C  CB    . GLN B  2  105 ? 61.421 -11.077 -18.088 1.00 48.10  ?  137 GLN B CB    1 
ATOM   4190  C  CG    . GLN B  2  105 ? 62.777 -10.943 -17.411 1.00 47.53  ?  137 GLN B CG    1 
ATOM   4191  C  CD    . GLN B  2  105 ? 63.947 -10.885 -18.401 1.00 49.29  ?  137 GLN B CD    1 
ATOM   4192  O  OE1   . GLN B  2  105 ? 63.756 -10.795 -19.603 1.00 43.54  ?  137 GLN B OE1   1 
ATOM   4193  N  NE2   . GLN B  2  105 ? 65.172 -10.946 -17.885 1.00 54.31  ?  137 GLN B NE2   1 
ATOM   4194  N  N     . SER B  2  106 ? 58.052 -11.451 -18.377 1.00 53.16  ?  138 SER B N     1 
ATOM   4195  C  CA    . SER B  2  106 ? 56.775 -11.027 -19.011 1.00 52.06  ?  138 SER B CA    1 
ATOM   4196  C  C     . SER B  2  106 ? 55.651 -10.815 -18.018 1.00 54.76  ?  138 SER B C     1 
ATOM   4197  O  O     . SER B  2  106 ? 54.908 -9.842  -18.148 1.00 61.77  ?  138 SER B O     1 
ATOM   4198  C  CB    . SER B  2  106 ? 56.302 -12.029 -20.050 1.00 51.22  ?  138 SER B CB    1 
ATOM   4199  O  OG    . SER B  2  106 ? 57.028 -11.839 -21.242 1.00 56.23  ?  138 SER B OG    1 
ATOM   4200  N  N     . LEU B  2  107 ? 55.502 -11.731 -17.052 1.00 53.33  ?  139 LEU B N     1 
ATOM   4201  C  CA    . LEU B  2  107 ? 54.544 -11.545 -15.956 1.00 49.13  ?  139 LEU B CA    1 
ATOM   4202  C  C     . LEU B  2  107 ? 54.948 -10.387 -15.036 1.00 48.86  ?  139 LEU B C     1 
ATOM   4203  O  O     . LEU B  2  107 ? 54.068 -9.691  -14.520 1.00 48.86  ?  139 LEU B O     1 
ATOM   4204  C  CB    . LEU B  2  107 ? 54.364 -12.833 -15.151 1.00 48.16  ?  139 LEU B CB    1 
ATOM   4205  C  CG    . LEU B  2  107 ? 53.358 -13.831 -15.742 1.00 51.09  ?  139 LEU B CG    1 
ATOM   4206  C  CD1   . LEU B  2  107 ? 53.521 -15.176 -15.056 1.00 52.03  ?  139 LEU B CD1   1 
ATOM   4207  C  CD2   . LEU B  2  107 ? 51.895 -13.378 -15.655 1.00 50.23  ?  139 LEU B CD2   1 
ATOM   4208  N  N     . PHE B  2  108 ? 56.263 -10.168 -14.873 1.00 47.95  ?  140 PHE B N     1 
ATOM   4209  C  CA    . PHE B  2  108 ? 56.821 -9.191  -13.916 1.00 48.23  ?  140 PHE B CA    1 
ATOM   4210  C  C     . PHE B  2  108 ? 57.742 -8.149  -14.560 1.00 52.81  ?  140 PHE B C     1 
ATOM   4211  O  O     . PHE B  2  108 ? 58.936 -8.057  -14.197 1.00 49.91  ?  140 PHE B O     1 
ATOM   4212  C  CB    . PHE B  2  108 ? 57.584 -9.930  -12.801 1.00 47.77  ?  140 PHE B CB    1 
ATOM   4213  C  CG    . PHE B  2  108 ? 56.737 -10.914 -12.056 1.00 43.97  ?  140 PHE B CG    1 
ATOM   4214  C  CD1   . PHE B  2  108 ? 55.672 -10.468 -11.278 1.00 40.94  ?  140 PHE B CD1   1 
ATOM   4215  C  CD2   . PHE B  2  108 ? 56.974 -12.267 -12.151 1.00 41.57  ?  140 PHE B CD2   1 
ATOM   4216  C  CE1   . PHE B  2  108 ? 54.864 -11.348 -10.608 1.00 39.22  ?  140 PHE B CE1   1 
ATOM   4217  C  CE2   . PHE B  2  108 ? 56.167 -13.155 -11.476 1.00 41.64  ?  140 PHE B CE2   1 
ATOM   4218  C  CZ    . PHE B  2  108 ? 55.112 -12.698 -10.704 1.00 40.34  ?  140 PHE B CZ    1 
ATOM   4219  N  N     . PRO B  2  109 ? 57.181 -7.330  -15.484 1.00 60.07  ?  141 PRO B N     1 
ATOM   4220  C  CA    . PRO B  2  109 ? 57.972 -6.425  -16.352 1.00 63.05  ?  141 PRO B CA    1 
ATOM   4221  C  C     . PRO B  2  109 ? 58.865 -5.428  -15.601 1.00 67.72  ?  141 PRO B C     1 
ATOM   4222  O  O     . PRO B  2  109 ? 60.047 -5.254  -15.947 1.00 72.24  ?  141 PRO B O     1 
ATOM   4223  C  CB    . PRO B  2  109 ? 56.902 -5.694  -17.185 1.00 60.01  ?  141 PRO B CB    1 
ATOM   4224  C  CG    . PRO B  2  109 ? 55.608 -5.901  -16.468 1.00 57.63  ?  141 PRO B CG    1 
ATOM   4225  C  CD    . PRO B  2  109 ? 55.727 -7.185  -15.714 1.00 57.65  ?  141 PRO B CD    1 
ATOM   4226  N  N     . ASN B  2  110 ? 58.306 -4.812  -14.563 1.00 68.19  ?  142 ASN B N     1 
ATOM   4227  C  CA    . ASN B  2  110 ? 58.990 -3.754  -13.828 1.00 68.32  ?  142 ASN B CA    1 
ATOM   4228  C  C     . ASN B  2  110 ? 59.940 -4.299  -12.777 1.00 59.04  ?  142 ASN B C     1 
ATOM   4229  O  O     . ASN B  2  110 ? 60.969 -3.700  -12.495 1.00 51.79  ?  142 ASN B O     1 
ATOM   4230  C  CB    . ASN B  2  110 ? 57.955 -2.852  -13.163 1.00 76.65  ?  142 ASN B CB    1 
ATOM   4231  C  CG    . ASN B  2  110 ? 56.801 -2.519  -14.090 1.00 82.21  ?  142 ASN B CG    1 
ATOM   4232  O  OD1   . ASN B  2  110 ? 55.627 -2.723  -13.746 1.00 84.49  ?  142 ASN B OD1   1 
ATOM   4233  N  ND2   . ASN B  2  110 ? 57.130 -2.034  -15.290 1.00 81.84  ?  142 ASN B ND2   1 
ATOM   4234  N  N     . LEU B  2  111 ? 59.590 -5.455  -12.230 1.00 56.11  ?  143 LEU B N     1 
ATOM   4235  C  CA    . LEU B  2  111 ? 60.234 -5.982  -11.039 1.00 54.83  ?  143 LEU B CA    1 
ATOM   4236  C  C     . LEU B  2  111 ? 61.596 -6.623  -11.256 1.00 53.89  ?  143 LEU B C     1 
ATOM   4237  O  O     . LEU B  2  111 ? 61.729 -7.580  -12.031 1.00 58.48  ?  143 LEU B O     1 
ATOM   4238  C  CB    . LEU B  2  111 ? 59.343 -7.029  -10.416 1.00 54.37  ?  143 LEU B CB    1 
ATOM   4239  C  CG    . LEU B  2  111 ? 59.908 -7.550  -9.111  1.00 53.50  ?  143 LEU B CG    1 
ATOM   4240  C  CD1   . LEU B  2  111 ? 59.717 -6.511  -8.019  1.00 52.15  ?  143 LEU B CD1   1 
ATOM   4241  C  CD2   . LEU B  2  111 ? 59.224 -8.862  -8.783  1.00 56.17  ?  143 LEU B CD2   1 
ATOM   4242  N  N     . GLN B  2  112 ? 62.579 -6.121  -10.504 1.00 50.72  ?  144 GLN B N     1 
ATOM   4243  C  CA    . GLN B  2  112 ? 63.960 -6.606  -10.554 1.00 46.68  ?  144 GLN B CA    1 
ATOM   4244  C  C     . GLN B  2  112 ? 64.020 -7.931  -9.785  1.00 44.01  ?  144 GLN B C     1 
ATOM   4245  O  O     . GLN B  2  112 ? 63.292 -8.160  -8.829  1.00 41.44  ?  144 GLN B O     1 
ATOM   4246  C  CB    . GLN B  2  112 ? 64.938 -5.564  -9.968  1.00 42.80  ?  144 GLN B CB    1 
ATOM   4247  C  CG    . GLN B  2  112 ? 66.426 -5.850  -10.185 1.00 40.45  ?  144 GLN B CG    1 
ATOM   4248  C  CD    . GLN B  2  112 ? 67.360 -4.816  -9.522  1.00 39.40  ?  144 GLN B CD    1 
ATOM   4249  O  OE1   . GLN B  2  112 ? 66.914 -3.883  -8.846  1.00 36.41  ?  144 GLN B OE1   1 
ATOM   4250  N  NE2   . GLN B  2  112 ? 68.667 -4.987  -9.716  1.00 38.74  ?  144 GLN B NE2   1 
ATOM   4251  N  N     . VAL B  2  113 ? 64.895 -8.802  -10.241 1.00 40.91  ?  145 VAL B N     1 
ATOM   4252  C  CA    . VAL B  2  113 ? 64.963 -10.146 -9.765  1.00 39.05  ?  145 VAL B CA    1 
ATOM   4253  C  C     . VAL B  2  113 ? 66.448 -10.453 -9.684  1.00 40.07  ?  145 VAL B C     1 
ATOM   4254  O  O     . VAL B  2  113 ? 67.226 -9.969  -10.507 1.00 37.81  ?  145 VAL B O     1 
ATOM   4255  C  CB    . VAL B  2  113 ? 64.269 -11.073 -10.774 1.00 38.99  ?  145 VAL B CB    1 
ATOM   4256  C  CG1   . VAL B  2  113 ? 64.383 -12.531 -10.363 1.00 38.32  ?  145 VAL B CG1   1 
ATOM   4257  C  CG2   . VAL B  2  113 ? 62.817 -10.643 -10.991 1.00 39.78  ?  145 VAL B CG2   1 
ATOM   4258  N  N     . PHE B  2  114 ? 66.842 -11.231 -8.683  1.00 43.10  ?  146 PHE B N     1 
ATOM   4259  C  CA    . PHE B  2  114 ? 68.250 -11.599 -8.482  1.00 45.30  ?  146 PHE B CA    1 
ATOM   4260  C  C     . PHE B  2  114 ? 68.441 -13.117 -8.440  1.00 46.31  ?  146 PHE B C     1 
ATOM   4261  O  O     . PHE B  2  114 ? 68.334 -13.747 -7.369  1.00 41.27  ?  146 PHE B O     1 
ATOM   4262  C  CB    . PHE B  2  114 ? 68.815 -11.017 -7.192  1.00 45.81  ?  146 PHE B CB    1 
ATOM   4263  C  CG    . PHE B  2  114 ? 68.708 -9.535  -7.088  1.00 43.82  ?  146 PHE B CG    1 
ATOM   4264  C  CD1   . PHE B  2  114 ? 67.486 -8.947  -6.822  1.00 43.45  ?  146 PHE B CD1   1 
ATOM   4265  C  CD2   . PHE B  2  114 ? 69.828 -8.745  -7.196  1.00 42.79  ?  146 PHE B CD2   1 
ATOM   4266  C  CE1   . PHE B  2  114 ? 67.381 -7.592  -6.687  1.00 43.72  ?  146 PHE B CE1   1 
ATOM   4267  C  CE2   . PHE B  2  114 ? 69.722 -7.386  -7.066  1.00 44.11  ?  146 PHE B CE2   1 
ATOM   4268  C  CZ    . PHE B  2  114 ? 68.499 -6.811  -6.805  1.00 43.68  ?  146 PHE B CZ    1 
ATOM   4269  N  N     . PRO B  2  115 ? 68.747 -13.700 -9.615  1.00 49.00  ?  147 PRO B N     1 
ATOM   4270  C  CA    . PRO B  2  115 ? 69.050 -15.118 -9.730  1.00 46.88  ?  147 PRO B CA    1 
ATOM   4271  C  C     . PRO B  2  115 ? 70.361 -15.537 -9.095  1.00 42.65  ?  147 PRO B C     1 
ATOM   4272  O  O     . PRO B  2  115 ? 71.352 -14.803 -9.116  1.00 41.43  ?  147 PRO B O     1 
ATOM   4273  C  CB    . PRO B  2  115 ? 69.126 -15.343 -11.251 1.00 47.15  ?  147 PRO B CB    1 
ATOM   4274  C  CG    . PRO B  2  115 ? 68.356 -14.220 -11.846 1.00 48.44  ?  147 PRO B CG    1 
ATOM   4275  C  CD    . PRO B  2  115 ? 68.673 -13.066 -10.949 1.00 48.84  ?  147 PRO B CD    1 
ATOM   4276  N  N     . ALA B  2  116 ? 70.347 -16.723 -8.522  1.00 40.27  ?  148 ALA B N     1 
ATOM   4277  C  CA    . ALA B  2  116 ? 71.568 -17.422 -8.300  1.00 42.19  ?  148 ALA B CA    1 
ATOM   4278  C  C     . ALA B  2  116 ? 71.434 -18.655 -9.141  1.00 41.99  ?  148 ALA B C     1 
ATOM   4279  O  O     . ALA B  2  116 ? 70.329 -19.050 -9.555  1.00 37.90  ?  148 ALA B O     1 
ATOM   4280  C  CB    . ALA B  2  116 ? 71.776 -17.765 -6.830  1.00 43.35  ?  148 ALA B CB    1 
ATOM   4281  N  N     . LEU B  2  117 ? 72.592 -19.226 -9.426  1.00 43.68  ?  149 LEU B N     1 
ATOM   4282  C  CA    . LEU B  2  117 ? 72.654 -20.480 -10.106 1.00 43.13  ?  149 LEU B CA    1 
ATOM   4283  C  C     . LEU B  2  117 ? 72.686 -21.553 -9.055  1.00 40.31  ?  149 LEU B C     1 
ATOM   4284  O  O     . LEU B  2  117 ? 73.209 -21.361 -7.950  1.00 39.40  ?  149 LEU B O     1 
ATOM   4285  C  CB    . LEU B  2  117 ? 73.888 -20.562 -11.001 1.00 43.66  ?  149 LEU B CB    1 
ATOM   4286  C  CG    . LEU B  2  117 ? 73.802 -19.688 -12.243 1.00 42.19  ?  149 LEU B CG    1 
ATOM   4287  C  CD1   . LEU B  2  117 ? 75.167 -19.659 -12.910 1.00 43.70  ?  149 LEU B CD1   1 
ATOM   4288  C  CD2   . LEU B  2  117 ? 72.735 -20.234 -13.175 1.00 41.13  ?  149 LEU B CD2   1 
ATOM   4289  N  N     . GLY B  2  118 ? 72.083 -22.668 -9.429  1.00 39.73  ?  150 GLY B N     1 
ATOM   4290  C  CA    . GLY B  2  118 ? 72.093 -23.875 -8.664  1.00 38.95  ?  150 GLY B CA    1 
ATOM   4291  C  C     . GLY B  2  118 ? 72.785 -24.870 -9.542  1.00 38.82  ?  150 GLY B C     1 
ATOM   4292  O  O     . GLY B  2  118 ? 73.362 -24.515 -10.575 1.00 36.45  ?  150 GLY B O     1 
ATOM   4293  N  N     . ASN B  2  119 ? 72.694 -26.121 -9.135  1.00 40.95  ?  151 ASN B N     1 
ATOM   4294  C  CA    . ASN B  2  119 ? 73.480 -27.187 -9.732  1.00 43.58  ?  151 ASN B CA    1 
ATOM   4295  C  C     . ASN B  2  119 ? 72.792 -28.045 -10.793 1.00 38.50  ?  151 ASN B C     1 
ATOM   4296  O  O     . ASN B  2  119 ? 73.397 -28.948 -11.331 1.00 37.83  ?  151 ASN B O     1 
ATOM   4297  C  CB    . ASN B  2  119 ? 74.060 -28.097 -8.624  1.00 51.07  ?  151 ASN B CB    1 
ATOM   4298  C  CG    . ASN B  2  119 ? 72.996 -28.705 -7.722  1.00 54.93  ?  151 ASN B CG    1 
ATOM   4299  O  OD1   . ASN B  2  119 ? 72.240 -27.982 -7.069  1.00 64.70  ?  151 ASN B OD1   1 
ATOM   4300  N  ND2   . ASN B  2  119 ? 72.955 -30.040 -7.654  1.00 55.40  ?  151 ASN B ND2   1 
ATOM   4301  N  N     . HIS B  2  120 ? 71.530 -27.829 -11.074 1.00 35.42  ?  152 HIS B N     1 
ATOM   4302  C  CA    . HIS B  2  120 ? 70.947 -28.543 -12.173 1.00 34.70  ?  152 HIS B CA    1 
ATOM   4303  C  C     . HIS B  2  120 ? 70.923 -27.625 -13.387 1.00 33.15  ?  152 HIS B C     1 
ATOM   4304  O  O     . HIS B  2  120 ? 70.790 -28.087 -14.510 1.00 29.53  ?  152 HIS B O     1 
ATOM   4305  C  CB    . HIS B  2  120 ? 69.578 -29.081 -11.782 1.00 36.57  ?  152 HIS B CB    1 
ATOM   4306  C  CG    . HIS B  2  120 ? 69.636 -30.364 -10.997 1.00 37.29  ?  152 HIS B CG    1 
ATOM   4307  N  ND1   . HIS B  2  120 ? 69.296 -31.592 -11.537 1.00 37.53  ?  152 HIS B ND1   1 
ATOM   4308  C  CD2   . HIS B  2  120 ? 69.971 -30.608 -9.705  1.00 35.69  ?  152 HIS B CD2   1 
ATOM   4309  C  CE1   . HIS B  2  120 ? 69.424 -32.533 -10.613 1.00 35.84  ?  152 HIS B CE1   1 
ATOM   4310  N  NE2   . HIS B  2  120 ? 69.829 -31.961 -9.493  1.00 34.42  ?  152 HIS B NE2   1 
ATOM   4311  N  N     . ASP B  2  121 ? 71.108 -26.331 -13.143 1.00 34.52  ?  153 ASP B N     1 
ATOM   4312  C  CA    . ASP B  2  121 ? 71.232 -25.315 -14.192 1.00 36.75  ?  153 ASP B CA    1 
ATOM   4313  C  C     . ASP B  2  121 ? 72.581 -25.453 -14.894 1.00 40.74  ?  153 ASP B C     1 
ATOM   4314  O  O     . ASP B  2  121 ? 73.410 -24.529 -14.893 1.00 41.90  ?  153 ASP B O     1 
ATOM   4315  C  CB    . ASP B  2  121 ? 71.158 -23.920 -13.576 1.00 35.51  ?  153 ASP B CB    1 
ATOM   4316  C  CG    . ASP B  2  121 ? 69.976 -23.759 -12.700 1.00 34.06  ?  153 ASP B CG    1 
ATOM   4317  O  OD1   . ASP B  2  121 ? 68.890 -24.146 -13.142 1.00 32.87  ?  153 ASP B OD1   1 
ATOM   4318  O  OD2   . ASP B  2  121 ? 70.126 -23.272 -11.570 1.00 33.95  -1 153 ASP B OD2   1 
ATOM   4319  N  N     . TYR B  2  122 ? 72.789 -26.626 -15.485 1.00 44.45  ?  154 TYR B N     1 
ATOM   4320  C  CA    . TYR B  2  122 ? 74.038 -26.995 -16.147 1.00 44.34  ?  154 TYR B CA    1 
ATOM   4321  C  C     . TYR B  2  122 ? 73.901 -28.447 -16.659 1.00 43.69  ?  154 TYR B C     1 
ATOM   4322  O  O     . TYR B  2  122 ? 73.117 -29.267 -16.115 1.00 39.44  ?  154 TYR B O     1 
ATOM   4323  C  CB    . TYR B  2  122 ? 75.241 -26.878 -15.178 1.00 44.91  ?  154 TYR B CB    1 
ATOM   4324  C  CG    . TYR B  2  122 ? 76.573 -26.521 -15.821 1.00 45.20  ?  154 TYR B CG    1 
ATOM   4325  C  CD1   . TYR B  2  122 ? 77.053 -25.208 -15.798 1.00 42.61  ?  154 TYR B CD1   1 
ATOM   4326  C  CD2   . TYR B  2  122 ? 77.373 -27.506 -16.425 1.00 44.63  ?  154 TYR B CD2   1 
ATOM   4327  C  CE1   . TYR B  2  122 ? 78.267 -24.886 -16.367 1.00 41.73  ?  154 TYR B CE1   1 
ATOM   4328  C  CE2   . TYR B  2  122 ? 78.588 -27.182 -17.006 1.00 43.25  ?  154 TYR B CE2   1 
ATOM   4329  C  CZ    . TYR B  2  122 ? 79.020 -25.870 -16.977 1.00 41.85  ?  154 TYR B CZ    1 
ATOM   4330  O  OH    . TYR B  2  122 ? 80.210 -25.537 -17.558 1.00 41.12  ?  154 TYR B OH    1 
ATOM   4331  N  N     . TRP B  2  123 ? 74.674 -28.739 -17.704 1.00 44.53  ?  155 TRP B N     1 
ATOM   4332  C  CA    . TRP B  2  123 ? 74.830 -30.089 -18.244 1.00 44.36  ?  155 TRP B CA    1 
ATOM   4333  C  C     . TRP B  2  123 ? 76.319 -30.520 -18.450 1.00 43.22  ?  155 TRP B C     1 
ATOM   4334  O  O     . TRP B  2  123 ? 77.065 -29.860 -19.183 1.00 40.09  ?  155 TRP B O     1 
ATOM   4335  C  CB    . TRP B  2  123 ? 74.074 -30.196 -19.555 1.00 45.64  ?  155 TRP B CB    1 
ATOM   4336  C  CG    . TRP B  2  123 ? 74.030 -31.561 -19.957 1.00 49.10  ?  155 TRP B CG    1 
ATOM   4337  C  CD1   . TRP B  2  123 ? 73.041 -32.462 -19.698 1.00 49.09  ?  155 TRP B CD1   1 
ATOM   4338  C  CD2   . TRP B  2  123 ? 75.063 -32.262 -20.635 1.00 53.97  ?  155 TRP B CD2   1 
ATOM   4339  N  NE1   . TRP B  2  123 ? 73.386 -33.686 -20.200 1.00 51.07  ?  155 TRP B NE1   1 
ATOM   4340  C  CE2   . TRP B  2  123 ? 74.627 -33.592 -20.780 1.00 55.23  ?  155 TRP B CE2   1 
ATOM   4341  C  CE3   . TRP B  2  123 ? 76.323 -31.892 -21.144 1.00 52.20  ?  155 TRP B CE3   1 
ATOM   4342  C  CZ2   . TRP B  2  123 ? 75.406 -34.557 -21.411 1.00 57.44  ?  155 TRP B CZ2   1 
ATOM   4343  C  CZ3   . TRP B  2  123 ? 77.086 -32.835 -21.762 1.00 53.50  ?  155 TRP B CZ3   1 
ATOM   4344  C  CH2   . TRP B  2  123 ? 76.630 -34.159 -21.897 1.00 56.92  ?  155 TRP B CH2   1 
ATOM   4345  N  N     . PRO B  2  124 ? 76.770 -31.607 -17.808 1.00 44.40  ?  156 PRO B N     1 
ATOM   4346  C  CA    . PRO B  2  124 ? 76.012 -32.378 -16.795 1.00 45.30  ?  156 PRO B CA    1 
ATOM   4347  C  C     . PRO B  2  124 ? 75.717 -31.618 -15.474 1.00 43.82  ?  156 PRO B C     1 
ATOM   4348  O  O     . PRO B  2  124 ? 76.449 -30.693 -15.082 1.00 43.77  ?  156 PRO B O     1 
ATOM   4349  C  CB    . PRO B  2  124 ? 76.916 -33.604 -16.518 1.00 44.96  ?  156 PRO B CB    1 
ATOM   4350  C  CG    . PRO B  2  124 ? 78.267 -33.267 -17.041 1.00 43.46  ?  156 PRO B CG    1 
ATOM   4351  C  CD    . PRO B  2  124 ? 78.141 -32.117 -18.004 1.00 44.64  ?  156 PRO B CD    1 
ATOM   4352  N  N     . GLN B  2  125 ? 74.649 -32.002 -14.796 1.00 39.46  ?  157 GLN B N     1 
ATOM   4353  C  CA    . GLN B  2  125 ? 74.382 -31.410 -13.516 1.00 38.99  ?  157 GLN B CA    1 
ATOM   4354  C  C     . GLN B  2  125 ? 75.627 -31.365 -12.668 1.00 39.70  ?  157 GLN B C     1 
ATOM   4355  O  O     . GLN B  2  125 ? 76.535 -32.141 -12.852 1.00 37.20  ?  157 GLN B O     1 
ATOM   4356  C  CB    . GLN B  2  125 ? 73.275 -32.152 -12.773 1.00 39.45  ?  157 GLN B CB    1 
ATOM   4357  C  CG    . GLN B  2  125 ? 73.489 -33.623 -12.445 1.00 37.63  ?  157 GLN B CG    1 
ATOM   4358  C  CD    . GLN B  2  125 ? 72.157 -34.316 -12.167 1.00 37.82  ?  157 GLN B CD    1 
ATOM   4359  O  OE1   . GLN B  2  125 ? 71.346 -34.547 -13.087 1.00 39.84  ?  157 GLN B OE1   1 
ATOM   4360  N  NE2   . GLN B  2  125 ? 71.901 -34.614 -10.903 1.00 36.54  ?  157 GLN B NE2   1 
ATOM   4361  N  N     . ASP B  2  126 ? 75.665 -30.396 -11.767 1.00 47.06  ?  158 ASP B N     1 
ATOM   4362  C  CA    . ASP B  2  126 ? 76.721 -30.231 -10.737 1.00 51.37  ?  158 ASP B CA    1 
ATOM   4363  C  C     . ASP B  2  126 ? 78.096 -29.733 -11.214 1.00 49.05  ?  158 ASP B C     1 
ATOM   4364  O  O     . ASP B  2  126 ? 78.899 -29.292 -10.399 1.00 52.49  ?  158 ASP B O     1 
ATOM   4365  C  CB    . ASP B  2  126 ? 76.915 -31.516 -9.898  1.00 53.96  ?  158 ASP B CB    1 
ATOM   4366  C  CG    . ASP B  2  126 ? 75.599 -32.107 -9.376  1.00 57.83  ?  158 ASP B CG    1 
ATOM   4367  O  OD1   . ASP B  2  126 ? 74.558 -31.400 -9.361  1.00 54.23  ?  158 ASP B OD1   1 
ATOM   4368  O  OD2   . ASP B  2  126 ? 75.622 -33.301 -8.983  1.00 60.93  -1 158 ASP B OD2   1 
ATOM   4369  N  N     . GLN B  2  127 ? 78.370 -29.750 -12.508 1.00 44.60  ?  159 GLN B N     1 
ATOM   4370  C  CA    . GLN B  2  127 ? 79.734 -29.592 -12.951 1.00 42.89  ?  159 GLN B CA    1 
ATOM   4371  C  C     . GLN B  2  127 ? 80.114 -28.135 -13.209 1.00 46.66  ?  159 GLN B C     1 
ATOM   4372  O  O     . GLN B  2  127 ? 80.982 -27.839 -14.023 1.00 53.01  ?  159 GLN B O     1 
ATOM   4373  C  CB    . GLN B  2  127 ? 79.935 -30.458 -14.181 1.00 40.72  ?  159 GLN B CB    1 
ATOM   4374  C  CG    . GLN B  2  127 ? 79.565 -31.905 -13.930 1.00 39.99  ?  159 GLN B CG    1 
ATOM   4375  C  CD    . GLN B  2  127 ? 80.285 -32.458 -12.723 1.00 40.25  ?  159 GLN B CD    1 
ATOM   4376  O  OE1   . GLN B  2  127 ? 81.511 -32.507 -12.694 1.00 43.64  ?  159 GLN B OE1   1 
ATOM   4377  N  NE2   . GLN B  2  127 ? 79.540 -32.853 -11.721 1.00 39.13  ?  159 GLN B NE2   1 
ATOM   4378  N  N     . LEU B  2  128 ? 79.505 -27.212 -12.481 1.00 48.91  ?  160 LEU B N     1 
ATOM   4379  C  CA    . LEU B  2  128 ? 79.699 -25.801 -12.781 1.00 47.86  ?  160 LEU B CA    1 
ATOM   4380  C  C     . LEU B  2  128 ? 81.191 -25.559 -12.666 1.00 46.08  ?  160 LEU B C     1 
ATOM   4381  O  O     . LEU B  2  128 ? 81.812 -26.078 -11.755 1.00 41.26  ?  160 LEU B O     1 
ATOM   4382  C  CB    . LEU B  2  128 ? 78.866 -24.893 -11.856 1.00 49.12  ?  160 LEU B CB    1 
ATOM   4383  C  CG    . LEU B  2  128 ? 77.346 -24.816 -12.173 1.00 50.34  ?  160 LEU B CG    1 
ATOM   4384  C  CD1   . LEU B  2  128 ? 76.562 -25.997 -11.589 1.00 50.57  ?  160 LEU B CD1   1 
ATOM   4385  C  CD2   . LEU B  2  128 ? 76.690 -23.520 -11.716 1.00 49.87  ?  160 LEU B CD2   1 
ATOM   4386  N  N     . PRO B  2  129 ? 81.778 -24.854 -13.651 1.00 51.31  ?  161 PRO B N     1 
ATOM   4387  C  CA    . PRO B  2  129 ? 83.215 -24.593 -13.730 1.00 54.15  ?  161 PRO B CA    1 
ATOM   4388  C  C     . PRO B  2  129 ? 83.777 -23.255 -13.144 1.00 57.01  ?  161 PRO B C     1 
ATOM   4389  O  O     . PRO B  2  129 ? 83.041 -22.369 -12.636 1.00 48.15  ?  161 PRO B O     1 
ATOM   4390  C  CB    . PRO B  2  129 ? 83.461 -24.638 -15.242 1.00 52.00  ?  161 PRO B CB    1 
ATOM   4391  C  CG    . PRO B  2  129 ? 82.234 -24.007 -15.792 1.00 50.09  ?  161 PRO B CG    1 
ATOM   4392  C  CD    . PRO B  2  129 ? 81.143 -24.629 -14.963 1.00 50.96  ?  161 PRO B CD    1 
ATOM   4393  N  N     . VAL B  2  130 ? 85.109 -23.179 -13.251 1.00 62.94  ?  162 VAL B N     1 
ATOM   4394  C  CA    . VAL B  2  130 ? 85.978 -22.105 -12.754 1.00 65.46  ?  162 VAL B CA    1 
ATOM   4395  C  C     . VAL B  2  130 ? 86.109 -20.956 -13.744 1.00 62.57  ?  162 VAL B C     1 
ATOM   4396  O  O     . VAL B  2  130 ? 86.156 -19.785 -13.356 1.00 65.12  ?  162 VAL B O     1 
ATOM   4397  C  CB    . VAL B  2  130 ? 87.412 -22.666 -12.540 1.00 71.53  ?  162 VAL B CB    1 
ATOM   4398  C  CG1   . VAL B  2  130 ? 88.447 -21.555 -12.260 1.00 70.38  ?  162 VAL B CG1   1 
ATOM   4399  C  CG2   . VAL B  2  130 ? 87.398 -23.757 -11.464 1.00 72.21  ?  162 VAL B CG2   1 
ATOM   4400  N  N     . VAL B  2  131 ? 86.201 -21.312 -15.023 1.00 58.10  ?  163 VAL B N     1 
ATOM   4401  C  CA    . VAL B  2  131 ? 86.412 -20.344 -16.092 1.00 54.15  ?  163 VAL B CA    1 
ATOM   4402  C  C     . VAL B  2  131 ? 85.134 -20.288 -16.921 1.00 55.25  ?  163 VAL B C     1 
ATOM   4403  O  O     . VAL B  2  131 ? 84.208 -21.079 -16.700 1.00 53.03  ?  163 VAL B O     1 
ATOM   4404  C  CB    . VAL B  2  131 ? 87.614 -20.722 -16.976 1.00 51.46  ?  163 VAL B CB    1 
ATOM   4405  C  CG1   . VAL B  2  131 ? 88.463 -19.487 -17.255 1.00 50.80  ?  163 VAL B CG1   1 
ATOM   4406  C  CG2   . VAL B  2  131 ? 88.467 -21.802 -16.313 1.00 49.51  ?  163 VAL B CG2   1 
ATOM   4407  N  N     . THR B  2  132 ? 85.073 -19.352 -17.866 1.00 58.87  ?  164 THR B N     1 
ATOM   4408  C  CA    . THR B  2  132 ? 83.824 -19.091 -18.608 1.00 60.16  ?  164 THR B CA    1 
ATOM   4409  C  C     . THR B  2  132 ? 83.288 -20.333 -19.370 1.00 59.82  ?  164 THR B C     1 
ATOM   4410  O  O     . THR B  2  132 ? 84.005 -21.324 -19.555 1.00 63.50  ?  164 THR B O     1 
ATOM   4411  C  CB    . THR B  2  132 ? 83.959 -17.862 -19.547 1.00 59.38  ?  164 THR B CB    1 
ATOM   4412  O  OG1   . THR B  2  132 ? 82.666 -17.471 -20.042 1.00 53.52  ?  164 THR B OG1   1 
ATOM   4413  C  CG2   . THR B  2  132 ? 84.932 -18.160 -20.714 1.00 61.92  ?  164 THR B CG2   1 
ATOM   4414  N  N     . SER B  2  133 ? 82.021 -20.268 -19.788 1.00 55.98  ?  165 SER B N     1 
ATOM   4415  C  CA    . SER B  2  133 ? 81.321 -21.419 -20.353 1.00 51.03  ?  165 SER B CA    1 
ATOM   4416  C  C     . SER B  2  133 ? 80.113 -20.948 -21.128 1.00 46.89  ?  165 SER B C     1 
ATOM   4417  O  O     . SER B  2  133 ? 79.670 -19.811 -20.972 1.00 40.33  ?  165 SER B O     1 
ATOM   4418  C  CB    . SER B  2  133 ? 80.841 -22.351 -19.236 1.00 50.90  ?  165 SER B CB    1 
ATOM   4419  O  OG    . SER B  2  133 ? 79.715 -21.780 -18.573 1.00 51.08  ?  165 SER B OG    1 
ATOM   4420  N  N     . LYS B  2  134 ? 79.570 -21.857 -21.927 1.00 46.57  ?  166 LYS B N     1 
ATOM   4421  C  CA    . LYS B  2  134 ? 78.331 -21.615 -22.660 1.00 48.85  ?  166 LYS B CA    1 
ATOM   4422  C  C     . LYS B  2  134 ? 77.141 -21.186 -21.771 1.00 49.95  ?  166 LYS B C     1 
ATOM   4423  O  O     . LYS B  2  134 ? 76.538 -20.131 -22.018 1.00 44.62  ?  166 LYS B O     1 
ATOM   4424  C  CB    . LYS B  2  134 ? 77.954 -22.864 -23.470 1.00 51.00  ?  166 LYS B CB    1 
ATOM   4425  C  CG    . LYS B  2  134 ? 76.894 -22.617 -24.547 1.00 51.94  ?  166 LYS B CG    1 
ATOM   4426  C  CD    . LYS B  2  134 ? 76.736 -23.814 -25.477 1.00 51.19  ?  166 LYS B CD    1 
ATOM   4427  C  CE    . LYS B  2  134 ? 75.834 -23.496 -26.651 1.00 51.28  ?  166 LYS B CE    1 
ATOM   4428  N  NZ    . LYS B  2  134 ? 75.436 -24.763 -27.314 1.00 52.86  1  166 LYS B NZ    1 
ATOM   4429  N  N     . VAL B  2  135 ? 76.799 -21.996 -20.758 1.00 52.06  ?  167 VAL B N     1 
ATOM   4430  C  CA    . VAL B  2  135 ? 75.628 -21.701 -19.894 1.00 53.17  ?  167 VAL B CA    1 
ATOM   4431  C  C     . VAL B  2  135 ? 75.826 -20.406 -19.075 1.00 50.69  ?  167 VAL B C     1 
ATOM   4432  O  O     . VAL B  2  135 ? 74.871 -19.612 -18.918 1.00 46.86  ?  167 VAL B O     1 
ATOM   4433  C  CB    . VAL B  2  135 ? 75.187 -22.916 -18.997 1.00 53.84  ?  167 VAL B CB    1 
ATOM   4434  C  CG1   . VAL B  2  135 ? 76.212 -23.245 -17.938 1.00 53.49  ?  167 VAL B CG1   1 
ATOM   4435  C  CG2   . VAL B  2  135 ? 73.829 -22.678 -18.330 1.00 53.06  ?  167 VAL B CG2   1 
ATOM   4436  N  N     . TYR B  2  136 ? 77.050 -20.175 -18.589 1.00 45.75  ?  168 TYR B N     1 
ATOM   4437  C  CA    . TYR B  2  136 ? 77.335 -18.921 -17.886 1.00 45.61  ?  168 TYR B CA    1 
ATOM   4438  C  C     . TYR B  2  136 ? 77.052 -17.693 -18.777 1.00 45.38  ?  168 TYR B C     1 
ATOM   4439  O  O     . TYR B  2  136 ? 76.301 -16.792 -18.382 1.00 40.43  ?  168 TYR B O     1 
ATOM   4440  C  CB    . TYR B  2  136 ? 78.776 -18.876 -17.354 1.00 44.24  ?  168 TYR B CB    1 
ATOM   4441  C  CG    . TYR B  2  136 ? 79.112 -19.775 -16.166 1.00 42.04  ?  168 TYR B CG    1 
ATOM   4442  C  CD1   . TYR B  2  136 ? 78.137 -20.462 -15.428 1.00 41.48  ?  168 TYR B CD1   1 
ATOM   4443  C  CD2   . TYR B  2  136 ? 80.425 -19.902 -15.768 1.00 41.88  ?  168 TYR B CD2   1 
ATOM   4444  C  CE1   . TYR B  2  136 ? 78.493 -21.280 -14.354 1.00 41.26  ?  168 TYR B CE1   1 
ATOM   4445  C  CE2   . TYR B  2  136 ? 80.787 -20.706 -14.707 1.00 42.87  ?  168 TYR B CE2   1 
ATOM   4446  C  CZ    . TYR B  2  136 ? 79.834 -21.390 -13.996 1.00 41.73  ?  168 TYR B CZ    1 
ATOM   4447  O  OH    . TYR B  2  136 ? 80.295 -22.160 -12.945 1.00 40.52  ?  168 TYR B OH    1 
ATOM   4448  N  N     . ASN B  2  137 ? 77.645 -17.678 -19.975 1.00 49.71  ?  169 ASN B N     1 
ATOM   4449  C  CA    . ASN B  2  137 ? 77.417 -16.604 -20.974 1.00 50.85  ?  169 ASN B CA    1 
ATOM   4450  C  C     . ASN B  2  137 ? 75.975 -16.537 -21.474 1.00 51.56  ?  169 ASN B C     1 
ATOM   4451  O  O     . ASN B  2  137 ? 75.527 -15.475 -21.921 1.00 47.28  ?  169 ASN B O     1 
ATOM   4452  C  CB    . ASN B  2  137 ? 78.323 -16.791 -22.195 1.00 50.53  ?  169 ASN B CB    1 
ATOM   4453  C  CG    . ASN B  2  137 ? 79.752 -16.430 -21.913 1.00 49.97  ?  169 ASN B CG    1 
ATOM   4454  O  OD1   . ASN B  2  137 ? 80.565 -17.282 -21.554 1.00 50.22  ?  169 ASN B OD1   1 
ATOM   4455  N  ND2   . ASN B  2  137 ? 80.069 -15.161 -22.060 1.00 50.63  ?  169 ASN B ND2   1 
ATOM   4456  N  N     . ALA B  2  138 ? 75.292 -17.693 -21.439 1.00 53.79  ?  170 ALA B N     1 
ATOM   4457  C  CA    . ALA B  2  138 ? 73.874 -17.844 -21.841 1.00 52.39  ?  170 ALA B CA    1 
ATOM   4458  C  C     . ALA B  2  138 ? 72.909 -17.091 -20.910 1.00 52.40  ?  170 ALA B C     1 
ATOM   4459  O  O     . ALA B  2  138 ? 72.009 -16.374 -21.374 1.00 46.65  ?  170 ALA B O     1 
ATOM   4460  C  CB    . ALA B  2  138 ? 73.497 -19.333 -21.896 1.00 49.20  ?  170 ALA B CB    1 
ATOM   4461  N  N     . VAL B  2  139 ? 73.118 -17.286 -19.602 1.00 52.50  ?  171 VAL B N     1 
ATOM   4462  C  CA    . VAL B  2  139 ? 72.298 -16.685 -18.546 1.00 47.20  ?  171 VAL B CA    1 
ATOM   4463  C  C     . VAL B  2  139 ? 72.597 -15.191 -18.324 1.00 47.72  ?  171 VAL B C     1 
ATOM   4464  O  O     . VAL B  2  139 ? 71.665 -14.423 -18.063 1.00 43.95  ?  171 VAL B O     1 
ATOM   4465  C  CB    . VAL B  2  139 ? 72.441 -17.481 -17.240 1.00 44.00  ?  171 VAL B CB    1 
ATOM   4466  C  CG1   . VAL B  2  139 ? 72.024 -18.918 -17.464 1.00 44.06  ?  171 VAL B CG1   1 
ATOM   4467  C  CG2   . VAL B  2  139 ? 73.863 -17.446 -16.714 1.00 43.95  ?  171 VAL B CG2   1 
ATOM   4468  N  N     . ALA B  2  140 ? 73.870 -14.779 -18.453 1.00 48.83  ?  172 ALA B N     1 
ATOM   4469  C  CA    . ALA B  2  140 ? 74.241 -13.345 -18.408 1.00 52.04  ?  172 ALA B CA    1 
ATOM   4470  C  C     . ALA B  2  140 ? 73.419 -12.532 -19.412 1.00 53.98  ?  172 ALA B C     1 
ATOM   4471  O  O     . ALA B  2  140 ? 72.884 -11.475 -19.062 1.00 52.06  ?  172 ALA B O     1 
ATOM   4472  C  CB    . ALA B  2  140 ? 75.736 -13.138 -18.651 1.00 51.05  ?  172 ALA B CB    1 
ATOM   4473  N  N     . ASN B  2  141 ? 73.311 -13.048 -20.642 1.00 57.62  ?  173 ASN B N     1 
ATOM   4474  C  CA    . ASN B  2  141 ? 72.411 -12.484 -21.679 1.00 62.10  ?  173 ASN B CA    1 
ATOM   4475  C  C     . ASN B  2  141 ? 70.967 -12.434 -21.189 1.00 59.98  ?  173 ASN B C     1 
ATOM   4476  O  O     . ASN B  2  141 ? 70.292 -11.439 -21.372 1.00 63.84  ?  173 ASN B O     1 
ATOM   4477  C  CB    . ASN B  2  141 ? 72.417 -13.291 -23.008 1.00 65.86  ?  173 ASN B CB    1 
ATOM   4478  C  CG    . ASN B  2  141 ? 73.790 -13.351 -23.697 1.00 72.04  ?  173 ASN B CG    1 
ATOM   4479  O  OD1   . ASN B  2  141 ? 74.743 -12.652 -23.329 1.00 76.20  ?  173 ASN B OD1   1 
ATOM   4480  N  ND2   . ASN B  2  141 ? 73.886 -14.204 -24.716 1.00 73.89  ?  173 ASN B ND2   1 
ATOM   4481  N  N     . LEU B  2  142 ? 70.499 -13.517 -20.577 1.00 57.61  ?  174 LEU B N     1 
ATOM   4482  C  CA    . LEU B  2  142 ? 69.125 -13.606 -20.118 1.00 53.08  ?  174 LEU B CA    1 
ATOM   4483  C  C     . LEU B  2  142 ? 68.818 -12.618 -19.001 1.00 51.00  ?  174 LEU B C     1 
ATOM   4484  O  O     . LEU B  2  142 ? 67.714 -12.070 -18.904 1.00 46.67  ?  174 LEU B O     1 
ATOM   4485  C  CB    . LEU B  2  142 ? 68.845 -15.021 -19.647 1.00 55.59  ?  174 LEU B CB    1 
ATOM   4486  C  CG    . LEU B  2  142 ? 68.975 -16.118 -20.708 1.00 61.44  ?  174 LEU B CG    1 
ATOM   4487  C  CD1   . LEU B  2  142 ? 68.626 -17.481 -20.107 1.00 64.25  ?  174 LEU B CD1   1 
ATOM   4488  C  CD2   . LEU B  2  142 ? 68.105 -15.852 -21.934 1.00 61.34  ?  174 LEU B CD2   1 
ATOM   4489  N  N     . TRP B  2  143 ? 69.801 -12.368 -18.159 1.00 50.19  ?  175 TRP B N     1 
ATOM   4490  C  CA    . TRP B  2  143 ? 69.549 -11.567 -16.985 1.00 52.18  ?  175 TRP B CA    1 
ATOM   4491  C  C     . TRP B  2  143 ? 70.059 -10.143 -17.105 1.00 53.36  ?  175 TRP B C     1 
ATOM   4492  O  O     . TRP B  2  143 ? 69.914 -9.353  -16.176 1.00 49.88  ?  175 TRP B O     1 
ATOM   4493  C  CB    . TRP B  2  143 ? 70.111 -12.294 -15.769 1.00 53.52  ?  175 TRP B CB    1 
ATOM   4494  C  CG    . TRP B  2  143 ? 69.537 -13.689 -15.630 1.00 53.64  ?  175 TRP B CG    1 
ATOM   4495  C  CD1   . TRP B  2  143 ? 68.347 -14.163 -16.157 1.00 53.42  ?  175 TRP B CD1   1 
ATOM   4496  C  CD2   . TRP B  2  143 ? 70.107 -14.772 -14.902 1.00 54.82  ?  175 TRP B CD2   1 
ATOM   4497  N  NE1   . TRP B  2  143 ? 68.157 -15.480 -15.810 1.00 54.98  ?  175 TRP B NE1   1 
ATOM   4498  C  CE2   . TRP B  2  143 ? 69.219 -15.882 -15.035 1.00 59.12  ?  175 TRP B CE2   1 
ATOM   4499  C  CE3   . TRP B  2  143 ? 71.280 -14.921 -14.140 1.00 54.62  ?  175 TRP B CE3   1 
ATOM   4500  C  CZ2   . TRP B  2  143 ? 69.479 -17.122 -14.437 1.00 60.35  ?  175 TRP B CZ2   1 
ATOM   4501  C  CZ3   . TRP B  2  143 ? 71.545 -16.150 -13.550 1.00 56.79  ?  175 TRP B CZ3   1 
ATOM   4502  C  CH2   . TRP B  2  143 ? 70.643 -17.237 -13.700 1.00 61.67  ?  175 TRP B CH2   1 
ATOM   4503  N  N     . LYS B  2  144 ? 70.629 -9.808  -18.264 1.00 58.64  ?  176 LYS B N     1 
ATOM   4504  C  CA    . LYS B  2  144 ? 70.893 -8.406  -18.643 1.00 59.06  ?  176 LYS B CA    1 
ATOM   4505  C  C     . LYS B  2  144 ? 69.788 -7.447  -18.153 1.00 56.69  ?  176 LYS B C     1 
ATOM   4506  O  O     . LYS B  2  144 ? 70.099 -6.468  -17.464 1.00 56.30  ?  176 LYS B O     1 
ATOM   4507  C  CB    . LYS B  2  144 ? 71.048 -8.248  -20.181 1.00 59.31  ?  176 LYS B CB    1 
ATOM   4508  C  CG    . LYS B  2  144 ? 72.473 -8.162  -20.757 1.00 57.94  ?  176 LYS B CG    1 
ATOM   4509  C  CD    . LYS B  2  144 ? 72.493 -8.078  -22.297 1.00 54.96  ?  176 LYS B CD    1 
ATOM   4510  C  CE    . LYS B  2  144 ? 71.623 -6.944  -22.860 1.00 53.90  ?  176 LYS B CE    1 
ATOM   4511  N  NZ    . LYS B  2  144 ? 71.259 -7.135  -24.290 1.00 52.55  1  176 LYS B NZ    1 
ATOM   4512  N  N     . PRO B  2  145 ? 68.497 -7.718  -18.492 1.00 54.54  ?  177 PRO B N     1 
ATOM   4513  C  CA    . PRO B  2  145 ? 67.547 -6.656  -18.140 1.00 55.92  ?  177 PRO B CA    1 
ATOM   4514  C  C     . PRO B  2  145 ? 67.559 -6.333  -16.633 1.00 60.84  ?  177 PRO B C     1 
ATOM   4515  O  O     . PRO B  2  145 ? 67.206 -5.206  -16.274 1.00 69.10  ?  177 PRO B O     1 
ATOM   4516  C  CB    . PRO B  2  145 ? 66.170 -7.198  -18.620 1.00 51.32  ?  177 PRO B CB    1 
ATOM   4517  C  CG    . PRO B  2  145 ? 66.472 -8.395  -19.456 1.00 51.11  ?  177 PRO B CG    1 
ATOM   4518  C  CD    . PRO B  2  145 ? 67.793 -8.930  -18.960 1.00 53.15  ?  177 PRO B CD    1 
ATOM   4519  N  N     . TRP B  2  146 ? 67.990 -7.290  -15.787 1.00 58.06  ?  178 TRP B N     1 
ATOM   4520  C  CA    . TRP B  2  146 ? 68.038 -7.123  -14.316 1.00 56.03  ?  178 TRP B CA    1 
ATOM   4521  C  C     . TRP B  2  146 ? 69.384 -6.667  -13.722 1.00 60.60  ?  178 TRP B C     1 
ATOM   4522  O  O     . TRP B  2  146 ? 69.372 -5.925  -12.746 1.00 68.94  ?  178 TRP B O     1 
ATOM   4523  C  CB    . TRP B  2  146 ? 67.622 -8.410  -13.585 1.00 51.10  ?  178 TRP B CB    1 
ATOM   4524  C  CG    . TRP B  2  146 ? 66.259 -8.944  -13.935 1.00 45.20  ?  178 TRP B CG    1 
ATOM   4525  C  CD1   . TRP B  2  146 ? 65.122 -8.215  -14.175 1.00 42.70  ?  178 TRP B CD1   1 
ATOM   4526  C  CD2   . TRP B  2  146 ? 65.886 -10.337 -14.053 1.00 39.75  ?  178 TRP B CD2   1 
ATOM   4527  N  NE1   . TRP B  2  146 ? 64.071 -9.072  -14.446 1.00 42.33  ?  178 TRP B NE1   1 
ATOM   4528  C  CE2   . TRP B  2  146 ? 64.513 -10.373 -14.383 1.00 39.05  ?  178 TRP B CE2   1 
ATOM   4529  C  CE3   . TRP B  2  146 ? 66.580 -11.555 -13.900 1.00 35.11  ?  178 TRP B CE3   1 
ATOM   4530  C  CZ2   . TRP B  2  146 ? 63.821 -11.580 -14.570 1.00 35.41  ?  178 TRP B CZ2   1 
ATOM   4531  C  CZ3   . TRP B  2  146 ? 65.887 -12.752 -14.089 1.00 33.05  ?  178 TRP B CZ3   1 
ATOM   4532  C  CH2   . TRP B  2  146 ? 64.525 -12.751 -14.420 1.00 33.29  ?  178 TRP B CH2   1 
ATOM   4533  N  N     . LEU B  2  147 ? 70.524 -7.110  -14.259 1.00 61.89  ?  179 LEU B N     1 
ATOM   4534  C  CA    . LEU B  2  147 ? 71.846 -6.690  -13.730 1.00 62.73  ?  179 LEU B CA    1 
ATOM   4535  C  C     . LEU B  2  147 ? 72.548 -5.720  -14.670 1.00 67.94  ?  179 LEU B C     1 
ATOM   4536  O  O     . LEU B  2  147 ? 72.033 -5.397  -15.746 1.00 77.57  ?  179 LEU B O     1 
ATOM   4537  C  CB    . LEU B  2  147 ? 72.760 -7.892  -13.498 1.00 61.17  ?  179 LEU B CB    1 
ATOM   4538  C  CG    . LEU B  2  147 ? 72.090 -9.188  -13.067 1.00 57.54  ?  179 LEU B CG    1 
ATOM   4539  C  CD1   . LEU B  2  147 ? 73.175 -10.234 -12.885 1.00 55.89  ?  179 LEU B CD1   1 
ATOM   4540  C  CD2   . LEU B  2  147 ? 71.288 -8.975  -11.795 1.00 55.31  ?  179 LEU B CD2   1 
ATOM   4541  N  N     . ASP B  2  148 ? 73.727 -5.256  -14.282 1.00 66.97  ?  180 ASP B N     1 
ATOM   4542  C  CA    . ASP B  2  148 ? 74.440 -4.318  -15.129 1.00 68.67  ?  180 ASP B CA    1 
ATOM   4543  C  C     . ASP B  2  148 ? 75.846 -4.809  -15.372 1.00 73.68  ?  180 ASP B C     1 
ATOM   4544  O  O     . ASP B  2  148 ? 76.245 -5.820  -14.806 1.00 76.93  ?  180 ASP B O     1 
ATOM   4545  C  CB    . ASP B  2  148 ? 74.344 -2.927  -14.521 1.00 69.23  ?  180 ASP B CB    1 
ATOM   4546  C  CG    . ASP B  2  148 ? 72.890 -2.463  -14.406 1.00 72.07  ?  180 ASP B CG    1 
ATOM   4547  O  OD1   . ASP B  2  148 ? 72.206 -2.396  -15.451 1.00 69.78  ?  180 ASP B OD1   1 
ATOM   4548  O  OD2   . ASP B  2  148 ? 72.408 -2.210  -13.280 1.00 74.16  -1 180 ASP B OD2   1 
ATOM   4549  N  N     . GLU B  2  149 ? 76.577 -4.113  -16.241 1.00 79.78  ?  181 GLU B N     1 
ATOM   4550  C  CA    . GLU B  2  149 ? 77.832 -4.628  -16.819 1.00 82.20  ?  181 GLU B CA    1 
ATOM   4551  C  C     . GLU B  2  149 ? 78.761 -5.307  -15.805 1.00 84.62  ?  181 GLU B C     1 
ATOM   4552  O  O     . GLU B  2  149 ? 79.293 -6.387  -16.092 1.00 89.01  ?  181 GLU B O     1 
ATOM   4553  C  CB    . GLU B  2  149 ? 78.635 -3.517  -17.499 1.00 83.47  ?  181 GLU B CB    1 
ATOM   4554  C  CG    . GLU B  2  149 ? 77.932 -2.743  -18.606 1.00 85.78  ?  181 GLU B CG    1 
ATOM   4555  C  CD    . GLU B  2  149 ? 78.368 -1.280  -18.652 1.00 87.24  ?  181 GLU B CD    1 
ATOM   4556  O  OE1   . GLU B  2  149 ? 79.422 -0.942  -18.060 1.00 83.04  ?  181 GLU B OE1   1 
ATOM   4557  O  OE2   . GLU B  2  149 ? 77.657 -0.460  -19.277 1.00 83.98  -1 181 GLU B OE2   1 
ATOM   4558  N  N     . GLU B  2  150 ? 78.963 -4.674  -14.641 1.00 81.58  ?  182 GLU B N     1 
ATOM   4559  C  CA    . GLU B  2  150 ? 79.913 -5.182  -13.622 1.00 82.04  ?  182 GLU B CA    1 
ATOM   4560  C  C     . GLU B  2  150 ? 79.398 -6.511  -13.082 1.00 84.65  ?  182 GLU B C     1 
ATOM   4561  O  O     . GLU B  2  150 ? 80.172 -7.463  -12.891 1.00 84.49  ?  182 GLU B O     1 
ATOM   4562  C  CB    . GLU B  2  150 ? 80.109 -4.219  -12.439 1.00 78.90  ?  182 GLU B CB    1 
ATOM   4563  C  CG    . GLU B  2  150 ? 80.461 -2.794  -12.813 1.00 79.06  ?  182 GLU B CG    1 
ATOM   4564  C  CD    . GLU B  2  150 ? 79.258 -2.016  -13.307 1.00 76.81  ?  182 GLU B CD    1 
ATOM   4565  O  OE1   . GLU B  2  150 ? 78.163 -2.167  -12.719 1.00 73.47  ?  182 GLU B OE1   1 
ATOM   4566  O  OE2   . GLU B  2  150 ? 79.406 -1.271  -14.297 1.00 73.97  -1 182 GLU B OE2   1 
ATOM   4567  N  N     . ALA B  2  151 ? 78.087 -6.551  -12.826 1.00 79.46  ?  183 ALA B N     1 
ATOM   4568  C  CA    . ALA B  2  151 ? 77.394 -7.786  -12.474 1.00 73.47  ?  183 ALA B CA    1 
ATOM   4569  C  C     . ALA B  2  151 ? 77.600 -8.811  -13.582 1.00 69.82  ?  183 ALA B C     1 
ATOM   4570  O  O     . ALA B  2  151 ? 78.147 -9.894  -13.340 1.00 69.00  ?  183 ALA B O     1 
ATOM   4571  C  CB    . ALA B  2  151 ? 75.902 -7.526  -12.252 1.00 70.68  ?  183 ALA B CB    1 
ATOM   4572  N  N     . ILE B  2  152 ? 77.194 -8.422  -14.794 1.00 63.37  ?  184 ILE B N     1 
ATOM   4573  C  CA    . ILE B  2  152 ? 77.213 -9.277  -15.978 1.00 59.14  ?  184 ILE B CA    1 
ATOM   4574  C  C     . ILE B  2  152 ? 78.581 -9.860  -16.284 1.00 56.97  ?  184 ILE B C     1 
ATOM   4575  O  O     . ILE B  2  152 ? 78.688 -11.010 -16.717 1.00 52.21  ?  184 ILE B O     1 
ATOM   4576  C  CB    . ILE B  2  152 ? 76.730 -8.487  -17.200 1.00 63.00  ?  184 ILE B CB    1 
ATOM   4577  C  CG1   . ILE B  2  152 ? 75.215 -8.258  -17.112 1.00 67.44  ?  184 ILE B CG1   1 
ATOM   4578  C  CG2   . ILE B  2  152 ? 77.085 -9.198  -18.503 1.00 66.19  ?  184 ILE B CG2   1 
ATOM   4579  C  CD1   . ILE B  2  152 ? 74.374 -9.517  -17.279 1.00 69.14  ?  184 ILE B CD1   1 
ATOM   4580  N  N     . SER B  2  153 ? 79.611 -9.053  -16.067 1.00 57.69  ?  185 SER B N     1 
ATOM   4581  C  CA    . SER B  2  153 ? 80.995 -9.456  -16.297 1.00 59.71  ?  185 SER B CA    1 
ATOM   4582  C  C     . SER B  2  153 ? 81.431 -10.715 -15.539 1.00 59.40  ?  185 SER B C     1 
ATOM   4583  O  O     . SER B  2  153 ? 81.800 -11.697 -16.164 1.00 55.74  ?  185 SER B O     1 
ATOM   4584  C  CB    . SER B  2  153 ? 81.947 -8.312  -15.951 1.00 60.00  ?  185 SER B CB    1 
ATOM   4585  O  OG    . SER B  2  153 ? 83.267 -8.815  -15.852 1.00 62.82  ?  185 SER B OG    1 
ATOM   4586  N  N     . THR B  2  154 ? 81.421 -10.678 -14.204 1.00 64.96  ?  186 THR B N     1 
ATOM   4587  C  CA    . THR B  2  154 ? 81.794 -11.866 -13.401 1.00 67.56  ?  186 THR B CA    1 
ATOM   4588  C  C     . THR B  2  154 ? 80.770 -13.012 -13.558 1.00 61.86  ?  186 THR B C     1 
ATOM   4589  O  O     . THR B  2  154 ? 81.110 -14.174 -13.329 1.00 58.99  ?  186 THR B O     1 
ATOM   4590  C  CB    . THR B  2  154 ? 82.013 -11.581 -11.867 1.00 70.31  ?  186 THR B CB    1 
ATOM   4591  O  OG1   . THR B  2  154 ? 81.114 -10.557 -11.406 1.00 73.08  ?  186 THR B OG1   1 
ATOM   4592  C  CG2   . THR B  2  154 ? 83.501 -11.206 -11.537 1.00 69.46  ?  186 THR B CG2   1 
ATOM   4593  N  N     . LEU B  2  155 ? 79.533 -12.693 -13.945 1.00 57.32  ?  187 LEU B N     1 
ATOM   4594  C  CA    . LEU B  2  155 ? 78.499 -13.728 -14.166 1.00 56.18  ?  187 LEU B CA    1 
ATOM   4595  C  C     . LEU B  2  155 ? 78.830 -14.767 -15.274 1.00 56.91  ?  187 LEU B C     1 
ATOM   4596  O  O     . LEU B  2  155 ? 78.350 -15.896 -15.194 1.00 58.99  ?  187 LEU B O     1 
ATOM   4597  C  CB    . LEU B  2  155 ? 77.125 -13.073 -14.418 1.00 53.22  ?  187 LEU B CB    1 
ATOM   4598  C  CG    . LEU B  2  155 ? 75.906 -13.961 -14.679 1.00 49.90  ?  187 LEU B CG    1 
ATOM   4599  C  CD1   . LEU B  2  155 ? 75.719 -15.042 -13.634 1.00 50.24  ?  187 LEU B CD1   1 
ATOM   4600  C  CD2   . LEU B  2  155 ? 74.679 -13.083 -14.738 1.00 48.26  ?  187 LEU B CD2   1 
ATOM   4601  N  N     . ARG B  2  156 ? 79.639 -14.391 -16.279 1.00 55.50  ?  188 ARG B N     1 
ATOM   4602  C  CA    . ARG B  2  156 ? 80.093 -15.317 -17.329 1.00 50.47  ?  188 ARG B CA    1 
ATOM   4603  C  C     . ARG B  2  156 ? 81.481 -15.896 -17.032 1.00 51.19  ?  188 ARG B C     1 
ATOM   4604  O  O     . ARG B  2  156 ? 81.878 -16.852 -17.677 1.00 46.82  ?  188 ARG B O     1 
ATOM   4605  C  CB    . ARG B  2  156 ? 80.178 -14.653 -18.697 1.00 51.56  ?  188 ARG B CB    1 
ATOM   4606  C  CG    . ARG B  2  156 ? 79.331 -13.423 -18.979 1.00 52.60  ?  188 ARG B CG    1 
ATOM   4607  C  CD    . ARG B  2  156 ? 80.064 -12.590 -20.032 1.00 55.44  ?  188 ARG B CD    1 
ATOM   4608  N  NE    . ARG B  2  156 ? 79.286 -11.477 -20.525 1.00 57.16  ?  188 ARG B NE    1 
ATOM   4609  C  CZ    . ARG B  2  156 ? 78.232 -11.591 -21.322 1.00 60.11  ?  188 ARG B CZ    1 
ATOM   4610  N  NH1   . ARG B  2  156 ? 77.808 -12.785 -21.743 1.00 59.98  1  188 ARG B NH1   1 
ATOM   4611  N  NH2   . ARG B  2  156 ? 77.595 -10.493 -21.699 1.00 63.65  ?  188 ARG B NH2   1 
ATOM   4612  N  N     . LYS B  2  157 ? 82.231 -15.268 -16.115 1.00 55.62  ?  189 LYS B N     1 
ATOM   4613  C  CA    . LYS B  2  157 ? 83.534 -15.782 -15.577 1.00 60.09  ?  189 LYS B CA    1 
ATOM   4614  C  C     . LYS B  2  157 ? 83.400 -17.056 -14.702 1.00 54.07  ?  189 LYS B C     1 
ATOM   4615  O  O     . LYS B  2  157 ? 84.082 -18.050 -14.910 1.00 46.59  ?  189 LYS B O     1 
ATOM   4616  C  CB    . LYS B  2  157 ? 84.249 -14.698 -14.709 1.00 66.59  ?  189 LYS B CB    1 
ATOM   4617  C  CG    . LYS B  2  157 ? 85.241 -13.745 -15.386 1.00 69.04  ?  189 LYS B CG    1 
ATOM   4618  C  CD    . LYS B  2  157 ? 84.582 -12.814 -16.396 1.00 72.44  ?  189 LYS B CD    1 
ATOM   4619  C  CE    . LYS B  2  157 ? 84.532 -13.446 -17.798 1.00 74.27  ?  189 LYS B CE    1 
ATOM   4620  N  NZ    . LYS B  2  157 ? 83.556 -12.829 -18.747 1.00 70.98  1  189 LYS B NZ    1 
ATOM   4621  N  N     . GLY B  2  158 ? 82.559 -16.980 -13.679 1.00 53.25  ?  190 GLY B N     1 
ATOM   4622  C  CA    . GLY B  2  158 ? 82.326 -18.104 -12.781 1.00 53.14  ?  190 GLY B CA    1 
ATOM   4623  C  C     . GLY B  2  158 ? 80.921 -18.205 -12.182 1.00 54.51  ?  190 GLY B C     1 
ATOM   4624  O  O     . GLY B  2  158 ? 80.745 -18.900 -11.181 1.00 56.48  ?  190 GLY B O     1 
ATOM   4625  N  N     . GLY B  2  159 ? 79.925 -17.531 -12.771 1.00 51.72  ?  191 GLY B N     1 
ATOM   4626  C  CA    . GLY B  2  159 ? 78.515 -17.702 -12.375 1.00 49.28  ?  191 GLY B CA    1 
ATOM   4627  C  C     . GLY B  2  159 ? 78.066 -16.966 -11.127 1.00 48.03  ?  191 GLY B C     1 
ATOM   4628  O  O     . GLY B  2  159 ? 77.026 -17.302 -10.534 1.00 48.60  ?  191 GLY B O     1 
ATOM   4629  N  N     . PHE B  2  160 ? 78.839 -15.955 -10.734 1.00 47.92  ?  192 PHE B N     1 
ATOM   4630  C  CA    . PHE B  2  160 ? 78.490 -15.077 -9.611  1.00 47.85  ?  192 PHE B CA    1 
ATOM   4631  C  C     . PHE B  2  160 ? 78.534 -13.567 -9.957  1.00 52.00  ?  192 PHE B C     1 
ATOM   4632  O  O     . PHE B  2  160 ? 79.279 -13.126 -10.846 1.00 54.54  ?  192 PHE B O     1 
ATOM   4633  C  CB    . PHE B  2  160 ? 79.391 -15.380 -8.404  1.00 46.33  ?  192 PHE B CB    1 
ATOM   4634  C  CG    . PHE B  2  160 ? 80.872 -15.154 -8.647  1.00 43.73  ?  192 PHE B CG    1 
ATOM   4635  C  CD1   . PHE B  2  160 ? 81.410 -13.869 -8.695  1.00 43.11  ?  192 PHE B CD1   1 
ATOM   4636  C  CD2   . PHE B  2  160 ? 81.733 -16.228 -8.773  1.00 42.77  ?  192 PHE B CD2   1 
ATOM   4637  C  CE1   . PHE B  2  160 ? 82.764 -13.669 -8.887  1.00 43.00  ?  192 PHE B CE1   1 
ATOM   4638  C  CE2   . PHE B  2  160 ? 83.086 -16.035 -8.966  1.00 42.09  ?  192 PHE B CE2   1 
ATOM   4639  C  CZ    . PHE B  2  160 ? 83.603 -14.759 -9.021  1.00 42.98  ?  192 PHE B CZ    1 
ATOM   4640  N  N     . TYR B  2  161 ? 77.733 -12.778 -9.240  1.00 55.38  ?  193 TYR B N     1 
ATOM   4641  C  CA    . TYR B  2  161 ? 77.699 -11.315 -9.408  1.00 53.59  ?  193 TYR B CA    1 
ATOM   4642  C  C     . TYR B  2  161 ? 77.277 -10.713 -8.069  1.00 49.61  ?  193 TYR B C     1 
ATOM   4643  O  O     . TYR B  2  161 ? 76.938 -11.450 -7.144  1.00 43.31  ?  193 TYR B O     1 
ATOM   4644  C  CB    . TYR B  2  161 ? 76.695 -10.922 -10.508 1.00 53.99  ?  193 TYR B CB    1 
ATOM   4645  C  CG    . TYR B  2  161 ? 75.265 -11.195 -10.090 1.00 54.98  ?  193 TYR B CG    1 
ATOM   4646  C  CD1   . TYR B  2  161 ? 74.695 -12.451 -10.272 1.00 55.96  ?  193 TYR B CD1   1 
ATOM   4647  C  CD2   . TYR B  2  161 ? 74.502 -10.210 -9.460  1.00 55.50  ?  193 TYR B CD2   1 
ATOM   4648  C  CE1   . TYR B  2  161 ? 73.403 -12.711 -9.868  1.00 53.86  ?  193 TYR B CE1   1 
ATOM   4649  C  CE2   . TYR B  2  161 ? 73.209 -10.459 -9.049  1.00 53.78  ?  193 TYR B CE2   1 
ATOM   4650  C  CZ    . TYR B  2  161 ? 72.670 -11.707 -9.261  1.00 53.92  ?  193 TYR B CZ    1 
ATOM   4651  O  OH    . TYR B  2  161 ? 71.397 -11.945 -8.850  1.00 55.89  ?  193 TYR B OH    1 
ATOM   4652  N  N     . SER B  2  162 ? 77.325 -9.384  -7.975  1.00 49.76  ?  194 SER B N     1 
ATOM   4653  C  CA    . SER B  2  162 ? 76.736 -8.628  -6.851  1.00 50.00  ?  194 SER B CA    1 
ATOM   4654  C  C     . SER B  2  162 ? 76.174 -7.326  -7.350  1.00 45.90  ?  194 SER B C     1 
ATOM   4655  O  O     . SER B  2  162 ? 76.704 -6.729  -8.263  1.00 46.91  ?  194 SER B O     1 
ATOM   4656  C  CB    . SER B  2  162 ? 77.764 -8.281  -5.785  1.00 53.64  ?  194 SER B CB    1 
ATOM   4657  O  OG    . SER B  2  162 ? 78.700 -7.326  -6.269  1.00 53.77  ?  194 SER B OG    1 
ATOM   4658  N  N     . GLN B  2  163 ? 75.124 -6.844  -6.733  1.00 43.69  ?  195 GLN B N     1 
ATOM   4659  C  CA    . GLN B  2  163 ? 74.424 -5.777  -7.369  1.00 46.89  ?  195 GLN B CA    1 
ATOM   4660  C  C     . GLN B  2  163 ? 73.784 -4.924  -6.345  1.00 48.67  ?  195 GLN B C     1 
ATOM   4661  O  O     . GLN B  2  163 ? 73.255 -5.415  -5.375  1.00 51.02  ?  195 GLN B O     1 
ATOM   4662  C  CB    . GLN B  2  163 ? 73.352 -6.354  -8.299  1.00 48.94  ?  195 GLN B CB    1 
ATOM   4663  C  CG    . GLN B  2  163 ? 72.514 -5.317  -9.056  1.00 47.49  ?  195 GLN B CG    1 
ATOM   4664  C  CD    . GLN B  2  163 ? 73.239 -4.705  -10.240 1.00 44.98  ?  195 GLN B CD    1 
ATOM   4665  O  OE1   . GLN B  2  163 ? 74.225 -5.263  -10.758 1.00 43.19  ?  195 GLN B OE1   1 
ATOM   4666  N  NE2   . GLN B  2  163 ? 72.741 -3.563  -10.691 1.00 42.70  ?  195 GLN B NE2   1 
ATOM   4667  N  N     . LYS B  2  164 ? 73.815 -3.630  -6.589  1.00 52.34  ?  196 LYS B N     1 
ATOM   4668  C  CA    . LYS B  2  164 ? 73.034 -2.700  -5.813  1.00 53.77  ?  196 LYS B CA    1 
ATOM   4669  C  C     . LYS B  2  164 ? 71.563 -2.790  -6.276  1.00 51.36  ?  196 LYS B C     1 
ATOM   4670  O  O     . LYS B  2  164 ? 71.280 -2.952  -7.477  1.00 52.18  ?  196 LYS B O     1 
ATOM   4671  C  CB    . LYS B  2  164 ? 73.648 -1.306  -5.964  1.00 55.47  ?  196 LYS B CB    1 
ATOM   4672  C  CG    . LYS B  2  164 ? 75.104 -1.281  -5.487  1.00 57.10  ?  196 LYS B CG    1 
ATOM   4673  C  CD    . LYS B  2  164 ? 75.811 0.037   -5.769  1.00 58.43  ?  196 LYS B CD    1 
ATOM   4674  C  CE    . LYS B  2  164 ? 76.658 -0.008  -7.029  1.00 56.51  ?  196 LYS B CE    1 
ATOM   4675  N  NZ    . LYS B  2  164 ? 77.839 0.865   -6.810  1.00 55.40  1  196 LYS B NZ    1 
ATOM   4676  N  N     . VAL B  2  165 ? 70.634 -2.746  -5.324  1.00 46.83  ?  197 VAL B N     1 
ATOM   4677  C  CA    . VAL B  2  165 ? 69.228 -2.804  -5.667  1.00 48.02  ?  197 VAL B CA    1 
ATOM   4678  C  C     . VAL B  2  165 ? 68.874 -1.451  -6.282  1.00 47.72  ?  197 VAL B C     1 
ATOM   4679  O  O     . VAL B  2  165 ? 69.274 -0.412  -5.757  1.00 43.35  ?  197 VAL B O     1 
ATOM   4680  C  CB    . VAL B  2  165 ? 68.328 -3.111  -4.440  1.00 51.32  ?  197 VAL B CB    1 
ATOM   4681  C  CG1   . VAL B  2  165 ? 66.859 -3.131  -4.847  1.00 52.35  ?  197 VAL B CG1   1 
ATOM   4682  C  CG2   . VAL B  2  165 ? 68.674 -4.451  -3.809  1.00 51.78  ?  197 VAL B CG2   1 
ATOM   4683  N  N     . THR B  2  166 ? 68.160 -1.467  -7.411  1.00 50.91  ?  198 THR B N     1 
ATOM   4684  C  CA    . THR B  2  166 ? 67.654 -0.220  -8.045  1.00 51.87  ?  198 THR B CA    1 
ATOM   4685  C  C     . THR B  2  166 ? 66.903 0.637   -6.992  1.00 53.99  ?  198 THR B C     1 
ATOM   4686  O  O     . THR B  2  166 ? 67.334 1.746   -6.698  1.00 60.85  ?  198 THR B O     1 
ATOM   4687  C  CB    . THR B  2  166 ? 66.795 -0.493  -9.344  1.00 49.09  ?  198 THR B CB    1 
ATOM   4688  O  OG1   . THR B  2  166 ? 67.649 -0.595  -10.488 1.00 44.15  ?  198 THR B OG1   1 
ATOM   4689  C  CG2   . THR B  2  166 ? 65.749 0.601   -9.630  1.00 46.91  ?  198 THR B CG2   1 
ATOM   4690  N  N     . THR B  2  167 ? 65.833 0.110   -6.386  1.00 54.25  ?  199 THR B N     1 
ATOM   4691  C  CA    . THR B  2  167 ? 64.985 0.910   -5.465  1.00 51.10  ?  199 THR B CA    1 
ATOM   4692  C  C     . THR B  2  167 ? 65.485 1.004   -4.028  1.00 44.17  ?  199 THR B C     1 
ATOM   4693  O  O     . THR B  2  167 ? 64.758 1.466   -3.187  1.00 39.58  ?  199 THR B O     1 
ATOM   4694  C  CB    . THR B  2  167 ? 63.509 0.397   -5.361  1.00 54.12  ?  199 THR B CB    1 
ATOM   4695  O  OG1   . THR B  2  167 ? 63.440 -0.738  -4.479  1.00 57.38  ?  199 THR B OG1   1 
ATOM   4696  C  CG2   . THR B  2  167 ? 62.883 0.075   -6.757  1.00 53.96  ?  199 THR B CG2   1 
ATOM   4697  N  N     . ASN B  2  168 ? 66.701 0.627   -3.692  1.00 43.36  ?  200 ASN B N     1 
ATOM   4698  C  CA    . ASN B  2  168 ? 67.179 0.697   -2.306  1.00 45.94  ?  200 ASN B CA    1 
ATOM   4699  C  C     . ASN B  2  168 ? 68.647 0.622   -2.547  1.00 48.25  ?  200 ASN B C     1 
ATOM   4700  O  O     . ASN B  2  168 ? 69.300 -0.326  -2.212  1.00 51.23  ?  200 ASN B O     1 
ATOM   4701  C  CB    . ASN B  2  168 ? 66.712 -0.574  -1.584  1.00 47.29  ?  200 ASN B CB    1 
ATOM   4702  C  CG    . ASN B  2  168 ? 65.226 -0.624  -1.331  1.00 48.86  ?  200 ASN B CG    1 
ATOM   4703  O  OD1   . ASN B  2  168 ? 64.713 -0.042  -0.380  1.00 48.66  ?  200 ASN B OD1   1 
ATOM   4704  N  ND2   . ASN B  2  168 ? 64.534 -1.367  -2.152  1.00 47.34  ?  200 ASN B ND2   1 
ATOM   4705  N  N     . PRO B  2  169 ? 69.194 1.643   -3.142  1.00 53.28  ?  201 PRO B N     1 
ATOM   4706  C  CA    . PRO B  2  169 ? 70.519 1.520   -3.784  1.00 56.25  ?  201 PRO B CA    1 
ATOM   4707  C  C     . PRO B  2  169 ? 71.748 1.337   -2.891  1.00 57.93  ?  201 PRO B C     1 
ATOM   4708  O  O     . PRO B  2  169 ? 72.855 1.201   -3.434  1.00 58.32  ?  201 PRO B O     1 
ATOM   4709  C  CB    . PRO B  2  169 ? 70.648 2.811   -4.615  1.00 58.77  ?  201 PRO B CB    1 
ATOM   4710  C  CG    . PRO B  2  169 ? 69.293 3.455   -4.598  1.00 58.96  ?  201 PRO B CG    1 
ATOM   4711  C  CD    . PRO B  2  169 ? 68.589 2.967   -3.363  1.00 57.12  ?  201 PRO B CD    1 
ATOM   4712  N  N     . ASN B  2  170 ? 71.572 1.349   -1.564  1.00 59.71  ?  202 ASN B N     1 
ATOM   4713  C  CA    . ASN B  2  170 ? 72.639 0.930   -0.613  1.00 61.58  ?  202 ASN B CA    1 
ATOM   4714  C  C     . ASN B  2  170 ? 72.376 -0.484  -0.023  1.00 63.61  ?  202 ASN B C     1 
ATOM   4715  O  O     . ASN B  2  170 ? 73.002 -0.905  0.964   1.00 62.49  ?  202 ASN B O     1 
ATOM   4716  C  CB    . ASN B  2  170 ? 72.847 1.976   0.494   1.00 58.82  ?  202 ASN B CB    1 
ATOM   4717  C  CG    . ASN B  2  170 ? 71.561 2.339   1.193   1.00 58.09  ?  202 ASN B CG    1 
ATOM   4718  O  OD1   . ASN B  2  170 ? 70.473 2.248   0.608   1.00 56.10  ?  202 ASN B OD1   1 
ATOM   4719  N  ND2   . ASN B  2  170 ? 71.669 2.745   2.449   1.00 57.24  ?  202 ASN B ND2   1 
ATOM   4720  N  N     . LEU B  2  171 ? 71.438 -1.199  -0.651  1.00 61.07  ?  203 LEU B N     1 
ATOM   4721  C  CA    . LEU B  2  171 ? 71.249 -2.617  -0.459  1.00 55.47  ?  203 LEU B CA    1 
ATOM   4722  C  C     . LEU B  2  171 ? 71.958 -3.291  -1.620  1.00 53.64  ?  203 LEU B C     1 
ATOM   4723  O  O     . LEU B  2  171 ? 71.577 -3.073  -2.768  1.00 49.47  ?  203 LEU B O     1 
ATOM   4724  C  CB    . LEU B  2  171 ? 69.753 -2.942  -0.493  1.00 55.39  ?  203 LEU B CB    1 
ATOM   4725  C  CG    . LEU B  2  171 ? 69.347 -4.381  -0.153  1.00 56.32  ?  203 LEU B CG    1 
ATOM   4726  C  CD1   . LEU B  2  171 ? 69.899 -4.778  1.214   1.00 55.13  ?  203 LEU B CD1   1 
ATOM   4727  C  CD2   . LEU B  2  171 ? 67.834 -4.576  -0.223  1.00 54.38  ?  203 LEU B CD2   1 
ATOM   4728  N  N     . ARG B  2  172 ? 73.005 -4.067  -1.327  1.00 54.91  ?  204 ARG B N     1 
ATOM   4729  C  CA    . ARG B  2  172 ? 73.677 -4.901  -2.342  1.00 57.43  ?  204 ARG B CA    1 
ATOM   4730  C  C     . ARG B  2  172 ? 73.453 -6.414  -2.140  1.00 55.99  ?  204 ARG B C     1 
ATOM   4731  O  O     . ARG B  2  172 ? 74.010 -7.027  -1.229  1.00 60.50  ?  204 ARG B O     1 
ATOM   4732  C  CB    . ARG B  2  172 ? 75.196 -4.654  -2.399  1.00 59.76  ?  204 ARG B CB    1 
ATOM   4733  C  CG    . ARG B  2  172 ? 75.897 -5.534  -3.443  1.00 62.99  ?  204 ARG B CG    1 
ATOM   4734  C  CD    . ARG B  2  172 ? 77.350 -5.888  -3.131  1.00 67.71  ?  204 ARG B CD    1 
ATOM   4735  N  NE    . ARG B  2  172 ? 78.227 -4.755  -2.812  1.00 76.21  ?  204 ARG B NE    1 
ATOM   4736  C  CZ    . ARG B  2  172 ? 78.581 -3.767  -3.645  1.00 79.51  ?  204 ARG B CZ    1 
ATOM   4737  N  NH1   . ARG B  2  172 ? 78.113 -3.689  -4.891  1.00 77.86  1  204 ARG B NH1   1 
ATOM   4738  N  NH2   . ARG B  2  172 ? 79.402 -2.815  -3.207  1.00 83.79  ?  204 ARG B NH2   1 
ATOM   4739  N  N     . ILE B  2  173 ? 72.690 -7.022  -3.038  1.00 49.28  ?  205 ILE B N     1 
ATOM   4740  C  CA    . ILE B  2  173 ? 72.572 -8.461  -3.074  1.00 43.55  ?  205 ILE B CA    1 
ATOM   4741  C  C     . ILE B  2  173 ? 73.899 -8.986  -3.552  1.00 40.18  ?  205 ILE B C     1 
ATOM   4742  O  O     . ILE B  2  173 ? 74.349 -8.585  -4.617  1.00 39.86  ?  205 ILE B O     1 
ATOM   4743  C  CB    . ILE B  2  173 ? 71.506 -8.937  -4.085  1.00 44.08  ?  205 ILE B CB    1 
ATOM   4744  C  CG1   . ILE B  2  173 ? 70.177 -8.171  -3.913  1.00 44.35  ?  205 ILE B CG1   1 
ATOM   4745  C  CG2   . ILE B  2  173 ? 71.312 -10.445 -3.957  1.00 44.24  ?  205 ILE B CG2   1 
ATOM   4746  C  CD1   . ILE B  2  173 ? 69.722 -8.019  -2.471  1.00 45.88  ?  205 ILE B CD1   1 
ATOM   4747  N  N     . ILE B  2  174 ? 74.524 -9.865  -2.775  1.00 37.53  ?  206 ILE B N     1 
ATOM   4748  C  CA    . ILE B  2  174 ? 75.586 -10.745 -3.305  1.00 36.78  ?  206 ILE B CA    1 
ATOM   4749  C  C     . ILE B  2  174 ? 75.117 -12.204 -3.627  1.00 38.48  ?  206 ILE B C     1 
ATOM   4750  O  O     . ILE B  2  174 ? 75.162 -13.090 -2.763  1.00 40.59  ?  206 ILE B O     1 
ATOM   4751  C  CB    . ILE B  2  174 ? 76.767 -10.809 -2.342  1.00 34.62  ?  206 ILE B CB    1 
ATOM   4752  C  CG1   . ILE B  2  174 ? 77.287 -9.410  -2.046  1.00 35.52  ?  206 ILE B CG1   1 
ATOM   4753  C  CG2   . ILE B  2  174 ? 77.877 -11.672 -2.910  1.00 32.72  ?  206 ILE B CG2   1 
ATOM   4754  C  CD1   . ILE B  2  174 ? 78.468 -9.422  -1.077  1.00 36.65  ?  206 ILE B CD1   1 
ATOM   4755  N  N     . SER B  2  175 ? 74.689 -12.437 -4.877  1.00 40.80  ?  207 SER B N     1 
ATOM   4756  C  CA    . SER B  2  175 ? 74.355 -13.783 -5.423  1.00 39.79  ?  207 SER B CA    1 
ATOM   4757  C  C     . SER B  2  175 ? 75.605 -14.600 -5.741  1.00 39.46  ?  207 SER B C     1 
ATOM   4758  O  O     . SER B  2  175 ? 76.341 -14.267 -6.692  1.00 33.36  ?  207 SER B O     1 
ATOM   4759  C  CB    . SER B  2  175 ? 73.511 -13.666 -6.708  1.00 40.57  ?  207 SER B CB    1 
ATOM   4760  O  OG    . SER B  2  175 ? 73.769 -14.719 -7.632  1.00 40.74  ?  207 SER B OG    1 
ATOM   4761  N  N     . LEU B  2  176 ? 75.806 -15.670 -4.950  1.00 42.13  ?  208 LEU B N     1 
ATOM   4762  C  CA    . LEU B  2  176 ? 76.950 -16.587 -5.074  1.00 42.44  ?  208 LEU B CA    1 
ATOM   4763  C  C     . LEU B  2  176 ? 76.571 -17.898 -5.740  1.00 44.84  ?  208 LEU B C     1 
ATOM   4764  O  O     . LEU B  2  176 ? 75.406 -18.339 -5.761  1.00 48.71  ?  208 LEU B O     1 
ATOM   4765  C  CB    . LEU B  2  176 ? 77.529 -16.948 -3.708  1.00 43.42  ?  208 LEU B CB    1 
ATOM   4766  C  CG    . LEU B  2  176 ? 78.246 -15.918 -2.820  1.00 45.72  ?  208 LEU B CG    1 
ATOM   4767  C  CD1   . LEU B  2  176 ? 78.230 -16.418 -1.386  1.00 46.70  ?  208 LEU B CD1   1 
ATOM   4768  C  CD2   . LEU B  2  176 ? 79.684 -15.628 -3.240  1.00 46.36  ?  208 LEU B CD2   1 
ATOM   4769  N  N     . ASN B  2  177 ? 77.606 -18.517 -6.279  1.00 47.33  ?  209 ASN B N     1 
ATOM   4770  C  CA    . ASN B  2  177 ? 77.541 -19.843 -6.871  1.00 48.86  ?  209 ASN B CA    1 
ATOM   4771  C  C     . ASN B  2  177 ? 78.193 -20.801 -5.902  1.00 47.00  ?  209 ASN B C     1 
ATOM   4772  O  O     . ASN B  2  177 ? 79.422 -21.005 -5.937  1.00 48.19  ?  209 ASN B O     1 
ATOM   4773  C  CB    . ASN B  2  177 ? 78.295 -19.857 -8.206  1.00 51.12  ?  209 ASN B CB    1 
ATOM   4774  C  CG    . ASN B  2  177 ? 78.356 -21.233 -8.850  1.00 52.07  ?  209 ASN B CG    1 
ATOM   4775  O  OD1   . ASN B  2  177 ? 78.431 -22.269 -8.173  1.00 53.41  ?  209 ASN B OD1   1 
ATOM   4776  N  ND2   . ASN B  2  177 ? 78.350 -21.246 -10.178 1.00 54.37  ?  209 ASN B ND2   1 
ATOM   4777  N  N     . THR B  2  178 ? 77.367 -21.378 -5.038  1.00 41.35  ?  210 THR B N     1 
ATOM   4778  C  CA    . THR B  2  178 ? 77.839 -22.313 -4.050  1.00 38.63  ?  210 THR B CA    1 
ATOM   4779  C  C     . THR B  2  178 ? 77.787 -23.727 -4.599  1.00 38.15  ?  210 THR B C     1 
ATOM   4780  O  O     . THR B  2  178 ? 78.134 -24.693 -3.903  1.00 38.86  ?  210 THR B O     1 
ATOM   4781  C  CB    . THR B  2  178 ? 76.975 -22.194 -2.820  1.00 38.03  ?  210 THR B CB    1 
ATOM   4782  O  OG1   . THR B  2  178 ? 75.622 -22.005 -3.252  1.00 36.55  ?  210 THR B OG1   1 
ATOM   4783  C  CG2   . THR B  2  178 ? 77.437 -21.006 -2.012  1.00 37.54  ?  210 THR B CG2   1 
ATOM   4784  N  N     . ASN B  2  179 ? 77.368 -23.835 -5.856  1.00 35.23  ?  211 ASN B N     1 
ATOM   4785  C  CA    . ASN B  2  179 ? 77.511 -25.057 -6.610  1.00 35.92  ?  211 ASN B CA    1 
ATOM   4786  C  C     . ASN B  2  179 ? 78.982 -25.385 -6.912  1.00 38.42  ?  211 ASN B C     1 
ATOM   4787  O  O     . ASN B  2  179 ? 79.316 -26.531 -7.210  1.00 39.07  ?  211 ASN B O     1 
ATOM   4788  C  CB    . ASN B  2  179 ? 76.720 -24.955 -7.909  1.00 35.29  ?  211 ASN B CB    1 
ATOM   4789  C  CG    . ASN B  2  179 ? 75.300 -24.461 -7.695  1.00 33.92  ?  211 ASN B CG    1 
ATOM   4790  O  OD1   . ASN B  2  179 ? 74.876 -23.488 -8.293  1.00 34.18  ?  211 ASN B OD1   1 
ATOM   4791  N  ND2   . ASN B  2  179 ? 74.566 -25.132 -6.852  1.00 33.67  ?  211 ASN B ND2   1 
ATOM   4792  N  N     . LEU B  2  180 ? 79.853 -24.380 -6.827  1.00 41.04  ?  212 LEU B N     1 
ATOM   4793  C  CA    . LEU B  2  180 ? 81.330 -24.572 -6.889  1.00 45.44  ?  212 LEU B CA    1 
ATOM   4794  C  C     . LEU B  2  180 ? 81.908 -25.369 -5.693  1.00 44.95  ?  212 LEU B C     1 
ATOM   4795  O  O     . LEU B  2  180 ? 82.932 -26.050 -5.816  1.00 47.58  ?  212 LEU B O     1 
ATOM   4796  C  CB    . LEU B  2  180 ? 82.056 -23.205 -6.988  1.00 47.43  ?  212 LEU B CB    1 
ATOM   4797  C  CG    . LEU B  2  180 ? 81.631 -22.264 -8.148  1.00 47.67  ?  212 LEU B CG    1 
ATOM   4798  C  CD1   . LEU B  2  180 ? 82.048 -20.813 -7.907  1.00 45.60  ?  212 LEU B CD1   1 
ATOM   4799  C  CD2   . LEU B  2  180 ? 82.108 -22.779 -9.514  1.00 46.95  ?  212 LEU B CD2   1 
ATOM   4800  N  N     . TYR B  2  181 ? 81.236 -25.275 -4.547  1.00 42.95  ?  213 TYR B N     1 
ATOM   4801  C  CA    . TYR B  2  181 ? 81.642 -25.948 -3.330  1.00 39.50  ?  213 TYR B CA    1 
ATOM   4802  C  C     . TYR B  2  181 ? 80.848 -27.206 -3.034  1.00 37.96  ?  213 TYR B C     1 
ATOM   4803  O  O     . TYR B  2  181 ? 81.035 -27.799 -1.985  1.00 34.65  ?  213 TYR B O     1 
ATOM   4804  C  CB    . TYR B  2  181 ? 81.460 -24.989 -2.185  1.00 41.25  ?  213 TYR B CB    1 
ATOM   4805  C  CG    . TYR B  2  181 ? 82.044 -23.641 -2.476  1.00 45.53  ?  213 TYR B CG    1 
ATOM   4806  C  CD1   . TYR B  2  181 ? 83.327 -23.512 -3.018  1.00 44.34  ?  213 TYR B CD1   1 
ATOM   4807  C  CD2   . TYR B  2  181 ? 81.308 -22.479 -2.215  1.00 48.42  ?  213 TYR B CD2   1 
ATOM   4808  C  CE1   . TYR B  2  181 ? 83.846 -22.262 -3.290  1.00 47.30  ?  213 TYR B CE1   1 
ATOM   4809  C  CE2   . TYR B  2  181 ? 81.830 -21.221 -2.475  1.00 48.34  ?  213 TYR B CE2   1 
ATOM   4810  C  CZ    . TYR B  2  181 ? 83.087 -21.124 -3.017  1.00 48.65  ?  213 TYR B CZ    1 
ATOM   4811  O  OH    . TYR B  2  181 ? 83.578 -19.880 -3.270  1.00 50.59  ?  213 TYR B OH    1 
ATOM   4812  N  N     . TYR B  2  182 ? 79.970 -27.613 -3.953  1.00 39.69  ?  214 TYR B N     1 
ATOM   4813  C  CA    . TYR B  2  182 ? 79.093 -28.782 -3.770  1.00 38.85  ?  214 TYR B CA    1 
ATOM   4814  C  C     . TYR B  2  182 ? 79.818 -30.094 -3.979  1.00 41.11  ?  214 TYR B C     1 
ATOM   4815  O  O     . TYR B  2  182 ? 80.573 -30.251 -4.950  1.00 44.68  ?  214 TYR B O     1 
ATOM   4816  C  CB    . TYR B  2  182 ? 77.960 -28.714 -4.771  1.00 38.05  ?  214 TYR B CB    1 
ATOM   4817  C  CG    . TYR B  2  182 ? 76.922 -29.784 -4.630  1.00 38.05  ?  214 TYR B CG    1 
ATOM   4818  C  CD1   . TYR B  2  182 ? 76.581 -30.315 -3.380  1.00 38.73  ?  214 TYR B CD1   1 
ATOM   4819  C  CD2   . TYR B  2  182 ? 76.237 -30.235 -5.748  1.00 38.42  ?  214 TYR B CD2   1 
ATOM   4820  C  CE1   . TYR B  2  182 ? 75.607 -31.285 -3.261  1.00 39.35  ?  214 TYR B CE1   1 
ATOM   4821  C  CE2   . TYR B  2  182 ? 75.261 -31.198 -5.644  1.00 40.16  ?  214 TYR B CE2   1 
ATOM   4822  C  CZ    . TYR B  2  182 ? 74.949 -31.710 -4.402  1.00 40.68  ?  214 TYR B CZ    1 
ATOM   4823  O  OH    . TYR B  2  182 ? 73.970 -32.647 -4.339  1.00 42.11  ?  214 TYR B OH    1 
ATOM   4824  N  N     . GLY B  2  183 ? 79.582 -31.042 -3.080  1.00 41.96  ?  215 GLY B N     1 
ATOM   4825  C  CA    . GLY B  2  183 ? 80.294 -32.320 -3.101  1.00 41.49  ?  215 GLY B CA    1 
ATOM   4826  C  C     . GLY B  2  183 ? 80.536 -32.873 -4.488  1.00 39.81  ?  215 GLY B C     1 
ATOM   4827  O  O     . GLY B  2  183 ? 81.669 -32.851 -4.958  1.00 37.90  ?  215 GLY B O     1 
ATOM   4828  N  N     . PRO B  2  184 ? 79.465 -33.333 -5.165  1.00 42.26  ?  216 PRO B N     1 
ATOM   4829  C  CA    . PRO B  2  184 ? 79.496 -33.952 -6.515  1.00 43.36  ?  216 PRO B CA    1 
ATOM   4830  C  C     . PRO B  2  184 ? 80.179 -33.175 -7.664  1.00 43.82  ?  216 PRO B C     1 
ATOM   4831  O  O     . PRO B  2  184 ? 80.398 -33.769 -8.736  1.00 42.51  ?  216 PRO B O     1 
ATOM   4832  C  CB    . PRO B  2  184 ? 78.011 -34.140 -6.852  1.00 42.51  ?  216 PRO B CB    1 
ATOM   4833  C  CG    . PRO B  2  184 ? 77.341 -34.235 -5.526  1.00 43.31  ?  216 PRO B CG    1 
ATOM   4834  C  CD    . PRO B  2  184 ? 78.094 -33.309 -4.616  1.00 43.23  ?  216 PRO B CD    1 
ATOM   4835  N  N     . ASN B  2  185 ? 80.506 -31.889 -7.451  1.00 43.67  ?  217 ASN B N     1 
ATOM   4836  C  CA    . ASN B  2  185 ? 81.168 -31.062 -8.466  1.00 43.51  ?  217 ASN B CA    1 
ATOM   4837  C  C     . ASN B  2  185 ? 82.616 -31.472 -8.700  1.00 45.64  ?  217 ASN B C     1 
ATOM   4838  O  O     . ASN B  2  185 ? 83.491 -31.134 -7.900  1.00 46.47  ?  217 ASN B O     1 
ATOM   4839  C  CB    . ASN B  2  185 ? 81.122 -29.593 -8.062  1.00 42.92  ?  217 ASN B CB    1 
ATOM   4840  C  CG    . ASN B  2  185 ? 81.520 -28.659 -9.195  1.00 44.30  ?  217 ASN B CG    1 
ATOM   4841  O  OD1   . ASN B  2  185 ? 81.872 -29.088 -10.297 1.00 42.20  ?  217 ASN B OD1   1 
ATOM   4842  N  ND2   . ASN B  2  185 ? 81.438 -27.364 -8.930  1.00 46.98  ?  217 ASN B ND2   1 
ATOM   4843  N  N     . ILE B  2  186 ? 82.859 -32.189 -9.803  1.00 47.47  ?  218 ILE B N     1 
ATOM   4844  C  CA    . ILE B  2  186 ? 84.191 -32.751 -10.110 1.00 47.51  ?  218 ILE B CA    1 
ATOM   4845  C  C     . ILE B  2  186 ? 85.193 -31.694 -10.599 1.00 46.94  ?  218 ILE B C     1 
ATOM   4846  O  O     . ILE B  2  186 ? 86.396 -31.844 -10.382 1.00 42.23  ?  218 ILE B O     1 
ATOM   4847  C  CB    . ILE B  2  186 ? 84.107 -33.892 -11.155 1.00 47.15  ?  218 ILE B CB    1 
ATOM   4848  C  CG1   . ILE B  2  186 ? 83.265 -35.068 -10.639 1.00 46.85  ?  218 ILE B CG1   1 
ATOM   4849  C  CG2   . ILE B  2  186 ? 85.498 -34.373 -11.553 1.00 47.19  ?  218 ILE B CG2   1 
ATOM   4850  C  CD1   . ILE B  2  186 ? 83.940 -35.948 -9.603  1.00 48.59  ?  218 ILE B CD1   1 
ATOM   4851  N  N     . MET B  2  187 ? 84.706 -30.638 -11.254 1.00 50.25  ?  219 MET B N     1 
ATOM   4852  C  CA    . MET B  2  187 ? 85.571 -29.519 -11.677 1.00 55.35  ?  219 MET B CA    1 
ATOM   4853  C  C     . MET B  2  187 ? 86.372 -28.888 -10.535 1.00 54.47  ?  219 MET B C     1 
ATOM   4854  O  O     . MET B  2  187 ? 87.534 -28.573 -10.733 1.00 54.01  ?  219 MET B O     1 
ATOM   4855  C  CB    . MET B  2  187 ? 84.767 -28.407 -12.382 1.00 59.14  ?  219 MET B CB    1 
ATOM   4856  C  CG    . MET B  2  187 ? 84.154 -28.789 -13.728 1.00 62.73  ?  219 MET B CG    1 
ATOM   4857  S  SD    . MET B  2  187 ? 85.131 -29.920 -14.760 1.00 64.37  ?  219 MET B SD    1 
ATOM   4858  C  CE    . MET B  2  187 ? 84.488 -31.532 -14.287 1.00 57.34  ?  219 MET B CE    1 
ATOM   4859  N  N     . THR B  2  188 ? 85.757 -28.718 -9.356  1.00 55.52  ?  220 THR B N     1 
ATOM   4860  C  CA    . THR B  2  188 ? 86.373 -27.991 -8.223  1.00 53.43  ?  220 THR B CA    1 
ATOM   4861  C  C     . THR B  2  188 ? 87.072 -28.863 -7.164  1.00 51.69  ?  220 THR B C     1 
ATOM   4862  O  O     . THR B  2  188 ? 87.476 -28.346 -6.125  1.00 51.48  ?  220 THR B O     1 
ATOM   4863  C  CB    . THR B  2  188 ? 85.356 -27.045 -7.504  1.00 54.05  ?  220 THR B CB    1 
ATOM   4864  O  OG1   . THR B  2  188 ? 84.314 -27.809 -6.868  1.00 51.54  ?  220 THR B OG1   1 
ATOM   4865  C  CG2   . THR B  2  188 ? 84.753 -26.016 -8.496  1.00 52.61  ?  220 THR B CG2   1 
ATOM   4866  N  N     . LEU B  2  189 ? 87.225 -30.164 -7.419  1.00 52.18  ?  221 LEU B N     1 
ATOM   4867  C  CA    . LEU B  2  189 ? 88.035 -31.042 -6.538  1.00 54.35  ?  221 LEU B CA    1 
ATOM   4868  C  C     . LEU B  2  189 ? 89.453 -30.512 -6.265  1.00 60.87  ?  221 LEU B C     1 
ATOM   4869  O  O     . LEU B  2  189 ? 90.123 -29.975 -7.153  1.00 65.29  ?  221 LEU B O     1 
ATOM   4870  C  CB    . LEU B  2  189 ? 88.151 -32.469 -7.096  1.00 49.16  ?  221 LEU B CB    1 
ATOM   4871  C  CG    . LEU B  2  189 ? 87.250 -33.490 -6.408  1.00 46.41  ?  221 LEU B CG    1 
ATOM   4872  C  CD1   . LEU B  2  189 ? 86.888 -34.632 -7.349  1.00 46.80  ?  221 LEU B CD1   1 
ATOM   4873  C  CD2   . LEU B  2  189 ? 87.919 -34.017 -5.151  1.00 44.17  ?  221 LEU B CD2   1 
ATOM   4874  N  N     . ASN B  2  190 ? 89.890 -30.661 -5.016  1.00 64.51  ?  222 ASN B N     1 
ATOM   4875  C  CA    . ASN B  2  190 ? 91.227 -30.279 -4.591  1.00 63.46  ?  222 ASN B CA    1 
ATOM   4876  C  C     . ASN B  2  190 ? 91.607 -28.821 -4.877  1.00 60.72  ?  222 ASN B C     1 
ATOM   4877  O  O     . ASN B  2  190 ? 92.776 -28.484 -4.769  1.00 59.77  ?  222 ASN B O     1 
ATOM   4878  C  CB    . ASN B  2  190 ? 92.249 -31.228 -5.227  1.00 67.26  ?  222 ASN B CB    1 
ATOM   4879  C  CG    . ASN B  2  190 ? 93.218 -31.801 -4.215  1.00 74.92  ?  222 ASN B CG    1 
ATOM   4880  O  OD1   . ASN B  2  190 ? 92.821 -32.189 -3.107  1.00 78.19  ?  222 ASN B OD1   1 
ATOM   4881  N  ND2   . ASN B  2  190 ? 94.495 -31.874 -4.590  1.00 77.77  ?  222 ASN B ND2   1 
ATOM   4882  N  N     . LYS B  2  191 ? 90.629 -27.968 -5.213  1.00 60.81  ?  223 LYS B N     1 
ATOM   4883  C  CA    . LYS B  2  191 ? 90.867 -26.540 -5.482  1.00 62.36  ?  223 LYS B CA    1 
ATOM   4884  C  C     . LYS B  2  191 ? 90.745 -25.672 -4.209  1.00 64.79  ?  223 LYS B C     1 
ATOM   4885  O  O     . LYS B  2  191 ? 89.677 -25.545 -3.617  1.00 61.34  ?  223 LYS B O     1 
ATOM   4886  C  CB    . LYS B  2  191 ? 89.911 -26.000 -6.566  1.00 61.68  ?  223 LYS B CB    1 
ATOM   4887  C  CG    . LYS B  2  191 ? 90.268 -26.364 -8.001  1.00 61.83  ?  223 LYS B CG    1 
ATOM   4888  C  CD    . LYS B  2  191 ? 90.228 -25.140 -8.918  1.00 64.64  ?  223 LYS B CD    1 
ATOM   4889  C  CE    . LYS B  2  191 ? 90.560 -25.492 -10.370 1.00 67.23  ?  223 LYS B CE    1 
ATOM   4890  N  NZ    . LYS B  2  191 ? 91.044 -24.331 -11.183 1.00 67.93  1  223 LYS B NZ    1 
ATOM   4891  N  N     . THR B  2  192 ? 91.867 -25.087 -3.807  1.00 71.09  ?  224 THR B N     1 
ATOM   4892  C  CA    . THR B  2  192 ? 91.946 -24.102 -2.722  1.00 72.73  ?  224 THR B CA    1 
ATOM   4893  C  C     . THR B  2  192 ? 90.851 -22.992 -2.728  1.00 71.99  ?  224 THR B C     1 
ATOM   4894  O  O     . THR B  2  192 ? 90.288 -22.656 -1.679  1.00 64.38  ?  224 THR B O     1 
ATOM   4895  C  CB    . THR B  2  192 ? 93.360 -23.456 -2.735  1.00 75.98  ?  224 THR B CB    1 
ATOM   4896  O  OG1   . THR B  2  192 ? 93.481 -22.554 -1.637  1.00 80.38  ?  224 THR B OG1   1 
ATOM   4897  C  CG2   . THR B  2  192 ? 93.676 -22.705 -4.094  1.00 75.02  ?  224 THR B CG2   1 
ATOM   4898  N  N     . ASP B  2  193 ? 90.555 -22.433 -3.903  1.00 71.63  ?  225 ASP B N     1 
ATOM   4899  C  CA    . ASP B  2  193 ? 89.572 -21.352 -4.034  1.00 70.68  ?  225 ASP B CA    1 
ATOM   4900  C  C     . ASP B  2  193 ? 89.026 -21.315 -5.471  1.00 69.83  ?  225 ASP B C     1 
ATOM   4901  O  O     . ASP B  2  193 ? 89.592 -20.640 -6.342  1.00 72.49  ?  225 ASP B O     1 
ATOM   4902  C  CB    . ASP B  2  193 ? 90.193 -19.998 -3.643  1.00 69.79  ?  225 ASP B CB    1 
ATOM   4903  C  CG    . ASP B  2  193 ? 89.221 -18.821 -3.808  1.00 71.78  ?  225 ASP B CG    1 
ATOM   4904  O  OD1   . ASP B  2  193 ? 87.985 -19.040 -3.926  1.00 81.08  ?  225 ASP B OD1   1 
ATOM   4905  O  OD2   . ASP B  2  193 ? 89.700 -17.668 -3.816  1.00 63.95  -1 225 ASP B OD2   1 
ATOM   4906  N  N     . PRO B  2  194 ? 87.918 -22.037 -5.721  1.00 64.82  ?  226 PRO B N     1 
ATOM   4907  C  CA    . PRO B  2  194 ? 87.386 -22.139 -7.078  1.00 62.26  ?  226 PRO B CA    1 
ATOM   4908  C  C     . PRO B  2  194 ? 86.948 -20.787 -7.621  1.00 55.70  ?  226 PRO B C     1 
ATOM   4909  O  O     . PRO B  2  194 ? 86.460 -19.971 -6.850  1.00 65.57  ?  226 PRO B O     1 
ATOM   4910  C  CB    . PRO B  2  194 ? 86.179 -23.088 -6.939  1.00 64.22  ?  226 PRO B CB    1 
ATOM   4911  C  CG    . PRO B  2  194 ? 86.248 -23.677 -5.583  1.00 65.12  ?  226 PRO B CG    1 
ATOM   4912  C  CD    . PRO B  2  194 ? 87.118 -22.787 -4.743  1.00 65.93  ?  226 PRO B CD    1 
ATOM   4913  N  N     . ALA B  2  195 ? 87.152 -20.572 -8.922  1.00 47.26  ?  227 ALA B N     1 
ATOM   4914  C  CA    . ALA B  2  195 ? 86.800 -19.338 -9.649  1.00 43.22  ?  227 ALA B CA    1 
ATOM   4915  C  C     . ALA B  2  195 ? 87.025 -18.048 -8.868  1.00 44.71  ?  227 ALA B C     1 
ATOM   4916  O  O     . ALA B  2  195 ? 86.302 -17.074 -9.089  1.00 38.68  ?  227 ALA B O     1 
ATOM   4917  C  CB    . ALA B  2  195 ? 85.340 -19.355 -9.996  1.00 42.26  ?  227 ALA B CB    1 
ATOM   4918  N  N     . ASN B  2  196 ? 88.074 -18.041 -8.027  1.00 51.41  ?  228 ASN B N     1 
ATOM   4919  C  CA    . ASN B  2  196 ? 88.385 -16.975 -7.043  1.00 56.55  ?  228 ASN B CA    1 
ATOM   4920  C  C     . ASN B  2  196 ? 87.182 -16.250 -6.412  1.00 56.49  ?  228 ASN B C     1 
ATOM   4921  O  O     . ASN B  2  196 ? 86.998 -15.046 -6.553  1.00 58.10  ?  228 ASN B O     1 
ATOM   4922  C  CB    . ASN B  2  196 ? 89.345 -15.995 -7.736  1.00 60.09  ?  228 ASN B CB    1 
ATOM   4923  C  CG    . ASN B  2  196 ? 90.641 -16.661 -8.172  1.00 62.12  ?  228 ASN B CG    1 
ATOM   4924  O  OD1   . ASN B  2  196 ? 91.107 -17.632 -7.553  1.00 60.43  ?  228 ASN B OD1   1 
ATOM   4925  N  ND2   . ASN B  2  196 ? 91.226 -16.152 -9.253  1.00 64.57  ?  228 ASN B ND2   1 
ATOM   4926  N  N     . GLN B  2  197 ? 86.387 -17.013 -5.681  1.00 57.56  ?  229 GLN B N     1 
ATOM   4927  C  CA    . GLN B  2  197 ? 85.116 -16.543 -5.184  1.00 57.36  ?  229 GLN B CA    1 
ATOM   4928  C  C     . GLN B  2  197 ? 85.220 -16.013 -3.777  1.00 59.17  ?  229 GLN B C     1 
ATOM   4929  O  O     . GLN B  2  197 ? 84.496 -15.081 -3.402  1.00 58.55  ?  229 GLN B O     1 
ATOM   4930  C  CB    . GLN B  2  197 ? 84.121 -17.691 -5.202  1.00 57.53  ?  229 GLN B CB    1 
ATOM   4931  C  CG    . GLN B  2  197 ? 82.763 -17.326 -4.620  1.00 57.01  ?  229 GLN B CG    1 
ATOM   4932  C  CD    . GLN B  2  197 ? 81.655 -18.200 -5.151  1.00 53.27  ?  229 GLN B CD    1 
ATOM   4933  O  OE1   . GLN B  2  197 ? 81.566 -19.384 -4.815  1.00 50.64  ?  229 GLN B OE1   1 
ATOM   4934  N  NE2   . GLN B  2  197 ? 80.799 -17.619 -5.989  1.00 49.46  ?  229 GLN B NE2   1 
ATOM   4935  N  N     . PHE B  2  198 ? 86.079 -16.639 -2.981  1.00 61.60  ?  230 PHE B N     1 
ATOM   4936  C  CA    . PHE B  2  198 ? 86.264 -16.208 -1.607  1.00 66.85  ?  230 PHE B CA    1 
ATOM   4937  C  C     . PHE B  2  198 ? 86.987 -14.857 -1.606  1.00 71.69  ?  230 PHE B C     1 
ATOM   4938  O  O     . PHE B  2  198 ? 86.646 -13.956 -0.822  1.00 74.75  ?  230 PHE B O     1 
ATOM   4939  C  CB    . PHE B  2  198 ? 87.045 -17.256 -0.807  1.00 66.40  ?  230 PHE B CB    1 
ATOM   4940  C  CG    . PHE B  2  198 ? 86.399 -18.609 -0.787  1.00 65.75  ?  230 PHE B CG    1 
ATOM   4941  C  CD1   . PHE B  2  198 ? 85.063 -18.748 -0.443  1.00 67.07  ?  230 PHE B CD1   1 
ATOM   4942  C  CD2   . PHE B  2  198 ? 87.132 -19.749 -1.103  1.00 67.05  ?  230 PHE B CD2   1 
ATOM   4943  C  CE1   . PHE B  2  198 ? 84.468 -19.994 -0.426  1.00 68.45  ?  230 PHE B CE1   1 
ATOM   4944  C  CE2   . PHE B  2  198 ? 86.542 -20.999 -1.092  1.00 67.94  ?  230 PHE B CE2   1 
ATOM   4945  C  CZ    . PHE B  2  198 ? 85.209 -21.122 -0.745  1.00 69.01  ?  230 PHE B CZ    1 
ATOM   4946  N  N     . GLU B  2  199 ? 87.970 -14.732 -2.502  1.00 70.04  ?  231 GLU B N     1 
ATOM   4947  C  CA    . GLU B  2  199 ? 88.716 -13.491 -2.719  1.00 71.50  ?  231 GLU B CA    1 
ATOM   4948  C  C     . GLU B  2  199 ? 87.774 -12.335 -3.070  1.00 68.52  ?  231 GLU B C     1 
ATOM   4949  O  O     . GLU B  2  199 ? 87.861 -11.251 -2.502  1.00 65.85  ?  231 GLU B O     1 
ATOM   4950  C  CB    . GLU B  2  199 ? 89.712 -13.712 -3.858  1.00 79.82  ?  231 GLU B CB    1 
ATOM   4951  C  CG    . GLU B  2  199 ? 90.740 -12.614 -4.073  1.00 86.27  ?  231 GLU B CG    1 
ATOM   4952  C  CD    . GLU B  2  199 ? 91.687 -12.931 -5.227  1.00 91.17  ?  231 GLU B CD    1 
ATOM   4953  O  OE1   . GLU B  2  199 ? 91.377 -13.835 -6.044  1.00 87.79  ?  231 GLU B OE1   1 
ATOM   4954  O  OE2   . GLU B  2  199 ? 92.753 -12.276 -5.317  1.00 95.18  -1 231 GLU B OE2   1 
ATOM   4955  N  N     . TRP B  2  200 ? 86.870 -12.595 -4.007  1.00 67.26  ?  232 TRP B N     1 
ATOM   4956  C  CA    . TRP B  2  200 ? 85.856 -11.627 -4.446  1.00 66.86  ?  232 TRP B CA    1 
ATOM   4957  C  C     . TRP B  2  200 ? 84.741 -11.376 -3.401  1.00 63.86  ?  232 TRP B C     1 
ATOM   4958  O  O     . TRP B  2  200 ? 84.188 -10.270 -3.328  1.00 58.95  ?  232 TRP B O     1 
ATOM   4959  C  CB    . TRP B  2  200 ? 85.247 -12.115 -5.770  1.00 69.13  ?  232 TRP B CB    1 
ATOM   4960  C  CG    . TRP B  2  200 ? 84.317 -11.148 -6.429  1.00 68.51  ?  232 TRP B CG    1 
ATOM   4961  C  CD1   . TRP B  2  200 ? 84.644 -10.149 -7.306  1.00 73.18  ?  232 TRP B CD1   1 
ATOM   4962  C  CD2   . TRP B  2  200 ? 82.906 -11.098 -6.273  1.00 63.56  ?  232 TRP B CD2   1 
ATOM   4963  N  NE1   . TRP B  2  200 ? 83.510 -9.473  -7.694  1.00 72.19  ?  232 TRP B NE1   1 
ATOM   4964  C  CE2   . TRP B  2  200 ? 82.431 -10.036 -7.069  1.00 64.82  ?  232 TRP B CE2   1 
ATOM   4965  C  CE3   . TRP B  2  200 ? 81.995 -11.846 -5.531  1.00 62.67  ?  232 TRP B CE3   1 
ATOM   4966  C  CZ2   . TRP B  2  200 ? 81.091 -9.709  -7.145  1.00 62.22  ?  232 TRP B CZ2   1 
ATOM   4967  C  CZ3   . TRP B  2  200 ? 80.665 -11.524 -5.612  1.00 62.11  ?  232 TRP B CZ3   1 
ATOM   4968  C  CH2   . TRP B  2  200 ? 80.225 -10.466 -6.413  1.00 61.71  ?  232 TRP B CH2   1 
ATOM   4969  N  N     . LEU B  2  201 ? 84.407 -12.405 -2.618  1.00 62.61  ?  233 LEU B N     1 
ATOM   4970  C  CA    . LEU B  2  201 ? 83.468 -12.273 -1.495  1.00 61.13  ?  233 LEU B CA    1 
ATOM   4971  C  C     . LEU B  2  201 ? 84.047 -11.330 -0.435  1.00 60.37  ?  233 LEU B C     1 
ATOM   4972  O  O     . LEU B  2  201 ? 83.439 -10.300 -0.103  1.00 53.82  ?  233 LEU B O     1 
ATOM   4973  C  CB    . LEU B  2  201 ? 83.156 -13.652 -0.881  1.00 59.33  ?  233 LEU B CB    1 
ATOM   4974  C  CG    . LEU B  2  201 ? 82.171 -13.699 0.293   1.00 55.07  ?  233 LEU B CG    1 
ATOM   4975  C  CD1   . LEU B  2  201 ? 80.829 -13.128 -0.112  1.00 53.78  ?  233 LEU B CD1   1 
ATOM   4976  C  CD2   . LEU B  2  201 ? 82.015 -15.132 0.735   1.00 54.91  ?  233 LEU B CD2   1 
ATOM   4977  N  N     . GLU B  2  202 ? 85.228 -11.696 0.072   1.00 59.83  ?  234 GLU B N     1 
ATOM   4978  C  CA    . GLU B  2  202 ? 85.998 -10.844 0.970   1.00 62.48  ?  234 GLU B CA    1 
ATOM   4979  C  C     . GLU B  2  202 ? 86.135 -9.425  0.409   1.00 65.46  ?  234 GLU B C     1 
ATOM   4980  O  O     . GLU B  2  202 ? 85.887 -8.450  1.125   1.00 65.96  ?  234 GLU B O     1 
ATOM   4981  C  CB    . GLU B  2  202 ? 87.380 -11.458 1.243   1.00 63.63  ?  234 GLU B CB    1 
ATOM   4982  C  CG    . GLU B  2  202 ? 87.423 -12.328 2.494   1.00 67.84  ?  234 GLU B CG    1 
ATOM   4983  C  CD    . GLU B  2  202 ? 88.494 -13.409 2.470   1.00 69.13  ?  234 GLU B CD    1 
ATOM   4984  O  OE1   . GLU B  2  202 ? 88.858 -13.879 1.365   1.00 62.13  ?  234 GLU B OE1   1 
ATOM   4985  O  OE2   . GLU B  2  202 ? 88.947 -13.803 3.574   1.00 71.68  -1 234 GLU B OE2   1 
ATOM   4986  N  N     . SER B  2  203 ? 86.515 -9.332  -0.871  1.00 68.27  ?  235 SER B N     1 
ATOM   4987  C  CA    . SER B  2  203 ? 86.647 -8.050  -1.603  1.00 69.11  ?  235 SER B CA    1 
ATOM   4988  C  C     . SER B  2  203 ? 85.349 -7.226  -1.638  1.00 72.81  ?  235 SER B C     1 
ATOM   4989  O  O     . SER B  2  203 ? 85.367 -6.025  -1.335  1.00 73.50  ?  235 SER B O     1 
ATOM   4990  C  CB    . SER B  2  203 ? 87.136 -8.308  -3.046  1.00 65.55  ?  235 SER B CB    1 
ATOM   4991  O  OG    . SER B  2  203 ? 87.183 -7.126  -3.831  1.00 59.60  ?  235 SER B OG    1 
ATOM   4992  N  N     . THR B  2  204 ? 84.238 -7.868  -2.005  1.00 74.93  ?  236 THR B N     1 
ATOM   4993  C  CA    . THR B  2  204 ? 82.946 -7.181  -2.130  1.00 79.18  ?  236 THR B CA    1 
ATOM   4994  C  C     . THR B  2  204 ? 82.338 -6.794  -0.774  1.00 88.16  ?  236 THR B C     1 
ATOM   4995  O  O     . THR B  2  204 ? 81.685 -5.750  -0.659  1.00 91.42  ?  236 THR B O     1 
ATOM   4996  C  CB    . THR B  2  204 ? 81.918 -8.034  -2.900  1.00 76.85  ?  236 THR B CB    1 
ATOM   4997  O  OG1   . THR B  2  204 ? 82.524 -8.565  -4.086  1.00 78.91  ?  236 THR B OG1   1 
ATOM   4998  C  CG2   . THR B  2  204 ? 80.683 -7.190  -3.277  1.00 71.41  ?  236 THR B CG2   1 
ATOM   4999  N  N     . LEU B  2  205 ? 82.533 -7.640  0.240   1.00 91.81  ?  237 LEU B N     1 
ATOM   5000  C  CA    . LEU B  2  205 ? 82.029 -7.357  1.591   1.00 86.52  ?  237 LEU B CA    1 
ATOM   5001  C  C     . LEU B  2  205 ? 82.819 -6.209  2.218   1.00 84.88  ?  237 LEU B C     1 
ATOM   5002  O  O     . LEU B  2  205 ? 82.226 -5.214  2.643   1.00 84.68  ?  237 LEU B O     1 
ATOM   5003  C  CB    . LEU B  2  205 ? 82.081 -8.615  2.470   1.00 83.13  ?  237 LEU B CB    1 
ATOM   5004  C  CG    . LEU B  2  205 ? 81.097 -9.727  2.075   1.00 76.28  ?  237 LEU B CG    1 
ATOM   5005  C  CD1   . LEU B  2  205 ? 81.463 -11.038 2.764   1.00 74.32  ?  237 LEU B CD1   1 
ATOM   5006  C  CD2   . LEU B  2  205 ? 79.661 -9.312  2.371   1.00 70.79  ?  237 LEU B CD2   1 
ATOM   5007  N  N     . ASN B  2  206 ? 84.147 -6.350  2.250   1.00 81.56  ?  238 ASN B N     1 
ATOM   5008  C  CA    . ASN B  2  206 ? 85.061 -5.266  2.650   1.00 77.73  ?  238 ASN B CA    1 
ATOM   5009  C  C     . ASN B  2  206 ? 84.661 -3.923  2.021   1.00 76.06  ?  238 ASN B C     1 
ATOM   5010  O  O     . ASN B  2  206 ? 84.527 -2.909  2.725   1.00 73.32  ?  238 ASN B O     1 
ATOM   5011  C  CB    . ASN B  2  206 ? 86.509 -5.635  2.283   1.00 76.98  ?  238 ASN B CB    1 
ATOM   5012  C  CG    . ASN B  2  206 ? 87.544 -4.799  3.026   1.00 78.32  ?  238 ASN B CG    1 
ATOM   5013  O  OD1   . ASN B  2  206 ? 87.469 -3.572  3.046   1.00 77.87  ?  238 ASN B OD1   1 
ATOM   5014  N  ND2   . ASN B  2  206 ? 88.524 -5.463  3.632   1.00 76.81  ?  238 ASN B ND2   1 
ATOM   5015  N  N     . ASN B  2  207 ? 84.449 -3.943  0.702   1.00 72.93  ?  239 ASN B N     1 
ATOM   5016  C  CA    . ASN B  2  207 ? 83.964 -2.782  -0.059  1.00 68.73  ?  239 ASN B CA    1 
ATOM   5017  C  C     . ASN B  2  207 ? 82.662 -2.185  0.532   1.00 68.30  ?  239 ASN B C     1 
ATOM   5018  O  O     . ASN B  2  207 ? 82.546 -0.977  0.684   1.00 66.82  ?  239 ASN B O     1 
ATOM   5019  C  CB    . ASN B  2  207 ? 83.825 -3.160  -1.557  1.00 66.28  ?  239 ASN B CB    1 
ATOM   5020  C  CG    . ASN B  2  207 ? 83.278 -2.027  -2.423  1.00 68.36  ?  239 ASN B CG    1 
ATOM   5021  O  OD1   . ASN B  2  207 ? 83.338 -0.864  -2.050  1.00 72.26  ?  239 ASN B OD1   1 
ATOM   5022  N  ND2   . ASN B  2  207 ? 82.745 -2.369  -3.598  1.00 69.15  ?  239 ASN B ND2   1 
ATOM   5023  N  N     . SER B  2  208 ? 81.696 -3.022  0.894   1.00 72.32  ?  240 SER B N     1 
ATOM   5024  C  CA    . SER B  2  208 ? 80.417 -2.526  1.433   1.00 74.57  ?  240 SER B CA    1 
ATOM   5025  C  C     . SER B  2  208 ? 80.547 -1.977  2.862   1.00 75.16  ?  240 SER B C     1 
ATOM   5026  O  O     . SER B  2  208 ? 79.786 -1.077  3.278   1.00 64.73  ?  240 SER B O     1 
ATOM   5027  C  CB    . SER B  2  208 ? 79.366 -3.640  1.400   1.00 76.91  ?  240 SER B CB    1 
ATOM   5028  O  OG    . SER B  2  208 ? 79.020 -3.985  0.069   1.00 75.98  ?  240 SER B OG    1 
ATOM   5029  N  N     . GLN B  2  209 ? 81.517 -2.532  3.597   1.00 79.50  ?  241 GLN B N     1 
ATOM   5030  C  CA    . GLN B  2  209 ? 81.750 -2.205  5.006   1.00 79.92  ?  241 GLN B CA    1 
ATOM   5031  C  C     . GLN B  2  209 ? 82.021 -0.729  5.199   1.00 83.68  ?  241 GLN B C     1 
ATOM   5032  O  O     . GLN B  2  209 ? 81.628 -0.163  6.215   1.00 88.11  ?  241 GLN B O     1 
ATOM   5033  C  CB    . GLN B  2  209 ? 82.922 -3.016  5.564   1.00 76.29  ?  241 GLN B CB    1 
ATOM   5034  C  CG    . GLN B  2  209 ? 83.119 -2.889  7.067   1.00 76.21  ?  241 GLN B CG    1 
ATOM   5035  C  CD    . GLN B  2  209 ? 83.658 -4.174  7.698   1.00 77.95  ?  241 GLN B CD    1 
ATOM   5036  O  OE1   . GLN B  2  209 ? 82.951 -5.180  7.764   1.00 77.27  ?  241 GLN B OE1   1 
ATOM   5037  N  NE2   . GLN B  2  209 ? 84.910 -4.144  8.169   1.00 74.53  ?  241 GLN B NE2   1 
ATOM   5038  N  N     . GLN B  2  210 ? 82.686 -0.114  4.221   1.00 86.14  ?  242 GLN B N     1 
ATOM   5039  C  CA    . GLN B  2  210 ? 83.030 1.310   4.286   1.00 87.60  ?  242 GLN B CA    1 
ATOM   5040  C  C     . GLN B  2  210 ? 82.037 2.227   3.585   1.00 85.41  ?  242 GLN B C     1 
ATOM   5041  O  O     . GLN B  2  210 ? 81.849 3.360   4.018   1.00 91.65  ?  242 GLN B O     1 
ATOM   5042  C  CB    . GLN B  2  210 ? 84.424 1.555   3.714   1.00 83.36  ?  242 GLN B CB    1 
ATOM   5043  C  CG    . GLN B  2  210 ? 85.511 0.894   4.529   1.00 80.64  ?  242 GLN B CG    1 
ATOM   5044  C  CD    . GLN B  2  210 ? 86.402 0.064   3.653   1.00 80.71  ?  242 GLN B CD    1 
ATOM   5045  O  OE1   . GLN B  2  210 ? 87.165 0.603   2.861   1.00 81.02  ?  242 GLN B OE1   1 
ATOM   5046  N  NE2   . GLN B  2  210 ? 86.291 -1.258  3.764   1.00 81.78  ?  242 GLN B NE2   1 
ATOM   5047  N  N     . ASN B  2  211 ? 81.389 1.749   2.526   1.00 83.52  ?  243 ASN B N     1 
ATOM   5048  C  CA    . ASN B  2  211 ? 80.474 2.602   1.743   1.00 82.57  ?  243 ASN B CA    1 
ATOM   5049  C  C     . ASN B  2  211 ? 79.077 2.702   2.356   1.00 81.76  ?  243 ASN B C     1 
ATOM   5050  O  O     . ASN B  2  211 ? 78.109 3.014   1.640   1.00 73.07  ?  243 ASN B O     1 
ATOM   5051  C  CB    . ASN B  2  211 ? 80.365 2.106   0.290   1.00 81.18  ?  243 ASN B CB    1 
ATOM   5052  C  CG    . ASN B  2  211 ? 81.722 1.868   -0.350  1.00 78.70  ?  243 ASN B CG    1 
ATOM   5053  O  OD1   . ASN B  2  211 ? 82.726 1.708   0.344   1.00 77.99  ?  243 ASN B OD1   1 
ATOM   5054  N  ND2   . ASN B  2  211 ? 81.760 1.846   -1.672  1.00 75.12  ?  243 ASN B ND2   1 
ATOM   5055  N  N     . LYS B  2  212 ? 78.983 2.455   3.672   1.00 81.79  ?  244 LYS B N     1 
ATOM   5056  C  CA    . LYS B  2  212 ? 77.713 2.443   4.379   1.00 83.02  ?  244 LYS B CA    1 
ATOM   5057  C  C     . LYS B  2  212 ? 76.728 1.592   3.589   1.00 82.41  ?  244 LYS B C     1 
ATOM   5058  O  O     . LYS B  2  212 ? 75.654 2.066   3.188   1.00 81.57  ?  244 LYS B O     1 
ATOM   5059  C  CB    . LYS B  2  212 ? 77.178 3.879   4.582   1.00 85.73  ?  244 LYS B CB    1 
ATOM   5060  C  CG    . LYS B  2  212 ? 76.995 4.305   6.038   1.00 88.47  ?  244 LYS B CG    1 
ATOM   5061  C  CD    . LYS B  2  212 ? 75.731 5.146   6.213   1.00 89.08  ?  244 LYS B CD    1 
ATOM   5062  C  CE    . LYS B  2  212 ? 75.425 5.453   7.674   1.00 89.77  ?  244 LYS B CE    1 
ATOM   5063  N  NZ    . LYS B  2  212 ? 76.037 6.740   8.105   1.00 92.59  1  244 LYS B NZ    1 
ATOM   5064  N  N     . GLU B  2  213 ? 77.115 0.344   3.329   1.00 79.40  ?  245 GLU B N     1 
ATOM   5065  C  CA    . GLU B  2  213 ? 76.240 -0.565  2.594   1.00 76.92  ?  245 GLU B CA    1 
ATOM   5066  C  C     . GLU B  2  213 ? 75.895 -1.822  3.386   1.00 70.01  ?  245 GLU B C     1 
ATOM   5067  O  O     . GLU B  2  213 ? 76.681 -2.313  4.198   1.00 61.88  ?  245 GLU B O     1 
ATOM   5068  C  CB    . GLU B  2  213 ? 76.808 -0.904  1.205   1.00 82.02  ?  245 GLU B CB    1 
ATOM   5069  C  CG    . GLU B  2  213 ? 76.390 0.100   0.124   1.00 86.77  ?  245 GLU B CG    1 
ATOM   5070  C  CD    . GLU B  2  213 ? 76.511 -0.427  -1.306  1.00 89.93  ?  245 GLU B CD    1 
ATOM   5071  O  OE1   . GLU B  2  213 ? 77.234 -1.425  -1.536  1.00 89.60  ?  245 GLU B OE1   1 
ATOM   5072  O  OE2   . GLU B  2  213 ? 75.883 0.174   -2.209  1.00 88.87  -1 245 GLU B OE2   1 
ATOM   5073  N  N     . LYS B  2  214 ? 74.675 -2.299  3.150   1.00 69.34  ?  246 LYS B N     1 
ATOM   5074  C  CA    . LYS B  2  214 ? 74.169 -3.536  3.733   1.00 65.88  ?  246 LYS B CA    1 
ATOM   5075  C  C     . LYS B  2  214 ? 74.077 -4.609  2.632   1.00 60.73  ?  246 LYS B C     1 
ATOM   5076  O  O     . LYS B  2  214 ? 73.594 -4.357  1.513   1.00 58.59  ?  246 LYS B O     1 
ATOM   5077  C  CB    . LYS B  2  214 ? 72.806 -3.297  4.413   1.00 62.95  ?  246 LYS B CB    1 
ATOM   5078  C  CG    . LYS B  2  214 ? 72.818 -2.196  5.474   1.00 61.42  ?  246 LYS B CG    1 
ATOM   5079  C  CD    . LYS B  2  214 ? 73.707 -2.513  6.682   1.00 59.78  ?  246 LYS B CD    1 
ATOM   5080  C  CE    . LYS B  2  214 ? 72.948 -3.281  7.753   1.00 59.99  ?  246 LYS B CE    1 
ATOM   5081  N  NZ    . LYS B  2  214 ? 73.834 -3.970  8.732   1.00 58.15  1  246 LYS B NZ    1 
ATOM   5082  N  N     . VAL B  2  215 ? 74.567 -5.797  2.966   1.00 52.94  ?  247 VAL B N     1 
ATOM   5083  C  CA    . VAL B  2  215 ? 74.595 -6.911  2.048   1.00 49.98  ?  247 VAL B CA    1 
ATOM   5084  C  C     . VAL B  2  215 ? 73.532 -7.938  2.454   1.00 48.08  ?  247 VAL B C     1 
ATOM   5085  O  O     . VAL B  2  215 ? 73.333 -8.196  3.630   1.00 47.30  ?  247 VAL B O     1 
ATOM   5086  C  CB    . VAL B  2  215 ? 76.004 -7.553  2.010   1.00 49.93  ?  247 VAL B CB    1 
ATOM   5087  C  CG1   . VAL B  2  215 ? 75.952 -9.002  1.542   1.00 51.05  ?  247 VAL B CG1   1 
ATOM   5088  C  CG2   . VAL B  2  215 ? 76.937 -6.751  1.113   1.00 48.73  ?  247 VAL B CG2   1 
ATOM   5089  N  N     . TYR B  2  216 ? 72.843 -8.477  1.447   1.00 46.95  ?  248 TYR B N     1 
ATOM   5090  C  CA    . TYR B  2  216 ? 71.969 -9.654  1.545   1.00 44.07  ?  248 TYR B CA    1 
ATOM   5091  C  C     . TYR B  2  216 ? 72.608 -10.786 0.762   1.00 43.26  ?  248 TYR B C     1 
ATOM   5092  O  O     . TYR B  2  216 ? 72.847 -10.618 -0.436  1.00 49.92  ?  248 TYR B O     1 
ATOM   5093  C  CB    . TYR B  2  216 ? 70.612 -9.356  0.886   1.00 42.16  ?  248 TYR B CB    1 
ATOM   5094  C  CG    . TYR B  2  216 ? 69.597 -8.652  1.749   1.00 41.20  ?  248 TYR B CG    1 
ATOM   5095  C  CD1   . TYR B  2  216 ? 69.856 -8.339  3.093   1.00 40.38  ?  248 TYR B CD1   1 
ATOM   5096  C  CD2   . TYR B  2  216 ? 68.349 -8.346  1.235   1.00 41.42  ?  248 TYR B CD2   1 
ATOM   5097  C  CE1   . TYR B  2  216 ? 68.901 -7.727  3.883   1.00 41.17  ?  248 TYR B CE1   1 
ATOM   5098  C  CE2   . TYR B  2  216 ? 67.387 -7.730  2.021   1.00 43.59  ?  248 TYR B CE2   1 
ATOM   5099  C  CZ    . TYR B  2  216 ? 67.670 -7.421  3.346   1.00 42.97  ?  248 TYR B CZ    1 
ATOM   5100  O  OH    . TYR B  2  216 ? 66.718 -6.802  4.124   1.00 45.17  ?  248 TYR B OH    1 
ATOM   5101  N  N     . ILE B  2  217 ? 72.870 -11.932 1.380   1.00 39.23  ?  249 ILE B N     1 
ATOM   5102  C  CA    . ILE B  2  217 ? 73.466 -13.018 0.618   1.00 38.47  ?  249 ILE B CA    1 
ATOM   5103  C  C     . ILE B  2  217 ? 72.440 -13.956 0.007   1.00 39.15  ?  249 ILE B C     1 
ATOM   5104  O  O     . ILE B  2  217 ? 71.591 -14.517 0.687   1.00 40.30  ?  249 ILE B O     1 
ATOM   5105  C  CB    . ILE B  2  217 ? 74.408 -13.864 1.445   1.00 39.47  ?  249 ILE B CB    1 
ATOM   5106  C  CG1   . ILE B  2  217 ? 75.445 -12.996 2.138   1.00 40.72  ?  249 ILE B CG1   1 
ATOM   5107  C  CG2   . ILE B  2  217 ? 75.100 -14.861 0.542   1.00 40.71  ?  249 ILE B CG2   1 
ATOM   5108  C  CD1   . ILE B  2  217 ? 76.379 -12.283 1.196   1.00 40.55  ?  249 ILE B CD1   1 
ATOM   5109  N  N     . ILE B  2  218 ? 72.570 -14.140 -1.293  1.00 39.67  ?  250 ILE B N     1 
ATOM   5110  C  CA    . ILE B  2  218 ? 71.762 -15.055 -2.075  1.00 41.13  ?  250 ILE B CA    1 
ATOM   5111  C  C     . ILE B  2  218 ? 72.719 -16.176 -2.474  1.00 42.08  ?  250 ILE B C     1 
ATOM   5112  O  O     . ILE B  2  218 ? 73.823 -15.922 -2.995  1.00 40.69  ?  250 ILE B O     1 
ATOM   5113  C  CB    . ILE B  2  218 ? 71.184 -14.317 -3.329  1.00 42.35  ?  250 ILE B CB    1 
ATOM   5114  C  CG1   . ILE B  2  218 ? 69.825 -13.755 -3.006  1.00 44.82  ?  250 ILE B CG1   1 
ATOM   5115  C  CG2   . ILE B  2  218 ? 71.005 -15.215 -4.548  1.00 40.64  ?  250 ILE B CG2   1 
ATOM   5116  C  CD1   . ILE B  2  218 ? 69.780 -12.958 -1.727  1.00 47.20  ?  250 ILE B CD1   1 
ATOM   5117  N  N     . ALA B  2  219 ? 72.328 -17.415 -2.208  1.00 40.31  ?  251 ALA B N     1 
ATOM   5118  C  CA    . ALA B  2  219 ? 72.999 -18.536 -2.843  1.00 39.28  ?  251 ALA B CA    1 
ATOM   5119  C  C     . ALA B  2  219 ? 72.049 -19.712 -2.960  1.00 40.72  ?  251 ALA B C     1 
ATOM   5120  O  O     . ALA B  2  219 ? 70.896 -19.635 -2.500  1.00 39.73  ?  251 ALA B O     1 
ATOM   5121  C  CB    . ALA B  2  219 ? 74.247 -18.912 -2.069  1.00 38.78  ?  251 ALA B CB    1 
ATOM   5122  N  N     . HIS B  2  220 ? 72.540 -20.785 -3.595  1.00 43.33  ?  252 HIS B N     1 
ATOM   5123  C  CA    . HIS B  2  220 ? 71.792 -22.068 -3.736  1.00 43.29  ?  252 HIS B CA    1 
ATOM   5124  C  C     . HIS B  2  220 ? 72.062 -23.122 -2.638  1.00 39.83  ?  252 HIS B C     1 
ATOM   5125  O  O     . HIS B  2  220 ? 71.230 -23.326 -1.741  1.00 37.25  ?  252 HIS B O     1 
ATOM   5126  C  CB    . HIS B  2  220 ? 72.060 -22.707 -5.114  1.00 43.46  ?  252 HIS B CB    1 
ATOM   5127  C  CG    . HIS B  2  220 ? 71.204 -23.898 -5.387  1.00 41.02  ?  252 HIS B CG    1 
ATOM   5128  N  ND1   . HIS B  2  220 ? 69.836 -23.806 -5.521  1.00 41.28  ?  252 HIS B ND1   1 
ATOM   5129  C  CD2   . HIS B  2  220 ? 71.510 -25.205 -5.527  1.00 41.94  ?  252 HIS B CD2   1 
ATOM   5130  C  CE1   . HIS B  2  220 ? 69.336 -25.005 -5.746  1.00 41.60  ?  252 HIS B CE1   1 
ATOM   5131  N  NE2   . HIS B  2  220 ? 70.331 -25.872 -5.755  1.00 42.71  ?  252 HIS B NE2   1 
ATOM   5132  N  N     . VAL B  2  221 ? 73.210 -23.791 -2.732  1.00 36.61  ?  253 VAL B N     1 
ATOM   5133  C  CA    . VAL B  2  221 ? 73.590 -24.772 -1.739  1.00 36.06  ?  253 VAL B CA    1 
ATOM   5134  C  C     . VAL B  2  221 ? 73.898 -23.950 -0.488  1.00 35.91  ?  253 VAL B C     1 
ATOM   5135  O  O     . VAL B  2  221 ? 74.791 -23.108 -0.519  1.00 41.78  ?  253 VAL B O     1 
ATOM   5136  C  CB    . VAL B  2  221 ? 74.798 -25.614 -2.226  1.00 34.66  ?  253 VAL B CB    1 
ATOM   5137  C  CG1   . VAL B  2  221 ? 75.188 -26.702 -1.222  1.00 34.16  ?  253 VAL B CG1   1 
ATOM   5138  C  CG2   . VAL B  2  221 ? 74.449 -26.266 -3.549  1.00 33.87  ?  253 VAL B CG2   1 
ATOM   5139  N  N     . PRO B  2  222 ? 73.151 -24.156 0.605   1.00 34.66  ?  254 PRO B N     1 
ATOM   5140  C  CA    . PRO B  2  222 ? 73.465 -23.361 1.765   1.00 35.54  ?  254 PRO B CA    1 
ATOM   5141  C  C     . PRO B  2  222 ? 74.795 -23.795 2.452   1.00 36.36  ?  254 PRO B C     1 
ATOM   5142  O  O     . PRO B  2  222 ? 75.401 -24.821 2.112   1.00 34.58  ?  254 PRO B O     1 
ATOM   5143  C  CB    . PRO B  2  222 ? 72.269 -23.644 2.686   1.00 37.14  ?  254 PRO B CB    1 
ATOM   5144  C  CG    . PRO B  2  222 ? 71.932 -25.086 2.425   1.00 36.79  ?  254 PRO B CG    1 
ATOM   5145  C  CD    . PRO B  2  222 ? 72.242 -25.268 0.947   1.00 36.94  ?  254 PRO B CD    1 
ATOM   5146  N  N     . VAL B  2  223 ? 75.230 -22.993 3.411   1.00 36.17  ?  255 VAL B N     1 
ATOM   5147  C  CA    . VAL B  2  223 ? 76.204 -23.426 4.406   1.00 36.41  ?  255 VAL B CA    1 
ATOM   5148  C  C     . VAL B  2  223 ? 75.596 -24.310 5.527   1.00 33.96  ?  255 VAL B C     1 
ATOM   5149  O  O     . VAL B  2  223 ? 74.373 -24.502 5.648   1.00 30.25  ?  255 VAL B O     1 
ATOM   5150  C  CB    . VAL B  2  223 ? 76.902 -22.203 5.064   1.00 39.24  ?  255 VAL B CB    1 
ATOM   5151  C  CG1   . VAL B  2  223 ? 77.585 -21.346 3.999   1.00 38.86  ?  255 VAL B CG1   1 
ATOM   5152  C  CG2   . VAL B  2  223 ? 75.912 -21.382 5.909   1.00 39.13  ?  255 VAL B CG2   1 
ATOM   5153  N  N     . GLY B  2  224 ? 76.489 -24.848 6.343   1.00 34.05  ?  256 GLY B N     1 
ATOM   5154  C  CA    . GLY B  2  224 ? 76.108 -25.548 7.552   1.00 33.73  ?  256 GLY B CA    1 
ATOM   5155  C  C     . GLY B  2  224 ? 75.655 -26.960 7.284   1.00 32.86  ?  256 GLY B C     1 
ATOM   5156  O  O     . GLY B  2  224 ? 75.849 -27.503 6.199   1.00 31.30  ?  256 GLY B O     1 
ATOM   5157  N  N     . TYR B  2  225 ? 75.016 -27.539 8.287   1.00 33.05  ?  257 TYR B N     1 
ATOM   5158  C  CA    . TYR B  2  225 ? 74.694 -28.954 8.265   1.00 34.89  ?  257 TYR B CA    1 
ATOM   5159  C  C     . TYR B  2  225 ? 73.305 -29.204 7.684   1.00 35.50  ?  257 TYR B C     1 
ATOM   5160  O  O     . TYR B  2  225 ? 72.383 -28.417 7.870   1.00 36.86  ?  257 TYR B O     1 
ATOM   5161  C  CB    . TYR B  2  225 ? 74.931 -29.559 9.663   1.00 33.86  ?  257 TYR B CB    1 
ATOM   5162  C  CG    . TYR B  2  225 ? 76.432 -29.760 9.925   1.00 33.40  ?  257 TYR B CG    1 
ATOM   5163  C  CD1   . TYR B  2  225 ? 77.271 -28.685 10.225  1.00 32.85  ?  257 TYR B CD1   1 
ATOM   5164  C  CD2   . TYR B  2  225 ? 77.015 -31.005 9.798   1.00 34.11  ?  257 TYR B CD2   1 
ATOM   5165  C  CE1   . TYR B  2  225 ? 78.627 -28.864 10.421  1.00 32.58  ?  257 TYR B CE1   1 
ATOM   5166  C  CE2   . TYR B  2  225 ? 78.363 -31.186 9.988   1.00 34.36  ?  257 TYR B CE2   1 
ATOM   5167  C  CZ    . TYR B  2  225 ? 79.154 -30.125 10.304  1.00 33.99  ?  257 TYR B CZ    1 
ATOM   5168  O  OH    . TYR B  2  225 ? 80.476 -30.393 10.479  1.00 36.65  ?  257 TYR B OH    1 
ATOM   5169  N  N     . LEU B  2  226 ? 73.175 -30.264 6.908   1.00 36.07  ?  258 LEU B N     1 
ATOM   5170  C  CA    . LEU B  2  226 ? 71.869 -30.621 6.400   1.00 39.32  ?  258 LEU B CA    1 
ATOM   5171  C  C     . LEU B  2  226 ? 71.079 -31.039 7.602   1.00 39.60  ?  258 LEU B C     1 
ATOM   5172  O  O     . LEU B  2  226 ? 71.598 -31.790 8.440   1.00 42.37  ?  258 LEU B O     1 
ATOM   5173  C  CB    . LEU B  2  226 ? 71.943 -31.789 5.426   1.00 41.16  ?  258 LEU B CB    1 
ATOM   5174  C  CG    . LEU B  2  226 ? 72.612 -31.480 4.096   1.00 39.56  ?  258 LEU B CG    1 
ATOM   5175  C  CD1   . LEU B  2  226 ? 72.886 -32.799 3.384   1.00 37.39  ?  258 LEU B CD1   1 
ATOM   5176  C  CD2   . LEU B  2  226 ? 71.713 -30.522 3.304   1.00 39.98  ?  258 LEU B CD2   1 
ATOM   5177  N  N     . PRO B  2  227 ? 69.836 -30.546 7.727   1.00 37.99  ?  259 PRO B N     1 
ATOM   5178  C  CA    . PRO B  2  227 ? 69.230 -30.842 9.017   1.00 36.41  ?  259 PRO B CA    1 
ATOM   5179  C  C     . PRO B  2  227 ? 68.724 -32.292 9.135   1.00 34.28  ?  259 PRO B C     1 
ATOM   5180  O  O     . PRO B  2  227 ? 68.652 -32.825 10.242  1.00 33.47  ?  259 PRO B O     1 
ATOM   5181  C  CB    . PRO B  2  227 ? 68.111 -29.780 9.146   1.00 35.95  ?  259 PRO B CB    1 
ATOM   5182  C  CG    . PRO B  2  227 ? 68.087 -29.012 7.866   1.00 36.34  ?  259 PRO B CG    1 
ATOM   5183  C  CD    . PRO B  2  227 ? 68.967 -29.715 6.875   1.00 37.24  ?  259 PRO B CD    1 
ATOM   5184  N  N     . SER B  2  228 ? 68.433 -32.951 8.020   1.00 32.58  ?  260 SER B N     1 
ATOM   5185  C  CA    . SER B  2  228 ? 67.736 -34.219 8.125   1.00 33.11  ?  260 SER B CA    1 
ATOM   5186  C  C     . SER B  2  228 ? 68.672 -35.419 8.049   1.00 35.30  ?  260 SER B C     1 
ATOM   5187  O  O     . SER B  2  228 ? 68.253 -36.535 7.688   1.00 34.35  ?  260 SER B O     1 
ATOM   5188  C  CB    . SER B  2  228 ? 66.565 -34.273 7.141   1.00 31.32  ?  260 SER B CB    1 
ATOM   5189  O  OG    . SER B  2  228 ? 65.421 -33.752 7.811   1.00 28.76  ?  260 SER B OG    1 
ATOM   5190  N  N     . SER B  2  229 ? 69.921 -35.182 8.471   1.00 38.68  ?  261 SER B N     1 
ATOM   5191  C  CA    . SER B  2  229 ? 70.993 -36.195 8.483   1.00 41.80  ?  261 SER B CA    1 
ATOM   5192  C  C     . SER B  2  229 ? 72.211 -35.785 9.372   1.00 43.89  ?  261 SER B C     1 
ATOM   5193  O  O     . SER B  2  229 ? 72.447 -34.597 9.590   1.00 44.33  ?  261 SER B O     1 
ATOM   5194  C  CB    . SER B  2  229 ? 71.433 -36.545 7.030   1.00 41.99  ?  261 SER B CB    1 
ATOM   5195  O  OG    . SER B  2  229 ? 71.617 -35.411 6.183   1.00 39.15  ?  261 SER B OG    1 
ATOM   5196  N  N     . GLN B  2  230 ? 72.984 -36.767 9.857   1.00 47.14  ?  262 GLN B N     1 
ATOM   5197  C  CA    . GLN B  2  230 ? 74.059 -36.512 10.846  1.00 48.39  ?  262 GLN B CA    1 
ATOM   5198  C  C     . GLN B  2  230 ? 75.490 -36.205 10.313  1.00 48.72  ?  262 GLN B C     1 
ATOM   5199  O  O     . GLN B  2  230 ? 76.071 -36.964 9.519   1.00 52.39  ?  262 GLN B O     1 
ATOM   5200  C  CB    . GLN B  2  230 ? 74.102 -37.650 11.876  1.00 48.36  ?  262 GLN B CB    1 
ATOM   5201  C  CG    . GLN B  2  230 ? 75.147 -38.739 11.700  1.00 47.72  ?  262 GLN B CG    1 
ATOM   5202  C  CD    . GLN B  2  230 ? 75.239 -39.599 12.945  1.00 46.72  ?  262 GLN B CD    1 
ATOM   5203  O  OE1   . GLN B  2  230 ? 75.568 -39.111 14.024  1.00 40.76  ?  262 GLN B OE1   1 
ATOM   5204  N  NE2   . GLN B  2  230 ? 74.927 -40.885 12.805  1.00 48.72  ?  262 GLN B NE2   1 
ATOM   5205  N  N     . ASN B  2  231 ? 76.072 -35.113 10.806  1.00 45.88  ?  263 ASN B N     1 
ATOM   5206  C  CA    . ASN B  2  231 ? 77.429 -34.674 10.499  1.00 44.34  ?  263 ASN B CA    1 
ATOM   5207  C  C     . ASN B  2  231 ? 77.703 -34.340 9.063   1.00 42.47  ?  263 ASN B C     1 
ATOM   5208  O  O     . ASN B  2  231 ? 78.833 -34.238 8.671   1.00 45.49  ?  263 ASN B O     1 
ATOM   5209  C  CB    . ASN B  2  231 ? 78.434 -35.711 11.000  1.00 46.96  ?  263 ASN B CB    1 
ATOM   5210  C  CG    . ASN B  2  231 ? 79.871 -35.231 10.949  1.00 52.67  ?  263 ASN B CG    1 
ATOM   5211  O  OD1   . ASN B  2  231 ? 80.120 -34.060 10.866  1.00 55.02  ?  263 ASN B OD1   1 
ATOM   5212  N  ND2   . ASN B  2  231 ? 80.817 -36.150 10.968  1.00 59.37  ?  263 ASN B ND2   1 
ATOM   5213  N  N     . ILE B  2  232 ? 76.681 -34.150 8.253   1.00 38.59  ?  264 ILE B N     1 
ATOM   5214  C  CA    . ILE B  2  232 ? 76.925 -33.853 6.830   1.00 36.46  ?  264 ILE B CA    1 
ATOM   5215  C  C     . ILE B  2  232 ? 76.650 -32.394 6.491   1.00 35.32  ?  264 ILE B C     1 
ATOM   5216  O  O     . ILE B  2  232 ? 75.485 -31.966 6.460   1.00 36.39  ?  264 ILE B O     1 
ATOM   5217  C  CB    . ILE B  2  232 ? 76.066 -34.722 5.896   1.00 35.79  ?  264 ILE B CB    1 
ATOM   5218  C  CG1   . ILE B  2  232 ? 76.280 -36.209 6.204   1.00 36.85  ?  264 ILE B CG1   1 
ATOM   5219  C  CG2   . ILE B  2  232 ? 76.376 -34.395 4.436   1.00 34.05  ?  264 ILE B CG2   1 
ATOM   5220  C  CD1   . ILE B  2  232 ? 75.080 -37.079 5.899   1.00 36.94  ?  264 ILE B CD1   1 
ATOM   5221  N  N     . THR B  2  233 ? 77.710 -31.633 6.215   1.00 32.87  ?  265 THR B N     1 
ATOM   5222  C  CA    . THR B  2  233 ? 77.526 -30.290 5.705   1.00 31.70  ?  265 THR B CA    1 
ATOM   5223  C  C     . THR B  2  233 ? 76.986 -30.480 4.313   1.00 30.29  ?  265 THR B C     1 
ATOM   5224  O  O     . THR B  2  233 ? 77.009 -31.583 3.799   1.00 29.47  ?  265 THR B O     1 
ATOM   5225  C  CB    . THR B  2  233 ? 78.821 -29.512 5.679   1.00 32.08  ?  265 THR B CB    1 
ATOM   5226  O  OG1   . THR B  2  233 ? 79.753 -30.233 4.893   1.00 33.70  ?  265 THR B OG1   1 
ATOM   5227  C  CG2   . THR B  2  233 ? 79.374 -29.370 7.071   1.00 31.84  ?  265 THR B CG2   1 
ATOM   5228  N  N     . ALA B  2  234 ? 76.457 -29.430 3.720   1.00 31.19  ?  266 ALA B N     1 
ATOM   5229  C  CA    . ALA B  2  234 ? 75.795 -29.556 2.418   1.00 34.34  ?  266 ALA B CA    1 
ATOM   5230  C  C     . ALA B  2  234 ? 76.824 -29.398 1.299   1.00 35.77  ?  266 ALA B C     1 
ATOM   5231  O  O     . ALA B  2  234 ? 76.884 -30.178 0.338   1.00 34.21  ?  266 ALA B O     1 
ATOM   5232  C  CB    . ALA B  2  234 ? 74.700 -28.503 2.290   1.00 35.14  ?  266 ALA B CB    1 
ATOM   5233  N  N     . MET B  2  235 ? 77.634 -28.361 1.464   1.00 38.21  ?  267 MET B N     1 
ATOM   5234  C  CA    . MET B  2  235 ? 78.823 -28.118 0.671   1.00 38.67  ?  267 MET B CA    1 
ATOM   5235  C  C     . MET B  2  235 ? 79.845 -29.122 1.106   1.00 41.08  ?  267 MET B C     1 
ATOM   5236  O  O     . MET B  2  235 ? 79.538 -29.994 1.897   1.00 43.81  ?  267 MET B O     1 
ATOM   5237  C  CB    . MET B  2  235 ? 79.366 -26.715 0.990   1.00 37.96  ?  267 MET B CB    1 
ATOM   5238  C  CG    . MET B  2  235 ? 78.519 -25.566 0.444   1.00 37.43  ?  267 MET B CG    1 
ATOM   5239  S  SD    . MET B  2  235 ? 78.812 -23.970 1.228   1.00 33.15  ?  267 MET B SD    1 
ATOM   5240  C  CE    . MET B  2  235 ? 80.563 -24.134 1.491   1.00 33.60  ?  267 MET B CE    1 
ATOM   5241  N  N     . ARG B  2  236 ? 81.065 -28.993 0.597   1.00 46.24  ?  268 ARG B N     1 
ATOM   5242  C  CA    . ARG B  2  236 ? 82.225 -29.673 1.196   1.00 48.86  ?  268 ARG B CA    1 
ATOM   5243  C  C     . ARG B  2  236 ? 82.661 -28.998 2.523   1.00 47.45  ?  268 ARG B C     1 
ATOM   5244  O  O     . ARG B  2  236 ? 82.871 -27.777 2.610   1.00 40.53  ?  268 ARG B O     1 
ATOM   5245  C  CB    . ARG B  2  236 ? 83.405 -29.789 0.204   1.00 48.56  ?  268 ARG B CB    1 
ATOM   5246  C  CG    . ARG B  2  236 ? 83.290 -30.944 -0.786  1.00 46.65  ?  268 ARG B CG    1 
ATOM   5247  C  CD    . ARG B  2  236 ? 84.457 -30.969 -1.769  1.00 46.91  ?  268 ARG B CD    1 
ATOM   5248  N  NE    . ARG B  2  236 ? 83.998 -31.304 -3.126  1.00 48.80  ?  268 ARG B NE    1 
ATOM   5249  C  CZ    . ARG B  2  236 ? 84.244 -30.605 -4.239  1.00 48.11  ?  268 ARG B CZ    1 
ATOM   5250  N  NH1   . ARG B  2  236 ? 84.995 -29.505 -4.223  1.00 47.40  1  268 ARG B NH1   1 
ATOM   5251  N  NH2   . ARG B  2  236 ? 83.739 -31.030 -5.392  1.00 47.82  ?  268 ARG B NH2   1 
ATOM   5252  N  N     . GLU B  2  237 ? 82.764 -29.838 3.549   1.00 50.20  ?  269 GLU B N     1 
ATOM   5253  C  CA    . GLU B  2  237 ? 83.212 -29.444 4.862   1.00 53.84  ?  269 GLU B CA    1 
ATOM   5254  C  C     . GLU B  2  237 ? 84.210 -28.340 4.757   1.00 51.61  ?  269 GLU B C     1 
ATOM   5255  O  O     . GLU B  2  237 ? 84.104 -27.341 5.471   1.00 46.29  ?  269 GLU B O     1 
ATOM   5256  C  CB    . GLU B  2  237 ? 83.920 -30.636 5.524   1.00 59.88  ?  269 GLU B CB    1 
ATOM   5257  C  CG    . GLU B  2  237 ? 85.073 -30.318 6.471   1.00 67.45  ?  269 GLU B CG    1 
ATOM   5258  C  CD    . GLU B  2  237 ? 84.646 -30.219 7.921   1.00 72.79  ?  269 GLU B CD    1 
ATOM   5259  O  OE1   . GLU B  2  237 ? 84.219 -29.116 8.326   1.00 78.27  ?  269 GLU B OE1   1 
ATOM   5260  O  OE2   . GLU B  2  237 ? 84.760 -31.234 8.652   1.00 72.10  -1 269 GLU B OE2   1 
ATOM   5261  N  N     . TYR B  2  238 ? 85.155 -28.532 3.829   1.00 53.52  ?  270 TYR B N     1 
ATOM   5262  C  CA    . TYR B  2  238 ? 86.276 -27.604 3.644   1.00 58.48  ?  270 TYR B CA    1 
ATOM   5263  C  C     . TYR B  2  238 ? 85.824 -26.186 3.287   1.00 55.72  ?  270 TYR B C     1 
ATOM   5264  O  O     . TYR B  2  238 ? 86.338 -25.204 3.844   1.00 53.55  ?  270 TYR B O     1 
ATOM   5265  C  CB    . TYR B  2  238 ? 87.316 -28.123 2.606   1.00 61.85  ?  270 TYR B CB    1 
ATOM   5266  C  CG    . TYR B  2  238 ? 88.421 -27.100 2.331   1.00 66.93  ?  270 TYR B CG    1 
ATOM   5267  C  CD1   . TYR B  2  238 ? 89.526 -26.971 3.187   1.00 69.05  ?  270 TYR B CD1   1 
ATOM   5268  C  CD2   . TYR B  2  238 ? 88.327 -26.220 1.250   1.00 68.78  ?  270 TYR B CD2   1 
ATOM   5269  C  CE1   . TYR B  2  238 ? 90.509 -26.015 2.953   1.00 70.94  ?  270 TYR B CE1   1 
ATOM   5270  C  CE2   . TYR B  2  238 ? 89.303 -25.260 1.011   1.00 71.21  ?  270 TYR B CE2   1 
ATOM   5271  C  CZ    . TYR B  2  238 ? 90.392 -25.155 1.860   1.00 71.50  ?  270 TYR B CZ    1 
ATOM   5272  O  OH    . TYR B  2  238 ? 91.350 -24.188 1.613   1.00 66.27  ?  270 TYR B OH    1 
ATOM   5273  N  N     . TYR B  2  239 ? 84.882 -26.063 2.359   1.00 53.55  ?  271 TYR B N     1 
ATOM   5274  C  CA    . TYR B  2  239 ? 84.444 -24.738 1.982   1.00 52.59  ?  271 TYR B CA    1 
ATOM   5275  C  C     . TYR B  2  239 ? 83.454 -24.220 2.992   1.00 51.72  ?  271 TYR B C     1 
ATOM   5276  O  O     . TYR B  2  239 ? 83.437 -23.022 3.253   1.00 49.69  ?  271 TYR B O     1 
ATOM   5277  C  CB    . TYR B  2  239 ? 83.794 -24.712 0.623   1.00 54.43  ?  271 TYR B CB    1 
ATOM   5278  C  CG    . TYR B  2  239 ? 84.645 -25.188 -0.512  1.00 56.54  ?  271 TYR B CG    1 
ATOM   5279  C  CD1   . TYR B  2  239 ? 85.731 -24.470 -0.952  1.00 56.09  ?  271 TYR B CD1   1 
ATOM   5280  C  CD2   . TYR B  2  239 ? 84.315 -26.349 -1.176  1.00 59.90  ?  271 TYR B CD2   1 
ATOM   5281  C  CE1   . TYR B  2  239 ? 86.484 -24.921 -2.014  1.00 60.43  ?  271 TYR B CE1   1 
ATOM   5282  C  CE2   . TYR B  2  239 ? 85.047 -26.805 -2.235  1.00 61.92  ?  271 TYR B CE2   1 
ATOM   5283  C  CZ    . TYR B  2  239 ? 86.130 -26.099 -2.659  1.00 62.48  ?  271 TYR B CZ    1 
ATOM   5284  O  OH    . TYR B  2  239 ? 86.826 -26.607 -3.736  1.00 65.73  ?  271 TYR B OH    1 
ATOM   5285  N  N     . ASN B  2  240 ? 82.614 -25.093 3.555   1.00 52.01  ?  272 ASN B N     1 
ATOM   5286  C  CA    . ASN B  2  240 ? 81.655 -24.618 4.549   1.00 50.32  ?  272 ASN B CA    1 
ATOM   5287  C  C     . ASN B  2  240 ? 82.366 -23.845 5.636   1.00 50.53  ?  272 ASN B C     1 
ATOM   5288  O  O     . ASN B  2  240 ? 81.930 -22.748 5.988   1.00 46.54  ?  272 ASN B O     1 
ATOM   5289  C  CB    . ASN B  2  240 ? 80.859 -25.730 5.205   1.00 50.20  ?  272 ASN B CB    1 
ATOM   5290  C  CG    . ASN B  2  240 ? 80.066 -25.214 6.388   1.00 45.98  ?  272 ASN B CG    1 
ATOM   5291  O  OD1   . ASN B  2  240 ? 79.153 -24.418 6.211   1.00 43.07  ?  272 ASN B OD1   1 
ATOM   5292  N  ND2   . ASN B  2  240 ? 80.454 -25.601 7.597   1.00 43.04  ?  272 ASN B ND2   1 
ATOM   5293  N  N     . GLU B  2  241 ? 83.460 -24.430 6.142   1.00 52.62  ?  273 GLU B N     1 
ATOM   5294  C  CA    . GLU B  2  241 ? 84.313 -23.813 7.186   1.00 54.80  ?  273 GLU B CA    1 
ATOM   5295  C  C     . GLU B  2  241 ? 84.864 -22.437 6.788   1.00 55.83  ?  273 GLU B C     1 
ATOM   5296  O  O     . GLU B  2  241 ? 84.907 -21.506 7.607   1.00 54.32  ?  273 GLU B O     1 
ATOM   5297  C  CB    . GLU B  2  241 ? 85.499 -24.727 7.514   1.00 52.95  ?  273 GLU B CB    1 
ATOM   5298  C  CG    . GLU B  2  241 ? 85.139 -26.031 8.216   1.00 54.49  ?  273 GLU B CG    1 
ATOM   5299  C  CD    . GLU B  2  241 ? 84.657 -25.836 9.647   1.00 56.91  ?  273 GLU B CD    1 
ATOM   5300  O  OE1   . GLU B  2  241 ? 84.974 -24.803 10.278  1.00 58.07  ?  273 GLU B OE1   1 
ATOM   5301  O  OE2   . GLU B  2  241 ? 83.954 -26.734 10.150  1.00 60.61  -1 273 GLU B OE2   1 
ATOM   5302  N  N     . LYS B  2  242 ? 85.275 -22.351 5.522   1.00 54.89  ?  274 LYS B N     1 
ATOM   5303  C  CA    . LYS B  2  242 ? 85.927 -21.179 4.936   1.00 54.60  ?  274 LYS B CA    1 
ATOM   5304  C  C     . LYS B  2  242 ? 84.952 -20.024 4.748   1.00 50.65  ?  274 LYS B C     1 
ATOM   5305  O  O     . LYS B  2  242 ? 85.325 -18.874 4.886   1.00 49.25  ?  274 LYS B O     1 
ATOM   5306  C  CB    . LYS B  2  242 ? 86.521 -21.589 3.582   1.00 59.55  ?  274 LYS B CB    1 
ATOM   5307  C  CG    . LYS B  2  242 ? 87.805 -20.899 3.154   1.00 63.41  ?  274 LYS B CG    1 
ATOM   5308  C  CD    . LYS B  2  242 ? 88.672 -21.872 2.352   1.00 66.31  ?  274 LYS B CD    1 
ATOM   5309  C  CE    . LYS B  2  242 ? 89.662 -21.160 1.443   1.00 68.84  ?  274 LYS B CE    1 
ATOM   5310  N  NZ    . LYS B  2  242 ? 90.730 -20.479 2.224   1.00 71.59  1  274 LYS B NZ    1 
ATOM   5311  N  N     . LEU B  2  243 ? 83.707 -20.348 4.414   1.00 49.84  ?  275 LEU B N     1 
ATOM   5312  C  CA    . LEU B  2  243 ? 82.641 -19.361 4.249   1.00 48.40  ?  275 LEU B CA    1 
ATOM   5313  C  C     . LEU B  2  243 ? 82.065 -18.913 5.580   1.00 52.36  ?  275 LEU B C     1 
ATOM   5314  O  O     . LEU B  2  243 ? 81.610 -17.773 5.707   1.00 52.85  ?  275 LEU B O     1 
ATOM   5315  C  CB    . LEU B  2  243 ? 81.490 -19.949 3.444   1.00 47.51  ?  275 LEU B CB    1 
ATOM   5316  C  CG    . LEU B  2  243 ? 81.624 -20.055 1.938   1.00 47.94  ?  275 LEU B CG    1 
ATOM   5317  C  CD1   . LEU B  2  243 ? 80.380 -20.718 1.366   1.00 48.88  ?  275 LEU B CD1   1 
ATOM   5318  C  CD2   . LEU B  2  243 ? 81.835 -18.685 1.308   1.00 49.16  ?  275 LEU B CD2   1 
ATOM   5319  N  N     . ILE B  2  244 ? 82.029 -19.825 6.555   1.00 54.45  ?  276 ILE B N     1 
ATOM   5320  C  CA    . ILE B  2  244 ? 81.563 -19.494 7.907   1.00 53.96  ?  276 ILE B CA    1 
ATOM   5321  C  C     . ILE B  2  244 ? 82.424 -18.374 8.469   1.00 52.21  ?  276 ILE B C     1 
ATOM   5322  O  O     . ILE B  2  244 ? 81.917 -17.321 8.856   1.00 45.95  ?  276 ILE B O     1 
ATOM   5323  C  CB    . ILE B  2  244 ? 81.605 -20.734 8.831   1.00 54.74  ?  276 ILE B CB    1 
ATOM   5324  C  CG1   . ILE B  2  244 ? 80.486 -21.713 8.459   1.00 59.60  ?  276 ILE B CG1   1 
ATOM   5325  C  CG2   . ILE B  2  244 ? 81.476 -20.340 10.291  1.00 54.92  ?  276 ILE B CG2   1 
ATOM   5326  C  CD1   . ILE B  2  244 ? 79.150 -21.064 8.122   1.00 60.93  ?  276 ILE B CD1   1 
ATOM   5327  N  N     . ASP B  2  245 ? 83.731 -18.609 8.462   1.00 53.80  ?  277 ASP B N     1 
ATOM   5328  C  CA    . ASP B  2  245 ? 84.688 -17.632 8.921   1.00 56.39  ?  277 ASP B CA    1 
ATOM   5329  C  C     . ASP B  2  245 ? 84.466 -16.307 8.209   1.00 54.67  ?  277 ASP B C     1 
ATOM   5330  O  O     . ASP B  2  245 ? 84.380 -15.268 8.866   1.00 55.80  ?  277 ASP B O     1 
ATOM   5331  C  CB    . ASP B  2  245 ? 86.108 -18.156 8.729   1.00 63.04  ?  277 ASP B CB    1 
ATOM   5332  C  CG    . ASP B  2  245 ? 86.439 -19.316 9.686   1.00 72.28  ?  277 ASP B CG    1 
ATOM   5333  O  OD1   . ASP B  2  245 ? 86.235 -19.150 10.909  1.00 77.87  ?  277 ASP B OD1   1 
ATOM   5334  O  OD2   . ASP B  2  245 ? 86.899 -20.393 9.225   1.00 77.95  -1 277 ASP B OD2   1 
ATOM   5335  N  N     . ILE B  2  246 ? 84.316 -16.343 6.887   1.00 51.67  ?  278 ILE B N     1 
ATOM   5336  C  CA    . ILE B  2  246 ? 84.041 -15.120 6.117   1.00 52.57  ?  278 ILE B CA    1 
ATOM   5337  C  C     . ILE B  2  246 ? 82.751 -14.469 6.586   1.00 52.90  ?  278 ILE B C     1 
ATOM   5338  O  O     . ILE B  2  246 ? 82.674 -13.239 6.658   1.00 53.36  ?  278 ILE B O     1 
ATOM   5339  C  CB    . ILE B  2  246 ? 83.947 -15.353 4.572   1.00 53.68  ?  278 ILE B CB    1 
ATOM   5340  C  CG1   . ILE B  2  246 ? 85.319 -15.718 3.987   1.00 53.86  ?  278 ILE B CG1   1 
ATOM   5341  C  CG2   . ILE B  2  246 ? 83.411 -14.105 3.839   1.00 52.44  ?  278 ILE B CG2   1 
ATOM   5342  C  CD1   . ILE B  2  246 ? 85.261 -16.424 2.643   1.00 53.40  ?  278 ILE B CD1   1 
ATOM   5343  N  N     . PHE B  2  247 ? 81.732 -15.281 6.869   1.00 54.12  ?  279 PHE B N     1 
ATOM   5344  C  CA    . PHE B  2  247 ? 80.435 -14.739 7.289   1.00 55.78  ?  279 PHE B CA    1 
ATOM   5345  C  C     . PHE B  2  247 ? 80.585 -14.174 8.694   1.00 51.74  ?  279 PHE B C     1 
ATOM   5346  O  O     . PHE B  2  247 ? 80.033 -13.124 9.016   1.00 45.45  ?  279 PHE B O     1 
ATOM   5347  C  CB    . PHE B  2  247 ? 79.308 -15.800 7.229   1.00 60.38  ?  279 PHE B CB    1 
ATOM   5348  C  CG    . PHE B  2  247 ? 78.888 -16.211 5.817   1.00 63.85  ?  279 PHE B CG    1 
ATOM   5349  C  CD1   . PHE B  2  247 ? 78.770 -15.268 4.776   1.00 65.30  ?  279 PHE B CD1   1 
ATOM   5350  C  CD2   . PHE B  2  247 ? 78.558 -17.541 5.536   1.00 62.93  ?  279 PHE B CD2   1 
ATOM   5351  C  CE1   . PHE B  2  247 ? 78.373 -15.652 3.493   1.00 64.36  ?  279 PHE B CE1   1 
ATOM   5352  C  CE2   . PHE B  2  247 ? 78.160 -17.921 4.254   1.00 64.01  ?  279 PHE B CE2   1 
ATOM   5353  C  CZ    . PHE B  2  247 ? 78.068 -16.982 3.233   1.00 64.72  ?  279 PHE B CZ    1 
ATOM   5354  N  N     . GLN B  2  248 ? 81.368 -14.869 9.513   1.00 51.92  ?  280 GLN B N     1 
ATOM   5355  C  CA    . GLN B  2  248 ? 81.668 -14.414 10.857  1.00 51.77  ?  280 GLN B CA    1 
ATOM   5356  C  C     . GLN B  2  248 ? 82.340 -13.052 10.869  1.00 55.97  ?  280 GLN B C     1 
ATOM   5357  O  O     . GLN B  2  248 ? 81.815 -12.112 11.484  1.00 56.79  ?  280 GLN B O     1 
ATOM   5358  C  CB    . GLN B  2  248 ? 82.532 -15.432 11.580  1.00 49.44  ?  280 GLN B CB    1 
ATOM   5359  C  CG    . GLN B  2  248 ? 81.692 -16.458 12.303  1.00 48.28  ?  280 GLN B CG    1 
ATOM   5360  C  CD    . GLN B  2  248 ? 82.467 -17.704 12.658  1.00 48.79  ?  280 GLN B CD    1 
ATOM   5361  O  OE1   . GLN B  2  248 ? 83.527 -17.995 12.095  1.00 48.87  ?  280 GLN B OE1   1 
ATOM   5362  N  NE2   . GLN B  2  248 ? 81.930 -18.463 13.590  1.00 48.85  ?  280 GLN B NE2   1 
ATOM   5363  N  N     . LYS B  2  249 ? 83.486 -12.940 10.195  1.00 57.92  ?  281 LYS B N     1 
ATOM   5364  C  CA    . LYS B  2  249 ? 84.203 -11.656 10.123  1.00 59.53  ?  281 LYS B CA    1 
ATOM   5365  C  C     . LYS B  2  249 ? 83.267 -10.480 9.721   1.00 59.75  ?  281 LYS B C     1 
ATOM   5366  O  O     . LYS B  2  249 ? 83.205 -9.474  10.427  1.00 61.90  ?  281 LYS B O     1 
ATOM   5367  C  CB    . LYS B  2  249 ? 85.432 -11.743 9.193   1.00 61.68  ?  281 LYS B CB    1 
ATOM   5368  C  CG    . LYS B  2  249 ? 86.509 -12.744 9.637   1.00 66.62  ?  281 LYS B CG    1 
ATOM   5369  C  CD    . LYS B  2  249 ? 87.917 -12.439 9.096   1.00 68.21  ?  281 LYS B CD    1 
ATOM   5370  C  CE    . LYS B  2  249 ? 88.044 -12.489 7.565   1.00 70.26  ?  281 LYS B CE    1 
ATOM   5371  N  NZ    . LYS B  2  249 ? 88.278 -13.854 6.989   1.00 67.68  1  281 LYS B NZ    1 
ATOM   5372  N  N     . TYR B  2  250 ? 82.504 -10.633 8.638   1.00 59.11  ?  282 TYR B N     1 
ATOM   5373  C  CA    . TYR B  2  250 ? 81.718 -9.529  8.062   1.00 57.47  ?  282 TYR B CA    1 
ATOM   5374  C  C     . TYR B  2  250 ? 80.224 -9.523  8.441   1.00 56.46  ?  282 TYR B C     1 
ATOM   5375  O  O     . TYR B  2  250 ? 79.393 -9.031  7.663   1.00 54.35  ?  282 TYR B O     1 
ATOM   5376  C  CB    . TYR B  2  250 ? 81.864 -9.555  6.532   1.00 59.08  ?  282 TYR B CB    1 
ATOM   5377  C  CG    . TYR B  2  250 ? 83.257 -9.200  6.056   1.00 62.42  ?  282 TYR B CG    1 
ATOM   5378  C  CD1   . TYR B  2  250 ? 83.562 -7.900  5.643   1.00 61.51  ?  282 TYR B CD1   1 
ATOM   5379  C  CD2   . TYR B  2  250 ? 84.277 -10.161 6.030   1.00 64.80  ?  282 TYR B CD2   1 
ATOM   5380  C  CE1   . TYR B  2  250 ? 84.832 -7.572  5.219   1.00 62.03  ?  282 TYR B CE1   1 
ATOM   5381  C  CE2   . TYR B  2  250 ? 85.556 -9.838  5.604   1.00 64.73  ?  282 TYR B CE2   1 
ATOM   5382  C  CZ    . TYR B  2  250 ? 85.821 -8.540  5.204   1.00 65.18  ?  282 TYR B CZ    1 
ATOM   5383  O  OH    . TYR B  2  250 ? 87.076 -8.196  4.786   1.00 69.61  ?  282 TYR B OH    1 
ATOM   5384  N  N     . SER B  2  251 ? 79.883 -10.031 9.631   1.00 54.25  ?  283 SER B N     1 
ATOM   5385  C  CA    . SER B  2  251 ? 78.465 -10.218 10.016  1.00 52.35  ?  283 SER B CA    1 
ATOM   5386  C  C     . SER B  2  251 ? 77.729 -8.896  10.213  1.00 52.30  ?  283 SER B C     1 
ATOM   5387  O  O     . SER B  2  251 ? 76.507 -8.817  10.038  1.00 47.38  ?  283 SER B O     1 
ATOM   5388  C  CB    . SER B  2  251 ? 78.316 -11.123 11.262  1.00 51.60  ?  283 SER B CB    1 
ATOM   5389  O  OG    . SER B  2  251 ? 78.479 -10.416 12.480  1.00 50.82  ?  283 SER B OG    1 
ATOM   5390  N  N     . ASP B  2  252 ? 78.487 -7.864  10.576  1.00 57.35  ?  284 ASP B N     1 
ATOM   5391  C  CA    . ASP B  2  252 ? 77.945 -6.506  10.732  1.00 60.18  ?  284 ASP B CA    1 
ATOM   5392  C  C     . ASP B  2  252 ? 77.396 -5.958  9.405   1.00 56.32  ?  284 ASP B C     1 
ATOM   5393  O  O     . ASP B  2  252 ? 76.508 -5.116  9.413   1.00 54.07  ?  284 ASP B O     1 
ATOM   5394  C  CB    . ASP B  2  252 ? 78.981 -5.544  11.368  1.00 63.80  ?  284 ASP B CB    1 
ATOM   5395  C  CG    . ASP B  2  252 ? 80.432 -5.877  10.975  1.00 68.71  ?  284 ASP B CG    1 
ATOM   5396  O  OD1   . ASP B  2  252 ? 81.003 -6.839  11.554  1.00 65.95  ?  284 ASP B OD1   1 
ATOM   5397  O  OD2   . ASP B  2  252 ? 80.993 -5.178  10.094  1.00 69.22  -1 284 ASP B OD2   1 
ATOM   5398  N  N     . VAL B  2  253 ? 77.896 -6.463  8.276   1.00 57.75  ?  285 VAL B N     1 
ATOM   5399  C  CA    . VAL B  2  253 ? 77.444 -6.016  6.940   1.00 57.20  ?  285 VAL B CA    1 
ATOM   5400  C  C     . VAL B  2  253 ? 76.269 -6.832  6.388   1.00 56.18  ?  285 VAL B C     1 
ATOM   5401  O  O     . VAL B  2  253 ? 75.371 -6.263  5.753   1.00 57.19  ?  285 VAL B O     1 
ATOM   5402  C  CB    . VAL B  2  253 ? 78.561 -6.092  5.875   1.00 55.56  ?  285 VAL B CB    1 
ATOM   5403  C  CG1   . VAL B  2  253 ? 78.225 -5.162  4.716   1.00 53.14  ?  285 VAL B CG1   1 
ATOM   5404  C  CG2   . VAL B  2  253 ? 79.919 -5.739  6.475   1.00 57.43  ?  285 VAL B CG2   1 
ATOM   5405  N  N     . ILE B  2  254 ? 76.295 -8.152  6.612   1.00 51.51  ?  286 ILE B N     1 
ATOM   5406  C  CA    . ILE B  2  254 ? 75.269 -9.058  6.099   1.00 48.06  ?  286 ILE B CA    1 
ATOM   5407  C  C     . ILE B  2  254 ? 74.037 -8.957  7.007   1.00 48.38  ?  286 ILE B C     1 
ATOM   5408  O  O     . ILE B  2  254 ? 74.137 -9.170  8.213   1.00 53.32  ?  286 ILE B O     1 
ATOM   5409  C  CB    . ILE B  2  254 ? 75.730 -10.536 6.075   1.00 48.45  ?  286 ILE B CB    1 
ATOM   5410  C  CG1   . ILE B  2  254 ? 77.150 -10.703 5.529   1.00 49.31  ?  286 ILE B CG1   1 
ATOM   5411  C  CG2   . ILE B  2  254 ? 74.776 -11.385 5.244   1.00 48.32  ?  286 ILE B CG2   1 
ATOM   5412  C  CD1   . ILE B  2  254 ? 77.712 -12.097 5.755   1.00 48.44  ?  286 ILE B CD1   1 
ATOM   5413  N  N     . ALA B  2  255 ? 72.883 -8.636  6.431   1.00 46.36  ?  287 ALA B N     1 
ATOM   5414  C  CA    . ALA B  2  255 ? 71.663 -8.398  7.190   1.00 45.94  ?  287 ALA B CA    1 
ATOM   5415  C  C     . ALA B  2  255 ? 70.608 -9.492  6.964   1.00 47.16  ?  287 ALA B C     1 
ATOM   5416  O  O     . ALA B  2  255 ? 69.413 -9.291  7.236   1.00 51.26  ?  287 ALA B O     1 
ATOM   5417  C  CB    . ALA B  2  255 ? 71.105 -7.038  6.808   1.00 47.02  ?  287 ALA B CB    1 
ATOM   5418  N  N     . GLY B  2  256 ? 71.065 -10.650 6.489   1.00 46.93  ?  288 GLY B N     1 
ATOM   5419  C  CA    . GLY B  2  256 ? 70.199 -11.755 6.054   1.00 44.17  ?  288 GLY B CA    1 
ATOM   5420  C  C     . GLY B  2  256 ? 70.941 -12.552 5.002   1.00 41.65  ?  288 GLY B C     1 
ATOM   5421  O  O     . GLY B  2  256 ? 71.660 -11.984 4.194   1.00 39.94  ?  288 GLY B O     1 
ATOM   5422  N  N     . GLN B  2  257 ? 70.817 -13.870 5.028   1.00 41.83  ?  289 GLN B N     1 
ATOM   5423  C  CA    . GLN B  2  257 ? 71.374 -14.707 3.967   1.00 41.36  ?  289 GLN B CA    1 
ATOM   5424  C  C     . GLN B  2  257 ? 70.264 -15.613 3.502   1.00 44.37  ?  289 GLN B C     1 
ATOM   5425  O  O     . GLN B  2  257 ? 69.389 -15.968 4.306   1.00 46.52  ?  289 GLN B O     1 
ATOM   5426  C  CB    . GLN B  2  257 ? 72.534 -15.542 4.465   1.00 40.53  ?  289 GLN B CB    1 
ATOM   5427  C  CG    . GLN B  2  257 ? 73.708 -14.735 4.986   1.00 42.87  ?  289 GLN B CG    1 
ATOM   5428  C  CD    . GLN B  2  257 ? 74.835 -15.611 5.552   1.00 44.83  ?  289 GLN B CD    1 
ATOM   5429  O  OE1   . GLN B  2  257 ? 74.997 -16.778 5.166   1.00 44.82  ?  289 GLN B OE1   1 
ATOM   5430  N  NE2   . GLN B  2  257 ? 75.619 -15.048 6.476   1.00 45.59  ?  289 GLN B NE2   1 
ATOM   5431  N  N     . PHE B  2  258 ? 70.290 -15.993 2.218   1.00 44.97  ?  290 PHE B N     1 
ATOM   5432  C  CA    . PHE B  2  258 ? 69.140 -16.680 1.588   1.00 45.28  ?  290 PHE B CA    1 
ATOM   5433  C  C     . PHE B  2  258 ? 69.478 -17.842 0.599   1.00 45.39  ?  290 PHE B C     1 
ATOM   5434  O  O     . PHE B  2  258 ? 70.137 -17.646 -0.435  1.00 48.71  ?  290 PHE B O     1 
ATOM   5435  C  CB    . PHE B  2  258 ? 68.222 -15.638 0.933   1.00 42.24  ?  290 PHE B CB    1 
ATOM   5436  C  CG    . PHE B  2  258 ? 67.898 -14.454 1.822   1.00 39.50  ?  290 PHE B CG    1 
ATOM   5437  C  CD1   . PHE B  2  258 ? 66.679 -14.357 2.456   1.00 39.96  ?  290 PHE B CD1   1 
ATOM   5438  C  CD2   . PHE B  2  258 ? 68.807 -13.428 2.002   1.00 37.37  ?  290 PHE B CD2   1 
ATOM   5439  C  CE1   . PHE B  2  258 ? 66.361 -13.252 3.244   1.00 40.02  ?  290 PHE B CE1   1 
ATOM   5440  C  CE2   . PHE B  2  258 ? 68.507 -12.346 2.805   1.00 38.04  ?  290 PHE B CE2   1 
ATOM   5441  C  CZ    . PHE B  2  258 ? 67.281 -12.254 3.430   1.00 38.34  ?  290 PHE B CZ    1 
ATOM   5442  N  N     . TYR B  2  259 ? 68.962 -19.033 0.930   1.00 42.28  ?  291 TYR B N     1 
ATOM   5443  C  CA    . TYR B  2  259 ? 69.274 -20.293 0.255   1.00 38.99  ?  291 TYR B CA    1 
ATOM   5444  C  C     . TYR B  2  259 ? 68.030 -21.190 -0.089  1.00 40.46  ?  291 TYR B C     1 
ATOM   5445  O  O     . TYR B  2  259 ? 66.904 -20.946 0.371   1.00 39.65  ?  291 TYR B O     1 
ATOM   5446  C  CB    . TYR B  2  259 ? 70.207 -21.092 1.147   1.00 36.38  ?  291 TYR B CB    1 
ATOM   5447  C  CG    . TYR B  2  259 ? 71.346 -20.312 1.770   1.00 35.27  ?  291 TYR B CG    1 
ATOM   5448  C  CD1   . TYR B  2  259 ? 72.489 -20.056 1.049   1.00 36.94  ?  291 TYR B CD1   1 
ATOM   5449  C  CD2   . TYR B  2  259 ? 71.303 -19.878 3.094   1.00 33.48  ?  291 TYR B CD2   1 
ATOM   5450  C  CE1   . TYR B  2  259 ? 73.570 -19.374 1.609   1.00 36.72  ?  291 TYR B CE1   1 
ATOM   5451  C  CE2   . TYR B  2  259 ? 72.384 -19.212 3.675   1.00 33.17  ?  291 TYR B CE2   1 
ATOM   5452  C  CZ    . TYR B  2  259 ? 73.521 -18.958 2.921   1.00 34.48  ?  291 TYR B CZ    1 
ATOM   5453  O  OH    . TYR B  2  259 ? 74.616 -18.288 3.413   1.00 30.93  ?  291 TYR B OH    1 
ATOM   5454  N  N     . GLY B  2  260 ? 68.269 -22.207 -0.926  1.00 39.27  ?  292 GLY B N     1 
ATOM   5455  C  CA    . GLY B  2  260 ? 67.295 -23.237 -1.320  1.00 35.52  ?  292 GLY B CA    1 
ATOM   5456  C  C     . GLY B  2  260 ? 68.091 -24.544 -1.271  1.00 37.41  ?  292 GLY B C     1 
ATOM   5457  O  O     . GLY B  2  260 ? 68.771 -24.791 -0.271  1.00 38.04  ?  292 GLY B O     1 
ATOM   5458  N  N     . HIS B  2  261 ? 68.037 -25.360 -2.341  1.00 37.49  ?  293 HIS B N     1 
ATOM   5459  C  CA    . HIS B  2  261 ? 68.770 -26.670 -2.512  1.00 35.16  ?  293 HIS B CA    1 
ATOM   5460  C  C     . HIS B  2  261 ? 68.152 -27.753 -1.681  1.00 33.13  ?  293 HIS B C     1 
ATOM   5461  O  O     . HIS B  2  261 ? 67.863 -28.798 -2.205  1.00 33.91  ?  293 HIS B O     1 
ATOM   5462  C  CB    . HIS B  2  261 ? 70.317 -26.601 -2.310  1.00 36.91  ?  293 HIS B CB    1 
ATOM   5463  C  CG    . HIS B  2  261 ? 71.028 -27.946 -2.313  1.00 41.25  ?  293 HIS B CG    1 
ATOM   5464  N  ND1   . HIS B  2  261 ? 70.974 -28.838 -3.366  1.00 42.09  ?  293 HIS B ND1   1 
ATOM   5465  C  CD2   . HIS B  2  261 ? 71.860 -28.522 -1.396  1.00 44.44  ?  293 HIS B CD2   1 
ATOM   5466  C  CE1   . HIS B  2  261 ? 71.698 -29.915 -3.082  1.00 42.58  ?  293 HIS B CE1   1 
ATOM   5467  N  NE2   . HIS B  2  261 ? 72.250 -29.747 -1.893  1.00 42.88  ?  293 HIS B NE2   1 
ATOM   5468  N  N     . THR B  2  262 ? 67.935 -27.516 -0.396  1.00 33.38  ?  294 THR B N     1 
ATOM   5469  C  CA    . THR B  2  262 ? 67.309 -28.525 0.475   1.00 34.09  ?  294 THR B CA    1 
ATOM   5470  C  C     . THR B  2  262 ? 65.867 -28.875 0.167   1.00 34.00  ?  294 THR B C     1 
ATOM   5471  O  O     . THR B  2  262 ? 65.426 -29.949 0.602   1.00 33.83  ?  294 THR B O     1 
ATOM   5472  C  CB    . THR B  2  262 ? 67.287 -28.089 1.951   1.00 36.20  ?  294 THR B CB    1 
ATOM   5473  O  OG1   . THR B  2  262 ? 66.354 -27.002 2.136   1.00 35.02  ?  294 THR B OG1   1 
ATOM   5474  C  CG2   . THR B  2  262 ? 68.715 -27.708 2.418   1.00 39.21  ?  294 THR B CG2   1 
ATOM   5475  N  N     . HIS B  2  263 ? 65.151 -27.966 -0.536  1.00 32.55  ?  295 HIS B N     1 
ATOM   5476  C  CA    . HIS B  2  263 ? 63.706 -28.085 -0.872  1.00 31.63  ?  295 HIS B CA    1 
ATOM   5477  C  C     . HIS B  2  263 ? 62.791 -27.953 0.350   1.00 33.06  ?  295 HIS B C     1 
ATOM   5478  O  O     . HIS B  2  263 ? 61.592 -28.312 0.286   1.00 32.96  ?  295 HIS B O     1 
ATOM   5479  C  CB    . HIS B  2  263 ? 63.383 -29.397 -1.590  1.00 29.59  ?  295 HIS B CB    1 
ATOM   5480  C  CG    . HIS B  2  263 ? 63.739 -29.375 -3.022  1.00 29.81  ?  295 HIS B CG    1 
ATOM   5481  N  ND1   . HIS B  2  263 ? 62.964 -29.977 -3.988  1.00 31.36  ?  295 HIS B ND1   1 
ATOM   5482  C  CD2   . HIS B  2  263 ? 64.757 -28.770 -3.677  1.00 30.35  ?  295 HIS B CD2   1 
ATOM   5483  C  CE1   . HIS B  2  263 ? 63.509 -29.778 -5.175  1.00 30.08  ?  295 HIS B CE1   1 
ATOM   5484  N  NE2   . HIS B  2  263 ? 64.594 -29.040 -5.016  1.00 29.77  ?  295 HIS B NE2   1 
ATOM   5485  N  N     . ARG B  2  264 ? 63.350 -27.394 1.432   1.00 31.54  ?  296 ARG B N     1 
ATOM   5486  C  CA    . ARG B  2  264 ? 62.754 -27.481 2.764   1.00 29.47  ?  296 ARG B CA    1 
ATOM   5487  C  C     . ARG B  2  264 ? 62.782 -26.122 3.472   1.00 27.79  ?  296 ARG B C     1 
ATOM   5488  O  O     . ARG B  2  264 ? 63.632 -25.281 3.175   1.00 25.03  ?  296 ARG B O     1 
ATOM   5489  C  CB    . ARG B  2  264 ? 63.524 -28.547 3.580   1.00 28.45  ?  296 ARG B CB    1 
ATOM   5490  C  CG    . ARG B  2  264 ? 63.516 -29.969 2.991   1.00 26.46  ?  296 ARG B CG    1 
ATOM   5491  C  CD    . ARG B  2  264 ? 62.279 -30.718 3.452   1.00 26.66  ?  296 ARG B CD    1 
ATOM   5492  N  NE    . ARG B  2  264 ? 62.155 -32.044 2.860   1.00 25.54  ?  296 ARG B NE    1 
ATOM   5493  C  CZ    . ARG B  2  264 ? 61.612 -32.306 1.681   1.00 23.03  ?  296 ARG B CZ    1 
ATOM   5494  N  NH1   . ARG B  2  264 ? 61.138 -31.328 0.944   1.00 23.35  1  296 ARG B NH1   1 
ATOM   5495  N  NH2   . ARG B  2  264 ? 61.558 -33.554 1.240   1.00 21.91  ?  296 ARG B NH2   1 
ATOM   5496  N  N     . ASP B  2  265 ? 61.851 -25.920 4.399   1.00 28.86  ?  297 ASP B N     1 
ATOM   5497  C  CA    . ASP B  2  265 ? 61.823 -24.689 5.225   1.00 32.19  ?  297 ASP B CA    1 
ATOM   5498  C  C     . ASP B  2  265 ? 62.660 -24.754 6.548   1.00 31.52  ?  297 ASP B C     1 
ATOM   5499  O  O     . ASP B  2  265 ? 62.293 -25.399 7.547   1.00 30.46  ?  297 ASP B O     1 
ATOM   5500  C  CB    . ASP B  2  265 ? 60.373 -24.277 5.524   1.00 33.51  ?  297 ASP B CB    1 
ATOM   5501  C  CG    . ASP B  2  265 ? 60.277 -22.925 6.241   1.00 35.05  ?  297 ASP B CG    1 
ATOM   5502  O  OD1   . ASP B  2  265 ? 61.248 -22.529 6.945   1.00 33.90  ?  297 ASP B OD1   1 
ATOM   5503  O  OD2   . ASP B  2  265 ? 59.221 -22.260 6.093   1.00 36.73  -1 297 ASP B OD2   1 
ATOM   5504  N  N     . SER B  2  266 ? 63.768 -24.034 6.557   1.00 30.66  ?  298 SER B N     1 
ATOM   5505  C  CA    . SER B  2  266 ? 64.736 -24.193 7.620   1.00 32.97  ?  298 SER B CA    1 
ATOM   5506  C  C     . SER B  2  266 ? 65.357 -22.867 8.063   1.00 34.01  ?  298 SER B C     1 
ATOM   5507  O  O     . SER B  2  266 ? 65.820 -22.132 7.197   1.00 37.95  ?  298 SER B O     1 
ATOM   5508  C  CB    . SER B  2  266 ? 65.839 -25.118 7.117   1.00 32.98  ?  298 SER B CB    1 
ATOM   5509  O  OG    . SER B  2  266 ? 65.601 -26.457 7.519   1.00 35.55  ?  298 SER B OG    1 
ATOM   5510  N  N     . ILE B  2  267 ? 65.394 -22.551 9.368   1.00 31.68  ?  299 ILE B N     1 
ATOM   5511  C  CA    . ILE B  2  267 ? 66.191 -21.415 9.778   1.00 32.74  ?  299 ILE B CA    1 
ATOM   5512  C  C     . ILE B  2  267 ? 67.518 -21.932 10.306  1.00 33.57  ?  299 ILE B C     1 
ATOM   5513  O  O     . ILE B  2  267 ? 67.631 -23.103 10.708  1.00 36.25  ?  299 ILE B O     1 
ATOM   5514  C  CB    . ILE B  2  267 ? 65.495 -20.472 10.771  1.00 35.48  ?  299 ILE B CB    1 
ATOM   5515  C  CG1   . ILE B  2  267 ? 65.427 -21.105 12.145  1.00 41.00  ?  299 ILE B CG1   1 
ATOM   5516  C  CG2   . ILE B  2  267 ? 64.095 -20.099 10.290  1.00 33.81  ?  299 ILE B CG2   1 
ATOM   5517  C  CD1   . ILE B  2  267 ? 64.771 -20.196 13.162  1.00 44.33  ?  299 ILE B CD1   1 
ATOM   5518  N  N     . MET B  2  268 ? 68.533 -21.068 10.218  1.00 32.76  ?  300 MET B N     1 
ATOM   5519  C  CA    . MET B  2  268 ? 69.865 -21.282 10.812  1.00 30.26  ?  300 MET B CA    1 
ATOM   5520  C  C     . MET B  2  268 ? 70.364 -19.926 11.329  1.00 30.04  ?  300 MET B C     1 
ATOM   5521  O  O     . MET B  2  268 ? 69.848 -18.858 10.952  1.00 27.46  ?  300 MET B O     1 
ATOM   5522  C  CB    . MET B  2  268 ? 70.876 -21.819 9.802   1.00 29.48  ?  300 MET B CB    1 
ATOM   5523  C  CG    . MET B  2  268 ? 70.936 -23.320 9.598   1.00 28.63  ?  300 MET B CG    1 
ATOM   5524  S  SD    . MET B  2  268 ? 72.306 -23.665 8.434   1.00 28.49  ?  300 MET B SD    1 
ATOM   5525  C  CE    . MET B  2  268 ? 71.682 -23.133 6.834   1.00 29.49  ?  300 MET B CE    1 
ATOM   5526  N  N     . VAL B  2  269 ? 71.386 -20.006 12.179  1.00 31.10  ?  301 VAL B N     1 
ATOM   5527  C  CA    . VAL B  2  269 ? 71.860 -18.893 12.983  1.00 31.76  ?  301 VAL B CA    1 
ATOM   5528  C  C     . VAL B  2  269 ? 73.352 -19.025 13.116  1.00 33.76  ?  301 VAL B C     1 
ATOM   5529  O  O     . VAL B  2  269 ? 73.859 -19.980 13.724  1.00 36.16  ?  301 VAL B O     1 
ATOM   5530  C  CB    . VAL B  2  269 ? 71.287 -18.920 14.418  1.00 31.92  ?  301 VAL B CB    1 
ATOM   5531  C  CG1   . VAL B  2  269 ? 71.749 -17.683 15.192  1.00 31.72  ?  301 VAL B CG1   1 
ATOM   5532  C  CG2   . VAL B  2  269 ? 69.760 -19.028 14.395  1.00 31.90  ?  301 VAL B CG2   1 
ATOM   5533  N  N     . LEU B  2  270 ? 74.060 -18.060 12.553  1.00 34.74  ?  302 LEU B N     1 
ATOM   5534  C  CA    . LEU B  2  270 ? 75.508 -18.025 12.648  1.00 34.79  ?  302 LEU B CA    1 
ATOM   5535  C  C     . LEU B  2  270 ? 75.822 -17.447 14.000  1.00 36.21  ?  302 LEU B C     1 
ATOM   5536  O  O     . LEU B  2  270 ? 75.263 -16.413 14.365  1.00 36.17  ?  302 LEU B O     1 
ATOM   5537  C  CB    . LEU B  2  270 ? 76.058 -17.134 11.529  1.00 33.69  ?  302 LEU B CB    1 
ATOM   5538  C  CG    . LEU B  2  270 ? 77.555 -16.876 11.413  1.00 32.93  ?  302 LEU B CG    1 
ATOM   5539  C  CD1   . LEU B  2  270 ? 78.352 -18.172 11.420  1.00 32.18  ?  302 LEU B CD1   1 
ATOM   5540  C  CD2   . LEU B  2  270 ? 77.779 -16.073 10.139  1.00 33.27  ?  302 LEU B CD2   1 
ATOM   5541  N  N     . SER B  2  271 ? 76.667 -18.118 14.771  1.00 40.10  ?  303 SER B N     1 
ATOM   5542  C  CA    . SER B  2  271 ? 77.236 -17.473 15.964  1.00 44.25  ?  303 SER B CA    1 
ATOM   5543  C  C     . SER B  2  271 ? 78.676 -16.990 15.676  1.00 46.79  ?  303 SER B C     1 
ATOM   5544  O  O     . SER B  2  271 ? 79.318 -17.453 14.740  1.00 48.82  ?  303 SER B O     1 
ATOM   5545  C  CB    . SER B  2  271 ? 77.145 -18.402 17.187  1.00 44.80  ?  303 SER B CB    1 
ATOM   5546  O  OG    . SER B  2  271 ? 75.795 -18.530 17.645  1.00 43.19  ?  303 SER B OG    1 
ATOM   5547  N  N     . ASP B  2  272 ? 79.163 -16.018 16.439  1.00 52.45  ?  304 ASP B N     1 
ATOM   5548  C  CA    . ASP B  2  272 ? 80.543 -15.551 16.270  1.00 55.73  ?  304 ASP B CA    1 
ATOM   5549  C  C     . ASP B  2  272 ? 81.481 -16.558 16.944  1.00 59.77  ?  304 ASP B C     1 
ATOM   5550  O  O     . ASP B  2  272 ? 81.021 -17.497 17.615  1.00 58.11  ?  304 ASP B O     1 
ATOM   5551  C  CB    . ASP B  2  272 ? 80.746 -14.116 16.808  1.00 57.27  ?  304 ASP B CB    1 
ATOM   5552  C  CG    . ASP B  2  272 ? 80.518 -13.991 18.331  1.00 59.79  ?  304 ASP B CG    1 
ATOM   5553  O  OD1   . ASP B  2  272 ? 80.437 -15.016 19.034  1.00 59.95  ?  304 ASP B OD1   1 
ATOM   5554  O  OD2   . ASP B  2  272 ? 80.413 -12.851 18.837  1.00 64.95  -1 304 ASP B OD2   1 
ATOM   5555  N  N     . LYS B  2  273 ? 82.786 -16.359 16.755  1.00 63.75  ?  305 LYS B N     1 
ATOM   5556  C  CA    . LYS B  2  273 ? 83.823 -17.235 17.324  1.00 64.17  ?  305 LYS B CA    1 
ATOM   5557  C  C     . LYS B  2  273 ? 83.675 -17.457 18.841  1.00 64.40  ?  305 LYS B C     1 
ATOM   5558  O  O     . LYS B  2  273 ? 83.954 -18.545 19.348  1.00 63.03  ?  305 LYS B O     1 
ATOM   5559  C  CB    . LYS B  2  273 ? 85.203 -16.660 16.997  1.00 66.23  ?  305 LYS B CB    1 
ATOM   5560  C  CG    . LYS B  2  273 ? 85.584 -16.765 15.523  1.00 68.82  ?  305 LYS B CG    1 
ATOM   5561  C  CD    . LYS B  2  273 ? 86.423 -18.015 15.285  1.00 71.44  ?  305 LYS B CD    1 
ATOM   5562  C  CE    . LYS B  2  273 ? 86.544 -18.386 13.814  1.00 75.17  ?  305 LYS B CE    1 
ATOM   5563  N  NZ    . LYS B  2  273 ? 87.342 -17.428 12.997  1.00 77.14  1  305 LYS B NZ    1 
ATOM   5564  N  N     . LYS B  2  274 ? 83.231 -16.416 19.547  1.00 68.40  ?  306 LYS B N     1 
ATOM   5565  C  CA    . LYS B  2  274 ? 82.934 -16.483 20.985  1.00 70.90  ?  306 LYS B CA    1 
ATOM   5566  C  C     . LYS B  2  274 ? 81.803 -17.485 21.269  1.00 67.79  ?  306 LYS B C     1 
ATOM   5567  O  O     . LYS B  2  274 ? 81.947 -18.330 22.136  1.00 73.64  ?  306 LYS B O     1 
ATOM   5568  C  CB    . LYS B  2  274 ? 82.541 -15.091 21.537  1.00 75.88  ?  306 LYS B CB    1 
ATOM   5569  C  CG    . LYS B  2  274 ? 83.378 -14.580 22.712  1.00 77.22  ?  306 LYS B CG    1 
ATOM   5570  C  CD    . LYS B  2  274 ? 84.493 -13.644 22.255  1.00 80.51  ?  306 LYS B CD    1 
ATOM   5571  C  CE    . LYS B  2  274 ? 85.735 -14.389 21.782  1.00 81.48  ?  306 LYS B CE    1 
ATOM   5572  N  NZ    . LYS B  2  274 ? 86.616 -14.767 22.922  1.00 81.34  1  306 LYS B NZ    1 
ATOM   5573  N  N     . GLY B  2  275 ? 80.698 -17.389 20.526  1.00 65.15  ?  307 GLY B N     1 
ATOM   5574  C  CA    . GLY B  2  275 ? 79.490 -18.206 20.761  1.00 60.09  ?  307 GLY B CA    1 
ATOM   5575  C  C     . GLY B  2  275 ? 78.163 -17.443 20.783  1.00 57.71  ?  307 GLY B C     1 
ATOM   5576  O  O     . GLY B  2  275 ? 77.119 -18.037 21.038  1.00 55.51  ?  307 GLY B O     1 
ATOM   5577  N  N     . SER B  2  276 ? 78.193 -16.137 20.504  1.00 56.16  ?  308 SER B N     1 
ATOM   5578  C  CA    . SER B  2  276 ? 76.990 -15.287 20.504  1.00 53.17  ?  308 SER B CA    1 
ATOM   5579  C  C     . SER B  2  276 ? 76.429 -15.020 19.090  1.00 49.80  ?  308 SER B C     1 
ATOM   5580  O  O     . SER B  2  276 ? 77.168 -14.642 18.197  1.00 47.30  ?  308 SER B O     1 
ATOM   5581  C  CB    . SER B  2  276 ? 77.295 -13.951 21.195  1.00 53.27  ?  308 SER B CB    1 
ATOM   5582  O  OG    . SER B  2  276 ? 77.342 -14.113 22.606  1.00 54.49  ?  308 SER B OG    1 
ATOM   5583  N  N     . PRO B  2  277 ? 75.107 -15.177 18.900  1.00 48.76  ?  309 PRO B N     1 
ATOM   5584  C  CA    . PRO B  2  277 ? 74.460 -15.104 17.587  1.00 46.43  ?  309 PRO B CA    1 
ATOM   5585  C  C     . PRO B  2  277 ? 74.676 -13.797 16.852  1.00 44.04  ?  309 PRO B C     1 
ATOM   5586  O  O     . PRO B  2  277 ? 74.397 -12.754 17.415  1.00 42.08  ?  309 PRO B O     1 
ATOM   5587  C  CB    . PRO B  2  277 ? 72.976 -15.221 17.934  1.00 49.17  ?  309 PRO B CB    1 
ATOM   5588  C  CG    . PRO B  2  277 ? 72.864 -14.755 19.349  1.00 49.89  ?  309 PRO B CG    1 
ATOM   5589  C  CD    . PRO B  2  277 ? 74.110 -15.285 19.982  1.00 50.83  ?  309 PRO B CD    1 
ATOM   5590  N  N     . VAL B  2  278 ? 75.128 -13.858 15.595  1.00 44.41  ?  310 VAL B N     1 
ATOM   5591  C  CA    . VAL B  2  278 ? 75.425 -12.644 14.798  1.00 42.77  ?  310 VAL B CA    1 
ATOM   5592  C  C     . VAL B  2  278 ? 74.756 -12.521 13.414  1.00 41.09  ?  310 VAL B C     1 
ATOM   5593  O  O     . VAL B  2  278 ? 74.534 -11.404 12.965  1.00 42.03  ?  310 VAL B O     1 
ATOM   5594  C  CB    . VAL B  2  278 ? 76.956 -12.416 14.617  1.00 43.24  ?  310 VAL B CB    1 
ATOM   5595  C  CG1   . VAL B  2  278 ? 77.635 -12.221 15.963  1.00 42.10  ?  310 VAL B CG1   1 
ATOM   5596  C  CG2   . VAL B  2  278 ? 77.624 -13.549 13.835  1.00 43.24  ?  310 VAL B CG2   1 
ATOM   5597  N  N     . ASN B  2  279 ? 74.448 -13.634 12.738  1.00 40.21  ?  311 ASN B N     1 
ATOM   5598  C  CA    . ASN B  2  279 ? 73.828 -13.599 11.387  1.00 39.37  ?  311 ASN B CA    1 
ATOM   5599  C  C     . ASN B  2  279 ? 72.620 -14.535 11.269  1.00 39.65  ?  311 ASN B C     1 
ATOM   5600  O  O     . ASN B  2  279 ? 72.670 -15.667 11.756  1.00 40.76  ?  311 ASN B O     1 
ATOM   5601  C  CB    . ASN B  2  279 ? 74.854 -13.984 10.303  1.00 39.09  ?  311 ASN B CB    1 
ATOM   5602  C  CG    . ASN B  2  279 ? 74.745 -13.122 9.060   1.00 37.44  ?  311 ASN B CG    1 
ATOM   5603  O  OD1   . ASN B  2  279 ? 74.173 -13.528 8.057   1.00 37.86  ?  311 ASN B OD1   1 
ATOM   5604  N  ND2   . ASN B  2  279 ? 75.267 -11.919 9.139   1.00 34.83  ?  311 ASN B ND2   1 
ATOM   5605  N  N     . SER B  2  280 ? 71.554 -14.055 10.618  1.00 39.75  ?  312 SER B N     1 
ATOM   5606  C  CA    . SER B  2  280 ? 70.331 -14.834 10.376  1.00 38.38  ?  312 SER B CA    1 
ATOM   5607  C  C     . SER B  2  280 ? 70.302 -15.424 8.982   1.00 38.39  ?  312 SER B C     1 
ATOM   5608  O  O     . SER B  2  280 ? 70.312 -14.673 8.005   1.00 37.53  ?  312 SER B O     1 
ATOM   5609  C  CB    . SER B  2  280 ? 69.090 -13.961 10.540  1.00 37.49  ?  312 SER B CB    1 
ATOM   5610  O  OG    . SER B  2  280 ? 68.556 -14.126 11.832  1.00 38.93  ?  312 SER B OG    1 
ATOM   5611  N  N     . LEU B  2  281 ? 70.220 -16.759 8.914   1.00 38.61  ?  313 LEU B N     1 
ATOM   5612  C  CA    . LEU B  2  281 ? 70.092 -17.502 7.652   1.00 39.89  ?  313 LEU B CA    1 
ATOM   5613  C  C     . LEU B  2  281 ? 68.683 -18.101 7.425   1.00 36.46  ?  313 LEU B C     1 
ATOM   5614  O  O     . LEU B  2  281 ? 67.962 -18.431 8.369   1.00 32.48  ?  313 LEU B O     1 
ATOM   5615  C  CB    . LEU B  2  281 ? 71.162 -18.589 7.587   1.00 44.09  ?  313 LEU B CB    1 
ATOM   5616  C  CG    . LEU B  2  281 ? 72.605 -18.050 7.553   1.00 49.79  ?  313 LEU B CG    1 
ATOM   5617  C  CD1   . LEU B  2  281 ? 73.037 -17.411 8.871   1.00 52.41  ?  313 LEU B CD1   1 
ATOM   5618  C  CD2   . LEU B  2  281 ? 73.615 -19.127 7.151   1.00 52.14  ?  313 LEU B CD2   1 
ATOM   5619  N  N     . PHE B  2  282 ? 68.301 -18.215 6.153   1.00 35.98  ?  314 PHE B N     1 
ATOM   5620  C  CA    . PHE B  2  282 ? 66.911 -18.533 5.776   1.00 36.12  ?  314 PHE B CA    1 
ATOM   5621  C  C     . PHE B  2  282 ? 66.756 -19.345 4.484   1.00 34.24  ?  314 PHE B C     1 
ATOM   5622  O  O     . PHE B  2  282 ? 66.531 -18.769 3.393   1.00 37.67  ?  314 PHE B O     1 
ATOM   5623  C  CB    . PHE B  2  282 ? 66.113 -17.246 5.604   1.00 35.55  ?  314 PHE B CB    1 
ATOM   5624  C  CG    . PHE B  2  282 ? 66.048 -16.410 6.829   1.00 34.52  ?  314 PHE B CG    1 
ATOM   5625  C  CD1   . PHE B  2  282 ? 65.061 -16.621 7.765   1.00 35.37  ?  314 PHE B CD1   1 
ATOM   5626  C  CD2   . PHE B  2  282 ? 66.966 -15.399 7.032   1.00 34.25  ?  314 PHE B CD2   1 
ATOM   5627  C  CE1   . PHE B  2  282 ? 64.981 -15.826 8.890   1.00 36.35  ?  314 PHE B CE1   1 
ATOM   5628  C  CE2   . PHE B  2  282 ? 66.901 -14.593 8.144   1.00 34.71  ?  314 PHE B CE2   1 
ATOM   5629  C  CZ    . PHE B  2  282 ? 65.906 -14.806 9.080   1.00 36.10  ?  314 PHE B CZ    1 
ATOM   5630  N  N     . VAL B  2  283 ? 66.803 -20.669 4.633   1.00 29.45  ?  315 VAL B N     1 
ATOM   5631  C  CA    . VAL B  2  283 ? 66.697 -21.594 3.520   1.00 27.87  ?  315 VAL B CA    1 
ATOM   5632  C  C     . VAL B  2  283 ? 65.227 -21.755 3.124   1.00 28.05  ?  315 VAL B C     1 
ATOM   5633  O  O     . VAL B  2  283 ? 64.422 -22.209 3.923   1.00 28.25  ?  315 VAL B O     1 
ATOM   5634  C  CB    . VAL B  2  283 ? 67.243 -22.985 3.900   1.00 27.31  ?  315 VAL B CB    1 
ATOM   5635  C  CG1   . VAL B  2  283 ? 67.079 -23.951 2.730   1.00 27.05  ?  315 VAL B CG1   1 
ATOM   5636  C  CG2   . VAL B  2  283 ? 68.694 -22.915 4.396   1.00 26.54  ?  315 VAL B CG2   1 
ATOM   5637  N  N     . ALA B  2  284 ? 64.879 -21.401 1.892   1.00 28.40  ?  316 ALA B N     1 
ATOM   5638  C  CA    . ALA B  2  284 ? 63.503 -21.525 1.407   1.00 29.39  ?  316 ALA B CA    1 
ATOM   5639  C  C     . ALA B  2  284 ? 63.180 -22.890 0.807   1.00 30.96  ?  316 ALA B C     1 
ATOM   5640  O  O     . ALA B  2  284 ? 64.039 -23.517 0.187   1.00 31.81  ?  316 ALA B O     1 
ATOM   5641  C  CB    . ALA B  2  284 ? 63.256 -20.472 0.346   1.00 30.82  ?  316 ALA B CB    1 
ATOM   5642  N  N     . PRO B  2  285 ? 61.916 -23.331 0.921   1.00 33.19  ?  317 PRO B N     1 
ATOM   5643  C  CA    . PRO B  2  285 ? 61.561 -24.553 0.190   1.00 33.80  ?  317 PRO B CA    1 
ATOM   5644  C  C     . PRO B  2  285 ? 61.325 -24.361 -1.331  1.00 33.22  ?  317 PRO B C     1 
ATOM   5645  O  O     . PRO B  2  285 ? 61.226 -23.256 -1.842  1.00 34.36  ?  317 PRO B O     1 
ATOM   5646  C  CB    . PRO B  2  285 ? 60.293 -25.049 0.915   1.00 33.45  ?  317 PRO B CB    1 
ATOM   5647  C  CG    . PRO B  2  285 ? 59.691 -23.823 1.515   1.00 34.11  ?  317 PRO B CG    1 
ATOM   5648  C  CD    . PRO B  2  285 ? 60.767 -22.773 1.660   1.00 33.82  ?  317 PRO B CD    1 
ATOM   5649  N  N     . ALA B  2  286 ? 61.225 -25.469 -2.034  1.00 33.41  ?  318 ALA B N     1 
ATOM   5650  C  CA    . ALA B  2  286 ? 61.013 -25.455 -3.457  1.00 32.90  ?  318 ALA B CA    1 
ATOM   5651  C  C     . ALA B  2  286 ? 59.583 -25.124 -3.842  1.00 32.64  ?  318 ALA B C     1 
ATOM   5652  O  O     . ALA B  2  286 ? 58.667 -25.064 -3.002  1.00 30.67  ?  318 ALA B O     1 
ATOM   5653  C  CB    . ALA B  2  286 ? 61.353 -26.824 -4.012  1.00 33.88  ?  318 ALA B CB    1 
ATOM   5654  N  N     . VAL B  2  287 ? 59.417 -24.944 -5.153  1.00 32.74  ?  319 VAL B N     1 
ATOM   5655  C  CA    . VAL B  2  287 ? 58.100 -24.931 -5.819  1.00 31.07  ?  319 VAL B CA    1 
ATOM   5656  C  C     . VAL B  2  287 ? 57.668 -26.354 -6.212  1.00 28.26  ?  319 VAL B C     1 
ATOM   5657  O  O     . VAL B  2  287 ? 56.489 -26.704 -6.123  1.00 25.69  ?  319 VAL B O     1 
ATOM   5658  C  CB    . VAL B  2  287 ? 58.112 -24.047 -7.083  1.00 31.10  ?  319 VAL B CB    1 
ATOM   5659  C  CG1   . VAL B  2  287 ? 56.748 -24.110 -7.752  1.00 31.14  ?  319 VAL B CG1   1 
ATOM   5660  C  CG2   . VAL B  2  287 ? 58.499 -22.606 -6.741  1.00 31.27  ?  319 VAL B CG2   1 
ATOM   5661  N  N     . THR B  2  288 ? 58.637 -27.159 -6.642  1.00 26.62  ?  320 THR B N     1 
ATOM   5662  C  CA    . THR B  2  288 ? 58.395 -28.572 -6.917  1.00 26.08  ?  320 THR B CA    1 
ATOM   5663  C  C     . THR B  2  288 ? 58.098 -29.389 -5.645  1.00 25.22  ?  320 THR B C     1 
ATOM   5664  O  O     . THR B  2  288 ? 58.658 -29.186 -4.564  1.00 22.19  ?  320 THR B O     1 
ATOM   5665  C  CB    . THR B  2  288 ? 59.543 -29.245 -7.756  1.00 26.52  ?  320 THR B CB    1 
ATOM   5666  O  OG1   . THR B  2  288 ? 59.158 -30.581 -8.143  1.00 25.88  ?  320 THR B OG1   1 
ATOM   5667  C  CG2   . THR B  2  288 ? 60.851 -29.312 -6.987  1.00 26.17  ?  320 THR B CG2   1 
ATOM   5668  N  N     . PRO B  2  289 ? 57.212 -30.347 -5.798  1.00 26.75  ?  321 PRO B N     1 
ATOM   5669  C  CA    . PRO B  2  289 ? 56.939 -31.285 -4.754  1.00 28.98  ?  321 PRO B CA    1 
ATOM   5670  C  C     . PRO B  2  289 ? 57.752 -32.575 -4.863  1.00 30.20  ?  321 PRO B C     1 
ATOM   5671  O  O     . PRO B  2  289 ? 57.549 -33.503 -4.072  1.00 30.82  ?  321 PRO B O     1 
ATOM   5672  C  CB    . PRO B  2  289 ? 55.442 -31.604 -4.978  1.00 28.43  ?  321 PRO B CB    1 
ATOM   5673  C  CG    . PRO B  2  289 ? 55.131 -31.209 -6.370  1.00 27.57  ?  321 PRO B CG    1 
ATOM   5674  C  CD    . PRO B  2  289 ? 56.370 -30.608 -6.972  1.00 27.47  ?  321 PRO B CD    1 
ATOM   5675  N  N     . VAL B  2  290 ? 58.640 -32.655 -5.841  1.00 31.95  ?  322 VAL B N     1 
ATOM   5676  C  CA    . VAL B  2  290 ? 59.164 -33.955 -6.273  1.00 33.89  ?  322 VAL B CA    1 
ATOM   5677  C  C     . VAL B  2  290 ? 59.887 -34.710 -5.140  1.00 33.65  ?  322 VAL B C     1 
ATOM   5678  O  O     . VAL B  2  290 ? 60.541 -34.079 -4.273  1.00 33.17  ?  322 VAL B O     1 
ATOM   5679  C  CB    . VAL B  2  290 ? 60.082 -33.807 -7.537  1.00 35.16  ?  322 VAL B CB    1 
ATOM   5680  C  CG1   . VAL B  2  290 ? 61.427 -33.109 -7.214  1.00 33.72  ?  322 VAL B CG1   1 
ATOM   5681  C  CG2   . VAL B  2  290 ? 60.281 -35.168 -8.223  1.00 34.94  ?  322 VAL B CG2   1 
ATOM   5682  N  N     . LYS B  2  291 ? 59.780 -36.048 -5.173  1.00 32.02  ?  323 LYS B N     1 
ATOM   5683  C  CA    . LYS B  2  291 ? 60.469 -36.938 -4.205  1.00 30.89  ?  323 LYS B CA    1 
ATOM   5684  C  C     . LYS B  2  291 ? 60.723 -38.395 -4.702  1.00 30.47  ?  323 LYS B C     1 
ATOM   5685  O  O     . LYS B  2  291 ? 60.193 -38.809 -5.738  1.00 31.59  ?  323 LYS B O     1 
ATOM   5686  C  CB    . LYS B  2  291 ? 59.698 -36.977 -2.893  1.00 29.45  ?  323 LYS B CB    1 
ATOM   5687  C  CG    . LYS B  2  291 ? 58.295 -37.543 -3.014  1.00 29.47  ?  323 LYS B CG    1 
ATOM   5688  C  CD    . LYS B  2  291 ? 58.065 -38.595 -1.929  1.00 29.87  ?  323 LYS B CD    1 
ATOM   5689  C  CE    . LYS B  2  291 ? 56.756 -39.367 -2.105  1.00 30.19  ?  323 LYS B CE    1 
ATOM   5690  N  NZ    . LYS B  2  291 ? 56.865 -40.816 -1.746  1.00 30.28  1  323 LYS B NZ    1 
ATOM   5691  N  N     . SER B  2  292 ? 61.539 -39.146 -3.954  1.00 29.90  ?  324 SER B N     1 
ATOM   5692  C  CA    A SER B  2  292 ? 61.814 -40.553 -4.261  0.50 30.16  ?  324 SER B CA    1 
ATOM   5693  C  CA    B SER B  2  292 ? 61.817 -40.566 -4.234  0.50 29.44  ?  324 SER B CA    1 
ATOM   5694  C  C     . SER B  2  292 ? 60.664 -41.433 -3.813  1.00 29.64  ?  324 SER B C     1 
ATOM   5695  O  O     . SER B  2  292 ? 59.990 -41.138 -2.839  1.00 31.08  ?  324 SER B O     1 
ATOM   5696  C  CB    A SER B  2  292 ? 63.086 -41.030 -3.559  0.50 31.27  ?  324 SER B CB    1 
ATOM   5697  C  CB    B SER B  2  292 ? 63.049 -41.061 -3.468  0.50 29.75  ?  324 SER B CB    1 
ATOM   5698  O  OG    A SER B  2  292 ? 64.228 -40.294 -3.976  0.50 32.57  ?  324 SER B OG    1 
ATOM   5699  O  OG    B SER B  2  292 ? 62.762 -42.250 -2.733  0.50 29.10  ?  324 SER B OG    1 
ATOM   5700  N  N     . VAL B  2  293 ? 60.477 -42.535 -4.509  1.00 29.16  ?  325 VAL B N     1 
ATOM   5701  C  CA    . VAL B  2  293 ? 59.405 -43.427 -4.173  1.00 29.29  ?  325 VAL B CA    1 
ATOM   5702  C  C     . VAL B  2  293 ? 59.526 -43.890 -2.715  1.00 31.43  ?  325 VAL B C     1 
ATOM   5703  O  O     . VAL B  2  293 ? 58.519 -43.989 -2.004  1.00 34.00  ?  325 VAL B O     1 
ATOM   5704  C  CB    . VAL B  2  293 ? 59.383 -44.611 -5.132  1.00 29.99  ?  325 VAL B CB    1 
ATOM   5705  C  CG1   . VAL B  2  293 ? 58.309 -45.605 -4.719  1.00 31.20  ?  325 VAL B CG1   1 
ATOM   5706  C  CG2   . VAL B  2  293 ? 59.153 -44.132 -6.563  1.00 29.93  ?  325 VAL B CG2   1 
ATOM   5707  N  N     . LEU B  2  294 ? 60.753 -44.102 -2.241  1.00 32.69  ?  326 LEU B N     1 
ATOM   5708  C  CA    . LEU B  2  294 ? 60.997 -44.675 -0.886  1.00 32.22  ?  326 LEU B CA    1 
ATOM   5709  C  C     . LEU B  2  294 ? 60.785 -43.720 0.293   1.00 29.37  ?  326 LEU B C     1 
ATOM   5710  O  O     . LEU B  2  294 ? 60.749 -44.136 1.438   1.00 25.80  ?  326 LEU B O     1 
ATOM   5711  C  CB    . LEU B  2  294 ? 62.422 -45.242 -0.831  1.00 33.89  ?  326 LEU B CB    1 
ATOM   5712  C  CG    . LEU B  2  294 ? 62.777 -46.232 -1.967  1.00 34.03  ?  326 LEU B CG    1 
ATOM   5713  C  CD1   . LEU B  2  294 ? 64.187 -46.792 -1.855  1.00 33.33  ?  326 LEU B CD1   1 
ATOM   5714  C  CD2   . LEU B  2  294 ? 61.760 -47.368 -1.961  1.00 35.73  ?  326 LEU B CD2   1 
ATOM   5715  N  N     . GLU B  2  295 ? 60.686 -42.443 -0.028  1.00 30.06  ?  327 GLU B N     1 
ATOM   5716  C  CA    . GLU B  2  295 ? 60.545 -41.351 0.907   1.00 30.31  ?  327 GLU B CA    1 
ATOM   5717  C  C     . GLU B  2  295 ? 59.152 -41.082 1.263   1.00 30.55  ?  327 GLU B C     1 
ATOM   5718  O  O     . GLU B  2  295 ? 58.351 -40.928 0.417   1.00 30.42  ?  327 GLU B O     1 
ATOM   5719  C  CB    . GLU B  2  295 ? 61.082 -40.114 0.249   1.00 29.50  ?  327 GLU B CB    1 
ATOM   5720  C  CG    . GLU B  2  295 ? 62.573 -40.140 0.106   1.00 29.95  ?  327 GLU B CG    1 
ATOM   5721  C  CD    . GLU B  2  295 ? 63.114 -38.937 -0.586  1.00 31.02  ?  327 GLU B CD    1 
ATOM   5722  O  OE1   . GLU B  2  295 ? 64.298 -38.898 -0.877  1.00 32.38  ?  327 GLU B OE1   1 
ATOM   5723  O  OE2   . GLU B  2  295 ? 62.372 -38.023 -0.863  1.00 31.37  -1 327 GLU B OE2   1 
ATOM   5724  N  N     . LYS B  2  296 ? 58.864 -41.005 2.539   1.00 33.23  ?  328 LYS B N     1 
ATOM   5725  C  CA    . LYS B  2  296 ? 57.514 -40.795 2.994   1.00 36.04  ?  328 LYS B CA    1 
ATOM   5726  C  C     . LYS B  2  296 ? 57.093 -39.405 2.904   1.00 37.08  ?  328 LYS B C     1 
ATOM   5727  O  O     . LYS B  2  296 ? 55.930 -39.132 2.783   1.00 42.85  ?  328 LYS B O     1 
ATOM   5728  C  CB    . LYS B  2  296 ? 57.352 -41.193 4.460   1.00 36.54  ?  328 LYS B CB    1 
ATOM   5729  C  CG    . LYS B  2  296 ? 55.979 -40.903 5.050   1.00 37.80  ?  328 LYS B CG    1 
ATOM   5730  C  CD    . LYS B  2  296 ? 55.584 -41.768 6.237   1.00 39.24  ?  328 LYS B CD    1 
ATOM   5731  C  CE    . LYS B  2  296 ? 56.123 -41.230 7.564   1.00 40.62  ?  328 LYS B CE    1 
ATOM   5732  N  NZ    . LYS B  2  296 ? 55.263 -41.341 8.780   1.00 39.26  1  328 LYS B NZ    1 
ATOM   5733  N  N     . GLN B  2  297 ? 58.056 -38.522 2.996   1.00 36.43  ?  329 GLN B N     1 
ATOM   5734  C  CA    . GLN B  2  297 ? 57.824 -37.109 3.034   1.00 34.92  ?  329 GLN B CA    1 
ATOM   5735  C  C     . GLN B  2  297 ? 58.446 -36.273 1.974   1.00 34.94  ?  329 GLN B C     1 
ATOM   5736  O  O     . GLN B  2  297 ? 59.543 -36.538 1.571   1.00 34.64  ?  329 GLN B O     1 
ATOM   5737  C  CB    . GLN B  2  297 ? 58.523 -36.618 4.284   1.00 34.18  ?  329 GLN B CB    1 
ATOM   5738  C  CG    . GLN B  2  297 ? 57.893 -37.009 5.572   1.00 34.28  ?  329 GLN B CG    1 
ATOM   5739  C  CD    . GLN B  2  297 ? 56.450 -36.702 5.593   1.00 35.10  ?  329 GLN B CD    1 
ATOM   5740  O  OE1   . GLN B  2  297 ? 55.696 -37.406 6.186   1.00 37.48  ?  329 GLN B OE1   1 
ATOM   5741  N  NE2   . GLN B  2  297 ? 56.055 -35.674 4.927   1.00 35.64  ?  329 GLN B NE2   1 
ATOM   5742  N  N     . THR B  2  298 ? 57.754 -35.209 1.582   1.00 34.76  ?  330 THR B N     1 
ATOM   5743  C  CA    . THR B  2  298 ? 58.263 -34.171 0.682   1.00 35.82  ?  330 THR B CA    1 
ATOM   5744  C  C     . THR B  2  298 ? 57.675 -32.860 1.122   1.00 36.26  ?  330 THR B C     1 
ATOM   5745  O  O     . THR B  2  298 ? 56.985 -32.849 2.094   1.00 36.56  ?  330 THR B O     1 
ATOM   5746  C  CB    . THR B  2  298 ? 58.059 -34.374 -0.830  1.00 34.75  ?  330 THR B CB    1 
ATOM   5747  O  OG1   . THR B  2  298 ? 58.916 -33.486 -1.534  1.00 31.91  ?  330 THR B OG1   1 
ATOM   5748  C  CG2   . THR B  2  298 ? 56.703 -34.085 -1.254  1.00 34.71  ?  330 THR B CG2   1 
ATOM   5749  N  N     . ASN B  2  299 ? 57.820 -31.818 0.357   1.00 35.20  ?  331 ASN B N     1 
ATOM   5750  C  CA    . ASN B  2  299 ? 57.235 -30.575 0.735   1.00 31.84  ?  331 ASN B CA    1 
ATOM   5751  C  C     . ASN B  2  299 ? 56.068 -30.238 -0.120  1.00 30.84  ?  331 ASN B C     1 
ATOM   5752  O  O     . ASN B  2  299 ? 55.867 -30.787 -1.146  1.00 29.81  ?  331 ASN B O     1 
ATOM   5753  C  CB    . ASN B  2  299 ? 58.259 -29.507 0.436   1.00 30.86  ?  331 ASN B CB    1 
ATOM   5754  C  CG    . ASN B  2  299 ? 58.879 -29.680 -0.926  1.00 31.30  ?  331 ASN B CG    1 
ATOM   5755  O  OD1   . ASN B  2  299 ? 59.324 -30.743 -1.227  1.00 31.66  ?  331 ASN B OD1   1 
ATOM   5756  N  ND2   . ASN B  2  299 ? 58.870 -28.669 -1.744  1.00 32.52  ?  331 ASN B ND2   1 
ATOM   5757  N  N     . ASN B  2  300 ? 55.277 -29.301 0.307   1.00 28.92  ?  332 ASN B N     1 
ATOM   5758  C  CA    . ASN B  2  300 ? 54.310 -28.754 -0.597  1.00 26.99  ?  332 ASN B CA    1 
ATOM   5759  C  C     . ASN B  2  300 ? 55.050 -27.617 -1.322  1.00 26.44  ?  332 ASN B C     1 
ATOM   5760  O  O     . ASN B  2  300 ? 55.984 -26.995 -0.737  1.00 22.02  ?  332 ASN B O     1 
ATOM   5761  C  CB    . ASN B  2  300 ? 53.066 -28.209 0.121   1.00 26.22  ?  332 ASN B CB    1 
ATOM   5762  C  CG    . ASN B  2  300 ? 52.047 -29.278 0.521   1.00 24.34  ?  332 ASN B CG    1 
ATOM   5763  O  OD1   . ASN B  2  300 ? 51.539 -29.241 1.634   1.00 24.28  ?  332 ASN B OD1   1 
ATOM   5764  N  ND2   . ASN B  2  300 ? 51.706 -30.183 -0.386  1.00 23.83  ?  332 ASN B ND2   1 
ATOM   5765  N  N     . PRO B  2  301 ? 54.639 -27.357 -2.595  1.00 27.84  ?  333 PRO B N     1 
ATOM   5766  C  CA    . PRO B  2  301 ? 55.111 -26.199 -3.348  1.00 29.04  ?  333 PRO B CA    1 
ATOM   5767  C  C     . PRO B  2  301 ? 55.014 -24.933 -2.493  1.00 31.46  ?  333 PRO B C     1 
ATOM   5768  O  O     . PRO B  2  301 ? 53.964 -24.663 -1.888  1.00 31.06  ?  333 PRO B O     1 
ATOM   5769  C  CB    . PRO B  2  301 ? 54.155 -26.151 -4.531  1.00 27.35  ?  333 PRO B CB    1 
ATOM   5770  C  CG    . PRO B  2  301 ? 53.810 -27.569 -4.760  1.00 26.79  ?  333 PRO B CG    1 
ATOM   5771  C  CD    . PRO B  2  301 ? 53.655 -28.130 -3.386  1.00 26.98  ?  333 PRO B CD    1 
ATOM   5772  N  N     . GLY B  2  302 ? 56.121 -24.196 -2.422  1.00 32.81  ?  334 GLY B N     1 
ATOM   5773  C  CA    . GLY B  2  302 ? 56.269 -23.133 -1.446  1.00 33.57  ?  334 GLY B CA    1 
ATOM   5774  C  C     . GLY B  2  302 ? 56.926 -21.910 -2.031  1.00 34.10  ?  334 GLY B C     1 
ATOM   5775  O  O     . GLY B  2  302 ? 57.807 -22.013 -2.889  1.00 34.76  ?  334 GLY B O     1 
ATOM   5776  N  N     . ILE B  2  303 ? 56.490 -20.763 -1.526  1.00 33.89  ?  335 ILE B N     1 
ATOM   5777  C  CA    . ILE B  2  303 ? 56.809 -19.452 -2.057  1.00 36.09  ?  335 ILE B CA    1 
ATOM   5778  C  C     . ILE B  2  303 ? 56.806 -18.647 -0.766  1.00 34.01  ?  335 ILE B C     1 
ATOM   5779  O  O     . ILE B  2  303 ? 56.024 -18.977 0.122   1.00 32.72  ?  335 ILE B O     1 
ATOM   5780  C  CB    . ILE B  2  303 ? 55.697 -18.997 -3.097  1.00 39.44  ?  335 ILE B CB    1 
ATOM   5781  C  CG1   . ILE B  2  303 ? 55.814 -19.735 -4.444  1.00 39.24  ?  335 ILE B CG1   1 
ATOM   5782  C  CG2   . ILE B  2  303 ? 55.701 -17.503 -3.408  1.00 40.59  ?  335 ILE B CG2   1 
ATOM   5783  C  CD1   . ILE B  2  303 ? 57.096 -19.485 -5.224  1.00 38.05  ?  335 ILE B CD1   1 
ATOM   5784  N  N     . ARG B  2  304 ? 57.678 -17.646 -0.627  1.00 32.97  ?  336 ARG B N     1 
ATOM   5785  C  CA    . ARG B  2  304 ? 57.646 -16.765 0.545   1.00 33.51  ?  336 ARG B CA    1 
ATOM   5786  C  C     . ARG B  2  304 ? 57.923 -15.311 0.267   1.00 38.24  ?  336 ARG B C     1 
ATOM   5787  O  O     . ARG B  2  304 ? 58.469 -14.922 -0.773  1.00 40.54  ?  336 ARG B O     1 
ATOM   5788  C  CB    . ARG B  2  304 ? 58.652 -17.211 1.577   1.00 32.59  ?  336 ARG B CB    1 
ATOM   5789  C  CG    . ARG B  2  304 ? 60.069 -17.181 1.077   1.00 32.19  ?  336 ARG B CG    1 
ATOM   5790  C  CD    . ARG B  2  304 ? 61.061 -17.554 2.157   1.00 33.81  ?  336 ARG B CD    1 
ATOM   5791  N  NE    . ARG B  2  304 ? 60.746 -18.806 2.859   1.00 36.08  ?  336 ARG B NE    1 
ATOM   5792  C  CZ    . ARG B  2  304 ? 61.595 -19.443 3.673   1.00 40.28  ?  336 ARG B CZ    1 
ATOM   5793  N  NH1   . ARG B  2  304 ? 62.834 -18.979 3.873   1.00 44.45  1  336 ARG B NH1   1 
ATOM   5794  N  NH2   . ARG B  2  304 ? 61.225 -20.564 4.291   1.00 40.63  ?  336 ARG B NH2   1 
ATOM   5795  N  N     . LEU B  2  305 ? 57.577 -14.512 1.264   1.00 43.64  ?  337 LEU B N     1 
ATOM   5796  C  CA    . LEU B  2  305 ? 57.693 -13.077 1.196   1.00 44.19  ?  337 LEU B CA    1 
ATOM   5797  C  C     . LEU B  2  305 ? 58.352 -12.521 2.459   1.00 47.54  ?  337 LEU B C     1 
ATOM   5798  O  O     . LEU B  2  305 ? 57.823 -12.660 3.599   1.00 43.85  ?  337 LEU B O     1 
ATOM   5799  C  CB    . LEU B  2  305 ? 56.307 -12.489 1.039   1.00 45.85  ?  337 LEU B CB    1 
ATOM   5800  C  CG    . LEU B  2  305 ? 56.223 -10.982 1.222   1.00 48.66  ?  337 LEU B CG    1 
ATOM   5801  C  CD1   . LEU B  2  305 ? 57.227 -10.255 0.333   1.00 49.54  ?  337 LEU B CD1   1 
ATOM   5802  C  CD2   . LEU B  2  305 ? 54.798 -10.566 0.918   1.00 49.67  ?  337 LEU B CD2   1 
ATOM   5803  N  N     . PHE B  2  306 ? 59.499 -11.876 2.231   1.00 49.77  ?  338 PHE B N     1 
ATOM   5804  C  CA    . PHE B  2  306 ? 60.261 -11.200 3.288   1.00 51.63  ?  338 PHE B CA    1 
ATOM   5805  C  C     . PHE B  2  306 ? 59.910 -9.727  3.439   1.00 51.41  ?  338 PHE B C     1 
ATOM   5806  O  O     . PHE B  2  306 ? 59.669 -9.033  2.440   1.00 48.34  ?  338 PHE B O     1 
ATOM   5807  C  CB    . PHE B  2  306 ? 61.774 -11.319 3.048   1.00 51.68  ?  338 PHE B CB    1 
ATOM   5808  C  CG    . PHE B  2  306 ? 62.322 -12.629 3.472   1.00 50.72  ?  338 PHE B CG    1 
ATOM   5809  C  CD1   . PHE B  2  306 ? 62.636 -12.857 4.804   1.00 50.83  ?  338 PHE B CD1   1 
ATOM   5810  C  CD2   . PHE B  2  306 ? 62.459 -13.656 2.560   1.00 49.80  ?  338 PHE B CD2   1 
ATOM   5811  C  CE1   . PHE B  2  306 ? 63.108 -14.096 5.218   1.00 51.31  ?  338 PHE B CE1   1 
ATOM   5812  C  CE2   . PHE B  2  306 ? 62.929 -14.896 2.960   1.00 51.62  ?  338 PHE B CE2   1 
ATOM   5813  C  CZ    . PHE B  2  306 ? 63.257 -15.119 4.294   1.00 52.53  ?  338 PHE B CZ    1 
ATOM   5814  N  N     . GLN B  2  307 ? 59.909 -9.284  4.705   1.00 50.02  ?  339 GLN B N     1 
ATOM   5815  C  CA    . GLN B  2  307 ? 59.772 -7.884  5.083   1.00 46.57  ?  339 GLN B CA    1 
ATOM   5816  C  C     . GLN B  2  307 ? 61.078 -7.388  5.692   1.00 49.09  ?  339 GLN B C     1 
ATOM   5817  O  O     . GLN B  2  307 ? 61.818 -8.155  6.326   1.00 49.54  ?  339 GLN B O     1 
ATOM   5818  C  CB    . GLN B  2  307 ? 58.622 -7.695  6.074   1.00 43.14  ?  339 GLN B CB    1 
ATOM   5819  C  CG    . GLN B  2  307 ? 57.244 -7.852  5.449   1.00 40.15  ?  339 GLN B CG    1 
ATOM   5820  C  CD    . GLN B  2  307 ? 56.120 -7.654  6.438   1.00 37.24  ?  339 GLN B CD    1 
ATOM   5821  O  OE1   . GLN B  2  307 ? 56.340 -7.345  7.599   1.00 36.14  ?  339 GLN B OE1   1 
ATOM   5822  N  NE2   . GLN B  2  307 ? 54.903 -7.842  5.980   1.00 36.49  ?  339 GLN B NE2   1 
ATOM   5823  N  N     . TYR B  2  308 ? 61.351 -6.103  5.466   1.00 52.47  ?  340 TYR B N     1 
ATOM   5824  C  CA    . TYR B  2  308 ? 62.546 -5.439  5.967   1.00 53.96  ?  340 TYR B CA    1 
ATOM   5825  C  C     . TYR B  2  308 ? 62.271 -3.964  6.287   1.00 54.74  ?  340 TYR B C     1 
ATOM   5826  O  O     . TYR B  2  308 ? 61.214 -3.404  5.954   1.00 50.18  ?  340 TYR B O     1 
ATOM   5827  C  CB    . TYR B  2  308 ? 63.718 -5.573  4.975   1.00 54.85  ?  340 TYR B CB    1 
ATOM   5828  C  CG    . TYR B  2  308 ? 63.481 -4.975  3.603   1.00 58.71  ?  340 TYR B CG    1 
ATOM   5829  C  CD1   . TYR B  2  308 ? 62.794 -5.685  2.612   1.00 59.88  ?  340 TYR B CD1   1 
ATOM   5830  C  CD2   . TYR B  2  308 ? 63.952 -3.705  3.285   1.00 64.11  ?  340 TYR B CD2   1 
ATOM   5831  C  CE1   . TYR B  2  308 ? 62.570 -5.148  1.355   1.00 57.66  ?  340 TYR B CE1   1 
ATOM   5832  C  CE2   . TYR B  2  308 ? 63.732 -3.161  2.023   1.00 66.32  ?  340 TYR B CE2   1 
ATOM   5833  C  CZ    . TYR B  2  308 ? 63.039 -3.892  1.066   1.00 61.34  ?  340 TYR B CZ    1 
ATOM   5834  O  OH    . TYR B  2  308 ? 62.831 -3.361  -0.183  1.00 62.84  ?  340 TYR B OH    1 
ATOM   5835  N  N     . ASP B  2  309 ? 63.234 -3.371  6.976   1.00 54.79  ?  341 ASP B N     1 
ATOM   5836  C  CA    . ASP B  2  309 ? 63.212 -1.982  7.329   1.00 55.39  ?  341 ASP B CA    1 
ATOM   5837  C  C     . ASP B  2  309 ? 64.061 -1.318  6.235   1.00 57.28  ?  341 ASP B C     1 
ATOM   5838  O  O     . ASP B  2  309 ? 65.225 -1.691  6.080   1.00 59.12  ?  341 ASP B O     1 
ATOM   5839  C  CB    . ASP B  2  309 ? 63.821 -1.843  8.733   1.00 57.43  ?  341 ASP B CB    1 
ATOM   5840  C  CG    . ASP B  2  309 ? 63.398 -0.570  9.443   1.00 60.75  ?  341 ASP B CG    1 
ATOM   5841  O  OD1   . ASP B  2  309 ? 64.004 0.473   9.152   1.00 65.04  ?  341 ASP B OD1   1 
ATOM   5842  O  OD2   . ASP B  2  309 ? 62.489 -0.602  10.307  1.00 59.14  -1 341 ASP B OD2   1 
ATOM   5843  N  N     . PRO B  2  310 ? 63.483 -0.376  5.438   1.00 57.21  ?  342 PRO B N     1 
ATOM   5844  C  CA    . PRO B  2  310 ? 64.219 0.323   4.356   1.00 57.91  ?  342 PRO B CA    1 
ATOM   5845  C  C     . PRO B  2  310 ? 65.427 1.178   4.794   1.00 57.30  ?  342 PRO B C     1 
ATOM   5846  O  O     . PRO B  2  310 ? 66.286 1.520   3.965   1.00 52.39  ?  342 PRO B O     1 
ATOM   5847  C  CB    . PRO B  2  310 ? 63.149 1.225   3.726   1.00 57.88  ?  342 PRO B CB    1 
ATOM   5848  C  CG    . PRO B  2  310 ? 61.856 0.593   4.063   1.00 57.17  ?  342 PRO B CG    1 
ATOM   5849  C  CD    . PRO B  2  310 ? 62.062 0.007   5.432   1.00 58.55  ?  342 PRO B CD    1 
ATOM   5850  N  N     . ARG B  2  311 ? 65.475 1.529   6.075   1.00 58.66  ?  343 ARG B N     1 
ATOM   5851  C  CA    . ARG B  2  311 ? 66.616 2.232   6.635   1.00 58.55  ?  343 ARG B CA    1 
ATOM   5852  C  C     . ARG B  2  311 ? 67.860 1.339   6.733   1.00 58.17  ?  343 ARG B C     1 
ATOM   5853  O  O     . ARG B  2  311 ? 68.836 1.604   6.043   1.00 59.87  ?  343 ARG B O     1 
ATOM   5854  C  CB    . ARG B  2  311 ? 66.259 2.827   7.997   1.00 61.00  ?  343 ARG B CB    1 
ATOM   5855  C  CG    . ARG B  2  311 ? 65.190 3.919   7.932   1.00 64.05  ?  343 ARG B CG    1 
ATOM   5856  C  CD    . ARG B  2  311 ? 64.835 4.418   9.330   1.00 65.49  ?  343 ARG B CD    1 
ATOM   5857  N  NE    . ARG B  2  311 ? 63.882 3.521   10.000  1.00 66.15  ?  343 ARG B NE    1 
ATOM   5858  C  CZ    . ARG B  2  311 ? 63.775 3.338   11.317  1.00 61.64  ?  343 ARG B CZ    1 
ATOM   5859  N  NH1   . ARG B  2  311 ? 64.583 3.962   12.174  1.00 60.58  1  343 ARG B NH1   1 
ATOM   5860  N  NH2   . ARG B  2  311 ? 62.853 2.495   11.779  1.00 59.24  ?  343 ARG B NH2   1 
ATOM   5861  N  N     . ASP B  2  312 ? 67.832 0.288   7.560   1.00 58.14  ?  344 ASP B N     1 
ATOM   5862  C  CA    . ASP B  2  312 ? 69.044 -0.565  7.786   1.00 57.84  ?  344 ASP B CA    1 
ATOM   5863  C  C     . ASP B  2  312 ? 68.972 -1.962  7.139   1.00 54.53  ?  344 ASP B C     1 
ATOM   5864  O  O     . ASP B  2  312 ? 69.929 -2.749  7.230   1.00 46.65  ?  344 ASP B O     1 
ATOM   5865  C  CB    . ASP B  2  312 ? 69.416 -0.671  9.292   1.00 58.96  ?  344 ASP B CB    1 
ATOM   5866  C  CG    . ASP B  2  312 ? 68.208 -0.961  10.204  1.00 62.14  ?  344 ASP B CG    1 
ATOM   5867  O  OD1   . ASP B  2  312 ? 67.046 -0.686  9.804   1.00 64.31  ?  344 ASP B OD1   1 
ATOM   5868  O  OD2   . ASP B  2  312 ? 68.429 -1.455  11.336  1.00 62.07  -1 344 ASP B OD2   1 
ATOM   5869  N  N     . TYR B  2  313 ? 67.848 -2.241  6.465   1.00 56.67  ?  345 TYR B N     1 
ATOM   5870  C  CA    . TYR B  2  313 ? 67.582 -3.554  5.828   1.00 57.82  ?  345 TYR B CA    1 
ATOM   5871  C  C     . TYR B  2  313 ? 67.691 -4.685  6.843   1.00 53.49  ?  345 TYR B C     1 
ATOM   5872  O  O     . TYR B  2  313 ? 68.252 -5.748  6.567   1.00 48.05  ?  345 TYR B O     1 
ATOM   5873  C  CB    . TYR B  2  313 ? 68.489 -3.766  4.604   1.00 59.34  ?  345 TYR B CB    1 
ATOM   5874  C  CG    . TYR B  2  313 ? 68.454 -2.561  3.681   1.00 59.30  ?  345 TYR B CG    1 
ATOM   5875  C  CD1   . TYR B  2  313 ? 67.330 -2.292  2.879   1.00 57.21  ?  345 TYR B CD1   1 
ATOM   5876  C  CD2   . TYR B  2  313 ? 69.518 -1.662  3.648   1.00 56.93  ?  345 TYR B CD2   1 
ATOM   5877  C  CE1   . TYR B  2  313 ? 67.292 -1.178  2.064   1.00 54.05  ?  345 TYR B CE1   1 
ATOM   5878  C  CE2   . TYR B  2  313 ? 69.478 -0.545  2.843   1.00 54.41  ?  345 TYR B CE2   1 
ATOM   5879  C  CZ    . TYR B  2  313 ? 68.375 -0.312  2.060   1.00 54.17  ?  345 TYR B CZ    1 
ATOM   5880  O  OH    . TYR B  2  313 ? 68.387 0.798   1.270   1.00 60.57  ?  345 TYR B OH    1 
ATOM   5881  N  N     . LYS B  2  314 ? 67.147 -4.401  8.026   1.00 52.06  ?  346 LYS B N     1 
ATOM   5882  C  CA    . LYS B  2  314 ? 67.012 -5.356  9.106   1.00 52.65  ?  346 LYS B CA    1 
ATOM   5883  C  C     . LYS B  2  314 ? 65.744 -6.152  8.800   1.00 52.04  ?  346 LYS B C     1 
ATOM   5884  O  O     . LYS B  2  314 ? 64.717 -5.576  8.409   1.00 52.06  ?  346 LYS B O     1 
ATOM   5885  C  CB    . LYS B  2  314 ? 66.909 -4.612  10.446  1.00 53.90  ?  346 LYS B CB    1 
ATOM   5886  C  CG    . LYS B  2  314 ? 66.395 -5.447  11.610  1.00 58.97  ?  346 LYS B CG    1 
ATOM   5887  C  CD    . LYS B  2  314 ? 66.580 -4.732  12.947  1.00 62.84  ?  346 LYS B CD    1 
ATOM   5888  C  CE    . LYS B  2  314 ? 65.596 -5.226  14.002  1.00 62.54  ?  346 LYS B CE    1 
ATOM   5889  N  NZ    . LYS B  2  314 ? 64.301 -4.501  13.860  1.00 64.01  1  346 LYS B NZ    1 
ATOM   5890  N  N     . LEU B  2  315 ? 65.812 -7.471  8.942   1.00 48.39  ?  347 LEU B N     1 
ATOM   5891  C  CA    . LEU B  2  315 ? 64.659 -8.302  8.610   1.00 48.22  ?  347 LEU B CA    1 
ATOM   5892  C  C     . LEU B  2  315 ? 63.541 -8.182  9.670   1.00 46.35  ?  347 LEU B C     1 
ATOM   5893  O  O     . LEU B  2  315 ? 63.756 -8.401  10.866  1.00 47.75  ?  347 LEU B O     1 
ATOM   5894  C  CB    . LEU B  2  315 ? 65.098 -9.758  8.401   1.00 47.84  ?  347 LEU B CB    1 
ATOM   5895  C  CG    . LEU B  2  315 ? 65.882 -10.017 7.118   1.00 47.14  ?  347 LEU B CG    1 
ATOM   5896  C  CD1   . LEU B  2  315 ? 66.458 -11.419 7.176   1.00 47.09  ?  347 LEU B CD1   1 
ATOM   5897  C  CD2   . LEU B  2  315 ? 64.997 -9.861  5.888   1.00 48.50  ?  347 LEU B CD2   1 
ATOM   5898  N  N     . LEU B  2  316 ? 62.351 -7.815  9.229   1.00 43.67  ?  348 LEU B N     1 
ATOM   5899  C  CA    . LEU B  2  316 ? 61.244 -7.662  10.149  1.00 44.40  ?  348 LEU B CA    1 
ATOM   5900  C  C     . LEU B  2  316 ? 60.465 -8.929  10.280  1.00 41.37  ?  348 LEU B C     1 
ATOM   5901  O  O     . LEU B  2  316 ? 60.005 -9.237  11.369  1.00 45.35  ?  348 LEU B O     1 
ATOM   5902  C  CB    . LEU B  2  316 ? 60.287 -6.552  9.706   1.00 47.67  ?  348 LEU B CB    1 
ATOM   5903  C  CG    . LEU B  2  316 ? 60.801 -5.111  9.800   1.00 51.16  ?  348 LEU B CG    1 
ATOM   5904  C  CD1   . LEU B  2  316 ? 59.650 -4.178  9.446   1.00 52.26  ?  348 LEU B CD1   1 
ATOM   5905  C  CD2   . LEU B  2  316 ? 61.408 -4.764  11.168  1.00 51.05  ?  348 LEU B CD2   1 
ATOM   5906  N  N     . ASP B  2  317 ? 60.275 -9.650  9.183   1.00 37.92  ?  349 ASP B N     1 
ATOM   5907  C  CA    . ASP B  2  317 ? 59.439 -10.838 9.230   1.00 37.41  ?  349 ASP B CA    1 
ATOM   5908  C  C     . ASP B  2  317 ? 59.581 -11.684 7.975   1.00 35.73  ?  349 ASP B C     1 
ATOM   5909  O  O     . ASP B  2  317 ? 60.266 -11.277 7.027   1.00 36.78  ?  349 ASP B O     1 
ATOM   5910  C  CB    . ASP B  2  317 ? 57.976 -10.417 9.397   1.00 39.38  ?  349 ASP B CB    1 
ATOM   5911  C  CG    . ASP B  2  317 ? 57.139 -11.459 10.129  1.00 40.59  ?  349 ASP B CG    1 
ATOM   5912  O  OD1   . ASP B  2  317 ? 57.208 -12.657 9.759   1.00 42.36  ?  349 ASP B OD1   1 
ATOM   5913  O  OD2   . ASP B  2  317 ? 56.395 -11.074 11.061  1.00 39.59  -1 349 ASP B OD2   1 
ATOM   5914  N  N     . MET B  2  318 ? 58.946 -12.857 7.988   1.00 32.40  ?  350 MET B N     1 
ATOM   5915  C  CA    . MET B  2  318 ? 58.743 -13.652 6.785   1.00 32.82  ?  350 MET B CA    1 
ATOM   5916  C  C     . MET B  2  318 ? 57.327 -14.277 6.690   1.00 31.58  ?  350 MET B C     1 
ATOM   5917  O  O     . MET B  2  318 ? 56.832 -14.874 7.665   1.00 29.35  ?  350 MET B O     1 
ATOM   5918  C  CB    . MET B  2  318 ? 59.807 -14.749 6.727   1.00 34.50  ?  350 MET B CB    1 
ATOM   5919  C  CG    . MET B  2  318 ? 59.782 -15.585 5.434   1.00 36.19  ?  350 MET B CG    1 
ATOM   5920  S  SD    . MET B  2  318 ? 59.005 -17.221 5.539   1.00 36.44  ?  350 MET B SD    1 
ATOM   5921  C  CE    . MET B  2  318 ? 60.283 -18.181 6.345   1.00 36.50  ?  350 MET B CE    1 
ATOM   5922  N  N     . LEU B  2  319 ? 56.679 -14.167 5.521   1.00 29.53  ?  351 LEU B N     1 
ATOM   5923  C  CA    . LEU B  2  319 ? 55.421 -14.906 5.319   1.00 28.50  ?  351 LEU B CA    1 
ATOM   5924  C  C     . LEU B  2  319 ? 55.671 -16.046 4.357   1.00 27.69  ?  351 LEU B C     1 
ATOM   5925  O  O     . LEU B  2  319 ? 56.363 -15.899 3.336   1.00 24.32  ?  351 LEU B O     1 
ATOM   5926  C  CB    . LEU B  2  319 ? 54.268 -14.040 4.821   1.00 28.48  ?  351 LEU B CB    1 
ATOM   5927  C  CG    . LEU B  2  319 ? 53.995 -12.721 5.548   1.00 29.24  ?  351 LEU B CG    1 
ATOM   5928  C  CD1   . LEU B  2  319 ? 55.129 -11.687 5.358   1.00 29.23  ?  351 LEU B CD1   1 
ATOM   5929  C  CD2   . LEU B  2  319 ? 52.646 -12.196 5.063   1.00 27.95  ?  351 LEU B CD2   1 
ATOM   5930  N  N     . GLN B  2  320 ? 55.120 -17.199 4.721   1.00 28.24  ?  352 GLN B N     1 
ATOM   5931  C  CA    . GLN B  2  320 ? 55.298 -18.392 3.937   1.00 28.53  ?  352 GLN B CA    1 
ATOM   5932  C  C     . GLN B  2  320 ? 54.008 -18.740 3.305   1.00 28.51  ?  352 GLN B C     1 
ATOM   5933  O  O     . GLN B  2  320 ? 53.023 -18.965 4.020   1.00 25.22  ?  352 GLN B O     1 
ATOM   5934  C  CB    . GLN B  2  320 ? 55.741 -19.577 4.773   1.00 30.20  ?  352 GLN B CB    1 
ATOM   5935  C  CG    . GLN B  2  320 ? 56.050 -20.814 3.916   1.00 32.40  ?  352 GLN B CG    1 
ATOM   5936  C  CD    . GLN B  2  320 ? 57.388 -20.735 3.177   1.00 33.59  ?  352 GLN B CD    1 
ATOM   5937  O  OE1   . GLN B  2  320 ? 58.426 -20.473 3.800   1.00 35.60  ?  352 GLN B OE1   1 
ATOM   5938  N  NE2   . GLN B  2  320 ? 57.375 -20.971 1.851   1.00 33.58  ?  352 GLN B NE2   1 
ATOM   5939  N  N     . TYR B  2  321 ? 54.046 -18.772 1.962   1.00 30.83  ?  353 TYR B N     1 
ATOM   5940  C  CA    . TYR B  2  321 ? 52.943 -19.217 1.104   1.00 30.89  ?  353 TYR B CA    1 
ATOM   5941  C  C     . TYR B  2  321 ? 53.204 -20.618 0.631   1.00 30.80  ?  353 TYR B C     1 
ATOM   5942  O  O     . TYR B  2  321 ? 54.348 -21.047 0.558   1.00 30.09  ?  353 TYR B O     1 
ATOM   5943  C  CB    . TYR B  2  321 ? 52.775 -18.304 -0.100  1.00 30.31  ?  353 TYR B CB    1 
ATOM   5944  C  CG    . TYR B  2  321 ? 52.480 -16.904 0.320   1.00 31.37  ?  353 TYR B CG    1 
ATOM   5945  C  CD1   . TYR B  2  321 ? 51.204 -16.552 0.768   1.00 30.58  ?  353 TYR B CD1   1 
ATOM   5946  C  CD2   . TYR B  2  321 ? 53.490 -15.932 0.317   1.00 31.95  ?  353 TYR B CD2   1 
ATOM   5947  C  CE1   . TYR B  2  321 ? 50.932 -15.262 1.157   1.00 31.37  ?  353 TYR B CE1   1 
ATOM   5948  C  CE2   . TYR B  2  321 ? 53.232 -14.633 0.703   1.00 32.38  ?  353 TYR B CE2   1 
ATOM   5949  C  CZ    . TYR B  2  321 ? 51.953 -14.302 1.121   1.00 33.26  ?  353 TYR B CZ    1 
ATOM   5950  O  OH    . TYR B  2  321 ? 51.708 -13.009 1.521   1.00 34.48  ?  353 TYR B OH    1 
ATOM   5951  N  N     . TYR B  2  322 ? 52.123 -21.321 0.303   1.00 32.32  ?  354 TYR B N     1 
ATOM   5952  C  CA    . TYR B  2  322 ? 52.200 -22.724 -0.076  1.00 31.41  ?  354 TYR B CA    1 
ATOM   5953  C  C     . TYR B  2  322 ? 50.971 -23.210 -0.878  1.00 30.97  ?  354 TYR B C     1 
ATOM   5954  O  O     . TYR B  2  322 ? 49.914 -22.544 -0.896  1.00 27.42  ?  354 TYR B O     1 
ATOM   5955  C  CB    . TYR B  2  322 ? 52.419 -23.555 1.181   1.00 30.90  ?  354 TYR B CB    1 
ATOM   5956  C  CG    . TYR B  2  322 ? 51.165 -24.065 1.880   1.00 31.58  ?  354 TYR B CG    1 
ATOM   5957  C  CD1   . TYR B  2  322 ? 50.402 -23.251 2.719   1.00 31.09  ?  354 TYR B CD1   1 
ATOM   5958  C  CD2   . TYR B  2  322 ? 50.781 -25.399 1.739   1.00 32.12  ?  354 TYR B CD2   1 
ATOM   5959  C  CE1   . TYR B  2  322 ? 49.288 -23.761 3.372   1.00 31.94  ?  354 TYR B CE1   1 
ATOM   5960  C  CE2   . TYR B  2  322 ? 49.679 -25.914 2.386   1.00 32.20  ?  354 TYR B CE2   1 
ATOM   5961  C  CZ    . TYR B  2  322 ? 48.933 -25.105 3.191   1.00 32.29  ?  354 TYR B CZ    1 
ATOM   5962  O  OH    . TYR B  2  322 ? 47.847 -25.691 3.797   1.00 33.80  ?  354 TYR B OH    1 
ATOM   5963  N  N     . LEU B  2  323 ? 51.141 -24.355 -1.555  1.00 31.75  ?  355 LEU B N     1 
ATOM   5964  C  CA    . LEU B  2  323 ? 50.053 -25.018 -2.310  1.00 32.62  ?  355 LEU B CA    1 
ATOM   5965  C  C     . LEU B  2  323 ? 49.773 -26.377 -1.667  1.00 33.52  ?  355 LEU B C     1 
ATOM   5966  O  O     . LEU B  2  323 ? 50.642 -27.232 -1.687  1.00 34.34  ?  355 LEU B O     1 
ATOM   5967  C  CB    . LEU B  2  323 ? 50.415 -25.175 -3.818  1.00 30.87  ?  355 LEU B CB    1 
ATOM   5968  C  CG    . LEU B  2  323 ? 49.350 -25.513 -4.909  1.00 29.37  ?  355 LEU B CG    1 
ATOM   5969  C  CD1   . LEU B  2  323 ? 48.212 -24.527 -4.928  1.00 29.10  ?  355 LEU B CD1   1 
ATOM   5970  C  CD2   . LEU B  2  323 ? 49.920 -25.524 -6.325  1.00 28.25  ?  355 LEU B CD2   1 
ATOM   5971  N  N     . ASN B  2  324 ? 48.595 -26.560 -1.057  1.00 34.90  ?  356 ASN B N     1 
ATOM   5972  C  CA    . ASN B  2  324 ? 48.133 -27.913 -0.712  1.00 35.42  ?  356 ASN B CA    1 
ATOM   5973  C  C     . ASN B  2  324 ? 47.833 -28.609 -2.058  1.00 35.61  ?  356 ASN B C     1 
ATOM   5974  O  O     . ASN B  2  324 ? 46.704 -28.540 -2.599  1.00 33.36  ?  356 ASN B O     1 
ATOM   5975  C  CB    . ASN B  2  324 ? 46.925 -27.934 0.262   1.00 36.39  ?  356 ASN B CB    1 
ATOM   5976  C  CG    . ASN B  2  324 ? 46.473 -29.355 0.606   1.00 37.49  ?  356 ASN B CG    1 
ATOM   5977  O  OD1   . ASN B  2  324 ? 46.705 -30.281 -0.177  1.00 38.23  ?  356 ASN B OD1   1 
ATOM   5978  N  ND2   . ASN B  2  324 ? 45.832 -29.545 1.780   1.00 40.28  ?  356 ASN B ND2   1 
ATOM   5979  N  N     . LEU B  2  325 ? 48.893 -29.246 -2.580  1.00 35.56  ?  357 LEU B N     1 
ATOM   5980  C  CA    . LEU B  2  325 ? 48.921 -29.937 -3.877  1.00 33.30  ?  357 LEU B CA    1 
ATOM   5981  C  C     . LEU B  2  325 ? 47.738 -30.903 -4.024  1.00 34.57  ?  357 LEU B C     1 
ATOM   5982  O  O     . LEU B  2  325 ? 46.936 -30.759 -4.939  1.00 31.83  ?  357 LEU B O     1 
ATOM   5983  C  CB    . LEU B  2  325 ? 50.274 -30.648 -4.044  1.00 31.04  ?  357 LEU B CB    1 
ATOM   5984  C  CG    . LEU B  2  325 ? 50.541 -31.420 -5.332  1.00 29.69  ?  357 LEU B CG    1 
ATOM   5985  C  CD1   . LEU B  2  325 ? 50.331 -30.516 -6.537  1.00 29.79  ?  357 LEU B CD1   1 
ATOM   5986  C  CD2   . LEU B  2  325 ? 51.942 -32.000 -5.303  1.00 28.05  ?  357 LEU B CD2   1 
ATOM   5987  N  N     . THR B  2  326 ? 47.608 -31.837 -3.081  1.00 38.23  ?  358 THR B N     1 
ATOM   5988  C  CA    . THR B  2  326 ? 46.508 -32.811 -3.071  1.00 40.47  ?  358 THR B CA    1 
ATOM   5989  C  C     . THR B  2  326 ? 45.128 -32.224 -3.249  1.00 42.13  ?  358 THR B C     1 
ATOM   5990  O  O     . THR B  2  326 ? 44.325 -32.760 -4.006  1.00 41.61  ?  358 THR B O     1 
ATOM   5991  C  CB    . THR B  2  326 ? 46.452 -33.539 -1.742  1.00 40.54  ?  358 THR B CB    1 
ATOM   5992  O  OG1   . THR B  2  326 ? 47.711 -34.170 -1.533  1.00 41.81  ?  358 THR B OG1   1 
ATOM   5993  C  CG2   . THR B  2  326 ? 45.322 -34.563 -1.754  1.00 40.50  ?  358 THR B CG2   1 
ATOM   5994  N  N     . GLU B  2  327 ? 44.848 -31.173 -2.484  1.00 45.98  ?  359 GLU B N     1 
ATOM   5995  C  CA    . GLU B  2  327 ? 43.614 -30.414 -2.607  1.00 48.13  ?  359 GLU B CA    1 
ATOM   5996  C  C     . GLU B  2  327 ? 43.720 -29.744 -3.957  1.00 44.57  ?  359 GLU B C     1 
ATOM   5997  O  O     . GLU B  2  327 ? 42.907 -30.013 -4.827  1.00 44.23  ?  359 GLU B O     1 
ATOM   5998  C  CB    . GLU B  2  327 ? 43.483 -29.391 -1.466  1.00 54.53  ?  359 GLU B CB    1 
ATOM   5999  C  CG    . GLU B  2  327 ? 42.287 -28.453 -1.536  1.00 59.75  ?  359 GLU B CG    1 
ATOM   6000  C  CD    . GLU B  2  327 ? 42.678 -26.978 -1.348  1.00 67.71  ?  359 GLU B CD    1 
ATOM   6001  O  OE1   . GLU B  2  327 ? 42.385 -26.422 -0.255  1.00 68.62  ?  359 GLU B OE1   1 
ATOM   6002  O  OE2   . GLU B  2  327 ? 43.282 -26.378 -2.291  1.00 65.79  -1 359 GLU B OE2   1 
ATOM   6003  N  N     . ALA B  2  328 ? 44.762 -28.937 -4.161  1.00 40.93  ?  360 ALA B N     1 
ATOM   6004  C  CA    . ALA B  2  328 ? 44.936 -28.219 -5.429  1.00 40.59  ?  360 ALA B CA    1 
ATOM   6005  C  C     . ALA B  2  328 ? 44.668 -29.087 -6.647  1.00 40.54  ?  360 ALA B C     1 
ATOM   6006  O  O     . ALA B  2  328 ? 44.156 -28.611 -7.643  1.00 40.25  ?  360 ALA B O     1 
ATOM   6007  C  CB    . ALA B  2  328 ? 46.320 -27.624 -5.531  1.00 40.38  ?  360 ALA B CB    1 
ATOM   6008  N  N     . ASN B  2  329 ? 45.016 -30.361 -6.575  1.00 40.92  ?  361 ASN B N     1 
ATOM   6009  C  CA    . ASN B  2  329 ? 44.635 -31.271 -7.626  1.00 41.10  ?  361 ASN B CA    1 
ATOM   6010  C  C     . ASN B  2  329 ? 43.180 -31.645 -7.456  1.00 43.86  ?  361 ASN B C     1 
ATOM   6011  O  O     . ASN B  2  329 ? 42.416 -31.401 -8.362  1.00 48.29  ?  361 ASN B O     1 
ATOM   6012  C  CB    . ASN B  2  329 ? 45.549 -32.494 -7.698  1.00 41.33  ?  361 ASN B CB    1 
ATOM   6013  C  CG    . ASN B  2  329 ? 46.865 -32.211 -8.430  1.00 42.41  ?  361 ASN B CG    1 
ATOM   6014  O  OD1   . ASN B  2  329 ? 46.986 -31.272 -9.225  1.00 41.24  ?  361 ASN B OD1   1 
ATOM   6015  N  ND2   . ASN B  2  329 ? 47.862 -33.039 -8.160  1.00 44.15  ?  361 ASN B ND2   1 
ATOM   6016  N  N     . LEU B  2  330 ? 42.774 -32.167 -6.297  1.00 49.83  ?  362 LEU B N     1 
ATOM   6017  C  CA    . LEU B  2  330 ? 41.357 -32.590 -6.060  1.00 52.23  ?  362 LEU B CA    1 
ATOM   6018  C  C     . LEU B  2  330 ? 40.307 -31.629 -6.619  1.00 53.16  ?  362 LEU B C     1 
ATOM   6019  O  O     . LEU B  2  330 ? 39.348 -32.076 -7.240  1.00 55.10  ?  362 LEU B O     1 
ATOM   6020  C  CB    . LEU B  2  330 ? 41.046 -32.806 -4.562  1.00 52.42  ?  362 LEU B CB    1 
ATOM   6021  C  CG    . LEU B  2  330 ? 41.281 -34.195 -3.954  1.00 52.74  ?  362 LEU B CG    1 
ATOM   6022  C  CD1   . LEU B  2  330 ? 40.880 -34.215 -2.481  1.00 51.45  ?  362 LEU B CD1   1 
ATOM   6023  C  CD2   . LEU B  2  330 ? 40.530 -35.258 -4.741  1.00 51.68  ?  362 LEU B CD2   1 
ATOM   6024  N  N     . LYS B  2  331 ? 40.480 -30.328 -6.372  1.00 55.10  ?  363 LYS B N     1 
ATOM   6025  C  CA    . LYS B  2  331 ? 39.561 -29.285 -6.872  1.00 56.58  ?  363 LYS B CA    1 
ATOM   6026  C  C     . LYS B  2  331 ? 39.933 -28.880 -8.299  1.00 53.98  ?  363 LYS B C     1 
ATOM   6027  O  O     . LYS B  2  331 ? 39.085 -28.455 -9.091  1.00 51.43  ?  363 LYS B O     1 
ATOM   6028  C  CB    . LYS B  2  331 ? 39.583 -28.049 -5.946  1.00 59.41  ?  363 LYS B CB    1 
ATOM   6029  C  CG    . LYS B  2  331 ? 38.907 -28.278 -4.598  1.00 62.38  ?  363 LYS B CG    1 
ATOM   6030  C  CD    . LYS B  2  331 ? 39.479 -27.395 -3.494  1.00 67.53  ?  363 LYS B CD    1 
ATOM   6031  C  CE    . LYS B  2  331 ? 38.946 -25.970 -3.525  1.00 71.86  ?  363 LYS B CE    1 
ATOM   6032  N  NZ    . LYS B  2  331 ? 39.054 -25.318 -2.184  1.00 72.50  1  363 LYS B NZ    1 
ATOM   6033  N  N     . GLY B  2  332 ? 41.213 -29.023 -8.619  1.00 50.88  ?  364 GLY B N     1 
ATOM   6034  C  CA    . GLY B  2  332 ? 41.728 -28.585 -9.888  1.00 49.19  ?  364 GLY B CA    1 
ATOM   6035  C  C     . GLY B  2  332 ? 41.714 -27.076 -9.894  1.00 49.88  ?  364 GLY B C     1 
ATOM   6036  O  O     . GLY B  2  332 ? 41.173 -26.486 -10.806 1.00 51.74  ?  364 GLY B O     1 
ATOM   6037  N  N     . GLU B  2  333 ? 42.279 -26.457 -8.854  1.00 52.10  ?  365 GLU B N     1 
ATOM   6038  C  CA    . GLU B  2  333 ? 42.491 -25.000 -8.805  1.00 52.43  ?  365 GLU B CA    1 
ATOM   6039  C  C     . GLU B  2  333 ? 43.796 -24.627 -8.044  1.00 48.74  ?  365 GLU B C     1 
ATOM   6040  O  O     . GLU B  2  333 ? 44.208 -25.339 -7.128  1.00 46.02  ?  365 GLU B O     1 
ATOM   6041  C  CB    . GLU B  2  333 ? 41.276 -24.307 -8.157  1.00 56.86  ?  365 GLU B CB    1 
ATOM   6042  C  CG    . GLU B  2  333 ? 39.951 -24.328 -8.947  1.00 59.92  ?  365 GLU B CG    1 
ATOM   6043  C  CD    . GLU B  2  333 ? 39.930 -23.470 -10.227 1.00 61.62  ?  365 GLU B CD    1 
ATOM   6044  O  OE1   . GLU B  2  333 ? 40.915 -22.745 -10.514 1.00 63.83  ?  365 GLU B OE1   1 
ATOM   6045  O  OE2   . GLU B  2  333 ? 38.910 -23.521 -10.961 1.00 62.28  -1 365 GLU B OE2   1 
ATOM   6046  N  N     . SER B  2  334 ? 44.427 -23.513 -8.426  1.00 47.28  ?  366 SER B N     1 
ATOM   6047  C  CA    . SER B  2  334 ? 45.637 -22.995 -7.755  1.00 48.53  ?  366 SER B CA    1 
ATOM   6048  C  C     . SER B  2  334 ? 45.355 -22.286 -6.456  1.00 50.62  ?  366 SER B C     1 
ATOM   6049  O  O     . SER B  2  334 ? 45.529 -21.063 -6.377  1.00 49.54  ?  366 SER B O     1 
ATOM   6050  C  CB    . SER B  2  334 ? 46.336 -21.951 -8.612  1.00 51.04  ?  366 SER B CB    1 
ATOM   6051  O  OG    . SER B  2  334 ? 46.711 -22.500 -9.836  1.00 59.17  ?  366 SER B OG    1 
ATOM   6052  N  N     . ILE B  2  335 ? 44.980 -23.036 -5.429  1.00 52.59  ?  367 ILE B N     1 
ATOM   6053  C  CA    . ILE B  2  335 ? 44.654 -22.440 -4.150  1.00 56.19  ?  367 ILE B CA    1 
ATOM   6054  C  C     . ILE B  2  335 ? 45.950 -22.148 -3.383  1.00 52.30  ?  367 ILE B C     1 
ATOM   6055  O  O     . ILE B  2  335 ? 46.342 -22.920 -2.485  1.00 56.62  ?  367 ILE B O     1 
ATOM   6056  C  CB    . ILE B  2  335 ? 43.722 -23.360 -3.324  1.00 65.11  ?  367 ILE B CB    1 
ATOM   6057  C  CG1   . ILE B  2  335 ? 42.543 -23.875 -4.167  1.00 68.71  ?  367 ILE B CG1   1 
ATOM   6058  C  CG2   . ILE B  2  335 ? 43.179 -22.611 -2.114  1.00 68.74  ?  367 ILE B CG2   1 
ATOM   6059  C  CD1   . ILE B  2  335 ? 41.745 -22.783 -4.862  1.00 68.20  ?  367 ILE B CD1   1 
ATOM   6060  N  N     . TRP B  2  336 ? 46.626 -21.054 -3.756  1.00 45.26  ?  368 TRP B N     1 
ATOM   6061  C  CA    . TRP B  2  336 ? 47.833 -20.626 -3.053  1.00 43.83  ?  368 TRP B CA    1 
ATOM   6062  C  C     . TRP B  2  336 ? 47.378 -20.044 -1.728  1.00 45.52  ?  368 TRP B C     1 
ATOM   6063  O  O     . TRP B  2  336 ? 46.704 -19.031 -1.692  1.00 46.16  ?  368 TRP B O     1 
ATOM   6064  C  CB    . TRP B  2  336 ? 48.707 -19.635 -3.870  1.00 42.99  ?  368 TRP B CB    1 
ATOM   6065  C  CG    . TRP B  2  336 ? 49.685 -20.359 -4.736  1.00 44.28  ?  368 TRP B CG    1 
ATOM   6066  C  CD1   . TRP B  2  336 ? 49.508 -20.747 -6.047  1.00 47.18  ?  368 TRP B CD1   1 
ATOM   6067  C  CD2   . TRP B  2  336 ? 50.957 -20.877 -4.339  1.00 44.60  ?  368 TRP B CD2   1 
ATOM   6068  N  NE1   . TRP B  2  336 ? 50.601 -21.466 -6.487  1.00 46.13  ?  368 TRP B NE1   1 
ATOM   6069  C  CE2   . TRP B  2  336 ? 51.502 -21.564 -5.457  1.00 46.45  ?  368 TRP B CE2   1 
ATOM   6070  C  CE3   . TRP B  2  336 ? 51.691 -20.841 -3.144  1.00 42.46  ?  368 TRP B CE3   1 
ATOM   6071  C  CZ2   . TRP B  2  336 ? 52.752 -22.196 -5.411  1.00 44.81  ?  368 TRP B CZ2   1 
ATOM   6072  C  CZ3   . TRP B  2  336 ? 52.934 -21.476 -3.104  1.00 41.34  ?  368 TRP B CZ3   1 
ATOM   6073  C  CH2   . TRP B  2  336 ? 53.445 -22.144 -4.227  1.00 42.13  ?  368 TRP B CH2   1 
ATOM   6074  N  N     . LYS B  2  337 ? 47.707 -20.727 -0.639  1.00 47.31  ?  369 LYS B N     1 
ATOM   6075  C  CA    . LYS B  2  337 ? 47.355 -20.263 0.693   1.00 47.45  ?  369 LYS B CA    1 
ATOM   6076  C  C     . LYS B  2  337 ? 48.584 -19.683 1.401   1.00 44.63  ?  369 LYS B C     1 
ATOM   6077  O  O     . LYS B  2  337 ? 49.711 -19.763 0.903   1.00 41.54  ?  369 LYS B O     1 
ATOM   6078  C  CB    . LYS B  2  337 ? 46.785 -21.414 1.539   1.00 51.17  ?  369 LYS B CB    1 
ATOM   6079  C  CG    . LYS B  2  337 ? 45.601 -22.169 0.949   1.00 52.54  ?  369 LYS B CG    1 
ATOM   6080  C  CD    . LYS B  2  337 ? 45.144 -23.253 1.923   1.00 56.14  ?  369 LYS B CD    1 
ATOM   6081  C  CE    . LYS B  2  337 ? 44.327 -24.342 1.239   1.00 60.62  ?  369 LYS B CE    1 
ATOM   6082  N  NZ    . LYS B  2  337 ? 44.436 -25.648 1.956   1.00 62.29  1  369 LYS B NZ    1 
ATOM   6083  N  N     . LEU B  2  338 ? 48.318 -19.084 2.558   1.00 42.08  ?  370 LEU B N     1 
ATOM   6084  C  CA    . LEU B  2  338 ? 49.327 -18.599 3.480   1.00 39.63  ?  370 LEU B CA    1 
ATOM   6085  C  C     . LEU B  2  338 ? 49.568 -19.710 4.499   1.00 38.93  ?  370 LEU B C     1 
ATOM   6086  O  O     . LEU B  2  338 ? 48.621 -20.220 5.093   1.00 38.76  ?  370 LEU B O     1 
ATOM   6087  C  CB    . LEU B  2  338 ? 48.787 -17.363 4.184   1.00 39.43  ?  370 LEU B CB    1 
ATOM   6088  C  CG    . LEU B  2  338 ? 49.550 -16.830 5.386   1.00 40.60  ?  370 LEU B CG    1 
ATOM   6089  C  CD1   . LEU B  2  338 ? 50.827 -16.104 4.961   1.00 42.68  ?  370 LEU B CD1   1 
ATOM   6090  C  CD2   . LEU B  2  338 ? 48.632 -15.928 6.190   1.00 39.81  ?  370 LEU B CD2   1 
ATOM   6091  N  N     . GLU B  2  339 ? 50.827 -20.090 4.708   1.00 38.15  ?  371 GLU B N     1 
ATOM   6092  C  CA    . GLU B  2  339 ? 51.156 -21.163 5.664   1.00 35.65  ?  371 GLU B CA    1 
ATOM   6093  C  C     . GLU B  2  339 ? 51.422 -20.523 6.998   1.00 33.12  ?  371 GLU B C     1 
ATOM   6094  O  O     . GLU B  2  339 ? 50.882 -20.971 7.993   1.00 34.90  ?  371 GLU B O     1 
ATOM   6095  C  CB    . GLU B  2  339 ? 52.385 -21.986 5.231   1.00 35.34  ?  371 GLU B CB    1 
ATOM   6096  C  CG    . GLU B  2  339 ? 52.554 -23.335 5.945   1.00 33.81  ?  371 GLU B CG    1 
ATOM   6097  C  CD    . GLU B  2  339 ? 53.998 -23.884 5.918   1.00 33.66  ?  371 GLU B CD    1 
ATOM   6098  O  OE1   . GLU B  2  339 ? 54.950 -23.125 5.661   1.00 31.37  ?  371 GLU B OE1   1 
ATOM   6099  O  OE2   . GLU B  2  339 ? 54.208 -25.092 6.174   1.00 33.95  -1 371 GLU B OE2   1 
ATOM   6100  N  N     . TYR B  2  340 ? 52.261 -19.492 7.023   1.00 31.19  ?  372 TYR B N     1 
ATOM   6101  C  CA    . TYR B  2  340 ? 52.514 -18.789 8.256   1.00 31.75  ?  372 TYR B CA    1 
ATOM   6102  C  C     . TYR B  2  340 ? 53.169 -17.451 8.062   1.00 33.49  ?  372 TYR B C     1 
ATOM   6103  O  O     . TYR B  2  340 ? 53.799 -17.189 7.034   1.00 32.08  ?  372 TYR B O     1 
ATOM   6104  C  CB    . TYR B  2  340 ? 53.373 -19.621 9.209   1.00 32.22  ?  372 TYR B CB    1 
ATOM   6105  C  CG    . TYR B  2  340 ? 54.815 -19.773 8.795   1.00 34.23  ?  372 TYR B CG    1 
ATOM   6106  C  CD1   . TYR B  2  340 ? 55.758 -18.794 9.094   1.00 36.38  ?  372 TYR B CD1   1 
ATOM   6107  C  CD2   . TYR B  2  340 ? 55.246 -20.908 8.132   1.00 35.59  ?  372 TYR B CD2   1 
ATOM   6108  C  CE1   . TYR B  2  340 ? 57.089 -18.927 8.722   1.00 37.08  ?  372 TYR B CE1   1 
ATOM   6109  C  CE2   . TYR B  2  340 ? 56.575 -21.060 7.755   1.00 36.74  ?  372 TYR B CE2   1 
ATOM   6110  C  CZ    . TYR B  2  340 ? 57.494 -20.070 8.043   1.00 36.92  ?  372 TYR B CZ    1 
ATOM   6111  O  OH    . TYR B  2  340 ? 58.802 -20.242 7.653   1.00 34.18  ?  372 TYR B OH    1 
ATOM   6112  N  N     . ILE B  2  341 ? 53.003 -16.622 9.101   1.00 37.28  ?  373 ILE B N     1 
ATOM   6113  C  CA    . ILE B  2  341 ? 53.766 -15.372 9.309   1.00 38.69  ?  373 ILE B CA    1 
ATOM   6114  C  C     . ILE B  2  341 ? 54.785 -15.582 10.449  1.00 35.25  ?  373 ILE B C     1 
ATOM   6115  O  O     . ILE B  2  341 ? 54.376 -15.807 11.583  1.00 35.86  ?  373 ILE B O     1 
ATOM   6116  C  CB    . ILE B  2  341 ? 52.832 -14.184 9.670   1.00 39.51  ?  373 ILE B CB    1 
ATOM   6117  C  CG1   . ILE B  2  341 ? 51.592 -14.181 8.759   1.00 40.71  ?  373 ILE B CG1   1 
ATOM   6118  C  CG2   . ILE B  2  341 ? 53.601 -12.851 9.601   1.00 38.35  ?  373 ILE B CG2   1 
ATOM   6119  C  CD1   . ILE B  2  341 ? 50.477 -13.261 9.223   1.00 42.25  ?  373 ILE B CD1   1 
ATOM   6120  N  N     . LEU B  2  342 ? 56.084 -15.493 10.157  1.00 31.41  ?  374 LEU B N     1 
ATOM   6121  C  CA    . LEU B  2  342 ? 57.082 -16.071 11.034  1.00 31.71  ?  374 LEU B CA    1 
ATOM   6122  C  C     . LEU B  2  342 ? 56.967 -15.640 12.493  1.00 33.82  ?  374 LEU B C     1 
ATOM   6123  O  O     . LEU B  2  342 ? 56.883 -16.499 13.400  1.00 33.32  ?  374 LEU B O     1 
ATOM   6124  C  CB    . LEU B  2  342 ? 58.481 -15.804 10.526  1.00 32.61  ?  374 LEU B CB    1 
ATOM   6125  C  CG    . LEU B  2  342 ? 59.510 -16.749 11.154  1.00 34.39  ?  374 LEU B CG    1 
ATOM   6126  C  CD1   . LEU B  2  342 ? 60.630 -17.005 10.174  1.00 35.15  ?  374 LEU B CD1   1 
ATOM   6127  C  CD2   . LEU B  2  342 ? 60.086 -16.209 12.461  1.00 35.72  ?  374 LEU B CD2   1 
ATOM   6128  N  N     . THR B  2  343 ? 56.951 -14.329 12.732  1.00 35.60  ?  375 THR B N     1 
ATOM   6129  C  CA    . THR B  2  343 ? 56.876 -13.800 14.117  1.00 36.32  ?  375 THR B CA    1 
ATOM   6130  C  C     . THR B  2  343 ? 55.558 -14.160 14.810  1.00 37.59  ?  375 THR B C     1 
ATOM   6131  O  O     . THR B  2  343 ? 55.533 -14.313 16.027  1.00 35.82  ?  375 THR B O     1 
ATOM   6132  C  CB    . THR B  2  343 ? 57.047 -12.264 14.207  1.00 35.68  ?  375 THR B CB    1 
ATOM   6133  O  OG1   . THR B  2  343 ? 55.927 -11.614 13.597  1.00 36.13  ?  375 THR B OG1   1 
ATOM   6134  C  CG2   . THR B  2  343 ? 58.364 -11.790 13.562  1.00 34.84  ?  375 THR B CG2   1 
ATOM   6135  N  N     . GLN B  2  344 ? 54.475 -14.283 14.034  1.00 40.62  ?  376 GLN B N     1 
ATOM   6136  C  CA    . GLN B  2  344 ? 53.166 -14.713 14.553  1.00 43.48  ?  376 GLN B CA    1 
ATOM   6137  C  C     . GLN B  2  344 ? 53.166 -16.099 15.182  1.00 40.60  ?  376 GLN B C     1 
ATOM   6138  O  O     . GLN B  2  344 ? 52.844 -16.233 16.353  1.00 39.29  ?  376 GLN B O     1 
ATOM   6139  C  CB    . GLN B  2  344 ? 52.110 -14.717 13.443  1.00 50.82  ?  376 GLN B CB    1 
ATOM   6140  C  CG    . GLN B  2  344 ? 51.625 -13.345 13.016  1.00 56.62  ?  376 GLN B CG    1 
ATOM   6141  C  CD    . GLN B  2  344 ? 50.822 -12.675 14.099  1.00 64.24  ?  376 GLN B CD    1 
ATOM   6142  O  OE1   . GLN B  2  344 ? 50.515 -13.286 15.127  1.00 70.40  ?  376 GLN B OE1   1 
ATOM   6143  N  NE2   . GLN B  2  344 ? 50.478 -11.411 13.883  1.00 70.58  ?  376 GLN B NE2   1 
ATOM   6144  N  N     . THR B  2  345 ? 53.508 -17.125 14.404  1.00 39.47  ?  377 THR B N     1 
ATOM   6145  C  CA    . THR B  2  345 ? 53.410 -18.521 14.872  1.00 38.61  ?  377 THR B CA    1 
ATOM   6146  C  C     . THR B  2  345 ? 54.470 -18.919 15.880  1.00 38.78  ?  377 THR B C     1 
ATOM   6147  O  O     . THR B  2  345 ? 54.338 -19.958 16.539  1.00 37.27  ?  377 THR B O     1 
ATOM   6148  C  CB    . THR B  2  345 ? 53.523 -19.535 13.727  1.00 37.07  ?  377 THR B CB    1 
ATOM   6149  O  OG1   . THR B  2  345 ? 54.645 -19.186 12.917  1.00 36.30  ?  377 THR B OG1   1 
ATOM   6150  C  CG2   . THR B  2  345 ? 52.259 -19.540 12.897  1.00 38.61  ?  377 THR B CG2   1 
ATOM   6151  N  N     . TYR B  2  346 ? 55.536 -18.138 15.973  1.00 39.43  ?  378 TYR B N     1 
ATOM   6152  C  CA    . TYR B  2  346 ? 56.552 -18.408 16.975  1.00 41.64  ?  378 TYR B CA    1 
ATOM   6153  C  C     . TYR B  2  346 ? 56.493 -17.443 18.149  1.00 43.18  ?  378 TYR B C     1 
ATOM   6154  O  O     . TYR B  2  346 ? 57.029 -17.726 19.227  1.00 43.93  ?  378 TYR B O     1 
ATOM   6155  C  CB    . TYR B  2  346 ? 57.930 -18.413 16.325  1.00 41.60  ?  378 TYR B CB    1 
ATOM   6156  C  CG    . TYR B  2  346 ? 58.095 -19.560 15.356  1.00 41.24  ?  378 TYR B CG    1 
ATOM   6157  C  CD1   . TYR B  2  346 ? 57.931 -20.884 15.776  1.00 40.55  ?  378 TYR B CD1   1 
ATOM   6158  C  CD2   . TYR B  2  346 ? 58.412 -19.326 14.018  1.00 42.09  ?  378 TYR B CD2   1 
ATOM   6159  C  CE1   . TYR B  2  346 ? 58.078 -21.943 14.886  1.00 42.16  ?  378 TYR B CE1   1 
ATOM   6160  C  CE2   . TYR B  2  346 ? 58.570 -20.376 13.116  1.00 42.53  ?  378 TYR B CE2   1 
ATOM   6161  C  CZ    . TYR B  2  346 ? 58.399 -21.683 13.546  1.00 42.02  ?  378 TYR B CZ    1 
ATOM   6162  O  OH    . TYR B  2  346 ? 58.559 -22.714 12.647  1.00 37.12  ?  378 TYR B OH    1 
ATOM   6163  N  N     . ASP B  2  347 ? 55.822 -16.318 17.939  1.00 44.90  ?  379 ASP B N     1 
ATOM   6164  C  CA    . ASP B  2  347 ? 55.727 -15.266 18.941  1.00 47.78  ?  379 ASP B CA    1 
ATOM   6165  C  C     . ASP B  2  347 ? 57.108 -14.739 19.383  1.00 47.23  ?  379 ASP B C     1 
ATOM   6166  O  O     . ASP B  2  347 ? 57.467 -14.781 20.555  1.00 48.67  ?  379 ASP B O     1 
ATOM   6167  C  CB    . ASP B  2  347 ? 54.875 -15.722 20.120  1.00 48.54  ?  379 ASP B CB    1 
ATOM   6168  C  CG    . ASP B  2  347 ? 54.010 -14.615 20.639  1.00 51.77  ?  379 ASP B CG    1 
ATOM   6169  O  OD1   . ASP B  2  347 ? 54.565 -13.684 21.253  1.00 53.67  ?  379 ASP B OD1   1 
ATOM   6170  O  OD2   . ASP B  2  347 ? 52.784 -14.657 20.402  1.00 56.79  -1 379 ASP B OD2   1 
ATOM   6171  N  N     . ILE B  2  348 ? 57.857 -14.241 18.402  1.00 45.64  ?  380 ILE B N     1 
ATOM   6172  C  CA    . ILE B  2  348 ? 59.148 -13.616 18.613  1.00 44.53  ?  380 ILE B CA    1 
ATOM   6173  C  C     . ILE B  2  348 ? 59.082 -12.234 17.962  1.00 46.36  ?  380 ILE B C     1 
ATOM   6174  O  O     . ILE B  2  348 ? 58.186 -11.987 17.156  1.00 43.83  ?  380 ILE B O     1 
ATOM   6175  C  CB    . ILE B  2  348 ? 60.283 -14.492 18.051  1.00 44.11  ?  380 ILE B CB    1 
ATOM   6176  C  CG1   . ILE B  2  348 ? 60.084 -14.767 16.557  1.00 45.79  ?  380 ILE B CG1   1 
ATOM   6177  C  CG2   . ILE B  2  348 ? 60.325 -15.815 18.798  1.00 43.23  ?  380 ILE B CG2   1 
ATOM   6178  C  CD1   . ILE B  2  348 ? 61.283 -15.400 15.878  1.00 45.57  ?  380 ILE B CD1   1 
ATOM   6179  N  N     . GLU B  2  349 ? 60.003 -11.341 18.331  1.00 51.37  ?  381 GLU B N     1 
ATOM   6180  C  CA    . GLU B  2  349 ? 59.910 -9.902  17.981  1.00 54.60  ?  381 GLU B CA    1 
ATOM   6181  C  C     . GLU B  2  349 ? 60.095 -9.605  16.492  1.00 54.10  ?  381 GLU B C     1 
ATOM   6182  O  O     . GLU B  2  349 ? 59.279 -8.914  15.874  1.00 51.55  ?  381 GLU B O     1 
ATOM   6183  C  CB    . GLU B  2  349 ? 60.947 -9.075  18.766  1.00 59.11  ?  381 GLU B CB    1 
ATOM   6184  C  CG    . GLU B  2  349 ? 60.687 -8.935  20.259  1.00 66.29  ?  381 GLU B CG    1 
ATOM   6185  C  CD    . GLU B  2  349 ? 59.237 -8.591  20.575  1.00 74.26  ?  381 GLU B CD    1 
ATOM   6186  O  OE1   . GLU B  2  349 ? 58.732 -7.583  20.032  1.00 81.32  ?  381 GLU B OE1   1 
ATOM   6187  O  OE2   . GLU B  2  349 ? 58.596 -9.335  21.354  1.00 77.22  -1 381 GLU B OE2   1 
ATOM   6188  N  N     . ASP B  2  350 ? 61.190 -10.125 15.940  1.00 53.13  ?  382 ASP B N     1 
ATOM   6189  C  CA    . ASP B  2  350 ? 61.613 -9.850  14.570  1.00 47.99  ?  382 ASP B CA    1 
ATOM   6190  C  C     . ASP B  2  350 ? 62.418 -11.051 14.040  1.00 45.04  ?  382 ASP B C     1 
ATOM   6191  O  O     . ASP B  2  350 ? 62.262 -12.168 14.538  1.00 44.25  ?  382 ASP B O     1 
ATOM   6192  C  CB    . ASP B  2  350 ? 62.430 -8.547  14.548  1.00 48.71  ?  382 ASP B CB    1 
ATOM   6193  C  CG    . ASP B  2  350 ? 63.624 -8.567  15.514  1.00 48.25  ?  382 ASP B CG    1 
ATOM   6194  O  OD1   . ASP B  2  350 ? 64.061 -9.656  15.934  1.00 48.84  ?  382 ASP B OD1   1 
ATOM   6195  O  OD2   . ASP B  2  350 ? 64.138 -7.483  15.850  1.00 48.52  -1 382 ASP B OD2   1 
ATOM   6196  N  N     . LEU B  2  351 ? 63.265 -10.827 13.038  1.00 41.93  ?  383 LEU B N     1 
ATOM   6197  C  CA    . LEU B  2  351 ? 64.110 -11.864 12.503  1.00 39.95  ?  383 LEU B CA    1 
ATOM   6198  C  C     . LEU B  2  351 ? 65.550 -11.507 12.766  1.00 42.41  ?  383 LEU B C     1 
ATOM   6199  O  O     . LEU B  2  351 ? 66.410 -11.749 11.936  1.00 48.57  ?  383 LEU B O     1 
ATOM   6200  C  CB    . LEU B  2  351 ? 63.848 -12.035 11.001  1.00 39.77  ?  383 LEU B CB    1 
ATOM   6201  C  CG    . LEU B  2  351 ? 62.834 -13.112 10.617  1.00 38.55  ?  383 LEU B CG    1 
ATOM   6202  C  CD1   . LEU B  2  351 ? 61.570 -12.979 11.440  1.00 39.30  ?  383 LEU B CD1   1 
ATOM   6203  C  CD2   . LEU B  2  351 ? 62.508 -13.036 9.148   1.00 38.21  ?  383 LEU B CD2   1 
ATOM   6204  N  N     . GLN B  2  352 ? 65.836 -10.941 13.930  1.00 45.24  ?  384 GLN B N     1 
ATOM   6205  C  CA    . GLN B  2  352 ? 67.224 -10.694 14.320  1.00 47.03  ?  384 GLN B CA    1 
ATOM   6206  C  C     . GLN B  2  352 ? 67.896 -12.013 14.669  1.00 44.54  ?  384 GLN B C     1 
ATOM   6207  O  O     . GLN B  2  352 ? 67.219 -13.019 14.815  1.00 43.45  ?  384 GLN B O     1 
ATOM   6208  C  CB    . GLN B  2  352 ? 67.272 -9.748  15.511  1.00 51.73  ?  384 GLN B CB    1 
ATOM   6209  C  CG    . GLN B  2  352 ? 67.004 -8.307  15.115  1.00 53.94  ?  384 GLN B CG    1 
ATOM   6210  C  CD    . GLN B  2  352 ? 68.255 -7.642  14.605  1.00 54.29  ?  384 GLN B CD    1 
ATOM   6211  O  OE1   . GLN B  2  352 ? 68.376 -7.364  13.419  1.00 53.53  ?  384 GLN B OE1   1 
ATOM   6212  N  NE2   . GLN B  2  352 ? 69.217 -7.424  15.502  1.00 55.98  ?  384 GLN B NE2   1 
ATOM   6213  N  N     . PRO B  2  353 ? 69.230 -12.028 14.771  1.00 45.11  ?  385 PRO B N     1 
ATOM   6214  C  CA    . PRO B  2  353 ? 69.895 -13.270 15.174  1.00 46.68  ?  385 PRO B CA    1 
ATOM   6215  C  C     . PRO B  2  353 ? 69.568 -13.693 16.608  1.00 48.99  ?  385 PRO B C     1 
ATOM   6216  O  O     . PRO B  2  353 ? 69.456 -14.908 16.879  1.00 49.63  ?  385 PRO B O     1 
ATOM   6217  C  CB    . PRO B  2  353 ? 71.389 -12.944 15.039  1.00 45.93  ?  385 PRO B CB    1 
ATOM   6218  C  CG    . PRO B  2  353 ? 71.446 -11.816 14.068  1.00 46.61  ?  385 PRO B CG    1 
ATOM   6219  C  CD    . PRO B  2  353 ? 70.189 -11.020 14.295  1.00 47.04  ?  385 PRO B CD    1 
ATOM   6220  N  N     . GLU B  2  354 ? 69.411 -12.712 17.505  1.00 48.44  ?  386 GLU B N     1 
ATOM   6221  C  CA    . GLU B  2  354 ? 69.095 -13.003 18.907  1.00 50.46  ?  386 GLU B CA    1 
ATOM   6222  C  C     . GLU B  2  354 ? 67.659 -13.569 18.954  1.00 46.62  ?  386 GLU B C     1 
ATOM   6223  O  O     . GLU B  2  354 ? 67.427 -14.632 19.543  1.00 46.18  ?  386 GLU B O     1 
ATOM   6224  C  CB    . GLU B  2  354 ? 69.280 -11.778 19.844  1.00 57.13  ?  386 GLU B CB    1 
ATOM   6225  C  CG    . GLU B  2  354 ? 70.580 -10.960 19.680  1.00 64.00  ?  386 GLU B CG    1 
ATOM   6226  C  CD    . GLU B  2  354 ? 70.447 -9.769  18.702  1.00 73.40  ?  386 GLU B CD    1 
ATOM   6227  O  OE1   . GLU B  2  354 ? 69.519 -8.931  18.877  1.00 79.77  ?  386 GLU B OE1   1 
ATOM   6228  O  OE2   . GLU B  2  354 ? 71.268 -9.663  17.750  1.00 70.35  -1 386 GLU B OE2   1 
ATOM   6229  N  N     . SER B  2  355 ? 66.717 -12.901 18.284  1.00 42.56  ?  387 SER B N     1 
ATOM   6230  C  CA    . SER B  2  355 ? 65.313 -13.366 18.227  1.00 40.86  ?  387 SER B CA    1 
ATOM   6231  C  C     . SER B  2  355 ? 65.122 -14.833 17.833  1.00 40.27  ?  387 SER B C     1 
ATOM   6232  O  O     . SER B  2  355 ? 64.282 -15.524 18.403  1.00 44.04  ?  387 SER B O     1 
ATOM   6233  C  CB    . SER B  2  355 ? 64.495 -12.506 17.265  1.00 39.34  ?  387 SER B CB    1 
ATOM   6234  O  OG    . SER B  2  355 ? 64.181 -11.269 17.858  1.00 38.57  ?  387 SER B OG    1 
ATOM   6235  N  N     . LEU B  2  356 ? 65.890 -15.286 16.849  1.00 40.42  ?  388 LEU B N     1 
ATOM   6236  C  CA    . LEU B  2  356 ? 65.803 -16.656 16.323  1.00 40.07  ?  388 LEU B CA    1 
ATOM   6237  C  C     . LEU B  2  356 ? 66.654 -17.653 17.097  1.00 40.42  ?  388 LEU B C     1 
ATOM   6238  O  O     . LEU B  2  356 ? 66.330 -18.850 17.105  1.00 37.92  ?  388 LEU B O     1 
ATOM   6239  C  CB    . LEU B  2  356 ? 66.252 -16.705 14.859  1.00 38.54  ?  388 LEU B CB    1 
ATOM   6240  C  CG    . LEU B  2  356 ? 65.476 -15.892 13.844  1.00 36.84  ?  388 LEU B CG    1 
ATOM   6241  C  CD1   . LEU B  2  356 ? 66.081 -16.133 12.473  1.00 37.03  ?  388 LEU B CD1   1 
ATOM   6242  C  CD2   . LEU B  2  356 ? 64.009 -16.282 13.880  1.00 36.92  ?  388 LEU B CD2   1 
ATOM   6243  N  N     . TYR B  2  357 ? 67.762 -17.182 17.687  1.00 40.87  ?  389 TYR B N     1 
ATOM   6244  C  CA    . TYR B  2  357 ? 68.543 -18.030 18.582  1.00 41.56  ?  389 TYR B CA    1 
ATOM   6245  C  C     . TYR B  2  357 ? 67.648 -18.442 19.723  1.00 40.28  ?  389 TYR B C     1 
ATOM   6246  O  O     . TYR B  2  357 ? 67.552 -19.635 20.060  1.00 38.94  ?  389 TYR B O     1 
ATOM   6247  C  CB    . TYR B  2  357 ? 69.759 -17.316 19.155  1.00 43.08  ?  389 TYR B CB    1 
ATOM   6248  C  CG    . TYR B  2  357 ? 70.724 -18.295 19.794  1.00 46.00  ?  389 TYR B CG    1 
ATOM   6249  C  CD1   . TYR B  2  357 ? 71.349 -19.267 19.007  1.00 47.45  ?  389 TYR B CD1   1 
ATOM   6250  C  CD2   . TYR B  2  357 ? 71.004 -18.269 21.170  1.00 45.84  ?  389 TYR B CD2   1 
ATOM   6251  C  CE1   . TYR B  2  357 ? 72.222 -20.181 19.555  1.00 49.74  ?  389 TYR B CE1   1 
ATOM   6252  C  CE2   . TYR B  2  357 ? 71.889 -19.182 21.726  1.00 47.60  ?  389 TYR B CE2   1 
ATOM   6253  C  CZ    . TYR B  2  357 ? 72.493 -20.136 20.900  1.00 49.96  ?  389 TYR B CZ    1 
ATOM   6254  O  OH    . TYR B  2  357 ? 73.372 -21.079 21.364  1.00 51.73  ?  389 TYR B OH    1 
ATOM   6255  N  N     . GLY B  2  358 ? 66.985 -17.431 20.288  1.00 37.69  ?  390 GLY B N     1 
ATOM   6256  C  CA    . GLY B  2  358 ? 66.013 -17.605 21.364  1.00 38.03  ?  390 GLY B CA    1 
ATOM   6257  C  C     . GLY B  2  358 ? 64.899 -18.597 21.088  1.00 37.09  ?  390 GLY B C     1 
ATOM   6258  O  O     . GLY B  2  358 ? 64.475 -19.339 21.996  1.00 37.16  ?  390 GLY B O     1 
ATOM   6259  N  N     . LEU B  2  359 ? 64.425 -18.596 19.841  1.00 34.72  ?  391 LEU B N     1 
ATOM   6260  C  CA    . LEU B  2  359 ? 63.477 -19.596 19.370  1.00 33.13  ?  391 LEU B CA    1 
ATOM   6261  C  C     . LEU B  2  359 ? 64.093 -21.030 19.301  1.00 33.80  ?  391 LEU B C     1 
ATOM   6262  O  O     . LEU B  2  359 ? 63.479 -21.984 19.777  1.00 32.76  ?  391 LEU B O     1 
ATOM   6263  C  CB    . LEU B  2  359 ? 62.891 -19.149 18.033  1.00 31.16  ?  391 LEU B CB    1 
ATOM   6264  C  CG    . LEU B  2  359 ? 61.756 -19.985 17.444  1.00 31.45  ?  391 LEU B CG    1 
ATOM   6265  C  CD1   . LEU B  2  359 ? 60.495 -19.981 18.298  1.00 30.80  ?  391 LEU B CD1   1 
ATOM   6266  C  CD2   . LEU B  2  359 ? 61.440 -19.476 16.047  1.00 32.85  ?  391 LEU B CD2   1 
ATOM   6267  N  N     . ALA B  2  360 ? 65.307 -21.175 18.753  1.00 35.63  ?  392 ALA B N     1 
ATOM   6268  C  CA    . ALA B  2  360 ? 65.999 -22.499 18.648  1.00 35.75  ?  392 ALA B CA    1 
ATOM   6269  C  C     . ALA B  2  360 ? 66.140 -23.232 20.002  1.00 36.33  ?  392 ALA B C     1 
ATOM   6270  O  O     . ALA B  2  360 ? 66.115 -24.479 20.078  1.00 32.44  ?  392 ALA B O     1 
ATOM   6271  C  CB    . ALA B  2  360 ? 67.379 -22.315 18.036  1.00 35.25  ?  392 ALA B CB    1 
ATOM   6272  N  N     . LYS B  2  361 ? 66.304 -22.421 21.052  1.00 35.27  ?  393 LYS B N     1 
ATOM   6273  C  CA    . LYS B  2  361 ? 66.397 -22.881 22.421  1.00 31.90  ?  393 LYS B CA    1 
ATOM   6274  C  C     . LYS B  2  361 ? 65.043 -23.410 22.864  1.00 30.88  ?  393 LYS B C     1 
ATOM   6275  O  O     . LYS B  2  361 ? 64.963 -24.457 23.487  1.00 29.65  ?  393 LYS B O     1 
ATOM   6276  C  CB    . LYS B  2  361 ? 66.908 -21.740 23.287  1.00 31.37  ?  393 LYS B CB    1 
ATOM   6277  C  CG    . LYS B  2  361 ? 68.296 -21.296 22.838  1.00 32.88  ?  393 LYS B CG    1 
ATOM   6278  C  CD    . LYS B  2  361 ? 69.423 -21.844 23.713  1.00 35.71  ?  393 LYS B CD    1 
ATOM   6279  C  CE    . LYS B  2  361 ? 70.151 -20.749 24.497  1.00 37.87  ?  393 LYS B CE    1 
ATOM   6280  N  NZ    . LYS B  2  361 ? 69.315 -19.551 24.855  1.00 39.09  1  393 LYS B NZ    1 
ATOM   6281  N  N     . GLN B  2  362 ? 63.970 -22.730 22.491  1.00 31.56  ?  394 GLN B N     1 
ATOM   6282  C  CA    . GLN B  2  362 ? 62.631 -23.211 22.826  1.00 33.81  ?  394 GLN B CA    1 
ATOM   6283  C  C     . GLN B  2  362 ? 62.325 -24.547 22.179  1.00 33.51  ?  394 GLN B C     1 
ATOM   6284  O  O     . GLN B  2  362 ? 61.547 -25.330 22.687  1.00 34.68  ?  394 GLN B O     1 
ATOM   6285  C  CB    . GLN B  2  362 ? 61.553 -22.217 22.402  1.00 37.37  ?  394 GLN B CB    1 
ATOM   6286  C  CG    . GLN B  2  362 ? 61.541 -20.871 23.130  1.00 39.59  ?  394 GLN B CG    1 
ATOM   6287  C  CD    . GLN B  2  362 ? 60.425 -19.969 22.610  1.00 42.56  ?  394 GLN B CD    1 
ATOM   6288  O  OE1   . GLN B  2  362 ? 60.675 -18.888 22.060  1.00 41.80  ?  394 GLN B OE1   1 
ATOM   6289  N  NE2   . GLN B  2  362 ? 59.175 -20.431 22.756  1.00 46.23  ?  394 GLN B NE2   1 
ATOM   6290  N  N     . PHE B  2  363 ? 62.915 -24.811 21.035  1.00 34.97  ?  395 PHE B N     1 
ATOM   6291  C  CA    . PHE B  2  363 ? 62.735 -26.117 20.428  1.00 37.02  ?  395 PHE B CA    1 
ATOM   6292  C  C     . PHE B  2  363 ? 63.364 -27.212 21.281  1.00 38.51  ?  395 PHE B C     1 
ATOM   6293  O  O     . PHE B  2  363 ? 62.848 -28.316 21.335  1.00 37.03  ?  395 PHE B O     1 
ATOM   6294  C  CB    . PHE B  2  363 ? 63.350 -26.170 19.027  1.00 38.73  ?  395 PHE B CB    1 
ATOM   6295  C  CG    . PHE B  2  363 ? 62.714 -25.241 18.021  1.00 40.07  ?  395 PHE B CG    1 
ATOM   6296  C  CD1   . PHE B  2  363 ? 61.511 -24.570 18.273  1.00 38.51  ?  395 PHE B CD1   1 
ATOM   6297  C  CD2   . PHE B  2  363 ? 63.326 -25.069 16.786  1.00 43.84  ?  395 PHE B CD2   1 
ATOM   6298  C  CE1   . PHE B  2  363 ? 60.963 -23.726 17.331  1.00 39.22  ?  395 PHE B CE1   1 
ATOM   6299  C  CE2   . PHE B  2  363 ? 62.785 -24.220 15.834  1.00 45.82  ?  395 PHE B CE2   1 
ATOM   6300  C  CZ    . PHE B  2  363 ? 61.599 -23.546 16.113  1.00 44.27  ?  395 PHE B CZ    1 
ATOM   6301  N  N     . THR B  2  364 ? 64.477 -26.892 21.945  1.00 41.28  ?  396 THR B N     1 
ATOM   6302  C  CA    . THR B  2  364 ? 65.228 -27.839 22.800  1.00 40.24  ?  396 THR B CA    1 
ATOM   6303  C  C     . THR B  2  364 ? 64.453 -28.327 24.067  1.00 45.01  ?  396 THR B C     1 
ATOM   6304  O  O     . THR B  2  364 ? 64.828 -29.331 24.731  1.00 45.23  ?  396 THR B O     1 
ATOM   6305  C  CB    . THR B  2  364 ? 66.551 -27.195 23.247  1.00 37.95  ?  396 THR B CB    1 
ATOM   6306  O  OG1   . THR B  2  364 ? 66.297 -26.177 24.222  1.00 34.83  ?  396 THR B OG1   1 
ATOM   6307  C  CG2   . THR B  2  364 ? 67.254 -26.576 22.067  1.00 38.60  ?  396 THR B CG2   1 
ATOM   6308  N  N     . ILE B  2  365 ? 63.386 -27.595 24.404  1.00 45.72  ?  397 ILE B N     1 
ATOM   6309  C  CA    . ILE B  2  365 ? 62.461 -27.973 25.470  1.00 43.91  ?  397 ILE B CA    1 
ATOM   6310  C  C     . ILE B  2  365 ? 61.950 -29.421 25.220  1.00 47.36  ?  397 ILE B C     1 
ATOM   6311  O  O     . ILE B  2  365 ? 61.515 -29.738 24.111  1.00 49.76  ?  397 ILE B O     1 
ATOM   6312  C  CB    . ILE B  2  365 ? 61.266 -26.982 25.501  1.00 40.43  ?  397 ILE B CB    1 
ATOM   6313  C  CG1   . ILE B  2  365 ? 61.698 -25.564 25.874  1.00 38.62  ?  397 ILE B CG1   1 
ATOM   6314  C  CG2   . ILE B  2  365 ? 60.186 -27.446 26.459  1.00 40.35  ?  397 ILE B CG2   1 
ATOM   6315  C  CD1   . ILE B  2  365 ? 60.631 -24.528 25.544  1.00 39.60  ?  397 ILE B CD1   1 
ATOM   6316  N  N     . LEU B  2  366 ? 61.997 -30.301 26.223  1.00 47.65  ?  398 LEU B N     1 
ATOM   6317  C  CA    . LEU B  2  366 ? 61.370 -31.630 26.076  1.00 45.39  ?  398 LEU B CA    1 
ATOM   6318  C  C     . LEU B  2  366 ? 59.936 -31.426 25.535  1.00 43.35  ?  398 LEU B C     1 
ATOM   6319  O  O     . LEU B  2  366 ? 59.156 -30.621 26.054  1.00 38.47  ?  398 LEU B O     1 
ATOM   6320  C  CB    . LEU B  2  366 ? 61.353 -32.410 27.414  1.00 48.29  ?  398 LEU B CB    1 
ATOM   6321  C  CG    . LEU B  2  366 ? 62.597 -33.030 28.116  1.00 47.54  ?  398 LEU B CG    1 
ATOM   6322  C  CD1   . LEU B  2  366 ? 63.952 -32.405 27.748  1.00 46.79  ?  398 LEU B CD1   1 
ATOM   6323  C  CD2   . LEU B  2  366 ? 62.376 -33.008 29.638  1.00 45.89  ?  398 LEU B CD2   1 
ATOM   6324  N  N     . ASP B  2  367 ? 59.610 -32.131 24.462  1.00 46.14  ?  399 ASP B N     1 
ATOM   6325  C  CA    . ASP B  2  367 ? 58.273 -32.063 23.840  1.00 47.41  ?  399 ASP B CA    1 
ATOM   6326  C  C     . ASP B  2  367 ? 57.831 -30.647 23.413  1.00 42.72  ?  399 ASP B C     1 
ATOM   6327  O  O     . ASP B  2  367 ? 56.637 -30.354 23.429  1.00 40.02  ?  399 ASP B O     1 
ATOM   6328  C  CB    . ASP B  2  367 ? 57.203 -32.695 24.775  1.00 51.05  ?  399 ASP B CB    1 
ATOM   6329  C  CG    . ASP B  2  367 ? 56.946 -34.191 24.497  1.00 53.10  ?  399 ASP B CG    1 
ATOM   6330  O  OD1   . ASP B  2  367 ? 57.010 -34.629 23.318  1.00 50.68  ?  399 ASP B OD1   1 
ATOM   6331  O  OD2   . ASP B  2  367 ? 56.627 -34.913 25.481  1.00 54.80  -1 399 ASP B OD2   1 
ATOM   6332  N  N     . SER B  2  368 ? 58.779 -29.797 23.007  1.00 40.84  ?  400 SER B N     1 
ATOM   6333  C  CA    . SER B  2  368 ? 58.474 -28.417 22.515  1.00 41.60  ?  400 SER B CA    1 
ATOM   6334  C  C     . SER B  2  368 ? 57.408 -28.351 21.416  1.00 43.85  ?  400 SER B C     1 
ATOM   6335  O  O     . SER B  2  368 ? 57.622 -28.834 20.308  1.00 44.52  ?  400 SER B O     1 
ATOM   6336  C  CB    . SER B  2  368 ? 59.728 -27.702 21.974  1.00 37.93  ?  400 SER B CB    1 
ATOM   6337  O  OG    . SER B  2  368 ? 59.426 -26.378 21.579  1.00 32.96  ?  400 SER B OG    1 
ATOM   6338  N  N     . LYS B  2  369 ? 56.280 -27.722 21.744  1.00 46.23  ?  401 LYS B N     1 
ATOM   6339  C  CA    . LYS B  2  369 ? 55.191 -27.456 20.804  1.00 45.95  ?  401 LYS B CA    1 
ATOM   6340  C  C     . LYS B  2  369 ? 55.688 -26.519 19.702  1.00 42.66  ?  401 LYS B C     1 
ATOM   6341  O  O     . LYS B  2  369 ? 55.124 -26.481 18.610  1.00 42.41  ?  401 LYS B O     1 
ATOM   6342  C  CB    . LYS B  2  369 ? 53.987 -26.813 21.537  1.00 49.56  ?  401 LYS B CB    1 
ATOM   6343  C  CG    . LYS B  2  369 ? 52.975 -27.771 22.172  1.00 54.62  ?  401 LYS B CG    1 
ATOM   6344  C  CD    . LYS B  2  369 ? 53.572 -28.740 23.201  1.00 60.67  ?  401 LYS B CD    1 
ATOM   6345  C  CE    . LYS B  2  369 ? 53.059 -30.177 23.005  1.00 65.07  ?  401 LYS B CE    1 
ATOM   6346  N  NZ    . LYS B  2  369 ? 54.003 -31.224 23.511  1.00 64.68  1  401 LYS B NZ    1 
ATOM   6347  N  N     . GLN B  2  370 ? 56.739 -25.755 20.002  1.00 40.94  ?  402 GLN B N     1 
ATOM   6348  C  CA    . GLN B  2  370 ? 57.355 -24.854 19.023  1.00 41.36  ?  402 GLN B CA    1 
ATOM   6349  C  C     . GLN B  2  370 ? 58.065 -25.625 17.898  1.00 41.74  ?  402 GLN B C     1 
ATOM   6350  O  O     . GLN B  2  370 ? 57.791 -25.372 16.720  1.00 45.46  ?  402 GLN B O     1 
ATOM   6351  C  CB    . GLN B  2  370 ? 58.344 -23.892 19.707  1.00 41.50  ?  402 GLN B CB    1 
ATOM   6352  C  CG    . GLN B  2  370 ? 57.721 -22.835 20.616  1.00 40.61  ?  402 GLN B CG    1 
ATOM   6353  C  CD    . GLN B  2  370 ? 56.980 -21.751 19.834  1.00 40.02  ?  402 GLN B CD    1 
ATOM   6354  O  OE1   . GLN B  2  370 ? 55.894 -21.989 19.266  1.00 39.54  ?  402 GLN B OE1   1 
ATOM   6355  N  NE2   . GLN B  2  370 ? 57.560 -20.551 19.800  1.00 38.67  ?  402 GLN B NE2   1 
ATOM   6356  N  N     . PHE B  2  371 ? 58.955 -26.560 18.268  1.00 37.87  ?  403 PHE B N     1 
ATOM   6357  C  CA    . PHE B  2  371 ? 59.652 -27.436 17.317  1.00 33.44  ?  403 PHE B CA    1 
ATOM   6358  C  C     . PHE B  2  371 ? 58.695 -28.300 16.540  1.00 34.83  ?  403 PHE B C     1 
ATOM   6359  O  O     . PHE B  2  371 ? 58.989 -28.658 15.394  1.00 38.96  ?  403 PHE B O     1 
ATOM   6360  C  CB    . PHE B  2  371 ? 60.642 -28.362 18.021  1.00 32.98  ?  403 PHE B CB    1 
ATOM   6361  C  CG    . PHE B  2  371 ? 61.345 -29.320 17.092  1.00 31.58  ?  403 PHE B CG    1 
ATOM   6362  C  CD1   . PHE B  2  371 ? 62.418 -28.887 16.307  1.00 30.65  ?  403 PHE B CD1   1 
ATOM   6363  C  CD2   . PHE B  2  371 ? 60.914 -30.653 16.989  1.00 30.17  ?  403 PHE B CD2   1 
ATOM   6364  C  CE1   . PHE B  2  371 ? 63.039 -29.769 15.440  1.00 30.40  ?  403 PHE B CE1   1 
ATOM   6365  C  CE2   . PHE B  2  371 ? 61.524 -31.527 16.128  1.00 29.14  ?  403 PHE B CE2   1 
ATOM   6366  C  CZ    . PHE B  2  371 ? 62.585 -31.086 15.349  1.00 30.24  ?  403 PHE B CZ    1 
ATOM   6367  N  N     . ILE B  2  372 ? 57.564 -28.660 17.141  1.00 35.51  ?  404 ILE B N     1 
ATOM   6368  C  CA    . ILE B  2  372 ? 56.568 -29.447 16.403  1.00 37.62  ?  404 ILE B CA    1 
ATOM   6369  C  C     . ILE B  2  372 ? 56.086 -28.611 15.214  1.00 35.66  ?  404 ILE B C     1 
ATOM   6370  O  O     . ILE B  2  372 ? 55.973 -29.143 14.109  1.00 33.81  ?  404 ILE B O     1 
ATOM   6371  C  CB    . ILE B  2  372 ? 55.332 -29.925 17.231  1.00 40.64  ?  404 ILE B CB    1 
ATOM   6372  C  CG1   . ILE B  2  372 ? 55.707 -30.510 18.625  1.00 41.37  ?  404 ILE B CG1   1 
ATOM   6373  C  CG2   . ILE B  2  372 ? 54.507 -30.933 16.413  1.00 41.09  ?  404 ILE B CG2   1 
ATOM   6374  C  CD1   . ILE B  2  372 ? 56.302 -31.905 18.651  1.00 40.91  ?  404 ILE B CD1   1 
ATOM   6375  N  N     . LYS B  2  373 ? 55.824 -27.313 15.432  1.00 35.31  ?  405 LYS B N     1 
ATOM   6376  C  CA    . LYS B  2  373 ? 55.430 -26.405 14.324  1.00 36.34  ?  405 LYS B CA    1 
ATOM   6377  C  C     . LYS B  2  373 ? 56.509 -26.361 13.243  1.00 32.21  ?  405 LYS B C     1 
ATOM   6378  O  O     . LYS B  2  373 ? 56.242 -26.598 12.046  1.00 28.36  ?  405 LYS B O     1 
ATOM   6379  C  CB    . LYS B  2  373 ? 55.207 -24.973 14.814  1.00 39.08  ?  405 LYS B CB    1 
ATOM   6380  C  CG    . LYS B  2  373 ? 53.931 -24.740 15.577  1.00 42.98  ?  405 LYS B CG    1 
ATOM   6381  C  CD    . LYS B  2  373 ? 53.727 -23.249 15.771  1.00 47.58  ?  405 LYS B CD    1 
ATOM   6382  C  CE    . LYS B  2  373 ? 52.748 -22.974 16.902  1.00 51.55  ?  405 LYS B CE    1 
ATOM   6383  N  NZ    . LYS B  2  373 ? 51.970 -21.741 16.609  1.00 53.38  1  405 LYS B NZ    1 
ATOM   6384  N  N     . TYR B  2  374 ? 57.721 -26.046 13.705  1.00 27.90  ?  406 TYR B N     1 
ATOM   6385  C  CA    . TYR B  2  374 ? 58.877 -25.985 12.862  1.00 26.15  ?  406 TYR B CA    1 
ATOM   6386  C  C     . TYR B  2  374 ? 58.947 -27.206 11.982  1.00 27.32  ?  406 TYR B C     1 
ATOM   6387  O  O     . TYR B  2  374 ? 59.217 -27.105 10.776  1.00 27.06  ?  406 TYR B O     1 
ATOM   6388  C  CB    . TYR B  2  374 ? 60.139 -25.902 13.697  1.00 24.63  ?  406 TYR B CB    1 
ATOM   6389  C  CG    . TYR B  2  374 ? 61.398 -25.693 12.874  1.00 23.96  ?  406 TYR B CG    1 
ATOM   6390  C  CD1   . TYR B  2  374 ? 61.795 -24.423 12.492  1.00 24.12  ?  406 TYR B CD1   1 
ATOM   6391  C  CD2   . TYR B  2  374 ? 62.191 -26.764 12.473  1.00 22.96  ?  406 TYR B CD2   1 
ATOM   6392  C  CE1   . TYR B  2  374 ? 62.932 -24.231 11.736  1.00 23.47  ?  406 TYR B CE1   1 
ATOM   6393  C  CE2   . TYR B  2  374 ? 63.334 -26.566 11.722  1.00 21.63  ?  406 TYR B CE2   1 
ATOM   6394  C  CZ    . TYR B  2  374 ? 63.686 -25.297 11.358  1.00 21.59  ?  406 TYR B CZ    1 
ATOM   6395  O  OH    . TYR B  2  374 ? 64.795 -25.060 10.622  1.00 20.06  ?  406 TYR B OH    1 
ATOM   6396  N  N     . TYR B  2  375 ? 58.699 -28.366 12.571  1.00 28.21  ?  407 TYR B N     1 
ATOM   6397  C  CA    . TYR B  2  375 ? 58.859 -29.603 11.829  1.00 30.59  ?  407 TYR B CA    1 
ATOM   6398  C  C     . TYR B  2  375 ? 57.697 -29.899 10.873  1.00 34.85  ?  407 TYR B C     1 
ATOM   6399  O  O     . TYR B  2  375 ? 57.877 -30.624 9.897   1.00 36.70  ?  407 TYR B O     1 
ATOM   6400  C  CB    . TYR B  2  375 ? 59.088 -30.756 12.788  1.00 30.24  ?  407 TYR B CB    1 
ATOM   6401  C  CG    . TYR B  2  375 ? 59.744 -31.954 12.144  1.00 30.04  ?  407 TYR B CG    1 
ATOM   6402  C  CD1   . TYR B  2  375 ? 61.084 -31.939 11.802  1.00 30.59  ?  407 TYR B CD1   1 
ATOM   6403  C  CD2   . TYR B  2  375 ? 59.028 -33.110 11.897  1.00 30.20  ?  407 TYR B CD2   1 
ATOM   6404  C  CE1   . TYR B  2  375 ? 61.677 -33.047 11.207  1.00 31.05  ?  407 TYR B CE1   1 
ATOM   6405  C  CE2   . TYR B  2  375 ? 59.621 -34.220 11.329  1.00 30.27  ?  407 TYR B CE2   1 
ATOM   6406  C  CZ    . TYR B  2  375 ? 60.938 -34.184 10.983  1.00 30.03  ?  407 TYR B CZ    1 
ATOM   6407  O  OH    . TYR B  2  375 ? 61.505 -35.295 10.430  1.00 30.00  ?  407 TYR B OH    1 
ATOM   6408  N  N     . ASN B  2  376 ? 56.507 -29.370 11.159  1.00 38.92  ?  408 ASN B N     1 
ATOM   6409  C  CA    . ASN B  2  376 ? 55.430 -29.379 10.178  1.00 41.24  ?  408 ASN B CA    1 
ATOM   6410  C  C     . ASN B  2  376 ? 55.899 -28.524 9.038   1.00 38.73  ?  408 ASN B C     1 
ATOM   6411  O  O     . ASN B  2  376 ? 56.013 -28.986 7.902   1.00 38.42  ?  408 ASN B O     1 
ATOM   6412  C  CB    . ASN B  2  376 ? 54.137 -28.763 10.747  1.00 48.84  ?  408 ASN B CB    1 
ATOM   6413  C  CG    . ASN B  2  376 ? 52.967 -29.738 10.768  1.00 53.47  ?  408 ASN B CG    1 
ATOM   6414  O  OD1   . ASN B  2  376 ? 52.465 -30.164 9.707   1.00 55.25  ?  408 ASN B OD1   1 
ATOM   6415  N  ND2   . ASN B  2  376 ? 52.501 -30.073 11.980  1.00 54.24  ?  408 ASN B ND2   1 
ATOM   6416  N  N     . TYR B  2  377 ? 56.191 -27.269 9.376   1.00 36.38  ?  409 TYR B N     1 
ATOM   6417  C  CA    . TYR B  2  377 ? 56.504 -26.261 8.385   1.00 35.46  ?  409 TYR B CA    1 
ATOM   6418  C  C     . TYR B  2  377 ? 57.668 -26.716 7.568   1.00 32.30  ?  409 TYR B C     1 
ATOM   6419  O  O     . TYR B  2  377 ? 57.730 -26.437 6.389   1.00 31.96  ?  409 TYR B O     1 
ATOM   6420  C  CB    . TYR B  2  377 ? 56.822 -24.910 9.038   1.00 37.06  ?  409 TYR B CB    1 
ATOM   6421  C  CG    . TYR B  2  377 ? 55.636 -24.210 9.688   1.00 38.58  ?  409 TYR B CG    1 
ATOM   6422  C  CD1   . TYR B  2  377 ? 54.334 -24.681 9.515   1.00 38.77  ?  409 TYR B CD1   1 
ATOM   6423  C  CD2   . TYR B  2  377 ? 55.814 -23.054 10.460  1.00 39.65  ?  409 TYR B CD2   1 
ATOM   6424  C  CE1   . TYR B  2  377 ? 53.258 -24.045 10.105  1.00 38.86  ?  409 TYR B CE1   1 
ATOM   6425  C  CE2   . TYR B  2  377 ? 54.734 -22.420 11.056  1.00 40.06  ?  409 TYR B CE2   1 
ATOM   6426  C  CZ    . TYR B  2  377 ? 53.461 -22.927 10.870  1.00 38.78  ?  409 TYR B CZ    1 
ATOM   6427  O  OH    . TYR B  2  377 ? 52.372 -22.320 11.431  1.00 40.33  ?  409 TYR B OH    1 
ATOM   6428  N  N     . PHE B  2  378 ? 58.576 -27.438 8.203   1.00 31.10  ?  410 PHE B N     1 
ATOM   6429  C  CA    . PHE B  2  378 ? 59.769 -27.958 7.533   1.00 31.25  ?  410 PHE B CA    1 
ATOM   6430  C  C     . PHE B  2  378 ? 59.491 -28.685 6.209   1.00 32.14  ?  410 PHE B C     1 
ATOM   6431  O  O     . PHE B  2  378 ? 60.216 -28.490 5.226   1.00 32.23  ?  410 PHE B O     1 
ATOM   6432  C  CB    . PHE B  2  378 ? 60.525 -28.881 8.469   1.00 28.42  ?  410 PHE B CB    1 
ATOM   6433  C  CG    . PHE B  2  378 ? 61.679 -29.553 7.833   1.00 26.57  ?  410 PHE B CG    1 
ATOM   6434  C  CD1   . PHE B  2  378 ? 62.816 -28.846 7.559   1.00 26.52  ?  410 PHE B CD1   1 
ATOM   6435  C  CD2   . PHE B  2  378 ? 61.624 -30.895 7.497   1.00 26.46  ?  410 PHE B CD2   1 
ATOM   6436  C  CE1   . PHE B  2  378 ? 63.921 -29.466 6.991   1.00 27.22  ?  410 PHE B CE1   1 
ATOM   6437  C  CE2   . PHE B  2  378 ? 62.708 -31.521 6.916   1.00 26.77  ?  410 PHE B CE2   1 
ATOM   6438  C  CZ    . PHE B  2  378 ? 63.867 -30.806 6.666   1.00 26.99  ?  410 PHE B CZ    1 
ATOM   6439  N  N     . PHE B  2  379 ? 58.450 -29.520 6.193   1.00 32.84  ?  411 PHE B N     1 
ATOM   6440  C  CA    . PHE B  2  379 ? 57.971 -30.161 4.953   1.00 33.03  ?  411 PHE B CA    1 
ATOM   6441  C  C     . PHE B  2  379 ? 56.856 -29.315 4.316   1.00 30.73  ?  411 PHE B C     1 
ATOM   6442  O  O     . PHE B  2  379 ? 56.042 -29.834 3.547   1.00 28.32  ?  411 PHE B O     1 
ATOM   6443  C  CB    . PHE B  2  379 ? 57.446 -31.588 5.232   1.00 34.03  ?  411 PHE B CB    1 
ATOM   6444  C  CG    . PHE B  2  379 ? 58.495 -32.563 5.744   1.00 35.80  ?  411 PHE B CG    1 
ATOM   6445  C  CD1   . PHE B  2  379 ? 59.486 -33.079 4.900   1.00 36.73  ?  411 PHE B CD1   1 
ATOM   6446  C  CD2   . PHE B  2  379 ? 58.476 -32.993 7.064   1.00 36.90  ?  411 PHE B CD2   1 
ATOM   6447  C  CE1   . PHE B  2  379 ? 60.439 -33.986 5.378   1.00 36.11  ?  411 PHE B CE1   1 
ATOM   6448  C  CE2   . PHE B  2  379 ? 59.427 -33.901 7.538   1.00 37.12  ?  411 PHE B CE2   1 
ATOM   6449  C  CZ    . PHE B  2  379 ? 60.398 -34.406 6.689   1.00 36.32  ?  411 PHE B CZ    1 
ATOM   6450  N  N     . VAL B  2  380 ? 56.826 -28.019 4.651   1.00 29.05  ?  412 VAL B N     1 
ATOM   6451  C  CA    . VAL B  2  380 ? 55.832 -27.094 4.140   1.00 27.15  ?  412 VAL B CA    1 
ATOM   6452  C  C     . VAL B  2  380 ? 54.442 -27.742 4.240   1.00 28.26  ?  412 VAL B C     1 
ATOM   6453  O  O     . VAL B  2  380 ? 53.717 -27.904 3.247   1.00 25.90  ?  412 VAL B O     1 
ATOM   6454  C  CB    . VAL B  2  380 ? 56.186 -26.682 2.716   1.00 26.12  ?  412 VAL B CB    1 
ATOM   6455  C  CG1   . VAL B  2  380 ? 55.381 -25.467 2.299   1.00 25.94  ?  412 VAL B CG1   1 
ATOM   6456  C  CG2   . VAL B  2  380 ? 57.687 -26.432 2.615   1.00 25.75  ?  412 VAL B CG2   1 
ATOM   6457  N  N     . SER B  2  381 ? 54.117 -28.149 5.474   1.00 28.95  ?  413 SER B N     1 
ATOM   6458  C  CA    . SER B  2  381 ? 52.775 -28.606 5.862   1.00 29.27  ?  413 SER B CA    1 
ATOM   6459  C  C     . SER B  2  381 ? 52.308 -29.822 5.063   1.00 31.47  ?  413 SER B C     1 
ATOM   6460  O  O     . SER B  2  381 ? 51.106 -30.072 4.932   1.00 31.23  ?  413 SER B O     1 
ATOM   6461  C  CB    . SER B  2  381 ? 51.750 -27.450 5.771   1.00 27.83  ?  413 SER B CB    1 
ATOM   6462  O  OG    . SER B  2  381 ? 51.940 -26.502 6.815   1.00 25.75  ?  413 SER B OG    1 
ATOM   6463  N  N     . TYR B  2  382 ? 53.262 -30.604 4.568   1.00 34.52  ?  414 TYR B N     1 
ATOM   6464  C  CA    . TYR B  2  382 ? 52.934 -31.744 3.715   1.00 36.60  ?  414 TYR B CA    1 
ATOM   6465  C  C     . TYR B  2  382 ? 52.166 -32.836 4.450   1.00 42.56  ?  414 TYR B C     1 
ATOM   6466  O  O     . TYR B  2  382 ? 51.190 -33.370 3.907   1.00 46.00  ?  414 TYR B O     1 
ATOM   6467  C  CB    . TYR B  2  382 ? 54.184 -32.338 3.061   1.00 33.17  ?  414 TYR B CB    1 
ATOM   6468  C  CG    . TYR B  2  382 ? 53.883 -33.575 2.243   1.00 30.15  ?  414 TYR B CG    1 
ATOM   6469  C  CD1   . TYR B  2  382 ? 53.283 -33.477 0.999   1.00 28.05  ?  414 TYR B CD1   1 
ATOM   6470  C  CD2   . TYR B  2  382 ? 54.182 -34.840 2.737   1.00 29.18  ?  414 TYR B CD2   1 
ATOM   6471  C  CE1   . TYR B  2  382 ? 53.004 -34.598 0.270   1.00 27.44  ?  414 TYR B CE1   1 
ATOM   6472  C  CE2   . TYR B  2  382 ? 53.908 -35.964 2.014   1.00 27.93  ?  414 TYR B CE2   1 
ATOM   6473  C  CZ    . TYR B  2  382 ? 53.319 -35.833 0.783   1.00 27.24  ?  414 TYR B CZ    1 
ATOM   6474  O  OH    . TYR B  2  382 ? 53.041 -36.963 0.072   1.00 28.04  ?  414 TYR B OH    1 
ATOM   6475  N  N     . ASP B  2  383 ? 52.614 -33.187 5.653   1.00 47.63  ?  415 ASP B N     1 
ATOM   6476  C  CA    . ASP B  2  383 ? 51.842 -34.079 6.496   1.00 56.44  ?  415 ASP B CA    1 
ATOM   6477  C  C     . ASP B  2  383 ? 51.456 -33.276 7.735   1.00 64.33  ?  415 ASP B C     1 
ATOM   6478  O  O     . ASP B  2  383 ? 52.323 -32.772 8.462   1.00 66.70  ?  415 ASP B O     1 
ATOM   6479  C  CB    . ASP B  2  383 ? 52.635 -35.349 6.837   1.00 61.12  ?  415 ASP B CB    1 
ATOM   6480  C  CG    . ASP B  2  383 ? 51.804 -36.394 7.609   1.00 63.84  ?  415 ASP B CG    1 
ATOM   6481  O  OD1   . ASP B  2  383 ? 50.560 -36.279 7.610   1.00 64.63  ?  415 ASP B OD1   1 
ATOM   6482  O  OD2   . ASP B  2  383 ? 52.393 -37.340 8.201   1.00 61.98  -1 415 ASP B OD2   1 
ATOM   6483  N  N     . SER B  2  384 ? 50.144 -33.119 7.931   1.00 68.57  ?  416 SER B N     1 
ATOM   6484  C  CA    . SER B  2  384 ? 49.612 -32.404 9.081   1.00 68.94  ?  416 SER B CA    1 
ATOM   6485  C  C     . SER B  2  384 ? 49.733 -33.290 10.276  1.00 63.46  ?  416 SER B C     1 
ATOM   6486  O  O     . SER B  2  384 ? 49.676 -32.812 11.400  1.00 68.58  ?  416 SER B O     1 
ATOM   6487  C  CB    . SER B  2  384 ? 48.141 -31.995 8.893   1.00 75.12  ?  416 SER B CB    1 
ATOM   6488  O  OG    . SER B  2  384 ? 47.985 -30.576 8.845   1.00 79.96  ?  416 SER B OG    1 
ATOM   6489  N  N     . SER B  2  385 ? 49.872 -34.586 10.032  1.00 59.17  ?  417 SER B N     1 
ATOM   6490  C  CA    . SER B  2  385 ? 50.110 -35.539 11.101  1.00 59.80  ?  417 SER B CA    1 
ATOM   6491  C  C     . SER B  2  385 ? 51.429 -36.257 10.885  1.00 57.66  ?  417 SER B C     1 
ATOM   6492  O  O     . SER B  2  385 ? 51.474 -37.491 10.780  1.00 57.04  ?  417 SER B O     1 
ATOM   6493  C  CB    . SER B  2  385 ? 48.963 -36.544 11.183  1.00 60.27  ?  417 SER B CB    1 
ATOM   6494  O  OG    . SER B  2  385 ? 48.998 -37.423 10.079  1.00 64.02  ?  417 SER B OG    1 
ATOM   6495  N  N     . VAL B  2  386 ? 52.500 -35.474 10.808  1.00 56.57  ?  418 VAL B N     1 
ATOM   6496  C  CA    . VAL B  2  386 ? 53.859 -36.027 10.812  1.00 58.60  ?  418 VAL B CA    1 
ATOM   6497  C  C     . VAL B  2  386 ? 54.435 -35.988 12.244  1.00 57.02  ?  418 VAL B C     1 
ATOM   6498  O  O     . VAL B  2  386 ? 53.914 -35.284 13.107  1.00 58.05  ?  418 VAL B O     1 
ATOM   6499  C  CB    . VAL B  2  386 ? 54.772 -35.283 9.804   1.00 57.64  ?  418 VAL B CB    1 
ATOM   6500  C  CG1   . VAL B  2  386 ? 55.494 -34.110 10.454  1.00 57.56  ?  418 VAL B CG1   1 
ATOM   6501  C  CG2   . VAL B  2  386 ? 55.765 -36.244 9.167   1.00 58.15  ?  418 VAL B CG2   1 
ATOM   6502  N  N     . THR B  2  387 ? 55.490 -36.753 12.505  1.00 53.04  ?  419 THR B N     1 
ATOM   6503  C  CA    . THR B  2  387 ? 56.077 -36.805 13.849  1.00 48.52  ?  419 THR B CA    1 
ATOM   6504  C  C     . THR B  2  387 ? 57.603 -36.860 13.761  1.00 44.45  ?  419 THR B C     1 
ATOM   6505  O  O     . THR B  2  387 ? 58.166 -36.793 12.670  1.00 43.18  ?  419 THR B O     1 
ATOM   6506  C  CB    . THR B  2  387 ? 55.485 -37.985 14.666  1.00 48.92  ?  419 THR B CB    1 
ATOM   6507  O  OG1   . THR B  2  387 ? 56.045 -37.991 15.988  1.00 48.54  ?  419 THR B OG1   1 
ATOM   6508  C  CG2   . THR B  2  387 ? 55.709 -39.354 13.961  1.00 46.81  ?  419 THR B CG2   1 
ATOM   6509  N  N     . CYS B  2  388 ? 58.279 -36.963 14.897  1.00 41.86  ?  420 CYS B N     1 
ATOM   6510  C  CA    . CYS B  2  388 ? 59.735 -36.881 14.895  1.00 42.35  ?  420 CYS B CA    1 
ATOM   6511  C  C     . CYS B  2  388 ? 60.336 -37.432 16.179  1.00 43.09  ?  420 CYS B C     1 
ATOM   6512  O  O     . CYS B  2  388 ? 60.027 -36.933 17.251  1.00 44.96  ?  420 CYS B O     1 
ATOM   6513  C  CB    . CYS B  2  388 ? 60.178 -35.420 14.714  1.00 40.42  ?  420 CYS B CB    1 
ATOM   6514  S  SG    . CYS B  2  388 ? 61.952 -35.196 14.447  1.00 38.82  ?  420 CYS B SG    1 
ATOM   6515  N  N     . ASP B  2  389 ? 61.198 -38.442 16.069  1.00 42.49  ?  421 ASP B N     1 
ATOM   6516  C  CA    . ASP B  2  389 ? 61.876 -39.003 17.254  1.00 42.36  ?  421 ASP B CA    1 
ATOM   6517  C  C     . ASP B  2  389 ? 63.079 -38.141 17.760  1.00 39.43  ?  421 ASP B C     1 
ATOM   6518  O  O     . ASP B  2  389 ? 63.435 -37.122 17.141  1.00 35.32  ?  421 ASP B O     1 
ATOM   6519  C  CB    . ASP B  2  389 ? 62.288 -40.465 16.992  1.00 42.86  ?  421 ASP B CB    1 
ATOM   6520  C  CG    . ASP B  2  389 ? 63.396 -40.590 15.982  1.00 43.99  ?  421 ASP B CG    1 
ATOM   6521  O  OD1   . ASP B  2  389 ? 63.413 -39.753 15.059  1.00 50.88  ?  421 ASP B OD1   1 
ATOM   6522  O  OD2   . ASP B  2  389 ? 64.235 -41.513 16.097  1.00 41.53  -1 421 ASP B OD2   1 
ATOM   6523  N  N     . LYS B  2  390 ? 63.678 -38.558 18.884  1.00 37.16  ?  422 LYS B N     1 
ATOM   6524  C  CA    . LYS B  2  390 ? 64.699 -37.765 19.570  1.00 38.18  ?  422 LYS B CA    1 
ATOM   6525  C  C     . LYS B  2  390 ? 65.905 -37.525 18.691  1.00 39.07  ?  422 LYS B C     1 
ATOM   6526  O  O     . LYS B  2  390 ? 66.590 -36.512 18.834  1.00 38.69  ?  422 LYS B O     1 
ATOM   6527  C  CB    . LYS B  2  390 ? 65.246 -38.451 20.819  1.00 39.94  ?  422 LYS B CB    1 
ATOM   6528  C  CG    . LYS B  2  390 ? 64.263 -38.879 21.896  1.00 43.01  ?  422 LYS B CG    1 
ATOM   6529  C  CD    . LYS B  2  390 ? 64.830 -40.101 22.644  1.00 46.87  ?  422 LYS B CD    1 
ATOM   6530  C  CE    . LYS B  2  390 ? 65.162 -41.279 21.699  1.00 45.10  ?  422 LYS B CE    1 
ATOM   6531  N  NZ    . LYS B  2  390 ? 65.191 -42.635 22.316  1.00 42.73  1  422 LYS B NZ    1 
ATOM   6532  N  N     . THR B  2  391 ? 66.214 -38.490 17.832  1.00 38.98  ?  423 THR B N     1 
ATOM   6533  C  CA    . THR B  2  391 ? 67.444 -38.435 17.058  1.00 38.23  ?  423 THR B CA    1 
ATOM   6534  C  C     . THR B  2  391 ? 67.254 -37.427 15.930  1.00 36.84  ?  423 THR B C     1 
ATOM   6535  O  O     . THR B  2  391 ? 68.086 -36.528 15.753  1.00 35.33  ?  423 THR B O     1 
ATOM   6536  C  CB    . THR B  2  391 ? 67.832 -39.828 16.500  1.00 39.02  ?  423 THR B CB    1 
ATOM   6537  O  OG1   . THR B  2  391 ? 67.425 -40.842 17.423  1.00 39.17  ?  423 THR B OG1   1 
ATOM   6538  C  CG2   . THR B  2  391 ? 69.344 -39.938 16.259  1.00 38.38  ?  423 THR B CG2   1 
ATOM   6539  N  N     . CYS B  2  392 ? 66.154 -37.566 15.186  1.00 35.77  ?  424 CYS B N     1 
ATOM   6540  C  CA    . CYS B  2  392 ? 65.866 -36.661 14.059  1.00 38.03  ?  424 CYS B CA    1 
ATOM   6541  C  C     . CYS B  2  392 ? 65.794 -35.206 14.524  1.00 36.29  ?  424 CYS B C     1 
ATOM   6542  O  O     . CYS B  2  392 ? 66.200 -34.303 13.790  1.00 35.09  ?  424 CYS B O     1 
ATOM   6543  C  CB    . CYS B  2  392 ? 64.565 -37.045 13.316  1.00 39.48  ?  424 CYS B CB    1 
ATOM   6544  S  SG    . CYS B  2  392 ? 64.765 -38.283 11.999  1.00 42.54  ?  424 CYS B SG    1 
ATOM   6545  N  N     . LYS B  2  393 ? 65.283 -35.012 15.746  1.00 33.39  ?  425 LYS B N     1 
ATOM   6546  C  CA    . LYS B  2  393 ? 65.171 -33.695 16.358  1.00 31.15  ?  425 LYS B CA    1 
ATOM   6547  C  C     . LYS B  2  393 ? 66.518 -33.144 16.770  1.00 30.23  ?  425 LYS B C     1 
ATOM   6548  O  O     . LYS B  2  393 ? 66.799 -31.992 16.546  1.00 29.70  ?  425 LYS B O     1 
ATOM   6549  C  CB    . LYS B  2  393 ? 64.236 -33.726 17.579  1.00 30.83  ?  425 LYS B CB    1 
ATOM   6550  C  CG    . LYS B  2  393 ? 64.278 -32.450 18.424  1.00 29.98  ?  425 LYS B CG    1 
ATOM   6551  C  CD    . LYS B  2  393 ? 62.995 -32.232 19.196  1.00 29.39  ?  425 LYS B CD    1 
ATOM   6552  C  CE    . LYS B  2  393 ? 63.239 -31.403 20.449  1.00 29.35  ?  425 LYS B CE    1 
ATOM   6553  N  NZ    . LYS B  2  393 ? 61.943 -31.087 21.103  1.00 29.37  1  425 LYS B NZ    1 
ATOM   6554  N  N     . ALA B  2  394 ? 67.340 -33.957 17.410  1.00 31.34  ?  426 ALA B N     1 
ATOM   6555  C  CA    . ALA B  2  394 ? 68.700 -33.554 17.701  1.00 31.23  ?  426 ALA B CA    1 
ATOM   6556  C  C     . ALA B  2  394 ? 69.409 -33.168 16.391  1.00 32.35  ?  426 ALA B C     1 
ATOM   6557  O  O     . ALA B  2  394 ? 70.132 -32.177 16.339  1.00 31.81  ?  426 ALA B O     1 
ATOM   6558  C  CB    . ALA B  2  394 ? 69.433 -34.680 18.405  1.00 31.14  ?  426 ALA B CB    1 
ATOM   6559  N  N     . PHE B  2  395 ? 69.178 -33.924 15.323  1.00 33.57  ?  427 PHE B N     1 
ATOM   6560  C  CA    . PHE B  2  395 ? 69.789 -33.592 14.041  1.00 36.01  ?  427 PHE B CA    1 
ATOM   6561  C  C     . PHE B  2  395 ? 69.368 -32.233 13.457  1.00 36.22  ?  427 PHE B C     1 
ATOM   6562  O  O     . PHE B  2  395 ? 70.129 -31.648 12.658  1.00 38.06  ?  427 PHE B O     1 
ATOM   6563  C  CB    . PHE B  2  395 ? 69.572 -34.720 13.024  1.00 36.58  ?  427 PHE B CB    1 
ATOM   6564  C  CG    . PHE B  2  395 ? 70.351 -35.978 13.343  1.00 38.16  ?  427 PHE B CG    1 
ATOM   6565  C  CD1   . PHE B  2  395 ? 71.579 -35.925 14.052  1.00 37.06  ?  427 PHE B CD1   1 
ATOM   6566  C  CD2   . PHE B  2  395 ? 69.871 -37.222 12.919  1.00 37.50  ?  427 PHE B CD2   1 
ATOM   6567  C  CE1   . PHE B  2  395 ? 72.276 -37.081 14.349  1.00 36.50  ?  427 PHE B CE1   1 
ATOM   6568  C  CE2   . PHE B  2  395 ? 70.568 -38.377 13.214  1.00 37.15  ?  427 PHE B CE2   1 
ATOM   6569  C  CZ    . PHE B  2  395 ? 71.770 -38.305 13.932  1.00 37.95  ?  427 PHE B CZ    1 
ATOM   6570  N  N     . GLN B  2  396 ? 68.185 -31.755 13.856  1.00 34.66  ?  428 GLN B N     1 
ATOM   6571  C  CA    . GLN B  2  396 ? 67.653 -30.445 13.457  1.00 35.53  ?  428 GLN B CA    1 
ATOM   6572  C  C     . GLN B  2  396 ? 68.183 -29.330 14.365  1.00 37.76  ?  428 GLN B C     1 
ATOM   6573  O  O     . GLN B  2  396 ? 68.632 -28.285 13.888  1.00 36.93  ?  428 GLN B O     1 
ATOM   6574  C  CB    . GLN B  2  396 ? 66.110 -30.428 13.525  1.00 35.72  ?  428 GLN B CB    1 
ATOM   6575  C  CG    . GLN B  2  396 ? 65.368 -31.314 12.520  1.00 35.86  ?  428 GLN B CG    1 
ATOM   6576  C  CD    . GLN B  2  396 ? 65.063 -30.637 11.191  1.00 35.34  ?  428 GLN B CD    1 
ATOM   6577  O  OE1   . GLN B  2  396 ? 65.373 -29.466 10.991  1.00 36.06  ?  428 GLN B OE1   1 
ATOM   6578  N  NE2   . GLN B  2  396 ? 64.467 -31.382 10.269  1.00 34.86  ?  428 GLN B NE2   1 
ATOM   6579  N  N     . ILE B  2  397 ? 68.118 -29.553 15.680  1.00 41.02  ?  429 ILE B N     1 
ATOM   6580  C  CA    . ILE B  2  397 ? 68.489 -28.530 16.679  1.00 41.77  ?  429 ILE B CA    1 
ATOM   6581  C  C     . ILE B  2  397 ? 69.942 -28.146 16.486  1.00 40.94  ?  429 ILE B C     1 
ATOM   6582  O  O     . ILE B  2  397 ? 70.279 -26.977 16.419  1.00 42.84  ?  429 ILE B O     1 
ATOM   6583  C  CB    . ILE B  2  397 ? 68.312 -29.007 18.159  1.00 43.28  ?  429 ILE B CB    1 
ATOM   6584  C  CG1   . ILE B  2  397 ? 66.847 -29.392 18.478  1.00 43.71  ?  429 ILE B CG1   1 
ATOM   6585  C  CG2   . ILE B  2  397 ? 68.818 -27.944 19.141  1.00 42.47  ?  429 ILE B CG2   1 
ATOM   6586  C  CD1   . ILE B  2  397 ? 65.819 -28.310 18.242  1.00 43.48  ?  429 ILE B CD1   1 
ATOM   6587  N  N     . CYS B  2  398 ? 70.765 -29.155 16.447  1.00 40.40  ?  430 CYS B N     1 
ATOM   6588  C  CA    . CYS B  2  398 ? 72.156 -28.927 16.330  1.00 41.73  ?  430 CYS B CA    1 
ATOM   6589  C  C     . CYS B  2  398 ? 72.544 -28.405 14.953  1.00 38.80  ?  430 CYS B C     1 
ATOM   6590  O  O     . CYS B  2  398 ? 73.694 -28.228 14.716  1.00 42.65  ?  430 CYS B O     1 
ATOM   6591  C  CB    . CYS B  2  398 ? 72.973 -30.148 16.861  1.00 44.66  ?  430 CYS B CB    1 
ATOM   6592  S  SG    . CYS B  2  398 ? 73.679 -29.994 18.546  1.00 51.21  ?  430 CYS B SG    1 
ATOM   6593  N  N     . ALA B  2  399 ? 71.604 -28.144 14.053  1.00 34.03  ?  431 ALA B N     1 
ATOM   6594  C  CA    . ALA B  2  399 ? 71.958 -27.612 12.766  1.00 29.83  ?  431 ALA B CA    1 
ATOM   6595  C  C     . ALA B  2  399 ? 71.502 -26.242 12.642  1.00 28.02  ?  431 ALA B C     1 
ATOM   6596  O  O     . ALA B  2  399 ? 72.061 -25.497 11.924  1.00 25.47  ?  431 ALA B O     1 
ATOM   6597  C  CB    . ALA B  2  399 ? 71.361 -28.453 11.684  1.00 29.19  ?  431 ALA B CB    1 
ATOM   6598  N  N     . ILE B  2  400 ? 70.466 -25.910 13.360  1.00 29.36  ?  432 ILE B N     1 
ATOM   6599  C  CA    . ILE B  2  400 ? 69.914 -24.582 13.360  1.00 30.45  ?  432 ILE B CA    1 
ATOM   6600  C  C     . ILE B  2  400 ? 70.829 -23.712 14.149  1.00 30.75  ?  432 ILE B C     1 
ATOM   6601  O  O     . ILE B  2  400 ? 70.948 -22.569 13.897  1.00 30.34  ?  432 ILE B O     1 
ATOM   6602  C  CB    . ILE B  2  400 ? 68.542 -24.557 14.048  1.00 28.47  ?  432 ILE B CB    1 
ATOM   6603  C  CG1   . ILE B  2  400 ? 67.693 -25.717 13.583  1.00 27.77  ?  432 ILE B CG1   1 
ATOM   6604  C  CG2   . ILE B  2  400 ? 67.835 -23.249 13.825  1.00 27.51  ?  432 ILE B CG2   1 
ATOM   6605  C  CD1   . ILE B  2  400 ? 66.248 -25.611 13.953  1.00 27.53  ?  432 ILE B CD1   1 
ATOM   6606  N  N     . MET B  2  401 ? 71.492 -24.288 15.119  1.00 33.63  ?  433 MET B N     1 
ATOM   6607  C  CA    . MET B  2  401 ? 72.356 -23.560 15.995  1.00 36.27  ?  433 MET B CA    1 
ATOM   6608  C  C     . MET B  2  401 ? 73.819 -23.670 15.753  1.00 33.93  ?  433 MET B C     1 
ATOM   6609  O  O     . MET B  2  401 ? 74.524 -22.772 16.090  1.00 34.98  ?  433 MET B O     1 
ATOM   6610  C  CB    . MET B  2  401 ? 72.088 -23.985 17.421  1.00 39.59  ?  433 MET B CB    1 
ATOM   6611  C  CG    . MET B  2  401 ? 71.087 -23.145 18.170  1.00 40.97  ?  433 MET B CG    1 
ATOM   6612  S  SD    . MET B  2  401 ? 70.240 -24.172 19.327  1.00 45.49  ?  433 MET B SD    1 
ATOM   6613  C  CE    . MET B  2  401 ? 70.635 -23.317 20.825  1.00 44.49  ?  433 MET B CE    1 
ATOM   6614  N  N     . ASN B  2  402 ? 74.291 -24.759 15.187  1.00 33.30  ?  434 ASN B N     1 
ATOM   6615  C  CA    . ASN B  2  402 ? 75.708 -24.914 14.927  1.00 33.95  ?  434 ASN B CA    1 
ATOM   6616  C  C     . ASN B  2  402 ? 76.049 -24.975 13.457  1.00 33.41  ?  434 ASN B C     1 
ATOM   6617  O  O     . ASN B  2  402 ? 75.497 -25.758 12.745  1.00 29.63  ?  434 ASN B O     1 
ATOM   6618  C  CB    . ASN B  2  402 ? 76.198 -26.156 15.612  1.00 34.20  ?  434 ASN B CB    1 
ATOM   6619  C  CG    . ASN B  2  402 ? 75.670 -26.290 16.999  1.00 33.83  ?  434 ASN B CG    1 
ATOM   6620  O  OD1   . ASN B  2  402 ? 76.085 -25.600 17.895  1.00 34.67  ?  434 ASN B OD1   1 
ATOM   6621  N  ND2   . ASN B  2  402 ? 74.757 -27.181 17.178  1.00 33.95  ?  434 ASN B ND2   1 
ATOM   6622  N  N     . LEU B  2  403 ? 76.962 -24.140 13.001  1.00 35.01  ?  435 LEU B N     1 
ATOM   6623  C  CA    . LEU B  2  403 ? 77.296 -24.113 11.597  1.00 37.12  ?  435 LEU B CA    1 
ATOM   6624  C  C     . LEU B  2  403 ? 78.608 -24.750 11.240  1.00 43.48  ?  435 LEU B C     1 
ATOM   6625  O  O     . LEU B  2  403 ? 78.712 -25.316 10.191  1.00 47.84  ?  435 LEU B O     1 
ATOM   6626  C  CB    . LEU B  2  403 ? 77.176 -22.717 11.043  1.00 35.79  ?  435 LEU B CB    1 
ATOM   6627  C  CG    . LEU B  2  403 ? 75.785 -22.367 10.568  1.00 35.67  ?  435 LEU B CG    1 
ATOM   6628  C  CD1   . LEU B  2  403 ? 74.834 -22.248 11.707  1.00 36.29  ?  435 LEU B CD1   1 
ATOM   6629  C  CD2   . LEU B  2  403 ? 75.762 -21.095 9.795   1.00 35.39  ?  435 LEU B CD2   1 
ATOM   6630  N  N     . ASP B  2  404 ? 79.607 -24.672 12.113  1.00 49.74  ?  436 ASP B N     1 
ATOM   6631  C  CA    . ASP B  2  404 ? 80.906 -25.296 11.883  1.00 52.43  ?  436 ASP B CA    1 
ATOM   6632  C  C     . ASP B  2  404 ? 80.980 -26.596 12.650  1.00 49.47  ?  436 ASP B C     1 
ATOM   6633  O  O     . ASP B  2  404 ? 80.054 -26.912 13.321  1.00 48.36  ?  436 ASP B O     1 
ATOM   6634  C  CB    . ASP B  2  404 ? 82.040 -24.363 12.226  1.00 54.10  ?  436 ASP B CB    1 
ATOM   6635  C  CG    . ASP B  2  404 ? 81.856 -23.684 13.522  1.00 57.70  ?  436 ASP B CG    1 
ATOM   6636  O  OD1   . ASP B  2  404 ? 82.623 -23.993 14.426  1.00 61.61  ?  436 ASP B OD1   1 
ATOM   6637  O  OD2   . ASP B  2  404 ? 80.987 -22.821 13.640  1.00 57.38  -1 436 ASP B OD2   1 
ATOM   6638  N  N     . ASN B  2  405 ? 82.048 -27.370 12.541  1.00 49.66  ?  437 ASN B N     1 
ATOM   6639  C  CA    . ASN B  2  405 ? 82.082 -28.682 13.195  1.00 53.65  ?  437 ASN B CA    1 
ATOM   6640  C  C     . ASN B  2  405 ? 82.561 -28.826 14.600  1.00 52.59  ?  437 ASN B C     1 
ATOM   6641  O  O     . ASN B  2  405 ? 82.390 -29.857 15.219  1.00 46.08  ?  437 ASN B O     1 
ATOM   6642  C  CB    . ASN B  2  405 ? 82.728 -29.733 12.324  1.00 56.77  ?  437 ASN B CB    1 
ATOM   6643  C  CG    . ASN B  2  405 ? 84.205 -29.777 12.483  1.00 58.28  ?  437 ASN B CG    1 
ATOM   6644  O  OD1   . ASN B  2  405 ? 84.791 -30.837 12.568  1.00 57.55  ?  437 ASN B OD1   1 
ATOM   6645  N  ND2   . ASN B  2  405 ? 84.816 -28.618 12.542  1.00 60.85  ?  437 ASN B ND2   1 
ATOM   6646  N  N     . ILE B  2  406 ? 83.159 -27.778 15.103  1.00 55.14  ?  438 ILE B N     1 
ATOM   6647  C  CA    . ILE B  2  406 ? 83.625 -27.788 16.443  1.00 57.61  ?  438 ILE B CA    1 
ATOM   6648  C  C     . ILE B  2  406 ? 82.342 -27.625 17.177  1.00 56.00  ?  438 ILE B C     1 
ATOM   6649  O  O     . ILE B  2  406 ? 82.012 -28.412 18.019  1.00 56.90  ?  438 ILE B O     1 
ATOM   6650  C  CB    . ILE B  2  406 ? 84.554 -26.599 16.705  1.00 60.84  ?  438 ILE B CB    1 
ATOM   6651  C  CG1   . ILE B  2  406 ? 85.958 -26.948 16.283  1.00 59.78  ?  438 ILE B CG1   1 
ATOM   6652  C  CG2   . ILE B  2  406 ? 84.636 -26.274 18.177  1.00 63.23  ?  438 ILE B CG2   1 
ATOM   6653  C  CD1   . ILE B  2  406 ? 86.412 -28.250 16.866  1.00 59.39  ?  438 ILE B CD1   1 
ATOM   6654  N  N     . SER B  2  407 ? 81.607 -26.593 16.833  1.00 51.24  ?  439 SER B N     1 
ATOM   6655  C  CA    . SER B  2  407 ? 80.356 -26.349 17.474  1.00 50.23  ?  439 SER B CA    1 
ATOM   6656  C  C     . SER B  2  407 ? 79.450 -27.527 17.309  1.00 47.34  ?  439 SER B C     1 
ATOM   6657  O  O     . SER B  2  407 ? 79.028 -28.126 18.268  1.00 44.07  ?  439 SER B O     1 
ATOM   6658  C  CB    . SER B  2  407 ? 79.734 -25.155 16.837  1.00 52.11  ?  439 SER B CB    1 
ATOM   6659  O  OG    . SER B  2  407 ? 80.563 -24.736 15.801  1.00 56.75  ?  439 SER B OG    1 
ATOM   6660  N  N     . TYR B  2  408 ? 79.153 -27.857 16.070  1.00 42.66  ?  440 TYR B N     1 
ATOM   6661  C  CA    . TYR B  2  408 ? 78.288 -28.950 15.751  1.00 40.84  ?  440 TYR B CA    1 
ATOM   6662  C  C     . TYR B  2  408 ? 78.608 -30.210 16.483  1.00 41.71  ?  440 TYR B C     1 
ATOM   6663  O  O     . TYR B  2  408 ? 77.748 -30.958 16.830  1.00 39.88  ?  440 TYR B O     1 
ATOM   6664  C  CB    . TYR B  2  408 ? 78.410 -29.248 14.292  1.00 40.65  ?  440 TYR B CB    1 
ATOM   6665  C  CG    . TYR B  2  408 ? 77.369 -30.203 13.821  1.00 40.43  ?  440 TYR B CG    1 
ATOM   6666  C  CD1   . TYR B  2  408 ? 76.088 -29.802 13.696  1.00 40.45  ?  440 TYR B CD1   1 
ATOM   6667  C  CD2   . TYR B  2  408 ? 77.669 -31.505 13.499  1.00 38.71  ?  440 TYR B CD2   1 
ATOM   6668  C  CE1   . TYR B  2  408 ? 75.131 -30.655 13.258  1.00 39.92  ?  440 TYR B CE1   1 
ATOM   6669  C  CE2   . TYR B  2  408 ? 76.701 -32.363 13.058  1.00 36.87  ?  440 TYR B CE2   1 
ATOM   6670  C  CZ    . TYR B  2  408 ? 75.440 -31.910 12.949  1.00 37.30  ?  440 TYR B CZ    1 
ATOM   6671  O  OH    . TYR B  2  408 ? 74.447 -32.698 12.544  1.00 36.55  ?  440 TYR B OH    1 
ATOM   6672  N  N     . ALA B  2  409 ? 79.877 -30.457 16.688  1.00 45.48  ?  441 ALA B N     1 
ATOM   6673  C  CA    . ALA B  2  409 ? 80.308 -31.651 17.350  1.00 47.34  ?  441 ALA B CA    1 
ATOM   6674  C  C     . ALA B  2  409 ? 80.101 -31.591 18.855  1.00 52.09  ?  441 ALA B C     1 
ATOM   6675  O  O     . ALA B  2  409 ? 79.632 -32.557 19.425  1.00 50.00  ?  441 ALA B O     1 
ATOM   6676  C  CB    . ALA B  2  409 ? 81.739 -31.921 17.006  1.00 46.14  ?  441 ALA B CB    1 
ATOM   6677  N  N     . ASP B  2  410 ? 80.403 -30.471 19.514  1.00 53.52  ?  442 ASP B N     1 
ATOM   6678  C  CA    . ASP B  2  410 ? 80.156 -30.403 20.942  1.00 55.61  ?  442 ASP B CA    1 
ATOM   6679  C  C     . ASP B  2  410 ? 78.698 -30.702 21.174  1.00 57.07  ?  442 ASP B C     1 
ATOM   6680  O  O     . ASP B  2  410 ? 78.314 -30.940 22.298  1.00 65.87  ?  442 ASP B O     1 
ATOM   6681  C  CB    . ASP B  2  410 ? 80.574 -29.094 21.612  1.00 56.07  ?  442 ASP B CB    1 
ATOM   6682  C  CG    . ASP B  2  410 ? 80.265 -29.083 23.118  1.00 56.09  ?  442 ASP B CG    1 
ATOM   6683  O  OD1   . ASP B  2  410 ? 80.300 -30.145 23.754  1.00 52.74  ?  442 ASP B OD1   1 
ATOM   6684  O  OD2   . ASP B  2  410 ? 79.974 -28.009 23.667  1.00 53.00  -1 442 ASP B OD2   1 
ATOM   6685  N  N     . CYS B  2  411 ? 77.908 -30.711 20.106  1.00 53.01  ?  443 CYS B N     1 
ATOM   6686  C  CA    . CYS B  2  411 ? 76.488 -31.056 20.148  1.00 54.46  ?  443 CYS B CA    1 
ATOM   6687  C  C     . CYS B  2  411 ? 76.455 -32.605 20.251  1.00 58.78  ?  443 CYS B C     1 
ATOM   6688  O  O     . CYS B  2  411 ? 75.656 -33.281 19.643  1.00 51.53  ?  443 CYS B O     1 
ATOM   6689  C  CB    . CYS B  2  411 ? 75.759 -30.529 18.888  1.00 54.37  ?  443 CYS B CB    1 
ATOM   6690  S  SG    . CYS B  2  411 ? 74.043 -29.916 18.878  1.00 47.76  ?  443 CYS B SG    1 
ATOM   6691  N  N     . LEU B  2  412 ? 77.381 -33.133 21.045  1.00 64.81  ?  444 LEU B N     1 
ATOM   6692  C  CA    . LEU B  2  412 ? 77.557 -34.576 21.395  1.00 64.96  ?  444 LEU B CA    1 
ATOM   6693  C  C     . LEU B  2  412 ? 76.879 -34.502 22.764  1.00 67.01  ?  444 LEU B C     1 
ATOM   6694  O  O     . LEU B  2  412 ? 76.751 -35.533 23.421  1.00 64.45  ?  444 LEU B O     1 
ATOM   6695  C  CB    . LEU B  2  412 ? 78.993 -35.104 21.568  1.00 69.44  ?  444 LEU B CB    1 
ATOM   6696  C  CG    . LEU B  2  412 ? 80.123 -34.329 22.337  1.00 74.49  ?  444 LEU B CG    1 
ATOM   6697  C  CD1   . LEU B  2  412 ? 79.939 -34.180 23.865  1.00 75.73  ?  444 LEU B CD1   1 
ATOM   6698  C  CD2   . LEU B  2  412 ? 81.508 -34.920 22.039  1.00 69.06  ?  444 LEU B CD2   1 
ATOM   6699  N  N     . LYS B  2  413 ? 76.476 -33.300 23.207  1.00 68.27  ?  445 LYS B N     1 
ATOM   6700  C  CA    . LYS B  2  413 ? 75.690 -33.105 24.438  1.00 65.99  ?  445 LYS B CA    1 
ATOM   6701  C  C     . LYS B  2  413 ? 74.421 -33.986 24.518  1.00 67.05  ?  445 LYS B C     1 
ATOM   6702  O  O     . LYS B  2  413 ? 73.732 -33.967 25.550  1.00 67.74  ?  445 LYS B O     1 
ATOM   6703  C  CB    . LYS B  2  413 ? 75.318 -31.624 24.589  1.00 63.79  ?  445 LYS B CB    1 
ATOM   6704  C  CG    . LYS B  2  413 ? 75.028 -31.167 26.007  1.00 66.68  ?  445 LYS B CG    1 
ATOM   6705  C  CD    . LYS B  2  413 ? 76.237 -31.389 26.907  1.00 76.12  ?  445 LYS B CD    1 
ATOM   6706  C  CE    . LYS B  2  413 ? 76.560 -30.188 27.779  1.00 81.17  ?  445 LYS B CE    1 
ATOM   6707  N  NZ    . LYS B  2  413 ? 75.381 -29.747 28.565  1.00 86.72  1  445 LYS B NZ    1 
ATOM   6708  N  N     . GLN B  2  414 ? 74.129 -34.732 23.433  1.00 67.15  ?  446 GLN B N     1 
ATOM   6709  C  CA    . GLN B  2  414 ? 73.135 -35.853 23.394  1.00 65.36  ?  446 GLN B CA    1 
ATOM   6710  C  C     . GLN B  2  414 ? 73.739 -37.262 23.058  1.00 65.30  ?  446 GLN B C     1 
ATOM   6711  O  O     . GLN B  2  414 ? 73.668 -38.164 23.891  1.00 58.32  ?  446 GLN B O     1 
ATOM   6712  C  CB    . GLN B  2  414 ? 71.925 -35.537 22.473  1.00 62.40  ?  446 GLN B CB    1 
ATOM   6713  C  CG    . GLN B  2  414 ? 72.144 -34.491 21.384  1.00 63.76  ?  446 GLN B CG    1 
ATOM   6714  C  CD    . GLN B  2  414 ? 72.215 -33.072 21.927  1.00 62.88  ?  446 GLN B CD    1 
ATOM   6715  O  OE1   . GLN B  2  414 ? 71.346 -32.664 22.676  1.00 56.73  ?  446 GLN B OE1   1 
ATOM   6716  N  NE2   . GLN B  2  414 ? 73.258 -32.319 21.555  1.00 64.14  ?  446 GLN B NE2   1 
ATOM   6717  N  N     . LEU B  2  415 ? 74.306 -37.463 21.861  1.00 71.06  ?  447 LEU B N     1 
ATOM   6718  C  CA    . LEU B  2  415 ? 75.021 -38.723 21.550  1.00 73.37  ?  447 LEU B CA    1 
ATOM   6719  C  C     . LEU B  2  415 ? 75.987 -38.575 20.354  1.00 71.06  ?  447 LEU B C     1 
ATOM   6720  O  O     . LEU B  2  415 ? 75.632 -38.826 19.204  1.00 63.27  ?  447 LEU B O     1 
ATOM   6721  C  CB    . LEU B  2  415 ? 74.016 -39.883 21.347  1.00 79.83  ?  447 LEU B CB    1 
ATOM   6722  C  CG    . LEU B  2  415 ? 74.422 -41.382 21.393  1.00 85.15  ?  447 LEU B CG    1 
ATOM   6723  C  CD1   . LEU B  2  415 ? 75.608 -41.691 22.309  1.00 85.95  ?  447 LEU B CD1   1 
ATOM   6724  C  CD2   . LEU B  2  415 ? 73.219 -42.260 21.775  1.00 80.78  ?  447 LEU B CD2   1 
ATOM   6725  N  N     . PRO C  2  1   ? 42.487 8.133   9.546   1.00 86.44  ?  33  PRO C N     1 
ATOM   6726  C  CA    . PRO C  2  1   ? 43.299 7.984   8.341   1.00 87.36  ?  33  PRO C CA    1 
ATOM   6727  C  C     . PRO C  2  1   ? 42.506 8.246   7.063   1.00 91.31  ?  33  PRO C C     1 
ATOM   6728  O  O     . PRO C  2  1   ? 41.286 8.321   7.105   1.00 88.20  ?  33  PRO C O     1 
ATOM   6729  C  CB    . PRO C  2  1   ? 43.723 6.516   8.375   1.00 83.94  ?  33  PRO C CB    1 
ATOM   6730  C  CG    . PRO C  2  1   ? 43.138 5.905   9.596   1.00 81.74  ?  33  PRO C CG    1 
ATOM   6731  C  CD    . PRO C  2  1   ? 42.155 6.848   10.175  1.00 82.02  ?  33  PRO C CD    1 
ATOM   6732  N  N     . PRO C  2  2   ? 43.249 8.403   5.902   1.00 91.43  ?  34  PRO C N     1 
ATOM   6733  C  CA    . PRO C  2  2   ? 42.465 8.572   4.684   1.00 81.44  ?  34  PRO C CA    1 
ATOM   6734  C  C     . PRO C  2  2   ? 42.544 7.232   4.011   1.00 73.93  ?  34  PRO C C     1 
ATOM   6735  O  O     . PRO C  2  2   ? 43.544 6.562   4.125   1.00 74.92  ?  34  PRO C O     1 
ATOM   6736  C  CB    . PRO C  2  2   ? 43.245 9.589   3.915   1.00 84.01  ?  34  PRO C CB    1 
ATOM   6737  C  CG    . PRO C  2  2   ? 44.629 9.172   4.133   1.00 93.25  ?  34  PRO C CG    1 
ATOM   6738  C  CD    . PRO C  2  2   ? 44.713 8.561   5.501   1.00 93.04  ?  34  PRO C CD    1 
ATOM   6739  N  N     . PRO C  2  3   ? 41.498 6.849   3.315   1.00 66.60  ?  35  PRO C N     1 
ATOM   6740  C  CA    . PRO C  2  3   ? 41.326 5.504   2.737   1.00 62.07  ?  35  PRO C CA    1 
ATOM   6741  C  C     . PRO C  2  3   ? 42.029 5.339   1.376   1.00 60.61  ?  35  PRO C C     1 
ATOM   6742  O  O     . PRO C  2  3   ? 42.373 4.214   1.002   1.00 58.75  ?  35  PRO C O     1 
ATOM   6743  C  CB    . PRO C  2  3   ? 39.812 5.285   2.613   1.00 61.16  ?  35  PRO C CB    1 
ATOM   6744  C  CG    . PRO C  2  3   ? 39.185 6.625   2.782   1.00 63.77  ?  35  PRO C CG    1 
ATOM   6745  C  CD    . PRO C  2  3   ? 40.247 7.649   3.092   1.00 67.19  ?  35  PRO C CD    1 
ATOM   6746  N  N     . ALA C  2  4   ? 42.224 6.432   0.639   1.00 61.07  ?  36  ALA C N     1 
ATOM   6747  C  CA    . ALA C  2  4   ? 43.144 6.436   -0.507  1.00 61.47  ?  36  ALA C CA    1 
ATOM   6748  C  C     . ALA C  2  4   ? 43.954 7.744   -0.518  1.00 62.93  ?  36  ALA C C     1 
ATOM   6749  O  O     . ALA C  2  4   ? 43.430 8.816   -0.178  1.00 66.18  ?  36  ALA C O     1 
ATOM   6750  C  CB    . ALA C  2  4   ? 42.398 6.238   -1.824  1.00 59.06  ?  36  ALA C CB    1 
ATOM   6751  N  N     . ILE C  2  5   ? 45.235 7.625   -0.881  1.00 60.06  ?  37  ILE C N     1 
ATOM   6752  C  CA    . ILE C  2  5   ? 46.180 8.747   -0.963  1.00 58.05  ?  37  ILE C CA    1 
ATOM   6753  C  C     . ILE C  2  5   ? 46.157 9.339   -2.370  1.00 53.62  ?  37  ILE C C     1 
ATOM   6754  O  O     . ILE C  2  5   ? 46.318 8.614   -3.366  1.00 47.92  ?  37  ILE C O     1 
ATOM   6755  C  CB    . ILE C  2  5   ? 47.647 8.294   -0.655  1.00 59.64  ?  37  ILE C CB    1 
ATOM   6756  C  CG1   . ILE C  2  5   ? 47.773 7.749   0.781   1.00 59.90  ?  37  ILE C CG1   1 
ATOM   6757  C  CG2   . ILE C  2  5   ? 48.660 9.413   -0.915  1.00 56.37  ?  37  ILE C CG2   1 
ATOM   6758  C  CD1   . ILE C  2  5   ? 47.268 8.680   1.864   1.00 59.20  ?  37  ILE C CD1   1 
ATOM   6759  N  N     . GLY C  2  6   ? 45.965 10.657  -2.435  1.00 49.60  ?  38  GLY C N     1 
ATOM   6760  C  CA    . GLY C  2  6   ? 46.172 11.416  -3.662  1.00 45.95  ?  38  GLY C CA    1 
ATOM   6761  C  C     . GLY C  2  6   ? 47.628 11.833  -3.790  1.00 44.06  ?  38  GLY C C     1 
ATOM   6762  O  O     . GLY C  2  6   ? 48.265 12.190  -2.791  1.00 42.51  ?  38  GLY C O     1 
ATOM   6763  N  N     . GLN C  2  7   ? 48.152 11.791  -5.019  1.00 41.94  ?  39  GLN C N     1 
ATOM   6764  C  CA    . GLN C  2  7   ? 49.529 12.214  -5.312  1.00 38.62  ?  39  GLN C CA    1 
ATOM   6765  C  C     . GLN C  2  7   ? 49.617 13.042  -6.579  1.00 36.99  ?  39  GLN C C     1 
ATOM   6766  O  O     . GLN C  2  7   ? 48.972 12.756  -7.592  1.00 33.17  ?  39  GLN C O     1 
ATOM   6767  C  CB    . GLN C  2  7   ? 50.471 11.018  -5.458  1.00 38.89  ?  39  GLN C CB    1 
ATOM   6768  C  CG    . GLN C  2  7   ? 50.525 10.116  -4.232  1.00 40.23  ?  39  GLN C CG    1 
ATOM   6769  C  CD    . GLN C  2  7   ? 51.573 9.004   -4.314  1.00 40.29  ?  39  GLN C CD    1 
ATOM   6770  O  OE1   . GLN C  2  7   ? 51.962 8.546   -5.395  1.00 40.05  ?  39  GLN C OE1   1 
ATOM   6771  N  NE2   . GLN C  2  7   ? 52.023 8.556   -3.152  1.00 40.89  ?  39  GLN C NE2   1 
ATOM   6772  N  N     . PHE C  2  8   ? 50.438 14.076  -6.499  1.00 37.69  ?  40  PHE C N     1 
ATOM   6773  C  CA    . PHE C  2  8   ? 50.834 14.833  -7.665  1.00 38.06  ?  40  PHE C CA    1 
ATOM   6774  C  C     . PHE C  2  8   ? 52.302 15.242  -7.593  1.00 36.68  ?  40  PHE C C     1 
ATOM   6775  O  O     . PHE C  2  8   ? 52.842 15.453  -6.509  1.00 36.01  ?  40  PHE C O     1 
ATOM   6776  C  CB    . PHE C  2  8   ? 49.911 16.035  -7.867  1.00 38.28  ?  40  PHE C CB    1 
ATOM   6777  C  CG    . PHE C  2  8   ? 49.965 17.046  -6.780  1.00 37.32  ?  40  PHE C CG    1 
ATOM   6778  C  CD1   . PHE C  2  8   ? 49.237 16.862  -5.631  1.00 38.24  ?  40  PHE C CD1   1 
ATOM   6779  C  CD2   . PHE C  2  8   ? 50.700 18.210  -6.939  1.00 37.69  ?  40  PHE C CD2   1 
ATOM   6780  C  CE1   . PHE C  2  8   ? 49.265 17.805  -4.616  1.00 40.92  ?  40  PHE C CE1   1 
ATOM   6781  C  CE2   . PHE C  2  8   ? 50.719 19.169  -5.952  1.00 40.28  ?  40  PHE C CE2   1 
ATOM   6782  C  CZ    . PHE C  2  8   ? 50.003 18.963  -4.779  1.00 42.56  ?  40  PHE C CZ    1 
ATOM   6783  N  N     . TRP C  2  9   ? 52.935 15.328  -8.768  1.00 37.74  ?  41  TRP C N     1 
ATOM   6784  C  CA    . TRP C  2  9   ? 54.358 15.725  -8.909  1.00 36.83  ?  41  TRP C CA    1 
ATOM   6785  C  C     . TRP C  2  9   ? 54.502 17.241  -8.985  1.00 33.82  ?  41  TRP C C     1 
ATOM   6786  O  O     . TRP C  2  9   ? 53.524 17.959  -9.200  1.00 32.23  ?  41  TRP C O     1 
ATOM   6787  C  CB    . TRP C  2  9   ? 55.008 15.092  -10.160 1.00 38.21  ?  41  TRP C CB    1 
ATOM   6788  C  CG    . TRP C  2  9   ? 55.073 13.599  -10.113 1.00 37.57  ?  41  TRP C CG    1 
ATOM   6789  C  CD1   . TRP C  2  9   ? 54.197 12.707  -10.689 1.00 38.22  ?  41  TRP C CD1   1 
ATOM   6790  C  CD2   . TRP C  2  9   ? 56.061 12.824  -9.446  1.00 37.38  ?  41  TRP C CD2   1 
ATOM   6791  N  NE1   . TRP C  2  9   ? 54.590 11.423  -10.410 1.00 39.71  ?  41  TRP C NE1   1 
ATOM   6792  C  CE2   . TRP C  2  9   ? 55.729 11.465  -9.644  1.00 39.01  ?  41  TRP C CE2   1 
ATOM   6793  C  CE3   . TRP C  2  9   ? 57.203 13.143  -8.706  1.00 36.67  ?  41  TRP C CE3   1 
ATOM   6794  C  CZ2   . TRP C  2  9   ? 56.501 10.428  -9.118  1.00 38.32  ?  41  TRP C CZ2   1 
ATOM   6795  C  CZ3   . TRP C  2  9   ? 57.972 12.115  -8.192  1.00 37.49  ?  41  TRP C CZ3   1 
ATOM   6796  C  CH2   . TRP C  2  9   ? 57.616 10.774  -8.395  1.00 38.57  ?  41  TRP C CH2   1 
ATOM   6797  N  N     . HIS C  2  10  ? 55.725 17.711  -8.764  1.00 32.23  ?  42  HIS C N     1 
ATOM   6798  C  CA    . HIS C  2  10  ? 56.055 19.142  -8.843  1.00 32.22  ?  42  HIS C CA    1 
ATOM   6799  C  C     . HIS C  2  10  ? 57.458 19.212  -9.388  1.00 33.13  ?  42  HIS C C     1 
ATOM   6800  O  O     . HIS C  2  10  ? 58.432 18.857  -8.690  1.00 33.11  ?  42  HIS C O     1 
ATOM   6801  C  CB    . HIS C  2  10  ? 55.972 19.873  -7.480  1.00 30.12  ?  42  HIS C CB    1 
ATOM   6802  C  CG    . HIS C  2  10  ? 56.303 21.343  -7.534  1.00 26.61  ?  42  HIS C CG    1 
ATOM   6803  N  ND1   . HIS C  2  10  ? 56.040 22.195  -6.486  1.00 24.61  ?  42  HIS C ND1   1 
ATOM   6804  C  CD2   . HIS C  2  10  ? 56.879 22.100  -8.497  1.00 24.95  ?  42  HIS C CD2   1 
ATOM   6805  C  CE1   . HIS C  2  10  ? 56.437 23.413  -6.802  1.00 24.35  ?  42  HIS C CE1   1 
ATOM   6806  N  NE2   . HIS C  2  10  ? 56.949 23.382  -8.016  1.00 24.12  ?  42  HIS C NE2   1 
ATOM   6807  N  N     . VAL C  2  11  ? 57.528 19.648  -10.647 1.00 33.32  ?  43  VAL C N     1 
ATOM   6808  C  CA    . VAL C  2  11  ? 58.777 19.914  -11.335 1.00 33.11  ?  43  VAL C CA    1 
ATOM   6809  C  C     . VAL C  2  11  ? 58.876 21.429  -11.514 1.00 34.56  ?  43  VAL C C     1 
ATOM   6810  O  O     . VAL C  2  11  ? 57.873 22.120  -11.661 1.00 37.00  ?  43  VAL C O     1 
ATOM   6811  C  CB    . VAL C  2  11  ? 58.859 19.154  -12.666 1.00 32.37  ?  43  VAL C CB    1 
ATOM   6812  C  CG1   . VAL C  2  11  ? 58.443 17.693  -12.446 1.00 31.65  ?  43  VAL C CG1   1 
ATOM   6813  C  CG2   . VAL C  2  11  ? 58.024 19.843  -13.753 1.00 32.56  ?  43  VAL C CG2   1 
ATOM   6814  N  N     . THR C  2  12  ? 60.081 21.956  -11.420 1.00 33.89  ?  44  THR C N     1 
ATOM   6815  C  CA    . THR C  2  12  ? 60.268 23.385  -11.515 1.00 32.92  ?  44  THR C CA    1 
ATOM   6816  C  C     . THR C  2  12  ? 61.663 23.623  -12.042 1.00 34.41  ?  44  THR C C     1 
ATOM   6817  O  O     . THR C  2  12  ? 62.520 22.713  -11.972 1.00 34.17  ?  44  THR C O     1 
ATOM   6818  C  CB    . THR C  2  12  ? 60.108 24.105  -10.159 1.00 32.88  ?  44  THR C CB    1 
ATOM   6819  O  OG1   . THR C  2  12  ? 60.220 25.531  -10.342 1.00 31.16  ?  44  THR C OG1   1 
ATOM   6820  C  CG2   . THR C  2  12  ? 61.168 23.639  -9.122  1.00 32.94  ?  44  THR C CG2   1 
ATOM   6821  N  N     . ASP C  2  13  ? 61.847 24.836  -12.588 1.00 33.78  ?  45  ASP C N     1 
ATOM   6822  C  CA    . ASP C  2  13  ? 63.140 25.383  -13.032 1.00 32.42  ?  45  ASP C CA    1 
ATOM   6823  C  C     . ASP C  2  13  ? 63.950 24.343  -13.819 1.00 32.09  ?  45  ASP C C     1 
ATOM   6824  O  O     . ASP C  2  13  ? 65.068 23.919  -13.415 1.00 29.09  ?  45  ASP C O     1 
ATOM   6825  C  CB    . ASP C  2  13  ? 63.894 25.987  -11.821 1.00 30.57  ?  45  ASP C CB    1 
ATOM   6826  C  CG    . ASP C  2  13  ? 63.089 27.089  -11.132 1.00 27.65  ?  45  ASP C CG    1 
ATOM   6827  O  OD1   . ASP C  2  13  ? 62.447 26.798  -10.099 1.00 26.54  ?  45  ASP C OD1   1 
ATOM   6828  O  OD2   . ASP C  2  13  ? 63.070 28.224  -11.652 1.00 23.91  -1 45  ASP C OD2   1 
ATOM   6829  N  N     . LEU C  2  14  ? 63.338 23.929  -14.937 1.00 34.10  ?  46  LEU C N     1 
ATOM   6830  C  CA    . LEU C  2  14  ? 63.891 22.863  -15.799 1.00 35.56  ?  46  LEU C CA    1 
ATOM   6831  C  C     . LEU C  2  14  ? 65.197 23.407  -16.436 1.00 35.68  ?  46  LEU C C     1 
ATOM   6832  O  O     . LEU C  2  14  ? 66.228 22.709  -16.415 1.00 35.56  ?  46  LEU C O     1 
ATOM   6833  C  CB    . LEU C  2  14  ? 62.839 22.322  -16.828 1.00 35.12  ?  46  LEU C CB    1 
ATOM   6834  C  CG    . LEU C  2  14  ? 61.538 21.605  -16.349 1.00 33.72  ?  46  LEU C CG    1 
ATOM   6835  C  CD1   . LEU C  2  14  ? 60.519 21.352  -17.439 1.00 31.90  ?  46  LEU C CD1   1 
ATOM   6836  C  CD2   . LEU C  2  14  ? 61.854 20.272  -15.725 1.00 33.84  ?  46  LEU C CD2   1 
ATOM   6837  N  N     . HIS C  2  15  ? 65.156 24.676  -16.888 1.00 33.98  ?  47  HIS C N     1 
ATOM   6838  C  CA    . HIS C  2  15  ? 66.327 25.423  -17.391 1.00 33.87  ?  47  HIS C CA    1 
ATOM   6839  C  C     . HIS C  2  15  ? 67.223 24.593  -18.309 1.00 33.90  ?  47  HIS C C     1 
ATOM   6840  O  O     . HIS C  2  15  ? 68.391 24.256  -17.935 1.00 29.94  ?  47  HIS C O     1 
ATOM   6841  C  CB    . HIS C  2  15  ? 67.197 25.973  -16.247 1.00 35.28  ?  47  HIS C CB    1 
ATOM   6842  C  CG    . HIS C  2  15  ? 66.642 27.184  -15.543 1.00 36.01  ?  47  HIS C CG    1 
ATOM   6843  N  ND1   . HIS C  2  15  ? 66.228 28.314  -16.213 1.00 36.13  ?  47  HIS C ND1   1 
ATOM   6844  C  CD2   . HIS C  2  15  ? 66.517 27.468  -14.222 1.00 35.74  ?  47  HIS C CD2   1 
ATOM   6845  C  CE1   . HIS C  2  15  ? 65.829 29.220  -15.341 1.00 35.58  ?  47  HIS C CE1   1 
ATOM   6846  N  NE2   . HIS C  2  15  ? 65.992 28.731  -14.126 1.00 35.63  ?  47  HIS C NE2   1 
ATOM   6847  N  N     . LEU C  2  16  ? 66.670 24.280  -19.494 1.00 33.68  ?  48  LEU C N     1 
ATOM   6848  C  CA    . LEU C  2  16  ? 67.370 23.487  -20.514 1.00 35.55  ?  48  LEU C CA    1 
ATOM   6849  C  C     . LEU C  2  16  ? 68.385 24.341  -21.243 1.00 36.82  ?  48  LEU C C     1 
ATOM   6850  O  O     . LEU C  2  16  ? 68.046 25.443  -21.700 1.00 37.55  ?  48  LEU C O     1 
ATOM   6851  C  CB    . LEU C  2  16  ? 66.397 22.896  -21.551 1.00 35.36  ?  48  LEU C CB    1 
ATOM   6852  C  CG    . LEU C  2  16  ? 66.988 22.329  -22.861 1.00 34.61  ?  48  LEU C CG    1 
ATOM   6853  C  CD1   . LEU C  2  16  ? 67.652 20.975  -22.672 1.00 34.85  ?  48  LEU C CD1   1 
ATOM   6854  C  CD2   . LEU C  2  16  ? 65.918 22.219  -23.926 1.00 35.24  ?  48  LEU C CD2   1 
ATOM   6855  N  N     . ASP C  2  17  ? 69.609 23.816  -21.356 1.00 36.79  ?  49  ASP C N     1 
ATOM   6856  C  CA    . ASP C  2  17  ? 70.659 24.410  -22.177 1.00 41.28  ?  49  ASP C CA    1 
ATOM   6857  C  C     . ASP C  2  17  ? 70.832 23.547  -23.431 1.00 42.23  ?  49  ASP C C     1 
ATOM   6858  O  O     . ASP C  2  17  ? 71.551 22.533  -23.408 1.00 41.41  ?  49  ASP C O     1 
ATOM   6859  C  CB    . ASP C  2  17  ? 71.971 24.484  -21.391 1.00 44.67  ?  49  ASP C CB    1 
ATOM   6860  C  CG    . ASP C  2  17  ? 72.980 25.481  -21.983 1.00 48.68  ?  49  ASP C CG    1 
ATOM   6861  O  OD1   . ASP C  2  17  ? 72.872 25.882  -23.166 1.00 49.32  ?  49  ASP C OD1   1 
ATOM   6862  O  OD2   . ASP C  2  17  ? 73.913 25.853  -21.239 1.00 51.37  -1 49  ASP C OD2   1 
ATOM   6863  N  N     . PRO C  2  18  ? 70.173 23.943  -24.538 1.00 42.48  ?  50  PRO C N     1 
ATOM   6864  C  CA    . PRO C  2  18  ? 70.280 23.154  -25.772 1.00 41.59  ?  50  PRO C CA    1 
ATOM   6865  C  C     . PRO C  2  18  ? 71.734 23.010  -26.268 1.00 40.99  ?  50  PRO C C     1 
ATOM   6866  O  O     . PRO C  2  18  ? 72.073 22.000  -26.862 1.00 41.56  ?  50  PRO C O     1 
ATOM   6867  C  CB    . PRO C  2  18  ? 69.425 23.937  -26.769 1.00 42.27  ?  50  PRO C CB    1 
ATOM   6868  C  CG    . PRO C  2  18  ? 68.576 24.854  -25.950 1.00 42.83  ?  50  PRO C CG    1 
ATOM   6869  C  CD    . PRO C  2  18  ? 69.381 25.171  -24.734 1.00 41.86  ?  50  PRO C CD    1 
ATOM   6870  N  N     . THR C  2  19  ? 72.574 24.011  -25.992 1.00 41.08  ?  51  THR C N     1 
ATOM   6871  C  CA    . THR C  2  19  ? 74.018 23.975  -26.258 1.00 37.59  ?  51  THR C CA    1 
ATOM   6872  C  C     . THR C  2  19  ? 74.773 22.802  -25.686 1.00 37.59  ?  51  THR C C     1 
ATOM   6873  O  O     . THR C  2  19  ? 75.744 22.364  -26.278 1.00 38.48  ?  51  THR C O     1 
ATOM   6874  C  CB    . THR C  2  19  ? 74.739 25.156  -25.594 1.00 36.44  ?  51  THR C CB    1 
ATOM   6875  O  OG1   . THR C  2  19  ? 74.076 26.391  -25.900 1.00 33.91  ?  51  THR C OG1   1 
ATOM   6876  C  CG2   . THR C  2  19  ? 76.212 25.200  -26.065 1.00 37.97  ?  51  THR C CG2   1 
ATOM   6877  N  N     . TYR C  2  20  ? 74.382 22.342  -24.502 1.00 39.11  ?  52  TYR C N     1 
ATOM   6878  C  CA    . TYR C  2  20  ? 75.238 21.429  -23.725 1.00 40.10  ?  52  TYR C CA    1 
ATOM   6879  C  C     . TYR C  2  20  ? 75.744 20.286  -24.585 1.00 41.79  ?  52  TYR C C     1 
ATOM   6880  O  O     . TYR C  2  20  ? 74.962 19.606  -25.236 1.00 42.69  ?  52  TYR C O     1 
ATOM   6881  C  CB    . TYR C  2  20  ? 74.518 20.852  -22.472 1.00 39.20  ?  52  TYR C CB    1 
ATOM   6882  C  CG    . TYR C  2  20  ? 75.475 20.260  -21.440 1.00 36.81  ?  52  TYR C CG    1 
ATOM   6883  C  CD1   . TYR C  2  20  ? 75.939 18.945  -21.544 1.00 36.55  ?  52  TYR C CD1   1 
ATOM   6884  C  CD2   . TYR C  2  20  ? 75.933 21.024  -20.376 1.00 36.22  ?  52  TYR C CD2   1 
ATOM   6885  C  CE1   . TYR C  2  20  ? 76.828 18.415  -20.616 1.00 35.11  ?  52  TYR C CE1   1 
ATOM   6886  C  CE2   . TYR C  2  20  ? 76.822 20.500  -19.446 1.00 35.56  ?  52  TYR C CE2   1 
ATOM   6887  C  CZ    . TYR C  2  20  ? 77.267 19.205  -19.576 1.00 35.00  ?  52  TYR C CZ    1 
ATOM   6888  O  OH    . TYR C  2  20  ? 78.149 18.732  -18.650 1.00 34.89  ?  52  TYR C OH    1 
ATOM   6889  N  N     . HIS C  2  21  ? 77.054 20.093  -24.599 1.00 44.94  ?  53  HIS C N     1 
ATOM   6890  C  CA    . HIS C  2  21  ? 77.621 18.843  -25.066 1.00 48.86  ?  53  HIS C CA    1 
ATOM   6891  C  C     . HIS C  2  21  ? 79.042 18.694  -24.514 1.00 48.48  ?  53  HIS C C     1 
ATOM   6892  O  O     . HIS C  2  21  ? 79.775 19.672  -24.403 1.00 49.14  ?  53  HIS C O     1 
ATOM   6893  C  CB    . HIS C  2  21  ? 77.606 18.785  -26.596 1.00 53.79  ?  53  HIS C CB    1 
ATOM   6894  C  CG    . HIS C  2  21  ? 78.548 19.750  -27.246 1.00 60.88  ?  53  HIS C CG    1 
ATOM   6895  N  ND1   . HIS C  2  21  ? 78.394 21.119  -27.158 1.00 63.17  ?  53  HIS C ND1   1 
ATOM   6896  C  CD2   . HIS C  2  21  ? 79.663 19.543  -27.988 1.00 65.09  ?  53  HIS C CD2   1 
ATOM   6897  C  CE1   . HIS C  2  21  ? 79.368 21.712  -27.825 1.00 64.98  ?  53  HIS C CE1   1 
ATOM   6898  N  NE2   . HIS C  2  21  ? 80.152 20.778  -28.335 1.00 67.93  ?  53  HIS C NE2   1 
ATOM   6899  N  N     . ILE C  2  22  ? 79.419 17.470  -24.157 1.00 48.49  ?  54  ILE C N     1 
ATOM   6900  C  CA    . ILE C  2  22  ? 80.789 17.170  -23.727 1.00 48.16  ?  54  ILE C CA    1 
ATOM   6901  C  C     . ILE C  2  22  ? 81.809 17.504  -24.832 1.00 51.20  ?  54  ILE C C     1 
ATOM   6902  O  O     . ILE C  2  22  ? 81.632 17.184  -26.019 1.00 50.65  ?  54  ILE C O     1 
ATOM   6903  C  CB    . ILE C  2  22  ? 80.934 15.686  -23.286 1.00 47.15  ?  54  ILE C CB    1 
ATOM   6904  C  CG1   . ILE C  2  22  ? 79.991 15.377  -22.114 1.00 46.95  ?  54  ILE C CG1   1 
ATOM   6905  C  CG2   . ILE C  2  22  ? 82.378 15.344  -22.918 1.00 46.03  ?  54  ILE C CG2   1 
ATOM   6906  C  CD1   . ILE C  2  22  ? 80.170 16.293  -20.917 1.00 47.16  ?  54  ILE C CD1   1 
ATOM   6907  N  N     . THR C  2  23  ? 82.878 18.173  -24.426 1.00 55.06  ?  55  THR C N     1 
ATOM   6908  C  CA    . THR C  2  23  ? 83.965 18.512  -25.332 1.00 57.99  ?  55  THR C CA    1 
ATOM   6909  C  C     . THR C  2  23  ? 85.204 18.874  -24.454 1.00 60.00  ?  55  THR C C     1 
ATOM   6910  O  O     . THR C  2  23  ? 85.059 19.139  -23.252 1.00 62.16  ?  55  THR C O     1 
ATOM   6911  C  CB    . THR C  2  23  ? 83.475 19.594  -26.348 1.00 57.21  ?  55  THR C CB    1 
ATOM   6912  O  OG1   . THR C  2  23  ? 83.882 19.237  -27.675 1.00 58.49  ?  55  THR C OG1   1 
ATOM   6913  C  CG2   . THR C  2  23  ? 83.931 21.014  -25.985 1.00 56.44  ?  55  THR C CG2   1 
ATOM   6914  N  N     . ASP C  2  24  ? 86.408 18.836  -25.025 1.00 60.76  ?  56  ASP C N     1 
ATOM   6915  C  CA    . ASP C  2  24  ? 87.656 19.045  -24.241 1.00 59.02  ?  56  ASP C CA    1 
ATOM   6916  C  C     . ASP C  2  24  ? 87.950 20.488  -23.825 1.00 55.31  ?  56  ASP C C     1 
ATOM   6917  O  O     . ASP C  2  24  ? 88.696 20.700  -22.874 1.00 57.11  ?  56  ASP C O     1 
ATOM   6918  C  CB    . ASP C  2  24  ? 88.865 18.522  -25.010 1.00 59.88  ?  56  ASP C CB    1 
ATOM   6919  C  CG    . ASP C  2  24  ? 88.754 17.062  -25.311 1.00 61.97  ?  56  ASP C CG    1 
ATOM   6920  O  OD1   . ASP C  2  24  ? 88.647 16.275  -24.338 1.00 61.51  ?  56  ASP C OD1   1 
ATOM   6921  O  OD2   . ASP C  2  24  ? 88.755 16.715  -26.515 1.00 63.24  -1 56  ASP C OD2   1 
ATOM   6922  N  N     . ASP C  2  25  ? 87.426 21.457  -24.577 1.00 51.12  ?  57  ASP C N     1 
ATOM   6923  C  CA    . ASP C  2  25  ? 87.446 22.867  -24.197 1.00 49.34  ?  57  ASP C CA    1 
ATOM   6924  C  C     . ASP C  2  25  ? 86.212 23.101  -23.323 1.00 51.18  ?  57  ASP C C     1 
ATOM   6925  O  O     . ASP C  2  25  ? 85.082 23.283  -23.819 1.00 48.88  ?  57  ASP C O     1 
ATOM   6926  C  CB    . ASP C  2  25  ? 87.423 23.763  -25.452 1.00 49.94  ?  57  ASP C CB    1 
ATOM   6927  C  CG    . ASP C  2  25  ? 87.516 25.277  -25.137 1.00 48.94  ?  57  ASP C CG    1 
ATOM   6928  O  OD1   . ASP C  2  25  ? 87.574 25.693  -23.951 1.00 45.37  ?  57  ASP C OD1   1 
ATOM   6929  O  OD2   . ASP C  2  25  ? 87.534 26.061  -26.112 1.00 47.31  -1 57  ASP C OD2   1 
ATOM   6930  N  N     . HIS C  2  26  ? 86.445 23.092  -22.011 1.00 51.76  ?  58  HIS C N     1 
ATOM   6931  C  CA    . HIS C  2  26  ? 85.374 23.212  -21.024 1.00 48.80  ?  58  HIS C CA    1 
ATOM   6932  C  C     . HIS C  2  26  ? 84.681 24.591  -21.048 1.00 48.96  ?  58  HIS C C     1 
ATOM   6933  O  O     . HIS C  2  26  ? 83.546 24.722  -20.562 1.00 54.18  ?  58  HIS C O     1 
ATOM   6934  C  CB    . HIS C  2  26  ? 85.896 22.854  -19.617 1.00 47.52  ?  58  HIS C CB    1 
ATOM   6935  C  CG    . HIS C  2  26  ? 86.081 21.378  -19.378 1.00 47.37  ?  58  HIS C CG    1 
ATOM   6936  N  ND1   . HIS C  2  26  ? 85.556 20.401  -20.208 1.00 46.28  ?  58  HIS C ND1   1 
ATOM   6937  C  CD2   . HIS C  2  26  ? 86.692 20.716  -18.362 1.00 45.74  ?  58  HIS C CD2   1 
ATOM   6938  C  CE1   . HIS C  2  26  ? 85.856 19.208  -19.728 1.00 45.83  ?  58  HIS C CE1   1 
ATOM   6939  N  NE2   . HIS C  2  26  ? 86.541 19.372  -18.607 1.00 47.98  ?  58  HIS C NE2   1 
ATOM   6940  N  N     . THR C  2  27  ? 85.323 25.600  -21.643 1.00 46.23  ?  59  THR C N     1 
ATOM   6941  C  CA    . THR C  2  27  ? 84.667 26.896  -21.852 1.00 46.33  ?  59  THR C CA    1 
ATOM   6942  C  C     . THR C  2  27  ? 83.541 26.820  -22.890 1.00 47.71  ?  59  THR C C     1 
ATOM   6943  O  O     . THR C  2  27  ? 82.657 27.679  -22.886 1.00 44.95  ?  59  THR C O     1 
ATOM   6944  C  CB    . THR C  2  27  ? 85.657 28.005  -22.276 1.00 45.48  ?  59  THR C CB    1 
ATOM   6945  O  OG1   . THR C  2  27  ? 86.276 27.646  -23.512 1.00 44.60  ?  59  THR C OG1   1 
ATOM   6946  C  CG2   . THR C  2  27  ? 86.740 28.231  -21.214 1.00 45.25  ?  59  THR C CG2   1 
ATOM   6947  N  N     . LYS C  2  28  ? 83.571 25.798  -23.761 1.00 52.52  ?  60  LYS C N     1 
ATOM   6948  C  CA    . LYS C  2  28  ? 82.556 25.617  -24.840 1.00 57.99  ?  60  LYS C CA    1 
ATOM   6949  C  C     . LYS C  2  28  ? 81.487 24.529  -24.580 1.00 58.46  ?  60  LYS C C     1 
ATOM   6950  O  O     . LYS C  2  28  ? 80.509 24.415  -25.355 1.00 62.39  ?  60  LYS C O     1 
ATOM   6951  C  CB    . LYS C  2  28  ? 83.226 25.331  -26.217 1.00 59.09  ?  60  LYS C CB    1 
ATOM   6952  C  CG    . LYS C  2  28  ? 84.008 26.477  -26.863 1.00 54.66  ?  60  LYS C CG    1 
ATOM   6953  C  CD    . LYS C  2  28  ? 83.199 27.763  -27.017 1.00 52.37  ?  60  LYS C CD    1 
ATOM   6954  C  CE    . LYS C  2  28  ? 84.134 28.930  -27.248 1.00 50.18  ?  60  LYS C CE    1 
ATOM   6955  N  NZ    . LYS C  2  28  ? 84.912 28.676  -28.486 1.00 50.31  1  60  LYS C NZ    1 
ATOM   6956  N  N     . VAL C  2  29  ? 81.661 23.749  -23.511 1.00 54.43  ?  61  VAL C N     1 
ATOM   6957  C  CA    . VAL C  2  29  ? 80.680 22.716  -23.134 1.00 51.13  ?  61  VAL C CA    1 
ATOM   6958  C  C     . VAL C  2  29  ? 79.240 23.267  -23.117 1.00 48.55  ?  61  VAL C C     1 
ATOM   6959  O  O     . VAL C  2  29  ? 78.315 22.632  -23.640 1.00 44.88  ?  61  VAL C O     1 
ATOM   6960  C  CB    . VAL C  2  29  ? 81.013 22.074  -21.766 1.00 49.97  ?  61  VAL C CB    1 
ATOM   6961  C  CG1   . VAL C  2  29  ? 79.850 21.235  -21.260 1.00 49.77  ?  61  VAL C CG1   1 
ATOM   6962  C  CG2   . VAL C  2  29  ? 82.262 21.209  -21.859 1.00 49.58  ?  61  VAL C CG2   1 
ATOM   6963  N  N     . CYS C  2  30  ? 79.052 24.450  -22.537 1.00 46.73  ?  62  CYS C N     1 
ATOM   6964  C  CA    . CYS C  2  30  ? 77.709 25.016  -22.455 1.00 46.66  ?  62  CYS C CA    1 
ATOM   6965  C  C     . CYS C  2  30  ? 77.715 26.538  -22.440 1.00 43.32  ?  62  CYS C C     1 
ATOM   6966  O  O     . CYS C  2  30  ? 78.534 27.157  -21.759 1.00 41.37  ?  62  CYS C O     1 
ATOM   6967  C  CB    . CYS C  2  30  ? 76.970 24.480  -21.214 1.00 46.40  ?  62  CYS C CB    1 
ATOM   6968  S  SG    . CYS C  2  30  ? 77.403 25.356  -19.697 1.00 45.65  ?  62  CYS C SG    1 
ATOM   6969  N  N     . ALA C  2  31  ? 76.759 27.110  -23.172 1.00 40.65  ?  63  ALA C N     1 
ATOM   6970  C  CA    . ALA C  2  31  ? 76.610 28.550  -23.305 1.00 41.51  ?  63  ALA C CA    1 
ATOM   6971  C  C     . ALA C  2  31  ? 76.247 29.243  -21.976 1.00 41.71  ?  63  ALA C C     1 
ATOM   6972  O  O     . ALA C  2  31  ? 76.677 30.382  -21.733 1.00 39.70  ?  63  ALA C O     1 
ATOM   6973  C  CB    . ALA C  2  31  ? 75.564 28.870  -24.364 1.00 41.23  ?  63  ALA C CB    1 
ATOM   6974  N  N     . SER C  2  32  ? 75.475 28.567  -21.119 1.00 41.23  ?  64  SER C N     1 
ATOM   6975  C  CA    . SER C  2  32  ? 75.083 29.148  -19.825 1.00 39.28  ?  64  SER C CA    1 
ATOM   6976  C  C     . SER C  2  32  ? 76.277 29.388  -18.892 1.00 38.14  ?  64  SER C C     1 
ATOM   6977  O  O     . SER C  2  32  ? 76.232 30.347  -18.113 1.00 36.51  ?  64  SER C O     1 
ATOM   6978  C  CB    . SER C  2  32  ? 74.016 28.307  -19.124 1.00 38.75  ?  64  SER C CB    1 
ATOM   6979  O  OG    . SER C  2  32  ? 74.458 26.979  -18.961 1.00 39.86  ?  64  SER C OG    1 
ATOM   6980  N  N     . SER C  2  33  ? 77.339 28.564  -18.981 1.00 34.96  ?  65  SER C N     1 
ATOM   6981  C  CA    . SER C  2  33  ? 78.556 28.813  -18.191 1.00 32.65  ?  65  SER C CA    1 
ATOM   6982  C  C     . SER C  2  33  ? 79.128 30.197  -18.524 1.00 33.55  ?  65  SER C C     1 
ATOM   6983  O  O     . SER C  2  33  ? 79.855 30.779  -17.726 1.00 34.65  ?  65  SER C O     1 
ATOM   6984  C  CB    . SER C  2  33  ? 79.626 27.739  -18.400 1.00 31.39  ?  65  SER C CB    1 
ATOM   6985  O  OG    . SER C  2  33  ? 80.656 28.167  -19.287 1.00 31.85  ?  65  SER C OG    1 
ATOM   6986  N  N     . LYS C  2  34  ? 78.797 30.713  -19.706 1.00 33.77  ?  66  LYS C N     1 
ATOM   6987  C  CA    . LYS C  2  34  ? 79.169 32.067  -20.124 1.00 34.66  ?  66  LYS C CA    1 
ATOM   6988  C  C     . LYS C  2  34  ? 80.693 32.204  -20.416 1.00 35.64  ?  66  LYS C C     1 
ATOM   6989  O  O     . LYS C  2  34  ? 81.279 33.283  -20.301 1.00 35.35  ?  66  LYS C O     1 
ATOM   6990  C  CB    . LYS C  2  34  ? 78.633 33.117  -19.124 1.00 33.82  ?  66  LYS C CB    1 
ATOM   6991  C  CG    . LYS C  2  34  ? 77.104 33.205  -19.049 1.00 33.88  ?  66  LYS C CG    1 
ATOM   6992  C  CD    . LYS C  2  34  ? 76.640 33.859  -17.744 1.00 33.67  ?  66  LYS C CD    1 
ATOM   6993  C  CE    . LYS C  2  34  ? 75.129 33.806  -17.535 1.00 33.27  ?  66  LYS C CE    1 
ATOM   6994  N  NZ    . LYS C  2  34  ? 74.726 32.533  -16.909 1.00 33.62  1  66  LYS C NZ    1 
ATOM   6995  N  N     . GLY C  2  35  ? 81.319 31.105  -20.831 1.00 35.43  ?  67  GLY C N     1 
ATOM   6996  C  CA    . GLY C  2  35  ? 82.708 31.143  -21.220 1.00 37.00  ?  67  GLY C CA    1 
ATOM   6997  C  C     . GLY C  2  35  ? 83.637 30.716  -20.105 1.00 38.54  ?  67  GLY C C     1 
ATOM   6998  O  O     . GLY C  2  35  ? 84.841 30.497  -20.335 1.00 38.94  ?  67  GLY C O     1 
ATOM   6999  N  N     . ALA C  2  36  ? 83.097 30.592  -18.896 1.00 39.74  ?  68  ALA C N     1 
ATOM   7000  C  CA    . ALA C  2  36  ? 83.845 29.979  -17.786 1.00 41.04  ?  68  ALA C CA    1 
ATOM   7001  C  C     . ALA C  2  36  ? 84.060 28.465  -18.010 1.00 38.07  ?  68  ALA C C     1 
ATOM   7002  O  O     . ALA C  2  36  ? 83.247 27.795  -18.669 1.00 35.35  ?  68  ALA C O     1 
ATOM   7003  C  CB    . ALA C  2  36  ? 83.131 30.229  -16.453 1.00 41.80  ?  68  ALA C CB    1 
ATOM   7004  N  N     . ASN C  2  37  ? 85.089 27.917  -17.410 1.00 36.31  ?  69  ASN C N     1 
ATOM   7005  C  CA    . ASN C  2  37  ? 85.320 26.510  -17.527 1.00 38.22  ?  69  ASN C CA    1 
ATOM   7006  C  C     . ASN C  2  37  ? 84.302 25.769  -16.686 1.00 38.60  ?  69  ASN C C     1 
ATOM   7007  O  O     . ASN C  2  37  ? 84.092 26.054  -15.537 1.00 35.65  ?  69  ASN C O     1 
ATOM   7008  C  CB    . ASN C  2  37  ? 86.737 26.158  -17.070 1.00 39.34  ?  69  ASN C CB    1 
ATOM   7009  C  CG    . ASN C  2  37  ? 87.672 25.834  -18.215 1.00 39.32  ?  69  ASN C CG    1 
ATOM   7010  O  OD1   . ASN C  2  37  ? 87.263 25.738  -19.334 1.00 38.58  ?  69  ASN C OD1   1 
ATOM   7011  N  ND2   . ASN C  2  37  ? 88.935 25.683  -17.923 1.00 41.72  ?  69  ASN C ND2   1 
ATOM   7012  N  N     . ALA C  2  38  ? 83.665 24.789  -17.278 1.00 42.83  ?  70  ALA C N     1 
ATOM   7013  C  CA    . ALA C  2  38  ? 82.698 23.981  -16.602 1.00 47.41  ?  70  ALA C CA    1 
ATOM   7014  C  C     . ALA C  2  38  ? 83.530 23.251  -15.598 1.00 50.46  ?  70  ALA C C     1 
ATOM   7015  O  O     . ALA C  2  38  ? 84.554 22.720  -15.931 1.00 54.44  ?  70  ALA C O     1 
ATOM   7016  C  CB    . ALA C  2  38  ? 82.073 23.019  -17.574 1.00 45.69  ?  70  ALA C CB    1 
ATOM   7017  N  N     . SER C  2  39  ? 83.106 23.224  -14.355 1.00 50.99  ?  71  SER C N     1 
ATOM   7018  C  CA    . SER C  2  39  ? 83.924 22.572  -13.324 1.00 51.21  ?  71  SER C CA    1 
ATOM   7019  C  C     . SER C  2  39  ? 84.396 21.158  -13.689 1.00 49.32  ?  71  SER C C     1 
ATOM   7020  O  O     . SER C  2  39  ? 85.600 20.916  -13.838 1.00 46.46  ?  71  SER C O     1 
ATOM   7021  C  CB    . SER C  2  39  ? 83.165 22.541  -11.994 1.00 51.78  ?  71  SER C CB    1 
ATOM   7022  O  OG    . SER C  2  39  ? 84.075 22.406  -10.925 1.00 51.88  ?  71  SER C OG    1 
ATOM   7023  N  N     . ASN C  2  40  ? 83.438 20.243  -13.835 1.00 48.24  ?  72  ASN C N     1 
ATOM   7024  C  CA    . ASN C  2  40  ? 83.714 18.833  -14.099 1.00 46.08  ?  72  ASN C CA    1 
ATOM   7025  C  C     . ASN C  2  40  ? 82.524 18.149  -14.777 1.00 42.08  ?  72  ASN C C     1 
ATOM   7026  O  O     . ASN C  2  40  ? 81.781 17.382  -14.173 1.00 39.01  ?  72  ASN C O     1 
ATOM   7027  C  CB    . ASN C  2  40  ? 84.062 18.123  -12.805 1.00 48.04  ?  72  ASN C CB    1 
ATOM   7028  C  CG    . ASN C  2  40  ? 84.393 16.673  -13.025 1.00 50.22  ?  72  ASN C CG    1 
ATOM   7029  O  OD1   . ASN C  2  40  ? 85.025 16.316  -14.021 1.00 51.82  ?  72  ASN C OD1   1 
ATOM   7030  N  ND2   . ASN C  2  40  ? 83.953 15.821  -12.108 1.00 52.20  ?  72  ASN C ND2   1 
ATOM   7031  N  N     . PRO C  2  41  ? 82.368 18.416  -16.062 1.00 41.06  ?  73  PRO C N     1 
ATOM   7032  C  CA    . PRO C  2  41  ? 81.112 18.151  -16.717 1.00 40.17  ?  73  PRO C CA    1 
ATOM   7033  C  C     . PRO C  2  41  ? 80.928 16.694  -17.034 1.00 40.08  ?  73  PRO C C     1 
ATOM   7034  O  O     . PRO C  2  41  ? 81.895 15.988  -17.287 1.00 40.15  ?  73  PRO C O     1 
ATOM   7035  C  CB    . PRO C  2  41  ? 81.234 18.945  -18.016 1.00 41.33  ?  73  PRO C CB    1 
ATOM   7036  C  CG    . PRO C  2  41  ? 82.710 19.008  -18.297 1.00 41.08  ?  73  PRO C CG    1 
ATOM   7037  C  CD    . PRO C  2  41  ? 83.441 18.772  -17.011 1.00 40.67  ?  73  PRO C CD    1 
ATOM   7038  N  N     . GLY C  2  42  ? 79.676 16.263  -17.034 1.00 41.28  ?  74  GLY C N     1 
ATOM   7039  C  CA    . GLY C  2  42  ? 79.327 14.900  -17.399 1.00 42.01  ?  74  GLY C CA    1 
ATOM   7040  C  C     . GLY C  2  42  ? 78.052 14.851  -18.216 1.00 43.07  ?  74  GLY C C     1 
ATOM   7041  O  O     . GLY C  2  42  ? 77.452 15.893  -18.509 1.00 41.26  ?  74  GLY C O     1 
ATOM   7042  N  N     . PRO C  2  43  ? 77.632 13.634  -18.609 1.00 45.63  ?  75  PRO C N     1 
ATOM   7043  C  CA    . PRO C  2  43  ? 76.443 13.488  -19.459 1.00 45.60  ?  75  PRO C CA    1 
ATOM   7044  C  C     . PRO C  2  43  ? 75.176 14.135  -18.884 1.00 45.84  ?  75  PRO C C     1 
ATOM   7045  O  O     . PRO C  2  43  ? 74.357 14.621  -19.653 1.00 47.33  ?  75  PRO C O     1 
ATOM   7046  C  CB    . PRO C  2  43  ? 76.270 11.964  -19.586 1.00 47.49  ?  75  PRO C CB    1 
ATOM   7047  C  CG    . PRO C  2  43  ? 77.194 11.342  -18.577 1.00 48.00  ?  75  PRO C CG    1 
ATOM   7048  C  CD    . PRO C  2  43  ? 78.281 12.339  -18.317 1.00 46.97  ?  75  PRO C CD    1 
ATOM   7049  N  N     . PHE C  2  44  ? 75.033 14.149  -17.553 1.00 47.24  ?  76  PHE C N     1 
ATOM   7050  C  CA    . PHE C  2  44  ? 73.842 14.706  -16.869 1.00 45.65  ?  76  PHE C CA    1 
ATOM   7051  C  C     . PHE C  2  44  ? 74.014 16.111  -16.292 1.00 41.69  ?  76  PHE C C     1 
ATOM   7052  O  O     . PHE C  2  44  ? 73.135 16.575  -15.561 1.00 39.22  ?  76  PHE C O     1 
ATOM   7053  C  CB    . PHE C  2  44  ? 73.405 13.772  -15.751 1.00 46.45  ?  76  PHE C CB    1 
ATOM   7054  C  CG    . PHE C  2  44  ? 73.282 12.357  -16.191 1.00 48.82  ?  76  PHE C CG    1 
ATOM   7055  C  CD1   . PHE C  2  44  ? 72.214 11.960  -16.975 1.00 50.89  ?  76  PHE C CD1   1 
ATOM   7056  C  CD2   . PHE C  2  44  ? 74.250 11.422  -15.858 1.00 50.43  ?  76  PHE C CD2   1 
ATOM   7057  C  CE1   . PHE C  2  44  ? 72.095 10.644  -17.399 1.00 51.23  ?  76  PHE C CE1   1 
ATOM   7058  C  CE2   . PHE C  2  44  ? 74.137 10.106  -16.285 1.00 50.90  ?  76  PHE C CE2   1 
ATOM   7059  C  CZ    . PHE C  2  44  ? 73.056 9.714   -17.050 1.00 49.23  ?  76  PHE C CZ    1 
ATOM   7060  N  N     . GLY C  2  45  ? 75.140 16.760  -16.607 1.00 39.00  ?  77  GLY C N     1 
ATOM   7061  C  CA    . GLY C  2  45  ? 75.348 18.181  -16.314 1.00 36.92  ?  77  GLY C CA    1 
ATOM   7062  C  C     . GLY C  2  45  ? 76.656 18.585  -15.632 1.00 35.30  ?  77  GLY C C     1 
ATOM   7063  O  O     . GLY C  2  45  ? 77.513 17.764  -15.281 1.00 33.52  ?  77  GLY C O     1 
ATOM   7064  N  N     . ASP C  2  46  ? 76.815 19.882  -15.469 1.00 33.63  ?  78  ASP C N     1 
ATOM   7065  C  CA    . ASP C  2  46  ? 77.846 20.393  -14.623 1.00 35.46  ?  78  ASP C CA    1 
ATOM   7066  C  C     . ASP C  2  46  ? 77.157 21.451  -13.759 1.00 38.06  ?  78  ASP C C     1 
ATOM   7067  O  O     . ASP C  2  46  ? 76.139 22.015  -14.181 1.00 38.09  ?  78  ASP C O     1 
ATOM   7068  C  CB    . ASP C  2  46  ? 78.967 20.992  -15.470 1.00 35.76  ?  78  ASP C CB    1 
ATOM   7069  C  CG    . ASP C  2  46  ? 80.156 21.477  -14.631 1.00 37.18  ?  78  ASP C CG    1 
ATOM   7070  O  OD1   . ASP C  2  46  ? 80.752 20.666  -13.902 1.00 36.06  ?  78  ASP C OD1   1 
ATOM   7071  O  OD2   . ASP C  2  46  ? 80.499 22.685  -14.698 1.00 38.40  -1 78  ASP C OD2   1 
ATOM   7072  N  N     . VAL C  2  47  ? 77.671 21.693  -12.543 1.00 38.62  ?  79  VAL C N     1 
ATOM   7073  C  CA    . VAL C  2  47  ? 77.365 22.949  -11.838 1.00 37.08  ?  79  VAL C CA    1 
ATOM   7074  C  C     . VAL C  2  47  ? 77.950 24.014  -12.778 1.00 36.77  ?  79  VAL C C     1 
ATOM   7075  O  O     . VAL C  2  47  ? 78.816 23.715  -13.593 1.00 39.73  ?  79  VAL C O     1 
ATOM   7076  C  CB    . VAL C  2  47  ? 77.958 23.020  -10.394 1.00 35.65  ?  79  VAL C CB    1 
ATOM   7077  C  CG1   . VAL C  2  47  ? 77.499 21.840  -9.554  1.00 35.51  ?  79  VAL C CG1   1 
ATOM   7078  C  CG2   . VAL C  2  47  ? 79.467 23.041  -10.413 1.00 36.66  ?  79  VAL C CG2   1 
ATOM   7079  N  N     . LEU C  2  48  ? 77.480 25.240  -12.745 1.00 35.64  ?  80  LEU C N     1 
ATOM   7080  C  CA    . LEU C  2  48  ? 77.985 26.211  -13.708 1.00 36.76  ?  80  LEU C CA    1 
ATOM   7081  C  C     . LEU C  2  48  ? 77.338 26.061  -15.086 1.00 35.65  ?  80  LEU C C     1 
ATOM   7082  O  O     . LEU C  2  48  ? 77.422 26.975  -15.889 1.00 35.79  ?  80  LEU C O     1 
ATOM   7083  C  CB    . LEU C  2  48  ? 79.510 26.047  -13.923 1.00 37.61  ?  80  LEU C CB    1 
ATOM   7084  C  CG    . LEU C  2  48  ? 80.476 26.993  -13.190 1.00 38.19  ?  80  LEU C CG    1 
ATOM   7085  C  CD1   . LEU C  2  48  ? 80.068 27.245  -11.759 1.00 38.82  ?  80  LEU C CD1   1 
ATOM   7086  C  CD2   . LEU C  2  48  ? 81.888 26.431  -13.238 1.00 38.94  ?  80  LEU C CD2   1 
ATOM   7087  N  N     . CYS C  2  49  ? 76.685 24.927  -15.337 1.00 35.44  ?  81  CYS C N     1 
ATOM   7088  C  CA    . CYS C  2  49  ? 76.001 24.647  -16.601 1.00 34.86  ?  81  CYS C CA    1 
ATOM   7089  C  C     . CYS C  2  49  ? 74.569 24.270  -16.331 1.00 32.37  ?  81  CYS C C     1 
ATOM   7090  O  O     . CYS C  2  49  ? 74.283 23.349  -15.595 1.00 30.34  ?  81  CYS C O     1 
ATOM   7091  C  CB    . CYS C  2  49  ? 76.619 23.487  -17.383 1.00 37.39  ?  81  CYS C CB    1 
ATOM   7092  S  SG    . CYS C  2  49  ? 78.071 23.910  -18.377 1.00 42.71  ?  81  CYS C SG    1 
ATOM   7093  N  N     . ASP C  2  50  ? 73.664 24.975  -16.964 1.00 32.29  ?  82  ASP C N     1 
ATOM   7094  C  CA    . ASP C  2  50  ? 72.285 24.601  -16.910 1.00 34.23  ?  82  ASP C CA    1 
ATOM   7095  C  C     . ASP C  2  50  ? 72.071 23.230  -17.490 1.00 33.39  ?  82  ASP C C     1 
ATOM   7096  O  O     . ASP C  2  50  ? 73.006 22.640  -18.014 1.00 30.02  ?  82  ASP C O     1 
ATOM   7097  C  CB    . ASP C  2  50  ? 71.463 25.575  -17.729 1.00 38.11  ?  82  ASP C CB    1 
ATOM   7098  C  CG    . ASP C  2  50  ? 70.834 26.629  -16.878 1.00 41.30  ?  82  ASP C CG    1 
ATOM   7099  O  OD1   . ASP C  2  50  ? 70.172 26.230  -15.893 1.00 47.34  ?  82  ASP C OD1   1 
ATOM   7100  O  OD2   . ASP C  2  50  ? 70.990 27.834  -17.184 1.00 41.43  -1 82  ASP C OD2   1 
ATOM   7101  N  N     . SER C  2  51  ? 70.843 22.722  -17.378 1.00 35.58  ?  83  SER C N     1 
ATOM   7102  C  CA    . SER C  2  51  ? 70.559 21.308  -17.649 1.00 38.17  ?  83  SER C CA    1 
ATOM   7103  C  C     . SER C  2  51  ? 70.812 20.853  -19.080 1.00 40.49  ?  83  SER C C     1 
ATOM   7104  O  O     . SER C  2  51  ? 70.272 21.466  -19.997 1.00 42.03  ?  83  SER C O     1 
ATOM   7105  C  CB    . SER C  2  51  ? 69.087 21.033  -17.336 1.00 37.78  ?  83  SER C CB    1 
ATOM   7106  O  OG    . SER C  2  51  ? 68.671 21.701  -16.157 1.00 37.83  ?  83  SER C OG    1 
ATOM   7107  N  N     . PRO C  2  52  ? 71.634 19.790  -19.280 1.00 42.67  ?  84  PRO C N     1 
ATOM   7108  C  CA    . PRO C  2  52  ? 71.587 19.099  -20.579 1.00 41.96  ?  84  PRO C CA    1 
ATOM   7109  C  C     . PRO C  2  52  ? 70.260 18.383  -20.733 1.00 42.28  ?  84  PRO C C     1 
ATOM   7110  O  O     . PRO C  2  52  ? 69.659 17.985  -19.729 1.00 42.18  ?  84  PRO C O     1 
ATOM   7111  C  CB    . PRO C  2  52  ? 72.731 18.074  -20.505 1.00 41.56  ?  84  PRO C CB    1 
ATOM   7112  C  CG    . PRO C  2  52  ? 73.123 17.980  -19.072 1.00 41.88  ?  84  PRO C CG    1 
ATOM   7113  C  CD    . PRO C  2  52  ? 72.702 19.262  -18.403 1.00 43.12  ?  84  PRO C CD    1 
ATOM   7114  N  N     . TYR C  2  53  ? 69.802 18.219  -21.969 1.00 41.91  ?  85  TYR C N     1 
ATOM   7115  C  CA    . TYR C  2  53  ? 68.533 17.535  -22.208 1.00 42.00  ?  85  TYR C CA    1 
ATOM   7116  C  C     . TYR C  2  53  ? 68.437 16.210  -21.467 1.00 40.32  ?  85  TYR C C     1 
ATOM   7117  O  O     . TYR C  2  53  ? 67.395 15.850  -20.921 1.00 39.12  ?  85  TYR C O     1 
ATOM   7118  C  CB    . TYR C  2  53  ? 68.350 17.255  -23.690 1.00 43.95  ?  85  TYR C CB    1 
ATOM   7119  C  CG    . TYR C  2  53  ? 66.981 16.708  -24.006 1.00 45.20  ?  85  TYR C CG    1 
ATOM   7120  C  CD1   . TYR C  2  53  ? 65.848 17.522  -23.879 1.00 44.80  ?  85  TYR C CD1   1 
ATOM   7121  C  CD2   . TYR C  2  53  ? 66.808 15.382  -24.422 1.00 43.29  ?  85  TYR C CD2   1 
ATOM   7122  C  CE1   . TYR C  2  53  ? 64.587 17.038  -24.162 1.00 44.02  ?  85  TYR C CE1   1 
ATOM   7123  C  CE2   . TYR C  2  53  ? 65.545 14.891  -24.704 1.00 43.86  ?  85  TYR C CE2   1 
ATOM   7124  C  CZ    . TYR C  2  53  ? 64.440 15.730  -24.575 1.00 44.60  ?  85  TYR C CZ    1 
ATOM   7125  O  OH    . TYR C  2  53  ? 63.178 15.278  -24.854 1.00 45.64  ?  85  TYR C OH    1 
ATOM   7126  N  N     . GLN C  2  54  ? 69.546 15.494  -21.453 1.00 40.25  ?  86  GLN C N     1 
ATOM   7127  C  CA    . GLN C  2  54  ? 69.575 14.155  -20.925 1.00 42.19  ?  86  GLN C CA    1 
ATOM   7128  C  C     . GLN C  2  54  ? 69.302 14.074  -19.417 1.00 39.79  ?  86  GLN C C     1 
ATOM   7129  O  O     . GLN C  2  54  ? 68.892 13.020  -18.926 1.00 38.22  ?  86  GLN C O     1 
ATOM   7130  C  CB    . GLN C  2  54  ? 70.916 13.539  -21.254 1.00 45.60  ?  86  GLN C CB    1 
ATOM   7131  C  CG    . GLN C  2  54  ? 70.916 12.031  -21.255 1.00 51.89  ?  86  GLN C CG    1 
ATOM   7132  C  CD    . GLN C  2  54  ? 72.331 11.486  -21.330 1.00 58.91  ?  86  GLN C CD    1 
ATOM   7133  O  OE1   . GLN C  2  54  ? 72.593 10.322  -21.002 1.00 62.77  ?  86  GLN C OE1   1 
ATOM   7134  N  NE2   . GLN C  2  54  ? 73.261 12.334  -21.757 1.00 62.05  ?  86  GLN C NE2   1 
ATOM   7135  N  N     . LEU C  2  55  ? 69.535 15.164  -18.684 1.00 38.91  ?  87  LEU C N     1 
ATOM   7136  C  CA    . LEU C  2  55  ? 69.154 15.231  -17.251 1.00 38.73  ?  87  LEU C CA    1 
ATOM   7137  C  C     . LEU C  2  55  ? 67.654 15.497  -17.129 1.00 37.87  ?  87  LEU C C     1 
ATOM   7138  O  O     . LEU C  2  55  ? 66.978 14.858  -16.320 1.00 34.83  ?  87  LEU C O     1 
ATOM   7139  C  CB    . LEU C  2  55  ? 69.962 16.296  -16.468 1.00 38.88  ?  87  LEU C CB    1 
ATOM   7140  C  CG    . LEU C  2  55  ? 69.441 16.818  -15.103 1.00 38.70  ?  87  LEU C CG    1 
ATOM   7141  C  CD1   . LEU C  2  55  ? 69.881 15.946  -13.955 1.00 38.84  ?  87  LEU C CD1   1 
ATOM   7142  C  CD2   . LEU C  2  55  ? 69.922 18.223  -14.811 1.00 40.11  ?  87  LEU C CD2   1 
ATOM   7143  N  N     . ILE C  2  56  ? 67.143 16.434  -17.934 1.00 37.80  ?  88  ILE C N     1 
ATOM   7144  C  CA    . ILE C  2  56  ? 65.704 16.721  -17.967 1.00 37.77  ?  88  ILE C CA    1 
ATOM   7145  C  C     . ILE C  2  56  ? 64.942 15.438  -18.265 1.00 40.79  ?  88  ILE C C     1 
ATOM   7146  O  O     . ILE C  2  56  ? 63.899 15.140  -17.667 1.00 38.62  ?  88  ILE C O     1 
ATOM   7147  C  CB    . ILE C  2  56  ? 65.320 17.698  -19.079 1.00 35.41  ?  88  ILE C CB    1 
ATOM   7148  C  CG1   . ILE C  2  56  ? 66.161 18.971  -19.006 1.00 36.11  ?  88  ILE C CG1   1 
ATOM   7149  C  CG2   . ILE C  2  56  ? 63.827 17.999  -19.010 1.00 34.30  ?  88  ILE C CG2   1 
ATOM   7150  C  CD1   . ILE C  2  56  ? 65.983 19.746  -17.732 1.00 37.41  ?  88  ILE C CD1   1 
ATOM   7151  N  N     . LEU C  2  57  ? 65.499 14.687  -19.208 1.00 42.97  ?  89  LEU C N     1 
ATOM   7152  C  CA    . LEU C  2  57  ? 64.879 13.479  -19.687 1.00 46.67  ?  89  LEU C CA    1 
ATOM   7153  C  C     . LEU C  2  57  ? 64.846 12.360  -18.645 1.00 47.64  ?  89  LEU C C     1 
ATOM   7154  O  O     . LEU C  2  57  ? 63.822 11.684  -18.510 1.00 45.39  ?  89  LEU C O     1 
ATOM   7155  C  CB    . LEU C  2  57  ? 65.616 12.999  -20.933 1.00 47.54  ?  89  LEU C CB    1 
ATOM   7156  C  CG    . LEU C  2  57  ? 64.869 11.976  -21.780 1.00 46.62  ?  89  LEU C CG    1 
ATOM   7157  C  CD1   . LEU C  2  57  ? 63.545 12.548  -22.283 1.00 44.54  ?  89  LEU C CD1   1 
ATOM   7158  C  CD2   . LEU C  2  57  ? 65.794 11.582  -22.917 1.00 47.40  ?  89  LEU C CD2   1 
ATOM   7159  N  N     . SER C  2  58  ? 65.970 12.171  -17.941 1.00 49.28  ?  90  SER C N     1 
ATOM   7160  C  CA    . SER C  2  58  ? 66.119 11.128  -16.898 1.00 49.47  ?  90  SER C CA    1 
ATOM   7161  C  C     . SER C  2  58  ? 65.331 11.415  -15.618 1.00 50.77  ?  90  SER C C     1 
ATOM   7162  O  O     . SER C  2  58  ? 64.983 10.499  -14.884 1.00 54.26  ?  90  SER C O     1 
ATOM   7163  C  CB    . SER C  2  58  ? 67.584 10.959  -16.508 1.00 48.97  ?  90  SER C CB    1 
ATOM   7164  O  OG    . SER C  2  58  ? 67.978 11.951  -15.571 1.00 47.79  ?  90  SER C OG    1 
ATOM   7165  N  N     . ALA C  2  59  ? 65.106 12.691  -15.335 1.00 50.13  ?  91  ALA C N     1 
ATOM   7166  C  CA    . ALA C  2  59  ? 64.147 13.110  -14.325 1.00 49.86  ?  91  ALA C CA    1 
ATOM   7167  C  C     . ALA C  2  59  ? 62.726 12.615  -14.654 1.00 47.45  ?  91  ALA C C     1 
ATOM   7168  O  O     . ALA C  2  59  ? 62.051 12.033  -13.801 1.00 46.16  ?  91  ALA C O     1 
ATOM   7169  C  CB    . ALA C  2  59  ? 64.151 14.634  -14.223 1.00 52.36  ?  91  ALA C CB    1 
ATOM   7170  N  N     . PHE C  2  60  ? 62.273 12.878  -15.879 1.00 46.19  ?  92  PHE C N     1 
ATOM   7171  C  CA    . PHE C  2  60  ? 60.941 12.461  -16.324 1.00 46.20  ?  92  PHE C CA    1 
ATOM   7172  C  C     . PHE C  2  60  ? 60.838 10.926  -16.524 1.00 48.06  ?  92  PHE C C     1 
ATOM   7173  O  O     . PHE C  2  60  ? 59.726 10.373  -16.491 1.00 47.44  ?  92  PHE C O     1 
ATOM   7174  C  CB    . PHE C  2  60  ? 60.526 13.192  -17.626 1.00 45.39  ?  92  PHE C CB    1 
ATOM   7175  C  CG    . PHE C  2  60  ? 60.058 14.628  -17.436 1.00 45.28  ?  92  PHE C CG    1 
ATOM   7176  C  CD1   . PHE C  2  60  ? 59.146 14.981  -16.430 1.00 45.67  ?  92  PHE C CD1   1 
ATOM   7177  C  CD2   . PHE C  2  60  ? 60.479 15.622  -18.311 1.00 45.31  ?  92  PHE C CD2   1 
ATOM   7178  C  CE1   . PHE C  2  60  ? 58.697 16.293  -16.287 1.00 44.27  ?  92  PHE C CE1   1 
ATOM   7179  C  CE2   . PHE C  2  60  ? 60.031 16.930  -18.168 1.00 44.93  ?  92  PHE C CE2   1 
ATOM   7180  C  CZ    . PHE C  2  60  ? 59.145 17.267  -17.152 1.00 43.60  ?  92  PHE C CZ    1 
ATOM   7181  N  N     . ASP C  2  61  ? 61.976 10.251  -16.751 1.00 48.80  ?  93  ASP C N     1 
ATOM   7182  C  CA    . ASP C  2  61  ? 61.998 8.788   -16.944 1.00 50.55  ?  93  ASP C CA    1 
ATOM   7183  C  C     . ASP C  2  61  ? 61.893 8.065   -15.603 1.00 53.58  ?  93  ASP C C     1 
ATOM   7184  O  O     . ASP C  2  61  ? 61.261 7.005   -15.513 1.00 61.21  ?  93  ASP C O     1 
ATOM   7185  C  CB    . ASP C  2  61  ? 63.264 8.316   -17.682 1.00 50.21  ?  93  ASP C CB    1 
ATOM   7186  C  CG    . ASP C  2  61  ? 63.251 8.631   -19.191 1.00 50.44  ?  93  ASP C CG    1 
ATOM   7187  O  OD1   . ASP C  2  61  ? 62.173 8.890   -19.792 1.00 45.18  ?  93  ASP C OD1   1 
ATOM   7188  O  OD2   . ASP C  2  61  ? 64.362 8.596   -19.778 1.00 52.71  -1 93  ASP C OD2   1 
ATOM   7189  N  N     . PHE C  2  62  ? 62.529 8.626   -14.573 1.00 51.84  ?  94  PHE C N     1 
ATOM   7190  C  CA    . PHE C  2  62  ? 62.313 8.186   -13.187 1.00 48.40  ?  94  PHE C CA    1 
ATOM   7191  C  C     . PHE C  2  62  ? 60.823 8.288   -12.803 1.00 49.22  ?  94  PHE C C     1 
ATOM   7192  O  O     . PHE C  2  62  ? 60.274 7.303   -12.327 1.00 52.80  ?  94  PHE C O     1 
ATOM   7193  C  CB    . PHE C  2  62  ? 63.216 8.964   -12.205 1.00 45.25  ?  94  PHE C CB    1 
ATOM   7194  C  CG    . PHE C  2  62  ? 62.927 8.690   -10.753 1.00 43.14  ?  94  PHE C CG    1 
ATOM   7195  C  CD1   . PHE C  2  62  ? 63.499 7.602   -10.107 1.00 43.10  ?  94  PHE C CD1   1 
ATOM   7196  C  CD2   . PHE C  2  62  ? 62.074 9.527   -10.026 1.00 42.63  ?  94  PHE C CD2   1 
ATOM   7197  C  CE1   . PHE C  2  62  ? 63.223 7.352   -8.766  1.00 43.50  ?  94  PHE C CE1   1 
ATOM   7198  C  CE2   . PHE C  2  62  ? 61.788 9.284   -8.681  1.00 41.45  ?  94  PHE C CE2   1 
ATOM   7199  C  CZ    . PHE C  2  62  ? 62.365 8.197   -8.051  1.00 42.45  ?  94  PHE C CZ    1 
ATOM   7200  N  N     . ILE C  2  63  ? 60.165 9.437   -13.026 1.00 48.13  ?  95  ILE C N     1 
ATOM   7201  C  CA    . ILE C  2  63  ? 58.717 9.574   -12.713 1.00 49.40  ?  95  ILE C CA    1 
ATOM   7202  C  C     . ILE C  2  63  ? 57.852 8.514   -13.403 1.00 54.93  ?  95  ILE C C     1 
ATOM   7203  O  O     . ILE C  2  63  ? 56.877 8.034   -12.822 1.00 58.69  ?  95  ILE C O     1 
ATOM   7204  C  CB    . ILE C  2  63  ? 58.111 10.936  -13.112 1.00 44.44  ?  95  ILE C CB    1 
ATOM   7205  C  CG1   . ILE C  2  63  ? 58.693 12.054  -12.255 1.00 43.92  ?  95  ILE C CG1   1 
ATOM   7206  C  CG2   . ILE C  2  63  ? 56.582 10.905  -12.975 1.00 41.77  ?  95  ILE C CG2   1 
ATOM   7207  C  CD1   . ILE C  2  63  ? 58.343 13.449  -12.754 1.00 42.55  ?  95  ILE C CD1   1 
ATOM   7208  N  N     . LYS C  2  64  ? 58.187 8.185   -14.647 1.00 58.32  ?  96  LYS C N     1 
ATOM   7209  C  CA    . LYS C  2  64  ? 57.407 7.234   -15.441 1.00 60.20  ?  96  LYS C CA    1 
ATOM   7210  C  C     . LYS C  2  64  ? 57.627 5.818   -14.885 1.00 60.94  ?  96  LYS C C     1 
ATOM   7211  O  O     . LYS C  2  64  ? 56.679 5.091   -14.586 1.00 58.03  ?  96  LYS C O     1 
ATOM   7212  C  CB    . LYS C  2  64  ? 57.827 7.339   -16.909 1.00 60.24  ?  96  LYS C CB    1 
ATOM   7213  C  CG    . LYS C  2  64  ? 56.877 6.733   -17.926 1.00 61.54  ?  96  LYS C CG    1 
ATOM   7214  C  CD    . LYS C  2  64  ? 57.436 7.010   -19.315 1.00 64.53  ?  96  LYS C CD    1 
ATOM   7215  C  CE    . LYS C  2  64  ? 56.579 6.454   -20.440 1.00 65.92  ?  96  LYS C CE    1 
ATOM   7216  N  NZ    . LYS C  2  64  ? 57.198 5.255   -21.070 1.00 66.55  1  96  LYS C NZ    1 
ATOM   7217  N  N     . ASN C  2  65  ? 58.890 5.459   -14.703 1.00 63.59  ?  97  ASN C N     1 
ATOM   7218  C  CA    . ASN C  2  65  ? 59.256 4.177   -14.115 1.00 66.07  ?  97  ASN C CA    1 
ATOM   7219  C  C     . ASN C  2  65  ? 59.269 4.210   -12.584 1.00 69.31  ?  97  ASN C C     1 
ATOM   7220  O  O     . ASN C  2  65  ? 59.825 3.308   -11.951 1.00 75.68  ?  97  ASN C O     1 
ATOM   7221  C  CB    . ASN C  2  65  ? 60.653 3.765   -14.597 1.00 67.24  ?  97  ASN C CB    1 
ATOM   7222  C  CG    . ASN C  2  65  ? 60.687 3.433   -16.068 1.00 69.51  ?  97  ASN C CG    1 
ATOM   7223  O  OD1   . ASN C  2  65  ? 60.749 2.259   -16.453 1.00 69.45  ?  97  ASN C OD1   1 
ATOM   7224  N  ND2   . ASN C  2  65  ? 60.644 4.467   -16.907 1.00 71.57  ?  97  ASN C ND2   1 
ATOM   7225  N  N     . SER C  2  66  ? 58.681 5.235   -11.972 1.00 65.88  ?  98  SER C N     1 
ATOM   7226  C  CA    . SER C  2  66  ? 58.860 5.421   -10.537 1.00 61.53  ?  98  SER C CA    1 
ATOM   7227  C  C     . SER C  2  66  ? 58.297 4.226   -9.804  1.00 60.53  ?  98  SER C C     1 
ATOM   7228  O  O     . SER C  2  66  ? 58.985 3.612   -9.000  1.00 67.48  ?  98  SER C O     1 
ATOM   7229  C  CB    . SER C  2  66  ? 58.210 6.722   -10.037 1.00 57.53  ?  98  SER C CB    1 
ATOM   7230  O  OG    . SER C  2  66  ? 56.813 6.599   -9.846  1.00 54.67  ?  98  SER C OG    1 
ATOM   7231  N  N     . GLY C  2  67  ? 57.066 3.869   -10.137 1.00 59.01  ?  99  GLY C N     1 
ATOM   7232  C  CA    . GLY C  2  67  ? 56.290 2.937   -9.338  1.00 60.89  ?  99  GLY C CA    1 
ATOM   7233  C  C     . GLY C  2  67  ? 55.258 3.667   -8.492  1.00 60.15  ?  99  GLY C C     1 
ATOM   7234  O  O     . GLY C  2  67  ? 54.595 3.056   -7.669  1.00 67.86  ?  99  GLY C O     1 
ATOM   7235  N  N     . GLN C  2  68  ? 55.134 4.978   -8.677  1.00 56.79  ?  100 GLN C N     1 
ATOM   7236  C  CA    . GLN C  2  68  ? 54.095 5.761   -8.025  1.00 55.50  ?  100 GLN C CA    1 
ATOM   7237  C  C     . GLN C  2  68  ? 53.053 6.004   -9.084  1.00 54.20  ?  100 GLN C C     1 
ATOM   7238  O  O     . GLN C  2  68  ? 53.270 5.648   -10.232 1.00 56.83  ?  100 GLN C O     1 
ATOM   7239  C  CB    . GLN C  2  68  ? 54.648 7.097   -7.528  1.00 55.56  ?  100 GLN C CB    1 
ATOM   7240  C  CG    . GLN C  2  68  ? 55.877 6.988   -6.626  1.00 54.87  ?  100 GLN C CG    1 
ATOM   7241  C  CD    . GLN C  2  68  ? 55.560 6.746   -5.155  1.00 51.18  ?  100 GLN C CD    1 
ATOM   7242  O  OE1   . GLN C  2  68  ? 54.397 6.717   -4.735  1.00 42.74  ?  100 GLN C OE1   1 
ATOM   7243  N  NE2   . GLN C  2  68  ? 56.617 6.585   -4.356  1.00 51.97  ?  100 GLN C NE2   1 
ATOM   7244  N  N     . GLU C  2  69  ? 51.922 6.586   -8.707  1.00 54.11  ?  101 GLU C N     1 
ATOM   7245  C  CA    . GLU C  2  69  ? 50.943 7.054   -9.686  1.00 59.19  ?  101 GLU C CA    1 
ATOM   7246  C  C     . GLU C  2  69  ? 50.291 8.323   -9.149  1.00 55.09  ?  101 GLU C C     1 
ATOM   7247  O  O     . GLU C  2  69  ? 50.006 8.441   -7.957  1.00 53.24  ?  101 GLU C O     1 
ATOM   7248  C  CB    . GLU C  2  69  ? 49.921 5.953   -10.099 1.00 65.98  ?  101 GLU C CB    1 
ATOM   7249  C  CG    . GLU C  2  69  ? 48.646 5.805   -9.265  1.00 74.19  ?  101 GLU C CG    1 
ATOM   7250  C  CD    . GLU C  2  69  ? 48.891 5.315   -7.836  1.00 81.70  ?  101 GLU C CD    1 
ATOM   7251  O  OE1   . GLU C  2  69  ? 50.016 4.861   -7.520  1.00 85.13  ?  101 GLU C OE1   1 
ATOM   7252  O  OE2   . GLU C  2  69  ? 47.942 5.376   -7.018  1.00 88.34  -1 101 GLU C OE2   1 
ATOM   7253  N  N     . ALA C  2  70  ? 50.084 9.280   -10.039 1.00 51.61  ?  102 ALA C N     1 
ATOM   7254  C  CA    . ALA C  2  70  ? 49.727 10.623  -9.639  1.00 48.55  ?  102 ALA C CA    1 
ATOM   7255  C  C     . ALA C  2  70  ? 48.478 11.010  -10.365 1.00 45.55  ?  102 ALA C C     1 
ATOM   7256  O  O     . ALA C  2  70  ? 48.291 10.618  -11.502 1.00 44.81  ?  102 ALA C O     1 
ATOM   7257  C  CB    . ALA C  2  70  ? 50.850 11.586  -9.996  1.00 48.39  ?  102 ALA C CB    1 
ATOM   7258  N  N     . SER C  2  71  ? 47.639 11.798  -9.711  1.00 43.83  ?  103 SER C N     1 
ATOM   7259  C  CA    . SER C  2  71  ? 46.454 12.363  -10.350 1.00 44.52  ?  103 SER C CA    1 
ATOM   7260  C  C     . SER C  2  71  ? 46.747 13.579  -11.250 1.00 43.14  ?  103 SER C C     1 
ATOM   7261  O  O     . SER C  2  71  ? 45.962 13.885  -12.151 1.00 40.25  ?  103 SER C O     1 
ATOM   7262  C  CB    . SER C  2  71  ? 45.443 12.747  -9.279  1.00 46.92  ?  103 SER C CB    1 
ATOM   7263  O  OG    . SER C  2  71  ? 44.871 11.583  -8.704  1.00 49.27  ?  103 SER C OG    1 
ATOM   7264  N  N     . PHE C  2  72  ? 47.846 14.284  -10.964 1.00 44.50  ?  104 PHE C N     1 
ATOM   7265  C  CA    . PHE C  2  72  ? 48.352 15.384  -11.808 1.00 43.23  ?  104 PHE C CA    1 
ATOM   7266  C  C     . PHE C  2  72  ? 49.817 15.740  -11.521 1.00 40.67  ?  104 PHE C C     1 
ATOM   7267  O  O     . PHE C  2  72  ? 50.535 15.010  -10.843 1.00 38.38  ?  104 PHE C O     1 
ATOM   7268  C  CB    . PHE C  2  72  ? 47.455 16.628  -11.704 1.00 45.07  ?  104 PHE C CB    1 
ATOM   7269  C  CG    . PHE C  2  72  ? 47.360 17.199  -10.335 1.00 46.36  ?  104 PHE C CG    1 
ATOM   7270  C  CD1   . PHE C  2  72  ? 46.523 16.614  -9.383  1.00 48.10  ?  104 PHE C CD1   1 
ATOM   7271  C  CD2   . PHE C  2  72  ? 48.070 18.332  -9.999  1.00 49.68  ?  104 PHE C CD2   1 
ATOM   7272  C  CE1   . PHE C  2  72  ? 46.415 17.135  -8.102  1.00 49.43  ?  104 PHE C CE1   1 
ATOM   7273  C  CE2   . PHE C  2  72  ? 47.963 18.867  -8.715  1.00 54.51  ?  104 PHE C CE2   1 
ATOM   7274  C  CZ    . PHE C  2  72  ? 47.135 18.265  -7.766  1.00 52.28  ?  104 PHE C CZ    1 
ATOM   7275  N  N     . MET C  2  73  ? 50.258 16.845  -12.106 1.00 41.68  ?  105 MET C N     1 
ATOM   7276  C  CA    . MET C  2  73  ? 51.624 17.351  -11.992 1.00 39.21  ?  105 MET C CA    1 
ATOM   7277  C  C     . MET C  2  73  ? 51.467 18.851  -11.966 1.00 35.50  ?  105 MET C C     1 
ATOM   7278  O  O     . MET C  2  73  ? 50.496 19.395  -12.446 1.00 32.56  ?  105 MET C O     1 
ATOM   7279  C  CB    . MET C  2  73  ? 52.505 16.895  -13.195 1.00 39.88  ?  105 MET C CB    1 
ATOM   7280  C  CG    . MET C  2  73  ? 53.951 17.425  -13.206 1.00 41.13  ?  105 MET C CG    1 
ATOM   7281  S  SD    . MET C  2  73  ? 55.114 16.813  -14.470 1.00 39.14  ?  105 MET C SD    1 
ATOM   7282  C  CE    . MET C  2  73  ? 55.639 15.321  -13.650 1.00 39.99  ?  105 MET C CE    1 
ATOM   7283  N  N     . ILE C  2  74  ? 52.418 19.513  -11.362 1.00 36.04  ?  106 ILE C N     1 
ATOM   7284  C  CA    A ILE C  2  74  ? 52.454 20.958  -11.261 0.50 38.41  ?  106 ILE C CA    1 
ATOM   7285  C  CA    B ILE C  2  74  ? 52.418 20.959  -11.386 0.50 37.63  ?  106 ILE C CA    1 
ATOM   7286  C  C     . ILE C  2  74  ? 53.797 21.420  -11.824 1.00 41.29  ?  106 ILE C C     1 
ATOM   7287  O  O     . ILE C  2  74  ? 54.841 21.035  -11.262 1.00 41.97  ?  106 ILE C O     1 
ATOM   7288  C  CB    A ILE C  2  74  ? 52.378 21.336  -9.772  0.50 38.49  ?  106 ILE C CB    1 
ATOM   7289  C  CB    B ILE C  2  74  ? 51.948 21.598  -10.063 0.50 36.56  ?  106 ILE C CB    1 
ATOM   7290  C  CG1   A ILE C  2  74  ? 50.946 21.207  -9.265  0.50 38.41  ?  106 ILE C CG1   1 
ATOM   7291  C  CG1   B ILE C  2  74  ? 52.765 21.124  -8.854  0.50 36.92  ?  106 ILE C CG1   1 
ATOM   7292  C  CG2   A ILE C  2  74  ? 52.944 22.716  -9.505  0.50 39.58  ?  106 ILE C CG2   1 
ATOM   7293  C  CG2   B ILE C  2  74  ? 50.479 21.286  -9.848  0.50 36.11  ?  106 ILE C CG2   1 
ATOM   7294  C  CD1   A ILE C  2  74  ? 49.903 21.581  -10.285 0.50 38.02  ?  106 ILE C CD1   1 
ATOM   7295  C  CD1   B ILE C  2  74  ? 52.406 21.854  -7.575  0.50 37.19  ?  106 ILE C CD1   1 
ATOM   7296  N  N     . TRP C  2  75  ? 53.811 22.221  -12.887 1.00 42.87  ?  107 TRP C N     1 
ATOM   7297  C  CA    . TRP C  2  75  ? 55.093 22.606  -13.453 1.00 45.77  ?  107 TRP C CA    1 
ATOM   7298  C  C     . TRP C  2  75  ? 55.190 24.128  -13.440 1.00 48.03  ?  107 TRP C C     1 
ATOM   7299  O  O     . TRP C  2  75  ? 54.452 24.811  -14.121 1.00 54.39  ?  107 TRP C O     1 
ATOM   7300  C  CB    . TRP C  2  75  ? 55.269 21.949  -14.817 1.00 45.54  ?  107 TRP C CB    1 
ATOM   7301  C  CG    . TRP C  2  75  ? 56.432 22.409  -15.610 1.00 48.11  ?  107 TRP C CG    1 
ATOM   7302  C  CD1   . TRP C  2  75  ? 57.676 22.711  -15.159 1.00 49.24  ?  107 TRP C CD1   1 
ATOM   7303  C  CD2   . TRP C  2  75  ? 56.460 22.593  -17.030 1.00 51.75  ?  107 TRP C CD2   1 
ATOM   7304  N  NE1   . TRP C  2  75  ? 58.482 23.099  -16.212 1.00 51.57  ?  107 TRP C NE1   1 
ATOM   7305  C  CE2   . TRP C  2  75  ? 57.753 23.027  -17.371 1.00 51.29  ?  107 TRP C CE2   1 
ATOM   7306  C  CE3   . TRP C  2  75  ? 55.506 22.446  -18.047 1.00 51.47  ?  107 TRP C CE3   1 
ATOM   7307  C  CZ2   . TRP C  2  75  ? 58.118 23.313  -18.685 1.00 51.07  ?  107 TRP C CZ2   1 
ATOM   7308  C  CZ3   . TRP C  2  75  ? 55.875 22.735  -19.349 1.00 50.57  ?  107 TRP C CZ3   1 
ATOM   7309  C  CH2   . TRP C  2  75  ? 57.166 23.161  -19.656 1.00 48.86  ?  107 TRP C CH2   1 
ATOM   7310  N  N     . THR C  2  76  ? 56.096 24.646  -12.614 1.00 49.50  ?  108 THR C N     1 
ATOM   7311  C  CA    . THR C  2  76  ? 56.165 26.081  -12.295 1.00 47.78  ?  108 THR C CA    1 
ATOM   7312  C  C     . THR C  2  76  ? 57.225 26.862  -13.113 1.00 45.35  ?  108 THR C C     1 
ATOM   7313  O  O     . THR C  2  76  ? 57.561 28.005  -12.778 1.00 43.96  ?  108 THR C O     1 
ATOM   7314  C  CB    . THR C  2  76  ? 56.394 26.286  -10.774 1.00 48.75  ?  108 THR C CB    1 
ATOM   7315  O  OG1   . THR C  2  76  ? 57.611 25.650  -10.365 1.00 47.29  ?  108 THR C OG1   1 
ATOM   7316  C  CG2   . THR C  2  76  ? 55.254 25.684  -9.984  1.00 49.77  ?  108 THR C CG2   1 
ATOM   7317  N  N     . GLY C  2  77  ? 57.764 26.233  -14.159 1.00 41.73  ?  109 GLY C N     1 
ATOM   7318  C  CA    . GLY C  2  77  ? 58.369 26.964  -15.250 1.00 40.19  ?  109 GLY C CA    1 
ATOM   7319  C  C     . GLY C  2  77  ? 59.876 27.074  -15.287 1.00 37.44  ?  109 GLY C C     1 
ATOM   7320  O  O     . GLY C  2  77  ? 60.566 26.098  -14.992 1.00 34.98  ?  109 GLY C O     1 
ATOM   7321  N  N     . ASP C  2  78  ? 60.340 28.269  -15.711 1.00 36.54  ?  110 ASP C N     1 
ATOM   7322  C  CA    . ASP C  2  78  ? 61.753 28.608  -15.995 1.00 35.50  ?  110 ASP C CA    1 
ATOM   7323  C  C     . ASP C  2  78  ? 62.485 27.527  -16.784 1.00 33.18  ?  110 ASP C C     1 
ATOM   7324  O  O     . ASP C  2  78  ? 63.320 26.758  -16.235 1.00 27.82  ?  110 ASP C O     1 
ATOM   7325  C  CB    . ASP C  2  78  ? 62.505 28.948  -14.703 1.00 38.27  ?  110 ASP C CB    1 
ATOM   7326  C  CG    . ASP C  2  78  ? 62.522 30.451  -14.391 1.00 39.34  ?  110 ASP C CG    1 
ATOM   7327  O  OD1   . ASP C  2  78  ? 62.085 31.276  -15.242 1.00 36.97  ?  110 ASP C OD1   1 
ATOM   7328  O  OD2   . ASP C  2  78  ? 63.006 30.793  -13.277 1.00 40.62  -1 110 ASP C OD2   1 
ATOM   7329  N  N     . SER C  2  79  ? 62.134 27.488  -18.073 1.00 32.24  ?  111 SER C N     1 
ATOM   7330  C  CA    . SER C  2  79  ? 62.620 26.473  -19.007 1.00 32.30  ?  111 SER C CA    1 
ATOM   7331  C  C     . SER C  2  79  ? 63.780 26.955  -19.893 1.00 34.72  ?  111 SER C C     1 
ATOM   7332  O  O     . SER C  2  79  ? 64.692 26.172  -20.203 1.00 36.27  ?  111 SER C O     1 
ATOM   7333  C  CB    . SER C  2  79  ? 61.460 25.963  -19.838 1.00 29.99  ?  111 SER C CB    1 
ATOM   7334  O  OG    . SER C  2  79  ? 60.388 25.713  -18.973 1.00 28.69  ?  111 SER C OG    1 
ATOM   7335  N  N     . PRO C  2  80  ? 63.770 28.238  -20.300 1.00 36.58  ?  112 PRO C N     1 
ATOM   7336  C  CA    . PRO C  2  80  ? 64.963 28.783  -20.970 1.00 38.26  ?  112 PRO C CA    1 
ATOM   7337  C  C     . PRO C  2  80  ? 66.221 28.907  -20.070 1.00 38.49  ?  112 PRO C C     1 
ATOM   7338  O  O     . PRO C  2  80  ? 66.099 29.340  -18.936 1.00 38.17  ?  112 PRO C O     1 
ATOM   7339  C  CB    . PRO C  2  80  ? 64.489 30.178  -21.389 1.00 37.41  ?  112 PRO C CB    1 
ATOM   7340  C  CG    . PRO C  2  80  ? 63.037 29.981  -21.619 1.00 35.98  ?  112 PRO C CG    1 
ATOM   7341  C  CD    . PRO C  2  80  ? 62.623 29.149  -20.457 1.00 35.91  ?  112 PRO C CD    1 
ATOM   7342  N  N     . PRO C  2  81  ? 67.425 28.594  -20.595 1.00 38.85  ?  113 PRO C N     1 
ATOM   7343  C  CA    . PRO C  2  81  ? 68.653 28.679  -19.783 1.00 39.12  ?  113 PRO C CA    1 
ATOM   7344  C  C     . PRO C  2  81  ? 69.154 30.114  -19.490 1.00 39.60  ?  113 PRO C C     1 
ATOM   7345  O  O     . PRO C  2  81  ? 68.566 31.118  -19.957 1.00 37.78  ?  113 PRO C O     1 
ATOM   7346  C  CB    . PRO C  2  81  ? 69.682 27.955  -20.646 1.00 39.30  ?  113 PRO C CB    1 
ATOM   7347  C  CG    . PRO C  2  81  ? 69.237 28.254  -22.044 1.00 40.34  ?  113 PRO C CG    1 
ATOM   7348  C  CD    . PRO C  2  81  ? 67.743 28.480  -22.030 1.00 38.93  ?  113 PRO C CD    1 
ATOM   7349  N  N     . HIS C  2  82  ? 70.240 30.178  -18.719 1.00 38.96  ?  114 HIS C N     1 
ATOM   7350  C  CA    . HIS C  2  82  ? 70.796 31.434  -18.237 1.00 40.69  ?  114 HIS C CA    1 
ATOM   7351  C  C     . HIS C  2  82  ? 71.923 31.904  -19.132 1.00 41.90  ?  114 HIS C C     1 
ATOM   7352  O  O     . HIS C  2  82  ? 73.099 31.554  -18.948 1.00 39.02  ?  114 HIS C O     1 
ATOM   7353  C  CB    . HIS C  2  82  ? 71.343 31.283  -16.828 1.00 43.55  ?  114 HIS C CB    1 
ATOM   7354  C  CG    . HIS C  2  82  ? 70.307 30.993  -15.794 1.00 44.02  ?  114 HIS C CG    1 
ATOM   7355  N  ND1   . HIS C  2  82  ? 69.969 29.708  -15.428 1.00 43.65  ?  114 HIS C ND1   1 
ATOM   7356  C  CD2   . HIS C  2  82  ? 69.563 31.820  -15.021 1.00 44.01  ?  114 HIS C CD2   1 
ATOM   7357  C  CE1   . HIS C  2  82  ? 69.044 29.756  -14.487 1.00 45.33  ?  114 HIS C CE1   1 
ATOM   7358  N  NE2   . HIS C  2  82  ? 68.783 31.025  -14.221 1.00 45.12  ?  114 HIS C NE2   1 
ATOM   7359  N  N     . VAL C  2  83  ? 71.532 32.695  -20.119 1.00 44.55  ?  115 VAL C N     1 
ATOM   7360  C  CA    . VAL C  2  83  ? 72.452 33.299  -21.063 1.00 42.84  ?  115 VAL C CA    1 
ATOM   7361  C  C     . VAL C  2  83  ? 71.994 34.755  -21.213 1.00 42.10  ?  115 VAL C C     1 
ATOM   7362  O  O     . VAL C  2  83  ? 70.876 35.112  -20.812 1.00 40.63  ?  115 VAL C O     1 
ATOM   7363  C  CB    . VAL C  2  83  ? 72.492 32.526  -22.416 1.00 41.46  ?  115 VAL C CB    1 
ATOM   7364  C  CG1   . VAL C  2  83  ? 72.938 31.084  -22.218 1.00 40.84  ?  115 VAL C CG1   1 
ATOM   7365  C  CG2   . VAL C  2  83  ? 71.140 32.515  -23.086 1.00 42.87  ?  115 VAL C CG2   1 
ATOM   7366  N  N     . PRO C  2  84  ? 72.866 35.610  -21.755 1.00 42.06  ?  116 PRO C N     1 
ATOM   7367  C  CA    . PRO C  2  84  ? 72.498 37.010  -21.819 1.00 41.66  ?  116 PRO C CA    1 
ATOM   7368  C  C     . PRO C  2  84  ? 71.447 37.259  -22.886 1.00 42.31  ?  116 PRO C C     1 
ATOM   7369  O  O     . PRO C  2  84  ? 71.345 36.497  -23.858 1.00 37.71  ?  116 PRO C O     1 
ATOM   7370  C  CB    . PRO C  2  84  ? 73.817 37.708  -22.167 1.00 43.16  ?  116 PRO C CB    1 
ATOM   7371  C  CG    . PRO C  2  84  ? 74.899 36.684  -21.978 1.00 42.61  ?  116 PRO C CG    1 
ATOM   7372  C  CD    . PRO C  2  84  ? 74.238 35.374  -22.235 1.00 42.45  ?  116 PRO C CD    1 
ATOM   7373  N  N     . VAL C  2  85  ? 70.677 38.326  -22.680 1.00 45.71  ?  117 VAL C N     1 
ATOM   7374  C  CA    . VAL C  2  85  ? 69.506 38.662  -23.516 1.00 49.17  ?  117 VAL C CA    1 
ATOM   7375  C  C     . VAL C  2  85  ? 69.781 38.620  -25.028 1.00 49.47  ?  117 VAL C C     1 
ATOM   7376  O  O     . VAL C  2  85  ? 69.067 37.943  -25.768 1.00 45.83  ?  117 VAL C O     1 
ATOM   7377  C  CB    . VAL C  2  85  ? 68.915 40.046  -23.124 1.00 50.80  ?  117 VAL C CB    1 
ATOM   7378  C  CG1   . VAL C  2  85  ? 67.862 40.509  -24.126 1.00 51.23  ?  117 VAL C CG1   1 
ATOM   7379  C  CG2   . VAL C  2  85  ? 68.331 39.995  -21.717 1.00 51.96  ?  117 VAL C CG2   1 
ATOM   7380  N  N     . PRO C  2  86  ? 70.809 39.351  -25.494 1.00 53.27  ?  118 PRO C N     1 
ATOM   7381  C  CA    . PRO C  2  86  ? 71.111 39.353  -26.918 1.00 52.74  ?  118 PRO C CA    1 
ATOM   7382  C  C     . PRO C  2  86  ? 71.393 37.978  -27.499 1.00 51.24  ?  118 PRO C C     1 
ATOM   7383  O  O     . PRO C  2  86  ? 71.173 37.775  -28.680 1.00 54.09  ?  118 PRO C O     1 
ATOM   7384  C  CB    . PRO C  2  86  ? 72.362 40.227  -27.016 1.00 53.73  ?  118 PRO C CB    1 
ATOM   7385  C  CG    . PRO C  2  86  ? 72.872 40.370  -25.617 1.00 54.24  ?  118 PRO C CG    1 
ATOM   7386  C  CD    . PRO C  2  86  ? 71.655 40.314  -24.769 1.00 54.92  ?  118 PRO C CD    1 
ATOM   7387  N  N     . GLU C  2  87  ? 71.867 37.038  -26.699 1.00 51.26  ?  119 GLU C N     1 
ATOM   7388  C  CA    . GLU C  2  87  ? 72.117 35.694  -27.223 1.00 53.86  ?  119 GLU C CA    1 
ATOM   7389  C  C     . GLU C  2  87  ? 70.824 34.865  -27.410 1.00 49.16  ?  119 GLU C C     1 
ATOM   7390  O  O     . GLU C  2  87  ? 70.813 33.889  -28.144 1.00 46.05  ?  119 GLU C O     1 
ATOM   7391  C  CB    . GLU C  2  87  ? 73.118 34.958  -26.330 1.00 58.99  ?  119 GLU C CB    1 
ATOM   7392  C  CG    . GLU C  2  87  ? 74.150 34.157  -27.102 1.00 63.28  ?  119 GLU C CG    1 
ATOM   7393  C  CD    . GLU C  2  87  ? 75.145 33.479  -26.186 1.00 69.44  ?  119 GLU C CD    1 
ATOM   7394  O  OE1   . GLU C  2  87  ? 75.593 32.353  -26.511 1.00 75.47  ?  119 GLU C OE1   1 
ATOM   7395  O  OE2   . GLU C  2  87  ? 75.473 34.074  -25.137 1.00 70.40  -1 119 GLU C OE2   1 
ATOM   7396  N  N     . LEU C  2  88  ? 69.740 35.264  -26.759 1.00 49.19  ?  120 LEU C N     1 
ATOM   7397  C  CA    . LEU C  2  88  ? 68.453 34.565  -26.875 1.00 49.79  ?  120 LEU C CA    1 
ATOM   7398  C  C     . LEU C  2  88  ? 67.441 35.334  -27.730 1.00 45.20  ?  120 LEU C C     1 
ATOM   7399  O  O     . LEU C  2  88  ? 67.704 36.455  -28.164 1.00 46.37  ?  120 LEU C O     1 
ATOM   7400  C  CB    . LEU C  2  88  ? 67.849 34.354  -25.480 1.00 54.36  ?  120 LEU C CB    1 
ATOM   7401  C  CG    . LEU C  2  88  ? 68.371 33.193  -24.634 1.00 56.11  ?  120 LEU C CG    1 
ATOM   7402  C  CD1   . LEU C  2  88  ? 67.842 33.340  -23.206 1.00 58.46  ?  120 LEU C CD1   1 
ATOM   7403  C  CD2   . LEU C  2  88  ? 68.001 31.833  -25.230 1.00 56.79  ?  120 LEU C CD2   1 
ATOM   7404  N  N     . SER C  2  89  ? 66.281 34.732  -27.961 1.00 39.88  ?  121 SER C N     1 
ATOM   7405  C  CA    . SER C  2  89  ? 65.181 35.441  -28.589 1.00 38.62  ?  121 SER C CA    1 
ATOM   7406  C  C     . SER C  2  89  ? 63.838 34.854  -28.172 1.00 39.40  ?  121 SER C C     1 
ATOM   7407  O  O     . SER C  2  89  ? 63.772 33.726  -27.666 1.00 37.62  ?  121 SER C O     1 
ATOM   7408  C  CB    . SER C  2  89  ? 65.327 35.443  -30.126 1.00 38.18  ?  121 SER C CB    1 
ATOM   7409  O  OG    . SER C  2  89  ? 64.879 34.242  -30.748 1.00 35.74  ?  121 SER C OG    1 
ATOM   7410  N  N     . THR C  2  90  ? 62.777 35.637  -28.401 1.00 39.72  ?  122 THR C N     1 
ATOM   7411  C  CA    . THR C  2  90  ? 61.387 35.176  -28.287 1.00 39.70  ?  122 THR C CA    1 
ATOM   7412  C  C     . THR C  2  90  ? 61.137 33.846  -29.030 1.00 43.72  ?  122 THR C C     1 
ATOM   7413  O  O     . THR C  2  90  ? 60.293 33.061  -28.603 1.00 51.44  ?  122 THR C O     1 
ATOM   7414  C  CB    . THR C  2  90  ? 60.376 36.242  -28.793 1.00 37.84  ?  122 THR C CB    1 
ATOM   7415  O  OG1   . THR C  2  90  ? 60.527 37.460  -28.056 1.00 35.86  ?  122 THR C OG1   1 
ATOM   7416  C  CG2   . THR C  2  90  ? 58.939 35.762  -28.644 1.00 37.59  ?  122 THR C CG2   1 
ATOM   7417  N  N     . ASP C  2  91  ? 61.846 33.575  -30.126 1.00 46.53  ?  123 ASP C N     1 
ATOM   7418  C  CA    . ASP C  2  91  ? 61.648 32.296  -30.850 1.00 49.26  ?  123 ASP C CA    1 
ATOM   7419  C  C     . ASP C  2  91  ? 62.334 31.098  -30.169 1.00 47.36  ?  123 ASP C C     1 
ATOM   7420  O  O     . ASP C  2  91  ? 61.818 29.973  -30.215 1.00 43.74  ?  123 ASP C O     1 
ATOM   7421  C  CB    . ASP C  2  91  ? 62.045 32.410  -32.341 1.00 50.09  ?  123 ASP C CB    1 
ATOM   7422  C  CG    . ASP C  2  91  ? 60.919 32.989  -33.207 1.00 49.62  ?  123 ASP C CG    1 
ATOM   7423  O  OD1   . ASP C  2  91  ? 60.220 33.941  -32.777 1.00 52.29  ?  123 ASP C OD1   1 
ATOM   7424  O  OD2   . ASP C  2  91  ? 60.729 32.485  -34.325 1.00 49.05  -1 123 ASP C OD2   1 
ATOM   7425  N  N     . THR C  2  92  ? 63.476 31.349  -29.532 1.00 47.12  ?  124 THR C N     1 
ATOM   7426  C  CA    . THR C  2  92  ? 64.203 30.299  -28.816 1.00 48.68  ?  124 THR C CA    1 
ATOM   7427  C  C     . THR C  2  92  ? 63.494 29.995  -27.491 1.00 49.10  ?  124 THR C C     1 
ATOM   7428  O  O     . THR C  2  92  ? 63.415 28.832  -27.065 1.00 50.51  ?  124 THR C O     1 
ATOM   7429  C  CB    . THR C  2  92  ? 65.670 30.689  -28.521 1.00 48.14  ?  124 THR C CB    1 
ATOM   7430  O  OG1   . THR C  2  92  ? 66.126 31.638  -29.487 1.00 49.88  ?  124 THR C OG1   1 
ATOM   7431  C  CG2   . THR C  2  92  ? 66.580 29.458  -28.542 1.00 47.48  ?  124 THR C CG2   1 
ATOM   7432  N  N     . VAL C  2  93  ? 62.990 31.035  -26.830 1.00 45.61  ?  125 VAL C N     1 
ATOM   7433  C  CA    . VAL C  2  93  ? 62.155 30.826  -25.651 1.00 42.38  ?  125 VAL C CA    1 
ATOM   7434  C  C     . VAL C  2  93  ? 61.045 29.823  -26.024 1.00 42.40  ?  125 VAL C C     1 
ATOM   7435  O  O     . VAL C  2  93  ? 60.938 28.759  -25.396 1.00 43.38  ?  125 VAL C O     1 
ATOM   7436  C  CB    . VAL C  2  93  ? 61.607 32.163  -25.079 1.00 40.23  ?  125 VAL C CB    1 
ATOM   7437  C  CG1   . VAL C  2  93  ? 60.352 31.967  -24.238 1.00 39.65  ?  125 VAL C CG1   1 
ATOM   7438  C  CG2   . VAL C  2  93  ? 62.679 32.861  -24.255 1.00 40.61  ?  125 VAL C CG2   1 
ATOM   7439  N  N     . ILE C  2  94  ? 60.281 30.122  -27.080 1.00 39.72  ?  126 ILE C N     1 
ATOM   7440  C  CA    . ILE C  2  94  ? 59.140 29.286  -27.464 1.00 37.67  ?  126 ILE C CA    1 
ATOM   7441  C  C     . ILE C  2  94  ? 59.560 27.875  -27.886 1.00 38.23  ?  126 ILE C C     1 
ATOM   7442  O  O     . ILE C  2  94  ? 58.842 26.917  -27.593 1.00 35.46  ?  126 ILE C O     1 
ATOM   7443  C  CB    . ILE C  2  94  ? 58.281 29.967  -28.544 1.00 36.46  ?  126 ILE C CB    1 
ATOM   7444  C  CG1   . ILE C  2  94  ? 57.632 31.204  -27.936 1.00 37.72  ?  126 ILE C CG1   1 
ATOM   7445  C  CG2   . ILE C  2  94  ? 57.194 29.028  -29.064 1.00 35.33  ?  126 ILE C CG2   1 
ATOM   7446  C  CD1   . ILE C  2  94  ? 56.998 32.137  -28.937 1.00 38.09  ?  126 ILE C CD1   1 
ATOM   7447  N  N     . ASN C  2  95  ? 60.723 27.746  -28.533 1.00 40.85  ?  127 ASN C N     1 
ATOM   7448  C  CA    . ASN C  2  95  ? 61.240 26.426  -28.944 1.00 44.47  ?  127 ASN C CA    1 
ATOM   7449  C  C     . ASN C  2  95  ? 61.567 25.550  -27.750 1.00 45.80  ?  127 ASN C C     1 
ATOM   7450  O  O     . ASN C  2  95  ? 61.218 24.369  -27.724 1.00 46.18  ?  127 ASN C O     1 
ATOM   7451  C  CB    . ASN C  2  95  ? 62.494 26.545  -29.824 1.00 47.01  ?  127 ASN C CB    1 
ATOM   7452  C  CG    . ASN C  2  95  ? 62.203 27.122  -31.206 1.00 49.58  ?  127 ASN C CG    1 
ATOM   7453  O  OD1   . ASN C  2  95  ? 61.156 26.863  -31.812 1.00 46.92  ?  127 ASN C OD1   1 
ATOM   7454  N  ND2   . ASN C  2  95  ? 63.145 27.915  -31.714 1.00 53.76  ?  127 ASN C ND2   1 
ATOM   7455  N  N     . VAL C  2  96  ? 62.233 26.144  -26.765 1.00 47.96  ?  128 VAL C N     1 
ATOM   7456  C  CA    . VAL C  2  96  ? 62.523 25.479  -25.483 1.00 49.75  ?  128 VAL C CA    1 
ATOM   7457  C  C     . VAL C  2  96  ? 61.280 25.133  -24.636 1.00 44.44  ?  128 VAL C C     1 
ATOM   7458  O  O     . VAL C  2  96  ? 61.200 24.042  -24.091 1.00 41.57  ?  128 VAL C O     1 
ATOM   7459  C  CB    . VAL C  2  96  ? 63.505 26.325  -24.643 1.00 55.85  ?  128 VAL C CB    1 
ATOM   7460  C  CG1   . VAL C  2  96  ? 63.567 25.850  -23.194 1.00 57.34  ?  128 VAL C CG1   1 
ATOM   7461  C  CG2   . VAL C  2  96  ? 64.893 26.288  -25.279 1.00 58.11  ?  128 VAL C CG2   1 
ATOM   7462  N  N     . ILE C  2  97  ? 60.330 26.052  -24.507 1.00 42.18  ?  129 ILE C N     1 
ATOM   7463  C  CA    . ILE C  2  97  ? 59.067 25.730  -23.842 1.00 41.34  ?  129 ILE C CA    1 
ATOM   7464  C  C     . ILE C  2  97  ? 58.333 24.644  -24.636 1.00 43.24  ?  129 ILE C C     1 
ATOM   7465  O  O     . ILE C  2  97  ? 57.793 23.711  -24.044 1.00 42.82  ?  129 ILE C O     1 
ATOM   7466  C  CB    . ILE C  2  97  ? 58.141 26.963  -23.697 1.00 40.23  ?  129 ILE C CB    1 
ATOM   7467  C  CG1   . ILE C  2  97  ? 58.783 28.032  -22.805 1.00 38.18  ?  129 ILE C CG1   1 
ATOM   7468  C  CG2   . ILE C  2  97  ? 56.780 26.567  -23.119 1.00 39.41  ?  129 ILE C CG2   1 
ATOM   7469  C  CD1   . ILE C  2  97  ? 58.079 29.372  -22.873 1.00 36.91  ?  129 ILE C CD1   1 
ATOM   7470  N  N     . THR C  2  98  ? 58.302 24.770  -25.966 1.00 44.47  ?  130 THR C N     1 
ATOM   7471  C  CA    . THR C  2  98  ? 57.621 23.786  -26.822 1.00 47.02  ?  130 THR C CA    1 
ATOM   7472  C  C     . THR C  2  98  ? 58.190 22.364  -26.660 1.00 47.59  ?  130 THR C C     1 
ATOM   7473  O  O     . THR C  2  98  ? 57.420 21.388  -26.627 1.00 45.60  ?  130 THR C O     1 
ATOM   7474  C  CB    . THR C  2  98  ? 57.699 24.192  -28.310 1.00 49.88  ?  130 THR C CB    1 
ATOM   7475  O  OG1   . THR C  2  98  ? 57.171 25.515  -28.466 1.00 51.84  ?  130 THR C OG1   1 
ATOM   7476  C  CG2   . THR C  2  98  ? 56.928 23.193  -29.229 1.00 48.70  ?  130 THR C CG2   1 
ATOM   7477  N  N     . ASN C  2  99  ? 59.525 22.258  -26.559 1.00 45.91  ?  131 ASN C N     1 
ATOM   7478  C  CA    . ASN C  2  99  ? 60.215 20.967  -26.348 1.00 45.33  ?  131 ASN C CA    1 
ATOM   7479  C  C     . ASN C  2  99  ? 59.797 20.312  -25.023 1.00 42.45  ?  131 ASN C C     1 
ATOM   7480  O  O     . ASN C  2  99  ? 59.325 19.176  -24.998 1.00 42.06  ?  131 ASN C O     1 
ATOM   7481  C  CB    . ASN C  2  99  ? 61.748 21.137  -26.419 1.00 47.08  ?  131 ASN C CB    1 
ATOM   7482  C  CG    . ASN C  2  99  ? 62.488 19.807  -26.451 1.00 51.86  ?  131 ASN C CG    1 
ATOM   7483  O  OD1   . ASN C  2  99  ? 62.183 18.907  -25.669 1.00 55.19  ?  131 ASN C OD1   1 
ATOM   7484  N  ND2   . ASN C  2  99  ? 63.478 19.676  -27.356 1.00 56.50  ?  131 ASN C ND2   1 
ATOM   7485  N  N     . MET C  2  100 ? 59.951 21.044  -23.927 1.00 40.82  ?  132 MET C N     1 
ATOM   7486  C  CA    . MET C  2  100 ? 59.519 20.558  -22.615 1.00 38.87  ?  132 MET C CA    1 
ATOM   7487  C  C     . MET C  2  100 ? 58.054 20.120  -22.697 1.00 38.92  ?  132 MET C C     1 
ATOM   7488  O  O     . MET C  2  100 ? 57.753 18.947  -22.487 1.00 37.70  ?  132 MET C O     1 
ATOM   7489  C  CB    . MET C  2  100 ? 59.713 21.628  -21.530 1.00 36.92  ?  132 MET C CB    1 
ATOM   7490  C  CG    . MET C  2  100 ? 61.158 22.070  -21.305 1.00 36.40  ?  132 MET C CG    1 
ATOM   7491  S  SD    . MET C  2  100 ? 62.303 20.781  -20.739 1.00 36.17  ?  132 MET C SD    1 
ATOM   7492  C  CE    . MET C  2  100 ? 63.175 20.352  -22.233 1.00 37.53  ?  132 MET C CE    1 
ATOM   7493  N  N     . THR C  2  101 ? 57.158 21.047  -23.052 1.00 38.91  ?  133 THR C N     1 
ATOM   7494  C  CA    . THR C  2  101 ? 55.741 20.723  -23.177 1.00 39.15  ?  133 THR C CA    1 
ATOM   7495  C  C     . THR C  2  101 ? 55.551 19.452  -23.994 1.00 40.95  ?  133 THR C C     1 
ATOM   7496  O  O     . THR C  2  101 ? 54.821 18.574  -23.577 1.00 43.89  ?  133 THR C O     1 
ATOM   7497  C  CB    . THR C  2  101 ? 54.901 21.833  -23.838 1.00 39.01  ?  133 THR C CB    1 
ATOM   7498  O  OG1   . THR C  2  101 ? 55.162 23.103  -23.226 1.00 38.25  ?  133 THR C OG1   1 
ATOM   7499  C  CG2   . THR C  2  101 ? 53.412 21.500  -23.709 1.00 37.78  ?  133 THR C CG2   1 
ATOM   7500  N  N     . THR C  2  102 ? 56.204 19.338  -25.145 1.00 42.42  ?  134 THR C N     1 
ATOM   7501  C  CA    . THR C  2  102 ? 56.061 18.120  -25.955 1.00 44.89  ?  134 THR C CA    1 
ATOM   7502  C  C     . THR C  2  102 ? 56.614 16.868  -25.256 1.00 44.82  ?  134 THR C C     1 
ATOM   7503  O  O     . THR C  2  102 ? 55.954 15.819  -25.254 1.00 44.19  ?  134 THR C O     1 
ATOM   7504  C  CB    . THR C  2  102 ? 56.748 18.249  -27.323 1.00 45.73  ?  134 THR C CB    1 
ATOM   7505  O  OG1   . THR C  2  102 ? 56.301 19.444  -27.964 1.00 46.24  ?  134 THR C OG1   1 
ATOM   7506  C  CG2   . THR C  2  102 ? 56.433 17.034  -28.210 1.00 45.81  ?  134 THR C CG2   1 
ATOM   7507  N  N     . THR C  2  103 ? 57.813 16.994  -24.678 1.00 43.08  ?  135 THR C N     1 
ATOM   7508  C  CA    . THR C  2  103 ? 58.501 15.881  -24.014 1.00 42.52  ?  135 THR C CA    1 
ATOM   7509  C  C     . THR C  2  103 ? 57.671 15.261  -22.883 1.00 44.24  ?  135 THR C C     1 
ATOM   7510  O  O     . THR C  2  103 ? 57.648 14.033  -22.731 1.00 43.04  ?  135 THR C O     1 
ATOM   7511  C  CB    . THR C  2  103 ? 59.858 16.327  -23.435 1.00 41.15  ?  135 THR C CB    1 
ATOM   7512  O  OG1   . THR C  2  103 ? 60.671 16.888  -24.471 1.00 39.79  ?  135 THR C OG1   1 
ATOM   7513  C  CG2   . THR C  2  103 ? 60.590 15.149  -22.822 1.00 41.62  ?  135 THR C CG2   1 
ATOM   7514  N  N     . ILE C  2  104 ? 57.009 16.121  -22.100 1.00 46.38  ?  136 ILE C N     1 
ATOM   7515  C  CA    . ILE C  2  104 ? 56.061 15.717  -21.038 1.00 46.62  ?  136 ILE C CA    1 
ATOM   7516  C  C     . ILE C  2  104 ? 54.806 15.056  -21.623 1.00 43.66  ?  136 ILE C C     1 
ATOM   7517  O  O     . ILE C  2  104 ? 54.335 14.037  -21.127 1.00 37.74  ?  136 ILE C O     1 
ATOM   7518  C  CB    . ILE C  2  104 ? 55.627 16.944  -20.180 1.00 48.91  ?  136 ILE C CB    1 
ATOM   7519  C  CG1   . ILE C  2  104 ? 56.803 17.455  -19.329 1.00 48.43  ?  136 ILE C CG1   1 
ATOM   7520  C  CG2   . ILE C  2  104 ? 54.416 16.618  -19.291 1.00 49.41  ?  136 ILE C CG2   1 
ATOM   7521  C  CD1   . ILE C  2  104 ? 56.595 18.864  -18.800 1.00 48.83  ?  136 ILE C CD1   1 
ATOM   7522  N  N     . GLN C  2  105 ? 54.266 15.668  -22.671 1.00 45.66  ?  137 GLN C N     1 
ATOM   7523  C  CA    . GLN C  2  105 ? 53.037 15.189  -23.293 1.00 47.98  ?  137 GLN C CA    1 
ATOM   7524  C  C     . GLN C  2  105 ? 53.252 13.830  -23.940 1.00 48.93  ?  137 GLN C C     1 
ATOM   7525  O  O     . GLN C  2  105 ? 52.328 13.024  -23.991 1.00 49.24  ?  137 GLN C O     1 
ATOM   7526  C  CB    . GLN C  2  105 ? 52.488 16.219  -24.295 1.00 48.50  ?  137 GLN C CB    1 
ATOM   7527  C  CG    . GLN C  2  105 ? 51.792 17.393  -23.603 1.00 50.72  ?  137 GLN C CG    1 
ATOM   7528  C  CD    . GLN C  2  105 ? 51.308 18.499  -24.539 1.00 56.17  ?  137 GLN C CD    1 
ATOM   7529  O  OE1   . GLN C  2  105 ? 51.282 18.334  -25.764 1.00 66.40  ?  137 GLN C OE1   1 
ATOM   7530  N  NE2   . GLN C  2  105 ? 50.915 19.639  -23.961 1.00 55.28  ?  137 GLN C NE2   1 
ATOM   7531  N  N     . SER C  2  106 ? 54.475 13.580  -24.405 1.00 50.98  ?  138 SER C N     1 
ATOM   7532  C  CA    . SER C  2  106 ? 54.847 12.288  -24.988 1.00 53.92  ?  138 SER C CA    1 
ATOM   7533  C  C     . SER C  2  106 ? 54.896 11.183  -23.957 1.00 52.97  ?  138 SER C C     1 
ATOM   7534  O  O     . SER C  2  106 ? 54.220 10.166  -24.114 1.00 54.59  ?  138 SER C O     1 
ATOM   7535  C  CB    . SER C  2  106 ? 56.214 12.366  -25.676 1.00 56.79  ?  138 SER C CB    1 
ATOM   7536  O  OG    . SER C  2  106 ? 56.194 13.307  -26.740 1.00 65.05  ?  138 SER C OG    1 
ATOM   7537  N  N     . LEU C  2  107 ? 55.708 11.384  -22.918 1.00 51.86  ?  139 LEU C N     1 
ATOM   7538  C  CA    . LEU C  2  107 ? 55.889 10.387  -21.853 1.00 49.18  ?  139 LEU C CA    1 
ATOM   7539  C  C     . LEU C  2  107 ? 54.678 10.264  -20.949 1.00 46.24  ?  139 LEU C C     1 
ATOM   7540  O  O     . LEU C  2  107 ? 54.440 9.198   -20.404 1.00 43.31  ?  139 LEU C O     1 
ATOM   7541  C  CB    . LEU C  2  107 ? 57.079 10.742  -20.967 1.00 51.11  ?  139 LEU C CB    1 
ATOM   7542  C  CG    . LEU C  2  107 ? 58.502 10.639  -21.514 1.00 53.58  ?  139 LEU C CG    1 
ATOM   7543  C  CD1   . LEU C  2  107 ? 59.396 11.482  -20.618 1.00 54.49  ?  139 LEU C CD1   1 
ATOM   7544  C  CD2   . LEU C  2  107 ? 59.008 9.196   -21.594 1.00 53.70  ?  139 LEU C CD2   1 
ATOM   7545  N  N     . PHE C  2  108 ? 53.947 11.364  -20.764 1.00 46.94  ?  140 PHE C N     1 
ATOM   7546  C  CA    . PHE C  2  108 ? 52.773 11.401  -19.875 1.00 49.69  ?  140 PHE C CA    1 
ATOM   7547  C  C     . PHE C  2  108 ? 51.511 11.820  -20.657 1.00 51.74  ?  140 PHE C C     1 
ATOM   7548  O  O     . PHE C  2  108 ? 50.932 12.895  -20.411 1.00 51.96  ?  140 PHE C O     1 
ATOM   7549  C  CB    . PHE C  2  108 ? 53.016 12.320  -18.654 1.00 47.16  ?  140 PHE C CB    1 
ATOM   7550  C  CG    . PHE C  2  108 ? 54.243 11.955  -17.843 1.00 46.24  ?  140 PHE C CG    1 
ATOM   7551  C  CD1   . PHE C  2  108 ? 54.358 10.708  -17.245 1.00 45.59  ?  140 PHE C CD1   1 
ATOM   7552  C  CD2   . PHE C  2  108 ? 55.278 12.860  -17.668 1.00 45.34  ?  140 PHE C CD2   1 
ATOM   7553  C  CE1   . PHE C  2  108 ? 55.485 10.369  -16.505 1.00 44.43  ?  140 PHE C CE1   1 
ATOM   7554  C  CE2   . PHE C  2  108 ? 56.397 12.523  -16.928 1.00 44.10  ?  140 PHE C CE2   1 
ATOM   7555  C  CZ    . PHE C  2  108 ? 56.502 11.279  -16.348 1.00 43.08  ?  140 PHE C CZ    1 
ATOM   7556  N  N     . PRO C  2  109 ? 51.075 10.958  -21.600 1.00 51.49  ?  141 PRO C N     1 
ATOM   7557  C  CA    . PRO C  2  109 ? 49.928 11.287  -22.464 1.00 51.85  ?  141 PRO C CA    1 
ATOM   7558  C  C     . PRO C  2  109 ? 48.640 11.492  -21.677 1.00 52.35  ?  141 PRO C C     1 
ATOM   7559  O  O     . PRO C  2  109 ? 47.882 12.413  -21.964 1.00 49.08  ?  141 PRO C O     1 
ATOM   7560  C  CB    . PRO C  2  109 ? 49.809 10.062  -23.380 1.00 50.30  ?  141 PRO C CB    1 
ATOM   7561  C  CG    . PRO C  2  109 ? 50.522 8.960   -22.669 1.00 50.09  ?  141 PRO C CG    1 
ATOM   7562  C  CD    . PRO C  2  109 ? 51.603 9.604   -21.865 1.00 49.24  ?  141 PRO C CD    1 
ATOM   7563  N  N     . ASN C  2  110 ? 48.432 10.646  -20.671 1.00 55.80  ?  142 ASN C N     1 
ATOM   7564  C  CA    . ASN C  2  110 ? 47.205 10.649  -19.876 1.00 57.98  ?  142 ASN C CA    1 
ATOM   7565  C  C     . ASN C  2  110 ? 47.272 11.542  -18.642 1.00 55.23  ?  142 ASN C C     1 
ATOM   7566  O  O     . ASN C  2  110 ? 46.335 11.559  -17.843 1.00 56.14  ?  142 ASN C O     1 
ATOM   7567  C  CB    . ASN C  2  110 ? 46.867 9.217   -19.434 1.00 59.69  ?  142 ASN C CB    1 
ATOM   7568  C  CG    . ASN C  2  110 ? 46.753 8.259   -20.603 1.00 59.48  ?  142 ASN C CG    1 
ATOM   7569  O  OD1   . ASN C  2  110 ? 47.449 7.241   -20.664 1.00 61.69  ?  142 ASN C OD1   1 
ATOM   7570  N  ND2   . ASN C  2  110 ? 45.884 8.588   -21.545 1.00 57.42  ?  142 ASN C ND2   1 
ATOM   7571  N  N     . LEU C  2  111 ? 48.370 12.273  -18.475 1.00 54.59  ?  143 LEU C N     1 
ATOM   7572  C  CA    . LEU C  2  111 ? 48.562 13.095  -17.278 1.00 52.39  ?  143 LEU C CA    1 
ATOM   7573  C  C     . LEU C  2  111 ? 48.205 14.570  -17.541 1.00 49.15  ?  143 LEU C C     1 
ATOM   7574  O  O     . LEU C  2  111 ? 48.615 15.171  -18.548 1.00 46.30  ?  143 LEU C O     1 
ATOM   7575  C  CB    . LEU C  2  111 ? 50.003 12.956  -16.756 1.00 51.23  ?  143 LEU C CB    1 
ATOM   7576  C  CG    . LEU C  2  111 ? 50.345 13.635  -15.423 1.00 52.28  ?  143 LEU C CG    1 
ATOM   7577  C  CD1   . LEU C  2  111 ? 49.389 13.222  -14.307 1.00 52.61  ?  143 LEU C CD1   1 
ATOM   7578  C  CD2   . LEU C  2  111 ? 51.805 13.362  -15.042 1.00 53.04  ?  143 LEU C CD2   1 
ATOM   7579  N  N     . GLN C  2  112 ? 47.409 15.128  -16.633 1.00 45.00  ?  144 GLN C N     1 
ATOM   7580  C  CA    . GLN C  2  112 ? 47.139 16.546  -16.618 1.00 41.47  ?  144 GLN C CA    1 
ATOM   7581  C  C     . GLN C  2  112 ? 48.301 17.207  -15.916 1.00 40.53  ?  144 GLN C C     1 
ATOM   7582  O  O     . GLN C  2  112 ? 48.882 16.635  -14.980 1.00 39.99  ?  144 GLN C O     1 
ATOM   7583  C  CB    . GLN C  2  112 ? 45.857 16.857  -15.863 1.00 41.78  ?  144 GLN C CB    1 
ATOM   7584  C  CG    . GLN C  2  112 ? 45.543 18.339  -15.805 1.00 42.15  ?  144 GLN C CG    1 
ATOM   7585  C  CD    . GLN C  2  112 ? 44.140 18.620  -15.311 1.00 42.94  ?  144 GLN C CD    1 
ATOM   7586  O  OE1   . GLN C  2  112 ? 43.537 17.815  -14.585 1.00 43.00  ?  144 GLN C OE1   1 
ATOM   7587  N  NE2   . GLN C  2  112 ? 43.618 19.787  -15.676 1.00 42.93  ?  144 GLN C NE2   1 
ATOM   7588  N  N     . VAL C  2  113 ? 48.635 18.405  -16.390 1.00 37.85  ?  145 VAL C N     1 
ATOM   7589  C  CA    . VAL C  2  113 ? 49.716 19.213  -15.855 1.00 35.39  ?  145 VAL C CA    1 
ATOM   7590  C  C     . VAL C  2  113 ? 49.187 20.647  -15.785 1.00 35.90  ?  145 VAL C C     1 
ATOM   7591  O  O     . VAL C  2  113 ? 48.356 21.040  -16.600 1.00 38.63  ?  145 VAL C O     1 
ATOM   7592  C  CB    . VAL C  2  113 ? 50.966 19.137  -16.756 1.00 33.62  ?  145 VAL C CB    1 
ATOM   7593  C  CG1   . VAL C  2  113 ? 52.113 19.924  -16.142 1.00 34.80  ?  145 VAL C CG1   1 
ATOM   7594  C  CG2   . VAL C  2  113 ? 51.392 17.694  -16.990 1.00 32.26  ?  145 VAL C CG2   1 
ATOM   7595  N  N     . PHE C  2  114 ? 49.635 21.423  -14.807 1.00 34.59  ?  146 PHE C N     1 
ATOM   7596  C  CA    . PHE C  2  114 ? 49.205 22.812  -14.701 1.00 34.36  ?  146 PHE C CA    1 
ATOM   7597  C  C     . PHE C  2  114 ? 50.407 23.732  -14.627 1.00 35.11  ?  146 PHE C C     1 
ATOM   7598  O  O     . PHE C  2  114 ? 50.995 23.947  -13.543 1.00 37.78  ?  146 PHE C O     1 
ATOM   7599  C  CB    . PHE C  2  114 ? 48.357 23.025  -13.476 1.00 34.35  ?  146 PHE C CB    1 
ATOM   7600  C  CG    . PHE C  2  114 ? 47.221 22.073  -13.348 1.00 35.47  ?  146 PHE C CG    1 
ATOM   7601  C  CD1   . PHE C  2  114 ? 47.428 20.797  -12.845 1.00 36.62  ?  146 PHE C CD1   1 
ATOM   7602  C  CD2   . PHE C  2  114 ? 45.939 22.470  -13.672 1.00 36.14  ?  146 PHE C CD2   1 
ATOM   7603  C  CE1   . PHE C  2  114 ? 46.383 19.924  -12.682 1.00 36.66  ?  146 PHE C CE1   1 
ATOM   7604  C  CE2   . PHE C  2  114 ? 44.889 21.608  -13.513 1.00 37.42  ?  146 PHE C CE2   1 
ATOM   7605  C  CZ    . PHE C  2  114 ? 45.112 20.333  -13.019 1.00 38.49  ?  146 PHE C CZ    1 
ATOM   7606  N  N     . PRO C  2  115 ? 50.789 24.283  -15.779 1.00 33.88  ?  147 PRO C N     1 
ATOM   7607  C  CA    . PRO C  2  115 ? 51.939 25.173  -15.791 1.00 32.65  ?  147 PRO C CA    1 
ATOM   7608  C  C     . PRO C  2  115 ? 51.668 26.586  -15.276 1.00 31.94  ?  147 PRO C C     1 
ATOM   7609  O  O     . PRO C  2  115 ? 50.542 27.037  -15.238 1.00 32.51  ?  147 PRO C O     1 
ATOM   7610  C  CB    . PRO C  2  115 ? 52.337 25.202  -17.264 1.00 33.02  ?  147 PRO C CB    1 
ATOM   7611  C  CG    . PRO C  2  115 ? 51.730 23.965  -17.843 1.00 33.82  ?  147 PRO C CG    1 
ATOM   7612  C  CD    . PRO C  2  115 ? 50.416 23.866  -17.139 1.00 33.95  ?  147 PRO C CD    1 
ATOM   7613  N  N     . ALA C  2  116 ? 52.722 27.250  -14.833 1.00 32.85  ?  148 ALA C N     1 
ATOM   7614  C  CA    . ALA C  2  116 ? 52.711 28.678  -14.591 1.00 33.17  ?  148 ALA C CA    1 
ATOM   7615  C  C     . ALA C  2  116 ? 53.950 29.214  -15.247 1.00 34.83  ?  148 ALA C C     1 
ATOM   7616  O  O     . ALA C  2  116 ? 54.927 28.476  -15.461 1.00 34.98  ?  148 ALA C O     1 
ATOM   7617  C  CB    . ALA C  2  116 ? 52.774 28.962  -13.121 1.00 33.60  ?  148 ALA C CB    1 
ATOM   7618  N  N     . LEU C  2  117 ? 53.937 30.502  -15.544 1.00 36.80  ?  149 LEU C N     1 
ATOM   7619  C  CA    . LEU C  2  117 ? 55.089 31.127  -16.204 1.00 39.68  ?  149 LEU C CA    1 
ATOM   7620  C  C     . LEU C  2  117 ? 56.204 31.546  -15.216 1.00 41.71  ?  149 LEU C C     1 
ATOM   7621  O  O     . LEU C  2  117 ? 55.925 32.131  -14.166 1.00 44.37  ?  149 LEU C O     1 
ATOM   7622  C  CB    . LEU C  2  117 ? 54.622 32.323  -17.056 1.00 38.11  ?  149 LEU C CB    1 
ATOM   7623  C  CG    . LEU C  2  117 ? 53.726 31.921  -18.228 1.00 36.83  ?  149 LEU C CG    1 
ATOM   7624  C  CD1   . LEU C  2  117 ? 53.130 33.165  -18.866 1.00 35.89  ?  149 LEU C CD1   1 
ATOM   7625  C  CD2   . LEU C  2  117 ? 54.508 31.076  -19.225 1.00 35.81  ?  149 LEU C CD2   1 
ATOM   7626  N  N     . GLY C  2  118 ? 57.455 31.219  -15.553 1.00 42.75  ?  150 GLY C N     1 
ATOM   7627  C  CA    . GLY C  2  118 ? 58.637 31.726  -14.834 1.00 43.36  ?  150 GLY C CA    1 
ATOM   7628  C  C     . GLY C  2  118 ? 59.218 32.923  -15.577 1.00 42.93  ?  150 GLY C C     1 
ATOM   7629  O  O     . GLY C  2  118 ? 58.801 33.206  -16.685 1.00 42.18  ?  150 GLY C O     1 
ATOM   7630  N  N     . ASN C  2  119 ? 60.192 33.619  -14.994 1.00 43.79  ?  151 ASN C N     1 
ATOM   7631  C  CA    . ASN C  2  119 ? 60.698 34.866  -15.605 1.00 44.11  ?  151 ASN C CA    1 
ATOM   7632  C  C     . ASN C  2  119 ? 61.634 34.649  -16.821 1.00 45.38  ?  151 ASN C C     1 
ATOM   7633  O  O     . ASN C  2  119 ? 61.721 35.519  -17.717 1.00 45.06  ?  151 ASN C O     1 
ATOM   7634  C  CB    . ASN C  2  119 ? 61.321 35.796  -14.555 1.00 42.72  ?  151 ASN C CB    1 
ATOM   7635  C  CG    . ASN C  2  119 ? 62.131 35.049  -13.542 1.00 42.50  ?  151 ASN C CG    1 
ATOM   7636  O  OD1   . ASN C  2  119 ? 61.653 34.075  -12.972 1.00 43.53  ?  151 ASN C OD1   1 
ATOM   7637  N  ND2   . ASN C  2  119 ? 63.358 35.490  -13.306 1.00 43.18  ?  151 ASN C ND2   1 
ATOM   7638  N  N     . HIS C  2  120 ? 62.297 33.489  -16.875 1.00 42.18  ?  152 HIS C N     1 
ATOM   7639  C  CA    . HIS C  2  120 ? 63.038 33.103  -18.080 1.00 38.40  ?  152 HIS C CA    1 
ATOM   7640  C  C     . HIS C  2  120 ? 62.179 32.545  -19.188 1.00 37.21  ?  152 HIS C C     1 
ATOM   7641  O  O     . HIS C  2  120 ? 62.661 32.356  -20.288 1.00 36.45  ?  152 HIS C O     1 
ATOM   7642  C  CB    . HIS C  2  120 ? 64.124 32.123  -17.732 1.00 36.23  ?  152 HIS C CB    1 
ATOM   7643  C  CG    . HIS C  2  120 ? 65.234 32.760  -16.980 1.00 36.60  ?  152 HIS C CG    1 
ATOM   7644  N  ND1   . HIS C  2  120 ? 66.474 32.985  -17.532 1.00 37.90  ?  152 HIS C ND1   1 
ATOM   7645  C  CD2   . HIS C  2  120 ? 65.275 33.283  -15.736 1.00 36.53  ?  152 HIS C CD2   1 
ATOM   7646  C  CE1   . HIS C  2  120 ? 67.245 33.582  -16.639 1.00 37.73  ?  152 HIS C CE1   1 
ATOM   7647  N  NE2   . HIS C  2  120 ? 66.542 33.770  -15.539 1.00 35.61  ?  152 HIS C NE2   1 
ATOM   7648  N  N     . ASP C  2  121 ? 60.913 32.279  -18.896 1.00 36.99  ?  153 ASP C N     1 
ATOM   7649  C  CA    . ASP C  2  121 ? 59.963 31.899  -19.916 1.00 38.40  ?  153 ASP C CA    1 
ATOM   7650  C  C     . ASP C  2  121 ? 59.461 33.150  -20.682 1.00 43.68  ?  153 ASP C C     1 
ATOM   7651  O  O     . ASP C  2  121 ? 58.308 33.192  -21.101 1.00 45.65  ?  153 ASP C O     1 
ATOM   7652  C  CB    . ASP C  2  121 ? 58.765 31.153  -19.299 1.00 36.48  ?  153 ASP C CB    1 
ATOM   7653  C  CG    . ASP C  2  121 ? 59.146 29.842  -18.595 1.00 34.76  ?  153 ASP C CG    1 
ATOM   7654  O  OD1   . ASP C  2  121 ? 60.130 29.134  -18.949 1.00 32.16  ?  153 ASP C OD1   1 
ATOM   7655  O  OD2   . ASP C  2  121 ? 58.388 29.508  -17.675 1.00 32.61  -1 153 ASP C OD2   1 
ATOM   7656  N  N     . TYR C  2  122 ? 60.306 34.170  -20.854 1.00 48.52  ?  154 TYR C N     1 
ATOM   7657  C  CA    . TYR C  2  122 ? 59.980 35.314  -21.713 1.00 46.79  ?  154 TYR C CA    1 
ATOM   7658  C  C     . TYR C  2  122 ? 61.267 35.880  -22.328 1.00 48.41  ?  154 TYR C C     1 
ATOM   7659  O  O     . TYR C  2  122 ? 62.381 35.580  -21.848 1.00 52.01  ?  154 TYR C O     1 
ATOM   7660  C  CB    . TYR C  2  122 ? 59.233 36.377  -20.912 1.00 45.40  ?  154 TYR C CB    1 
ATOM   7661  C  CG    . TYR C  2  122 ? 58.375 37.293  -21.773 1.00 49.17  ?  154 TYR C CG    1 
ATOM   7662  C  CD1   . TYR C  2  122 ? 57.116 36.883  -22.239 1.00 49.93  ?  154 TYR C CD1   1 
ATOM   7663  C  CD2   . TYR C  2  122 ? 58.814 38.575  -22.128 1.00 50.50  ?  154 TYR C CD2   1 
ATOM   7664  C  CE1   . TYR C  2  122 ? 56.338 37.723  -23.037 1.00 49.11  ?  154 TYR C CE1   1 
ATOM   7665  C  CE2   . TYR C  2  122 ? 58.035 39.420  -22.920 1.00 48.56  ?  154 TYR C CE2   1 
ATOM   7666  C  CZ    . TYR C  2  122 ? 56.805 38.991  -23.371 1.00 47.50  ?  154 TYR C CZ    1 
ATOM   7667  O  OH    . TYR C  2  122 ? 56.051 39.835  -24.139 1.00 42.56  ?  154 TYR C OH    1 
ATOM   7668  N  N     . TRP C  2  123 ? 61.116 36.652  -23.408 1.00 47.46  ?  155 TRP C N     1 
ATOM   7669  C  CA    . TRP C  2  123 ? 62.232 37.423  -23.995 1.00 48.86  ?  155 TRP C CA    1 
ATOM   7670  C  C     . TRP C  2  123 ? 61.866 38.914  -24.195 1.00 48.16  ?  155 TRP C C     1 
ATOM   7671  O  O     . TRP C  2  123 ? 60.932 39.242  -24.913 1.00 50.84  ?  155 TRP C O     1 
ATOM   7672  C  CB    . TRP C  2  123 ? 62.729 36.822  -25.326 1.00 48.66  ?  155 TRP C CB    1 
ATOM   7673  C  CG    . TRP C  2  123 ? 64.080 37.363  -25.715 1.00 50.20  ?  155 TRP C CG    1 
ATOM   7674  C  CD1   . TRP C  2  123 ? 65.300 36.832  -25.396 1.00 51.21  ?  155 TRP C CD1   1 
ATOM   7675  C  CD2   . TRP C  2  123 ? 64.349 38.571  -26.452 1.00 52.75  ?  155 TRP C CD2   1 
ATOM   7676  N  NE1   . TRP C  2  123 ? 66.310 37.626  -25.893 1.00 53.15  ?  155 TRP C NE1   1 
ATOM   7677  C  CE2   . TRP C  2  123 ? 65.758 38.698  -26.548 1.00 52.79  ?  155 TRP C CE2   1 
ATOM   7678  C  CE3   . TRP C  2  123 ? 63.538 39.554  -27.044 1.00 51.41  ?  155 TRP C CE3   1 
ATOM   7679  C  CZ2   . TRP C  2  123 ? 66.377 39.768  -27.227 1.00 51.02  ?  155 TRP C CZ2   1 
ATOM   7680  C  CZ3   . TRP C  2  123 ? 64.153 40.616  -27.708 1.00 51.37  ?  155 TRP C CZ3   1 
ATOM   7681  C  CH2   . TRP C  2  123 ? 65.562 40.710  -27.797 1.00 51.00  ?  155 TRP C CH2   1 
ATOM   7682  N  N     . PRO C  2  124 ? 62.610 39.829  -23.588 1.00 48.85  ?  156 PRO C N     1 
ATOM   7683  C  CA    . PRO C  2  124 ? 63.811 39.540  -22.755 1.00 49.27  ?  156 PRO C CA    1 
ATOM   7684  C  C     . PRO C  2  124 ? 63.423 38.968  -21.369 1.00 45.76  ?  156 PRO C C     1 
ATOM   7685  O  O     . PRO C  2  124 ? 62.283 39.137  -20.962 1.00 46.82  ?  156 PRO C O     1 
ATOM   7686  C  CB    . PRO C  2  124 ? 64.491 40.916  -22.631 1.00 49.80  ?  156 PRO C CB    1 
ATOM   7687  C  CG    . PRO C  2  124 ? 63.493 41.935  -23.139 1.00 49.41  ?  156 PRO C CG    1 
ATOM   7688  C  CD    . PRO C  2  124 ? 62.505 41.237  -24.018 1.00 48.10  ?  156 PRO C CD    1 
ATOM   7689  N  N     . GLN C  2  125 ? 64.323 38.309  -20.641 1.00 41.53  ?  157 GLN C N     1 
ATOM   7690  C  CA    . GLN C  2  125 ? 63.894 37.722  -19.366 1.00 41.78  ?  157 GLN C CA    1 
ATOM   7691  C  C     . GLN C  2  125 ? 63.250 38.761  -18.429 1.00 38.94  ?  157 GLN C C     1 
ATOM   7692  O  O     . GLN C  2  125 ? 63.514 39.955  -18.537 1.00 34.46  ?  157 GLN C O     1 
ATOM   7693  C  CB    . GLN C  2  125 ? 64.993 36.876  -18.665 1.00 44.07  ?  157 GLN C CB    1 
ATOM   7694  C  CG    . GLN C  2  125 ? 66.242 37.594  -18.160 1.00 44.52  ?  157 GLN C CG    1 
ATOM   7695  C  CD    . GLN C  2  125 ? 67.490 36.704  -18.253 1.00 48.31  ?  157 GLN C CD    1 
ATOM   7696  O  OE1   . GLN C  2  125 ? 67.817 36.148  -19.319 1.00 51.09  ?  157 GLN C OE1   1 
ATOM   7697  N  NE2   . GLN C  2  125 ? 68.193 36.564  -17.147 1.00 49.55  ?  157 GLN C NE2   1 
ATOM   7698  N  N     . ASP C  2  126 ? 62.340 38.276  -17.578 1.00 38.58  ?  158 ASP C N     1 
ATOM   7699  C  CA    . ASP C  2  126 ? 61.616 39.060  -16.566 1.00 38.95  ?  158 ASP C CA    1 
ATOM   7700  C  C     . ASP C  2  126 ? 60.676 40.169  -17.049 1.00 41.36  ?  158 ASP C C     1 
ATOM   7701  O  O     . ASP C  2  126 ? 60.064 40.842  -16.227 1.00 39.85  ?  158 ASP C O     1 
ATOM   7702  C  CB    . ASP C  2  126 ? 62.583 39.758  -15.627 1.00 38.50  ?  158 ASP C CB    1 
ATOM   7703  C  CG    . ASP C  2  126 ? 63.641 38.856  -15.129 1.00 38.24  ?  158 ASP C CG    1 
ATOM   7704  O  OD1   . ASP C  2  126 ? 63.801 37.752  -15.692 1.00 36.41  ?  158 ASP C OD1   1 
ATOM   7705  O  OD2   . ASP C  2  126 ? 64.327 39.271  -14.181 1.00 40.07  -1 158 ASP C OD2   1 
ATOM   7706  N  N     . GLN C  2  127 ? 60.540 40.350  -18.356 1.00 46.65  ?  159 GLN C N     1 
ATOM   7707  C  CA    . GLN C  2  127 ? 59.728 41.437  -18.908 1.00 51.55  ?  159 GLN C CA    1 
ATOM   7708  C  C     . GLN C  2  127 ? 58.367 40.867  -19.336 1.00 53.70  ?  159 GLN C C     1 
ATOM   7709  O  O     . GLN C  2  127 ? 57.929 41.061  -20.472 1.00 55.78  ?  159 GLN C O     1 
ATOM   7710  C  CB    . GLN C  2  127 ? 60.408 42.101  -20.111 1.00 53.38  ?  159 GLN C CB    1 
ATOM   7711  C  CG    . GLN C  2  127 ? 61.827 42.595  -19.857 1.00 54.29  ?  159 GLN C CG    1 
ATOM   7712  C  CD    . GLN C  2  127 ? 61.898 43.701  -18.820 1.00 54.25  ?  159 GLN C CD    1 
ATOM   7713  O  OE1   . GLN C  2  127 ? 61.463 44.839  -19.065 1.00 53.72  ?  159 GLN C OE1   1 
ATOM   7714  N  NE2   . GLN C  2  127 ? 62.480 43.380  -17.661 1.00 50.28  ?  159 GLN C NE2   1 
ATOM   7715  N  N     . LEU C  2  128 ? 57.704 40.162  -18.428 1.00 54.53  ?  160 LEU C N     1 
ATOM   7716  C  CA    . LEU C  2  128 ? 56.394 39.595  -18.712 1.00 56.26  ?  160 LEU C CA    1 
ATOM   7717  C  C     . LEU C  2  128 ? 55.349 40.731  -18.633 1.00 60.83  ?  160 LEU C C     1 
ATOM   7718  O  O     . LEU C  2  128 ? 55.309 41.462  -17.631 1.00 65.87  ?  160 LEU C O     1 
ATOM   7719  C  CB    . LEU C  2  128 ? 56.089 38.432  -17.745 1.00 54.33  ?  160 LEU C CB    1 
ATOM   7720  C  CG    . LEU C  2  128 ? 56.738 37.072  -18.107 1.00 52.81  ?  160 LEU C CG    1 
ATOM   7721  C  CD1   . LEU C  2  128 ? 58.193 36.996  -17.653 1.00 52.43  ?  160 LEU C CD1   1 
ATOM   7722  C  CD2   . LEU C  2  128 ? 55.947 35.876  -17.573 1.00 49.99  ?  160 LEU C CD2   1 
ATOM   7723  N  N     . PRO C  2  129 ? 54.531 40.909  -19.701 1.00 60.21  ?  161 PRO C N     1 
ATOM   7724  C  CA    . PRO C  2  129 ? 53.653 42.085  -19.786 1.00 60.10  ?  161 PRO C CA    1 
ATOM   7725  C  C     . PRO C  2  129 ? 52.250 41.977  -19.151 1.00 57.90  ?  161 PRO C C     1 
ATOM   7726  O  O     . PRO C  2  129 ? 51.832 40.902  -18.719 1.00 55.86  ?  161 PRO C O     1 
ATOM   7727  C  CB    . PRO C  2  129 ? 53.539 42.306  -21.306 1.00 60.57  ?  161 PRO C CB    1 
ATOM   7728  C  CG    . PRO C  2  129 ? 53.627 40.934  -21.881 1.00 59.50  ?  161 PRO C CG    1 
ATOM   7729  C  CD    . PRO C  2  129 ? 54.630 40.223  -21.007 1.00 60.46  ?  161 PRO C CD    1 
ATOM   7730  N  N     . VAL C  2  130 ? 51.570 43.132  -19.122 1.00 58.44  ?  162 VAL C N     1 
ATOM   7731  C  CA    . VAL C  2  130 ? 50.167 43.322  -18.691 1.00 55.82  ?  162 VAL C CA    1 
ATOM   7732  C  C     . VAL C  2  130 ? 49.155 42.781  -19.714 1.00 53.43  ?  162 VAL C C     1 
ATOM   7733  O  O     . VAL C  2  130 ? 48.071 42.305  -19.368 1.00 57.19  ?  162 VAL C O     1 
ATOM   7734  C  CB    . VAL C  2  130 ? 49.858 44.839  -18.552 1.00 55.48  ?  162 VAL C CB    1 
ATOM   7735  C  CG1   . VAL C  2  130 ? 48.402 45.086  -18.123 1.00 55.14  ?  162 VAL C CG1   1 
ATOM   7736  C  CG2   . VAL C  2  130 ? 50.855 45.505  -17.613 1.00 56.34  ?  162 VAL C CG2   1 
ATOM   7737  N  N     . VAL C  2  131 ? 49.516 42.886  -20.979 1.00 47.73  ?  163 VAL C N     1 
ATOM   7738  C  CA    . VAL C  2  131 ? 48.595 42.673  -22.064 1.00 45.72  ?  163 VAL C CA    1 
ATOM   7739  C  C     . VAL C  2  131 ? 49.045 41.465  -22.825 1.00 45.17  ?  163 VAL C C     1 
ATOM   7740  O  O     . VAL C  2  131 ? 50.128 40.945  -22.572 1.00 48.03  ?  163 VAL C O     1 
ATOM   7741  C  CB    . VAL C  2  131 ? 48.585 43.883  -23.014 1.00 46.16  ?  163 VAL C CB    1 
ATOM   7742  C  CG1   . VAL C  2  131 ? 48.249 45.157  -22.236 1.00 45.51  ?  163 VAL C CG1   1 
ATOM   7743  C  CG2   . VAL C  2  131 ? 49.911 44.005  -23.779 1.00 44.80  ?  163 VAL C CG2   1 
ATOM   7744  N  N     . THR C  2  132 ? 48.225 41.038  -23.776 1.00 44.39  ?  164 THR C N     1 
ATOM   7745  C  CA    . THR C  2  132 ? 48.542 39.865  -24.588 1.00 44.77  ?  164 THR C CA    1 
ATOM   7746  C  C     . THR C  2  132 ? 49.877 40.055  -25.347 1.00 41.86  ?  164 THR C C     1 
ATOM   7747  O  O     . THR C  2  132 ? 50.351 41.201  -25.547 1.00 38.37  ?  164 THR C O     1 
ATOM   7748  C  CB    . THR C  2  132 ? 47.358 39.439  -25.518 1.00 46.73  ?  164 THR C CB    1 
ATOM   7749  O  OG1   . THR C  2  132 ? 47.612 38.133  -26.075 1.00 45.31  ?  164 THR C OG1   1 
ATOM   7750  C  CG2   . THR C  2  132 ? 47.120 40.468  -26.647 1.00 47.08  ?  164 THR C CG2   1 
ATOM   7751  N  N     . SER C  2  133 ? 50.471 38.910  -25.712 1.00 38.70  ?  165 SER C N     1 
ATOM   7752  C  CA    . SER C  2  133 ? 51.868 38.820  -26.149 1.00 37.29  ?  165 SER C CA    1 
ATOM   7753  C  C     . SER C  2  133 ? 52.099 37.519  -26.906 1.00 37.20  ?  165 SER C C     1 
ATOM   7754  O  O     . SER C  2  133 ? 51.337 36.574  -26.748 1.00 37.01  ?  165 SER C O     1 
ATOM   7755  C  CB    . SER C  2  133 ? 52.819 38.876  -24.941 1.00 37.21  ?  165 SER C CB    1 
ATOM   7756  O  OG    . SER C  2  133 ? 53.072 37.581  -24.427 1.00 35.80  ?  165 SER C OG    1 
ATOM   7757  N  N     . LYS C  2  134 ? 53.167 37.474  -27.704 1.00 39.09  ?  166 LYS C N     1 
ATOM   7758  C  CA    . LYS C  2  134 ? 53.441 36.327  -28.595 1.00 41.20  ?  166 LYS C CA    1 
ATOM   7759  C  C     . LYS C  2  134 ? 53.768 35.037  -27.801 1.00 42.63  ?  166 LYS C C     1 
ATOM   7760  O  O     . LYS C  2  134 ? 53.497 33.927  -28.274 1.00 42.74  ?  166 LYS C O     1 
ATOM   7761  C  CB    . LYS C  2  134 ? 54.521 36.681  -29.664 1.00 39.58  ?  166 LYS C CB    1 
ATOM   7762  C  CG    . LYS C  2  134 ? 55.443 35.531  -30.052 1.00 38.38  ?  166 LYS C CG    1 
ATOM   7763  C  CD    . LYS C  2  134 ? 56.152 35.739  -31.367 1.00 37.03  ?  166 LYS C CD    1 
ATOM   7764  C  CE    . LYS C  2  134 ? 55.280 35.218  -32.481 1.00 37.32  ?  166 LYS C CE    1 
ATOM   7765  N  NZ    . LYS C  2  134 ? 56.039 35.251  -33.741 1.00 37.29  1  166 LYS C NZ    1 
ATOM   7766  N  N     . VAL C  2  135 ? 54.315 35.197  -26.594 1.00 45.11  ?  167 VAL C N     1 
ATOM   7767  C  CA    . VAL C  2  135 ? 54.616 34.066  -25.681 1.00 45.53  ?  167 VAL C CA    1 
ATOM   7768  C  C     . VAL C  2  135 ? 53.339 33.562  -24.953 1.00 41.48  ?  167 VAL C C     1 
ATOM   7769  O  O     . VAL C  2  135 ? 53.042 32.365  -24.927 1.00 37.99  ?  167 VAL C O     1 
ATOM   7770  C  CB    . VAL C  2  135 ? 55.717 34.474  -24.649 1.00 46.25  ?  167 VAL C CB    1 
ATOM   7771  C  CG1   . VAL C  2  135 ? 56.033 33.342  -23.678 1.00 45.26  ?  167 VAL C CG1   1 
ATOM   7772  C  CG2   . VAL C  2  135 ? 56.975 34.926  -25.378 1.00 47.01  ?  167 VAL C CG2   1 
ATOM   7773  N  N     . TYR C  2  136 ? 52.590 34.491  -24.377 1.00 39.14  ?  168 TYR C N     1 
ATOM   7774  C  CA    . TYR C  2  136 ? 51.309 34.184  -23.751 1.00 39.75  ?  168 TYR C CA    1 
ATOM   7775  C  C     . TYR C  2  136 ? 50.364 33.387  -24.687 1.00 40.81  ?  168 TYR C C     1 
ATOM   7776  O  O     . TYR C  2  136 ? 49.588 32.521  -24.247 1.00 38.18  ?  168 TYR C O     1 
ATOM   7777  C  CB    . TYR C  2  136 ? 50.643 35.499  -23.305 1.00 38.92  ?  168 TYR C CB    1 
ATOM   7778  C  CG    . TYR C  2  136 ? 51.272 36.197  -22.095 1.00 37.51  ?  168 TYR C CG    1 
ATOM   7779  C  CD1   . TYR C  2  136 ? 52.378 35.649  -21.403 1.00 37.97  ?  168 TYR C CD1   1 
ATOM   7780  C  CD2   . TYR C  2  136 ? 50.729 37.380  -21.610 1.00 35.40  ?  168 TYR C CD2   1 
ATOM   7781  C  CE1   . TYR C  2  136 ? 52.921 36.279  -20.286 1.00 35.85  ?  168 TYR C CE1   1 
ATOM   7782  C  CE2   . TYR C  2  136 ? 51.268 38.013  -20.504 1.00 36.19  ?  168 TYR C CE2   1 
ATOM   7783  C  CZ    . TYR C  2  136 ? 52.356 37.456  -19.839 1.00 35.76  ?  168 TYR C CZ    1 
ATOM   7784  O  OH    . TYR C  2  136 ? 52.880 38.097  -18.742 1.00 33.92  ?  168 TYR C OH    1 
ATOM   7785  N  N     . ASN C  2  137 ? 50.439 33.692  -25.979 1.00 42.30  ?  169 ASN C N     1 
ATOM   7786  C  CA    . ASN C  2  137 ? 49.633 33.007  -26.979 1.00 43.79  ?  169 ASN C CA    1 
ATOM   7787  C  C     . ASN C  2  137 ? 50.269 31.704  -27.395 1.00 46.69  ?  169 ASN C C     1 
ATOM   7788  O  O     . ASN C  2  137 ? 49.557 30.723  -27.659 1.00 48.21  ?  169 ASN C O     1 
ATOM   7789  C  CB    . ASN C  2  137 ? 49.417 33.900  -28.196 1.00 42.11  ?  169 ASN C CB    1 
ATOM   7790  C  CG    . ASN C  2  137 ? 48.418 35.004  -27.922 1.00 42.45  ?  169 ASN C CG    1 
ATOM   7791  O  OD1   . ASN C  2  137 ? 48.793 36.169  -27.769 1.00 43.59  ?  169 ASN C OD1   1 
ATOM   7792  N  ND2   . ASN C  2  137 ? 47.135 34.641  -27.825 1.00 41.15  ?  169 ASN C ND2   1 
ATOM   7793  N  N     . ALA C  2  138 ? 51.604 31.709  -27.458 1.00 47.90  ?  170 ALA C N     1 
ATOM   7794  C  CA    . ALA C  2  138 ? 52.392 30.523  -27.819 1.00 50.06  ?  170 ALA C CA    1 
ATOM   7795  C  C     . ALA C  2  138 ? 52.210 29.373  -26.821 1.00 53.89  ?  170 ALA C C     1 
ATOM   7796  O  O     . ALA C  2  138 ? 52.115 28.205  -27.223 1.00 55.32  ?  170 ALA C O     1 
ATOM   7797  C  CB    . ALA C  2  138 ? 53.869 30.877  -27.949 1.00 48.77  ?  170 ALA C CB    1 
ATOM   7798  N  N     . VAL C  2  139 ? 52.167 29.708  -25.528 1.00 53.93  ?  171 VAL C N     1 
ATOM   7799  C  CA    . VAL C  2  139 ? 51.903 28.710  -24.477 1.00 51.25  ?  171 VAL C CA    1 
ATOM   7800  C  C     . VAL C  2  139 ? 50.430 28.301  -24.421 1.00 50.27  ?  171 VAL C C     1 
ATOM   7801  O  O     . VAL C  2  139 ? 50.132 27.121  -24.274 1.00 49.61  ?  171 VAL C O     1 
ATOM   7802  C  CB    . VAL C  2  139 ? 52.389 29.161  -23.075 1.00 49.59  ?  171 VAL C CB    1 
ATOM   7803  C  CG1   . VAL C  2  139 ? 53.883 29.410  -23.107 1.00 49.92  ?  171 VAL C CG1   1 
ATOM   7804  C  CG2   . VAL C  2  139 ? 51.649 30.392  -22.561 1.00 49.43  ?  171 VAL C CG2   1 
ATOM   7805  N  N     . ALA C  2  140 ? 49.513 29.258  -24.557 1.00 49.17  ?  172 ALA C N     1 
ATOM   7806  C  CA    . ALA C  2  140 ? 48.089 28.928  -24.565 1.00 49.44  ?  172 ALA C CA    1 
ATOM   7807  C  C     . ALA C  2  140 ? 47.782 27.800  -25.571 1.00 49.72  ?  172 ALA C C     1 
ATOM   7808  O  O     . ALA C  2  140 ? 46.926 26.953  -25.305 1.00 46.85  ?  172 ALA C O     1 
ATOM   7809  C  CB    . ALA C  2  140 ? 47.245 30.166  -24.841 1.00 48.10  ?  172 ALA C CB    1 
ATOM   7810  N  N     . ASN C  2  141 ? 48.497 27.778  -26.700 1.00 52.04  ?  173 ASN C N     1 
ATOM   7811  C  CA    . ASN C  2  141 ? 48.368 26.692  -27.695 1.00 57.13  ?  173 ASN C CA    1 
ATOM   7812  C  C     . ASN C  2  141 ? 49.010 25.370  -27.232 1.00 55.36  ?  173 ASN C C     1 
ATOM   7813  O  O     . ASN C  2  141 ? 48.438 24.285  -27.394 1.00 56.78  ?  173 ASN C O     1 
ATOM   7814  C  CB    . ASN C  2  141 ? 48.963 27.106  -29.058 1.00 59.60  ?  173 ASN C CB    1 
ATOM   7815  C  CG    . ASN C  2  141 ? 48.240 28.298  -29.691 1.00 63.19  ?  173 ASN C CG    1 
ATOM   7816  O  OD1   . ASN C  2  141 ? 47.117 28.657  -29.314 1.00 61.88  ?  173 ASN C OD1   1 
ATOM   7817  N  ND2   . ASN C  2  141 ? 48.894 28.920  -30.663 1.00 65.95  ?  173 ASN C ND2   1 
ATOM   7818  N  N     . LEU C  2  142 ? 50.203 25.479  -26.658 1.00 51.68  ?  174 LEU C N     1 
ATOM   7819  C  CA    . LEU C  2  142 ? 50.943 24.331  -26.151 1.00 46.33  ?  174 LEU C CA    1 
ATOM   7820  C  C     . LEU C  2  142 ? 50.232 23.643  -24.996 1.00 44.41  ?  174 LEU C C     1 
ATOM   7821  O  O     . LEU C  2  142 ? 50.320 22.427  -24.860 1.00 43.45  ?  174 LEU C O     1 
ATOM   7822  C  CB    . LEU C  2  142 ? 52.323 24.784  -25.680 1.00 46.99  ?  174 LEU C CB    1 
ATOM   7823  C  CG    . LEU C  2  142 ? 53.299 25.256  -26.757 1.00 47.57  ?  174 LEU C CG    1 
ATOM   7824  C  CD1   . LEU C  2  142 ? 54.343 26.195  -26.169 1.00 47.79  ?  174 LEU C CD1   1 
ATOM   7825  C  CD2   . LEU C  2  142 ? 53.962 24.066  -27.437 1.00 46.86  ?  174 LEU C CD2   1 
ATOM   7826  N  N     . TRP C  2  143 ? 49.553 24.429  -24.157 1.00 45.04  ?  175 TRP C N     1 
ATOM   7827  C  CA    . TRP C  2  143 ? 48.903 23.923  -22.935 1.00 45.50  ?  175 TRP C CA    1 
ATOM   7828  C  C     . TRP C  2  143 ? 47.384 23.809  -23.063 1.00 47.74  ?  175 TRP C C     1 
ATOM   7829  O  O     . TRP C  2  143 ? 46.687 23.630  -22.062 1.00 49.18  ?  175 TRP C O     1 
ATOM   7830  C  CB    . TRP C  2  143 ? 49.278 24.786  -21.717 1.00 43.06  ?  175 TRP C CB    1 
ATOM   7831  C  CG    . TRP C  2  143 ? 50.759 24.870  -21.517 1.00 42.62  ?  175 TRP C CG    1 
ATOM   7832  C  CD1   . TRP C  2  143 ? 51.705 23.985  -21.974 1.00 42.55  ?  175 TRP C CD1   1 
ATOM   7833  C  CD2   . TRP C  2  143 ? 51.478 25.889  -20.812 1.00 43.31  ?  175 TRP C CD2   1 
ATOM   7834  N  NE1   . TRP C  2  143 ? 52.964 24.399  -21.610 1.00 42.37  ?  175 TRP C NE1   1 
ATOM   7835  C  CE2   . TRP C  2  143 ? 52.856 25.561  -20.890 1.00 42.52  ?  175 TRP C CE2   1 
ATOM   7836  C  CE3   . TRP C  2  143 ? 51.095 27.046  -20.113 1.00 45.26  ?  175 TRP C CE3   1 
ATOM   7837  C  CZ2   . TRP C  2  143 ? 53.851 26.346  -20.292 1.00 42.02  ?  175 TRP C CZ2   1 
ATOM   7838  C  CZ3   . TRP C  2  143 ? 52.090 27.833  -19.515 1.00 44.24  ?  175 TRP C CZ3   1 
ATOM   7839  C  CH2   . TRP C  2  143 ? 53.449 27.474  -19.612 1.00 43.41  ?  175 TRP C CH2   1 
ATOM   7840  N  N     . LYS C  2  144 ? 46.874 23.882  -24.292 1.00 48.85  ?  176 LYS C N     1 
ATOM   7841  C  CA    . LYS C  2  144 ? 45.469 23.595  -24.532 1.00 49.28  ?  176 LYS C CA    1 
ATOM   7842  C  C     . LYS C  2  144 ? 45.109 22.199  -24.053 1.00 46.57  ?  176 LYS C C     1 
ATOM   7843  O  O     . LYS C  2  144 ? 44.138 22.064  -23.308 1.00 49.96  ?  176 LYS C O     1 
ATOM   7844  C  CB    . LYS C  2  144 ? 45.074 23.800  -26.004 1.00 53.56  ?  176 LYS C CB    1 
ATOM   7845  C  CG    . LYS C  2  144 ? 44.192 25.035  -26.226 1.00 57.47  ?  176 LYS C CG    1 
ATOM   7846  C  CD    . LYS C  2  144 ? 44.508 25.794  -27.516 1.00 59.54  ?  176 LYS C CD    1 
ATOM   7847  C  CE    . LYS C  2  144 ? 44.358 24.938  -28.766 1.00 61.73  ?  176 LYS C CE    1 
ATOM   7848  N  NZ    . LYS C  2  144 ? 44.820 25.670  -29.974 1.00 64.08  1  176 LYS C NZ    1 
ATOM   7849  N  N     . PRO C  2  145 ? 45.909 21.170  -24.417 1.00 42.93  ?  177 PRO C N     1 
ATOM   7850  C  CA    . PRO C  2  145 ? 45.570 19.772  -24.070 1.00 42.68  ?  177 PRO C CA    1 
ATOM   7851  C  C     . PRO C  2  145 ? 45.285 19.529  -22.582 1.00 44.60  ?  177 PRO C C     1 
ATOM   7852  O  O     . PRO C  2  145 ? 44.679 18.522  -22.220 1.00 44.12  ?  177 PRO C O     1 
ATOM   7853  C  CB    . PRO C  2  145 ? 46.821 18.991  -24.479 1.00 41.85  ?  177 PRO C CB    1 
ATOM   7854  C  CG    . PRO C  2  145 ? 47.510 19.841  -25.478 1.00 41.81  ?  177 PRO C CG    1 
ATOM   7855  C  CD    . PRO C  2  145 ? 47.214 21.259  -25.095 1.00 42.16  ?  177 PRO C CD    1 
ATOM   7856  N  N     . TRP C  2  146 ? 45.733 20.454  -21.736 1.00 47.89  ?  178 TRP C N     1 
ATOM   7857  C  CA    . TRP C  2  146 ? 45.556 20.372  -20.294 1.00 46.05  ?  178 TRP C CA    1 
ATOM   7858  C  C     . TRP C  2  146 ? 44.594 21.404  -19.704 1.00 48.03  ?  178 TRP C C     1 
ATOM   7859  O  O     . TRP C  2  146 ? 44.293 21.320  -18.518 1.00 48.58  ?  178 TRP C O     1 
ATOM   7860  C  CB    . TRP C  2  146 ? 46.906 20.578  -19.611 1.00 44.41  ?  178 TRP C CB    1 
ATOM   7861  C  CG    . TRP C  2  146 ? 47.974 19.610  -19.986 1.00 41.73  ?  178 TRP C CG    1 
ATOM   7862  C  CD1   . TRP C  2  146 ? 47.827 18.279  -20.239 1.00 41.56  ?  178 TRP C CD1   1 
ATOM   7863  C  CD2   . TRP C  2  146 ? 49.367 19.895  -20.104 1.00 40.35  ?  178 TRP C CD2   1 
ATOM   7864  N  NE1   . TRP C  2  146 ? 49.046 17.718  -20.520 1.00 41.94  ?  178 TRP C NE1   1 
ATOM   7865  C  CE2   . TRP C  2  146 ? 50.011 18.689  -20.444 1.00 42.04  ?  178 TRP C CE2   1 
ATOM   7866  C  CE3   . TRP C  2  146 ? 50.132 21.055  -19.970 1.00 40.73  ?  178 TRP C CE3   1 
ATOM   7867  C  CZ2   . TRP C  2  146 ? 51.398 18.606  -20.641 1.00 42.54  ?  178 TRP C CZ2   1 
ATOM   7868  C  CZ3   . TRP C  2  146 ? 51.508 20.978  -20.174 1.00 41.61  ?  178 TRP C CZ3   1 
ATOM   7869  C  CH2   . TRP C  2  146 ? 52.128 19.758  -20.500 1.00 42.31  ?  178 TRP C CH2   1 
ATOM   7870  N  N     . LEU C  2  147 ? 44.125 22.380  -20.478 1.00 51.05  ?  179 LEU C N     1 
ATOM   7871  C  CA    . LEU C  2  147 ? 43.340 23.453  -19.878 1.00 57.89  ?  179 LEU C CA    1 
ATOM   7872  C  C     . LEU C  2  147 ? 42.006 23.785  -20.590 1.00 61.40  ?  179 LEU C C     1 
ATOM   7873  O  O     . LEU C  2  147 ? 41.843 23.534  -21.789 1.00 60.87  ?  179 LEU C O     1 
ATOM   7874  C  CB    . LEU C  2  147 ? 44.221 24.703  -19.718 1.00 60.67  ?  179 LEU C CB    1 
ATOM   7875  C  CG    . LEU C  2  147 ? 45.558 24.528  -18.957 1.00 65.20  ?  179 LEU C CG    1 
ATOM   7876  C  CD1   . LEU C  2  147 ? 46.374 25.824  -18.969 1.00 68.40  ?  179 LEU C CD1   1 
ATOM   7877  C  CD2   . LEU C  2  147 ? 45.397 24.041  -17.515 1.00 63.68  ?  179 LEU C CD2   1 
ATOM   7878  N  N     . ASP C  2  148 ? 41.064 24.325  -19.801 1.00 61.32  ?  180 ASP C N     1 
ATOM   7879  C  CA    . ASP C  2  148 ? 39.762 24.845  -20.257 1.00 61.34  ?  180 ASP C CA    1 
ATOM   7880  C  C     . ASP C  2  148 ? 39.901 25.842  -21.396 1.00 62.84  ?  180 ASP C C     1 
ATOM   7881  O  O     . ASP C  2  148 ? 40.992 26.293  -21.690 1.00 62.95  ?  180 ASP C O     1 
ATOM   7882  C  CB    . ASP C  2  148 ? 39.064 25.601  -19.105 1.00 62.83  ?  180 ASP C CB    1 
ATOM   7883  C  CG    . ASP C  2  148 ? 38.077 24.753  -18.299 1.00 63.67  ?  180 ASP C CG    1 
ATOM   7884  O  OD1   . ASP C  2  148 ? 37.861 23.553  -18.578 1.00 61.10  ?  180 ASP C OD1   1 
ATOM   7885  O  OD2   . ASP C  2  148 ? 37.491 25.333  -17.359 1.00 64.62  -1 180 ASP C OD2   1 
ATOM   7886  N  N     . GLU C  2  149 ? 38.779 26.197  -22.019 1.00 70.26  ?  181 GLU C N     1 
ATOM   7887  C  CA    . GLU C  2  149 ? 38.701 27.400  -22.868 1.00 71.31  ?  181 GLU C CA    1 
ATOM   7888  C  C     . GLU C  2  149 ? 38.779 28.624  -21.958 1.00 67.96  ?  181 GLU C C     1 
ATOM   7889  O  O     . GLU C  2  149 ? 39.301 29.667  -22.344 1.00 63.91  ?  181 GLU C O     1 
ATOM   7890  C  CB    . GLU C  2  149 ? 37.364 27.502  -23.614 1.00 74.28  ?  181 GLU C CB    1 
ATOM   7891  C  CG    . GLU C  2  149 ? 36.926 26.297  -24.435 1.00 75.47  ?  181 GLU C CG    1 
ATOM   7892  C  CD    . GLU C  2  149 ? 35.423 26.292  -24.688 1.00 74.42  ?  181 GLU C CD    1 
ATOM   7893  O  OE1   . GLU C  2  149 ? 34.756 27.326  -24.468 1.00 69.87  ?  181 GLU C OE1   1 
ATOM   7894  O  OE2   . GLU C  2  149 ? 34.904 25.245  -25.112 1.00 73.33  -1 181 GLU C OE2   1 
ATOM   7895  N  N     . GLU C  2  150 ? 38.196 28.477  -20.768 1.00 64.77  ?  182 GLU C N     1 
ATOM   7896  C  CA    . GLU C  2  150 ? 38.131 29.523  -19.759 1.00 65.40  ?  182 GLU C CA    1 
ATOM   7897  C  C     . GLU C  2  150 ? 39.519 29.853  -19.211 1.00 61.88  ?  182 GLU C C     1 
ATOM   7898  O  O     . GLU C  2  150 ? 39.897 31.025  -19.099 1.00 58.71  ?  182 GLU C O     1 
ATOM   7899  C  CB    . GLU C  2  150 ? 37.198 29.090  -18.613 1.00 69.66  ?  182 GLU C CB    1 
ATOM   7900  C  CG    . GLU C  2  150 ? 35.711 28.989  -18.975 1.00 73.42  ?  182 GLU C CG    1 
ATOM   7901  C  CD    . GLU C  2  150 ? 35.318 27.666  -19.636 1.00 77.28  ?  182 GLU C CD    1 
ATOM   7902  O  OE1   . GLU C  2  150 ? 35.273 26.618  -18.946 1.00 72.66  ?  182 GLU C OE1   1 
ATOM   7903  O  OE2   . GLU C  2  150 ? 35.039 27.677  -20.857 1.00 82.25  -1 182 GLU C OE2   1 
ATOM   7904  N  N     . ALA C  2  151 ? 40.266 28.811  -18.875 1.00 57.68  ?  183 ALA C N     1 
ATOM   7905  C  CA    . ALA C  2  151 ? 41.606 28.960  -18.337 1.00 57.82  ?  183 ALA C CA    1 
ATOM   7906  C  C     . ALA C  2  151 ? 42.490 29.630  -19.371 1.00 57.77  ?  183 ALA C C     1 
ATOM   7907  O  O     . ALA C  2  151 ? 43.117 30.660  -19.102 1.00 58.46  ?  183 ALA C O     1 
ATOM   7908  C  CB    . ALA C  2  151 ? 42.171 27.599  -17.966 1.00 58.67  ?  183 ALA C CB    1 
ATOM   7909  N  N     . ILE C  2  152 ? 42.513 29.024  -20.556 1.00 57.59  ?  184 ILE C N     1 
ATOM   7910  C  CA    . ILE C  2  152 ? 43.248 29.529  -21.729 1.00 57.32  ?  184 ILE C CA    1 
ATOM   7911  C  C     . ILE C  2  152 ? 42.962 31.021  -22.049 1.00 56.54  ?  184 ILE C C     1 
ATOM   7912  O  O     . ILE C  2  152 ? 43.862 31.752  -22.460 1.00 53.41  ?  184 ILE C O     1 
ATOM   7913  C  CB    . ILE C  2  152 ? 42.965 28.616  -22.960 1.00 54.75  ?  184 ILE C CB    1 
ATOM   7914  C  CG1   . ILE C  2  152 ? 43.710 27.273  -22.823 1.00 53.98  ?  184 ILE C CG1   1 
ATOM   7915  C  CG2   . ILE C  2  152 ? 43.307 29.291  -24.282 1.00 55.57  ?  184 ILE C CG2   1 
ATOM   7916  C  CD1   . ILE C  2  152 ? 45.219 27.334  -22.913 1.00 53.05  ?  184 ILE C CD1   1 
ATOM   7917  N  N     . SER C  2  153 ? 41.726 31.466  -21.846 1.00 58.41  ?  185 SER C N     1 
ATOM   7918  C  CA    . SER C  2  153 ? 41.361 32.866  -22.080 1.00 62.16  ?  185 SER C CA    1 
ATOM   7919  C  C     . SER C  2  153 ? 42.300 33.807  -21.348 1.00 62.61  ?  185 SER C C     1 
ATOM   7920  O  O     . SER C  2  153 ? 42.873 34.703  -21.961 1.00 63.63  ?  185 SER C O     1 
ATOM   7921  C  CB    . SER C  2  153 ? 39.934 33.152  -21.604 1.00 65.43  ?  185 SER C CB    1 
ATOM   7922  O  OG    . SER C  2  153 ? 39.081 32.058  -21.875 1.00 71.31  ?  185 SER C OG    1 
ATOM   7923  N  N     . THR C  2  154 ? 42.441 33.588  -20.036 1.00 59.08  ?  186 THR C N     1 
ATOM   7924  C  CA    . THR C  2  154 ? 43.293 34.422  -19.176 1.00 52.87  ?  186 THR C CA    1 
ATOM   7925  C  C     . THR C  2  154 ? 44.787 34.116  -19.339 1.00 50.99  ?  186 THR C C     1 
ATOM   7926  O  O     . THR C  2  154 ? 45.632 34.976  -19.075 1.00 48.64  ?  186 THR C O     1 
ATOM   7927  C  CB    . THR C  2  154 ? 42.917 34.311  -17.672 1.00 50.35  ?  186 THR C CB    1 
ATOM   7928  O  OG1   . THR C  2  154 ? 42.180 33.108  -17.428 1.00 47.28  ?  186 THR C OG1   1 
ATOM   7929  C  CG2   . THR C  2  154 ? 42.101 35.513  -17.226 1.00 49.78  ?  186 THR C CG2   1 
ATOM   7930  N  N     . LEU C  2  155 ? 45.122 32.897  -19.749 1.00 49.71  ?  187 LEU C N     1 
ATOM   7931  C  CA    . LEU C  2  155 ? 46.517 32.563  -20.008 1.00 50.29  ?  187 LEU C CA    1 
ATOM   7932  C  C     . LEU C  2  155 ? 47.125 33.500  -21.060 1.00 52.75  ?  187 LEU C C     1 
ATOM   7933  O  O     . LEU C  2  155 ? 48.211 34.041  -20.846 1.00 54.13  ?  187 LEU C O     1 
ATOM   7934  C  CB    . LEU C  2  155 ? 46.650 31.102  -20.433 1.00 49.39  ?  187 LEU C CB    1 
ATOM   7935  C  CG    . LEU C  2  155 ? 48.075 30.530  -20.483 1.00 48.96  ?  187 LEU C CG    1 
ATOM   7936  C  CD1   . LEU C  2  155 ? 48.931 30.856  -19.252 1.00 47.30  ?  187 LEU C CD1   1 
ATOM   7937  C  CD2   . LEU C  2  155 ? 47.989 29.027  -20.700 1.00 49.00  ?  187 LEU C CD2   1 
ATOM   7938  N  N     . ARG C  2  156 ? 46.403 33.714  -22.165 1.00 55.02  ?  188 ARG C N     1 
ATOM   7939  C  CA    . ARG C  2  156 ? 46.801 34.673  -23.229 1.00 54.57  ?  188 ARG C CA    1 
ATOM   7940  C  C     . ARG C  2  156 ? 46.775 36.125  -22.768 1.00 55.09  ?  188 ARG C C     1 
ATOM   7941  O  O     . ARG C  2  156 ? 47.592 36.914  -23.210 1.00 60.57  ?  188 ARG C O     1 
ATOM   7942  C  CB    . ARG C  2  156 ? 45.862 34.610  -24.439 1.00 55.52  ?  188 ARG C CB    1 
ATOM   7943  C  CG    . ARG C  2  156 ? 45.565 33.224  -24.990 1.00 57.35  ?  188 ARG C CG    1 
ATOM   7944  C  CD    . ARG C  2  156 ? 44.489 33.294  -26.058 1.00 55.89  ?  188 ARG C CD    1 
ATOM   7945  N  NE    . ARG C  2  156 ? 43.976 31.986  -26.474 1.00 53.23  ?  188 ARG C NE    1 
ATOM   7946  C  CZ    . ARG C  2  156 ? 44.637 31.084  -27.208 1.00 51.18  ?  188 ARG C CZ    1 
ATOM   7947  N  NH1   . ARG C  2  156 ? 45.900 31.277  -27.619 1.00 48.33  1  188 ARG C NH1   1 
ATOM   7948  N  NH2   . ARG C  2  156 ? 44.015 29.952  -27.520 1.00 51.54  ?  188 ARG C NH2   1 
ATOM   7949  N  N     . LYS C  2  157 ? 45.797 36.478  -21.931 1.00 54.60  ?  189 LYS C N     1 
ATOM   7950  C  CA    . LYS C  2  157 ? 45.635 37.847  -21.421 1.00 54.78  ?  189 LYS C CA    1 
ATOM   7951  C  C     . LYS C  2  157 ? 46.813 38.296  -20.535 1.00 55.03  ?  189 LYS C C     1 
ATOM   7952  O  O     . LYS C  2  157 ? 47.395 39.355  -20.792 1.00 57.21  ?  189 LYS C O     1 
ATOM   7953  C  CB    . LYS C  2  157 ? 44.305 38.005  -20.640 1.00 57.31  ?  189 LYS C CB    1 
ATOM   7954  C  CG    . LYS C  2  157 ? 43.087 38.561  -21.395 1.00 56.49  ?  189 LYS C CG    1 
ATOM   7955  C  CD    . LYS C  2  157 ? 42.561 37.626  -22.479 1.00 60.20  ?  189 LYS C CD    1 
ATOM   7956  C  CE    . LYS C  2  157 ? 42.993 38.057  -23.894 1.00 64.54  ?  189 LYS C CE    1 
ATOM   7957  N  NZ    . LYS C  2  157 ? 42.959 36.977  -24.934 1.00 62.99  1  189 LYS C NZ    1 
ATOM   7958  N  N     . GLY C  2  158 ? 47.154 37.505  -19.505 1.00 55.83  ?  190 GLY C N     1 
ATOM   7959  C  CA    . GLY C  2  158 ? 48.174 37.899  -18.493 1.00 54.05  ?  190 GLY C CA    1 
ATOM   7960  C  C     . GLY C  2  158 ? 49.242 36.903  -18.041 1.00 49.52  ?  190 GLY C C     1 
ATOM   7961  O  O     . GLY C  2  158 ? 50.119 37.254  -17.261 1.00 43.75  ?  190 GLY C O     1 
ATOM   7962  N  N     . GLY C  2  159 ? 49.194 35.676  -18.543 1.00 49.72  ?  191 GLY C N     1 
ATOM   7963  C  CA    . GLY C  2  159 ? 50.123 34.633  -18.102 1.00 51.41  ?  191 GLY C CA    1 
ATOM   7964  C  C     . GLY C  2  159 ? 49.541 33.683  -17.059 1.00 50.92  ?  191 GLY C C     1 
ATOM   7965  O  O     . GLY C  2  159 ? 50.209 32.724  -16.653 1.00 47.82  ?  191 GLY C O     1 
ATOM   7966  N  N     . PHE C  2  160 ? 48.288 33.925  -16.658 1.00 48.24  ?  192 PHE C N     1 
ATOM   7967  C  CA    . PHE C  2  160 ? 47.661 33.176  -15.570 1.00 44.99  ?  192 PHE C CA    1 
ATOM   7968  C  C     . PHE C  2  160 ? 46.290 32.578  -15.910 1.00 44.17  ?  192 PHE C C     1 
ATOM   7969  O  O     . PHE C  2  160 ? 45.714 32.828  -16.958 1.00 42.32  ?  192 PHE C O     1 
ATOM   7970  C  CB    . PHE C  2  160 ? 47.562 34.051  -14.333 1.00 42.12  ?  192 PHE C CB    1 
ATOM   7971  C  CG    . PHE C  2  160 ? 46.749 35.276  -14.530 1.00 41.77  ?  192 PHE C CG    1 
ATOM   7972  C  CD1   . PHE C  2  160 ? 45.400 35.281  -14.212 1.00 41.96  ?  192 PHE C CD1   1 
ATOM   7973  C  CD2   . PHE C  2  160 ? 47.336 36.441  -15.014 1.00 41.66  ?  192 PHE C CD2   1 
ATOM   7974  C  CE1   . PHE C  2  160 ? 44.644 36.430  -14.378 1.00 41.64  ?  192 PHE C CE1   1 
ATOM   7975  C  CE2   . PHE C  2  160 ? 46.591 37.594  -15.170 1.00 41.84  ?  192 PHE C CE2   1 
ATOM   7976  C  CZ    . PHE C  2  160 ? 45.240 37.587  -14.857 1.00 42.02  ?  192 PHE C CZ    1 
ATOM   7977  N  N     . TYR C  2  161 ? 45.797 31.750  -15.001 1.00 45.08  ?  193 TYR C N     1 
ATOM   7978  C  CA    . TYR C  2  161 ? 44.583 30.984  -15.215 1.00 45.89  ?  193 TYR C CA    1 
ATOM   7979  C  C     . TYR C  2  161 ? 44.231 30.244  -13.944 1.00 44.66  ?  193 TYR C C     1 
ATOM   7980  O  O     . TYR C  2  161 ? 45.050 30.163  -13.054 1.00 46.76  ?  193 TYR C O     1 
ATOM   7981  C  CB    . TYR C  2  161 ? 44.797 29.970  -16.338 1.00 46.23  ?  193 TYR C CB    1 
ATOM   7982  C  CG    . TYR C  2  161 ? 45.767 28.825  -16.048 1.00 45.25  ?  193 TYR C CG    1 
ATOM   7983  C  CD1   . TYR C  2  161 ? 47.092 28.875  -16.467 1.00 43.47  ?  193 TYR C CD1   1 
ATOM   7984  C  CD2   . TYR C  2  161 ? 45.340 27.668  -15.409 1.00 46.58  ?  193 TYR C CD2   1 
ATOM   7985  C  CE1   . TYR C  2  161 ? 47.960 27.815  -16.253 1.00 40.54  ?  193 TYR C CE1   1 
ATOM   7986  C  CE2   . TYR C  2  161 ? 46.212 26.606  -15.182 1.00 44.13  ?  193 TYR C CE2   1 
ATOM   7987  C  CZ    . TYR C  2  161 ? 47.513 26.686  -15.610 1.00 40.67  ?  193 TYR C CZ    1 
ATOM   7988  O  OH    . TYR C  2  161 ? 48.344 25.626  -15.371 1.00 38.94  ?  193 TYR C OH    1 
ATOM   7989  N  N     . SER C  2  162 ? 43.029 29.702  -13.849 1.00 42.79  ?  194 SER C N     1 
ATOM   7990  C  CA    . SER C  2  162 ? 42.718 28.807  -12.750 1.00 43.60  ?  194 SER C CA    1 
ATOM   7991  C  C     . SER C  2  162 ? 41.994 27.647  -13.347 1.00 46.10  ?  194 SER C C     1 
ATOM   7992  O  O     . SER C  2  162 ? 41.492 27.760  -14.457 1.00 51.59  ?  194 SER C O     1 
ATOM   7993  C  CB    . SER C  2  162 ? 41.842 29.480  -11.710 1.00 43.34  ?  194 SER C CB    1 
ATOM   7994  O  OG    . SER C  2  162 ? 40.526 29.582  -12.194 1.00 43.38  ?  194 SER C OG    1 
ATOM   7995  N  N     . GLN C  2  163 ? 41.915 26.533  -12.630 1.00 47.02  ?  195 GLN C N     1 
ATOM   7996  C  CA    . GLN C  2  163 ? 41.427 25.306  -13.257 1.00 46.93  ?  195 GLN C CA    1 
ATOM   7997  C  C     . GLN C  2  163 ? 41.113 24.172  -12.272 1.00 46.53  ?  195 GLN C C     1 
ATOM   7998  O  O     . GLN C  2  163 ? 41.980 23.726  -11.506 1.00 47.12  ?  195 GLN C O     1 
ATOM   7999  C  CB    . GLN C  2  163 ? 42.470 24.842  -14.307 1.00 46.62  ?  195 GLN C CB    1 
ATOM   8000  C  CG    . GLN C  2  163 ? 42.192 23.523  -15.042 1.00 45.20  ?  195 GLN C CG    1 
ATOM   8001  C  CD    . GLN C  2  163 ? 41.120 23.629  -16.106 1.00 41.72  ?  195 GLN C CD    1 
ATOM   8002  O  OE1   . GLN C  2  163 ? 41.028 24.630  -16.817 1.00 42.68  ?  195 GLN C OE1   1 
ATOM   8003  N  NE2   . GLN C  2  163 ? 40.319 22.590  -16.234 1.00 38.74  ?  195 GLN C NE2   1 
ATOM   8004  N  N     . LYS C  2  164 ? 39.878 23.686  -12.336 1.00 44.93  ?  196 LYS C N     1 
ATOM   8005  C  CA    . LYS C  2  164 ? 39.497 22.472  -11.638 1.00 45.30  ?  196 LYS C CA    1 
ATOM   8006  C  C     . LYS C  2  164 ? 40.379 21.342  -12.129 1.00 42.35  ?  196 LYS C C     1 
ATOM   8007  O  O     . LYS C  2  164 ? 40.701 21.288  -13.302 1.00 38.38  ?  196 LYS C O     1 
ATOM   8008  C  CB    . LYS C  2  164 ? 38.033 22.137  -11.924 1.00 50.74  ?  196 LYS C CB    1 
ATOM   8009  C  CG    . LYS C  2  164 ? 37.030 23.146  -11.366 1.00 57.21  ?  196 LYS C CG    1 
ATOM   8010  C  CD    . LYS C  2  164 ? 35.615 22.975  -11.931 1.00 61.43  ?  196 LYS C CD    1 
ATOM   8011  C  CE    . LYS C  2  164 ? 35.478 23.500  -13.362 1.00 64.61  ?  196 LYS C CE    1 
ATOM   8012  N  NZ    . LYS C  2  164 ? 34.071 23.856  -13.690 1.00 65.00  1  196 LYS C NZ    1 
ATOM   8013  N  N     . VAL C  2  165 ? 40.784 20.449  -11.235 1.00 44.78  ?  197 VAL C N     1 
ATOM   8014  C  CA    . VAL C  2  165 ? 41.551 19.266  -11.637 1.00 47.88  ?  197 VAL C CA    1 
ATOM   8015  C  C     . VAL C  2  165 ? 40.595 18.231  -12.203 1.00 50.60  ?  197 VAL C C     1 
ATOM   8016  O  O     . VAL C  2  165 ? 39.524 18.022  -11.641 1.00 49.26  ?  197 VAL C O     1 
ATOM   8017  C  CB    . VAL C  2  165 ? 42.306 18.634  -10.449 1.00 49.40  ?  197 VAL C CB    1 
ATOM   8018  C  CG1   . VAL C  2  165 ? 42.958 17.306  -10.841 1.00 50.13  ?  197 VAL C CG1   1 
ATOM   8019  C  CG2   . VAL C  2  165 ? 43.346 19.603  -9.902  1.00 49.68  ?  197 VAL C CG2   1 
ATOM   8020  N  N     . THR C  2  166 ? 40.992 17.580  -13.300 1.00 55.11  ?  198 THR C N     1 
ATOM   8021  C  CA    . THR C  2  166 ? 40.136 16.591  -13.993 1.00 55.96  ?  198 THR C CA    1 
ATOM   8022  C  C     . THR C  2  166 ? 39.753 15.448  -13.065 1.00 55.49  ?  198 THR C C     1 
ATOM   8023  O  O     . THR C  2  166 ? 38.583 15.093  -12.965 1.00 55.47  ?  198 THR C O     1 
ATOM   8024  C  CB    . THR C  2  166 ? 40.806 16.026  -15.277 1.00 54.87  ?  198 THR C CB    1 
ATOM   8025  O  OG1   . THR C  2  166 ? 40.622 16.957  -16.347 1.00 50.95  ?  198 THR C OG1   1 
ATOM   8026  C  CG2   . THR C  2  166 ? 40.215 14.655  -15.690 1.00 53.57  ?  198 THR C CG2   1 
ATOM   8027  N  N     . THR C  2  167 ? 40.739 14.891  -12.376 1.00 54.76  ?  199 THR C N     1 
ATOM   8028  C  CA    . THR C  2  167 ? 40.496 13.764  -11.493 1.00 56.10  ?  199 THR C CA    1 
ATOM   8029  C  C     . THR C  2  167 ? 40.013 14.151  -10.102 1.00 52.13  ?  199 THR C C     1 
ATOM   8030  O  O     . THR C  2  167 ? 39.909 13.282  -9.257  1.00 53.66  ?  199 THR C O     1 
ATOM   8031  C  CB    . THR C  2  167 ? 41.770 12.928  -11.306 1.00 60.89  ?  199 THR C CB    1 
ATOM   8032  O  OG1   . THR C  2  167 ? 42.734 13.692  -10.568 1.00 64.75  ?  199 THR C OG1   1 
ATOM   8033  C  CG2   . THR C  2  167 ? 42.342 12.510  -12.670 1.00 61.72  ?  199 THR C CG2   1 
ATOM   8034  N  N     . ASN C  2  168 ? 39.747 15.431  -9.856  1.00 49.39  ?  200 ASN C N     1 
ATOM   8035  C  CA    . ASN C  2  168 ? 39.333 15.918  -8.531  1.00 50.24  ?  200 ASN C CA    1 
ATOM   8036  C  C     . ASN C  2  168 ? 38.649 17.283  -8.666  1.00 56.14  ?  200 ASN C C     1 
ATOM   8037  O  O     . ASN C  2  168 ? 39.117 18.278  -8.112  1.00 58.43  ?  200 ASN C O     1 
ATOM   8038  C  CB    . ASN C  2  168 ? 40.545 16.093  -7.600  1.00 46.80  ?  200 ASN C CB    1 
ATOM   8039  C  CG    . ASN C  2  168 ? 41.119 14.785  -7.118  1.00 44.36  ?  200 ASN C CG    1 
ATOM   8040  O  OD1   . ASN C  2  168 ? 40.757 14.304  -6.038  1.00 42.04  ?  200 ASN C OD1   1 
ATOM   8041  N  ND2   . ASN C  2  168 ? 42.028 14.202  -7.908  1.00 43.42  ?  200 ASN C ND2   1 
ATOM   8042  N  N     . PRO C  2  169 ? 37.525 17.342  -9.384  1.00 59.77  ?  201 PRO C N     1 
ATOM   8043  C  CA    . PRO C  2  169 ? 37.017 18.637  -9.896  1.00 59.87  ?  201 PRO C CA    1 
ATOM   8044  C  C     . PRO C  2  169 ? 36.465 19.668  -8.877  1.00 58.68  ?  201 PRO C C     1 
ATOM   8045  O  O     . PRO C  2  169 ? 35.893 20.695  -9.277  1.00 56.90  ?  201 PRO C O     1 
ATOM   8046  C  CB    . PRO C  2  169 ? 35.932 18.212  -10.895 1.00 62.50  ?  201 PRO C CB    1 
ATOM   8047  C  CG    . PRO C  2  169 ? 36.099 16.723  -11.086 1.00 63.17  ?  201 PRO C CG    1 
ATOM   8048  C  CD    . PRO C  2  169 ? 36.681 16.215  -9.804  1.00 60.79  ?  201 PRO C CD    1 
ATOM   8049  N  N     . ASN C  2  170 ? 36.621 19.401  -7.585  1.00 57.70  ?  202 ASN C N     1 
ATOM   8050  C  CA    . ASN C  2  170 ? 36.434 20.440  -6.574  1.00 58.91  ?  202 ASN C CA    1 
ATOM   8051  C  C     . ASN C  2  170 ? 37.780 20.882  -5.973  1.00 60.31  ?  202 ASN C C     1 
ATOM   8052  O  O     . ASN C  2  170 ? 37.828 21.619  -4.982  1.00 68.47  ?  202 ASN C O     1 
ATOM   8053  C  CB    . ASN C  2  170 ? 35.441 19.998  -5.492  1.00 57.25  ?  202 ASN C CB    1 
ATOM   8054  C  CG    . ASN C  2  170 ? 35.819 18.692  -4.843  1.00 57.00  ?  202 ASN C CG    1 
ATOM   8055  O  OD1   . ASN C  2  170 ? 36.447 17.833  -5.463  1.00 56.19  ?  202 ASN C OD1   1 
ATOM   8056  N  ND2   . ASN C  2  170 ? 35.424 18.525  -3.589  1.00 58.11  ?  202 ASN C ND2   1 
ATOM   8057  N  N     . LEU C  2  171 ? 38.867 20.422  -6.588  1.00 55.03  ?  203 LEU C N     1 
ATOM   8058  C  CA    . LEU C  2  171 ? 40.198 20.952  -6.349  1.00 48.54  ?  203 LEU C CA    1 
ATOM   8059  C  C     . LEU C  2  171 ? 40.498 21.901  -7.510  1.00 44.11  ?  203 LEU C C     1 
ATOM   8060  O  O     . LEU C  2  171 ? 40.601 21.473  -8.660  1.00 39.21  ?  203 LEU C O     1 
ATOM   8061  C  CB    . LEU C  2  171 ? 41.214 19.800  -6.296  1.00 47.71  ?  203 LEU C CB    1 
ATOM   8062  C  CG    . LEU C  2  171 ? 42.681 20.163  -6.064  1.00 46.91  ?  203 LEU C CG    1 
ATOM   8063  C  CD1   . LEU C  2  171 ? 42.782 20.883  -4.726  1.00 47.89  ?  203 LEU C CD1   1 
ATOM   8064  C  CD2   . LEU C  2  171 ? 43.611 18.946  -6.148  1.00 44.18  ?  203 LEU C CD2   1 
ATOM   8065  N  N     . ARG C  2  172 ? 40.595 23.192  -7.233  1.00 42.93  ?  204 ARG C N     1 
ATOM   8066  C  CA    . ARG C  2  172 ? 41.007 24.123  -8.285  1.00 45.30  ?  204 ARG C CA    1 
ATOM   8067  C  C     . ARG C  2  172 ? 42.476 24.529  -8.152  1.00 44.28  ?  204 ARG C C     1 
ATOM   8068  O  O     . ARG C  2  172 ? 42.886 25.051  -7.121  1.00 47.27  ?  204 ARG C O     1 
ATOM   8069  C  CB    . ARG C  2  172 ? 40.133 25.377  -8.309  1.00 45.82  ?  204 ARG C CB    1 
ATOM   8070  C  CG    . ARG C  2  172 ? 40.558 26.388  -9.374  1.00 47.29  ?  204 ARG C CG    1 
ATOM   8071  C  CD    . ARG C  2  172 ? 39.730 27.650  -9.267  1.00 50.74  ?  204 ARG C CD    1 
ATOM   8072  N  NE    . ARG C  2  172 ? 38.305 27.344  -9.377  1.00 50.22  ?  204 ARG C NE    1 
ATOM   8073  C  CZ    . ARG C  2  172 ? 37.655 27.171  -10.524 1.00 47.50  ?  204 ARG C CZ    1 
ATOM   8074  N  NH1   . ARG C  2  172 ? 38.281 27.272  -11.702 1.00 47.20  1  204 ARG C NH1   1 
ATOM   8075  N  NH2   . ARG C  2  172 ? 36.368 26.875  -10.488 1.00 45.10  ?  204 ARG C NH2   1 
ATOM   8076  N  N     . ILE C  2  173 ? 43.250 24.308  -9.211  1.00 41.65  ?  205 ILE C N     1 
ATOM   8077  C  CA    . ILE C  2  173 ? 44.595 24.862  -9.320  1.00 40.26  ?  205 ILE C CA    1 
ATOM   8078  C  C     . ILE C  2  173 ? 44.516 26.330  -9.793  1.00 40.45  ?  205 ILE C C     1 
ATOM   8079  O  O     . ILE C  2  173 ? 43.948 26.601  -10.855 1.00 41.81  ?  205 ILE C O     1 
ATOM   8080  C  CB    . ILE C  2  173 ? 45.440 24.088  -10.350 1.00 39.32  ?  205 ILE C CB    1 
ATOM   8081  C  CG1   . ILE C  2  173 ? 45.427 22.576  -10.082 1.00 38.45  ?  205 ILE C CG1   1 
ATOM   8082  C  CG2   . ILE C  2  173 ? 46.857 24.630  -10.357 1.00 38.80  ?  205 ILE C CG2   1 
ATOM   8083  C  CD1   . ILE C  2  173 ? 45.914 22.187  -8.703  1.00 37.76  ?  205 ILE C CD1   1 
ATOM   8084  N  N     . ILE C  2  174 ? 45.064 27.261  -9.000  1.00 39.24  ?  206 ILE C N     1 
ATOM   8085  C  CA    . ILE C  2  174 ? 45.203 28.687  -9.381  1.00 39.14  ?  206 ILE C CA    1 
ATOM   8086  C  C     . ILE C  2  174 ? 46.659 28.966  -9.792  1.00 37.12  ?  206 ILE C C     1 
ATOM   8087  O  O     . ILE C  2  174 ? 47.504 29.143  -8.923  1.00 37.67  ?  206 ILE C O     1 
ATOM   8088  C  CB    . ILE C  2  174 ? 44.814 29.668  -8.218  1.00 40.00  ?  206 ILE C CB    1 
ATOM   8089  C  CG1   . ILE C  2  174 ? 43.357 29.465  -7.796  1.00 40.46  ?  206 ILE C CG1   1 
ATOM   8090  C  CG2   . ILE C  2  174 ? 45.049 31.146  -8.601  1.00 39.62  ?  206 ILE C CG2   1 
ATOM   8091  C  CD1   . ILE C  2  174 ? 42.903 30.391  -6.688  1.00 40.06  ?  206 ILE C CD1   1 
ATOM   8092  N  N     . SER C  2  175 ? 46.949 29.006  -11.094 1.00 34.58  ?  207 SER C N     1 
ATOM   8093  C  CA    . SER C  2  175 ? 48.284 29.342  -11.581 1.00 34.53  ?  207 SER C CA    1 
ATOM   8094  C  C     . SER C  2  175 ? 48.457 30.875  -11.677 1.00 37.17  ?  207 SER C C     1 
ATOM   8095  O  O     . SER C  2  175 ? 47.748 31.558  -12.416 1.00 39.21  ?  207 SER C O     1 
ATOM   8096  C  CB    . SER C  2  175 ? 48.559 28.643  -12.922 1.00 35.31  ?  207 SER C CB    1 
ATOM   8097  O  OG    . SER C  2  175 ? 49.757 29.095  -13.557 1.00 35.46  ?  207 SER C OG    1 
ATOM   8098  N  N     . LEU C  2  176 ? 49.397 31.407  -10.896 1.00 39.87  ?  208 LEU C N     1 
ATOM   8099  C  CA    . LEU C  2  176 ? 49.709 32.839  -10.874 1.00 40.45  ?  208 LEU C CA    1 
ATOM   8100  C  C     . LEU C  2  176 ? 50.960 33.182  -11.708 1.00 43.49  ?  208 LEU C C     1 
ATOM   8101  O  O     . LEU C  2  176 ? 51.961 32.406  -11.793 1.00 44.77  ?  208 LEU C O     1 
ATOM   8102  C  CB    . LEU C  2  176 ? 49.893 33.342  -9.429  1.00 38.72  ?  208 LEU C CB    1 
ATOM   8103  C  CG    . LEU C  2  176 ? 48.628 33.421  -8.578  1.00 40.46  ?  208 LEU C CG    1 
ATOM   8104  C  CD1   . LEU C  2  176 ? 48.977 33.586  -7.108  1.00 39.65  ?  208 LEU C CD1   1 
ATOM   8105  C  CD2   . LEU C  2  176 ? 47.722 34.553  -9.052  1.00 41.05  ?  208 LEU C CD2   1 
ATOM   8106  N  N     . ASN C  2  177 ? 50.888 34.358  -12.326 1.00 41.20  ?  209 ASN C N     1 
ATOM   8107  C  CA    . ASN C  2  177 ? 52.025 34.940  -12.975 1.00 39.01  ?  209 ASN C CA    1 
ATOM   8108  C  C     . ASN C  2  177 ? 52.555 35.973  -12.017 1.00 36.46  ?  209 ASN C C     1 
ATOM   8109  O  O     . ASN C  2  177 ? 52.140 37.125  -12.013 1.00 34.86  ?  209 ASN C O     1 
ATOM   8110  C  CB    . ASN C  2  177 ? 51.608 35.537  -14.299 1.00 40.58  ?  209 ASN C CB    1 
ATOM   8111  C  CG    . ASN C  2  177 ? 52.777 35.796  -15.195 1.00 42.09  ?  209 ASN C CG    1 
ATOM   8112  O  OD1   . ASN C  2  177 ? 53.736 35.023  -15.205 1.00 43.40  ?  209 ASN C OD1   1 
ATOM   8113  N  ND2   . ASN C  2  177 ? 52.711 36.884  -15.961 1.00 42.70  ?  209 ASN C ND2   1 
ATOM   8114  N  N     . THR C  2  178 ? 53.435 35.516  -11.140 1.00 36.17  ?  210 THR C N     1 
ATOM   8115  C  CA    . THR C  2  178 ? 53.988 36.368  -10.099 1.00 36.69  ?  210 THR C CA    1 
ATOM   8116  C  C     . THR C  2  178 ? 55.228 37.095  -10.632 1.00 37.80  ?  210 THR C C     1 
ATOM   8117  O  O     . THR C  2  178 ? 55.740 38.002  -9.962  1.00 37.96  ?  210 THR C O     1 
ATOM   8118  C  CB    . THR C  2  178 ? 54.305 35.580  -8.795  1.00 37.02  ?  210 THR C CB    1 
ATOM   8119  O  OG1   . THR C  2  178 ? 54.868 34.300  -9.111  1.00 38.59  ?  210 THR C OG1   1 
ATOM   8120  C  CG2   . THR C  2  178 ? 53.038 35.342  -7.957  1.00 37.22  ?  210 THR C CG2   1 
ATOM   8121  N  N     . ASN C  2  179 ? 55.682 36.726  -11.848 1.00 36.73  ?  211 ASN C N     1 
ATOM   8122  C  CA    . ASN C  2  179 ? 56.792 37.426  -12.533 1.00 34.19  ?  211 ASN C CA    1 
ATOM   8123  C  C     . ASN C  2  179 ? 56.387 38.834  -12.884 1.00 34.91  ?  211 ASN C C     1 
ATOM   8124  O  O     . ASN C  2  179 ? 57.241 39.670  -13.205 1.00 32.84  ?  211 ASN C O     1 
ATOM   8125  C  CB    . ASN C  2  179 ? 57.213 36.734  -13.821 1.00 32.35  ?  211 ASN C CB    1 
ATOM   8126  C  CG    . ASN C  2  179 ? 57.389 35.253  -13.660 1.00 31.15  ?  211 ASN C CG    1 
ATOM   8127  O  OD1   . ASN C  2  179 ? 56.663 34.477  -14.263 1.00 29.56  ?  211 ASN C OD1   1 
ATOM   8128  N  ND2   . ASN C  2  179 ? 58.349 34.848  -12.844 1.00 31.03  ?  211 ASN C ND2   1 
ATOM   8129  N  N     . LEU C  2  180 ? 55.068 39.056  -12.861 1.00 36.73  ?  212 LEU C N     1 
ATOM   8130  C  CA    . LEU C  2  180 ? 54.477 40.396  -12.855 1.00 39.50  ?  212 LEU C CA    1 
ATOM   8131  C  C     . LEU C  2  180 ? 54.962 41.198  -11.647 1.00 39.49  ?  212 LEU C C     1 
ATOM   8132  O  O     . LEU C  2  180 ? 54.928 42.440  -11.666 1.00 42.35  ?  212 LEU C O     1 
ATOM   8133  C  CB    . LEU C  2  180 ? 52.932 40.334  -12.858 1.00 40.15  ?  212 LEU C CB    1 
ATOM   8134  C  CG    . LEU C  2  180 ? 52.253 39.621  -14.053 1.00 42.90  ?  212 LEU C CG    1 
ATOM   8135  C  CD1   . LEU C  2  180 ? 50.737 39.710  -13.956 1.00 43.48  ?  212 LEU C CD1   1 
ATOM   8136  C  CD2   . LEU C  2  180 ? 52.699 40.128  -15.422 1.00 43.03  ?  212 LEU C CD2   1 
ATOM   8137  N  N     . TYR C  2  181 ? 55.427 40.492  -10.615 1.00 35.05  ?  213 TYR C N     1 
ATOM   8138  C  CA    . TYR C  2  181 ? 55.722 41.094  -9.355  1.00 32.37  ?  213 TYR C CA    1 
ATOM   8139  C  C     . TYR C  2  181 ? 57.201 41.096  -9.045  1.00 28.62  ?  213 TYR C C     1 
ATOM   8140  O  O     . TYR C  2  181 ? 57.631 41.667  -8.057  1.00 27.00  ?  213 TYR C O     1 
ATOM   8141  C  CB    . TYR C  2  181 ? 54.922 40.352  -8.293  1.00 36.52  ?  213 TYR C CB    1 
ATOM   8142  C  CG    . TYR C  2  181 ? 53.417 40.327  -8.575  1.00 41.62  ?  213 TYR C CG    1 
ATOM   8143  C  CD1   . TYR C  2  181 ? 52.738 41.493  -8.948  1.00 44.64  ?  213 TYR C CD1   1 
ATOM   8144  C  CD2   . TYR C  2  181 ? 52.665 39.159  -8.449  1.00 43.23  ?  213 TYR C CD2   1 
ATOM   8145  C  CE1   . TYR C  2  181 ? 51.378 41.493  -9.197  1.00 44.80  ?  213 TYR C CE1   1 
ATOM   8146  C  CE2   . TYR C  2  181 ? 51.294 39.161  -8.701  1.00 44.19  ?  213 TYR C CE2   1 
ATOM   8147  C  CZ    . TYR C  2  181 ? 50.667 40.343  -9.075  1.00 45.04  ?  213 TYR C CZ    1 
ATOM   8148  O  OH    . TYR C  2  181 ? 49.331 40.439  -9.347  1.00 47.06  ?  213 TYR C OH    1 
ATOM   8149  N  N     . TYR C  2  182 ? 57.990 40.508  -9.922  1.00 26.56  ?  214 TYR C N     1 
ATOM   8150  C  CA    . TYR C  2  182 ? 59.412 40.359  -9.679  1.00 27.00  ?  214 TYR C CA    1 
ATOM   8151  C  C     . TYR C  2  182 ? 60.132 41.662  -9.911  1.00 28.02  ?  214 TYR C C     1 
ATOM   8152  O  O     . TYR C  2  182 ? 59.810 42.383  -10.837 1.00 25.53  ?  214 TYR C O     1 
ATOM   8153  C  CB    . TYR C  2  182 ? 59.945 39.333  -10.656 1.00 27.79  ?  214 TYR C CB    1 
ATOM   8154  C  CG    . TYR C  2  182 ? 61.365 38.841  -10.475 1.00 26.83  ?  214 TYR C CG    1 
ATOM   8155  C  CD1   . TYR C  2  182 ? 61.927 38.680  -9.212  1.00 26.12  ?  214 TYR C CD1   1 
ATOM   8156  C  CD2   . TYR C  2  182 ? 62.112 38.452  -11.594 1.00 26.08  ?  214 TYR C CD2   1 
ATOM   8157  C  CE1   . TYR C  2  182 ? 63.208 38.190  -9.074  1.00 26.36  ?  214 TYR C CE1   1 
ATOM   8158  C  CE2   . TYR C  2  182 ? 63.393 37.970  -11.464 1.00 25.92  ?  214 TYR C CE2   1 
ATOM   8159  C  CZ    . TYR C  2  182 ? 63.937 37.838  -10.206 1.00 26.19  ?  214 TYR C CZ    1 
ATOM   8160  O  OH    . TYR C  2  182 ? 65.215 37.342  -10.084 1.00 26.45  ?  214 TYR C OH    1 
ATOM   8161  N  N     . GLY C  2  183 ? 61.123 41.943  -9.070  1.00 32.09  ?  215 GLY C N     1 
ATOM   8162  C  CA    . GLY C  2  183 ? 61.868 43.208  -9.093  1.00 34.76  ?  215 GLY C CA    1 
ATOM   8163  C  C     . GLY C  2  183 ? 62.262 43.685  -10.483 1.00 38.75  ?  215 GLY C C     1 
ATOM   8164  O  O     . GLY C  2  183 ? 61.786 44.743  -10.913 1.00 40.19  ?  215 GLY C O     1 
ATOM   8165  N  N     . PRO C  2  184 ? 63.103 42.898  -11.215 1.00 41.49  ?  216 PRO C N     1 
ATOM   8166  C  CA    . PRO C  2  184 ? 63.620 43.279  -12.559 1.00 40.71  ?  216 PRO C CA    1 
ATOM   8167  C  C     . PRO C  2  184 ? 62.616 43.464  -13.700 1.00 42.34  ?  216 PRO C C     1 
ATOM   8168  O  O     . PRO C  2  184 ? 63.064 43.709  -14.822 1.00 45.07  ?  216 PRO C O     1 
ATOM   8169  C  CB    . PRO C  2  184 ? 64.553 42.123  -12.942 1.00 40.12  ?  216 PRO C CB    1 
ATOM   8170  C  CG    . PRO C  2  184 ? 64.850 41.409  -11.674 1.00 41.47  ?  216 PRO C CG    1 
ATOM   8171  C  CD    . PRO C  2  184 ? 63.675 41.617  -10.755 1.00 41.74  ?  216 PRO C CD    1 
ATOM   8172  N  N     . ASN C  2  185 ? 61.306 43.331  -13.453 1.00 43.45  ?  217 ASN C N     1 
ATOM   8173  C  CA    . ASN C  2  185 ? 60.295 43.482  -14.516 1.00 44.73  ?  217 ASN C CA    1 
ATOM   8174  C  C     . ASN C  2  185 ? 59.921 44.931  -14.774 1.00 48.65  ?  217 ASN C C     1 
ATOM   8175  O  O     . ASN C  2  185 ? 59.041 45.472  -14.104 1.00 49.66  ?  217 ASN C O     1 
ATOM   8176  C  CB    . ASN C  2  185 ? 59.025 42.684  -14.211 1.00 44.54  ?  217 ASN C CB    1 
ATOM   8177  C  CG    . ASN C  2  185 ? 58.107 42.567  -15.418 1.00 44.90  ?  217 ASN C CG    1 
ATOM   8178  O  OD1   . ASN C  2  185 ? 58.357 43.170  -16.465 1.00 46.74  ?  217 ASN C OD1   1 
ATOM   8179  N  ND2   . ASN C  2  185 ? 57.052 41.770  -15.286 1.00 43.90  ?  217 ASN C ND2   1 
ATOM   8180  N  N     . ILE C  2  186 ? 60.557 45.531  -15.781 1.00 52.77  ?  218 ILE C N     1 
ATOM   8181  C  CA    . ILE C  2  186 ? 60.384 46.951  -16.077 1.00 56.15  ?  218 ILE C CA    1 
ATOM   8182  C  C     . ILE C  2  186 ? 58.939 47.291  -16.496 1.00 57.71  ?  218 ILE C C     1 
ATOM   8183  O  O     . ILE C  2  186 ? 58.498 48.427  -16.262 1.00 58.44  ?  218 ILE C O     1 
ATOM   8184  C  CB    . ILE C  2  186 ? 61.382 47.445  -17.158 1.00 58.33  ?  218 ILE C CB    1 
ATOM   8185  C  CG1   . ILE C  2  186 ? 62.843 47.231  -16.715 1.00 61.67  ?  218 ILE C CG1   1 
ATOM   8186  C  CG2   . ILE C  2  186 ? 61.146 48.920  -17.473 1.00 58.66  ?  218 ILE C CG2   1 
ATOM   8187  C  CD1   . ILE C  2  186 ? 63.367 48.243  -15.700 1.00 64.99  ?  218 ILE C CD1   1 
ATOM   8188  N  N     . MET C  2  187 ? 58.221 46.309  -17.075 1.00 55.01  ?  219 MET C N     1 
ATOM   8189  C  CA    . MET C  2  187 ? 56.850 46.484  -17.631 1.00 52.83  ?  219 MET C CA    1 
ATOM   8190  C  C     . MET C  2  187 ? 55.773 46.849  -16.599 1.00 50.70  ?  219 MET C C     1 
ATOM   8191  O  O     . MET C  2  187 ? 54.771 47.497  -16.929 1.00 48.91  ?  219 MET C O     1 
ATOM   8192  C  CB    . MET C  2  187 ? 56.380 45.192  -18.318 1.00 55.09  ?  219 MET C CB    1 
ATOM   8193  C  CG    . MET C  2  187 ? 57.226 44.674  -19.471 1.00 56.03  ?  219 MET C CG    1 
ATOM   8194  S  SD    . MET C  2  187 ? 57.131 45.725  -20.921 1.00 58.04  ?  219 MET C SD    1 
ATOM   8195  C  CE    . MET C  2  187 ? 58.617 46.722  -20.735 1.00 62.34  ?  219 MET C CE    1 
ATOM   8196  N  N     . THR C  2  188 ? 55.983 46.418  -15.360 1.00 50.36  ?  220 THR C N     1 
ATOM   8197  C  CA    . THR C  2  188 ? 55.000 46.568  -14.294 1.00 51.99  ?  220 THR C CA    1 
ATOM   8198  C  C     . THR C  2  188 ? 55.284 47.680  -13.262 1.00 52.07  ?  220 THR C C     1 
ATOM   8199  O  O     . THR C  2  188 ? 54.555 47.799  -12.278 1.00 51.36  ?  220 THR C O     1 
ATOM   8200  C  CB    . THR C  2  188 ? 54.876 45.232  -13.520 1.00 55.62  ?  220 THR C CB    1 
ATOM   8201  O  OG1   . THR C  2  188 ? 56.117 44.929  -12.852 1.00 51.62  ?  220 THR C OG1   1 
ATOM   8202  C  CG2   . THR C  2  188 ? 54.477 44.083  -14.481 1.00 57.07  ?  220 THR C CG2   1 
ATOM   8203  N  N     . LEU C  2  189 ? 56.323 48.485  -13.462 1.00 52.18  ?  221 LEU C N     1 
ATOM   8204  C  CA    . LEU C  2  189 ? 56.705 49.489  -12.463 1.00 51.69  ?  221 LEU C CA    1 
ATOM   8205  C  C     . LEU C  2  189 ? 55.579 50.485  -12.232 1.00 54.51  ?  221 LEU C C     1 
ATOM   8206  O  O     . LEU C  2  189 ? 54.880 50.876  -13.174 1.00 56.75  ?  221 LEU C O     1 
ATOM   8207  C  CB    . LEU C  2  189 ? 57.962 50.235  -12.895 1.00 52.71  ?  221 LEU C CB    1 
ATOM   8208  C  CG    . LEU C  2  189 ? 59.305 49.632  -12.468 1.00 52.81  ?  221 LEU C CG    1 
ATOM   8209  C  CD1   . LEU C  2  189 ? 60.377 49.831  -13.535 1.00 54.15  ?  221 LEU C CD1   1 
ATOM   8210  C  CD2   . LEU C  2  189 ? 59.737 50.249  -11.152 1.00 51.05  ?  221 LEU C CD2   1 
ATOM   8211  N  N     . ASN C  2  190 ? 55.406 50.869  -10.971 1.00 55.42  ?  222 ASN C N     1 
ATOM   8212  C  CA    . ASN C  2  190 ? 54.364 51.818  -10.536 1.00 57.18  ?  222 ASN C CA    1 
ATOM   8213  C  C     . ASN C  2  190 ? 52.893 51.431  -10.842 1.00 54.27  ?  222 ASN C C     1 
ATOM   8214  O  O     . ASN C  2  190 ? 52.022 52.292  -10.782 1.00 53.87  ?  222 ASN C O     1 
ATOM   8215  C  CB    . ASN C  2  190 ? 54.685 53.254  -11.043 1.00 57.96  ?  222 ASN C CB    1 
ATOM   8216  C  CG    . ASN C  2  190 ? 54.251 54.362  -10.051 1.00 60.42  ?  222 ASN C CG    1 
ATOM   8217  O  OD1   . ASN C  2  190 ? 54.332 54.205  -8.816  1.00 56.39  ?  222 ASN C OD1   1 
ATOM   8218  N  ND2   . ASN C  2  190 ? 53.798 55.498  -10.596 1.00 59.53  ?  222 ASN C ND2   1 
ATOM   8219  N  N     . LYS C  2  191 ? 52.611 50.150  -11.118 1.00 56.50  ?  223 LYS C N     1 
ATOM   8220  C  CA    . LYS C  2  191 ? 51.225 49.673  -11.373 1.00 58.34  ?  223 LYS C CA    1 
ATOM   8221  C  C     . LYS C  2  191 ? 50.565 49.089  -10.127 1.00 57.68  ?  223 LYS C C     1 
ATOM   8222  O  O     . LYS C  2  191 ? 51.000 48.070  -9.599  1.00 51.50  ?  223 LYS C O     1 
ATOM   8223  C  CB    . LYS C  2  191 ? 51.163 48.613  -12.485 1.00 59.34  ?  223 LYS C CB    1 
ATOM   8224  C  CG    . LYS C  2  191 ? 51.628 49.094  -13.851 1.00 61.81  ?  223 LYS C CG    1 
ATOM   8225  C  CD    . LYS C  2  191 ? 50.959 48.362  -15.017 1.00 63.38  ?  223 LYS C CD    1 
ATOM   8226  C  CE    . LYS C  2  191 ? 51.826 48.460  -16.271 1.00 65.04  ?  223 LYS C CE    1 
ATOM   8227  N  NZ    . LYS C  2  191 ? 51.068 48.641  -17.532 1.00 65.15  1  223 LYS C NZ    1 
ATOM   8228  N  N     . THR C  2  192 ? 49.509 49.760  -9.676  1.00 64.48  ?  224 THR C N     1 
ATOM   8229  C  CA    . THR C  2  192 ? 48.639 49.286  -8.589  1.00 66.12  ?  224 THR C CA    1 
ATOM   8230  C  C     . THR C  2  192 ? 48.321 47.793  -8.620  1.00 65.78  ?  224 THR C C     1 
ATOM   8231  O  O     . THR C  2  192 ? 48.342 47.136  -7.573  1.00 63.06  ?  224 THR C O     1 
ATOM   8232  C  CB    . THR C  2  192 ? 47.269 50.017  -8.586  1.00 68.42  ?  224 THR C CB    1 
ATOM   8233  O  OG1   . THR C  2  192 ? 46.387 49.346  -7.681  1.00 69.91  ?  224 THR C OG1   1 
ATOM   8234  C  CG2   . THR C  2  192 ? 46.593 50.046  -9.990  1.00 67.17  ?  224 THR C CG2   1 
ATOM   8235  N  N     . ASP C  2  193 ? 47.996 47.283  -9.814  1.00 64.73  ?  225 ASP C N     1 
ATOM   8236  C  CA    . ASP C  2  193 ? 47.602 45.876  -10.003 1.00 61.37  ?  225 ASP C CA    1 
ATOM   8237  C  C     . ASP C  2  193 ? 47.873 45.420  -11.440 1.00 56.25  ?  225 ASP C C     1 
ATOM   8238  O  O     . ASP C  2  193 ? 47.024 45.618  -12.307 1.00 53.80  ?  225 ASP C O     1 
ATOM   8239  C  CB    . ASP C  2  193 ? 46.113 45.669  -9.665  1.00 60.25  ?  225 ASP C CB    1 
ATOM   8240  C  CG    . ASP C  2  193 ? 45.655 44.215  -9.839  1.00 58.89  ?  225 ASP C CG    1 
ATOM   8241  O  OD1   . ASP C  2  193 ? 46.516 43.304  -9.925  1.00 57.09  ?  225 ASP C OD1   1 
ATOM   8242  O  OD2   . ASP C  2  193 ? 44.426 43.984  -9.888  1.00 58.89  -1 225 ASP C OD2   1 
ATOM   8243  N  N     . PRO C  2  194 ? 49.046 44.793  -11.689 1.00 52.07  ?  226 PRO C N     1 
ATOM   8244  C  CA    . PRO C  2  194 ? 49.374 44.329  -13.035 1.00 50.68  ?  226 PRO C CA    1 
ATOM   8245  C  C     . PRO C  2  194 ? 48.522 43.141  -13.491 1.00 47.81  ?  226 PRO C C     1 
ATOM   8246  O  O     . PRO C  2  194 ? 48.309 42.182  -12.737 1.00 43.91  ?  226 PRO C O     1 
ATOM   8247  C  CB    . PRO C  2  194 ? 50.865 43.949  -12.962 1.00 50.37  ?  226 PRO C CB    1 
ATOM   8248  C  CG    . PRO C  2  194 ? 51.290 44.130  -11.568 1.00 50.57  ?  226 PRO C CG    1 
ATOM   8249  C  CD    . PRO C  2  194 ? 50.107 44.488  -10.721 1.00 51.87  ?  226 PRO C CD    1 
ATOM   8250  N  N     . ALA C  2  195 ? 48.060 43.252  -14.735 1.00 46.79  ?  227 ALA C N     1 
ATOM   8251  C  CA    . ALA C  2  195 ? 47.184 42.290  -15.397 1.00 45.84  ?  227 ALA C CA    1 
ATOM   8252  C  C     . ALA C  2  195 ? 45.846 42.121  -14.681 1.00 43.46  ?  227 ALA C C     1 
ATOM   8253  O  O     . ALA C  2  195 ? 45.103 41.187  -14.972 1.00 38.24  ?  227 ALA C O     1 
ATOM   8254  C  CB    . ALA C  2  195 ? 47.895 40.956  -15.592 1.00 46.54  ?  227 ALA C CB    1 
ATOM   8255  N  N     . ASN C  2  196 ? 45.533 43.062  -13.790 1.00 44.47  ?  228 ASN C N     1 
ATOM   8256  C  CA    . ASN C  2  196 ? 44.364 42.980  -12.945 1.00 50.11  ?  228 ASN C CA    1 
ATOM   8257  C  C     . ASN C  2  196 ? 44.307 41.646  -12.190 1.00 52.37  ?  228 ASN C C     1 
ATOM   8258  O  O     . ASN C  2  196 ? 43.231 41.069  -11.992 1.00 55.08  ?  228 ASN C O     1 
ATOM   8259  C  CB    . ASN C  2  196 ? 43.100 43.198  -13.788 1.00 55.86  ?  228 ASN C CB    1 
ATOM   8260  C  CG    . ASN C  2  196 ? 42.767 44.666  -13.980 1.00 61.80  ?  228 ASN C CG    1 
ATOM   8261  O  OD1   . ASN C  2  196 ? 43.426 45.369  -14.742 1.00 66.93  ?  228 ASN C OD1   1 
ATOM   8262  N  ND2   . ASN C  2  196 ? 41.726 45.135  -13.295 1.00 67.69  ?  228 ASN C ND2   1 
ATOM   8263  N  N     . GLN C  2  197 ? 45.470 41.159  -11.757 1.00 54.47  ?  229 GLN C N     1 
ATOM   8264  C  CA    . GLN C  2  197 ? 45.590 39.793  -11.208 1.00 52.57  ?  229 GLN C CA    1 
ATOM   8265  C  C     . GLN C  2  197 ? 45.105 39.659  -9.740  1.00 52.38  ?  229 GLN C C     1 
ATOM   8266  O  O     . GLN C  2  197 ? 44.488 38.646  -9.397  1.00 49.15  ?  229 GLN C O     1 
ATOM   8267  C  CB    . GLN C  2  197 ? 47.020 39.264  -11.389 1.00 49.92  ?  229 GLN C CB    1 
ATOM   8268  C  CG    . GLN C  2  197 ? 47.315 37.989  -10.628 1.00 49.32  ?  229 GLN C CG    1 
ATOM   8269  C  CD    . GLN C  2  197 ? 48.533 37.275  -11.145 1.00 50.16  ?  229 GLN C CD    1 
ATOM   8270  O  OE1   . GLN C  2  197 ? 49.577 37.228  -10.495 1.00 51.53  ?  229 GLN C OE1   1 
ATOM   8271  N  NE2   . GLN C  2  197 ? 48.406 36.706  -12.318 1.00 50.74  ?  229 GLN C NE2   1 
ATOM   8272  N  N     . PHE C  2  198 ? 45.365 40.664  -8.895  1.00 52.46  ?  230 PHE C N     1 
ATOM   8273  C  CA    . PHE C  2  198 ? 44.794 40.689  -7.545  1.00 52.85  ?  230 PHE C CA    1 
ATOM   8274  C  C     . PHE C  2  198 ? 43.278 40.770  -7.625  1.00 56.65  ?  230 PHE C C     1 
ATOM   8275  O  O     . PHE C  2  198 ? 42.596 40.128  -6.833  1.00 66.34  ?  230 PHE C O     1 
ATOM   8276  C  CB    . PHE C  2  198 ? 45.269 41.873  -6.703  1.00 53.29  ?  230 PHE C CB    1 
ATOM   8277  C  CG    . PHE C  2  198 ? 46.748 42.034  -6.655  1.00 53.33  ?  230 PHE C CG    1 
ATOM   8278  C  CD1   . PHE C  2  198 ? 47.553 40.988  -6.300  1.00 54.78  ?  230 PHE C CD1   1 
ATOM   8279  C  CD2   . PHE C  2  198 ? 47.332 43.248  -6.963  1.00 56.32  ?  230 PHE C CD2   1 
ATOM   8280  C  CE1   . PHE C  2  198 ? 48.927 41.135  -6.268  1.00 55.37  ?  230 PHE C CE1   1 
ATOM   8281  C  CE2   . PHE C  2  198 ? 48.702 43.408  -6.930  1.00 55.50  ?  230 PHE C CE2   1 
ATOM   8282  C  CZ    . PHE C  2  198 ? 49.500 42.347  -6.584  1.00 55.30  ?  230 PHE C CZ    1 
ATOM   8283  N  N     . GLU C  2  199 ? 42.744 41.566  -8.551  1.00 53.59  ?  231 GLU C N     1 
ATOM   8284  C  CA    . GLU C  2  199 ? 41.295 41.658  -8.697  1.00 52.30  ?  231 GLU C CA    1 
ATOM   8285  C  C     . GLU C  2  199 ? 40.726 40.284  -9.083  1.00 46.97  ?  231 GLU C C     1 
ATOM   8286  O  O     . GLU C  2  199 ? 39.760 39.832  -8.486  1.00 43.08  ?  231 GLU C O     1 
ATOM   8287  C  CB    . GLU C  2  199 ? 40.911 42.745  -9.708  1.00 58.89  ?  231 GLU C CB    1 
ATOM   8288  C  CG    . GLU C  2  199 ? 39.488 43.282  -9.541  1.00 64.33  ?  231 GLU C CG    1 
ATOM   8289  C  CD    . GLU C  2  199 ? 38.956 44.011  -10.781 1.00 66.91  ?  231 GLU C CD    1 
ATOM   8290  O  OE1   . GLU C  2  199 ? 38.306 45.063  -10.613 1.00 76.82  ?  231 GLU C OE1   1 
ATOM   8291  O  OE2   . GLU C  2  199 ? 39.171 43.549  -11.924 1.00 61.65  -1 231 GLU C OE2   1 
ATOM   8292  N  N     . TRP C  2  200 ? 41.360 39.618  -10.052 1.00 47.74  ?  232 TRP C N     1 
ATOM   8293  C  CA    . TRP C  2  200 ? 40.996 38.245  -10.493 1.00 47.91  ?  232 TRP C CA    1 
ATOM   8294  C  C     . TRP C  2  200 ? 41.186 37.149  -9.415  1.00 49.30  ?  232 TRP C C     1 
ATOM   8295  O  O     . TRP C  2  200 ? 40.418 36.188  -9.376  1.00 48.21  ?  232 TRP C O     1 
ATOM   8296  C  CB    . TRP C  2  200 ? 41.798 37.868  -11.760 1.00 46.29  ?  232 TRP C CB    1 
ATOM   8297  C  CG    . TRP C  2  200 ? 41.597 36.452  -12.249 1.00 46.34  ?  232 TRP C CG    1 
ATOM   8298  C  CD1   . TRP C  2  200 ? 40.614 36.014  -13.077 1.00 45.97  ?  232 TRP C CD1   1 
ATOM   8299  C  CD2   . TRP C  2  200 ? 42.413 35.296  -11.949 1.00 48.84  ?  232 TRP C CD2   1 
ATOM   8300  N  NE1   . TRP C  2  200 ? 40.751 34.663  -13.312 1.00 48.32  ?  232 TRP C NE1   1 
ATOM   8301  C  CE2   . TRP C  2  200 ? 41.846 34.197  -12.632 1.00 48.75  ?  232 TRP C CE2   1 
ATOM   8302  C  CE3   . TRP C  2  200 ? 43.565 35.088  -11.172 1.00 48.04  ?  232 TRP C CE3   1 
ATOM   8303  C  CZ2   . TRP C  2  200 ? 42.391 32.904  -12.565 1.00 47.07  ?  232 TRP C CZ2   1 
ATOM   8304  C  CZ3   . TRP C  2  200 ? 44.110 33.801  -11.115 1.00 48.38  ?  232 TRP C CZ3   1 
ATOM   8305  C  CH2   . TRP C  2  200 ? 43.520 32.731  -11.812 1.00 46.89  ?  232 TRP C CH2   1 
ATOM   8306  N  N     . LEU C  2  201 ? 42.215 37.275  -8.571  1.00 50.71  ?  233 LEU C N     1 
ATOM   8307  C  CA    . LEU C  2  201 ? 42.443 36.334  -7.449  1.00 50.79  ?  233 LEU C CA    1 
ATOM   8308  C  C     . LEU C  2  201 ? 41.325 36.479  -6.412  1.00 55.30  ?  233 LEU C C     1 
ATOM   8309  O  O     . LEU C  2  201 ? 40.633 35.505  -6.108  1.00 59.19  ?  233 LEU C O     1 
ATOM   8310  C  CB    . LEU C  2  201 ? 43.820 36.573  -6.793  1.00 46.96  ?  233 LEU C CB    1 
ATOM   8311  C  CG    . LEU C  2  201 ? 44.509 35.546  -5.881  1.00 41.74  ?  233 LEU C CG    1 
ATOM   8312  C  CD1   . LEU C  2  201 ? 44.515 34.144  -6.467  1.00 41.92  ?  233 LEU C CD1   1 
ATOM   8313  C  CD2   . LEU C  2  201 ? 45.936 36.008  -5.649  1.00 38.97  ?  233 LEU C CD2   1 
ATOM   8314  N  N     . GLU C  2  202 ? 41.145 37.697  -5.889  1.00 59.03  ?  234 GLU C N     1 
ATOM   8315  C  CA    . GLU C  2  202 ? 40.025 38.023  -4.973  1.00 59.20  ?  234 GLU C CA    1 
ATOM   8316  C  C     . GLU C  2  202 ? 38.692 37.508  -5.511  1.00 55.14  ?  234 GLU C C     1 
ATOM   8317  O  O     . GLU C  2  202 ? 37.908 36.938  -4.762  1.00 53.23  ?  234 GLU C O     1 
ATOM   8318  C  CB    . GLU C  2  202 ? 39.943 39.536  -4.708  1.00 61.16  ?  234 GLU C CB    1 
ATOM   8319  C  CG    . GLU C  2  202 ? 40.813 40.001  -3.548  1.00 65.35  ?  234 GLU C CG    1 
ATOM   8320  C  CD    . GLU C  2  202 ? 41.303 41.439  -3.673  1.00 68.98  ?  234 GLU C CD    1 
ATOM   8321  O  OE1   . GLU C  2  202 ? 41.675 41.887  -4.786  1.00 65.81  ?  234 GLU C OE1   1 
ATOM   8322  O  OE2   . GLU C  2  202 ? 41.345 42.120  -2.626  1.00 74.17  -1 234 GLU C OE2   1 
ATOM   8323  N  N     . SER C  2  203 ? 38.465 37.712  -6.813  1.00 52.16  ?  235 SER C N     1 
ATOM   8324  C  CA    . SER C  2  203 ? 37.332 37.123  -7.539  1.00 50.51  ?  235 SER C CA    1 
ATOM   8325  C  C     . SER C  2  203 ? 37.337 35.582  -7.521  1.00 52.39  ?  235 SER C C     1 
ATOM   8326  O  O     . SER C  2  203 ? 36.347 34.993  -7.076  1.00 53.66  ?  235 SER C O     1 
ATOM   8327  C  CB    . SER C  2  203 ? 37.284 37.640  -8.990  1.00 47.75  ?  235 SER C CB    1 
ATOM   8328  O  OG    . SER C  2  203 ? 36.402 36.885  -9.809  1.00 43.70  ?  235 SER C OG    1 
ATOM   8329  N  N     . THR C  2  204 ? 38.424 34.942  -7.991  1.00 52.35  ?  236 THR C N     1 
ATOM   8330  C  CA    . THR C  2  204 ? 38.459 33.466  -8.159  1.00 51.74  ?  236 THR C CA    1 
ATOM   8331  C  C     . THR C  2  204 ? 38.362 32.738  -6.800  1.00 52.13  ?  236 THR C C     1 
ATOM   8332  O  O     . THR C  2  204 ? 37.706 31.694  -6.708  1.00 55.82  ?  236 THR C O     1 
ATOM   8333  C  CB    . THR C  2  204 ? 39.709 32.928  -8.943  1.00 52.04  ?  236 THR C CB    1 
ATOM   8334  O  OG1   . THR C  2  204 ? 39.964 33.690  -10.134 1.00 50.04  ?  236 THR C OG1   1 
ATOM   8335  C  CG2   . THR C  2  204 ? 39.501 31.469  -9.354  1.00 52.50  ?  236 THR C CG2   1 
ATOM   8336  N  N     . LEU C  2  205 ? 39.002 33.286  -5.758  1.00 50.82  ?  237 LEU C N     1 
ATOM   8337  C  CA    . LEU C  2  205 ? 38.997 32.681  -4.409  1.00 48.70  ?  237 LEU C CA    1 
ATOM   8338  C  C     . LEU C  2  205 ? 37.612 32.811  -3.781  1.00 51.98  ?  237 LEU C C     1 
ATOM   8339  O  O     . LEU C  2  205 ? 37.047 31.829  -3.298  1.00 53.57  ?  237 LEU C O     1 
ATOM   8340  C  CB    . LEU C  2  205 ? 40.049 33.336  -3.492  1.00 45.23  ?  237 LEU C CB    1 
ATOM   8341  C  CG    . LEU C  2  205 ? 41.528 33.096  -3.815  1.00 41.41  ?  237 LEU C CG    1 
ATOM   8342  C  CD1   . LEU C  2  205 ? 42.375 34.108  -3.073  1.00 39.95  ?  237 LEU C CD1   1 
ATOM   8343  C  CD2   . LEU C  2  205 ? 41.947 31.677  -3.473  1.00 40.85  ?  237 LEU C CD2   1 
ATOM   8344  N  N     . ASN C  2  206 ? 37.076 34.033  -3.799  1.00 55.58  ?  238 ASN C N     1 
ATOM   8345  C  CA    . ASN C  2  206 ? 35.711 34.319  -3.330  1.00 55.30  ?  238 ASN C CA    1 
ATOM   8346  C  C     . ASN C  2  206 ? 34.681 33.394  -3.980  1.00 56.09  ?  238 ASN C C     1 
ATOM   8347  O  O     . ASN C  2  206 ? 33.763 32.911  -3.321  1.00 57.98  ?  238 ASN C O     1 
ATOM   8348  C  CB    . ASN C  2  206 ? 35.358 35.775  -3.622  1.00 53.89  ?  238 ASN C CB    1 
ATOM   8349  C  CG    . ASN C  2  206 ? 34.278 36.334  -2.719  1.00 57.33  ?  238 ASN C CG    1 
ATOM   8350  O  OD1   . ASN C  2  206 ? 33.854 37.468  -2.931  1.00 64.92  ?  238 ASN C OD1   1 
ATOM   8351  N  ND2   . ASN C  2  206 ? 33.841 35.582  -1.704  1.00 57.51  ?  238 ASN C ND2   1 
ATOM   8352  N  N     . ASN C  2  207 ? 34.853 33.154  -5.276  1.00 56.14  ?  239 ASN C N     1 
ATOM   8353  C  CA    . ASN C  2  207 ? 34.120 32.117  -5.981  1.00 57.16  ?  239 ASN C CA    1 
ATOM   8354  C  C     . ASN C  2  207 ? 34.299 30.745  -5.295  1.00 58.51  ?  239 ASN C C     1 
ATOM   8355  O  O     . ASN C  2  207 ? 33.315 30.154  -4.853  1.00 70.42  ?  239 ASN C O     1 
ATOM   8356  C  CB    . ASN C  2  207 ? 34.559 32.063  -7.454  1.00 59.54  ?  239 ASN C CB    1 
ATOM   8357  C  CG    . ASN C  2  207 ? 33.496 31.480  -8.387  1.00 63.49  ?  239 ASN C CG    1 
ATOM   8358  O  OD1   . ASN C  2  207 ? 32.667 30.648  -7.995  1.00 67.38  ?  239 ASN C OD1   1 
ATOM   8359  N  ND2   . ASN C  2  207 ? 33.530 31.911  -9.647  1.00 63.81  ?  239 ASN C ND2   1 
ATOM   8360  N  N     . SER C  2  208 ? 35.530 30.249  -5.169  1.00 54.39  ?  240 SER C N     1 
ATOM   8361  C  CA    . SER C  2  208 ? 35.761 28.905  -4.598  1.00 51.13  ?  240 SER C CA    1 
ATOM   8362  C  C     . SER C  2  208 ? 35.286 28.764  -3.136  1.00 53.04  ?  240 SER C C     1 
ATOM   8363  O  O     . SER C  2  208 ? 34.943 27.664  -2.684  1.00 51.18  ?  240 SER C O     1 
ATOM   8364  C  CB    . SER C  2  208 ? 37.241 28.520  -4.712  1.00 49.89  ?  240 SER C CB    1 
ATOM   8365  O  OG    . SER C  2  208 ? 37.654 28.394  -6.069  1.00 46.67  ?  240 SER C OG    1 
ATOM   8366  N  N     . GLN C  2  209 ? 35.248 29.881  -2.410  1.00 56.99  ?  241 GLN C N     1 
ATOM   8367  C  CA    . GLN C  2  209 ? 34.820 29.895  -1.005  1.00 61.13  ?  241 GLN C CA    1 
ATOM   8368  C  C     . GLN C  2  209 ? 33.411 29.415  -0.809  1.00 64.62  ?  241 GLN C C     1 
ATOM   8369  O  O     . GLN C  2  209 ? 33.112 28.801  0.208   1.00 67.23  ?  241 GLN C O     1 
ATOM   8370  C  CB    . GLN C  2  209 ? 34.912 31.304  -0.421  1.00 61.61  ?  241 GLN C CB    1 
ATOM   8371  C  CG    . GLN C  2  209 ? 34.594 31.366  1.065   1.00 60.51  ?  241 GLN C CG    1 
ATOM   8372  C  CD    . GLN C  2  209 ? 35.577 32.219  1.843   1.00 62.18  ?  241 GLN C CD    1 
ATOM   8373  O  OE1   . GLN C  2  209 ? 36.565 32.729  1.301   1.00 57.17  ?  241 GLN C OE1   1 
ATOM   8374  N  NE2   . GLN C  2  209 ? 35.318 32.364  3.140   1.00 66.50  ?  241 GLN C NE2   1 
ATOM   8375  N  N     . GLN C  2  210 ? 32.554 29.723  -1.778  1.00 73.33  ?  242 GLN C N     1 
ATOM   8376  C  CA    . GLN C  2  210 ? 31.128 29.404  -1.714  1.00 79.15  ?  242 GLN C CA    1 
ATOM   8377  C  C     . GLN C  2  210 ? 30.726 28.099  -2.396  1.00 81.06  ?  242 GLN C C     1 
ATOM   8378  O  O     . GLN C  2  210 ? 29.625 27.605  -2.159  1.00 91.74  ?  242 GLN C O     1 
ATOM   8379  C  CB    . GLN C  2  210 ? 30.328 30.546  -2.320  1.00 79.58  ?  242 GLN C CB    1 
ATOM   8380  C  CG    . GLN C  2  210 ? 30.387 31.806  -1.476  1.00 84.08  ?  242 GLN C CG    1 
ATOM   8381  C  CD    . GLN C  2  210 ? 30.522 33.060  -2.312  1.00 85.98  ?  242 GLN C CD    1 
ATOM   8382  O  OE1   . GLN C  2  210 ? 30.350 33.027  -3.530  1.00 83.57  ?  242 GLN C OE1   1 
ATOM   8383  N  NE2   . GLN C  2  210 ? 30.834 34.176  -1.662  1.00 87.25  ?  242 GLN C NE2   1 
ATOM   8384  N  N     . ASN C  2  211 ? 31.597 27.538  -3.233  1.00 77.28  ?  243 ASN C N     1 
ATOM   8385  C  CA    . ASN C  2  211 ? 31.269 26.306  -3.954  1.00 75.63  ?  243 ASN C CA    1 
ATOM   8386  C  C     . ASN C  2  211 ? 31.966 25.080  -3.359  1.00 79.46  ?  243 ASN C C     1 
ATOM   8387  O  O     . ASN C  2  211 ? 32.268 24.131  -4.095  1.00 82.17  ?  243 ASN C O     1 
ATOM   8388  C  CB    . ASN C  2  211 ? 31.644 26.430  -5.439  1.00 72.58  ?  243 ASN C CB    1 
ATOM   8389  C  CG    . ASN C  2  211 ? 31.297 27.783  -6.024  1.00 67.49  ?  243 ASN C CG    1 
ATOM   8390  O  OD1   . ASN C  2  211 ? 30.842 28.681  -5.317  1.00 64.99  ?  243 ASN C OD1   1 
ATOM   8391  N  ND2   . ASN C  2  211 ? 31.522 27.940  -7.320  1.00 63.58  ?  243 ASN C ND2   1 
ATOM   8392  N  N     . LYS C  2  212 ? 32.207 25.086  -2.042  1.00 80.72  ?  244 LYS C N     1 
ATOM   8393  C  CA    . LYS C  2  212 ? 32.964 24.010  -1.381  1.00 83.02  ?  244 LYS C CA    1 
ATOM   8394  C  C     . LYS C  2  212 ? 34.136 23.553  -2.271  1.00 79.00  ?  244 LYS C C     1 
ATOM   8395  O  O     . LYS C  2  212 ? 34.204 22.383  -2.666  1.00 75.65  ?  244 LYS C O     1 
ATOM   8396  C  CB    . LYS C  2  212 ? 32.073 22.787  -1.074  1.00 88.35  ?  244 LYS C CB    1 
ATOM   8397  C  CG    . LYS C  2  212 ? 30.899 22.960  -0.108  1.00 92.21  ?  244 LYS C CG    1 
ATOM   8398  C  CD    . LYS C  2  212 ? 30.543 21.598  0.518   1.00 96.59  ?  244 LYS C CD    1 
ATOM   8399  C  CE    . LYS C  2  212 ? 29.104 21.465  1.031   1.00 95.10  ?  244 LYS C CE    1 
ATOM   8400  N  NZ    . LYS C  2  212 ? 28.205 20.654  0.153   1.00 89.86  1  244 LYS C NZ    1 
ATOM   8401  N  N     . GLU C  2  213 ? 35.032 24.476  -2.620  1.00 73.27  ?  245 GLU C N     1 
ATOM   8402  C  CA    . GLU C  2  213 ? 36.188 24.135  -3.463  1.00 69.78  ?  245 GLU C CA    1 
ATOM   8403  C  C     . GLU C  2  213 ? 37.518 24.378  -2.743  1.00 66.23  ?  245 GLU C C     1 
ATOM   8404  O  O     . GLU C  2  213 ? 37.682 25.404  -2.074  1.00 63.60  ?  245 GLU C O     1 
ATOM   8405  C  CB    . GLU C  2  213 ? 36.151 24.909  -4.787  1.00 69.80  ?  245 GLU C CB    1 
ATOM   8406  C  CG    . GLU C  2  213 ? 35.436 24.163  -5.905  1.00 72.79  ?  245 GLU C CG    1 
ATOM   8407  C  CD    . GLU C  2  213 ? 35.857 24.618  -7.291  1.00 73.86  ?  245 GLU C CD    1 
ATOM   8408  O  OE1   . GLU C  2  213 ? 36.043 25.838  -7.489  1.00 67.46  ?  245 GLU C OE1   1 
ATOM   8409  O  OE2   . GLU C  2  213 ? 35.999 23.747  -8.181  1.00 78.47  -1 245 GLU C OE2   1 
ATOM   8410  N  N     . LYS C  2  214 ? 38.453 23.425  -2.878  1.00 60.56  ?  246 LYS C N     1 
ATOM   8411  C  CA    . LYS C  2  214 ? 39.810 23.574  -2.338  1.00 57.11  ?  246 LYS C CA    1 
ATOM   8412  C  C     . LYS C  2  214 ? 40.809 24.003  -3.411  1.00 50.94  ?  246 LYS C C     1 
ATOM   8413  O  O     . LYS C  2  214 ? 40.885 23.439  -4.504  1.00 45.95  ?  246 LYS C O     1 
ATOM   8414  C  CB    . LYS C  2  214 ? 40.288 22.297  -1.652  1.00 59.90  ?  246 LYS C CB    1 
ATOM   8415  C  CG    . LYS C  2  214 ? 39.419 21.862  -0.474  1.00 63.27  ?  246 LYS C CG    1 
ATOM   8416  C  CD    . LYS C  2  214 ? 39.475 22.787  0.738   1.00 62.81  ?  246 LYS C CD    1 
ATOM   8417  C  CE    . LYS C  2  214 ? 40.810 22.697  1.442   1.00 66.01  ?  246 LYS C CE    1 
ATOM   8418  N  NZ    . LYS C  2  214 ? 40.797 23.224  2.833   1.00 69.85  1  246 LYS C NZ    1 
ATOM   8419  N  N     . VAL C  2  215 ? 41.571 25.028  -3.059  1.00 47.19  ?  247 VAL C N     1 
ATOM   8420  C  CA    . VAL C  2  215 ? 42.467 25.692  -3.969  1.00 45.08  ?  247 VAL C CA    1 
ATOM   8421  C  C     . VAL C  2  215 ? 43.905 25.309  -3.599  1.00 45.47  ?  247 VAL C C     1 
ATOM   8422  O  O     . VAL C  2  215 ? 44.259 25.248  -2.399  1.00 45.42  ?  247 VAL C O     1 
ATOM   8423  C  CB    . VAL C  2  215 ? 42.230 27.225  -3.918  1.00 42.96  ?  247 VAL C CB    1 
ATOM   8424  C  CG1   . VAL C  2  215 ? 43.454 28.029  -4.368  1.00 42.67  ?  247 VAL C CG1   1 
ATOM   8425  C  CG2   . VAL C  2  215 ? 41.020 27.568  -4.761  1.00 42.22  ?  247 VAL C CG2   1 
ATOM   8426  N  N     . TYR C  2  216 ? 44.701 25.006  -4.638  1.00 41.67  ?  248 TYR C N     1 
ATOM   8427  C  CA    . TYR C  2  216 ? 46.180 24.975  -4.567  1.00 37.81  ?  248 TYR C CA    1 
ATOM   8428  C  C     . TYR C  2  216 ? 46.817 26.102  -5.412  1.00 36.49  ?  248 TYR C C     1 
ATOM   8429  O  O     . TYR C  2  216 ? 46.685 26.122  -6.627  1.00 36.60  ?  248 TYR C O     1 
ATOM   8430  C  CB    . TYR C  2  216 ? 46.745 23.646  -5.082  1.00 34.93  ?  248 TYR C CB    1 
ATOM   8431  C  CG    . TYR C  2  216 ? 46.540 22.414  -4.223  1.00 32.65  ?  248 TYR C CG    1 
ATOM   8432  C  CD1   . TYR C  2  216 ? 46.073 22.491  -2.902  1.00 31.27  ?  248 TYR C CD1   1 
ATOM   8433  C  CD2   . TYR C  2  216 ? 46.876 21.163  -4.732  1.00 31.34  ?  248 TYR C CD2   1 
ATOM   8434  C  CE1   . TYR C  2  216 ? 45.904 21.340  -2.151  1.00 30.91  ?  248 TYR C CE1   1 
ATOM   8435  C  CE2   . TYR C  2  216 ? 46.719 20.019  -3.986  1.00 30.88  ?  248 TYR C CE2   1 
ATOM   8436  C  CZ    . TYR C  2  216 ? 46.227 20.110  -2.711  1.00 31.46  ?  248 TYR C CZ    1 
ATOM   8437  O  OH    . TYR C  2  216 ? 46.083 18.954  -1.990  1.00 34.22  ?  248 TYR C OH    1 
ATOM   8438  N  N     . ILE C  2  217 ? 47.541 27.011  -4.768  1.00 36.61  ?  249 ILE C N     1 
ATOM   8439  C  CA    . ILE C  2  217 ? 48.293 28.048  -5.474  1.00 35.17  ?  249 ILE C CA    1 
ATOM   8440  C  C     . ILE C  2  217 ? 49.578 27.459  -6.112  1.00 35.20  ?  249 ILE C C     1 
ATOM   8441  O  O     . ILE C  2  217 ? 50.401 26.833  -5.434  1.00 33.23  ?  249 ILE C O     1 
ATOM   8442  C  CB    . ILE C  2  217 ? 48.673 29.224  -4.538  1.00 34.07  ?  249 ILE C CB    1 
ATOM   8443  C  CG1   . ILE C  2  217 ? 47.472 29.768  -3.761  1.00 32.60  ?  249 ILE C CG1   1 
ATOM   8444  C  CG2   . ILE C  2  217 ? 49.281 30.344  -5.342  1.00 36.09  ?  249 ILE C CG2   1 
ATOM   8445  C  CD1   . ILE C  2  217 ? 46.260 30.090  -4.602  1.00 32.43  ?  249 ILE C CD1   1 
ATOM   8446  N  N     . ILE C  2  218 ? 49.709 27.651  -7.427  1.00 35.70  ?  250 ILE C N     1 
ATOM   8447  C  CA    . ILE C  2  218 ? 50.922 27.342  -8.218  1.00 38.24  ?  250 ILE C CA    1 
ATOM   8448  C  C     . ILE C  2  218 ? 51.452 28.683  -8.744  1.00 39.51  ?  250 ILE C C     1 
ATOM   8449  O  O     . ILE C  2  218 ? 50.690 29.463  -9.282  1.00 45.79  ?  250 ILE C O     1 
ATOM   8450  C  CB    . ILE C  2  218 ? 50.583 26.337  -9.373  1.00 39.23  ?  250 ILE C CB    1 
ATOM   8451  C  CG1   . ILE C  2  218 ? 50.876 24.922  -8.911  1.00 42.34  ?  250 ILE C CG1   1 
ATOM   8452  C  CG2   . ILE C  2  218 ? 51.355 26.563  -10.676 1.00 36.58  ?  250 ILE C CG2   1 
ATOM   8453  C  CD1   . ILE C  2  218 ? 50.127 24.503  -7.671  1.00 43.65  ?  250 ILE C CD1   1 
ATOM   8454  N  N     . ALA C  2  219 ? 52.730 28.993  -8.547  1.00 38.43  ?  251 ALA C N     1 
ATOM   8455  C  CA    . ALA C  2  219 ? 53.316 30.230  -9.094  1.00 35.13  ?  251 ALA C CA    1 
ATOM   8456  C  C     . ALA C  2  219 ? 54.798 30.056  -9.051  1.00 33.55  ?  251 ALA C C     1 
ATOM   8457  O  O     . ALA C  2  219 ? 55.304 29.211  -8.308  1.00 31.74  ?  251 ALA C O     1 
ATOM   8458  C  CB    . ALA C  2  219 ? 52.910 31.457  -8.285  1.00 35.19  ?  251 ALA C CB    1 
ATOM   8459  N  N     . HIS C  2  220 ? 55.545 30.814  -9.851  1.00 33.17  ?  252 HIS C N     1 
ATOM   8460  C  CA    . HIS C  2  220 ? 57.022 30.713  -9.888  1.00 34.19  ?  252 HIS C CA    1 
ATOM   8461  C  C     . HIS C  2  220 ? 57.758 31.544  -8.842  1.00 35.32  ?  252 HIS C C     1 
ATOM   8462  O  O     . HIS C  2  220 ? 58.417 30.987  -7.997  1.00 34.01  ?  252 HIS C O     1 
ATOM   8463  C  CB    . HIS C  2  220 ? 57.583 30.952  -11.312 1.00 33.49  ?  252 HIS C CB    1 
ATOM   8464  C  CG    . HIS C  2  220 ? 59.078 31.104  -11.407 1.00 32.21  ?  252 HIS C CG    1 
ATOM   8465  N  ND1   . HIS C  2  220 ? 59.939 30.043  -11.457 1.00 31.27  ?  252 HIS C ND1   1 
ATOM   8466  C  CD2   . HIS C  2  220 ? 59.849 32.203  -11.560 1.00 31.78  ?  252 HIS C CD2   1 
ATOM   8467  C  CE1   . HIS C  2  220 ? 61.177 30.483  -11.584 1.00 31.04  ?  252 HIS C CE1   1 
ATOM   8468  N  NE2   . HIS C  2  220 ? 61.155 31.795  -11.636 1.00 31.50  ?  252 HIS C NE2   1 
ATOM   8469  N  N     . VAL C  2  221 ? 57.658 32.865  -8.886  1.00 33.92  ?  253 VAL C N     1 
ATOM   8470  C  CA    . VAL C  2  221 ? 58.344 33.676  -7.900  1.00 34.02  ?  253 VAL C CA    1 
ATOM   8471  C  C     . VAL C  2  221 ? 57.524 33.473  -6.684  1.00 33.79  ?  253 VAL C C     1 
ATOM   8472  O  O     . VAL C  2  221 ? 56.329 33.479  -6.789  1.00 35.22  ?  253 VAL C O     1 
ATOM   8473  C  CB    . VAL C  2  221 ? 58.346 35.175  -8.241  1.00 33.95  ?  253 VAL C CB    1 
ATOM   8474  C  CG1   . VAL C  2  221 ? 58.860 35.989  -7.096  1.00 33.04  ?  253 VAL C CG1   1 
ATOM   8475  C  CG2   . VAL C  2  221 ? 59.224 35.468  -9.416  1.00 34.99  ?  253 VAL C CG2   1 
ATOM   8476  N  N     . PRO C  2  222 ? 58.205 33.274  -5.494  1.00 32.08  ?  254 PRO C N     1 
ATOM   8477  C  CA    . PRO C  2  222 ? 57.349 33.130  -4.339  1.00 31.17  ?  254 PRO C CA    1 
ATOM   8478  C  C     . PRO C  2  222 ? 57.096 34.417  -3.635  1.00 31.49  ?  254 PRO C C     1 
ATOM   8479  O  O     . PRO C  2  222 ? 57.661 35.420  -3.928  1.00 26.99  ?  254 PRO C O     1 
ATOM   8480  C  CB    . PRO C  2  222 ? 58.195 32.294  -3.389  1.00 31.54  ?  254 PRO C CB    1 
ATOM   8481  C  CG    . PRO C  2  222 ? 59.399 31.871  -4.093  1.00 32.19  ?  254 PRO C CG    1 
ATOM   8482  C  CD    . PRO C  2  222 ? 59.619 32.967  -5.020  1.00 31.86  ?  254 PRO C CD    1 
ATOM   8483  N  N     . VAL C  2  223 ? 56.196 34.347  -2.680  1.00 33.26  ?  255 VAL C N     1 
ATOM   8484  C  CA    . VAL C  2  223 ? 55.967 35.364  -1.676  1.00 32.96  ?  255 VAL C CA    1 
ATOM   8485  C  C     . VAL C  2  223 ? 56.977 35.105  -0.538  1.00 37.02  ?  255 VAL C C     1 
ATOM   8486  O  O     . VAL C  2  223 ? 57.687 34.066  -0.486  1.00 35.04  ?  255 VAL C O     1 
ATOM   8487  C  CB    . VAL C  2  223 ? 54.516 35.336  -1.141  1.00 31.24  ?  255 VAL C CB    1 
ATOM   8488  C  CG1   . VAL C  2  223 ? 53.533 35.362  -2.297  1.00 31.65  ?  255 VAL C CG1   1 
ATOM   8489  C  CG2   . VAL C  2  223 ? 54.255 34.120  -0.269  1.00 29.84  ?  255 VAL C CG2   1 
ATOM   8490  N  N     . GLY C  2  224 ? 57.065 36.075  0.363   1.00 41.73  ?  256 GLY C N     1 
ATOM   8491  C  CA    . GLY C  2  224 ? 57.963 35.977  1.510   1.00 43.11  ?  256 GLY C CA    1 
ATOM   8492  C  C     . GLY C  2  224 ? 59.389 36.389  1.209   1.00 43.93  ?  256 GLY C C     1 
ATOM   8493  O  O     . GLY C  2  224 ? 59.735 36.748  0.076   1.00 48.64  ?  256 GLY C O     1 
ATOM   8494  N  N     . TYR C  2  225 ? 60.213 36.325  2.250   1.00 41.20  ?  257 TYR C N     1 
ATOM   8495  C  CA    . TYR C  2  225 ? 61.588 36.814  2.214   1.00 38.42  ?  257 TYR C CA    1 
ATOM   8496  C  C     . TYR C  2  225 ? 62.553 35.708  1.709   1.00 39.06  ?  257 TYR C C     1 
ATOM   8497  O  O     . TYR C  2  225 ? 62.333 34.524  1.976   1.00 41.16  ?  257 TYR C O     1 
ATOM   8498  C  CB    . TYR C  2  225 ? 61.949 37.408  3.603   1.00 36.16  ?  257 TYR C CB    1 
ATOM   8499  C  CG    . TYR C  2  225 ? 61.218 38.713  3.816   1.00 33.69  ?  257 TYR C CG    1 
ATOM   8500  C  CD1   . TYR C  2  225 ? 59.877 38.737  4.189   1.00 32.80  ?  257 TYR C CD1   1 
ATOM   8501  C  CD2   . TYR C  2  225 ? 61.848 39.923  3.545   1.00 34.44  ?  257 TYR C CD2   1 
ATOM   8502  C  CE1   . TYR C  2  225 ? 59.189 39.928  4.319   1.00 32.90  ?  257 TYR C CE1   1 
ATOM   8503  C  CE2   . TYR C  2  225 ? 61.176 41.126  3.675   1.00 34.91  ?  257 TYR C CE2   1 
ATOM   8504  C  CZ    . TYR C  2  225 ? 59.845 41.121  4.057   1.00 35.22  ?  257 TYR C CZ    1 
ATOM   8505  O  OH    . TYR C  2  225 ? 59.181 42.319  4.168   1.00 38.39  ?  257 TYR C OH    1 
ATOM   8506  N  N     . LEU C  2  226 ? 63.575 36.085  0.930   1.00 37.70  ?  258 LEU C N     1 
ATOM   8507  C  CA    . LEU C  2  226 ? 64.554 35.119  0.435   1.00 35.45  ?  258 LEU C CA    1 
ATOM   8508  C  C     . LEU C  2  226 ? 65.391 34.721  1.610   1.00 36.73  ?  258 LEU C C     1 
ATOM   8509  O  O     . LEU C  2  226 ? 65.872 35.591  2.351   1.00 36.53  ?  258 LEU C O     1 
ATOM   8510  C  CB    . LEU C  2  226 ? 65.431 35.701  -0.655  1.00 34.43  ?  258 LEU C CB    1 
ATOM   8511  C  CG    . LEU C  2  226 ? 64.648 35.977  -1.935  1.00 33.89  ?  258 LEU C CG    1 
ATOM   8512  C  CD1   . LEU C  2  226 ? 65.372 37.046  -2.739  1.00 33.37  ?  258 LEU C CD1   1 
ATOM   8513  C  CD2   . LEU C  2  226 ? 64.388 34.687  -2.732  1.00 33.63  ?  258 LEU C CD2   1 
ATOM   8514  N  N     . PRO C  2  227 ? 65.541 33.407  1.814   1.00 39.75  ?  259 PRO C N     1 
ATOM   8515  C  CA    . PRO C  2  227 ? 66.048 32.972  3.108   1.00 41.52  ?  259 PRO C CA    1 
ATOM   8516  C  C     . PRO C  2  227 ? 67.560 33.199  3.301   1.00 41.84  ?  259 PRO C C     1 
ATOM   8517  O  O     . PRO C  2  227 ? 68.022 33.352  4.443   1.00 41.18  ?  259 PRO C O     1 
ATOM   8518  C  CB    . PRO C  2  227 ? 65.687 31.455  3.145   1.00 41.38  ?  259 PRO C CB    1 
ATOM   8519  C  CG    . PRO C  2  227 ? 64.927 31.158  1.890   1.00 40.60  ?  259 PRO C CG    1 
ATOM   8520  C  CD    . PRO C  2  227 ? 65.301 32.255  0.925   1.00 41.33  ?  259 PRO C CD    1 
ATOM   8521  N  N     A SER C  2  228 ? 68.336 33.189  2.214   0.50 41.10  ?  260 SER C N     1 
ATOM   8522  N  N     B SER C  2  228 ? 68.287 33.258  2.189   0.50 41.42  ?  260 SER C N     1 
ATOM   8523  C  CA    A SER C  2  228 ? 69.785 33.361  2.334   0.50 39.69  ?  260 SER C CA    1 
ATOM   8524  C  CA    B SER C  2  228 ? 69.731 33.364  2.195   0.50 40.25  ?  260 SER C CA    1 
ATOM   8525  C  C     A SER C  2  228 ? 70.218 34.828  2.222   0.50 40.81  ?  260 SER C C     1 
ATOM   8526  C  C     B SER C  2  228 ? 70.210 34.824  2.214   0.50 41.15  ?  260 SER C C     1 
ATOM   8527  O  O     A SER C  2  228 ? 71.359 35.116  1.874   0.50 41.27  ?  260 SER C O     1 
ATOM   8528  O  O     B SER C  2  228 ? 71.378 35.100  1.955   0.50 41.57  ?  260 SER C O     1 
ATOM   8529  C  CB    A SER C  2  228 ? 70.533 32.471  1.340   0.50 37.64  ?  260 SER C CB    1 
ATOM   8530  C  CB    B SER C  2  228 ? 70.241 32.623  0.972   0.50 38.69  ?  260 SER C CB    1 
ATOM   8531  O  OG    A SER C  2  228 ? 71.024 31.305  1.991   0.50 35.86  ?  260 SER C OG    1 
ATOM   8532  O  OG    B SER C  2  228 ? 69.133 32.299  0.142   0.50 37.75  ?  260 SER C OG    1 
ATOM   8533  N  N     . SER C  2  229 ? 69.319 35.755  2.544   1.00 41.25  ?  261 SER C N     1 
ATOM   8534  C  CA    . SER C  2  229 ? 69.681 37.163  2.611   1.00 42.88  ?  261 SER C CA    1 
ATOM   8535  C  C     . SER C  2  229 ? 68.626 37.983  3.363   1.00 44.72  ?  261 SER C C     1 
ATOM   8536  O  O     . SER C  2  229 ? 67.474 37.536  3.565   1.00 44.72  ?  261 SER C O     1 
ATOM   8537  C  CB    . SER C  2  229 ? 70.006 37.760  1.210   1.00 42.50  ?  261 SER C CB    1 
ATOM   8538  O  OG    . SER C  2  229 ? 68.993 37.552  0.244   1.00 40.32  ?  261 SER C OG    1 
ATOM   8539  N  N     . GLN C  2  230 ? 69.047 39.190  3.754   1.00 44.03  ?  262 GLN C N     1 
ATOM   8540  C  CA    . GLN C  2  230 ? 68.380 39.943  4.792   1.00 45.62  ?  262 GLN C CA    1 
ATOM   8541  C  C     . GLN C  2  230 ? 67.468 41.052  4.248   1.00 44.00  ?  262 GLN C C     1 
ATOM   8542  O  O     . GLN C  2  230 ? 67.880 41.877  3.450   1.00 43.37  ?  262 GLN C O     1 
ATOM   8543  C  CB    . GLN C  2  230 ? 69.417 40.448  5.826   1.00 50.06  ?  262 GLN C CB    1 
ATOM   8544  C  CG    . GLN C  2  230 ? 69.682 41.958  5.908   1.00 55.80  ?  262 GLN C CG    1 
ATOM   8545  C  CD    . GLN C  2  230 ? 70.365 42.394  7.215   1.00 55.29  ?  262 GLN C CD    1 
ATOM   8546  O  OE1   . GLN C  2  230 ? 69.936 43.362  7.854   1.00 56.47  ?  262 GLN C OE1   1 
ATOM   8547  N  NE2   . GLN C  2  230 ? 71.427 41.691  7.607   1.00 50.86  ?  262 GLN C NE2   1 
ATOM   8548  N  N     . ASN C  2  231 ? 66.216 41.024  4.703   1.00 44.86  ?  263 ASN C N     1 
ATOM   8549  C  CA    . ASN C  2  231 ? 65.179 41.995  4.357   1.00 45.69  ?  263 ASN C CA    1 
ATOM   8550  C  C     . ASN C  2  231 ? 64.950 42.087  2.840   1.00 46.14  ?  263 ASN C C     1 
ATOM   8551  O  O     . ASN C  2  231 ? 64.698 43.176  2.318   1.00 46.52  ?  263 ASN C O     1 
ATOM   8552  C  CB    . ASN C  2  231 ? 65.491 43.381  4.976   1.00 45.14  ?  263 ASN C CB    1 
ATOM   8553  C  CG    . ASN C  2  231 ? 64.241 44.262  5.152   1.00 46.00  ?  263 ASN C CG    1 
ATOM   8554  O  OD1   . ASN C  2  231 ? 63.147 43.772  5.450   1.00 43.87  ?  263 ASN C OD1   1 
ATOM   8555  N  ND2   . ASN C  2  231 ? 64.411 45.580  4.965   1.00 49.42  ?  263 ASN C ND2   1 
ATOM   8556  N  N     . ILE C  2  232 ? 65.039 40.955  2.132   1.00 44.56  ?  264 ILE C N     1 
ATOM   8557  C  CA    . ILE C  2  232 ? 64.784 40.954  0.675   1.00 42.30  ?  264 ILE C CA    1 
ATOM   8558  C  C     . ILE C  2  232 ? 63.661 40.007  0.268   1.00 37.54  ?  264 ILE C C     1 
ATOM   8559  O  O     . ILE C  2  232 ? 63.889 38.827  0.040   1.00 34.90  ?  264 ILE C O     1 
ATOM   8560  C  CB    . ILE C  2  232 ? 66.034 40.613  -0.175  1.00 43.93  ?  264 ILE C CB    1 
ATOM   8561  C  CG1   . ILE C  2  232 ? 67.186 41.585  0.115   1.00 44.53  ?  264 ILE C CG1   1 
ATOM   8562  C  CG2   . ILE C  2  232 ? 65.697 40.645  -1.670  1.00 42.65  ?  264 ILE C CG2   1 
ATOM   8563  C  CD1   . ILE C  2  232 ? 68.549 40.932  -0.054  1.00 45.14  ?  264 ILE C CD1   1 
ATOM   8564  N  N     . THR C  2  233 ? 62.459 40.570  0.175   1.00 35.13  ?  265 THR C N     1 
ATOM   8565  C  CA    . THR C  2  233 ? 61.324 39.984  -0.514  1.00 33.13  ?  265 THR C CA    1 
ATOM   8566  C  C     . THR C  2  233 ? 61.764 39.547  -1.874  1.00 33.69  ?  265 THR C C     1 
ATOM   8567  O  O     . THR C  2  233 ? 62.557 40.244  -2.508  1.00 34.34  ?  265 THR C O     1 
ATOM   8568  C  CB    . THR C  2  233 ? 60.279 41.060  -0.764  1.00 32.96  ?  265 THR C CB    1 
ATOM   8569  O  OG1   . THR C  2  233 ? 60.950 42.257  -1.235  1.00 29.34  ?  265 THR C OG1   1 
ATOM   8570  C  CG2   . THR C  2  233 ? 59.510 41.339  0.527   1.00 33.99  ?  265 THR C CG2   1 
ATOM   8571  N  N     . ALA C  2  234 ? 61.240 38.413  -2.329  1.00 33.31  ?  266 ALA C N     1 
ATOM   8572  C  CA    . ALA C  2  234 ? 61.602 37.864  -3.632  1.00 35.40  ?  266 ALA C CA    1 
ATOM   8573  C  C     . ALA C  2  234 ? 60.893 38.627  -4.755  1.00 37.91  ?  266 ALA C C     1 
ATOM   8574  O  O     . ALA C  2  234 ? 61.443 38.829  -5.862  1.00 36.26  ?  266 ALA C O     1 
ATOM   8575  C  CB    . ALA C  2  234 ? 61.251 36.386  -3.685  1.00 35.87  ?  266 ALA C CB    1 
ATOM   8576  N  N     . MET C  2  235 ? 59.646 39.005  -4.449  1.00 43.04  ?  267 MET C N     1 
ATOM   8577  C  CA    . MET C  2  235 ? 58.855 39.998  -5.211  1.00 45.33  ?  267 MET C CA    1 
ATOM   8578  C  C     . MET C  2  235 ? 59.219 41.443  -4.787  1.00 46.60  ?  267 MET C C     1 
ATOM   8579  O  O     . MET C  2  235 ? 59.980 41.669  -3.824  1.00 48.23  ?  267 MET C O     1 
ATOM   8580  C  CB    . MET C  2  235 ? 57.343 39.790  -4.961  1.00 42.34  ?  267 MET C CB    1 
ATOM   8581  C  CG    . MET C  2  235 ? 56.768 38.485  -5.490  1.00 41.17  ?  267 MET C CG    1 
ATOM   8582  S  SD    . MET C  2  235 ? 55.243 37.987  -4.673  1.00 39.22  ?  267 MET C SD    1 
ATOM   8583  C  CE    . MET C  2  235 ? 54.393 39.549  -4.588  1.00 38.75  ?  267 MET C CE    1 
ATOM   8584  N  N     . ARG C  2  236 ? 58.673 42.420  -5.506  1.00 44.75  ?  268 ARG C N     1 
ATOM   8585  C  CA    . ARG C  2  236 ? 58.654 43.770  -4.987  1.00 45.50  ?  268 ARG C CA    1 
ATOM   8586  C  C     . ARG C  2  236 ? 57.866 43.657  -3.652  1.00 50.96  ?  268 ARG C C     1 
ATOM   8587  O  O     . ARG C  2  236 ? 56.777 43.054  -3.595  1.00 49.85  ?  268 ARG C O     1 
ATOM   8588  C  CB    . ARG C  2  236 ? 58.110 44.753  -6.023  1.00 42.62  ?  268 ARG C CB    1 
ATOM   8589  C  CG    . ARG C  2  236 ? 59.164 45.391  -6.896  1.00 39.66  ?  268 ARG C CG    1 
ATOM   8590  C  CD    . ARG C  2  236 ? 58.558 46.411  -7.854  1.00 37.30  ?  268 ARG C CD    1 
ATOM   8591  N  NE    . ARG C  2  236 ? 59.073 46.132  -9.197  1.00 37.43  ?  268 ARG C NE    1 
ATOM   8592  C  CZ    . ARG C  2  236 ? 58.359 46.021  -10.324 1.00 35.88  ?  268 ARG C CZ    1 
ATOM   8593  N  NH1   . ARG C  2  236 ? 57.042 46.223  -10.352 1.00 36.15  1  268 ARG C NH1   1 
ATOM   8594  N  NH2   . ARG C  2  236 ? 58.987 45.732  -11.456 1.00 33.69  ?  268 ARG C NH2   1 
ATOM   8595  N  N     . GLU C  2  237 ? 58.467 44.208  -2.593  1.00 54.39  ?  269 GLU C N     1 
ATOM   8596  C  CA    . GLU C  2  237 ? 57.860 44.470  -1.287  1.00 57.50  ?  269 GLU C CA    1 
ATOM   8597  C  C     . GLU C  2  237 ? 56.398 44.860  -1.358  1.00 62.07  ?  269 GLU C C     1 
ATOM   8598  O  O     . GLU C  2  237 ? 55.545 44.301  -0.652  1.00 63.07  ?  269 GLU C O     1 
ATOM   8599  C  CB    . GLU C  2  237 ? 58.631 45.618  -0.631  1.00 59.54  ?  269 GLU C CB    1 
ATOM   8600  C  CG    . GLU C  2  237 ? 57.933 46.327  0.523   1.00 60.46  ?  269 GLU C CG    1 
ATOM   8601  C  CD    . GLU C  2  237 ? 58.152 45.641  1.850   1.00 64.26  ?  269 GLU C CD    1 
ATOM   8602  O  OE1   . GLU C  2  237 ? 59.139 44.877  2.010   1.00 64.62  ?  269 GLU C OE1   1 
ATOM   8603  O  OE2   . GLU C  2  237 ? 57.320 45.883  2.740   1.00 69.58  -1 269 GLU C OE2   1 
ATOM   8604  N  N     . TYR C  2  238 ? 56.127 45.864  -2.188  1.00 68.49  ?  270 TYR C N     1 
ATOM   8605  C  CA    . TYR C  2  238 ? 54.778 46.398  -2.327  1.00 66.60  ?  270 TYR C CA    1 
ATOM   8606  C  C     . TYR C  2  238 ? 53.799 45.260  -2.681  1.00 58.36  ?  270 TYR C C     1 
ATOM   8607  O  O     . TYR C  2  238 ? 52.809 45.055  -1.987  1.00 53.50  ?  270 TYR C O     1 
ATOM   8608  C  CB    . TYR C  2  238 ? 54.740 47.568  -3.335  1.00 64.74  ?  270 TYR C CB    1 
ATOM   8609  C  CG    . TYR C  2  238 ? 53.337 47.926  -3.687  1.00 65.38  ?  270 TYR C CG    1 
ATOM   8610  C  CD1   . TYR C  2  238 ? 52.548 48.704  -2.831  1.00 65.59  ?  270 TYR C CD1   1 
ATOM   8611  C  CD2   . TYR C  2  238 ? 52.767 47.425  -4.848  1.00 67.83  ?  270 TYR C CD2   1 
ATOM   8612  C  CE1   . TYR C  2  238 ? 51.225 48.991  -3.154  1.00 70.71  ?  270 TYR C CE1   1 
ATOM   8613  C  CE2   . TYR C  2  238 ? 51.457 47.704  -5.187  1.00 71.66  ?  270 TYR C CE2   1 
ATOM   8614  C  CZ    . TYR C  2  238 ? 50.682 48.480  -4.350  1.00 73.35  ?  270 TYR C CZ    1 
ATOM   8615  O  OH    . TYR C  2  238 ? 49.376 48.707  -4.752  1.00 73.35  ?  270 TYR C OH    1 
ATOM   8616  N  N     . TYR C  2  239 ? 54.117 44.492  -3.715  1.00 54.94  ?  271 TYR C N     1 
ATOM   8617  C  CA    . TYR C  2  239 ? 53.258 43.384  -4.133  1.00 54.91  ?  271 TYR C CA    1 
ATOM   8618  C  C     . TYR C  2  239 ? 53.164 42.259  -3.110  1.00 52.73  ?  271 TYR C C     1 
ATOM   8619  O  O     . TYR C  2  239 ? 52.098 41.665  -2.924  1.00 52.16  ?  271 TYR C O     1 
ATOM   8620  C  CB    . TYR C  2  239 ? 53.752 42.791  -5.446  1.00 55.35  ?  271 TYR C CB    1 
ATOM   8621  C  CG    . TYR C  2  239 ? 53.709 43.756  -6.596  1.00 59.65  ?  271 TYR C CG    1 
ATOM   8622  C  CD1   . TYR C  2  239 ? 52.549 44.461  -6.906  1.00 61.60  ?  271 TYR C CD1   1 
ATOM   8623  C  CD2   . TYR C  2  239 ? 54.830 43.961  -7.393  1.00 63.89  ?  271 TYR C CD2   1 
ATOM   8624  C  CE1   . TYR C  2  239 ? 52.512 45.351  -7.973  1.00 62.21  ?  271 TYR C CE1   1 
ATOM   8625  C  CE2   . TYR C  2  239 ? 54.799 44.842  -8.462  1.00 63.30  ?  271 TYR C CE2   1 
ATOM   8626  C  CZ    . TYR C  2  239 ? 53.640 45.533  -8.750  1.00 61.22  ?  271 TYR C CZ    1 
ATOM   8627  O  OH    . TYR C  2  239 ? 53.601 46.401  -9.808  1.00 58.59  ?  271 TYR C OH    1 
ATOM   8628  N  N     . ASN C  2  240 ? 54.283 41.938  -2.476  1.00 48.52  ?  272 ASN C N     1 
ATOM   8629  C  CA    . ASN C  2  240 ? 54.292 40.872  -1.503  1.00 43.49  ?  272 ASN C CA    1 
ATOM   8630  C  C     . ASN C  2  240 ? 53.318 41.137  -0.349  1.00 44.02  ?  272 ASN C C     1 
ATOM   8631  O  O     . ASN C  2  240 ? 52.575 40.253  0.029   1.00 45.74  ?  272 ASN C O     1 
ATOM   8632  C  CB    . ASN C  2  240 ? 55.694 40.622  -0.988  1.00 40.29  ?  272 ASN C CB    1 
ATOM   8633  C  CG    . ASN C  2  240 ? 55.681 39.715  0.186   1.00 38.26  ?  272 ASN C CG    1 
ATOM   8634  O  OD1   . ASN C  2  240 ? 55.250 38.567  0.089   1.00 34.37  ?  272 ASN C OD1   1 
ATOM   8635  N  ND2   . ASN C  2  240 ? 56.070 40.244  1.327   1.00 40.07  ?  272 ASN C ND2   1 
ATOM   8636  N  N     . GLU C  2  241 ? 53.284 42.354  0.183   1.00 46.07  ?  273 GLU C N     1 
ATOM   8637  C  CA    . GLU C  2  241 ? 52.323 42.685  1.254   1.00 48.91  ?  273 GLU C CA    1 
ATOM   8638  C  C     . GLU C  2  241 ? 50.862 42.509  0.803   1.00 51.99  ?  273 GLU C C     1 
ATOM   8639  O  O     . GLU C  2  241 ? 50.033 41.975  1.541   1.00 53.84  ?  273 GLU C O     1 
ATOM   8640  C  CB    . GLU C  2  241 ? 52.524 44.118  1.737   1.00 47.31  ?  273 GLU C CB    1 
ATOM   8641  C  CG    . GLU C  2  241 ? 53.850 44.368  2.419   1.00 48.99  ?  273 GLU C CG    1 
ATOM   8642  C  CD    . GLU C  2  241 ? 54.026 43.608  3.730   1.00 52.18  ?  273 GLU C CD    1 
ATOM   8643  O  OE1   . GLU C  2  241 ? 53.062 43.481  4.532   1.00 49.64  ?  273 GLU C OE1   1 
ATOM   8644  O  OE2   . GLU C  2  241 ? 55.172 43.149  3.964   1.00 55.59  -1 273 GLU C OE2   1 
ATOM   8645  N  N     . LYS C  2  242 ? 50.579 42.994  -0.408  1.00 53.26  ?  274 LYS C N     1 
ATOM   8646  C  CA    . LYS C  2  242 ? 49.290 42.859  -1.097  1.00 51.26  ?  274 LYS C CA    1 
ATOM   8647  C  C     . LYS C  2  242 ? 48.881 41.364  -1.214  1.00 49.52  ?  274 LYS C C     1 
ATOM   8648  O  O     . LYS C  2  242 ? 47.743 40.981  -0.900  1.00 47.34  ?  274 LYS C O     1 
ATOM   8649  C  CB    . LYS C  2  242 ? 49.434 43.492  -2.500  1.00 51.56  ?  274 LYS C CB    1 
ATOM   8650  C  CG    . LYS C  2  242 ? 48.177 44.040  -3.142  1.00 54.58  ?  274 LYS C CG    1 
ATOM   8651  C  CD    . LYS C  2  242 ? 48.232 45.558  -3.261  1.00 59.47  ?  274 LYS C CD    1 
ATOM   8652  C  CE    . LYS C  2  242 ? 47.348 46.068  -4.399  1.00 61.76  ?  274 LYS C CE    1 
ATOM   8653  N  NZ    . LYS C  2  242 ? 45.947 45.544  -4.324  1.00 63.19  1  274 LYS C NZ    1 
ATOM   8654  N  N     . LEU C  2  243 ? 49.827 40.529  -1.656  1.00 48.68  ?  275 LEU C N     1 
ATOM   8655  C  CA    . LEU C  2  243 ? 49.583 39.089  -1.895  1.00 46.80  ?  275 LEU C CA    1 
ATOM   8656  C  C     . LEU C  2  243 ? 49.346 38.317  -0.633  1.00 44.57  ?  275 LEU C C     1 
ATOM   8657  O  O     . LEU C  2  243 ? 48.576 37.355  -0.652  1.00 42.56  ?  275 LEU C O     1 
ATOM   8658  C  CB    . LEU C  2  243 ? 50.766 38.404  -2.606  1.00 46.07  ?  275 LEU C CB    1 
ATOM   8659  C  CG    . LEU C  2  243 ? 50.700 38.062  -4.092  1.00 44.60  ?  275 LEU C CG    1 
ATOM   8660  C  CD1   . LEU C  2  243 ? 51.790 37.054  -4.472  1.00 44.02  ?  275 LEU C CD1   1 
ATOM   8661  C  CD2   . LEU C  2  243 ? 49.337 37.489  -4.409  1.00 44.82  ?  275 LEU C CD2   1 
ATOM   8662  N  N     . ILE C  2  244 ? 50.062 38.706  0.427   1.00 44.19  ?  276 ILE C N     1 
ATOM   8663  C  CA    . ILE C  2  244 ? 49.917 38.099  1.751   1.00 45.84  ?  276 ILE C CA    1 
ATOM   8664  C  C     . ILE C  2  244 ? 48.552 38.500  2.339   1.00 46.19  ?  276 ILE C C     1 
ATOM   8665  O  O     . ILE C  2  244 ? 47.866 37.655  2.912   1.00 45.71  ?  276 ILE C O     1 
ATOM   8666  C  CB    . ILE C  2  244 ? 51.082 38.489  2.724   1.00 47.92  ?  276 ILE C CB    1 
ATOM   8667  C  CG1   . ILE C  2  244 ? 52.472 38.056  2.191   1.00 49.36  ?  276 ILE C CG1   1 
ATOM   8668  C  CG2   . ILE C  2  244 ? 50.865 37.908  4.128   1.00 47.27  ?  276 ILE C CG2   1 
ATOM   8669  C  CD1   . ILE C  2  244 ? 52.575 36.624  1.695   1.00 49.21  ?  276 ILE C CD1   1 
ATOM   8670  N  N     . ASP C  2  245 ? 48.154 39.768  2.183   1.00 46.63  ?  277 ASP C N     1 
ATOM   8671  C  CA    . ASP C  2  245 ? 46.840 40.232  2.659   1.00 48.40  ?  277 ASP C CA    1 
ATOM   8672  C  C     . ASP C  2  245 ? 45.697 39.475  2.006   1.00 49.02  ?  277 ASP C C     1 
ATOM   8673  O  O     . ASP C  2  245 ? 44.767 39.046  2.691   1.00 49.12  ?  277 ASP C O     1 
ATOM   8674  C  CB    . ASP C  2  245 ? 46.660 41.739  2.452   1.00 52.95  ?  277 ASP C CB    1 
ATOM   8675  C  CG    . ASP C  2  245 ? 47.014 42.556  3.707   1.00 61.01  ?  277 ASP C CG    1 
ATOM   8676  O  OD1   . ASP C  2  245 ? 47.524 41.990  4.703   1.00 69.51  ?  277 ASP C OD1   1 
ATOM   8677  O  OD2   . ASP C  2  245 ? 46.773 43.782  3.717   1.00 66.65  -1 277 ASP C OD2   1 
ATOM   8678  N  N     . ILE C  2  246 ? 45.779 39.284  0.692   1.00 47.76  ?  278 ILE C N     1 
ATOM   8679  C  CA    . ILE C  2  246 ? 44.845 38.386  0.000   1.00 46.28  ?  278 ILE C CA    1 
ATOM   8680  C  C     . ILE C  2  246 ? 44.836 36.934  0.580   1.00 44.16  ?  278 ILE C C     1 
ATOM   8681  O  O     . ILE C  2  246 ? 43.775 36.446  0.958   1.00 40.69  ?  278 ILE C O     1 
ATOM   8682  C  CB    . ILE C  2  246 ? 45.083 38.377  -1.531  1.00 44.58  ?  278 ILE C CB    1 
ATOM   8683  C  CG1   . ILE C  2  246 ? 44.861 39.778  -2.124  1.00 42.17  ?  278 ILE C CG1   1 
ATOM   8684  C  CG2   . ILE C  2  246 ? 44.142 37.377  -2.196  1.00 44.82  ?  278 ILE C CG2   1 
ATOM   8685  C  CD1   . ILE C  2  246 ? 45.436 39.974  -3.514  1.00 39.77  ?  278 ILE C CD1   1 
ATOM   8686  N  N     . PHE C  2  247 ? 45.998 36.263  0.649   1.00 46.69  ?  279 PHE C N     1 
ATOM   8687  C  CA    . PHE C  2  247 ? 46.104 34.868  1.204   1.00 46.89  ?  279 PHE C CA    1 
ATOM   8688  C  C     . PHE C  2  247 ? 45.636 34.778  2.673   1.00 44.89  ?  279 PHE C C     1 
ATOM   8689  O  O     . PHE C  2  247 ? 45.066 33.758  3.077   1.00 38.05  ?  279 PHE C O     1 
ATOM   8690  C  CB    . PHE C  2  247 ? 47.544 34.255  1.129   1.00 46.22  ?  279 PHE C CB    1 
ATOM   8691  C  CG    . PHE C  2  247 ? 48.118 34.065  -0.276  1.00 47.24  ?  279 PHE C CG    1 
ATOM   8692  C  CD1   . PHE C  2  247 ? 47.334 34.131  -1.435  1.00 49.12  ?  279 PHE C CD1   1 
ATOM   8693  C  CD2   . PHE C  2  247 ? 49.479 33.775  -0.426  1.00 47.70  ?  279 PHE C CD2   1 
ATOM   8694  C  CE1   . PHE C  2  247 ? 47.903 33.932  -2.697  1.00 49.31  ?  279 PHE C CE1   1 
ATOM   8695  C  CE2   . PHE C  2  247 ? 50.050 33.588  -1.683  1.00 48.06  ?  279 PHE C CE2   1 
ATOM   8696  C  CZ    . PHE C  2  247 ? 49.261 33.657  -2.818  1.00 48.99  ?  279 PHE C CZ    1 
ATOM   8697  N  N     . GLN C  2  248 ? 45.911 35.821  3.468   1.00 45.93  ?  280 GLN C N     1 
ATOM   8698  C  CA    . GLN C  2  248 ? 45.456 35.861  4.864   1.00 45.87  ?  280 GLN C CA    1 
ATOM   8699  C  C     . GLN C  2  248 ? 43.935 35.712  4.813   1.00 46.45  ?  280 GLN C C     1 
ATOM   8700  O  O     . GLN C  2  248 ? 43.411 34.818  5.454   1.00 45.95  ?  280 GLN C O     1 
ATOM   8701  C  CB    . GLN C  2  248 ? 45.932 37.135  5.644   1.00 45.97  ?  280 GLN C CB    1 
ATOM   8702  C  CG    . GLN C  2  248 ? 47.269 36.986  6.426   1.00 46.29  ?  280 GLN C CG    1 
ATOM   8703  C  CD    . GLN C  2  248 ? 47.971 38.300  6.917   1.00 45.42  ?  280 GLN C CD    1 
ATOM   8704  O  OE1   . GLN C  2  248 ? 47.632 39.413  6.511   1.00 43.65  ?  280 GLN C OE1   1 
ATOM   8705  N  NE2   . GLN C  2  248 ? 48.977 38.145  7.792   1.00 42.94  ?  280 GLN C NE2   1 
ATOM   8706  N  N     . LYS C  2  249 ? 43.255 36.511  3.977   1.00 49.23  ?  281 LYS C N     1 
ATOM   8707  C  CA    . LYS C  2  249 ? 41.763 36.568  3.935   1.00 49.17  ?  281 LYS C CA    1 
ATOM   8708  C  C     . LYS C  2  249 ? 41.081 35.288  3.469   1.00 46.43  ?  281 LYS C C     1 
ATOM   8709  O  O     . LYS C  2  249 ? 40.017 34.943  3.942   1.00 44.40  ?  281 LYS C O     1 
ATOM   8710  C  CB    . LYS C  2  249 ? 41.269 37.742  3.069   1.00 51.06  ?  281 LYS C CB    1 
ATOM   8711  C  CG    . LYS C  2  249 ? 41.683 39.142  3.562   1.00 53.02  ?  281 LYS C CG    1 
ATOM   8712  C  CD    . LYS C  2  249 ? 40.923 40.303  2.890   1.00 56.80  ?  281 LYS C CD    1 
ATOM   8713  C  CE    . LYS C  2  249 ? 40.561 40.118  1.389   1.00 58.87  ?  281 LYS C CE    1 
ATOM   8714  N  NZ    . LYS C  2  249 ? 41.602 40.517  0.388   1.00 56.78  1  281 LYS C NZ    1 
ATOM   8715  N  N     . TYR C  2  250 ? 41.707 34.579  2.551   1.00 50.11  ?  282 TYR C N     1 
ATOM   8716  C  CA    . TYR C  2  250 ? 41.136 33.360  2.004   1.00 54.49  ?  282 TYR C CA    1 
ATOM   8717  C  C     . TYR C  2  250 ? 41.917 32.085  2.375   1.00 54.44  ?  282 TYR C C     1 
ATOM   8718  O  O     . TYR C  2  250 ? 41.990 31.149  1.580   1.00 53.99  ?  282 TYR C O     1 
ATOM   8719  C  CB    . TYR C  2  250 ? 41.084 33.504  0.487   1.00 58.40  ?  282 TYR C CB    1 
ATOM   8720  C  CG    . TYR C  2  250 ? 40.187 34.608  0.022   1.00 62.20  ?  282 TYR C CG    1 
ATOM   8721  C  CD1   . TYR C  2  250 ? 38.838 34.359  -0.217  1.00 64.46  ?  282 TYR C CD1   1 
ATOM   8722  C  CD2   . TYR C  2  250 ? 40.675 35.901  -0.176  1.00 64.22  ?  282 TYR C CD2   1 
ATOM   8723  C  CE1   . TYR C  2  250 ? 37.989 35.362  -0.644  1.00 66.41  ?  282 TYR C CE1   1 
ATOM   8724  C  CE2   . TYR C  2  250 ? 39.836 36.919  -0.600  1.00 69.58  ?  282 TYR C CE2   1 
ATOM   8725  C  CZ    . TYR C  2  250 ? 38.492 36.638  -0.837  1.00 70.10  ?  282 TYR C CZ    1 
ATOM   8726  O  OH    . TYR C  2  250 ? 37.642 37.622  -1.275  1.00 68.94  ?  282 TYR C OH    1 
ATOM   8727  N  N     . SER C  2  251 ? 42.486 32.034  3.577   1.00 54.37  ?  283 SER C N     1 
ATOM   8728  C  CA    . SER C  2  251 ? 43.332 30.895  3.985   1.00 54.63  ?  283 SER C CA    1 
ATOM   8729  C  C     . SER C  2  251 ? 42.524 29.625  4.242   1.00 55.82  ?  283 SER C C     1 
ATOM   8730  O  O     . SER C  2  251 ? 43.042 28.483  4.148   1.00 51.88  ?  283 SER C O     1 
ATOM   8731  C  CB    . SER C  2  251 ? 44.087 31.248  5.253   1.00 55.28  ?  283 SER C CB    1 
ATOM   8732  O  OG    . SER C  2  251 ? 43.168 31.535  6.287   1.00 56.22  ?  283 SER C OG    1 
ATOM   8733  N  N     . ASP C  2  252 ? 41.264 29.852  4.615   1.00 55.78  ?  284 ASP C N     1 
ATOM   8734  C  CA    . ASP C  2  252 ? 40.258 28.802  4.702   1.00 54.25  ?  284 ASP C CA    1 
ATOM   8735  C  C     . ASP C  2  252 ? 40.203 27.959  3.403   1.00 49.83  ?  284 ASP C C     1 
ATOM   8736  O  O     . ASP C  2  252 ? 40.200 26.729  3.467   1.00 47.60  ?  284 ASP C O     1 
ATOM   8737  C  CB    . ASP C  2  252 ? 38.871 29.383  5.105   1.00 57.93  ?  284 ASP C CB    1 
ATOM   8738  C  CG    . ASP C  2  252 ? 38.612 30.820  4.569   1.00 61.39  ?  284 ASP C CG    1 
ATOM   8739  O  OD1   . ASP C  2  252 ? 39.335 31.780  4.950   1.00 58.00  ?  284 ASP C OD1   1 
ATOM   8740  O  OD2   . ASP C  2  252 ? 37.648 30.988  3.787   1.00 65.18  -1 284 ASP C OD2   1 
ATOM   8741  N  N     . VAL C  2  253 ? 40.249 28.620  2.239   1.00 47.31  ?  285 VAL C N     1 
ATOM   8742  C  CA    . VAL C  2  253 ? 40.109 27.955  0.904   1.00 43.97  ?  285 VAL C CA    1 
ATOM   8743  C  C     . VAL C  2  253 ? 41.379 27.247  0.361   1.00 39.57  ?  285 VAL C C     1 
ATOM   8744  O  O     . VAL C  2  253 ? 41.283 26.171  -0.258  1.00 35.00  ?  285 VAL C O     1 
ATOM   8745  C  CB    . VAL C  2  253 ? 39.664 28.954  -0.202  1.00 44.81  ?  285 VAL C CB    1 
ATOM   8746  C  CG1   . VAL C  2  253 ? 38.815 28.223  -1.238  1.00 45.10  ?  285 VAL C CG1   1 
ATOM   8747  C  CG2   . VAL C  2  253 ? 38.902 30.155  0.362   1.00 45.39  ?  285 VAL C CG2   1 
ATOM   8748  N  N     . ILE C  2  254 ? 42.541 27.875  0.608   1.00 36.39  ?  286 ILE C N     1 
ATOM   8749  C  CA    . ILE C  2  254 ? 43.846 27.474  0.077   1.00 32.81  ?  286 ILE C CA    1 
ATOM   8750  C  C     . ILE C  2  254 ? 44.358 26.312  0.859   1.00 32.40  ?  286 ILE C C     1 
ATOM   8751  O  O     . ILE C  2  254 ? 44.598 26.435  2.057   1.00 31.68  ?  286 ILE C O     1 
ATOM   8752  C  CB    . ILE C  2  254 ? 44.876 28.595  0.242   1.00 31.32  ?  286 ILE C CB    1 
ATOM   8753  C  CG1   . ILE C  2  254 ? 44.352 29.857  -0.412  1.00 31.83  ?  286 ILE C CG1   1 
ATOM   8754  C  CG2   . ILE C  2  254 ? 46.229 28.203  -0.362  1.00 30.39  ?  286 ILE C CG2   1 
ATOM   8755  C  CD1   . ILE C  2  254 ? 45.106 31.096  -0.010  1.00 32.77  ?  286 ILE C CD1   1 
ATOM   8756  N  N     . ALA C  2  255 ? 44.527 25.187  0.185   1.00 33.37  ?  287 ALA C N     1 
ATOM   8757  C  CA    . ALA C  2  255 ? 44.929 23.974  0.864   1.00 37.03  ?  287 ALA C CA    1 
ATOM   8758  C  C     . ALA C  2  255 ? 46.403 23.694  0.671   1.00 39.11  ?  287 ALA C C     1 
ATOM   8759  O  O     . ALA C  2  255 ? 46.869 22.630  1.049   1.00 43.18  ?  287 ALA C O     1 
ATOM   8760  C  CB    . ALA C  2  255 ? 44.092 22.787  0.406   1.00 37.11  ?  287 ALA C CB    1 
ATOM   8761  N  N     . GLY C  2  256 ? 47.139 24.638  0.094   1.00 41.04  ?  288 GLY C N     1 
ATOM   8762  C  CA    . GLY C  2  256 ? 48.610 24.561  0.060   1.00 41.57  ?  288 GLY C CA    1 
ATOM   8763  C  C     . GLY C  2  256 ? 49.201 25.404  -1.051  1.00 40.77  ?  288 GLY C C     1 
ATOM   8764  O  O     . GLY C  2  256 ? 48.489 25.799  -1.971  1.00 39.85  ?  288 GLY C O     1 
ATOM   8765  N  N     . GLN C  2  257 ? 50.497 25.694  -0.972  1.00 40.06  ?  289 GLN C N     1 
ATOM   8766  C  CA    . GLN C  2  257 ? 51.104 26.624  -1.933  1.00 38.97  ?  289 GLN C CA    1 
ATOM   8767  C  C     . GLN C  2  257 ? 52.435 26.131  -2.439  1.00 37.33  ?  289 GLN C C     1 
ATOM   8768  O  O     . GLN C  2  257 ? 53.227 25.607  -1.669  1.00 37.11  ?  289 GLN C O     1 
ATOM   8769  C  CB    . GLN C  2  257 ? 51.255 28.001  -1.320  1.00 37.51  ?  289 GLN C CB    1 
ATOM   8770  C  CG    . GLN C  2  257 ? 49.923 28.624  -1.013  1.00 37.06  ?  289 GLN C CG    1 
ATOM   8771  C  CD    . GLN C  2  257 ? 50.079 30.030  -0.548  1.00 37.41  ?  289 GLN C CD    1 
ATOM   8772  O  OE1   . GLN C  2  257 ? 50.489 30.903  -1.308  1.00 37.81  ?  289 GLN C OE1   1 
ATOM   8773  N  NE2   . GLN C  2  257 ? 49.742 30.270  0.706   1.00 38.35  ?  289 GLN C NE2   1 
ATOM   8774  N  N     . PHE C  2  258 ? 52.667 26.332  -3.738  1.00 36.42  ?  290 PHE C N     1 
ATOM   8775  C  CA    . PHE C  2  258 ? 53.734 25.668  -4.473  1.00 33.98  ?  290 PHE C CA    1 
ATOM   8776  C  C     . PHE C  2  258 ? 54.457 26.689  -5.344  1.00 31.42  ?  290 PHE C C     1 
ATOM   8777  O  O     . PHE C  2  258 ? 53.825 27.468  -6.059  1.00 27.46  ?  290 PHE C O     1 
ATOM   8778  C  CB    . PHE C  2  258 ? 53.136 24.517  -5.291  1.00 34.81  ?  290 PHE C CB    1 
ATOM   8779  C  CG    . PHE C  2  258 ? 52.287 23.590  -4.468  1.00 36.16  ?  290 PHE C CG    1 
ATOM   8780  C  CD1   . PHE C  2  258 ? 52.875 22.670  -3.596  1.00 39.29  ?  290 PHE C CD1   1 
ATOM   8781  C  CD2   . PHE C  2  258 ? 50.907 23.673  -4.502  1.00 36.22  ?  290 PHE C CD2   1 
ATOM   8782  C  CE1   . PHE C  2  258 ? 52.081 21.838  -2.794  1.00 40.02  ?  290 PHE C CE1   1 
ATOM   8783  C  CE2   . PHE C  2  258 ? 50.122 22.845  -3.722  1.00 36.96  ?  290 PHE C CE2   1 
ATOM   8784  C  CZ    . PHE C  2  258 ? 50.701 21.931  -2.866  1.00 38.14  ?  290 PHE C CZ    1 
ATOM   8785  N  N     . TYR C  2  259 ? 55.787 26.701  -5.233  1.00 30.84  ?  291 TYR C N     1 
ATOM   8786  C  CA    . TYR C  2  259 ? 56.634 27.681  -5.930  1.00 29.63  ?  291 TYR C CA    1 
ATOM   8787  C  C     . TYR C  2  259 ? 58.007 27.111  -6.228  1.00 27.68  ?  291 TYR C C     1 
ATOM   8788  O  O     . TYR C  2  259 ? 58.408 26.097  -5.688  1.00 26.69  ?  291 TYR C O     1 
ATOM   8789  C  CB    . TYR C  2  259 ? 56.871 28.939  -5.098  1.00 30.03  ?  291 TYR C CB    1 
ATOM   8790  C  CG    . TYR C  2  259 ? 55.672 29.680  -4.575  1.00 31.58  ?  291 TYR C CG    1 
ATOM   8791  C  CD1   . TYR C  2  259 ? 55.039 30.633  -5.344  1.00 31.71  ?  291 TYR C CD1   1 
ATOM   8792  C  CD2   . TYR C  2  259 ? 55.217 29.475  -3.261  1.00 32.84  ?  291 TYR C CD2   1 
ATOM   8793  C  CE1   . TYR C  2  259 ? 53.947 31.336  -4.845  1.00 34.31  ?  291 TYR C CE1   1 
ATOM   8794  C  CE2   . TYR C  2  259 ? 54.131 30.173  -2.743  1.00 33.17  ?  291 TYR C CE2   1 
ATOM   8795  C  CZ    . TYR C  2  259 ? 53.486 31.113  -3.534  1.00 34.85  ?  291 TYR C CZ    1 
ATOM   8796  O  OH    . TYR C  2  259 ? 52.393 31.848  -3.040  1.00 34.16  ?  291 TYR C OH    1 
ATOM   8797  N  N     . GLY C  2  260 ? 58.742 27.806  -7.079  1.00 27.25  ?  292 GLY C N     1 
ATOM   8798  C  CA    . GLY C  2  260 ? 60.068 27.377  -7.478  1.00 25.84  ?  292 GLY C CA    1 
ATOM   8799  C  C     . GLY C  2  260 ? 60.953 28.569  -7.334  1.00 24.80  ?  292 GLY C C     1 
ATOM   8800  O  O     . GLY C  2  260 ? 61.097 29.108  -6.239  1.00 22.75  ?  292 GLY C O     1 
ATOM   8801  N  N     . HIS C  2  261 ? 61.551 28.973  -8.445  1.00 25.58  ?  293 HIS C N     1 
ATOM   8802  C  CA    . HIS C  2  261 ? 62.372 30.195  -8.519  1.00 26.10  ?  293 HIS C CA    1 
ATOM   8803  C  C     . HIS C  2  261 ? 63.670 30.176  -7.616  1.00 25.83  ?  293 HIS C C     1 
ATOM   8804  O  O     . HIS C  2  261 ? 64.772 30.299  -8.177  1.00 26.22  ?  293 HIS C O     1 
ATOM   8805  C  CB    . HIS C  2  261 ? 61.453 31.449  -8.338  1.00 26.45  ?  293 HIS C CB    1 
ATOM   8806  C  CG    . HIS C  2  261 ? 62.164 32.768  -8.359  1.00 25.29  ?  293 HIS C CG    1 
ATOM   8807  N  ND1   . HIS C  2  261 ? 63.152 33.071  -9.262  1.00 25.01  ?  293 HIS C ND1   1 
ATOM   8808  C  CD2   . HIS C  2  261 ? 62.006 33.871  -7.594  1.00 25.62  ?  293 HIS C CD2   1 
ATOM   8809  C  CE1   . HIS C  2  261 ? 63.601 34.290  -9.038  1.00 25.34  ?  293 HIS C CE1   1 
ATOM   8810  N  NE2   . HIS C  2  261 ? 62.912 34.805  -8.038  1.00 26.34  ?  293 HIS C NE2   1 
ATOM   8811  N  N     A THR C  2  262 ? 63.565 30.007  -6.278  0.50 24.68  ?  294 THR C N     1 
ATOM   8812  N  N     B THR C  2  262 ? 63.511 30.001  -6.295  0.50 24.73  ?  294 THR C N     1 
ATOM   8813  C  CA    A THR C  2  262 ? 64.769 30.041  -5.403  0.50 22.78  ?  294 THR C CA    1 
ATOM   8814  C  CA    B THR C  2  262 ? 64.617 30.002  -5.330  0.50 22.69  ?  294 THR C CA    1 
ATOM   8815  C  C     A THR C  2  262 ? 65.796 28.951  -5.736  0.50 22.50  ?  294 THR C C     1 
ATOM   8816  C  C     B THR C  2  262 ? 65.711 28.930  -5.643  0.50 22.49  ?  294 THR C C     1 
ATOM   8817  O  O     A THR C  2  262 ? 66.977 29.101  -5.438  0.50 21.54  ?  294 THR C O     1 
ATOM   8818  O  O     B THR C  2  262 ? 66.863 29.094  -5.262  0.50 21.69  ?  294 THR C O     1 
ATOM   8819  C  CB    A THR C  2  262 ? 64.452 30.004  -3.885  0.50 21.82  ?  294 THR C CB    1 
ATOM   8820  C  CB    B THR C  2  262 ? 64.028 29.937  -3.889  0.50 21.69  ?  294 THR C CB    1 
ATOM   8821  O  OG1   A THR C  2  262 ? 64.140 28.669  -3.476  0.50 20.67  ?  294 THR C OG1   1 
ATOM   8822  O  OG1   B THR C  2  262 ? 63.635 31.257  -3.452  0.50 20.90  ?  294 THR C OG1   1 
ATOM   8823  C  CG2   A THR C  2  262 ? 63.319 30.995  -3.525  0.50 21.53  ?  294 THR C CG2   1 
ATOM   8824  C  CG2   B THR C  2  262 ? 65.000 29.365  -2.922  0.50 21.11  ?  294 THR C CG2   1 
ATOM   8825  N  N     . HIS C  2  263 ? 65.346 27.894  -6.410  1.00 23.21  ?  295 HIS C N     1 
ATOM   8826  C  CA    . HIS C  2  263 ? 66.183 26.698  -6.722  1.00 23.88  ?  295 HIS C CA    1 
ATOM   8827  C  C     . HIS C  2  263 ? 66.505 25.942  -5.400  1.00 25.23  ?  295 HIS C C     1 
ATOM   8828  O  O     . HIS C  2  263 ? 67.438 25.123  -5.308  1.00 24.28  ?  295 HIS C O     1 
ATOM   8829  C  CB    . HIS C  2  263 ? 67.453 27.002  -7.544  1.00 24.47  ?  295 HIS C CB    1 
ATOM   8830  C  CG    . HIS C  2  263 ? 67.218 27.372  -8.995  1.00 25.78  ?  295 HIS C CG    1 
ATOM   8831  N  ND1   . HIS C  2  263 ? 68.226 27.324  -9.945  1.00 26.15  ?  295 HIS C ND1   1 
ATOM   8832  C  CD2   . HIS C  2  263 ? 66.121 27.822  -9.653  1.00 25.80  ?  295 HIS C CD2   1 
ATOM   8833  C  CE1   . HIS C  2  263 ? 67.764 27.741  -11.111 1.00 25.03  ?  295 HIS C CE1   1 
ATOM   8834  N  NE2   . HIS C  2  263 ? 66.487 28.032  -10.967 1.00 24.46  ?  295 HIS C NE2   1 
ATOM   8835  N  N     . ARG C  2  264 ? 65.682 26.181  -4.380  1.00 26.33  ?  296 ARG C N     1 
ATOM   8836  C  CA    . ARG C  2  264 ? 65.948 25.634  -3.074  1.00 26.81  ?  296 ARG C CA    1 
ATOM   8837  C  C     . ARG C  2  264 ? 64.724 24.954  -2.498  1.00 26.77  ?  296 ARG C C     1 
ATOM   8838  O  O     . ARG C  2  264 ? 63.586 25.246  -2.881  1.00 25.17  ?  296 ARG C O     1 
ATOM   8839  C  CB    . ARG C  2  264 ? 66.468 26.706  -2.093  1.00 26.83  ?  296 ARG C CB    1 
ATOM   8840  C  CG    . ARG C  2  264 ? 67.699 27.444  -2.579  1.00 26.76  ?  296 ARG C CG    1 
ATOM   8841  C  CD    . ARG C  2  264 ? 68.917 26.534  -2.558  1.00 27.55  ?  296 ARG C CD    1 
ATOM   8842  N  NE    . ARG C  2  264 ? 70.120 27.133  -3.166  1.00 28.55  ?  296 ARG C NE    1 
ATOM   8843  C  CZ    . ARG C  2  264 ? 70.601 26.854  -4.384  1.00 29.10  ?  296 ARG C CZ    1 
ATOM   8844  N  NH1   . ARG C  2  264 ? 70.005 25.992  -5.213  1.00 30.89  1  296 ARG C NH1   1 
ATOM   8845  N  NH2   . ARG C  2  264 ? 71.701 27.447  -4.789  1.00 29.26  ?  296 ARG C NH2   1 
ATOM   8846  N  N     . ASP C  2  265 ? 65.020 24.041  -1.568  1.00 26.99  ?  297 ASP C N     1 
ATOM   8847  C  CA    . ASP C  2  265 ? 64.045 23.326  -0.784  1.00 27.77  ?  297 ASP C CA    1 
ATOM   8848  C  C     . ASP C  2  265 ? 63.751 24.096  0.501   1.00 27.65  ?  297 ASP C C     1 
ATOM   8849  O  O     . ASP C  2  265 ? 64.387 23.871  1.558   1.00 26.34  ?  297 ASP C O     1 
ATOM   8850  C  CB    . ASP C  2  265 ? 64.580 21.933  -0.463  1.00 28.78  ?  297 ASP C CB    1 
ATOM   8851  C  CG    . ASP C  2  265 ? 63.566 21.071  0.284   1.00 29.39  ?  297 ASP C CG    1 
ATOM   8852  O  OD1   . ASP C  2  265 ? 62.752 21.613  1.052   1.00 33.18  ?  297 ASP C OD1   1 
ATOM   8853  O  OD2   . ASP C  2  265 ? 63.582 19.842  0.127   1.00 28.94  -1 297 ASP C OD2   1 
ATOM   8854  N  N     . SER C  2  266 ? 62.764 24.988  0.396   1.00 28.59  ?  298 SER C N     1 
ATOM   8855  C  CA    . SER C  2  266 ? 62.325 25.838  1.515   1.00 30.26  ?  298 SER C CA    1 
ATOM   8856  C  C     . SER C  2  266 ? 60.856 25.609  1.912   1.00 30.02  ?  298 SER C C     1 
ATOM   8857  O  O     . SER C  2  266 ? 60.037 25.261  1.062   1.00 32.02  ?  298 SER C O     1 
ATOM   8858  C  CB    . SER C  2  266 ? 62.542 27.317  1.160   1.00 30.35  ?  298 SER C CB    1 
ATOM   8859  O  OG    . SER C  2  266 ? 63.862 27.747  1.472   1.00 30.96  ?  298 SER C OG    1 
ATOM   8860  N  N     . ILE C  2  267 ? 60.537 25.764  3.199   1.00 29.68  ?  299 ILE C N     1 
ATOM   8861  C  CA    . ILE C  2  267 ? 59.127 25.792  3.664   1.00 30.02  ?  299 ILE C CA    1 
ATOM   8862  C  C     . ILE C  2  267 ? 58.798 27.194  4.161   1.00 30.19  ?  299 ILE C C     1 
ATOM   8863  O  O     . ILE C  2  267 ? 59.679 27.908  4.632   1.00 30.66  ?  299 ILE C O     1 
ATOM   8864  C  CB    . ILE C  2  267 ? 58.804 24.766  4.794   1.00 29.11  ?  299 ILE C CB    1 
ATOM   8865  C  CG1   . ILE C  2  267 ? 59.373 25.210  6.155   1.00 28.86  ?  299 ILE C CG1   1 
ATOM   8866  C  CG2   . ILE C  2  267 ? 59.340 23.394  4.444   1.00 29.33  ?  299 ILE C CG2   1 
ATOM   8867  C  CD1   . ILE C  2  267 ? 58.573 24.731  7.347   1.00 28.20  ?  299 ILE C CD1   1 
ATOM   8868  N  N     . MET C  2  268 ? 57.539 27.591  4.031   1.00 30.47  ?  300 MET C N     1 
ATOM   8869  C  CA    . MET C  2  268 ? 57.047 28.814  4.667   1.00 30.97  ?  300 MET C CA    1 
ATOM   8870  C  C     . MET C  2  268 ? 55.715 28.536  5.288   1.00 30.08  ?  300 MET C C     1 
ATOM   8871  O  O     . MET C  2  268 ? 54.998 27.646  4.847   1.00 28.47  ?  300 MET C O     1 
ATOM   8872  C  CB    . MET C  2  268 ? 56.902 29.981  3.690   1.00 31.51  ?  300 MET C CB    1 
ATOM   8873  C  CG    . MET C  2  268 ? 57.987 31.037  3.812   1.00 31.18  ?  300 MET C CG    1 
ATOM   8874  S  SD    . MET C  2  268 ? 57.974 32.221  2.453   1.00 33.59  ?  300 MET C SD    1 
ATOM   8875  C  CE    . MET C  2  268 ? 58.027 31.212  0.947   1.00 30.50  ?  300 MET C CE    1 
ATOM   8876  N  N     . VAL C  2  269 ? 55.416 29.316  6.320   1.00 31.59  ?  301 VAL C N     1 
ATOM   8877  C  CA    . VAL C  2  269 ? 54.189 29.190  7.087   1.00 34.62  ?  301 VAL C CA    1 
ATOM   8878  C  C     . VAL C  2  269 ? 53.553 30.561  7.144   1.00 34.90  ?  301 VAL C C     1 
ATOM   8879  O  O     . VAL C  2  269 ? 54.083 31.466  7.781   1.00 34.57  ?  301 VAL C O     1 
ATOM   8880  C  CB    . VAL C  2  269 ? 54.433 28.646  8.531   1.00 36.47  ?  301 VAL C CB    1 
ATOM   8881  C  CG1   . VAL C  2  269 ? 53.142 28.661  9.349   1.00 36.78  ?  301 VAL C CG1   1 
ATOM   8882  C  CG2   . VAL C  2  269 ? 55.014 27.224  8.505   1.00 37.36  ?  301 VAL C CG2   1 
ATOM   8883  N  N     . LEU C  2  270 ? 52.429 30.721  6.460   1.00 37.27  ?  302 LEU C N     1 
ATOM   8884  C  CA    . LEU C  2  270 ? 51.660 31.938  6.607   1.00 43.18  ?  302 LEU C CA    1 
ATOM   8885  C  C     . LEU C  2  270 ? 50.851 31.918  7.922   1.00 45.02  ?  302 LEU C C     1 
ATOM   8886  O  O     . LEU C  2  270 ? 50.290 30.869  8.308   1.00 42.59  ?  302 LEU C O     1 
ATOM   8887  C  CB    . LEU C  2  270 ? 50.732 32.139  5.410   1.00 45.44  ?  302 LEU C CB    1 
ATOM   8888  C  CG    . LEU C  2  270 ? 49.800 33.360  5.522   1.00 46.83  ?  302 LEU C CG    1 
ATOM   8889  C  CD1   . LEU C  2  270 ? 50.599 34.656  5.615   1.00 45.69  ?  302 LEU C CD1   1 
ATOM   8890  C  CD2   . LEU C  2  270 ? 48.816 33.400  4.351   1.00 48.27  ?  302 LEU C CD2   1 
ATOM   8891  N  N     . SER C  2  271 ? 50.807 33.080  8.589   1.00 46.74  ?  303 SER C N     1 
ATOM   8892  C  CA    . SER C  2  271 ? 50.019 33.284  9.814   1.00 50.96  ?  303 SER C CA    1 
ATOM   8893  C  C     . SER C  2  271 ? 48.970 34.403  9.651   1.00 54.20  ?  303 SER C C     1 
ATOM   8894  O  O     . SER C  2  271 ? 49.185 35.341  8.882   1.00 54.81  ?  303 SER C O     1 
ATOM   8895  C  CB    . SER C  2  271 ? 50.951 33.610  10.992  1.00 51.05  ?  303 SER C CB    1 
ATOM   8896  O  OG    . SER C  2  271 ? 51.971 32.625  11.130  1.00 52.08  ?  303 SER C OG    1 
ATOM   8897  N  N     . ASP C  2  272 ? 47.839 34.311  10.367  1.00 56.34  ?  304 ASP C N     1 
ATOM   8898  C  CA    . ASP C  2  272 ? 46.819 35.367  10.299  1.00 54.41  ?  304 ASP C CA    1 
ATOM   8899  C  C     . ASP C  2  272 ? 47.407 36.626  10.953  1.00 51.78  ?  304 ASP C C     1 
ATOM   8900  O  O     . ASP C  2  272 ? 48.457 36.573  11.592  1.00 46.62  ?  304 ASP C O     1 
ATOM   8901  C  CB    . ASP C  2  272 ? 45.435 34.898  10.849  1.00 56.84  ?  304 ASP C CB    1 
ATOM   8902  C  CG    . ASP C  2  272 ? 45.375 34.739  12.387  1.00 58.33  ?  304 ASP C CG    1 
ATOM   8903  O  OD1   . ASP C  2  272 ? 46.231 35.276  13.106  1.00 61.91  ?  304 ASP C OD1   1 
ATOM   8904  O  OD2   . ASP C  2  272 ? 44.425 34.097  12.888  1.00 55.37  -1 304 ASP C OD2   1 
ATOM   8905  N  N     . LYS C  2  273 ? 46.795 37.779  10.772  1.00 53.03  ?  305 LYS C N     1 
ATOM   8906  C  CA    . LYS C  2  273 ? 47.443 38.950  11.321  1.00 57.60  ?  305 LYS C CA    1 
ATOM   8907  C  C     . LYS C  2  273 ? 47.455 38.900  12.860  1.00 59.48  ?  305 LYS C C     1 
ATOM   8908  O  O     . LYS C  2  273 ? 48.175 39.669  13.497  1.00 62.09  ?  305 LYS C O     1 
ATOM   8909  C  CB    . LYS C  2  273 ? 46.838 40.253  10.779  1.00 61.78  ?  305 LYS C CB    1 
ATOM   8910  C  CG    . LYS C  2  273 ? 47.881 41.358  10.487  1.00 67.45  ?  305 LYS C CG    1 
ATOM   8911  C  CD    . LYS C  2  273 ? 48.378 42.175  11.710  1.00 68.30  ?  305 LYS C CD    1 
ATOM   8912  C  CE    . LYS C  2  273 ? 49.831 41.901  12.116  1.00 66.10  ?  305 LYS C CE    1 
ATOM   8913  N  NZ    . LYS C  2  273 ? 50.855 42.396  11.144  1.00 65.91  1  305 LYS C NZ    1 
ATOM   8914  N  N     . LYS C  2  274 ? 46.688 37.987  13.459  1.00 61.96  ?  306 LYS C N     1 
ATOM   8915  C  CA    . LYS C  2  274 ? 46.772 37.750  14.917  1.00 62.83  ?  306 LYS C CA    1 
ATOM   8916  C  C     . LYS C  2  274 ? 48.060 36.990  15.332  1.00 57.80  ?  306 LYS C C     1 
ATOM   8917  O  O     . LYS C  2  274 ? 48.564 37.200  16.423  1.00 55.71  ?  306 LYS C O     1 
ATOM   8918  C  CB    . LYS C  2  274 ? 45.496 37.039  15.444  1.00 66.18  ?  306 LYS C CB    1 
ATOM   8919  C  CG    . LYS C  2  274 ? 45.129 37.301  16.920  1.00 66.45  ?  306 LYS C CG    1 
ATOM   8920  C  CD    . LYS C  2  274 ? 44.722 38.752  17.231  1.00 65.01  ?  306 LYS C CD    1 
ATOM   8921  C  CE    . LYS C  2  274 ? 45.816 39.550  17.959  1.00 63.52  ?  306 LYS C CE    1 
ATOM   8922  N  NZ    . LYS C  2  274 ? 46.009 39.166  19.395  1.00 59.49  1  306 LYS C NZ    1 
ATOM   8923  N  N     . GLY C  2  275 ? 48.594 36.129  14.466  1.00 56.32  ?  307 GLY C N     1 
ATOM   8924  C  CA    . GLY C  2  275 ? 49.879 35.442  14.723  1.00 54.45  ?  307 GLY C CA    1 
ATOM   8925  C  C     . GLY C  2  275 ? 49.825 33.921  14.792  1.00 54.95  ?  307 GLY C C     1 
ATOM   8926  O  O     . GLY C  2  275 ? 50.760 33.259  15.269  1.00 56.48  ?  307 GLY C O     1 
ATOM   8927  N  N     . SER C  2  276 ? 48.733 33.352  14.308  1.00 55.10  ?  308 SER C N     1 
ATOM   8928  C  CA    . SER C  2  276 ? 48.496 31.926  14.443  1.00 54.91  ?  308 SER C CA    1 
ATOM   8929  C  C     . SER C  2  276 ? 48.788 31.301  13.077  1.00 50.75  ?  308 SER C C     1 
ATOM   8930  O  O     . SER C  2  276 ? 48.393 31.882  12.070  1.00 49.56  ?  308 SER C O     1 
ATOM   8931  C  CB    . SER C  2  276 ? 47.029 31.694  14.872  1.00 55.38  ?  308 SER C CB    1 
ATOM   8932  O  OG    . SER C  2  276 ? 46.896 30.593  15.766  1.00 56.47  ?  308 SER C OG    1 
ATOM   8933  N  N     . PRO C  2  277 ? 49.469 30.127  13.036  1.00 46.62  ?  309 PRO C N     1 
ATOM   8934  C  CA    . PRO C  2  277 ? 49.731 29.461  11.748  1.00 43.02  ?  309 PRO C CA    1 
ATOM   8935  C  C     . PRO C  2  277 ? 48.445 29.098  11.007  1.00 39.57  ?  309 PRO C C     1 
ATOM   8936  O  O     . PRO C  2  277 ? 47.552 28.504  11.617  1.00 35.12  ?  309 PRO C O     1 
ATOM   8937  C  CB    . PRO C  2  277 ? 50.488 28.190  12.154  1.00 44.89  ?  309 PRO C CB    1 
ATOM   8938  C  CG    . PRO C  2  277 ? 50.073 27.918  13.573  1.00 47.38  ?  309 PRO C CG    1 
ATOM   8939  C  CD    . PRO C  2  277 ? 49.893 29.289  14.181  1.00 48.37  ?  309 PRO C CD    1 
ATOM   8940  N  N     . VAL C  2  278 ? 48.350 29.473  9.723   1.00 38.34  ?  310 VAL C N     1 
ATOM   8941  C  CA    . VAL C  2  278 ? 47.118 29.252  8.933   1.00 37.96  ?  310 VAL C CA    1 
ATOM   8942  C  C     . VAL C  2  278 ? 47.295 28.633  7.544   1.00 37.33  ?  310 VAL C C     1 
ATOM   8943  O  O     . VAL C  2  278 ? 46.306 28.215  6.965   1.00 37.72  ?  310 VAL C O     1 
ATOM   8944  C  CB    . VAL C  2  278 ? 46.253 30.543  8.773   1.00 38.32  ?  310 VAL C CB    1 
ATOM   8945  C  CG1   . VAL C  2  278 ? 45.743 31.028  10.118  1.00 38.80  ?  310 VAL C CG1   1 
ATOM   8946  C  CG2   . VAL C  2  278 ? 47.004 31.667  8.056   1.00 38.25  ?  310 VAL C CG2   1 
ATOM   8947  N  N     . ASN C  2  279 ? 48.514 28.572  7.001   1.00 37.20  ?  311 ASN C N     1 
ATOM   8948  C  CA    . ASN C  2  279 ? 48.722 27.999  5.651   1.00 36.48  ?  311 ASN C CA    1 
ATOM   8949  C  C     . ASN C  2  279 ? 50.148 27.502  5.480   1.00 36.39  ?  311 ASN C C     1 
ATOM   8950  O  O     . ASN C  2  279 ? 51.056 28.039  6.111   1.00 39.48  ?  311 ASN C O     1 
ATOM   8951  C  CB    . ASN C  2  279 ? 48.437 29.050  4.584   1.00 35.95  ?  311 ASN C CB    1 
ATOM   8952  C  CG    . ASN C  2  279 ? 47.821 28.458  3.360   1.00 35.55  ?  311 ASN C CG    1 
ATOM   8953  O  OD1   . ASN C  2  279 ? 48.469 27.712  2.595   1.00 35.28  ?  311 ASN C OD1   1 
ATOM   8954  N  ND2   . ASN C  2  279 ? 46.545 28.748  3.179   1.00 34.58  ?  311 ASN C ND2   1 
ATOM   8955  N  N     . SER C  2  280 ? 50.355 26.474  4.661   1.00 33.14  ?  312 SER C N     1 
ATOM   8956  C  CA    . SER C  2  280 ? 51.720 26.025  4.387   1.00 30.12  ?  312 SER C CA    1 
ATOM   8957  C  C     . SER C  2  280 ? 52.068 26.298  2.937   1.00 31.11  ?  312 SER C C     1 
ATOM   8958  O  O     . SER C  2  280 ? 51.212 26.216  2.012   1.00 29.85  ?  312 SER C O     1 
ATOM   8959  C  CB    . SER C  2  280 ? 51.923 24.550  4.708   1.00 28.61  ?  312 SER C CB    1 
ATOM   8960  O  OG    . SER C  2  280 ? 51.737 24.329  6.071   1.00 26.24  ?  312 SER C OG    1 
ATOM   8961  N  N     . LEU C  2  281 ? 53.343 26.649  2.775   1.00 31.08  ?  313 LEU C N     1 
ATOM   8962  C  CA    . LEU C  2  281 ? 53.937 27.010  1.487   1.00 30.67  ?  313 LEU C CA    1 
ATOM   8963  C  C     . LEU C  2  281 ? 55.174 26.154  1.266   1.00 29.02  ?  313 LEU C C     1 
ATOM   8964  O  O     . LEU C  2  281 ? 55.882 25.801  2.227   1.00 29.82  ?  313 LEU C O     1 
ATOM   8965  C  CB    . LEU C  2  281 ? 54.319 28.495  1.424   1.00 29.83  ?  313 LEU C CB    1 
ATOM   8966  C  CG    . LEU C  2  281 ? 53.130 29.453  1.372   1.00 29.90  ?  313 LEU C CG    1 
ATOM   8967  C  CD1   . LEU C  2  281 ? 52.573 29.675  2.762   1.00 31.18  ?  313 LEU C CD1   1 
ATOM   8968  C  CD2   . LEU C  2  281 ? 53.515 30.793  0.780   1.00 30.49  ?  313 LEU C CD2   1 
ATOM   8969  N  N     . PHE C  2  282 ? 55.405 25.823  -0.004  1.00 26.58  ?  314 PHE C N     1 
ATOM   8970  C  CA    . PHE C  2  282 ? 56.413 24.868  -0.403  1.00 25.35  ?  314 PHE C CA    1 
ATOM   8971  C  C     . PHE C  2  282 ? 57.111 25.326  -1.652  1.00 23.96  ?  314 PHE C C     1 
ATOM   8972  O  O     . PHE C  2  282 ? 56.565 25.304  -2.759  1.00 21.77  ?  314 PHE C O     1 
ATOM   8973  C  CB    . PHE C  2  282 ? 55.797 23.511  -0.653  1.00 26.12  ?  314 PHE C CB    1 
ATOM   8974  C  CG    . PHE C  2  282 ? 55.203 22.907  0.567   1.00 27.39  ?  314 PHE C CG    1 
ATOM   8975  C  CD1   . PHE C  2  282 ? 55.990 22.127  1.427   1.00 27.20  ?  314 PHE C CD1   1 
ATOM   8976  C  CD2   . PHE C  2  282 ? 53.848 23.138  0.878   1.00 28.31  ?  314 PHE C CD2   1 
ATOM   8977  C  CE1   . PHE C  2  282 ? 55.428 21.584  2.561   1.00 28.11  ?  314 PHE C CE1   1 
ATOM   8978  C  CE2   . PHE C  2  282 ? 53.284 22.608  2.021   1.00 28.30  ?  314 PHE C CE2   1 
ATOM   8979  C  CZ    . PHE C  2  282 ? 54.074 21.830  2.863   1.00 29.03  ?  314 PHE C CZ    1 
ATOM   8980  N  N     . VAL C  2  283 ? 58.343 25.743  -1.424  1.00 24.01  ?  315 VAL C N     1 
ATOM   8981  C  CA    . VAL C  2  283 ? 59.295 25.987  -2.463  1.00 24.06  ?  315 VAL C CA    1 
ATOM   8982  C  C     . VAL C  2  283 ? 60.126 24.717  -2.730  1.00 24.20  ?  315 VAL C C     1 
ATOM   8983  O  O     . VAL C  2  283 ? 60.783 24.125  -1.865  1.00 21.47  ?  315 VAL C O     1 
ATOM   8984  C  CB    . VAL C  2  283 ? 60.192 27.187  -2.141  1.00 24.04  ?  315 VAL C CB    1 
ATOM   8985  C  CG1   . VAL C  2  283 ? 61.190 27.385  -3.258  1.00 24.63  ?  315 VAL C CG1   1 
ATOM   8986  C  CG2   . VAL C  2  283 ? 59.359 28.459  -1.924  1.00 23.68  ?  315 VAL C CG2   1 
ATOM   8987  N  N     . ALA C  2  284 ? 60.049 24.332  -3.991  1.00 26.59  ?  316 ALA C N     1 
ATOM   8988  C  CA    . ALA C  2  284 ? 60.718 23.186  -4.532  1.00 28.29  ?  316 ALA C CA    1 
ATOM   8989  C  C     . ALA C  2  284 ? 62.073 23.593  -5.098  1.00 28.73  ?  316 ALA C C     1 
ATOM   8990  O  O     . ALA C  2  284 ? 62.209 24.623  -5.759  1.00 28.79  ?  316 ALA C O     1 
ATOM   8991  C  CB    . ALA C  2  284 ? 59.848 22.567  -5.637  1.00 29.15  ?  316 ALA C CB    1 
ATOM   8992  N  N     . PRO C  2  285 ? 63.085 22.768  -4.859  1.00 29.45  ?  317 PRO C N     1 
ATOM   8993  C  CA    . PRO C  2  285 ? 64.320 23.054  -5.536  1.00 29.27  ?  317 PRO C CA    1 
ATOM   8994  C  C     . PRO C  2  285 ? 64.259 22.678  -7.007  1.00 28.17  ?  317 PRO C C     1 
ATOM   8995  O  O     . PRO C  2  285 ? 63.391 21.906  -7.442  1.00 26.74  ?  317 PRO C O     1 
ATOM   8996  C  CB    . PRO C  2  285 ? 65.323 22.169  -4.803  1.00 30.11  ?  317 PRO C CB    1 
ATOM   8997  C  CG    . PRO C  2  285 ? 64.527 20.970  -4.389  1.00 30.31  ?  317 PRO C CG    1 
ATOM   8998  C  CD    . PRO C  2  285 ? 63.124 21.474  -4.152  1.00 30.16  ?  317 PRO C CD    1 
ATOM   8999  N  N     . ALA C  2  286 ? 65.234 23.217  -7.727  1.00 29.23  ?  318 ALA C N     1 
ATOM   9000  C  CA    . ALA C  2  286 ? 65.324 23.144  -9.179  1.00 30.20  ?  318 ALA C CA    1 
ATOM   9001  C  C     . ALA C  2  286 ? 65.851 21.789  -9.708  1.00 29.49  ?  318 ALA C C     1 
ATOM   9002  O  O     . ALA C  2  286 ? 66.408 20.998  -8.942  1.00 27.31  ?  318 ALA C O     1 
ATOM   9003  C  CB    . ALA C  2  286 ? 66.190 24.299  -9.688  1.00 29.92  ?  318 ALA C CB    1 
ATOM   9004  N  N     . VAL C  2  287 ? 65.611 21.542  -11.010 1.00 30.32  ?  319 VAL C N     1 
ATOM   9005  C  CA    . VAL C  2  287 ? 66.183 20.402  -11.764 1.00 31.58  ?  319 VAL C CA    1 
ATOM   9006  C  C     . VAL C  2  287 ? 67.539 20.837  -12.327 1.00 33.03  ?  319 VAL C C     1 
ATOM   9007  O  O     . VAL C  2  287 ? 68.495 20.022  -12.338 1.00 35.22  ?  319 VAL C O     1 
ATOM   9008  C  CB    . VAL C  2  287 ? 65.282 19.854  -12.941 1.00 30.58  ?  319 VAL C CB    1 
ATOM   9009  C  CG1   . VAL C  2  287 ? 65.985 18.710  -13.710 1.00 29.22  ?  319 VAL C CG1   1 
ATOM   9010  C  CG2   . VAL C  2  287 ? 63.894 19.416  -12.451 1.00 29.42  ?  319 VAL C CG2   1 
ATOM   9011  N  N     . THR C  2  288 ? 67.652 22.087  -12.792 1.00 31.65  ?  320 THR C N     1 
ATOM   9012  C  CA    . THR C  2  288 ? 68.984 22.552  -13.107 1.00 32.98  ?  320 THR C CA    1 
ATOM   9013  C  C     . THR C  2  288 ? 69.791 22.516  -11.810 1.00 36.38  ?  320 THR C C     1 
ATOM   9014  O  O     . THR C  2  288 ? 69.247 22.804  -10.748 1.00 41.37  ?  320 THR C O     1 
ATOM   9015  C  CB    . THR C  2  288 ? 69.039 23.962  -13.689 1.00 30.50  ?  320 THR C CB    1 
ATOM   9016  O  OG1   . THR C  2  288 ? 70.395 24.238  -14.089 1.00 28.66  ?  320 THR C OG1   1 
ATOM   9017  C  CG2   . THR C  2  288 ? 68.585 24.976  -12.670 1.00 29.11  ?  320 THR C CG2   1 
ATOM   9018  N  N     . PRO C  2  289 ? 71.074 22.142  -11.887 1.00 36.76  ?  321 PRO C N     1 
ATOM   9019  C  CA    . PRO C  2  289 ? 71.987 22.299  -10.770 1.00 37.38  ?  321 PRO C CA    1 
ATOM   9020  C  C     . PRO C  2  289 ? 72.834 23.593  -10.854 1.00 37.93  ?  321 PRO C C     1 
ATOM   9021  O  O     . PRO C  2  289 ? 73.752 23.784  -10.043 1.00 41.63  ?  321 PRO C O     1 
ATOM   9022  C  CB    . PRO C  2  289 ? 72.897 21.084  -10.922 1.00 38.44  ?  321 PRO C CB    1 
ATOM   9023  C  CG    . PRO C  2  289 ? 72.979 20.882  -12.405 1.00 39.19  ?  321 PRO C CG    1 
ATOM   9024  C  CD    . PRO C  2  289 ? 71.733 21.482  -13.025 1.00 37.81  ?  321 PRO C CD    1 
ATOM   9025  N  N     . VAL C  2  290 ? 72.529 24.470  -11.806 1.00 35.00  ?  322 VAL C N     1 
ATOM   9026  C  CA    . VAL C  2  290 ? 73.428 25.560  -12.165 1.00 33.95  ?  322 VAL C CA    1 
ATOM   9027  C  C     . VAL C  2  290 ? 73.689 26.579  -11.021 1.00 31.27  ?  322 VAL C C     1 
ATOM   9028  O  O     . VAL C  2  290 ? 72.887 26.736  -10.113 1.00 33.46  ?  322 VAL C O     1 
ATOM   9029  C  CB    . VAL C  2  290 ? 72.874 26.251  -13.434 1.00 36.76  ?  322 VAL C CB    1 
ATOM   9030  C  CG1   . VAL C  2  290 ? 71.701 27.159  -13.086 1.00 38.53  ?  322 VAL C CG1   1 
ATOM   9031  C  CG2   . VAL C  2  290 ? 73.957 27.012  -14.184 1.00 37.59  ?  322 VAL C CG2   1 
ATOM   9032  N  N     . LYS C  2  291 ? 74.825 27.261  -11.060 1.00 28.35  ?  323 LYS C N     1 
ATOM   9033  C  CA    . LYS C  2  291 ? 75.154 28.265  -10.065 1.00 27.55  ?  323 LYS C CA    1 
ATOM   9034  C  C     . LYS C  2  291 ? 76.243 29.180  -10.581 1.00 27.26  ?  323 LYS C C     1 
ATOM   9035  O  O     . LYS C  2  291 ? 76.737 28.999  -11.715 1.00 28.80  ?  323 LYS C O     1 
ATOM   9036  C  CB    . LYS C  2  291 ? 75.608 27.605  -8.784  1.00 29.06  ?  323 LYS C CB    1 
ATOM   9037  C  CG    . LYS C  2  291 ? 76.807 26.705  -8.952  1.00 30.90  ?  323 LYS C CG    1 
ATOM   9038  C  CD    . LYS C  2  291 ? 77.734 26.722  -7.756  1.00 31.45  ?  323 LYS C CD    1 
ATOM   9039  C  CE    . LYS C  2  291 ? 79.006 25.984  -8.106  1.00 32.15  ?  323 LYS C CE    1 
ATOM   9040  N  NZ    . LYS C  2  291 ? 80.179 26.845  -7.833  1.00 32.80  1  323 LYS C NZ    1 
ATOM   9041  N  N     . SER C  2  292 ? 76.594 30.185  -9.785  1.00 25.99  ?  324 SER C N     1 
ATOM   9042  C  CA    A SER C  2  292 ? 77.674 31.102  -10.151 0.50 26.52  ?  324 SER C CA    1 
ATOM   9043  C  CA    B SER C  2  292 ? 77.660 31.093  -10.162 0.50 26.35  ?  324 SER C CA    1 
ATOM   9044  C  C     . SER C  2  292 ? 79.026 30.449  -9.930  1.00 26.89  ?  324 SER C C     1 
ATOM   9045  O  O     . SER C  2  292 ? 79.160 29.427  -9.228  1.00 24.38  ?  324 SER C O     1 
ATOM   9046  C  CB    A SER C  2  292 ? 77.646 32.390  -9.319  0.50 27.07  ?  324 SER C CB    1 
ATOM   9047  C  CB    B SER C  2  292 ? 77.554 32.389  -9.362  0.50 26.71  ?  324 SER C CB    1 
ATOM   9048  O  OG    A SER C  2  292 ? 76.571 33.242  -9.650  0.50 27.67  ?  324 SER C OG    1 
ATOM   9049  O  OG    B SER C  2  292 ? 78.535 33.327  -9.758  0.50 26.90  ?  324 SER C OG    1 
ATOM   9050  N  N     . VAL C  2  293 ? 80.043 31.063  -10.512 1.00 28.67  ?  325 VAL C N     1 
ATOM   9051  C  CA    . VAL C  2  293 ? 81.393 30.621  -10.279 1.00 29.75  ?  325 VAL C CA    1 
ATOM   9052  C  C     . VAL C  2  293 ? 81.789 30.937  -8.841  1.00 32.18  ?  325 VAL C C     1 
ATOM   9053  O  O     . VAL C  2  293 ? 82.521 30.148  -8.222  1.00 31.90  ?  325 VAL C O     1 
ATOM   9054  C  CB    . VAL C  2  293 ? 82.357 31.323  -11.216 1.00 28.40  ?  325 VAL C CB    1 
ATOM   9055  C  CG1   . VAL C  2  293 ? 83.777 30.872  -10.904 1.00 29.02  ?  325 VAL C CG1   1 
ATOM   9056  C  CG2   . VAL C  2  293 ? 81.983 30.989  -12.641 1.00 28.98  ?  325 VAL C CG2   1 
ATOM   9057  N  N     . LEU C  2  294 ? 81.313 32.097  -8.341  1.00 33.14  ?  326 LEU C N     1 
ATOM   9058  C  CA    . LEU C  2  294 ? 81.661 32.636  -7.003  1.00 33.05  ?  326 LEU C CA    1 
ATOM   9059  C  C     . LEU C  2  294 ? 80.865 31.981  -5.850  1.00 36.85  ?  326 LEU C C     1 
ATOM   9060  O  O     . LEU C  2  294 ? 81.168 32.227  -4.662  1.00 39.83  ?  326 LEU C O     1 
ATOM   9061  C  CB    . LEU C  2  294 ? 81.503 34.181  -6.964  1.00 29.89  ?  326 LEU C CB    1 
ATOM   9062  C  CG    . LEU C  2  294 ? 82.453 34.966  -7.896  1.00 29.84  ?  326 LEU C CG    1 
ATOM   9063  C  CD1   . LEU C  2  294 ? 82.291 36.473  -7.771  1.00 29.90  ?  326 LEU C CD1   1 
ATOM   9064  C  CD2   . LEU C  2  294 ? 83.920 34.601  -7.677  1.00 28.64  ?  326 LEU C CD2   1 
ATOM   9065  N  N     . GLU C  2  295 ? 79.872 31.147  -6.188  1.00 36.37  ?  327 GLU C N     1 
ATOM   9066  C  CA    . GLU C  2  295 ? 79.030 30.490  -5.189  1.00 37.22  ?  327 GLU C CA    1 
ATOM   9067  C  C     . GLU C  2  295 ? 79.557 29.068  -4.833  1.00 39.83  ?  327 GLU C C     1 
ATOM   9068  O  O     . GLU C  2  295 ? 79.702 28.204  -5.701  1.00 41.21  ?  327 GLU C O     1 
ATOM   9069  C  CB    . GLU C  2  295 ? 77.581 30.423  -5.709  1.00 38.26  ?  327 GLU C CB    1 
ATOM   9070  C  CG    . GLU C  2  295 ? 76.823 31.750  -5.735  1.00 39.34  ?  327 GLU C CG    1 
ATOM   9071  C  CD    . GLU C  2  295 ? 75.619 31.751  -6.673  1.00 41.92  ?  327 GLU C CD    1 
ATOM   9072  O  OE1   . GLU C  2  295 ? 75.117 32.838  -7.041  1.00 46.11  ?  327 GLU C OE1   1 
ATOM   9073  O  OE2   . GLU C  2  295 ? 75.177 30.668  -7.081  1.00 44.70  -1 327 GLU C OE2   1 
ATOM   9074  N  N     . LYS C  2  296 ? 79.844 28.818  -3.559  1.00 41.28  ?  328 LYS C N     1 
ATOM   9075  C  CA    . LYS C  2  296 ? 80.268 27.483  -3.117  1.00 41.84  ?  328 LYS C CA    1 
ATOM   9076  C  C     . LYS C  2  296 ? 79.182 26.444  -3.350  1.00 40.07  ?  328 LYS C C     1 
ATOM   9077  O  O     . LYS C  2  296 ? 79.417 25.363  -3.868  1.00 38.58  ?  328 LYS C O     1 
ATOM   9078  C  CB    . LYS C  2  296 ? 80.578 27.555  -1.625  1.00 47.61  ?  328 LYS C CB    1 
ATOM   9079  C  CG    . LYS C  2  296 ? 81.107 26.268  -1.019  1.00 51.58  ?  328 LYS C CG    1 
ATOM   9080  C  CD    . LYS C  2  296 ? 82.191 26.557  0.011   1.00 55.47  ?  328 LYS C CD    1 
ATOM   9081  C  CE    . LYS C  2  296 ? 82.826 25.278  0.537   1.00 58.40  ?  328 LYS C CE    1 
ATOM   9082  N  NZ    . LYS C  2  296 ? 83.515 24.483  -0.526  1.00 58.41  1  328 LYS C NZ    1 
ATOM   9083  N  N     . GLN C  2  297 ? 77.976 26.832  -2.972  1.00 41.36  ?  329 GLN C N     1 
ATOM   9084  C  CA    . GLN C  2  297 ? 76.842 25.959  -2.892  1.00 40.77  ?  329 GLN C CA    1 
ATOM   9085  C  C     . GLN C  2  297 ? 75.976 26.033  -4.128  1.00 40.23  ?  329 GLN C C     1 
ATOM   9086  O  O     . GLN C  2  297 ? 75.949 27.034  -4.852  1.00 36.67  ?  329 GLN C O     1 
ATOM   9087  C  CB    . GLN C  2  297 ? 76.005 26.374  -1.682  1.00 43.75  ?  329 GLN C CB    1 
ATOM   9088  C  CG    . GLN C  2  297 ? 76.689 26.044  -0.372  1.00 46.76  ?  329 GLN C CG    1 
ATOM   9089  C  CD    . GLN C  2  297 ? 77.082 24.575  -0.332  1.00 51.93  ?  329 GLN C CD    1 
ATOM   9090  O  OE1   . GLN C  2  297 ? 78.262 24.220  -0.257  1.00 54.51  ?  329 GLN C OE1   1 
ATOM   9091  N  NE2   . GLN C  2  297 ? 76.084 23.705  -0.425  1.00 56.60  ?  329 GLN C NE2   1 
ATOM   9092  N  N     . THR C  2  298 ? 75.264 24.937  -4.350  1.00 40.17  ?  330 THR C N     1 
ATOM   9093  C  CA    . THR C  2  298 ? 74.187 24.869  -5.325  1.00 36.89  ?  330 THR C CA    1 
ATOM   9094  C  C     . THR C  2  298 ? 73.213 23.783  -4.816  1.00 35.25  ?  330 THR C C     1 
ATOM   9095  O  O     . THR C  2  298 ? 73.355 23.296  -3.693  1.00 34.54  ?  330 THR C O     1 
ATOM   9096  C  CB    . THR C  2  298 ? 74.738 24.644  -6.779  1.00 34.20  ?  330 THR C CB    1 
ATOM   9097  O  OG1   . THR C  2  298 ? 73.689 24.794  -7.747  1.00 32.98  ?  330 THR C OG1   1 
ATOM   9098  C  CG2   . THR C  2  298 ? 75.370 23.301  -6.933  1.00 32.73  ?  330 THR C CG2   1 
ATOM   9099  N  N     . ASN C  2  299 ? 72.213 23.452  -5.622  1.00 35.01  ?  331 ASN C N     1 
ATOM   9100  C  CA    . ASN C  2  299 ? 71.343 22.302  -5.377  1.00 35.27  ?  331 ASN C CA    1 
ATOM   9101  C  C     . ASN C  2  299 ? 71.682 21.164  -6.343  1.00 37.09  ?  331 ASN C C     1 
ATOM   9102  O  O     . ASN C  2  299 ? 72.129 21.423  -7.465  1.00 38.87  ?  331 ASN C O     1 
ATOM   9103  C  CB    . ASN C  2  299 ? 69.907 22.673  -5.672  1.00 35.60  ?  331 ASN C CB    1 
ATOM   9104  C  CG    . ASN C  2  299 ? 69.713 23.018  -7.144  1.00 34.29  ?  331 ASN C CG    1 
ATOM   9105  O  OD1   . ASN C  2  299 ? 70.335 23.978  -7.627  1.00 34.79  ?  331 ASN C OD1   1 
ATOM   9106  N  ND2   . ASN C  2  299 ? 68.922 22.212  -7.876  1.00 30.24  ?  331 ASN C ND2   1 
ATOM   9107  N  N     . ASN C  2  300 ? 71.462 19.917  -5.907  1.00 37.83  ?  332 ASN C N     1 
ATOM   9108  C  CA    . ASN C  2  300 ? 71.362 18.742  -6.809  1.00 37.27  ?  332 ASN C CA    1 
ATOM   9109  C  C     . ASN C  2  300 ? 70.035 18.711  -7.543  1.00 38.13  ?  332 ASN C C     1 
ATOM   9110  O  O     . ASN C  2  300 ? 69.029 19.229  -7.048  1.00 37.24  ?  332 ASN C O     1 
ATOM   9111  C  CB    . ASN C  2  300 ? 71.444 17.402  -6.062  1.00 34.98  ?  332 ASN C CB    1 
ATOM   9112  C  CG    . ASN C  2  300 ? 72.858 16.995  -5.710  1.00 33.72  ?  332 ASN C CG    1 
ATOM   9113  O  OD1   . ASN C  2  300 ? 73.124 16.646  -4.570  1.00 32.99  ?  332 ASN C OD1   1 
ATOM   9114  N  ND2   . ASN C  2  300 ? 73.764 17.028  -6.675  1.00 33.69  ?  332 ASN C ND2   1 
ATOM   9115  N  N     . PRO C  2  301 ? 70.017 18.075  -8.723  1.00 38.30  ?  333 PRO C N     1 
ATOM   9116  C  CA    . PRO C  2  301 ? 68.723 17.990  -9.374  1.00 36.98  ?  333 PRO C CA    1 
ATOM   9117  C  C     . PRO C  2  301 ? 67.703 17.278  -8.488  1.00 33.40  ?  333 PRO C C     1 
ATOM   9118  O  O     . PRO C  2  301 ? 68.053 16.397  -7.713  1.00 29.74  ?  333 PRO C O     1 
ATOM   9119  C  CB    . PRO C  2  301 ? 69.045 17.249  -10.681 1.00 39.15  ?  333 PRO C CB    1 
ATOM   9120  C  CG    . PRO C  2  301 ? 70.451 17.674  -10.988 1.00 38.71  ?  333 PRO C CG    1 
ATOM   9121  C  CD    . PRO C  2  301 ? 71.123 17.740  -9.642  1.00 37.88  ?  333 PRO C CD    1 
ATOM   9122  N  N     . GLY C  2  302 ? 66.455 17.696  -8.608  1.00 33.62  ?  334 GLY C N     1 
ATOM   9123  C  CA    . GLY C  2  302 ? 65.421 17.304  -7.675  1.00 36.37  ?  334 GLY C CA    1 
ATOM   9124  C  C     . GLY C  2  302 ? 63.983 17.407  -8.197  1.00 38.63  ?  334 GLY C C     1 
ATOM   9125  O  O     . GLY C  2  302 ? 63.592 18.357  -8.902  1.00 36.19  ?  334 GLY C O     1 
ATOM   9126  N  N     . ILE C  2  303 ? 63.196 16.431  -7.752  1.00 40.32  ?  335 ILE C N     1 
ATOM   9127  C  CA    . ILE C  2  303 ? 61.857 16.118  -8.219  1.00 39.77  ?  335 ILE C CA    1 
ATOM   9128  C  C     . ILE C  2  303 ? 61.074 15.781  -6.972  1.00 39.56  ?  335 ILE C C     1 
ATOM   9129  O  O     . ILE C  2  303 ? 61.599 15.067  -6.106  1.00 39.05  ?  335 ILE C O     1 
ATOM   9130  C  CB    . ILE C  2  303 ? 61.939 14.844  -9.076  1.00 41.41  ?  335 ILE C CB    1 
ATOM   9131  C  CG1   . ILE C  2  303 ? 62.463 15.197  -10.453 1.00 44.75  ?  335 ILE C CG1   1 
ATOM   9132  C  CG2   . ILE C  2  303 ? 60.614 14.106  -9.139  1.00 41.64  ?  335 ILE C CG2   1 
ATOM   9133  C  CD1   . ILE C  2  303 ? 61.766 16.388  -11.090 1.00 47.74  ?  335 ILE C CD1   1 
ATOM   9134  N  N     . ARG C  2  304 ? 59.842 16.269  -6.848  1.00 37.04  ?  336 ARG C N     1 
ATOM   9135  C  CA    . ARG C  2  304 ? 59.071 15.963  -5.637  1.00 36.48  ?  336 ARG C CA    1 
ATOM   9136  C  C     . ARG C  2  304 ? 57.627 15.580  -5.945  1.00 38.44  ?  336 ARG C C     1 
ATOM   9137  O  O     . ARG C  2  304 ? 57.114 15.838  -7.030  1.00 40.78  ?  336 ARG C O     1 
ATOM   9138  C  CB    . ARG C  2  304 ? 59.174 17.085  -4.541  1.00 33.77  ?  336 ARG C CB    1 
ATOM   9139  C  CG    . ARG C  2  304 ? 58.415 18.378  -4.833  1.00 31.55  ?  336 ARG C CG    1 
ATOM   9140  C  CD    . ARG C  2  304 ? 58.233 19.288  -3.636  1.00 28.35  ?  336 ARG C CD    1 
ATOM   9141  N  NE    . ARG C  2  304 ? 59.487 19.635  -2.987  1.00 26.39  ?  336 ARG C NE    1 
ATOM   9142  C  CZ    . ARG C  2  304 ? 59.686 20.708  -2.221  1.00 25.15  ?  336 ARG C CZ    1 
ATOM   9143  N  NH1   . ARG C  2  304 ? 58.720 21.600  -2.020  1.00 25.43  1  336 ARG C NH1   1 
ATOM   9144  N  NH2   . ARG C  2  304 ? 60.882 20.908  -1.672  1.00 23.87  ?  336 ARG C NH2   1 
ATOM   9145  N  N     . LEU C  2  305 ? 57.007 14.966  -4.937  1.00 39.27  ?  337 LEU C N     1 
ATOM   9146  C  CA    . LEU C  2  305 ? 55.743 14.299  -5.017  1.00 37.45  ?  337 LEU C CA    1 
ATOM   9147  C  C     . LEU C  2  305 ? 55.002 14.579  -3.721  1.00 38.75  ?  337 LEU C C     1 
ATOM   9148  O  O     . LEU C  2  305 ? 55.392 14.078  -2.640  1.00 38.06  ?  337 LEU C O     1 
ATOM   9149  C  CB    . LEU C  2  305 ? 56.020 12.813  -5.129  1.00 39.88  ?  337 LEU C CB    1 
ATOM   9150  C  CG    . LEU C  2  305 ? 54.852 11.834  -5.110  1.00 43.84  ?  337 LEU C CG    1 
ATOM   9151  C  CD1   . LEU C  2  305 ? 54.016 11.988  -6.375  1.00 46.43  ?  337 LEU C CD1   1 
ATOM   9152  C  CD2   . LEU C  2  305 ? 55.354 10.405  -4.970  1.00 45.09  ?  337 LEU C CD2   1 
ATOM   9153  N  N     . PHE C  2  306 ? 53.952 15.398  -3.827  1.00 39.52  ?  338 PHE C N     1 
ATOM   9154  C  CA    . PHE C  2  306 ? 53.020 15.660  -2.710  1.00 37.69  ?  338 PHE C CA    1 
ATOM   9155  C  C     . PHE C  2  306 ? 51.943 14.597  -2.549  1.00 42.06  ?  338 PHE C C     1 
ATOM   9156  O  O     . PHE C  2  306 ? 51.528 13.958  -3.511  1.00 47.05  ?  338 PHE C O     1 
ATOM   9157  C  CB    . PHE C  2  306 ? 52.325 16.980  -2.931  1.00 33.85  ?  338 PHE C CB    1 
ATOM   9158  C  CG    . PHE C  2  306 ? 53.178 18.145  -2.596  1.00 31.93  ?  338 PHE C CG    1 
ATOM   9159  C  CD1   . PHE C  2  306 ? 53.379 18.497  -1.288  1.00 30.39  ?  338 PHE C CD1   1 
ATOM   9160  C  CD2   . PHE C  2  306 ? 53.802 18.872  -3.580  1.00 29.83  ?  338 PHE C CD2   1 
ATOM   9161  C  CE1   . PHE C  2  306 ? 54.149 19.586  -0.974  1.00 29.52  ?  338 PHE C CE1   1 
ATOM   9162  C  CE2   . PHE C  2  306 ? 54.579 19.961  -3.269  1.00 27.78  ?  338 PHE C CE2   1 
ATOM   9163  C  CZ    . PHE C  2  306 ? 54.750 20.318  -1.972  1.00 27.94  ?  338 PHE C CZ    1 
ATOM   9164  N  N     . GLN C  2  307 ? 51.477 14.418  -1.323  1.00 45.72  ?  339 GLN C N     1 
ATOM   9165  C  CA    . GLN C  2  307 ? 50.396 13.481  -1.040  1.00 44.29  ?  339 GLN C CA    1 
ATOM   9166  C  C     . GLN C  2  307 ? 49.228 14.221  -0.466  1.00 47.10  ?  339 GLN C C     1 
ATOM   9167  O  O     . GLN C  2  307 ? 49.398 15.185  0.289   1.00 52.30  ?  339 GLN C O     1 
ATOM   9168  C  CB    . GLN C  2  307 ? 50.839 12.446  -0.029  1.00 41.83  ?  339 GLN C CB    1 
ATOM   9169  C  CG    . GLN C  2  307 ? 51.895 11.514  -0.566  1.00 41.23  ?  339 GLN C CG    1 
ATOM   9170  C  CD    . GLN C  2  307 ? 52.120 10.355  0.357   1.00 41.29  ?  339 GLN C CD    1 
ATOM   9171  O  OE1   . GLN C  2  307 ? 51.782 10.420  1.548   1.00 44.19  ?  339 GLN C OE1   1 
ATOM   9172  N  NE2   . GLN C  2  307 ? 52.684 9.282   -0.174  1.00 40.66  ?  339 GLN C NE2   1 
ATOM   9173  N  N     . TYR C  2  308 ? 48.032 13.756  -0.779  1.00 47.71  ?  340 TYR C N     1 
ATOM   9174  C  CA    . TYR C  2  308 ? 46.873 14.349  -0.167  1.00 46.85  ?  340 TYR C CA    1 
ATOM   9175  C  C     . TYR C  2  308 ? 45.750 13.389  0.171   1.00 47.25  ?  340 TYR C C     1 
ATOM   9176  O  O     . TYR C  2  308 ? 45.772 12.191  -0.164  1.00 42.85  ?  340 TYR C O     1 
ATOM   9177  C  CB    . TYR C  2  308 ? 46.360 15.478  -1.040  1.00 48.68  ?  340 TYR C CB    1 
ATOM   9178  C  CG    . TYR C  2  308 ? 45.931 15.084  -2.445  1.00 50.00  ?  340 TYR C CG    1 
ATOM   9179  C  CD1   . TYR C  2  308 ? 46.872 14.894  -3.447  1.00 50.87  ?  340 TYR C CD1   1 
ATOM   9180  C  CD2   . TYR C  2  308 ? 44.572 14.970  -2.786  1.00 48.72  ?  340 TYR C CD2   1 
ATOM   9181  C  CE1   . TYR C  2  308 ? 46.482 14.581  -4.747  1.00 52.06  ?  340 TYR C CE1   1 
ATOM   9182  C  CE2   . TYR C  2  308 ? 44.175 14.660  -4.079  1.00 47.49  ?  340 TYR C CE2   1 
ATOM   9183  C  CZ    . TYR C  2  308 ? 45.134 14.467  -5.062  1.00 49.43  ?  340 TYR C CZ    1 
ATOM   9184  O  OH    . TYR C  2  308 ? 44.780 14.160  -6.365  1.00 47.10  ?  340 TYR C OH    1 
ATOM   9185  N  N     . ASP C  2  309 ? 44.801 13.967  0.904   1.00 49.93  ?  341 ASP C N     1 
ATOM   9186  C  CA    . ASP C  2  309 ? 43.543 13.358  1.283   1.00 49.39  ?  341 ASP C CA    1 
ATOM   9187  C  C     . ASP C  2  309 ? 42.463 13.847  0.318   1.00 44.93  ?  341 ASP C C     1 
ATOM   9188  O  O     . ASP C  2  309 ? 42.088 15.034  0.337   1.00 44.03  ?  341 ASP C O     1 
ATOM   9189  C  CB    . ASP C  2  309 ? 43.194 13.792  2.703   1.00 53.83  ?  341 ASP C CB    1 
ATOM   9190  C  CG    . ASP C  2  309 ? 42.107 12.958  3.312   1.00 58.85  ?  341 ASP C CG    1 
ATOM   9191  O  OD1   . ASP C  2  309 ? 41.733 11.937  2.677   1.00 64.89  ?  341 ASP C OD1   1 
ATOM   9192  O  OD2   . ASP C  2  309 ? 41.648 13.320  4.429   1.00 60.67  -1 341 ASP C OD2   1 
ATOM   9193  N  N     . PRO C  2  310 ? 41.944 12.942  -0.517  1.00 39.85  ?  342 PRO C N     1 
ATOM   9194  C  CA    . PRO C  2  310 ? 41.055 13.344  -1.595  1.00 40.13  ?  342 PRO C CA    1 
ATOM   9195  C  C     . PRO C  2  310 ? 39.754 14.025  -1.178  1.00 40.73  ?  342 PRO C C     1 
ATOM   9196  O  O     . PRO C  2  310 ? 38.989 14.438  -2.049  1.00 45.32  ?  342 PRO C O     1 
ATOM   9197  C  CB    . PRO C  2  310 ? 40.757 12.030  -2.297  1.00 40.04  ?  342 PRO C CB    1 
ATOM   9198  C  CG    . PRO C  2  310 ? 41.943 11.184  -2.020  1.00 39.53  ?  342 PRO C CG    1 
ATOM   9199  C  CD    . PRO C  2  310 ? 42.309 11.524  -0.615  1.00 39.86  ?  342 PRO C CD    1 
ATOM   9200  N  N     . ARG C  2  311 ? 39.518 14.158  0.121   1.00 40.48  ?  343 ARG C N     1 
ATOM   9201  C  CA    . ARG C  2  311 ? 38.282 14.719  0.647   1.00 41.19  ?  343 ARG C CA    1 
ATOM   9202  C  C     . ARG C  2  311 ? 38.374 16.218  0.846   1.00 38.76  ?  343 ARG C C     1 
ATOM   9203  O  O     . ARG C  2  311 ? 37.635 16.971  0.234   1.00 37.61  ?  343 ARG C O     1 
ATOM   9204  C  CB    . ARG C  2  311 ? 37.927 14.016  1.966   1.00 44.79  ?  343 ARG C CB    1 
ATOM   9205  C  CG    . ARG C  2  311 ? 37.719 12.509  1.783   1.00 49.38  ?  343 ARG C CG    1 
ATOM   9206  C  CD    . ARG C  2  311 ? 37.514 11.763  3.091   1.00 52.08  ?  343 ARG C CD    1 
ATOM   9207  N  NE    . ARG C  2  311 ? 38.764 11.297  3.689   1.00 52.78  ?  343 ARG C NE    1 
ATOM   9208  C  CZ    . ARG C  2  311 ? 38.949 11.100  4.993   1.00 54.68  ?  343 ARG C CZ    1 
ATOM   9209  N  NH1   . ARG C  2  311 ? 37.973 11.330  5.859   1.00 54.96  1  343 ARG C NH1   1 
ATOM   9210  N  NH2   . ARG C  2  311 ? 40.128 10.679  5.441   1.00 57.90  ?  343 ARG C NH2   1 
ATOM   9211  N  N     . ASP C  2  312 ? 39.285 16.643  1.707   1.00 39.52  ?  344 ASP C N     1 
ATOM   9212  C  CA    . ASP C  2  312 ? 39.501 18.074  1.981   1.00 41.10  ?  344 ASP C CA    1 
ATOM   9213  C  C     . ASP C  2  312 ? 40.752 18.620  1.257   1.00 41.05  ?  344 ASP C C     1 
ATOM   9214  O  O     . ASP C  2  312 ? 41.013 19.828  1.325   1.00 38.15  ?  344 ASP C O     1 
ATOM   9215  C  CB    . ASP C  2  312 ? 39.564 18.380  3.510   1.00 41.14  ?  344 ASP C CB    1 
ATOM   9216  C  CG    . ASP C  2  312 ? 40.378 17.320  4.342   1.00 40.73  ?  344 ASP C CG    1 
ATOM   9217  O  OD1   . ASP C  2  312 ? 41.117 16.492  3.755   1.00 41.82  ?  344 ASP C OD1   1 
ATOM   9218  O  OD2   . ASP C  2  312 ? 40.268 17.305  5.593   1.00 36.04  -1 344 ASP C OD2   1 
ATOM   9219  N  N     . TYR C  2  313 ? 41.491 17.730  0.569   1.00 40.42  ?  345 TYR C N     1 
ATOM   9220  C  CA    . TYR C  2  313 ? 42.748 18.063  -0.155  1.00 42.51  ?  345 TYR C CA    1 
ATOM   9221  C  C     . TYR C  2  313 ? 43.865 18.548  0.787   1.00 48.15  ?  345 TYR C C     1 
ATOM   9222  O  O     . TYR C  2  313 ? 44.789 19.266  0.375   1.00 48.24  ?  345 TYR C O     1 
ATOM   9223  C  CB    . TYR C  2  313 ? 42.493 19.030  -1.347  1.00 40.58  ?  345 TYR C CB    1 
ATOM   9224  C  CG    . TYR C  2  313 ? 41.522 18.399  -2.284  1.00 37.13  ?  345 TYR C CG    1 
ATOM   9225  C  CD1   . TYR C  2  313 ? 41.928 17.373  -3.118  1.00 36.30  ?  345 TYR C CD1   1 
ATOM   9226  C  CD2   . TYR C  2  313 ? 40.184 18.729  -2.244  1.00 35.50  ?  345 TYR C CD2   1 
ATOM   9227  C  CE1   . TYR C  2  313 ? 41.034 16.724  -3.926  1.00 36.23  ?  345 TYR C CE1   1 
ATOM   9228  C  CE2   . TYR C  2  313 ? 39.275 18.080  -3.037  1.00 35.40  ?  345 TYR C CE2   1 
ATOM   9229  C  CZ    . TYR C  2  313 ? 39.711 17.078  -3.874  1.00 36.61  ?  345 TYR C CZ    1 
ATOM   9230  O  OH    . TYR C  2  313 ? 38.824 16.422  -4.674  1.00 38.53  ?  345 TYR C OH    1 
ATOM   9231  N  N     . LYS C  2  314 ? 43.761 18.118  2.048   1.00 51.50  ?  346 LYS C N     1 
ATOM   9232  C  CA    . LYS C  2  314 ? 44.775 18.327  3.078   1.00 54.88  ?  346 LYS C CA    1 
ATOM   9233  C  C     . LYS C  2  314 ? 46.078 17.593  2.680   1.00 50.67  ?  346 LYS C C     1 
ATOM   9234  O  O     . LYS C  2  314 ? 46.041 16.527  2.057   1.00 48.17  ?  346 LYS C O     1 
ATOM   9235  C  CB    . LYS C  2  314 ? 44.196 17.849  4.433   1.00 64.69  ?  346 LYS C CB    1 
ATOM   9236  C  CG    . LYS C  2  314 ? 45.126 17.799  5.650   1.00 73.78  ?  346 LYS C CG    1 
ATOM   9237  C  CD    . LYS C  2  314 ? 44.326 17.682  6.962   1.00 76.99  ?  346 LYS C CD    1 
ATOM   9238  C  CE    . LYS C  2  314 ? 45.036 16.823  8.008   1.00 81.01  ?  346 LYS C CE    1 
ATOM   9239  N  NZ    . LYS C  2  314 ? 44.883 15.360  7.724   1.00 83.37  1  346 LYS C NZ    1 
ATOM   9240  N  N     . LEU C  2  315 ? 47.223 18.196  3.012   1.00 47.32  ?  347 LEU C N     1 
ATOM   9241  C  CA    . LEU C  2  315 ? 48.536 17.685  2.591   1.00 43.08  ?  347 LEU C CA    1 
ATOM   9242  C  C     . LEU C  2  315 ? 49.137 16.756  3.615   1.00 39.98  ?  347 LEU C C     1 
ATOM   9243  O  O     . LEU C  2  315 ? 49.472 17.179  4.706   1.00 38.34  ?  347 LEU C O     1 
ATOM   9244  C  CB    . LEU C  2  315 ? 49.495 18.842  2.322   1.00 40.86  ?  347 LEU C CB    1 
ATOM   9245  C  CG    . LEU C  2  315 ? 49.210 19.518  0.986   1.00 38.60  ?  347 LEU C CG    1 
ATOM   9246  C  CD1   . LEU C  2  315 ? 50.113 20.734  0.779   1.00 36.89  ?  347 LEU C CD1   1 
ATOM   9247  C  CD2   . LEU C  2  315 ? 49.340 18.492  -0.146  1.00 38.05  ?  347 LEU C CD2   1 
ATOM   9248  N  N     . LEU C  2  316 ? 49.279 15.489  3.249   1.00 39.46  ?  348 LEU C N     1 
ATOM   9249  C  CA    . LEU C  2  316 ? 49.638 14.454  4.219   1.00 41.34  ?  348 LEU C CA    1 
ATOM   9250  C  C     . LEU C  2  316 ? 51.149 14.315  4.310   1.00 40.18  ?  348 LEU C C     1 
ATOM   9251  O  O     . LEU C  2  316 ? 51.725 14.198  5.410   1.00 37.09  ?  348 LEU C O     1 
ATOM   9252  C  CB    . LEU C  2  316 ? 48.963 13.114  3.864   1.00 41.51  ?  348 LEU C CB    1 
ATOM   9253  C  CG    . LEU C  2  316 ? 47.420 13.205  3.895   1.00 41.78  ?  348 LEU C CG    1 
ATOM   9254  C  CD1   . LEU C  2  316 ? 46.800 11.879  3.493   1.00 41.96  ?  348 LEU C CD1   1 
ATOM   9255  C  CD2   . LEU C  2  316 ? 46.870 13.673  5.240   1.00 41.32  ?  348 LEU C CD2   1 
ATOM   9256  N  N     . ASP C  2  317 ? 51.794 14.364  3.154   1.00 37.82  ?  349 ASP C N     1 
ATOM   9257  C  CA    . ASP C  2  317 ? 53.227 14.310  3.140   1.00 34.52  ?  349 ASP C CA    1 
ATOM   9258  C  C     . ASP C  2  317 ? 53.769 14.831  1.817   1.00 33.12  ?  349 ASP C C     1 
ATOM   9259  O  O     . ASP C  2  317 ? 53.028 15.196  0.908   1.00 31.57  ?  349 ASP C O     1 
ATOM   9260  C  CB    . ASP C  2  317 ? 53.674 12.868  3.407   1.00 33.40  ?  349 ASP C CB    1 
ATOM   9261  C  CG    . ASP C  2  317 ? 54.980 12.774  4.212   1.00 32.19  ?  349 ASP C CG    1 
ATOM   9262  O  OD1   . ASP C  2  317 ? 55.753 13.742  4.305   1.00 30.14  ?  349 ASP C OD1   1 
ATOM   9263  O  OD2   . ASP C  2  317 ? 55.248 11.687  4.738   1.00 31.83  -1 349 ASP C OD2   1 
ATOM   9264  N  N     . MET C  2  318 ? 55.087 14.904  1.764   1.00 33.94  ?  350 MET C N     1 
ATOM   9265  C  CA    . MET C  2  318 ? 55.821 15.273  0.583   1.00 33.59  ?  350 MET C CA    1 
ATOM   9266  C  C     . MET C  2  318 ? 57.114 14.457  0.580   1.00 32.85  ?  350 MET C C     1 
ATOM   9267  O  O     . MET C  2  318 ? 57.867 14.435  1.572   1.00 30.77  ?  350 MET C O     1 
ATOM   9268  C  CB    . MET C  2  318 ? 56.103 16.779  0.617   1.00 34.19  ?  350 MET C CB    1 
ATOM   9269  C  CG    . MET C  2  318 ? 56.826 17.288  -0.607  1.00 34.55  ?  350 MET C CG    1 
ATOM   9270  S  SD    . MET C  2  318 ? 58.537 17.580  -0.216  1.00 34.11  ?  350 MET C SD    1 
ATOM   9271  C  CE    . MET C  2  318 ? 58.306 19.276  0.338   1.00 33.78  ?  350 MET C CE    1 
ATOM   9272  N  N     . LEU C  2  319 ? 57.340 13.758  -0.527  1.00 33.02  ?  351 LEU C N     1 
ATOM   9273  C  CA    . LEU C  2  319 ? 58.530 12.934  -0.697  1.00 33.85  ?  351 LEU C CA    1 
ATOM   9274  C  C     . LEU C  2  319 ? 59.463 13.584  -1.721  1.00 35.60  ?  351 LEU C C     1 
ATOM   9275  O  O     . LEU C  2  319 ? 59.079 13.723  -2.884  1.00 35.11  ?  351 LEU C O     1 
ATOM   9276  C  CB    . LEU C  2  319 ? 58.152 11.561  -1.228  1.00 33.78  ?  351 LEU C CB    1 
ATOM   9277  C  CG    . LEU C  2  319 ? 57.087 10.783  -0.482  1.00 33.06  ?  351 LEU C CG    1 
ATOM   9278  C  CD1   . LEU C  2  319 ? 55.676 11.215  -0.874  1.00 31.55  ?  351 LEU C CD1   1 
ATOM   9279  C  CD2   . LEU C  2  319 ? 57.319 9.327   -0.828  1.00 34.04  ?  351 LEU C CD2   1 
ATOM   9280  N  N     . GLN C  2  320 ? 60.690 13.925  -1.293  1.00 36.54  ?  352 GLN C N     1 
ATOM   9281  C  CA    . GLN C  2  320 ? 61.698 14.610  -2.117  1.00 36.11  ?  352 GLN C CA    1 
ATOM   9282  C  C     . GLN C  2  320 ? 62.717 13.632  -2.761  1.00 34.07  ?  352 GLN C C     1 
ATOM   9283  O  O     . GLN C  2  320 ? 63.549 13.068  -2.048  1.00 35.57  ?  352 GLN C O     1 
ATOM   9284  C  CB    . GLN C  2  320 ? 62.434 15.639  -1.240  1.00 37.56  ?  352 GLN C CB    1 
ATOM   9285  C  CG    . GLN C  2  320 ? 63.429 16.532  -1.980  1.00 39.77  ?  352 GLN C CG    1 
ATOM   9286  C  CD    . GLN C  2  320 ? 62.785 17.598  -2.865  1.00 41.16  ?  352 GLN C CD    1 
ATOM   9287  O  OE1   . GLN C  2  320 ? 61.817 18.240  -2.463  1.00 44.53  ?  352 GLN C OE1   1 
ATOM   9288  N  NE2   . GLN C  2  320 ? 63.346 17.816  -4.060  1.00 42.22  ?  352 GLN C NE2   1 
ATOM   9289  N  N     . TYR C  2  321 ? 62.654 13.451  -4.094  1.00 31.49  ?  353 TYR C N     1 
ATOM   9290  C  CA    . TYR C  2  321 ? 63.631 12.635  -4.855  1.00 28.30  ?  353 TYR C CA    1 
ATOM   9291  C  C     . TYR C  2  321 ? 64.755 13.492  -5.381  1.00 26.89  ?  353 TYR C C     1 
ATOM   9292  O  O     . TYR C  2  321 ? 64.596 14.716  -5.509  1.00 25.48  ?  353 TYR C O     1 
ATOM   9293  C  CB    . TYR C  2  321 ? 62.959 11.899  -6.014  1.00 26.78  ?  353 TYR C CB    1 
ATOM   9294  C  CG    . TYR C  2  321 ? 61.895 10.961  -5.533  1.00 27.12  ?  353 TYR C CG    1 
ATOM   9295  C  CD1   . TYR C  2  321 ? 62.207 9.677   -5.051  1.00 27.12  ?  353 TYR C CD1   1 
ATOM   9296  C  CD2   . TYR C  2  321 ? 60.576 11.368  -5.493  1.00 27.81  ?  353 TYR C CD2   1 
ATOM   9297  C  CE1   . TYR C  2  321 ? 61.211 8.829   -4.572  1.00 26.43  ?  353 TYR C CE1   1 
ATOM   9298  C  CE2   . TYR C  2  321 ? 59.582 10.536  -5.008  1.00 27.78  ?  353 TYR C CE2   1 
ATOM   9299  C  CZ    . TYR C  2  321 ? 59.897 9.278   -4.561  1.00 26.87  ?  353 TYR C CZ    1 
ATOM   9300  O  OH    . TYR C  2  321 ? 58.857 8.518   -4.132  1.00 26.47  ?  353 TYR C OH    1 
ATOM   9301  N  N     . TYR C  2  322 ? 65.892 12.864  -5.684  1.00 26.77  ?  354 TYR C N     1 
ATOM   9302  C  CA    . TYR C  2  322 ? 67.043 13.622  -6.209  1.00 27.06  ?  354 TYR C CA    1 
ATOM   9303  C  C     . TYR C  2  322 ? 68.028 12.862  -7.049  1.00 25.41  ?  354 TYR C C     1 
ATOM   9304  O  O     . TYR C  2  322 ? 67.879 11.682  -7.233  1.00 22.92  ?  354 TYR C O     1 
ATOM   9305  C  CB    . TYR C  2  322 ? 67.769 14.344  -5.076  1.00 28.50  ?  354 TYR C CB    1 
ATOM   9306  C  CG    . TYR C  2  322 ? 68.787 13.576  -4.246  1.00 28.44  ?  354 TYR C CG    1 
ATOM   9307  C  CD1   . TYR C  2  322 ? 68.404 12.558  -3.351  1.00 28.11  ?  354 TYR C CD1   1 
ATOM   9308  C  CD2   . TYR C  2  322 ? 70.137 13.947  -4.280  1.00 27.62  ?  354 TYR C CD2   1 
ATOM   9309  C  CE1   . TYR C  2  322 ? 69.370 11.920  -2.569  1.00 27.30  ?  354 TYR C CE1   1 
ATOM   9310  C  CE2   . TYR C  2  322 ? 71.084 13.309  -3.506  1.00 26.28  ?  354 TYR C CE2   1 
ATOM   9311  C  CZ    . TYR C  2  322 ? 70.696 12.317  -2.665  1.00 25.77  ?  354 TYR C CZ    1 
ATOM   9312  O  OH    . TYR C  2  322 ? 71.670 11.747  -1.956  1.00 25.34  ?  354 TYR C OH    1 
ATOM   9313  N  N     . LEU C  2  323 ? 69.065 13.550  -7.491  1.00 26.99  ?  355 LEU C N     1 
ATOM   9314  C  CA    . LEU C  2  323 ? 70.133 12.962  -8.274  1.00 30.04  ?  355 LEU C CA    1 
ATOM   9315  C  C     . LEU C  2  323 ? 71.522 13.408  -7.794  1.00 34.16  ?  355 LEU C C     1 
ATOM   9316  O  O     . LEU C  2  323 ? 71.793 14.568  -7.844  1.00 35.05  ?  355 LEU C O     1 
ATOM   9317  C  CB    . LEU C  2  323 ? 69.966 13.398  -9.707  1.00 28.46  ?  355 LEU C CB    1 
ATOM   9318  C  CG    . LEU C  2  323 ? 71.021 13.050  -10.711 1.00 27.80  ?  355 LEU C CG    1 
ATOM   9319  C  CD1   . LEU C  2  323 ? 70.982 11.600  -10.987 1.00 27.64  ?  355 LEU C CD1   1 
ATOM   9320  C  CD2   . LEU C  2  323 ? 70.773 13.790  -11.984 1.00 28.21  ?  355 LEU C CD2   1 
ATOM   9321  N  N     . ASN C  2  324 ? 72.396 12.505  -7.333  1.00 37.10  ?  356 ASN C N     1 
ATOM   9322  C  CA    . ASN C  2  324 ? 73.738 12.897  -6.917  1.00 39.30  ?  356 ASN C CA    1 
ATOM   9323  C  C     . ASN C  2  324 ? 74.434 13.162  -8.204  1.00 40.67  ?  356 ASN C C     1 
ATOM   9324  O  O     . ASN C  2  324 ? 74.723 12.255  -8.931  1.00 43.40  ?  356 ASN C O     1 
ATOM   9325  C  CB    . ASN C  2  324 ? 74.458 11.799  -6.177  1.00 41.18  ?  356 ASN C CB    1 
ATOM   9326  C  CG    . ASN C  2  324 ? 75.756 12.262  -5.615  1.00 45.87  ?  356 ASN C CG    1 
ATOM   9327  O  OD1   . ASN C  2  324 ? 76.238 13.289  -6.011  1.00 45.70  ?  356 ASN C OD1   1 
ATOM   9328  N  ND2   . ASN C  2  324 ? 76.319 11.533  -4.670  1.00 51.11  ?  356 ASN C ND2   1 
ATOM   9329  N  N     . LEU C  2  325 ? 74.707 14.409  -8.506  1.00 38.09  ?  357 LEU C N     1 
ATOM   9330  C  CA    . LEU C  2  325 ? 75.190 14.782  -9.833  1.00 36.25  ?  357 LEU C CA    1 
ATOM   9331  C  C     . LEU C  2  325 ? 76.575 14.258  -10.007 1.00 32.75  ?  357 LEU C C     1 
ATOM   9332  O  O     . LEU C  2  325 ? 76.830 13.466  -10.890 1.00 32.06  ?  357 LEU C O     1 
ATOM   9333  C  CB    . LEU C  2  325 ? 75.172 16.304  -10.044 1.00 39.27  ?  357 LEU C CB    1 
ATOM   9334  C  CG    . LEU C  2  325 ? 75.519 16.820  -11.461 1.00 40.73  ?  357 LEU C CG    1 
ATOM   9335  C  CD1   . LEU C  2  325 ? 74.523 16.265  -12.484 1.00 40.87  ?  357 LEU C CD1   1 
ATOM   9336  C  CD2   . LEU C  2  325 ? 75.604 18.357  -11.535 1.00 39.65  ?  357 LEU C CD2   1 
ATOM   9337  N  N     . THR C  2  326 ? 77.466 14.681  -9.134  1.00 30.93  ?  358 THR C N     1 
ATOM   9338  C  CA    . THR C  2  326 ? 78.780 14.146  -9.153  1.00 31.34  ?  358 THR C CA    1 
ATOM   9339  C  C     . THR C  2  326 ? 78.716 12.659  -9.396  1.00 33.91  ?  358 THR C C     1 
ATOM   9340  O  O     . THR C  2  326 ? 79.379 12.201  -10.283 1.00 36.47  ?  358 THR C O     1 
ATOM   9341  C  CB    . THR C  2  326 ? 79.554 14.471  -7.877  1.00 30.72  ?  358 THR C CB    1 
ATOM   9342  O  OG1   . THR C  2  326 ? 80.289 15.675  -8.096  1.00 28.99  ?  358 THR C OG1   1 
ATOM   9343  C  CG2   . THR C  2  326 ? 80.553 13.387  -7.543  1.00 31.52  ?  358 THR C CG2   1 
ATOM   9344  N  N     . GLU C  2  327 ? 77.922 11.907  -8.648  1.00 39.32  ?  359 GLU C N     1 
ATOM   9345  C  CA    . GLU C  2  327 ? 77.933 10.427  -8.781  1.00 48.98  ?  359 GLU C CA    1 
ATOM   9346  C  C     . GLU C  2  327 ? 77.397 9.949   -10.134 1.00 50.98  ?  359 GLU C C     1 
ATOM   9347  O  O     . GLU C  2  327 ? 77.999 9.076   -10.787 1.00 48.89  ?  359 GLU C O     1 
ATOM   9348  C  CB    . GLU C  2  327 ? 77.155 9.717   -7.624  1.00 55.43  ?  359 GLU C CB    1 
ATOM   9349  C  CG    . GLU C  2  327 ? 76.826 8.226   -7.863  1.00 55.74  ?  359 GLU C CG    1 
ATOM   9350  C  CD    . GLU C  2  327 ? 76.128 7.571   -6.689  1.00 55.29  ?  359 GLU C CD    1 
ATOM   9351  O  OE1   . GLU C  2  327 ? 76.843 7.249   -5.727  1.00 53.52  ?  359 GLU C OE1   1 
ATOM   9352  O  OE2   . GLU C  2  327 ? 74.886 7.366   -6.736  1.00 57.01  -1 359 GLU C OE2   1 
ATOM   9353  N  N     . ALA C  2  328 ? 76.249 10.498  -10.524 1.00 53.43  ?  360 ALA C N     1 
ATOM   9354  C  CA    . ALA C  2  328 ? 75.597 10.121  -11.772 1.00 55.37  ?  360 ALA C CA    1 
ATOM   9355  C  C     . ALA C  2  328 ? 76.567 10.260  -12.928 1.00 53.11  ?  360 ALA C C     1 
ATOM   9356  O  O     . ALA C  2  328 ? 76.587 9.425   -13.816 1.00 53.90  ?  360 ALA C O     1 
ATOM   9357  C  CB    . ALA C  2  328 ? 74.357 10.975  -12.016 1.00 58.50  ?  360 ALA C CB    1 
ATOM   9358  N  N     . ASN C  2  329 ? 77.382 11.309  -12.906 1.00 52.24  ?  361 ASN C N     1 
ATOM   9359  C  CA    . ASN C  2  329 ? 78.444 11.456  -13.899 1.00 52.72  ?  361 ASN C CA    1 
ATOM   9360  C  C     . ASN C  2  329 ? 79.585 10.399  -13.759 1.00 55.62  ?  361 ASN C C     1 
ATOM   9361  O  O     . ASN C  2  329 ? 79.937 9.791   -14.759 1.00 60.96  ?  361 ASN C O     1 
ATOM   9362  C  CB    . ASN C  2  329 ? 78.924 12.915  -13.963 1.00 47.87  ?  361 ASN C CB    1 
ATOM   9363  C  CG    . ASN C  2  329 ? 77.826 13.862  -14.463 1.00 45.36  ?  361 ASN C CG    1 
ATOM   9364  O  OD1   . ASN C  2  329 ? 76.934 13.466  -15.207 1.00 41.27  ?  361 ASN C OD1   1 
ATOM   9365  N  ND2   . ASN C  2  329 ? 77.894 15.111  -14.057 1.00 44.64  ?  361 ASN C ND2   1 
ATOM   9366  N  N     . LEU C  2  330 ? 80.099 10.118  -12.554 1.00 56.71  ?  362 LEU C N     1 
ATOM   9367  C  CA    . LEU C  2  330 ? 81.120 9.047   -12.370 1.00 58.33  ?  362 LEU C CA    1 
ATOM   9368  C  C     . LEU C  2  330 ? 80.660 7.657   -12.860 1.00 61.93  ?  362 LEU C C     1 
ATOM   9369  O  O     . LEU C  2  330 ? 81.401 6.966   -13.578 1.00 57.95  ?  362 LEU C O     1 
ATOM   9370  C  CB    . LEU C  2  330 ? 81.566 8.899   -10.908 1.00 58.15  ?  362 LEU C CB    1 
ATOM   9371  C  CG    . LEU C  2  330 ? 81.899 10.122  -10.045 1.00 61.65  ?  362 LEU C CG    1 
ATOM   9372  C  CD1   . LEU C  2  330 ? 82.718 9.690   -8.830  1.00 59.61  ?  362 LEU C CD1   1 
ATOM   9373  C  CD2   . LEU C  2  330 ? 82.586 11.248  -10.826 1.00 62.07  ?  362 LEU C CD2   1 
ATOM   9374  N  N     . LYS C  2  331 ? 79.460 7.240   -12.442 1.00 65.66  ?  363 LYS C N     1 
ATOM   9375  C  CA    . LYS C  2  331 ? 78.848 5.972   -12.915 1.00 65.39  ?  363 LYS C CA    1 
ATOM   9376  C  C     . LYS C  2  331 ? 78.408 6.068   -14.382 1.00 60.21  ?  363 LYS C C     1 
ATOM   9377  O  O     . LYS C  2  331 ? 78.440 5.085   -15.122 1.00 51.63  ?  363 LYS C O     1 
ATOM   9378  C  CB    . LYS C  2  331 ? 77.640 5.568   -12.041 1.00 66.62  ?  363 LYS C CB    1 
ATOM   9379  C  CG    . LYS C  2  331 ? 78.003 5.199   -10.599 1.00 70.23  ?  363 LYS C CG    1 
ATOM   9380  C  CD    . LYS C  2  331 ? 76.791 4.879   -9.717  1.00 73.84  ?  363 LYS C CD    1 
ATOM   9381  C  CE    . LYS C  2  331 ? 76.055 3.611   -10.160 1.00 77.45  ?  363 LYS C CE    1 
ATOM   9382  N  NZ    . LYS C  2  331 ? 75.170 3.028   -9.104  1.00 79.23  1  363 LYS C NZ    1 
ATOM   9383  N  N     . GLY C  2  332 ? 78.012 7.270   -14.787 1.00 59.53  ?  364 GLY C N     1 
ATOM   9384  C  CA    . GLY C  2  332 ? 77.402 7.497   -16.085 1.00 57.67  ?  364 GLY C CA    1 
ATOM   9385  C  C     . GLY C  2  332 ? 75.986 6.959   -16.124 1.00 58.05  ?  364 GLY C C     1 
ATOM   9386  O  O     . GLY C  2  332 ? 75.532 6.535   -17.181 1.00 58.43  ?  364 GLY C O     1 
ATOM   9387  N  N     . GLU C  2  333 ? 75.294 6.972   -14.975 1.00 60.30  ?  365 GLU C N     1 
ATOM   9388  C  CA    . GLU C  2  333 ? 73.901 6.502   -14.872 1.00 61.27  ?  365 GLU C CA    1 
ATOM   9389  C  C     . GLU C  2  333 ? 73.027 7.455   -14.044 1.00 59.90  ?  365 GLU C C     1 
ATOM   9390  O  O     . GLU C  2  333 ? 73.502 8.042   -13.071 1.00 58.68  ?  365 GLU C O     1 
ATOM   9391  C  CB    . GLU C  2  333 ? 73.853 5.103   -14.243 1.00 65.81  ?  365 GLU C CB    1 
ATOM   9392  C  CG    . GLU C  2  333 ? 74.557 3.992   -15.027 1.00 69.78  ?  365 GLU C CG    1 
ATOM   9393  C  CD    . GLU C  2  333 ? 73.935 3.660   -16.394 1.00 71.90  ?  365 GLU C CD    1 
ATOM   9394  O  OE1   . GLU C  2  333 ? 72.756 4.003   -16.662 1.00 72.42  ?  365 GLU C OE1   1 
ATOM   9395  O  OE2   . GLU C  2  333 ? 74.645 3.030   -17.214 1.00 70.66  -1 365 GLU C OE2   1 
ATOM   9396  N  N     . SER C  2  334 ? 71.753 7.590   -14.435 1.00 59.30  ?  366 SER C N     1 
ATOM   9397  C  CA    . SER C  2  334 ? 70.773 8.449   -13.734 1.00 56.86  ?  366 SER C CA    1 
ATOM   9398  C  C     . SER C  2  334 ? 70.186 7.779   -12.497 1.00 56.40  ?  366 SER C C     1 
ATOM   9399  O  O     . SER C  2  334 ? 69.063 7.269   -12.527 1.00 55.36  ?  366 SER C O     1 
ATOM   9400  C  CB    . SER C  2  334 ? 69.621 8.821   -14.665 1.00 55.56  ?  366 SER C CB    1 
ATOM   9401  O  OG    . SER C  2  334 ? 70.079 9.678   -15.676 1.00 56.77  ?  366 SER C OG    1 
ATOM   9402  N  N     . ILE C  2  335 ? 70.933 7.826   -11.401 1.00 56.51  ?  367 ILE C N     1 
ATOM   9403  C  CA    . ILE C  2  335 ? 70.537 7.172   -10.155 1.00 57.11  ?  367 ILE C CA    1 
ATOM   9404  C  C     . ILE C  2  335 ? 69.573 8.073   -9.362  1.00 49.86  ?  367 ILE C C     1 
ATOM   9405  O  O     . ILE C  2  335 ? 69.939 8.545   -8.292  1.00 52.97  ?  367 ILE C O     1 
ATOM   9406  C  CB    . ILE C  2  335 ? 71.783 6.839   -9.260  1.00 61.13  ?  367 ILE C CB    1 
ATOM   9407  C  CG1   . ILE C  2  335 ? 72.948 6.263   -10.085 1.00 60.18  ?  367 ILE C CG1   1 
ATOM   9408  C  CG2   . ILE C  2  335 ? 71.402 5.868   -8.134  1.00 62.57  ?  367 ILE C CG2   1 
ATOM   9409  C  CD1   . ILE C  2  335 ? 72.564 5.058   -10.922 1.00 60.98  ?  367 ILE C CD1   1 
ATOM   9410  N  N     . TRP C  2  336 ? 68.358 8.318   -9.863  1.00 43.46  ?  368 TRP C N     1 
ATOM   9411  C  CA    . TRP C  2  336 ? 67.386 9.148   -9.113  1.00 41.82  ?  368 TRP C CA    1 
ATOM   9412  C  C     . TRP C  2  336 ? 66.943 8.440   -7.821  1.00 41.53  ?  368 TRP C C     1 
ATOM   9413  O  O     . TRP C  2  336 ? 66.162 7.494   -7.866  1.00 42.16  ?  368 TRP C O     1 
ATOM   9414  C  CB    . TRP C  2  336 ? 66.148 9.552   -9.947  1.00 39.85  ?  368 TRP C CB    1 
ATOM   9415  C  CG    . TRP C  2  336 ? 66.353 10.781  -10.811 1.00 37.74  ?  368 TRP C CG    1 
ATOM   9416  C  CD1   . TRP C  2  336 ? 66.699 10.804  -12.140 1.00 38.37  ?  368 TRP C CD1   1 
ATOM   9417  C  CD2   . TRP C  2  336 ? 66.223 12.152  -10.416 1.00 33.29  ?  368 TRP C CD2   1 
ATOM   9418  N  NE1   . TRP C  2  336 ? 66.784 12.102  -12.592 1.00 36.27  ?  368 TRP C NE1   1 
ATOM   9419  C  CE2   . TRP C  2  336 ? 66.510 12.946  -11.551 1.00 32.74  ?  368 TRP C CE2   1 
ATOM   9420  C  CE3   . TRP C  2  336 ? 65.889 12.781  -9.228  1.00 30.92  ?  368 TRP C CE3   1 
ATOM   9421  C  CZ2   . TRP C  2  336 ? 66.498 14.309  -11.517 1.00 29.87  ?  368 TRP C CZ2   1 
ATOM   9422  C  CZ3   . TRP C  2  336 ? 65.866 14.137  -9.207  1.00 30.43  ?  368 TRP C CZ3   1 
ATOM   9423  C  CH2   . TRP C  2  336 ? 66.173 14.890  -10.342 1.00 30.51  ?  368 TRP C CH2   1 
ATOM   9424  N  N     . LYS C  2  337 ? 67.476 8.903   -6.685  1.00 40.98  ?  369 LYS C N     1 
ATOM   9425  C  CA    . LYS C  2  337 ? 67.159 8.375   -5.354  1.00 37.95  ?  369 LYS C CA    1 
ATOM   9426  C  C     . LYS C  2  337 ? 66.067 9.230   -4.698  1.00 35.73  ?  369 LYS C C     1 
ATOM   9427  O  O     . LYS C  2  337 ? 65.664 10.275  -5.218  1.00 37.07  ?  369 LYS C O     1 
ATOM   9428  C  CB    . LYS C  2  337 ? 68.409 8.340   -4.421  1.00 37.11  ?  369 LYS C CB    1 
ATOM   9429  C  CG    . LYS C  2  337 ? 69.624 7.576   -4.936  1.00 37.29  ?  369 LYS C CG    1 
ATOM   9430  C  CD    . LYS C  2  337 ? 70.869 7.840   -4.091  1.00 38.20  ?  369 LYS C CD    1 
ATOM   9431  C  CE    . LYS C  2  337 ? 72.163 7.705   -4.905  1.00 39.20  ?  369 LYS C CE    1 
ATOM   9432  N  NZ    . LYS C  2  337 ? 73.229 8.649   -4.447  1.00 38.62  1  369 LYS C NZ    1 
ATOM   9433  N  N     . LEU C  2  338 ? 65.593 8.723   -3.564  1.00 33.07  ?  370 LEU C N     1 
ATOM   9434  C  CA    . LEU C  2  338 ? 64.816 9.454   -2.579  1.00 30.29  ?  370 LEU C CA    1 
ATOM   9435  C  C     . LEU C  2  338 ? 65.767 10.193  -1.599  1.00 29.22  ?  370 LEU C C     1 
ATOM   9436  O  O     . LEU C  2  338 ? 66.658 9.574   -0.988  1.00 27.05  ?  370 LEU C O     1 
ATOM   9437  C  CB    . LEU C  2  338 ? 63.948 8.450   -1.813  1.00 29.42  ?  370 LEU C CB    1 
ATOM   9438  C  CG    . LEU C  2  338 ? 63.086 8.963   -0.657  1.00 29.19  ?  370 LEU C CG    1 
ATOM   9439  C  CD1   . LEU C  2  338 ? 61.874 9.669   -1.232  1.00 29.15  ?  370 LEU C CD1   1 
ATOM   9440  C  CD2   . LEU C  2  338 ? 62.665 7.865   0.317   1.00 27.63  ?  370 LEU C CD2   1 
ATOM   9441  N  N     . GLU C  2  339 ? 65.576 11.504  -1.458  1.00 28.14  ?  371 GLU C N     1 
ATOM   9442  C  CA    . GLU C  2  339 ? 66.277 12.285  -0.440  1.00 28.81  ?  371 GLU C CA    1 
ATOM   9443  C  C     . GLU C  2  339 ? 65.742 12.061  0.995   1.00 29.50  ?  371 GLU C C     1 
ATOM   9444  O  O     . GLU C  2  339 ? 66.524 11.835  1.938   1.00 31.54  ?  371 GLU C O     1 
ATOM   9445  C  CB    . GLU C  2  339 ? 66.245 13.787  -0.779  1.00 28.99  ?  371 GLU C CB    1 
ATOM   9446  C  CG    . GLU C  2  339 ? 67.409 14.584  -0.170  1.00 30.43  ?  371 GLU C CG    1 
ATOM   9447  C  CD    . GLU C  2  339 ? 67.205 16.097  -0.222  1.00 32.01  ?  371 GLU C CD    1 
ATOM   9448  O  OE1   . GLU C  2  339 ? 66.055 16.528  -0.438  1.00 32.91  ?  371 GLU C OE1   1 
ATOM   9449  O  OE2   . GLU C  2  339 ? 68.180 16.864  -0.018  1.00 32.54  -1 371 GLU C OE2   1 
ATOM   9450  N  N     . TYR C  2  340 ? 64.421 12.154  1.160   1.00 30.13  ?  372 TYR C N     1 
ATOM   9451  C  CA    . TYR C  2  340 ? 63.758 12.162  2.499   1.00 29.25  ?  372 TYR C CA    1 
ATOM   9452  C  C     . TYR C  2  340 ? 62.230 12.147  2.358   1.00 29.10  ?  372 TYR C C     1 
ATOM   9453  O  O     . TYR C  2  340 ? 61.679 12.603  1.344   1.00 26.33  ?  372 TYR C O     1 
ATOM   9454  C  CB    . TYR C  2  340 ? 64.169 13.396  3.359   1.00 27.69  ?  372 TYR C CB    1 
ATOM   9455  C  CG    . TYR C  2  340 ? 63.544 14.739  2.946   1.00 26.69  ?  372 TYR C CG    1 
ATOM   9456  C  CD1   . TYR C  2  340 ? 62.312 15.129  3.432   1.00 26.07  ?  372 TYR C CD1   1 
ATOM   9457  C  CD2   . TYR C  2  340 ? 64.201 15.607  2.074   1.00 25.83  ?  372 TYR C CD2   1 
ATOM   9458  C  CE1   . TYR C  2  340 ? 61.749 16.327  3.072   1.00 25.49  ?  372 TYR C CE1   1 
ATOM   9459  C  CE2   . TYR C  2  340 ? 63.655 16.806  1.720   1.00 25.00  ?  372 TYR C CE2   1 
ATOM   9460  C  CZ    . TYR C  2  340 ? 62.428 17.150  2.232   1.00 26.23  ?  372 TYR C CZ    1 
ATOM   9461  O  OH    . TYR C  2  340 ? 61.850 18.338  1.895   1.00 29.54  ?  372 TYR C OH    1 
ATOM   9462  N  N     . ILE C  2  341 ? 61.562 11.630  3.386   1.00 30.25  ?  373 ILE C N     1 
ATOM   9463  C  CA    . ILE C  2  341 ? 60.123 11.849  3.550   1.00 32.83  ?  373 ILE C CA    1 
ATOM   9464  C  C     . ILE C  2  341 ? 59.854 12.964  4.596   1.00 33.82  ?  373 ILE C C     1 
ATOM   9465  O  O     . ILE C  2  341 ? 60.351 12.919  5.762   1.00 34.51  ?  373 ILE C O     1 
ATOM   9466  C  CB    . ILE C  2  341 ? 59.398 10.554  3.938   1.00 33.55  ?  373 ILE C CB    1 
ATOM   9467  C  CG1   . ILE C  2  341 ? 59.694 9.463   2.917   1.00 35.07  ?  373 ILE C CG1   1 
ATOM   9468  C  CG2   . ILE C  2  341 ? 57.895 10.797  4.016   1.00 33.41  ?  373 ILE C CG2   1 
ATOM   9469  C  CD1   . ILE C  2  341 ? 59.347 8.096   3.441   1.00 36.68  ?  373 ILE C CD1   1 
ATOM   9470  N  N     . LEU C  2  342 ? 59.080 13.982  4.200   1.00 31.76  ?  374 LEU C N     1 
ATOM   9471  C  CA    . LEU C  2  342 ? 59.022 15.174  5.043   1.00 29.13  ?  374 LEU C CA    1 
ATOM   9472  C  C     . LEU C  2  342 ? 58.478 14.875  6.485   1.00 28.57  ?  374 LEU C C     1 
ATOM   9473  O  O     . LEU C  2  342 ? 58.968 15.434  7.472   1.00 30.50  ?  374 LEU C O     1 
ATOM   9474  C  CB    . LEU C  2  342 ? 58.329 16.347  4.330   1.00 26.70  ?  374 LEU C CB    1 
ATOM   9475  C  CG    . LEU C  2  342 ? 58.646 17.708  4.971   1.00 26.22  ?  374 LEU C CG    1 
ATOM   9476  C  CD1   . LEU C  2  342 ? 58.306 18.849  4.052   1.00 25.94  ?  374 LEU C CD1   1 
ATOM   9477  C  CD2   . LEU C  2  342 ? 57.909 17.939  6.286   1.00 27.44  ?  374 LEU C CD2   1 
ATOM   9478  N  N     . THR C  2  343 ? 57.513 13.977  6.634   1.00 27.53  ?  375 THR C N     1 
ATOM   9479  C  CA    . THR C  2  343 ? 56.962 13.737  7.964   1.00 26.68  ?  375 THR C CA    1 
ATOM   9480  C  C     . THR C  2  343 ? 57.853 12.803  8.755   1.00 26.80  ?  375 THR C C     1 
ATOM   9481  O  O     . THR C  2  343 ? 57.936 12.929  9.971   1.00 25.97  ?  375 THR C O     1 
ATOM   9482  C  CB    . THR C  2  343 ? 55.534 13.183  7.932   1.00 26.01  ?  375 THR C CB    1 
ATOM   9483  O  OG1   . THR C  2  343 ? 55.542 11.892  7.338   1.00 26.02  ?  375 THR C OG1   1 
ATOM   9484  C  CG2   . THR C  2  343 ? 54.589 14.100  7.167   1.00 26.14  ?  375 THR C CG2   1 
ATOM   9485  N  N     . GLN C  2  344 ? 58.531 11.895  8.062   1.00 28.05  ?  376 GLN C N     1 
ATOM   9486  C  CA    . GLN C  2  344 ? 59.433 10.952  8.700   1.00 31.76  ?  376 GLN C CA    1 
ATOM   9487  C  C     . GLN C  2  344 ? 60.661 11.626  9.214   1.00 31.48  ?  376 GLN C C     1 
ATOM   9488  O  O     . GLN C  2  344 ? 61.121 11.351  10.337  1.00 33.44  ?  376 GLN C O     1 
ATOM   9489  C  CB    . GLN C  2  344 ? 59.935 9.903   7.718   1.00 37.49  ?  376 GLN C CB    1 
ATOM   9490  C  CG    . GLN C  2  344 ? 58.868 9.001   7.130   1.00 43.97  ?  376 GLN C CG    1 
ATOM   9491  C  CD    . GLN C  2  344 ? 58.156 8.196   8.197   1.00 51.29  ?  376 GLN C CD    1 
ATOM   9492  O  OE1   . GLN C  2  344 ? 58.649 7.141   8.631   1.00 57.33  ?  376 GLN C OE1   1 
ATOM   9493  N  NE2   . GLN C  2  344 ? 56.993 8.695   8.644   1.00 54.26  ?  376 GLN C NE2   1 
ATOM   9494  N  N     . THR C  2  345 ? 61.222 12.493  8.379   1.00 30.50  ?  377 THR C N     1 
ATOM   9495  C  CA    . THR C  2  345 ? 62.572 12.979  8.630   1.00 29.62  ?  377 THR C CA    1 
ATOM   9496  C  C     . THR C  2  345 ? 62.547 13.871  9.892   1.00 31.20  ?  377 THR C C     1 
ATOM   9497  O  O     . THR C  2  345 ? 63.377 13.716  10.802  1.00 30.62  ?  377 THR C O     1 
ATOM   9498  C  CB    . THR C  2  345 ? 63.190 13.585  7.328   1.00 26.84  ?  377 THR C CB    1 
ATOM   9499  O  OG1   . THR C  2  345 ? 64.617 13.486  7.381   1.00 24.78  ?  377 THR C OG1   1 
ATOM   9500  C  CG2   . THR C  2  345 ? 62.757 14.998  7.082   1.00 25.78  ?  377 THR C CG2   1 
ATOM   9501  N  N     . TYR C  2  346 ? 61.513 14.708  9.969   1.00 33.57  ?  378 TYR C N     1 
ATOM   9502  C  CA    . TYR C  2  346 ? 61.336 15.689  11.031  1.00 36.00  ?  378 TYR C CA    1 
ATOM   9503  C  C     . TYR C  2  346 ? 60.403 15.211  12.163  1.00 36.80  ?  378 TYR C C     1 
ATOM   9504  O  O     . TYR C  2  346 ? 60.054 15.995  13.070  1.00 36.02  ?  378 TYR C O     1 
ATOM   9505  C  CB    . TYR C  2  346 ? 60.752 16.971  10.430  1.00 38.48  ?  378 TYR C CB    1 
ATOM   9506  C  CG    . TYR C  2  346 ? 61.634 17.686  9.451   1.00 39.28  ?  378 TYR C CG    1 
ATOM   9507  C  CD1   . TYR C  2  346 ? 62.812 18.280  9.867   1.00 40.94  ?  378 TYR C CD1   1 
ATOM   9508  C  CD2   . TYR C  2  346 ? 61.267 17.800  8.109   1.00 40.38  ?  378 TYR C CD2   1 
ATOM   9509  C  CE1   . TYR C  2  346 ? 63.628 18.960  8.969   1.00 45.60  ?  378 TYR C CE1   1 
ATOM   9510  C  CE2   . TYR C  2  346 ? 62.075 18.457  7.193   1.00 43.05  ?  378 TYR C CE2   1 
ATOM   9511  C  CZ    . TYR C  2  346 ? 63.264 19.043  7.621   1.00 46.54  ?  378 TYR C CZ    1 
ATOM   9512  O  OH    . TYR C  2  346 ? 64.082 19.714  6.721   1.00 43.89  ?  378 TYR C OH    1 
ATOM   9513  N  N     . ASP C  2  347 ? 59.983 13.983  12.083  1.00 38.26  ?  379 ASP C N     1 
ATOM   9514  C  CA    . ASP C  2  347 ? 59.173 13.443  13.103  1.00 41.91  ?  379 ASP C CA    1 
ATOM   9515  C  C     . ASP C  2  347 ? 58.049 14.367  13.389  1.00 40.73  ?  379 ASP C C     1 
ATOM   9516  O  O     . ASP C  2  347 ? 58.004 14.986  14.412  1.00 38.46  ?  379 ASP C O     1 
ATOM   9517  C  CB    . ASP C  2  347 ? 60.068 13.257  14.294  1.00 47.35  ?  379 ASP C CB    1 
ATOM   9518  C  CG    . ASP C  2  347 ? 59.340 12.844  15.520  1.00 54.21  ?  379 ASP C CG    1 
ATOM   9519  O  OD1   . ASP C  2  347 ? 59.141 11.634  15.683  1.00 58.44  ?  379 ASP C OD1   1 
ATOM   9520  O  OD2   . ASP C  2  347 ? 59.019 13.707  16.366  1.00 59.25  -1 379 ASP C OD2   1 
ATOM   9521  N  N     . ILE C  2  348 ? 57.126 14.430  12.438  1.00 41.32  ?  380 ILE C N     1 
ATOM   9522  C  CA    . ILE C  2  348 ? 55.887 15.242  12.499  1.00 41.18  ?  380 ILE C CA    1 
ATOM   9523  C  C     . ILE C  2  348 ? 54.677 14.547  11.862  1.00 38.55  ?  380 ILE C C     1 
ATOM   9524  O  O     . ILE C  2  348 ? 54.834 13.747  10.982  1.00 33.94  ?  380 ILE C O     1 
ATOM   9525  C  CB    . ILE C  2  348 ? 56.049 16.633  11.826  1.00 41.07  ?  380 ILE C CB    1 
ATOM   9526  C  CG1   . ILE C  2  348 ? 56.437 16.463  10.348  1.00 43.99  ?  380 ILE C CG1   1 
ATOM   9527  C  CG2   . ILE C  2  348 ? 57.062 17.488  12.588  1.00 39.06  ?  380 ILE C CG2   1 
ATOM   9528  C  CD1   . ILE C  2  348 ? 56.472 17.753  9.550   1.00 46.33  ?  380 ILE C CD1   1 
ATOM   9529  N  N     . GLU C  2  349 ? 53.484 14.911  12.329  1.00 40.81  ?  381 GLU C N     1 
ATOM   9530  C  CA    . GLU C  2  349 ? 52.180 14.438  11.837  1.00 42.01  ?  381 GLU C CA    1 
ATOM   9531  C  C     . GLU C  2  349 ? 51.904 14.553  10.332  1.00 43.66  ?  381 GLU C C     1 
ATOM   9532  O  O     . GLU C  2  349 ? 51.616 13.571  9.660   1.00 46.52  ?  381 GLU C O     1 
ATOM   9533  C  CB    . GLU C  2  349 ? 51.077 15.268  12.519  1.00 44.25  ?  381 GLU C CB    1 
ATOM   9534  C  CG    . GLU C  2  349 ? 50.571 14.718  13.812  1.00 46.24  ?  381 GLU C CG    1 
ATOM   9535  C  CD    . GLU C  2  349 ? 50.102 13.302  13.621  1.00 52.37  ?  381 GLU C CD    1 
ATOM   9536  O  OE1   . GLU C  2  349 ? 49.083 13.078  12.924  1.00 53.70  ?  381 GLU C OE1   1 
ATOM   9537  O  OE2   . GLU C  2  349 ? 50.785 12.406  14.145  1.00 60.27  -1 381 GLU C OE2   1 
ATOM   9538  N  N     . ASP C  2  350 ? 51.916 15.779  9.829   1.00 45.82  ?  382 ASP C N     1 
ATOM   9539  C  CA    . ASP C  2  350 ? 51.358 16.096  8.512   1.00 48.93  ?  382 ASP C CA    1 
ATOM   9540  C  C     . ASP C  2  350 ? 52.073 17.351  7.896   1.00 49.42  ?  382 ASP C C     1 
ATOM   9541  O  O     . ASP C  2  350 ? 53.231 17.641  8.246   1.00 54.02  ?  382 ASP C O     1 
ATOM   9542  C  CB    . ASP C  2  350 ? 49.807 16.214  8.616   1.00 52.63  ?  382 ASP C CB    1 
ATOM   9543  C  CG    . ASP C  2  350 ? 49.327 17.073  9.824   1.00 57.06  ?  382 ASP C CG    1 
ATOM   9544  O  OD1   . ASP C  2  350 ? 49.954 18.121  10.111  1.00 55.42  ?  382 ASP C OD1   1 
ATOM   9545  O  OD2   . ASP C  2  350 ? 48.307 16.705  10.479  1.00 58.00  -1 382 ASP C OD2   1 
ATOM   9546  N  N     . LEU C  2  351 ? 51.440 18.055  6.951   1.00 44.29  ?  383 LEU C N     1 
ATOM   9547  C  CA    . LEU C  2  351 ? 52.007 19.290  6.379   1.00 39.33  ?  383 LEU C CA    1 
ATOM   9548  C  C     . LEU C  2  351 ? 51.098 20.467  6.678   1.00 38.08  ?  383 LEU C C     1 
ATOM   9549  O  O     . LEU C  2  351 ? 51.101 21.491  5.978   1.00 32.70  ?  383 LEU C O     1 
ATOM   9550  C  CB    . LEU C  2  351 ? 52.215 19.127  4.882   1.00 37.77  ?  383 LEU C CB    1 
ATOM   9551  C  CG    . LEU C  2  351 ? 53.542 18.511  4.417   1.00 37.63  ?  383 LEU C CG    1 
ATOM   9552  C  CD1   . LEU C  2  351 ? 54.218 17.552  5.408   1.00 36.51  ?  383 LEU C CD1   1 
ATOM   9553  C  CD2   . LEU C  2  351 ? 53.293 17.844  3.064   1.00 37.51  ?  383 LEU C CD2   1 
ATOM   9554  N  N     . GLN C  2  352 ? 50.334 20.294  7.755   1.00 41.28  ?  384 GLN C N     1 
ATOM   9555  C  CA    . GLN C  2  352 ? 49.410 21.294  8.258   1.00 44.34  ?  384 GLN C CA    1 
ATOM   9556  C  C     . GLN C  2  352 ? 50.226 22.460  8.768   1.00 44.16  ?  384 GLN C C     1 
ATOM   9557  O  O     . GLN C  2  352 ? 51.344 22.241  9.238   1.00 47.53  ?  384 GLN C O     1 
ATOM   9558  C  CB    . GLN C  2  352 ? 48.582 20.720  9.418   1.00 47.58  ?  384 GLN C CB    1 
ATOM   9559  C  CG    . GLN C  2  352 ? 47.475 19.765  9.010   1.00 49.13  ?  384 GLN C CG    1 
ATOM   9560  C  CD    . GLN C  2  352 ? 46.329 20.500  8.350   1.00 51.64  ?  384 GLN C CD    1 
ATOM   9561  O  OE1   . GLN C  2  352 ? 46.030 20.266  7.175   1.00 52.93  ?  384 GLN C OE1   1 
ATOM   9562  N  NE2   . GLN C  2  352 ? 45.714 21.442  9.085   1.00 51.18  ?  384 GLN C NE2   1 
ATOM   9563  N  N     . PRO C  2  353 ? 49.680 23.691  8.718   1.00 41.43  ?  385 PRO C N     1 
ATOM   9564  C  CA    . PRO C  2  353 ? 50.508 24.852  9.097   1.00 42.01  ?  385 PRO C CA    1 
ATOM   9565  C  C     . PRO C  2  353 ? 50.897 24.920  10.604  1.00 42.69  ?  385 PRO C C     1 
ATOM   9566  O  O     . PRO C  2  353 ? 51.917 25.514  10.964  1.00 41.41  ?  385 PRO C O     1 
ATOM   9567  C  CB    . PRO C  2  353 ? 49.646 26.042  8.659   1.00 40.78  ?  385 PRO C CB    1 
ATOM   9568  C  CG    . PRO C  2  353 ? 48.651 25.452  7.703   1.00 39.25  ?  385 PRO C CG    1 
ATOM   9569  C  CD    . PRO C  2  353 ? 48.357 24.109  8.249   1.00 38.74  ?  385 PRO C CD    1 
ATOM   9570  N  N     . GLU C  2  354 ? 50.094 24.294  11.456  1.00 44.89  ?  386 GLU C N     1 
ATOM   9571  C  CA    . GLU C  2  354 ? 50.401 24.137  12.883  1.00 46.22  ?  386 GLU C CA    1 
ATOM   9572  C  C     . GLU C  2  354 ? 51.590 23.177  13.016  1.00 42.06  ?  386 GLU C C     1 
ATOM   9573  O  O     . GLU C  2  354 ? 52.470 23.355  13.856  1.00 40.20  ?  386 GLU C O     1 
ATOM   9574  C  CB    . GLU C  2  354 ? 49.186 23.553  13.646  1.00 53.43  ?  386 GLU C CB    1 
ATOM   9575  C  CG    . GLU C  2  354 ? 47.786 23.995  13.159  1.00 60.15  ?  386 GLU C CG    1 
ATOM   9576  C  CD    . GLU C  2  354 ? 47.128 23.046  12.120  1.00 61.81  ?  386 GLU C CD    1 
ATOM   9577  O  OE1   . GLU C  2  354 ? 46.983 21.830  12.445  1.00 61.02  ?  386 GLU C OE1   1 
ATOM   9578  O  OE2   . GLU C  2  354 ? 46.737 23.519  10.998  1.00 53.67  -1 386 GLU C OE2   1 
ATOM   9579  N  N     . SER C  2  355 ? 51.591 22.150  12.167  1.00 38.63  ?  387 SER C N     1 
ATOM   9580  C  CA    . SER C  2  355 ? 52.653 21.135  12.113  1.00 35.43  ?  387 SER C CA    1 
ATOM   9581  C  C     . SER C  2  355 ? 54.016 21.685  11.641  1.00 33.46  ?  387 SER C C     1 
ATOM   9582  O  O     . SER C  2  355 ? 55.065 21.221  12.093  1.00 32.65  ?  387 SER C O     1 
ATOM   9583  C  CB    . SER C  2  355 ? 52.220 19.955  11.202  1.00 34.34  ?  387 SER C CB    1 
ATOM   9584  O  OG    . SER C  2  355 ? 51.358 19.037  11.854  1.00 32.75  ?  387 SER C OG    1 
ATOM   9585  N  N     . LEU C  2  356 ? 53.999 22.635  10.711  1.00 31.16  ?  388 LEU C N     1 
ATOM   9586  C  CA    . LEU C  2  356 ? 55.224 23.174  10.157  1.00 31.70  ?  388 LEU C CA    1 
ATOM   9587  C  C     . LEU C  2  356 ? 55.726 24.368  10.947  1.00 34.76  ?  388 LEU C C     1 
ATOM   9588  O  O     . LEU C  2  356 ? 56.931 24.536  11.104  1.00 37.73  ?  388 LEU C O     1 
ATOM   9589  C  CB    . LEU C  2  356 ? 55.033 23.592  8.707   1.00 30.65  ?  388 LEU C CB    1 
ATOM   9590  C  CG    . LEU C  2  356 ? 54.804 22.448  7.743   1.00 30.58  ?  388 LEU C CG    1 
ATOM   9591  C  CD1   . LEU C  2  356 ? 54.769 22.981  6.310   1.00 30.87  ?  388 LEU C CD1   1 
ATOM   9592  C  CD2   . LEU C  2  356 ? 55.869 21.373  7.914   1.00 30.99  ?  388 LEU C CD2   1 
ATOM   9593  N  N     . TYR C  2  357 ? 54.815 25.218  11.408  1.00 35.99  ?  389 TYR C N     1 
ATOM   9594  C  CA    . TYR C  2  357 ? 55.167 26.277  12.348  1.00 36.66  ?  389 TYR C CA    1 
ATOM   9595  C  C     . TYR C  2  357 ? 55.855 25.729  13.612  1.00 37.17  ?  389 TYR C C     1 
ATOM   9596  O  O     . TYR C  2  357 ? 56.685 26.422  14.208  1.00 37.05  ?  389 TYR C O     1 
ATOM   9597  C  CB    . TYR C  2  357 ? 53.917 27.022  12.748  1.00 37.09  ?  389 TYR C CB    1 
ATOM   9598  C  CG    . TYR C  2  357 ? 54.097 28.119  13.779  1.00 38.37  ?  389 TYR C CG    1 
ATOM   9599  C  CD1   . TYR C  2  357 ? 54.747 29.320  13.459  1.00 38.84  ?  389 TYR C CD1   1 
ATOM   9600  C  CD2   . TYR C  2  357 ? 53.550 27.980  15.058  1.00 38.32  ?  389 TYR C CD2   1 
ATOM   9601  C  CE1   . TYR C  2  357 ? 54.852 30.336  14.395  1.00 38.20  ?  389 TYR C CE1   1 
ATOM   9602  C  CE2   . TYR C  2  357 ? 53.653 28.980  15.997  1.00 38.29  ?  389 TYR C CE2   1 
ATOM   9603  C  CZ    . TYR C  2  357 ? 54.292 30.151  15.667  1.00 38.67  ?  389 TYR C CZ    1 
ATOM   9604  O  OH    . TYR C  2  357 ? 54.360 31.106  16.643  1.00 39.67  ?  389 TYR C OH    1 
ATOM   9605  N  N     . GLY C  2  358 ? 55.504 24.498  14.009  1.00 37.36  ?  390 GLY C N     1 
ATOM   9606  C  CA    . GLY C  2  358 ? 56.094 23.814  15.184  1.00 35.49  ?  390 GLY C CA    1 
ATOM   9607  C  C     . GLY C  2  358 ? 57.480 23.249  14.942  1.00 33.45  ?  390 GLY C C     1 
ATOM   9608  O  O     . GLY C  2  358 ? 58.326 23.247  15.831  1.00 33.23  ?  390 GLY C O     1 
ATOM   9609  N  N     . LEU C  2  359 ? 57.698 22.743  13.730  1.00 31.71  ?  391 LEU C N     1 
ATOM   9610  C  CA    . LEU C  2  359 ? 59.015 22.294  13.297  1.00 28.89  ?  391 LEU C CA    1 
ATOM   9611  C  C     . LEU C  2  359 ? 59.903 23.504  13.244  1.00 27.69  ?  391 LEU C C     1 
ATOM   9612  O  O     . LEU C  2  359 ? 61.090 23.420  13.522  1.00 28.39  ?  391 LEU C O     1 
ATOM   9613  C  CB    . LEU C  2  359 ? 58.946 21.645  11.903  1.00 28.32  ?  391 LEU C CB    1 
ATOM   9614  C  CG    . LEU C  2  359 ? 60.262 21.196  11.247  1.00 27.82  ?  391 LEU C CG    1 
ATOM   9615  C  CD1   . LEU C  2  359 ? 61.013 20.186  12.083  1.00 27.16  ?  391 LEU C CD1   1 
ATOM   9616  C  CD2   . LEU C  2  359 ? 59.993 20.598  9.886   1.00 28.36  ?  391 LEU C CD2   1 
ATOM   9617  N  N     . ALA C  2  360 ? 59.322 24.632  12.873  1.00 25.25  ?  392 ALA C N     1 
ATOM   9618  C  CA    . ALA C  2  360 ? 60.096 25.799  12.693  1.00 24.91  ?  392 ALA C CA    1 
ATOM   9619  C  C     . ALA C  2  360 ? 60.608 26.243  14.025  1.00 25.57  ?  392 ALA C C     1 
ATOM   9620  O  O     . ALA C  2  360 ? 61.756 26.599  14.138  1.00 24.64  ?  392 ALA C O     1 
ATOM   9621  C  CB    . ALA C  2  360 ? 59.269 26.871  12.053  1.00 26.06  ?  392 ALA C CB    1 
ATOM   9622  N  N     . LYS C  2  361 ? 59.772 26.191  15.055  1.00 29.12  ?  393 LYS C N     1 
ATOM   9623  C  CA    . LYS C  2  361 ? 60.197 26.619  16.414  1.00 30.31  ?  393 LYS C CA    1 
ATOM   9624  C  C     . LYS C  2  361 ? 61.292 25.698  16.921  1.00 29.99  ?  393 LYS C C     1 
ATOM   9625  O  O     . LYS C  2  361 ? 62.235 26.150  17.532  1.00 29.89  ?  393 LYS C O     1 
ATOM   9626  C  CB    . LYS C  2  361 ? 59.026 26.608  17.409  1.00 32.36  ?  393 LYS C CB    1 
ATOM   9627  C  CG    . LYS C  2  361 ? 58.003 27.751  17.308  1.00 34.94  ?  393 LYS C CG    1 
ATOM   9628  C  CD    . LYS C  2  361 ? 58.593 29.128  17.636  1.00 37.58  ?  393 LYS C CD    1 
ATOM   9629  C  CE    . LYS C  2  361 ? 57.497 30.160  17.894  1.00 40.12  ?  393 LYS C CE    1 
ATOM   9630  N  NZ    . LYS C  2  361 ? 58.029 31.456  18.423  1.00 41.58  1  393 LYS C NZ    1 
ATOM   9631  N  N     . GLN C  2  362 ? 61.150 24.402  16.656  1.00 32.14  ?  394 GLN C N     1 
ATOM   9632  C  CA    . GLN C  2  362 ? 62.200 23.390  16.892  1.00 33.14  ?  394 GLN C CA    1 
ATOM   9633  C  C     . GLN C  2  362 ? 63.548 23.763  16.201  1.00 29.55  ?  394 GLN C C     1 
ATOM   9634  O  O     . GLN C  2  362 ? 64.633 23.451  16.697  1.00 27.13  ?  394 GLN C O     1 
ATOM   9635  C  CB    . GLN C  2  362 ? 61.708 22.001  16.388  1.00 37.46  ?  394 GLN C CB    1 
ATOM   9636  C  CG    . GLN C  2  362 ? 61.001 21.059  17.377  1.00 40.48  ?  394 GLN C CG    1 
ATOM   9637  C  CD    . GLN C  2  362 ? 61.176 19.561  16.987  1.00 47.66  ?  394 GLN C CD    1 
ATOM   9638  O  OE1   . GLN C  2  362 ? 60.608 19.097  15.983  1.00 49.21  ?  394 GLN C OE1   1 
ATOM   9639  N  NE2   . GLN C  2  362 ? 61.967 18.800  17.785  1.00 48.90  ?  394 GLN C NE2   1 
ATOM   9640  N  N     . PHE C  2  363 ? 63.456 24.392  15.034  1.00 27.05  ?  395 PHE C N     1 
ATOM   9641  C  CA    . PHE C  2  363 ? 64.608 24.909  14.363  1.00 26.45  ?  395 PHE C CA    1 
ATOM   9642  C  C     . PHE C  2  363 ? 65.369 25.923  15.217  1.00 29.78  ?  395 PHE C C     1 
ATOM   9643  O  O     . PHE C  2  363 ? 66.606 25.927  15.182  1.00 30.03  ?  395 PHE C O     1 
ATOM   9644  C  CB    . PHE C  2  363 ? 64.216 25.579  13.047  1.00 25.30  ?  395 PHE C CB    1 
ATOM   9645  C  CG    . PHE C  2  363 ? 63.871 24.634  11.919  1.00 24.81  ?  395 PHE C CG    1 
ATOM   9646  C  CD1   . PHE C  2  363 ? 64.037 23.251  12.023  1.00 25.37  ?  395 PHE C CD1   1 
ATOM   9647  C  CD2   . PHE C  2  363 ? 63.420 25.154  10.715  1.00 23.92  ?  395 PHE C CD2   1 
ATOM   9648  C  CE1   . PHE C  2  363 ? 63.724 22.412  10.958  1.00 25.27  ?  395 PHE C CE1   1 
ATOM   9649  C  CE2   . PHE C  2  363 ? 63.102 24.319  9.664   1.00 24.31  ?  395 PHE C CE2   1 
ATOM   9650  C  CZ    . PHE C  2  363 ? 63.257 22.945  9.781   1.00 24.46  ?  395 PHE C CZ    1 
ATOM   9651  N  N     . THR C  2  364 ? 64.642 26.762  15.984  1.00 35.21  ?  396 THR C N     1 
ATOM   9652  C  CA    . THR C  2  364 ? 65.212 27.898  16.809  1.00 36.55  ?  396 THR C CA    1 
ATOM   9653  C  C     . THR C  2  364 ? 66.011 27.530  18.115  1.00 35.68  ?  396 THR C C     1 
ATOM   9654  O  O     . THR C  2  364 ? 66.765 28.360  18.628  1.00 38.83  ?  396 THR C O     1 
ATOM   9655  C  CB    . THR C  2  364 ? 64.127 28.984  17.150  1.00 38.20  ?  396 THR C CB    1 
ATOM   9656  O  OG1   . THR C  2  364 ? 63.146 28.467  18.052  1.00 39.72  ?  396 THR C OG1   1 
ATOM   9657  C  CG2   . THR C  2  364 ? 63.393 29.470  15.918  1.00 39.01  ?  396 THR C CG2   1 
ATOM   9658  N  N     . ILE C  2  365 ? 65.824 26.310  18.633  1.00 33.70  ?  397 ILE C N     1 
ATOM   9659  C  CA    . ILE C  2  365 ? 66.704 25.683  19.644  1.00 32.71  ?  397 ILE C CA    1 
ATOM   9660  C  C     . ILE C  2  365 ? 68.182 25.876  19.292  1.00 34.53  ?  397 ILE C C     1 
ATOM   9661  O  O     . ILE C  2  365 ? 68.557 25.801  18.136  1.00 33.01  ?  397 ILE C O     1 
ATOM   9662  C  CB    . ILE C  2  365 ? 66.396 24.158  19.738  1.00 31.50  ?  397 ILE C CB    1 
ATOM   9663  C  CG1   . ILE C  2  365 ? 65.039 23.938  20.439  1.00 30.86  ?  397 ILE C CG1   1 
ATOM   9664  C  CG2   . ILE C  2  365 ? 67.536 23.368  20.405  1.00 30.18  ?  397 ILE C CG2   1 
ATOM   9665  C  CD1   . ILE C  2  365 ? 64.463 22.544  20.308  1.00 29.75  ?  397 ILE C CD1   1 
ATOM   9666  N  N     . LEU C  2  366 ? 69.023 26.129  20.290  1.00 38.64  ?  398 LEU C N     1 
ATOM   9667  C  CA    . LEU C  2  366 ? 70.446 26.312  20.039  1.00 43.30  ?  398 LEU C CA    1 
ATOM   9668  C  C     . LEU C  2  366 ? 70.925 25.015  19.428  1.00 47.62  ?  398 LEU C C     1 
ATOM   9669  O  O     . LEU C  2  366 ? 70.423 23.955  19.780  1.00 53.05  ?  398 LEU C O     1 
ATOM   9670  C  CB    . LEU C  2  366 ? 71.217 26.619  21.331  1.00 46.15  ?  398 LEU C CB    1 
ATOM   9671  C  CG    . LEU C  2  366 ? 71.062 27.977  22.080  1.00 47.70  ?  398 LEU C CG    1 
ATOM   9672  C  CD1   . LEU C  2  366 ? 70.178 29.034  21.393  1.00 46.52  ?  398 LEU C CD1   1 
ATOM   9673  C  CD2   . LEU C  2  366 ? 70.594 27.727  23.522  1.00 46.65  ?  398 LEU C CD2   1 
ATOM   9674  N  N     . ASP C  2  367 ? 71.874 25.125  18.502  1.00 54.01  ?  399 ASP C N     1 
ATOM   9675  C  CA    . ASP C  2  367 ? 72.374 24.015  17.652  1.00 59.88  ?  399 ASP C CA    1 
ATOM   9676  C  C     . ASP C  2  367 ? 71.313 22.926  17.296  1.00 55.73  ?  399 ASP C C     1 
ATOM   9677  O  O     . ASP C  2  367 ? 71.554 21.723  17.500  1.00 56.58  ?  399 ASP C O     1 
ATOM   9678  C  CB    . ASP C  2  367 ? 73.711 23.422  18.227  1.00 66.96  ?  399 ASP C CB    1 
ATOM   9679  C  CG    . ASP C  2  367 ? 74.959 24.387  18.037  1.00 78.07  ?  399 ASP C CG    1 
ATOM   9680  O  OD1   . ASP C  2  367 ? 74.968 25.492  18.642  1.00 87.30  ?  399 ASP C OD1   1 
ATOM   9681  O  OD2   . ASP C  2  367 ? 75.936 24.045  17.299  1.00 74.64  -1 399 ASP C OD2   1 
ATOM   9682  N  N     . SER C  2  368 ? 70.161 23.345  16.742  1.00 49.51  ?  400 SER C N     1 
ATOM   9683  C  CA    . SER C  2  368 ? 69.044 22.408  16.497  1.00 42.75  ?  400 SER C CA    1 
ATOM   9684  C  C     . SER C  2  368 ? 69.439 21.424  15.463  1.00 41.32  ?  400 SER C C     1 
ATOM   9685  O  O     . SER C  2  368 ? 69.747 21.801  14.345  1.00 37.82  ?  400 SER C O     1 
ATOM   9686  C  CB    . SER C  2  368 ? 67.758 23.069  15.997  1.00 39.13  ?  400 SER C CB    1 
ATOM   9687  O  OG    . SER C  2  368 ? 66.748 22.084  15.816  1.00 33.84  ?  400 SER C OG    1 
ATOM   9688  N  N     . LYS C  2  369 ? 69.404 20.166  15.867  1.00 42.68  ?  401 LYS C N     1 
ATOM   9689  C  CA    . LYS C  2  369 ? 69.586 19.031  14.982  1.00 45.04  ?  401 LYS C CA    1 
ATOM   9690  C  C     . LYS C  2  369 ? 68.663 19.065  13.758  1.00 41.49  ?  401 LYS C C     1 
ATOM   9691  O  O     . LYS C  2  369 ? 69.028 18.595  12.691  1.00 39.59  ?  401 LYS C O     1 
ATOM   9692  C  CB    . LYS C  2  369 ? 69.270 17.760  15.773  1.00 52.21  ?  401 LYS C CB    1 
ATOM   9693  C  CG    . LYS C  2  369 ? 70.192 16.587  15.508  1.00 58.20  ?  401 LYS C CG    1 
ATOM   9694  C  CD    . LYS C  2  369 ? 71.267 16.484  16.580  1.00 60.70  ?  401 LYS C CD    1 
ATOM   9695  C  CE    . LYS C  2  369 ? 72.385 15.573  16.109  1.00 64.38  ?  401 LYS C CE    1 
ATOM   9696  N  NZ    . LYS C  2  369 ? 73.623 15.921  16.842  1.00 69.79  1  401 LYS C NZ    1 
ATOM   9697  N  N     . GLN C  2  370 ? 67.449 19.591  13.939  1.00 41.52  ?  402 GLN C N     1 
ATOM   9698  C  CA    . GLN C  2  370 ? 66.409 19.640  12.877  1.00 38.22  ?  402 GLN C CA    1 
ATOM   9699  C  C     . GLN C  2  370 ? 66.763 20.638  11.812  1.00 33.56  ?  402 GLN C C     1 
ATOM   9700  O  O     . GLN C  2  370 ? 66.736 20.349  10.623  1.00 33.14  ?  402 GLN C O     1 
ATOM   9701  C  CB    . GLN C  2  370 ? 65.047 20.050  13.452  1.00 38.98  ?  402 GLN C CB    1 
ATOM   9702  C  CG    . GLN C  2  370 ? 64.423 19.033  14.383  1.00 39.93  ?  402 GLN C CG    1 
ATOM   9703  C  CD    . GLN C  2  370 ? 63.904 17.826  13.631  1.00 43.17  ?  402 GLN C CD    1 
ATOM   9704  O  OE1   . GLN C  2  370 ? 64.636 17.138  12.882  1.00 44.04  ?  402 GLN C OE1   1 
ATOM   9705  N  NE2   . GLN C  2  370 ? 62.620 17.558  13.816  1.00 45.99  ?  402 GLN C NE2   1 
ATOM   9706  N  N     . PHE C  2  371 ? 67.095 21.836  12.240  1.00 29.45  ?  403 PHE C N     1 
ATOM   9707  C  CA    . PHE C  2  371 ? 67.580 22.802  11.290  1.00 27.79  ?  403 PHE C CA    1 
ATOM   9708  C  C     . PHE C  2  371 ? 68.792 22.279  10.495  1.00 27.39  ?  403 PHE C C     1 
ATOM   9709  O  O     . PHE C  2  371 ? 68.959 22.605  9.301   1.00 26.62  ?  403 PHE C O     1 
ATOM   9710  C  CB    . PHE C  2  371 ? 67.947 24.094  11.997  1.00 25.56  ?  403 PHE C CB    1 
ATOM   9711  C  CG    . PHE C  2  371 ? 68.381 25.161  11.069  1.00 22.59  ?  403 PHE C CG    1 
ATOM   9712  C  CD1   . PHE C  2  371 ? 67.468 25.869  10.361  1.00 21.91  ?  403 PHE C CD1   1 
ATOM   9713  C  CD2   . PHE C  2  371 ? 69.705 25.409  10.888  1.00 22.07  ?  403 PHE C CD2   1 
ATOM   9714  C  CE1   . PHE C  2  371 ? 67.868 26.839  9.497   1.00 22.30  ?  403 PHE C CE1   1 
ATOM   9715  C  CE2   . PHE C  2  371 ? 70.130 26.384  10.032  1.00 21.97  ?  403 PHE C CE2   1 
ATOM   9716  C  CZ    . PHE C  2  371 ? 69.208 27.101  9.332   1.00 22.74  ?  403 PHE C CZ    1 
ATOM   9717  N  N     . ILE C  2  372 ? 69.634 21.486  11.142  1.00 26.03  ?  404 ILE C N     1 
ATOM   9718  C  CA    . ILE C  2  372 ? 70.821 21.047  10.460  1.00 28.43  ?  404 ILE C CA    1 
ATOM   9719  C  C     . ILE C  2  372 ? 70.352 20.231  9.239   1.00 30.35  ?  404 ILE C C     1 
ATOM   9720  O  O     . ILE C  2  372 ? 70.754 20.507  8.097   1.00 29.73  ?  404 ILE C O     1 
ATOM   9721  C  CB    . ILE C  2  372 ? 71.813 20.235  11.344  1.00 28.63  ?  404 ILE C CB    1 
ATOM   9722  C  CG1   . ILE C  2  372 ? 71.965 20.787  12.763  1.00 30.06  ?  404 ILE C CG1   1 
ATOM   9723  C  CG2   . ILE C  2  372 ? 73.194 20.222  10.704  1.00 28.59  ?  404 ILE C CG2   1 
ATOM   9724  C  CD1   . ILE C  2  372 ? 72.363 22.258  12.878  1.00 30.73  ?  404 ILE C CD1   1 
ATOM   9725  N  N     . LYS C  2  373 ? 69.487 19.245  9.485   1.00 31.75  ?  405 LYS C N     1 
ATOM   9726  C  CA    . LYS C  2  373 ? 68.885 18.462  8.404   1.00 32.13  ?  405 LYS C CA    1 
ATOM   9727  C  C     . LYS C  2  373 ? 68.450 19.428  7.332   1.00 31.23  ?  405 LYS C C     1 
ATOM   9728  O  O     . LYS C  2  373 ? 68.827 19.285  6.176   1.00 27.44  ?  405 LYS C O     1 
ATOM   9729  C  CB    . LYS C  2  373 ? 67.630 17.685  8.881   1.00 32.93  ?  405 LYS C CB    1 
ATOM   9730  C  CG    . LYS C  2  373 ? 67.825 16.199  9.073   1.00 33.62  ?  405 LYS C CG    1 
ATOM   9731  C  CD    . LYS C  2  373 ? 66.557 15.512  9.563   1.00 35.86  ?  405 LYS C CD    1 
ATOM   9732  C  CE    . LYS C  2  373 ? 66.904 14.179  10.256  1.00 38.17  ?  405 LYS C CE    1 
ATOM   9733  N  NZ    . LYS C  2  373 ? 65.795 13.184  10.429  1.00 38.02  1  405 LYS C NZ    1 
ATOM   9734  N  N     . TYR C  2  374 ? 67.645 20.410  7.769   1.00 32.52  ?  406 TYR C N     1 
ATOM   9735  C  CA    . TYR C  2  374 ? 66.869 21.290  6.885   1.00 33.01  ?  406 TYR C CA    1 
ATOM   9736  C  C     . TYR C  2  374 ? 67.765 22.079  5.954   1.00 35.45  ?  406 TYR C C     1 
ATOM   9737  O  O     . TYR C  2  374 ? 67.348 22.382  4.828   1.00 39.37  ?  406 TYR C O     1 
ATOM   9738  C  CB    . TYR C  2  374 ? 65.922 22.222  7.688   1.00 30.78  ?  406 TYR C CB    1 
ATOM   9739  C  CG    . TYR C  2  374 ? 65.225 23.310  6.869   1.00 28.04  ?  406 TYR C CG    1 
ATOM   9740  C  CD1   . TYR C  2  374 ? 63.981 23.101  6.258   1.00 27.69  ?  406 TYR C CD1   1 
ATOM   9741  C  CD2   . TYR C  2  374 ? 65.816 24.540  6.716   1.00 26.81  ?  406 TYR C CD2   1 
ATOM   9742  C  CE1   . TYR C  2  374 ? 63.373 24.104  5.515   1.00 26.96  ?  406 TYR C CE1   1 
ATOM   9743  C  CE2   . TYR C  2  374 ? 65.228 25.528  5.978   1.00 26.41  ?  406 TYR C CE2   1 
ATOM   9744  C  CZ    . TYR C  2  374 ? 64.026 25.313  5.392   1.00 26.55  ?  406 TYR C CZ    1 
ATOM   9745  O  OH    . TYR C  2  374 ? 63.539 26.374  4.706   1.00 28.17  ?  406 TYR C OH    1 
ATOM   9746  N  N     . TYR C  2  375 ? 68.983 22.394  6.406   1.00 37.28  ?  407 TYR C N     1 
ATOM   9747  C  CA    . TYR C  2  375 ? 69.949 23.156  5.586   1.00 36.86  ?  407 TYR C CA    1 
ATOM   9748  C  C     . TYR C  2  375 ? 70.766 22.240  4.613   1.00 37.99  ?  407 TYR C C     1 
ATOM   9749  O  O     . TYR C  2  375 ? 71.054 22.598  3.443   1.00 35.38  ?  407 TYR C O     1 
ATOM   9750  C  CB    . TYR C  2  375 ? 70.836 24.000  6.518   1.00 34.51  ?  407 TYR C CB    1 
ATOM   9751  C  CG    . TYR C  2  375 ? 71.444 25.226  5.862   1.00 31.70  ?  407 TYR C CG    1 
ATOM   9752  C  CD1   . TYR C  2  375 ? 70.674 26.334  5.540   1.00 29.64  ?  407 TYR C CD1   1 
ATOM   9753  C  CD2   . TYR C  2  375 ? 72.795 25.270  5.581   1.00 31.80  ?  407 TYR C CD2   1 
ATOM   9754  C  CE1   . TYR C  2  375 ? 71.239 27.442  4.951   1.00 28.77  ?  407 TYR C CE1   1 
ATOM   9755  C  CE2   . TYR C  2  375 ? 73.373 26.378  4.993   1.00 31.28  ?  407 TYR C CE2   1 
ATOM   9756  C  CZ    . TYR C  2  375 ? 72.595 27.458  4.677   1.00 29.55  ?  407 TYR C CZ    1 
ATOM   9757  O  OH    . TYR C  2  375 ? 73.221 28.540  4.100   1.00 29.03  ?  407 TYR C OH    1 
ATOM   9758  N  N     . ASN C  2  376 ? 71.109 21.058  5.117   1.00 40.62  ?  408 ASN C N     1 
ATOM   9759  C  CA    . ASN C  2  376 ? 71.662 19.973  4.314   1.00 43.44  ?  408 ASN C CA    1 
ATOM   9760  C  C     . ASN C  2  376 ? 70.768 19.741  3.102   1.00 41.07  ?  408 ASN C C     1 
ATOM   9761  O  O     . ASN C  2  376 ? 71.254 19.648  1.990   1.00 40.93  ?  408 ASN C O     1 
ATOM   9762  C  CB    . ASN C  2  376 ? 71.735 18.677  5.159   1.00 48.63  ?  408 ASN C CB    1 
ATOM   9763  C  CG    . ASN C  2  376 ? 72.744 18.751  6.323   1.00 54.07  ?  408 ASN C CG    1 
ATOM   9764  O  OD1   . ASN C  2  376 ? 73.759 19.465  6.262   1.00 59.25  ?  408 ASN C OD1   1 
ATOM   9765  N  ND2   . ASN C  2  376 ? 72.463 17.990  7.397   1.00 54.57  ?  408 ASN C ND2   1 
ATOM   9766  N  N     . TYR C  2  377 ? 69.460 19.683  3.367   1.00 41.66  ?  409 TYR C N     1 
ATOM   9767  C  CA    . TYR C  2  377 ? 68.387 19.455  2.390   1.00 42.59  ?  409 TYR C CA    1 
ATOM   9768  C  C     . TYR C  2  377 ? 67.930 20.714  1.637   1.00 42.08  ?  409 TYR C C     1 
ATOM   9769  O  O     . TYR C  2  377 ? 67.230 20.595  0.637   1.00 43.30  ?  409 TYR C O     1 
ATOM   9770  C  CB    . TYR C  2  377 ? 67.131 18.920  3.102   1.00 46.94  ?  409 TYR C CB    1 
ATOM   9771  C  CG    . TYR C  2  377 ? 67.141 17.477  3.615   1.00 53.20  ?  409 TYR C CG    1 
ATOM   9772  C  CD1   . TYR C  2  377 ? 67.986 16.491  3.056   1.00 56.98  ?  409 TYR C CD1   1 
ATOM   9773  C  CD2   . TYR C  2  377 ? 66.242 17.072  4.626   1.00 53.85  ?  409 TYR C CD2   1 
ATOM   9774  C  CE1   . TYR C  2  377 ? 67.963 15.170  3.511   1.00 54.47  ?  409 TYR C CE1   1 
ATOM   9775  C  CE2   . TYR C  2  377 ? 66.211 15.751  5.075   1.00 53.83  ?  409 TYR C CE2   1 
ATOM   9776  C  CZ    . TYR C  2  377 ? 67.074 14.811  4.517   1.00 52.39  ?  409 TYR C CZ    1 
ATOM   9777  O  OH    . TYR C  2  377 ? 67.059 13.515  4.957   1.00 48.46  ?  409 TYR C OH    1 
ATOM   9778  N  N     . PHE C  2  378 ? 68.259 21.906  2.139   1.00 40.09  ?  410 PHE C N     1 
ATOM   9779  C  CA    . PHE C  2  378 ? 67.966 23.180  1.454   1.00 36.14  ?  410 PHE C CA    1 
ATOM   9780  C  C     . PHE C  2  378 ? 68.741 23.323  0.112   1.00 35.81  ?  410 PHE C C     1 
ATOM   9781  O  O     . PHE C  2  378 ? 68.161 23.790  -0.869  1.00 37.52  ?  410 PHE C O     1 
ATOM   9782  C  CB    . PHE C  2  378 ? 68.241 24.350  2.417   1.00 35.24  ?  410 PHE C CB    1 
ATOM   9783  C  CG    . PHE C  2  378 ? 68.168 25.718  1.786   1.00 35.20  ?  410 PHE C CG    1 
ATOM   9784  C  CD1   . PHE C  2  378 ? 66.954 26.341  1.563   1.00 36.01  ?  410 PHE C CD1   1 
ATOM   9785  C  CD2   . PHE C  2  378 ? 69.326 26.398  1.450   1.00 35.02  ?  410 PHE C CD2   1 
ATOM   9786  C  CE1   . PHE C  2  378 ? 66.903 27.596  0.984   1.00 35.97  ?  410 PHE C CE1   1 
ATOM   9787  C  CE2   . PHE C  2  378 ? 69.280 27.657  0.886   1.00 34.87  ?  410 PHE C CE2   1 
ATOM   9788  C  CZ    . PHE C  2  378 ? 68.068 28.260  0.656   1.00 35.60  ?  410 PHE C CZ    1 
ATOM   9789  N  N     . PHE C  2  379 ? 70.019 22.903  0.053   1.00 32.55  ?  411 PHE C N     1 
ATOM   9790  C  CA    . PHE C  2  379 ? 70.783 22.824  -1.219  1.00 29.74  ?  411 PHE C CA    1 
ATOM   9791  C  C     . PHE C  2  379 ? 70.709 21.441  -1.837  1.00 27.80  ?  411 PHE C C     1 
ATOM   9792  O  O     . PHE C  2  379 ? 71.625 21.014  -2.539  1.00 26.93  ?  411 PHE C O     1 
ATOM   9793  C  CB    . PHE C  2  379 ? 72.252 23.134  -0.990  1.00 30.83  ?  411 PHE C CB    1 
ATOM   9794  C  CG    . PHE C  2  379 ? 72.489 24.445  -0.326  1.00 32.95  ?  411 PHE C CG    1 
ATOM   9795  C  CD1   . PHE C  2  379 ? 72.474 25.628  -1.069  1.00 32.36  ?  411 PHE C CD1   1 
ATOM   9796  C  CD2   . PHE C  2  379 ? 72.725 24.511  1.063   1.00 32.92  ?  411 PHE C CD2   1 
ATOM   9797  C  CE1   . PHE C  2  379 ? 72.683 26.855  -0.439  1.00 32.21  ?  411 PHE C CE1   1 
ATOM   9798  C  CE2   . PHE C  2  379 ? 72.946 25.730  1.680   1.00 31.21  ?  411 PHE C CE2   1 
ATOM   9799  C  CZ    . PHE C  2  379 ? 72.923 26.904  0.932   1.00 30.98  ?  411 PHE C CZ    1 
ATOM   9800  N  N     . VAL C  2  380 ? 69.614 20.755  -1.528  1.00 26.56  ?  412 VAL C N     1 
ATOM   9801  C  CA    . VAL C  2  380 ? 69.252 19.403  -1.987  1.00 24.85  ?  412 VAL C CA    1 
ATOM   9802  C  C     . VAL C  2  380 ? 70.301 18.292  -1.707  1.00 25.12  ?  412 VAL C C     1 
ATOM   9803  O  O     . VAL C  2  380 ? 70.608 17.470  -2.563  1.00 24.66  ?  412 VAL C O     1 
ATOM   9804  C  CB    . VAL C  2  380 ? 68.734 19.452  -3.441  1.00 22.51  ?  412 VAL C CB    1 
ATOM   9805  C  CG1   . VAL C  2  380 ? 68.085 18.138  -3.804  1.00 22.74  ?  412 VAL C CG1   1 
ATOM   9806  C  CG2   . VAL C  2  380 ? 67.732 20.574  -3.605  1.00 21.16  ?  412 VAL C CG2   1 
ATOM   9807  N  N     . SER C  2  381 ? 70.799 18.258  -0.475  1.00 26.79  ?  413 SER C N     1 
ATOM   9808  C  CA    . SER C  2  381 ? 71.886 17.356  -0.075  1.00 30.12  ?  413 SER C CA    1 
ATOM   9809  C  C     . SER C  2  381 ? 73.213 17.556  -0.907  1.00 32.77  ?  413 SER C C     1 
ATOM   9810  O  O     . SER C  2  381 ? 74.110 16.678  -0.880  1.00 35.16  ?  413 SER C O     1 
ATOM   9811  C  CB    . SER C  2  381 ? 71.413 15.865  -0.077  1.00 30.58  ?  413 SER C CB    1 
ATOM   9812  O  OG    . SER C  2  381 ? 70.501 15.538  0.978   1.00 30.34  ?  413 SER C OG    1 
ATOM   9813  N  N     . TYR C  2  382 ? 73.356 18.700  -1.603  1.00 33.73  ?  414 TYR C N     1 
ATOM   9814  C  CA    . TYR C  2  382 ? 74.482 18.920  -2.546  1.00 35.52  ?  414 TYR C CA    1 
ATOM   9815  C  C     . TYR C  2  382 ? 75.818 18.574  -1.864  1.00 39.77  ?  414 TYR C C     1 
ATOM   9816  O  O     . TYR C  2  382 ? 76.426 17.532  -2.173  1.00 37.63  ?  414 TYR C O     1 
ATOM   9817  C  CB    . TYR C  2  382 ? 74.472 20.360  -3.188  1.00 34.61  ?  414 TYR C CB    1 
ATOM   9818  C  CG    . TYR C  2  382 ? 75.774 20.736  -3.960  1.00 32.50  ?  414 TYR C CG    1 
ATOM   9819  C  CD1   . TYR C  2  382 ? 76.161 20.032  -5.120  1.00 30.76  ?  414 TYR C CD1   1 
ATOM   9820  C  CD2   . TYR C  2  382 ? 76.605 21.778  -3.514  1.00 29.88  ?  414 TYR C CD2   1 
ATOM   9821  C  CE1   . TYR C  2  382 ? 77.329 20.343  -5.783  1.00 29.88  ?  414 TYR C CE1   1 
ATOM   9822  C  CE2   . TYR C  2  382 ? 77.765 22.095  -4.172  1.00 28.84  ?  414 TYR C CE2   1 
ATOM   9823  C  CZ    . TYR C  2  382 ? 78.127 21.370  -5.293  1.00 28.80  ?  414 TYR C CZ    1 
ATOM   9824  O  OH    . TYR C  2  382 ? 79.285 21.675  -5.933  1.00 25.48  ?  414 TYR C OH    1 
ATOM   9825  N  N     . ASP C  2  383 ? 76.241 19.453  -0.945  1.00 49.32  ?  415 ASP C N     1 
ATOM   9826  C  CA    . ASP C  2  383 ? 77.284 19.171  0.046   1.00 57.73  ?  415 ASP C CA    1 
ATOM   9827  C  C     . ASP C  2  383 ? 76.591 18.884  1.384   1.00 62.93  ?  415 ASP C C     1 
ATOM   9828  O  O     . ASP C  2  383 ? 75.663 19.616  1.792   1.00 62.27  ?  415 ASP C O     1 
ATOM   9829  C  CB    . ASP C  2  383 ? 78.271 20.342  0.196   1.00 59.45  ?  415 ASP C CB    1 
ATOM   9830  C  CG    . ASP C  2  383 ? 79.459 19.999  1.104   1.00 58.63  ?  415 ASP C CG    1 
ATOM   9831  O  OD1   . ASP C  2  383 ? 79.935 18.848  1.039   1.00 54.07  ?  415 ASP C OD1   1 
ATOM   9832  O  OD2   . ASP C  2  383 ? 79.916 20.878  1.877   1.00 60.81  -1 415 ASP C OD2   1 
ATOM   9833  N  N     . SER C  2  384 ? 77.030 17.800  2.030   1.00 66.59  ?  416 SER C N     1 
ATOM   9834  C  CA    . SER C  2  384 ? 76.433 17.322  3.271   1.00 70.14  ?  416 SER C CA    1 
ATOM   9835  C  C     . SER C  2  384 ? 77.321 17.619  4.484   1.00 70.52  ?  416 SER C C     1 
ATOM   9836  O  O     . SER C  2  384 ? 76.859 17.579  5.632   1.00 69.74  ?  416 SER C O     1 
ATOM   9837  C  CB    . SER C  2  384 ? 76.116 15.833  3.150   1.00 74.35  ?  416 SER C CB    1 
ATOM   9838  O  OG    . SER C  2  384 ? 74.912 15.642  2.421   1.00 77.07  ?  416 SER C OG    1 
ATOM   9839  N  N     . SER C  2  385 ? 78.585 17.943  4.224   1.00 68.93  ?  417 SER C N     1 
ATOM   9840  C  CA    . SER C  2  385 ? 79.397 18.671  5.195   1.00 67.32  ?  417 SER C CA    1 
ATOM   9841  C  C     . SER C  2  385 ? 79.227 20.216  5.021   1.00 68.69  ?  417 SER C C     1 
ATOM   9842  O  O     . SER C  2  385 ? 80.148 20.997  5.300   1.00 69.00  ?  417 SER C O     1 
ATOM   9843  C  CB    . SER C  2  385 ? 80.863 18.236  5.077   1.00 64.61  ?  417 SER C CB    1 
ATOM   9844  O  OG    . SER C  2  385 ? 81.531 18.946  4.057   1.00 61.29  ?  417 SER C OG    1 
ATOM   9845  N  N     . VAL C  2  386 ? 78.025 20.644  4.683   1.00 62.84  ?  418 VAL C N     1 
ATOM   9846  C  CA    . VAL C  2  386 ? 77.742 22.042  4.566   1.00 59.40  ?  418 VAL C CA    1 
ATOM   9847  C  C     . VAL C  2  386 ? 77.404 22.516  5.950   1.00 55.20  ?  418 VAL C C     1 
ATOM   9848  O  O     . VAL C  2  386 ? 76.783 21.811  6.699   1.00 55.58  ?  418 VAL C O     1 
ATOM   9849  C  CB    . VAL C  2  386 ? 76.474 22.224  3.751   1.00 64.13  ?  418 VAL C CB    1 
ATOM   9850  C  CG1   . VAL C  2  386 ? 75.383 21.352  4.313   1.00 64.90  ?  418 VAL C CG1   1 
ATOM   9851  C  CG2   . VAL C  2  386 ? 76.014 23.667  3.746   1.00 66.05  ?  418 VAL C CG2   1 
ATOM   9852  N  N     . THR C  2  387 ? 77.774 23.735  6.272   1.00 48.21  ?  419 THR C N     1 
ATOM   9853  C  CA    . THR C  2  387 ? 77.476 24.344  7.575   1.00 41.70  ?  419 THR C CA    1 
ATOM   9854  C  C     . THR C  2  387 ? 76.819 25.720  7.441   1.00 38.13  ?  419 THR C C     1 
ATOM   9855  O  O     . THR C  2  387 ? 76.626 26.241  6.344   1.00 37.23  ?  419 THR C O     1 
ATOM   9856  C  CB    . THR C  2  387 ? 78.752 24.475  8.424   1.00 42.24  ?  419 THR C CB    1 
ATOM   9857  O  OG1   . THR C  2  387 ? 78.401 24.793  9.765   1.00 39.57  ?  419 THR C OG1   1 
ATOM   9858  C  CG2   . THR C  2  387 ? 79.677 25.576  7.885   1.00 44.11  ?  419 THR C CG2   1 
ATOM   9859  N  N     . CYS C  2  388 ? 76.508 26.307  8.583   1.00 37.81  ?  420 CYS C N     1 
ATOM   9860  C  CA    . CYS C  2  388 ? 75.711 27.530  8.670   1.00 40.59  ?  420 CYS C CA    1 
ATOM   9861  C  C     . CYS C  2  388 ? 76.034 28.303  9.974   1.00 39.46  ?  420 CYS C C     1 
ATOM   9862  O  O     . CYS C  2  388 ? 76.126 27.674  11.017  1.00 41.04  ?  420 CYS C O     1 
ATOM   9863  C  CB    . CYS C  2  388 ? 74.224 27.159  8.665   1.00 41.48  ?  420 CYS C CB    1 
ATOM   9864  S  SG    . CYS C  2  388 ? 73.158 28.607  8.462   1.00 50.80  ?  420 CYS C SG    1 
ATOM   9865  N  N     . ASP C  2  389 ? 76.200 29.635  9.926   1.00 37.35  ?  421 ASP C N     1 
ATOM   9866  C  CA    . ASP C  2  389 ? 76.527 30.450  11.127  1.00 35.59  ?  421 ASP C CA    1 
ATOM   9867  C  C     . ASP C  2  389 ? 75.284 31.163  11.644  1.00 35.42  ?  421 ASP C C     1 
ATOM   9868  O  O     . ASP C  2  389 ? 74.306 31.214  10.932  1.00 34.58  ?  421 ASP C O     1 
ATOM   9869  C  CB    . ASP C  2  389 ? 77.606 31.475  10.807  1.00 34.93  ?  421 ASP C CB    1 
ATOM   9870  C  CG    . ASP C  2  389 ? 77.094 32.549  9.938   1.00 34.12  ?  421 ASP C CG    1 
ATOM   9871  O  OD1   . ASP C  2  389 ? 76.536 32.178  8.907   1.00 37.18  ?  421 ASP C OD1   1 
ATOM   9872  O  OD2   . ASP C  2  389 ? 77.206 33.737  10.271  1.00 33.38  -1 421 ASP C OD2   1 
ATOM   9873  N  N     . LYS C  2  390 ? 75.330 31.724  12.861  1.00 39.53  ?  422 LYS C N     1 
ATOM   9874  C  CA    . LYS C  2  390 ? 74.099 32.210  13.565  1.00 43.85  ?  422 LYS C CA    1 
ATOM   9875  C  C     . LYS C  2  390 ? 73.246 33.154  12.700  1.00 45.47  ?  422 LYS C C     1 
ATOM   9876  O  O     . LYS C  2  390 ? 72.011 33.093  12.762  1.00 49.07  ?  422 LYS C O     1 
ATOM   9877  C  CB    . LYS C  2  390 ? 74.368 32.957  14.895  1.00 45.31  ?  422 LYS C CB    1 
ATOM   9878  C  CG    . LYS C  2  390 ? 75.338 32.346  15.896  1.00 48.48  ?  422 LYS C CG    1 
ATOM   9879  C  CD    . LYS C  2  390 ? 76.054 33.431  16.721  1.00 54.12  ?  422 LYS C CD    1 
ATOM   9880  C  CE    . LYS C  2  390 ? 76.670 34.557  15.861  1.00 55.50  ?  422 LYS C CE    1 
ATOM   9881  N  NZ    . LYS C  2  390 ? 77.875 35.246  16.422  1.00 55.25  1  422 LYS C NZ    1 
ATOM   9882  N  N     . THR C  2  391 ? 73.898 34.027  11.920  1.00 43.16  ?  423 THR C N     1 
ATOM   9883  C  CA    . THR C  2  391 ? 73.205 35.022  11.087  1.00 40.66  ?  423 THR C CA    1 
ATOM   9884  C  C     . THR C  2  391 ? 72.402 34.365  9.937   1.00 43.83  ?  423 THR C C     1 
ATOM   9885  O  O     . THR C  2  391 ? 71.159 34.462  9.920   1.00 42.98  ?  423 THR C O     1 
ATOM   9886  C  CB    . THR C  2  391 ? 74.213 36.055  10.579  1.00 37.94  ?  423 THR C CB    1 
ATOM   9887  O  OG1   . THR C  2  391 ? 75.081 36.379  11.658  1.00 34.80  ?  423 THR C OG1   1 
ATOM   9888  C  CG2   . THR C  2  391 ? 73.534 37.308  10.116  1.00 37.28  ?  423 THR C CG2   1 
ATOM   9889  N  N     . CYS C  2  392 ? 73.087 33.664  9.021   1.00 45.70  ?  424 CYS C N     1 
ATOM   9890  C  CA    . CYS C  2  392 ? 72.405 32.818  8.020   1.00 48.20  ?  424 CYS C CA    1 
ATOM   9891  C  C     . CYS C  2  392 ? 71.231 32.089  8.627   1.00 44.35  ?  424 CYS C C     1 
ATOM   9892  O  O     . CYS C  2  392 ? 70.118 32.185  8.118   1.00 48.26  ?  424 CYS C O     1 
ATOM   9893  C  CB    . CYS C  2  392 ? 73.343 31.801  7.372   1.00 52.14  ?  424 CYS C CB    1 
ATOM   9894  S  SG    . CYS C  2  392 ? 74.229 32.511  5.958   1.00 68.48  ?  424 CYS C SG    1 
ATOM   9895  N  N     . LYS C  2  393 ? 71.466 31.385  9.729   1.00 38.78  ?  425 LYS C N     1 
ATOM   9896  C  CA    . LYS C  2  393 ? 70.377 30.725  10.422  1.00 35.53  ?  425 LYS C CA    1 
ATOM   9897  C  C     . LYS C  2  393 ? 69.281 31.692  10.876  1.00 34.60  ?  425 LYS C C     1 
ATOM   9898  O  O     . LYS C  2  393 ? 68.116 31.361  10.762  1.00 38.16  ?  425 LYS C O     1 
ATOM   9899  C  CB    . LYS C  2  393 ? 70.871 29.898  11.602  1.00 34.57  ?  425 LYS C CB    1 
ATOM   9900  C  CG    . LYS C  2  393 ? 69.726 29.439  12.501  1.00 35.52  ?  425 LYS C CG    1 
ATOM   9901  C  CD    . LYS C  2  393 ? 70.067 28.285  13.416  1.00 34.00  ?  425 LYS C CD    1 
ATOM   9902  C  CE    . LYS C  2  393 ? 68.966 28.091  14.446  1.00 33.52  ?  425 LYS C CE    1 
ATOM   9903  N  NZ    . LYS C  2  393 ? 69.161 26.775  15.112  1.00 34.39  1  425 LYS C NZ    1 
ATOM   9904  N  N     . ALA C  2  394 ? 69.623 32.863  11.394  1.00 31.38  ?  426 ALA C N     1 
ATOM   9905  C  CA    . ALA C  2  394 ? 68.598 33.795  11.804  1.00 31.08  ?  426 ALA C CA    1 
ATOM   9906  C  C     . ALA C  2  394 ? 67.737 34.133  10.626  1.00 33.33  ?  426 ALA C C     1 
ATOM   9907  O  O     . ALA C  2  394 ? 66.513 34.169  10.736  1.00 32.55  ?  426 ALA C O     1 
ATOM   9908  C  CB    . ALA C  2  394 ? 69.215 35.057  12.320  1.00 31.74  ?  426 ALA C CB    1 
ATOM   9909  N  N     . PHE C  2  395 ? 68.395 34.387  9.493   1.00 36.89  ?  427 PHE C N     1 
ATOM   9910  C  CA    . PHE C  2  395 ? 67.720 34.819  8.245   1.00 39.56  ?  427 PHE C CA    1 
ATOM   9911  C  C     . PHE C  2  395 ? 66.822 33.759  7.673   1.00 38.57  ?  427 PHE C C     1 
ATOM   9912  O  O     . PHE C  2  395 ? 65.778 34.079  7.095   1.00 39.14  ?  427 PHE C O     1 
ATOM   9913  C  CB    . PHE C  2  395 ? 68.722 35.145  7.124   1.00 40.23  ?  427 PHE C CB    1 
ATOM   9914  C  CG    . PHE C  2  395 ? 69.587 36.324  7.390   1.00 38.81  ?  427 PHE C CG    1 
ATOM   9915  C  CD1   . PHE C  2  395 ? 69.227 37.288  8.334   1.00 38.28  ?  427 PHE C CD1   1 
ATOM   9916  C  CD2   . PHE C  2  395 ? 70.756 36.484  6.656   1.00 39.30  ?  427 PHE C CD2   1 
ATOM   9917  C  CE1   . PHE C  2  395 ? 70.035 38.373  8.554   1.00 40.26  ?  427 PHE C CE1   1 
ATOM   9918  C  CE2   . PHE C  2  395 ? 71.573 37.570  6.869   1.00 40.33  ?  427 PHE C CE2   1 
ATOM   9919  C  CZ    . PHE C  2  395 ? 71.208 38.519  7.818   1.00 41.91  ?  427 PHE C CZ    1 
ATOM   9920  N  N     . GLN C  2  396 ? 67.312 32.521  7.747   1.00 37.46  ?  428 GLN C N     1 
ATOM   9921  C  CA    . GLN C  2  396 ? 66.556 31.338  7.372   1.00 38.66  ?  428 GLN C CA    1 
ATOM   9922  C  C     . GLN C  2  396 ? 65.319 31.218  8.263   1.00 37.69  ?  428 GLN C C     1 
ATOM   9923  O  O     . GLN C  2  396 ? 64.204 31.011  7.775   1.00 38.06  ?  428 GLN C O     1 
ATOM   9924  C  CB    . GLN C  2  396 ? 67.422 30.073  7.507   1.00 40.04  ?  428 GLN C CB    1 
ATOM   9925  C  CG    . GLN C  2  396 ? 68.311 29.731  6.312   1.00 41.29  ?  428 GLN C CG    1 
ATOM   9926  C  CD    . GLN C  2  396 ? 67.576 29.077  5.137   1.00 43.15  ?  428 GLN C CD    1 
ATOM   9927  O  OE1   . GLN C  2  396 ? 66.461 28.568  5.268   1.00 44.13  ?  428 GLN C OE1   1 
ATOM   9928  N  NE2   . GLN C  2  396 ? 68.214 29.094  3.971   1.00 45.46  ?  428 GLN C NE2   1 
ATOM   9929  N  N     . ILE C  2  397 ? 65.527 31.364  9.569   1.00 36.06  ?  429 ILE C N     1 
ATOM   9930  C  CA    . ILE C  2  397 ? 64.454 31.214  10.527  1.00 34.82  ?  429 ILE C CA    1 
ATOM   9931  C  C     . ILE C  2  397 ? 63.366 32.241  10.310  1.00 33.69  ?  429 ILE C C     1 
ATOM   9932  O  O     . ILE C  2  397 ? 62.193 31.860  10.227  1.00 33.66  ?  429 ILE C O     1 
ATOM   9933  C  CB    . ILE C  2  397 ? 64.960 31.309  11.970  1.00 35.23  ?  429 ILE C CB    1 
ATOM   9934  C  CG1   . ILE C  2  397 ? 65.762 30.060  12.333  1.00 35.04  ?  429 ILE C CG1   1 
ATOM   9935  C  CG2   . ILE C  2  397 ? 63.796 31.443  12.936  1.00 36.85  ?  429 ILE C CG2   1 
ATOM   9936  C  CD1   . ILE C  2  397 ? 65.021 28.759  12.146  1.00 33.95  ?  429 ILE C CD1   1 
ATOM   9937  N  N     . CYS C  2  398 ? 63.738 33.519  10.224  1.00 31.34  ?  430 CYS C N     1 
ATOM   9938  C  CA    . CYS C  2  398 ? 62.753 34.573  10.077  1.00 31.22  ?  430 CYS C CA    1 
ATOM   9939  C  C     . CYS C  2  398 ? 61.887 34.402  8.863   1.00 32.62  ?  430 CYS C C     1 
ATOM   9940  O  O     . CYS C  2  398 ? 60.692 34.713  8.904   1.00 31.74  ?  430 CYS C O     1 
ATOM   9941  C  CB    . CYS C  2  398 ? 63.427 35.912  9.972   1.00 32.31  ?  430 CYS C CB    1 
ATOM   9942  S  SG    . CYS C  2  398 ? 63.974 36.430  11.580  1.00 38.85  ?  430 CYS C SG    1 
ATOM   9943  N  N     . ALA C  2  399 ? 62.511 33.923  7.783   1.00 33.34  ?  431 ALA C N     1 
ATOM   9944  C  CA    . ALA C  2  399 ? 61.887 33.784  6.472   1.00 31.96  ?  431 ALA C CA    1 
ATOM   9945  C  C     . ALA C  2  399 ? 60.877 32.667  6.484   1.00 32.16  ?  431 ALA C C     1 
ATOM   9946  O  O     . ALA C  2  399 ? 59.819 32.775  5.876   1.00 34.14  ?  431 ALA C O     1 
ATOM   9947  C  CB    . ALA C  2  399 ? 62.953 33.493  5.436   1.00 32.12  ?  431 ALA C CB    1 
ATOM   9948  N  N     . ILE C  2  400 ? 61.210 31.586  7.176   1.00 32.57  ?  432 ILE C N     1 
ATOM   9949  C  CA    . ILE C  2  400 ? 60.292 30.457  7.303   1.00 34.16  ?  432 ILE C CA    1 
ATOM   9950  C  C     . ILE C  2  400 ? 59.025 30.825  8.080   1.00 33.64  ?  432 ILE C C     1 
ATOM   9951  O  O     . ILE C  2  400 ? 57.955 30.291  7.786   1.00 33.55  ?  432 ILE C O     1 
ATOM   9952  C  CB    . ILE C  2  400 ? 60.948 29.230  7.976   1.00 34.93  ?  432 ILE C CB    1 
ATOM   9953  C  CG1   . ILE C  2  400 ? 62.194 28.793  7.200   1.00 36.44  ?  432 ILE C CG1   1 
ATOM   9954  C  CG2   . ILE C  2  400 ? 59.972 28.053  8.036   1.00 34.17  ?  432 ILE C CG2   1 
ATOM   9955  C  CD1   . ILE C  2  400 ? 63.218 28.134  8.091   1.00 37.68  ?  432 ILE C CD1   1 
ATOM   9956  N  N     . MET C  2  401 ? 59.146 31.725  9.059   1.00 33.22  ?  433 MET C N     1 
ATOM   9957  C  CA    . MET C  2  401 ? 58.027 32.071  9.934   1.00 31.79  ?  433 MET C CA    1 
ATOM   9958  C  C     . MET C  2  401 ? 57.376 33.418  9.640   1.00 30.29  ?  433 MET C C     1 
ATOM   9959  O  O     . MET C  2  401 ? 56.287 33.664  10.109  1.00 31.78  ?  433 MET C O     1 
ATOM   9960  C  CB    . MET C  2  401 ? 58.478 32.004  11.379  1.00 32.42  ?  433 MET C CB    1 
ATOM   9961  C  CG    . MET C  2  401 ? 58.368 30.609  11.935  1.00 35.32  ?  433 MET C CG    1 
ATOM   9962  S  SD    . MET C  2  401 ? 59.596 30.237  13.210  1.00 41.77  ?  433 MET C SD    1 
ATOM   9963  C  CE    . MET C  2  401 ? 58.496 29.299  14.273  1.00 39.20  ?  433 MET C CE    1 
ATOM   9964  N  N     . ASN C  2  402 ? 58.009 34.285  8.863   1.00 28.35  ?  434 ASN C N     1 
ATOM   9965  C  CA    . ASN C  2  402 ? 57.470 35.614  8.647   1.00 27.46  ?  434 ASN C CA    1 
ATOM   9966  C  C     . ASN C  2  402 ? 57.480 36.014  7.176   1.00 29.68  ?  434 ASN C C     1 
ATOM   9967  O  O     . ASN C  2  402 ? 58.517 36.068  6.498   1.00 29.65  ?  434 ASN C O     1 
ATOM   9968  C  CB    . ASN C  2  402 ? 58.230 36.610  9.511   1.00 26.79  ?  434 ASN C CB    1 
ATOM   9969  C  CG    . ASN C  2  402 ? 58.440 36.095  10.929  1.00 26.17  ?  434 ASN C CG    1 
ATOM   9970  O  OD1   . ASN C  2  402 ? 57.480 35.990  11.715  1.00 25.46  ?  434 ASN C OD1   1 
ATOM   9971  N  ND2   . ASN C  2  402 ? 59.688 35.731  11.254  1.00 24.94  ?  434 ASN C ND2   1 
ATOM   9972  N  N     . LEU C  2  403 ? 56.291 36.283  6.677   1.00 33.05  ?  435 LEU C N     1 
ATOM   9973  C  CA    . LEU C  2  403 ? 56.096 36.591  5.273   1.00 34.38  ?  435 LEU C CA    1 
ATOM   9974  C  C     . LEU C  2  403 ? 55.725 38.052  4.958   1.00 33.14  ?  435 LEU C C     1 
ATOM   9975  O  O     . LEU C  2  403 ? 55.784 38.434  3.811   1.00 30.20  ?  435 LEU C O     1 
ATOM   9976  C  CB    . LEU C  2  403 ? 55.032 35.642  4.736   1.00 35.81  ?  435 LEU C CB    1 
ATOM   9977  C  CG    . LEU C  2  403 ? 55.576 34.241  4.417   1.00 37.92  ?  435 LEU C CG    1 
ATOM   9978  C  CD1   . LEU C  2  403 ? 56.161 33.482  5.597   1.00 36.34  ?  435 LEU C CD1   1 
ATOM   9979  C  CD2   . LEU C  2  403 ? 54.448 33.442  3.781   1.00 40.41  ?  435 LEU C CD2   1 
ATOM   9980  N  N     . ASP C  2  404 ? 55.335 38.847  5.963   1.00 36.21  ?  436 ASP C N     1 
ATOM   9981  C  CA    . ASP C  2  404 ? 54.984 40.266  5.759   1.00 38.42  ?  436 ASP C CA    1 
ATOM   9982  C  C     . ASP C  2  404 ? 56.010 41.146  6.453   1.00 39.90  ?  436 ASP C C     1 
ATOM   9983  O  O     . ASP C  2  404 ? 56.842 40.649  7.197   1.00 39.60  ?  436 ASP C O     1 
ATOM   9984  C  CB    . ASP C  2  404 ? 53.527 40.606  6.181   1.00 38.35  ?  436 ASP C CB    1 
ATOM   9985  C  CG    . ASP C  2  404 ? 53.273 40.465  7.681   1.00 38.60  ?  436 ASP C CG    1 
ATOM   9986  O  OD1   . ASP C  2  404 ? 53.779 41.296  8.483   1.00 38.14  ?  436 ASP C OD1   1 
ATOM   9987  O  OD2   . ASP C  2  404 ? 52.521 39.536  8.041   1.00 35.86  -1 436 ASP C OD2   1 
ATOM   9988  N  N     . ASN C  2  405 ? 55.949 42.448  6.196   1.00 42.88  ?  437 ASN C N     1 
ATOM   9989  C  CA    . ASN C  2  405 ? 57.027 43.328  6.563   1.00 44.47  ?  437 ASN C CA    1 
ATOM   9990  C  C     . ASN C  2  405 ? 57.119 43.449  8.033   1.00 44.42  ?  437 ASN C C     1 
ATOM   9991  O  O     . ASN C  2  405 ? 58.206 43.398  8.599   1.00 46.06  ?  437 ASN C O     1 
ATOM   9992  C  CB    . ASN C  2  405 ? 56.837 44.725  6.014   1.00 47.35  ?  437 ASN C CB    1 
ATOM   9993  C  CG    . ASN C  2  405 ? 57.948 45.660  6.461   1.00 51.05  ?  437 ASN C CG    1 
ATOM   9994  O  OD1   . ASN C  2  405 ? 59.002 45.762  5.819   1.00 57.24  ?  437 ASN C OD1   1 
ATOM   9995  N  ND2   . ASN C  2  405 ? 57.747 46.305  7.591   1.00 51.14  ?  437 ASN C ND2   1 
ATOM   9996  N  N     . ILE C  2  406 ? 55.969 43.648  8.652   1.00 44.81  ?  438 ILE C N     1 
ATOM   9997  C  CA    . ILE C  2  406 ? 55.931 43.844  10.095  1.00 48.55  ?  438 ILE C CA    1 
ATOM   9998  C  C     . ILE C  2  406 ? 56.585 42.670  10.843  1.00 44.72  ?  438 ILE C C     1 
ATOM   9999  O  O     . ILE C  2  406 ? 57.549 42.869  11.586  1.00 41.46  ?  438 ILE C O     1 
ATOM   10000 C  CB    . ILE C  2  406 ? 54.479 44.192  10.583  1.00 53.42  ?  438 ILE C CB    1 
ATOM   10001 C  CG1   . ILE C  2  406 ? 54.353 45.711  10.766  1.00 55.08  ?  438 ILE C CG1   1 
ATOM   10002 C  CG2   . ILE C  2  406 ? 54.061 43.477  11.877  1.00 53.91  ?  438 ILE C CG2   1 
ATOM   10003 C  CD1   . ILE C  2  406 ? 55.259 46.320  11.833  1.00 57.23  ?  438 ILE C CD1   1 
ATOM   10004 N  N     . SER C  2  407 ? 56.081 41.458  10.610  1.00 41.57  ?  439 SER C N     1 
ATOM   10005 C  CA    . SER C  2  407 ? 56.551 40.254  11.315  1.00 39.67  ?  439 SER C CA    1 
ATOM   10006 C  C     . SER C  2  407 ? 58.037 39.839  11.022  1.00 37.99  ?  439 SER C C     1 
ATOM   10007 O  O     . SER C  2  407 ? 58.701 39.261  11.903  1.00 35.50  ?  439 SER C O     1 
ATOM   10008 C  CB    . SER C  2  407 ? 55.565 39.091  11.074  1.00 38.82  ?  439 SER C CB    1 
ATOM   10009 O  OG    . SER C  2  407 ? 55.039 39.097  9.741   1.00 39.16  ?  439 SER C OG    1 
ATOM   10010 N  N     . TYR C  2  408 ? 58.544 40.157  9.818   1.00 35.32  ?  440 TYR C N     1 
ATOM   10011 C  CA    . TYR C  2  408 ? 59.914 39.832  9.417   1.00 33.74  ?  440 TYR C CA    1 
ATOM   10012 C  C     . TYR C  2  408 ? 60.967 40.700  10.040  1.00 37.86  ?  440 TYR C C     1 
ATOM   10013 O  O     . TYR C  2  408 ? 62.135 40.307  10.092  1.00 41.31  ?  440 TYR C O     1 
ATOM   10014 C  CB    . TYR C  2  408 ? 60.117 40.006  7.940   1.00 32.05  ?  440 TYR C CB    1 
ATOM   10015 C  CG    . TYR C  2  408 ? 61.470 39.524  7.548   1.00 30.80  ?  440 TYR C CG    1 
ATOM   10016 C  CD1   . TYR C  2  408 ? 61.682 38.181  7.357   1.00 30.94  ?  440 TYR C CD1   1 
ATOM   10017 C  CD2   . TYR C  2  408 ? 62.546 40.392  7.416   1.00 30.69  ?  440 TYR C CD2   1 
ATOM   10018 C  CE1   . TYR C  2  408 ? 62.913 37.684  7.008   1.00 31.94  ?  440 TYR C CE1   1 
ATOM   10019 C  CE2   . TYR C  2  408 ? 63.808 39.912  7.072   1.00 31.92  ?  440 TYR C CE2   1 
ATOM   10020 C  CZ    . TYR C  2  408 ? 63.986 38.535  6.865   1.00 33.86  ?  440 TYR C CZ    1 
ATOM   10021 O  OH    . TYR C  2  408 ? 65.200 37.926  6.505   1.00 35.06  ?  440 TYR C OH    1 
ATOM   10022 N  N     . ALA C  2  409 ? 60.581 41.909  10.435  1.00 41.56  ?  441 ALA C N     1 
ATOM   10023 C  CA    . ALA C  2  409 ? 61.468 42.797  11.192  1.00 43.70  ?  441 ALA C CA    1 
ATOM   10024 C  C     . ALA C  2  409 ? 61.463 42.428  12.684  1.00 44.50  ?  441 ALA C C     1 
ATOM   10025 O  O     . ALA C  2  409 ? 62.529 42.237  13.270  1.00 42.96  ?  441 ALA C O     1 
ATOM   10026 C  CB    . ALA C  2  409 ? 61.056 44.248  10.990  1.00 44.92  ?  441 ALA C CB    1 
ATOM   10027 N  N     . ASP C  2  410 ? 60.257 42.322  13.263  1.00 45.60  ?  442 ASP C N     1 
ATOM   10028 C  CA    . ASP C  2  410 ? 60.029 41.864  14.647  1.00 47.52  ?  442 ASP C CA    1 
ATOM   10029 C  C     . ASP C  2  410 ? 60.939 40.667  14.928  1.00 46.28  ?  442 ASP C C     1 
ATOM   10030 O  O     . ASP C  2  410 ? 61.468 40.507  16.037  1.00 43.66  ?  442 ASP C O     1 
ATOM   10031 C  CB    . ASP C  2  410 ? 58.529 41.466  14.867  1.00 51.38  ?  442 ASP C CB    1 
ATOM   10032 C  CG    . ASP C  2  410 ? 58.000 41.752  16.323  1.00 55.36  ?  442 ASP C CG    1 
ATOM   10033 O  OD1   . ASP C  2  410 ? 57.059 42.585  16.463  1.00 52.94  ?  442 ASP C OD1   1 
ATOM   10034 O  OD2   . ASP C  2  410 ? 58.502 41.142  17.312  1.00 55.37  -1 442 ASP C OD2   1 
ATOM   10035 N  N     . CYS C  2  411 ? 61.114 39.827  13.911  1.00 45.48  ?  443 CYS C N     1 
ATOM   10036 C  CA    . CYS C  2  411 ? 61.914 38.608  14.036  1.00 45.09  ?  443 CYS C CA    1 
ATOM   10037 C  C     . CYS C  2  411 ? 63.411 38.925  14.141  1.00 46.49  ?  443 CYS C C     1 
ATOM   10038 O  O     . CYS C  2  411 ? 64.123 38.371  14.996  1.00 43.74  ?  443 CYS C O     1 
ATOM   10039 C  CB    . CYS C  2  411 ? 61.593 37.705  12.858  1.00 43.94  ?  443 CYS C CB    1 
ATOM   10040 S  SG    . CYS C  2  411 ? 62.389 36.095  12.828  1.00 43.64  ?  443 CYS C SG    1 
ATOM   10041 N  N     . LEU C  2  412 ? 63.813 39.985  13.473  1.00 49.57  ?  444 LEU C N     1 
ATOM   10042 C  CA    . LEU C  2  412 ? 65.149 40.496  13.566  1.00 51.68  ?  444 LEU C CA    1 
ATOM   10043 C  C     . LEU C  2  412 ? 65.251 41.419  14.771  1.00 57.11  ?  444 LEU C C     1 
ATOM   10044 O  O     . LEU C  2  412 ? 65.677 42.544  14.662  1.00 54.03  ?  444 LEU C O     1 
ATOM   10045 C  CB    . LEU C  2  412 ? 65.464 41.240  12.303  1.00 51.00  ?  444 LEU C CB    1 
ATOM   10046 C  CG    . LEU C  2  412 ? 65.491 40.286  11.125  1.00 49.80  ?  444 LEU C CG    1 
ATOM   10047 C  CD1   . LEU C  2  412 ? 65.803 41.014  9.849   1.00 48.45  ?  444 LEU C CD1   1 
ATOM   10048 C  CD2   . LEU C  2  412 ? 66.586 39.300  11.407  1.00 50.26  ?  444 LEU C CD2   1 
ATOM   10049 N  N     . LYS C  2  413 ? 64.818 40.892  15.917  1.00 66.16  ?  445 LYS C N     1 
ATOM   10050 C  CA    . LYS C  2  413 ? 64.837 41.483  17.253  1.00 65.66  ?  445 LYS C CA    1 
ATOM   10051 C  C     . LYS C  2  413 ? 65.752 40.503  17.906  1.00 66.92  ?  445 LYS C C     1 
ATOM   10052 O  O     . LYS C  2  413 ? 65.536 40.007  18.993  1.00 61.32  ?  445 LYS C O     1 
ATOM   10053 C  CB    . LYS C  2  413 ? 63.464 41.457  17.884  1.00 71.16  ?  445 LYS C CB    1 
ATOM   10054 C  CG    . LYS C  2  413 ? 63.429 41.489  19.416  1.00 72.94  ?  445 LYS C CG    1 
ATOM   10055 C  CD    . LYS C  2  413 ? 62.568 42.615  20.002  1.00 71.64  ?  445 LYS C CD    1 
ATOM   10056 C  CE    . LYS C  2  413 ? 61.086 42.505  19.695  1.00 68.50  ?  445 LYS C CE    1 
ATOM   10057 N  NZ    . LYS C  2  413 ? 60.554 41.182  20.088  1.00 67.43  1  445 LYS C NZ    1 
ATOM   10058 N  N     . GLN C  2  414 ? 66.777 40.196  17.137  1.00 70.14  ?  446 GLN C N     1 
ATOM   10059 C  CA    . GLN C  2  414 ? 67.846 39.233  17.441  1.00 65.45  ?  446 GLN C CA    1 
ATOM   10060 C  C     . GLN C  2  414 ? 69.134 39.913  16.920  1.00 65.03  ?  446 GLN C C     1 
ATOM   10061 O  O     . GLN C  2  414 ? 70.045 40.210  17.695  1.00 59.24  ?  446 GLN C O     1 
ATOM   10062 C  CB    . GLN C  2  414 ? 67.533 37.927  16.717  1.00 61.94  ?  446 GLN C CB    1 
ATOM   10063 C  CG    . GLN C  2  414 ? 68.708 36.962  16.697  1.00 64.21  ?  446 GLN C CG    1 
ATOM   10064 C  CD    . GLN C  2  414 ? 68.280 35.503  16.756  1.00 66.41  ?  446 GLN C CD    1 
ATOM   10065 O  OE1   . GLN C  2  414 ? 67.330 35.109  16.086  1.00 66.23  ?  446 GLN C OE1   1 
ATOM   10066 N  NE2   . GLN C  2  414 ? 68.981 34.694  17.566  1.00 65.48  ?  446 GLN C NE2   1 
ATOM   10067 N  N     . LEU C  2  415 ? 69.167 40.191  15.612  1.00 65.24  ?  447 LEU C N     1 
ATOM   10068 C  CA    . LEU C  2  415 ? 70.236 40.980  15.006  1.00 60.23  ?  447 LEU C CA    1 
ATOM   10069 C  C     . LEU C  2  415 ? 70.168 42.447  15.443  1.00 56.99  ?  447 LEU C C     1 
ATOM   10070 O  O     . LEU C  2  415 ? 70.975 42.875  16.252  1.00 56.03  ?  447 LEU C O     1 
ATOM   10071 C  CB    . LEU C  2  415 ? 70.171 40.924  13.477  1.00 55.77  ?  447 LEU C CB    1 
ATOM   10072 C  CG    . LEU C  2  415 ? 70.698 39.605  12.923  1.00 54.31  ?  447 LEU C CG    1 
ATOM   10073 C  CD1   . LEU C  2  415 ? 69.651 38.493  12.982  1.00 51.13  ?  447 LEU C CD1   1 
ATOM   10074 C  CD2   . LEU C  2  415 ? 71.207 39.858  11.512  1.00 54.45  ?  447 LEU C CD2   1 
HETATM 10075 C  C1    . NAG D  3  .   ? 5.864  22.321  -15.809 1.00 26.64  ?  601 NAG A C1    1 
HETATM 10076 C  C2    . NAG D  3  .   ? 4.301  22.427  -15.637 1.00 27.24  ?  601 NAG A C2    1 
HETATM 10077 C  C3    . NAG D  3  .   ? 3.644  23.679  -16.195 1.00 27.24  ?  601 NAG A C3    1 
HETATM 10078 C  C4    . NAG D  3  .   ? 4.370  24.944  -15.727 1.00 28.55  ?  601 NAG A C4    1 
HETATM 10079 C  C5    . NAG D  3  .   ? 5.817  24.853  -16.278 1.00 28.43  ?  601 NAG A C5    1 
HETATM 10080 C  C6    . NAG D  3  .   ? 6.695  26.009  -15.840 1.00 28.96  ?  601 NAG A C6    1 
HETATM 10081 C  C7    . NAG D  3  .   ? 3.506  20.098  -15.415 1.00 28.40  ?  601 NAG A C7    1 
HETATM 10082 C  C8    . NAG D  3  .   ? 2.835  18.879  -16.092 1.00 28.56  ?  601 NAG A C8    1 
HETATM 10083 N  N2    . NAG D  3  .   ? 3.663  21.212  -16.195 1.00 27.16  ?  601 NAG A N2    1 
HETATM 10084 O  O3    . NAG D  3  .   ? 2.353  23.686  -15.624 1.00 26.62  ?  601 NAG A O3    1 
HETATM 10085 O  O4    . NAG D  3  .   ? 3.625  26.220  -16.103 1.00 30.60  ?  601 NAG A O4    1 
HETATM 10086 O  O5    . NAG D  3  .   ? 6.510  23.676  -15.766 1.00 27.91  ?  601 NAG A O5    1 
HETATM 10087 O  O6    . NAG D  3  .   ? 6.624  26.013  -14.405 1.00 29.37  ?  601 NAG A O6    1 
HETATM 10088 O  O7    . NAG D  3  .   ? 3.882  20.002  -14.234 1.00 27.97  ?  601 NAG A O7    1 
HETATM 10089 C  C1    . NAG E  3  .   ? 25.468 3.991   -24.534 1.00 36.03  ?  602 NAG A C1    1 
HETATM 10090 C  C2    . NAG E  3  .   ? 26.459 4.482   -25.609 1.00 35.82  ?  602 NAG A C2    1 
HETATM 10091 C  C3    . NAG E  3  .   ? 26.748 5.955   -25.402 1.00 36.49  ?  602 NAG A C3    1 
HETATM 10092 C  C4    . NAG E  3  .   ? 25.510 6.798   -25.633 1.00 36.88  ?  602 NAG A C4    1 
HETATM 10093 C  C5    . NAG E  3  .   ? 24.475 6.415   -24.520 1.00 37.69  ?  602 NAG A C5    1 
HETATM 10094 C  C6    . NAG E  3  .   ? 23.170 7.237   -24.674 1.00 37.70  ?  602 NAG A C6    1 
HETATM 10095 C  C7    . NAG E  3  .   ? 27.810 2.424   -25.861 1.00 40.46  ?  602 NAG A C7    1 
HETATM 10096 C  C8    . NAG E  3  .   ? 29.170 1.735   -25.641 1.00 39.65  ?  602 NAG A C8    1 
HETATM 10097 N  N2    . NAG E  3  .   ? 27.715 3.724   -25.475 1.00 37.83  ?  602 NAG A N2    1 
HETATM 10098 O  O3    . NAG E  3  .   ? 27.766 6.404   -26.296 1.00 37.28  ?  602 NAG A O3    1 
HETATM 10099 O  O4    . NAG E  3  .   ? 25.900 8.238   -25.606 1.00 36.54  ?  602 NAG A O4    1 
HETATM 10100 O  O5    . NAG E  3  .   ? 24.282 4.938   -24.478 1.00 37.62  ?  602 NAG A O5    1 
HETATM 10101 O  O6    . NAG E  3  .   ? 22.083 6.317   -24.902 1.00 37.80  ?  602 NAG A O6    1 
HETATM 10102 O  O7    . NAG E  3  .   ? 26.863 1.781   -26.322 1.00 40.75  ?  602 NAG A O7    1 
HETATM 10103 C  C1    . NAG F  3  .   ? 1.628  -10.650 7.608   1.00 49.23  ?  603 NAG A C1    1 
HETATM 10104 C  C2    . NAG F  3  .   ? 0.363  -11.080 8.341   1.00 52.62  ?  603 NAG A C2    1 
HETATM 10105 C  C3    . NAG F  3  .   ? 0.034  -12.546 7.939   1.00 56.30  ?  603 NAG A C3    1 
HETATM 10106 C  C4    . NAG F  3  .   ? -0.327 -12.550 6.452   1.00 57.86  ?  603 NAG A C4    1 
HETATM 10107 C  C5    . NAG F  3  .   ? 0.907  -12.161 5.667   1.00 55.16  ?  603 NAG A C5    1 
HETATM 10108 C  C6    . NAG F  3  .   ? 0.485  -11.864 4.245   1.00 54.21  ?  603 NAG A C6    1 
HETATM 10109 C  C7    . NAG F  3  .   ? 0.116  -9.868  10.471  1.00 48.69  ?  603 NAG A C7    1 
HETATM 10110 C  C8    . NAG F  3  .   ? 0.715  -9.625  11.874  1.00 47.77  ?  603 NAG A C8    1 
HETATM 10111 N  N2    . NAG F  3  .   ? 0.715  -10.834 9.751   1.00 51.82  ?  603 NAG A N2    1 
HETATM 10112 O  O3    . NAG F  3  .   ? -1.101 -13.044 8.633   1.00 61.51  ?  603 NAG A O3    1 
HETATM 10113 O  O4    . NAG F  3  .   ? -0.893 -13.829 5.997   1.00 56.31  ?  603 NAG A O4    1 
HETATM 10114 O  O5    . NAG F  3  .   ? 1.428  -10.894 6.166   1.00 55.17  ?  603 NAG A O5    1 
HETATM 10115 O  O6    . NAG F  3  .   ? 1.502  -12.466 3.448   1.00 51.71  ?  603 NAG A O6    1 
HETATM 10116 O  O7    . NAG F  3  .   ? -0.837 -9.210  10.056  1.00 45.33  ?  603 NAG A O7    1 
HETATM 10117 C  C1    . NAG G  3  .   ? 24.734 18.335  -0.267  1.00 31.66  ?  604 NAG A C1    1 
HETATM 10118 C  C2    . NAG G  3  .   ? 24.944 18.616  1.330   1.00 33.33  ?  604 NAG A C2    1 
HETATM 10119 C  C3    . NAG G  3  .   ? 23.993 19.633  2.020   1.00 34.54  ?  604 NAG A C3    1 
HETATM 10120 C  C4    . NAG G  3  .   ? 24.125 20.987  1.359   1.00 37.85  ?  604 NAG A C4    1 
HETATM 10121 C  C5    . NAG G  3  .   ? 23.743 20.771  -0.123  1.00 38.48  ?  604 NAG A C5    1 
HETATM 10122 C  C6    . NAG G  3  .   ? 23.971 22.085  -0.845  1.00 39.30  ?  604 NAG A C6    1 
HETATM 10123 C  C7    . NAG G  3  .   ? 25.945 16.541  2.157   1.00 33.44  ?  604 NAG A C7    1 
HETATM 10124 C  C8    . NAG G  3  .   ? 25.792 15.326  3.052   1.00 33.80  ?  604 NAG A C8    1 
HETATM 10125 N  N2    . NAG G  3  .   ? 24.904 17.388  2.132   1.00 32.84  ?  604 NAG A N2    1 
HETATM 10126 O  O4    . NAG G  3  .   ? 23.260 22.066  1.986   1.00 37.96  ?  604 NAG A O4    1 
HETATM 10127 O  O5    . NAG G  3  .   ? 24.489 19.651  -0.881  1.00 34.43  ?  604 NAG A O5    1 
HETATM 10128 O  O6    . NAG G  3  .   ? 25.132 21.726  -1.625  1.00 42.68  ?  604 NAG A O6    1 
HETATM 10129 O  O7    . NAG G  3  .   ? 26.960 16.670  1.477   1.00 36.62  ?  604 NAG A O7    1 
HETATM 10130 ZN ZN    . ZN  H  4  .   ? 14.467 -4.096  -8.727  1.00 27.67  ?  605 ZN  A ZN    1 
HETATM 10131 ZN ZN    . ZN  I  4  .   ? 15.944 -0.895  -9.188  1.00 14.20  ?  606 ZN  A ZN    1 
HETATM 10132 O  O3P   . C5P J  5  .   ? 11.837 -0.701  -9.316  1.00 52.29  ?  607 C5P A O3P   1 
HETATM 10133 P  P     . C5P J  5  .   ? 12.931 -1.661  -8.895  1.00 50.37  ?  607 C5P A P     1 
HETATM 10134 O  O1P   . C5P J  5  .   ? 12.930 -3.023  -9.521  1.00 51.04  -1 607 C5P A O1P   1 
HETATM 10135 O  O2P   . C5P J  5  .   ? 14.312 -1.090  -8.699  1.00 48.14  ?  607 C5P A O2P   1 
HETATM 10136 O  "O5'" . C5P J  5  .   ? 12.445 -1.999  -7.425  1.00 62.02  ?  607 C5P A "O5'" 1 
HETATM 10137 C  "C5'" . C5P J  5  .   ? 12.737 -1.019  -6.441  1.00 72.49  ?  607 C5P A "C5'" 1 
HETATM 10138 C  "C4'" . C5P J  5  .   ? 11.911 -1.188  -5.168  1.00 77.08  ?  607 C5P A "C4'" 1 
HETATM 10139 O  "O4'" . C5P J  5  .   ? 12.230 -0.096  -4.294  1.00 80.79  ?  607 C5P A "O4'" 1 
HETATM 10140 C  "C3'" . C5P J  5  .   ? 10.407 -1.179  -5.435  1.00 76.77  ?  607 C5P A "C3'" 1 
HETATM 10141 O  "O3'" . C5P J  5  .   ? 9.733  -2.233  -4.728  1.00 68.04  ?  607 C5P A "O3'" 1 
HETATM 10142 C  "C2'" . C5P J  5  .   ? 9.953  0.189   -4.970  1.00 79.58  ?  607 C5P A "C2'" 1 
HETATM 10143 O  "O2'" . C5P J  5  .   ? 8.837  0.045   -4.087  1.00 76.48  ?  607 C5P A "O2'" 1 
HETATM 10144 C  "C1'" . C5P J  5  .   ? 11.152 0.838   -4.270  1.00 82.42  ?  607 C5P A "C1'" 1 
HETATM 10145 N  N1    . C5P J  5  .   ? 11.605 2.122   -4.864  1.00 84.06  ?  607 C5P A N1    1 
HETATM 10146 C  C2    . C5P J  5  .   ? 11.532 3.272   -4.032  1.00 84.81  ?  607 C5P A C2    1 
HETATM 10147 N  N3    . C5P J  5  .   ? 11.925 4.465   -4.507  1.00 83.63  ?  607 C5P A N3    1 
HETATM 10148 C  C4    . C5P J  5  .   ? 12.394 4.570   -5.762  1.00 81.89  ?  607 C5P A C4    1 
HETATM 10149 C  C5    . C5P J  5  .   ? 12.481 3.471   -6.618  1.00 77.34  ?  607 C5P A C5    1 
HETATM 10150 C  C6    . C5P J  5  .   ? 12.080 2.238   -6.132  1.00 77.16  ?  607 C5P A C6    1 
HETATM 10151 O  O2    . C5P J  5  .   ? 11.093 3.202   -2.856  1.00 82.75  ?  607 C5P A O2    1 
HETATM 10152 N  N4    . C5P J  5  .   ? 12.780 5.787   -6.156  1.00 80.30  ?  607 C5P A N4    1 
HETATM 10153 C  C1    . NAG K  3  .   ? 51.490 -48.887 -12.756 1.00 42.53  ?  601 NAG B C1    1 
HETATM 10154 C  C2    . NAG K  3  .   ? 52.192 -50.277 -12.598 1.00 43.66  ?  601 NAG B C2    1 
HETATM 10155 C  C3    . NAG K  3  .   ? 51.420 -51.529 -13.050 1.00 42.67  ?  601 NAG B C3    1 
HETATM 10156 C  C4    . NAG K  3  .   ? 49.977 -51.430 -12.627 1.00 42.49  ?  601 NAG B C4    1 
HETATM 10157 C  C5    . NAG K  3  .   ? 49.386 -50.238 -13.390 1.00 43.67  ?  601 NAG B C5    1 
HETATM 10158 C  C6    . NAG K  3  .   ? 47.935 -50.056 -13.024 1.00 45.90  ?  601 NAG B C6    1 
HETATM 10159 C  C7    . NAG K  3  .   ? 54.556 -49.709 -12.703 1.00 46.07  ?  601 NAG B C7    1 
HETATM 10160 C  C8    . NAG K  3  .   ? 55.834 -49.644 -13.544 1.00 46.04  ?  601 NAG B C8    1 
HETATM 10161 N  N2    . NAG K  3  .   ? 53.461 -50.183 -13.333 1.00 44.53  ?  601 NAG B N2    1 
HETATM 10162 O  O3    . NAG K  3  .   ? 52.007 -52.677 -12.381 1.00 41.05  ?  601 NAG B O3    1 
HETATM 10163 O  O4    . NAG K  3  .   ? 49.262 -52.693 -12.881 1.00 38.88  ?  601 NAG B O4    1 
HETATM 10164 O  O5    . NAG K  3  .   ? 50.033 -48.982 -13.047 1.00 44.24  ?  601 NAG B O5    1 
HETATM 10165 O  O6    . NAG K  3  .   ? 47.922 -50.148 -11.593 1.00 46.49  ?  601 NAG B O6    1 
HETATM 10166 O  O7    . NAG K  3  .   ? 54.559 -49.328 -11.529 1.00 44.92  ?  601 NAG B O7    1 
HETATM 10167 C  C1    . NAG L  3  .   ? 57.793 -22.500 -21.994 1.00 51.38  ?  602 NAG B C1    1 
HETATM 10168 C  C2    . NAG L  3  .   ? 56.917 -23.765 -21.571 1.00 55.47  ?  602 NAG B C2    1 
HETATM 10169 C  C3    . NAG L  3  .   ? 55.591 -23.775 -22.323 1.00 56.72  ?  602 NAG B C3    1 
HETATM 10170 C  C4    . NAG L  3  .   ? 54.852 -22.442 -22.266 1.00 56.57  ?  602 NAG B C4    1 
HETATM 10171 C  C5    . NAG L  3  .   ? 55.772 -21.284 -22.671 1.00 52.90  ?  602 NAG B C5    1 
HETATM 10172 C  C6    . NAG L  3  .   ? 55.154 -19.916 -22.375 1.00 57.86  ?  602 NAG B C6    1 
HETATM 10173 C  C7    . NAG L  3  .   ? 57.374 -26.318 -21.571 1.00 68.64  ?  602 NAG B C7    1 
HETATM 10174 C  C8    . NAG L  3  .   ? 56.301 -26.593 -20.522 1.00 70.21  ?  602 NAG B C8    1 
HETATM 10175 N  N2    . NAG L  3  .   ? 57.619 -25.026 -21.958 1.00 62.97  ?  602 NAG B N2    1 
HETATM 10176 O  O3    . NAG L  3  .   ? 54.733 -24.783 -21.767 1.00 58.13  ?  602 NAG B O3    1 
HETATM 10177 O  O4    . NAG L  3  .   ? 53.655 -22.513 -23.141 1.00 59.84  ?  602 NAG B O4    1 
HETATM 10178 O  O5    . NAG L  3  .   ? 56.970 -21.309 -21.922 1.00 46.24  ?  602 NAG B O5    1 
HETATM 10179 O  O6    . NAG L  3  .   ? 53.825 -20.079 -21.804 1.00 60.08  ?  602 NAG B O6    1 
HETATM 10180 O  O7    . NAG L  3  .   ? 58.022 -27.275 -22.003 1.00 74.62  ?  602 NAG B O7    1 
HETATM 10181 C  C1    . NAG M  3  .   ? 52.888 -23.560 -23.507 1.00 70.29  ?  603 NAG B C1    1 
HETATM 10182 C  C2    . NAG M  3  .   ? 52.827 -25.003 -24.006 1.00 72.55  ?  603 NAG B C2    1 
HETATM 10183 C  C3    . NAG M  3  .   ? 51.493 -25.178 -24.724 1.00 71.45  ?  603 NAG B C3    1 
HETATM 10184 C  C4    . NAG M  3  .   ? 50.500 -25.413 -23.592 1.00 68.96  ?  603 NAG B C4    1 
HETATM 10185 C  C5    . NAG M  3  .   ? 50.588 -24.263 -22.516 1.00 69.29  ?  603 NAG B C5    1 
HETATM 10186 C  C6    . NAG M  3  .   ? 50.327 -24.860 -21.152 1.00 66.54  ?  603 NAG B C6    1 
HETATM 10187 C  C7    . NAG M  3  .   ? 54.438 -26.674 -24.792 1.00 78.56  ?  603 NAG B C7    1 
HETATM 10188 C  C8    . NAG M  3  .   ? 53.728 -27.682 -23.828 1.00 77.33  ?  603 NAG B C8    1 
HETATM 10189 N  N2    . NAG M  3  .   ? 53.963 -25.410 -24.847 1.00 73.26  ?  603 NAG B N2    1 
HETATM 10190 O  O3    . NAG M  3  .   ? 51.507 -26.266 -25.694 1.00 67.42  ?  603 NAG B O3    1 
HETATM 10191 O  O4    . NAG M  3  .   ? 49.160 -25.481 -24.101 1.00 67.56  ?  603 NAG B O4    1 
HETATM 10192 O  O5    . NAG M  3  .   ? 51.885 -23.482 -22.428 1.00 70.58  ?  603 NAG B O5    1 
HETATM 10193 O  O6    . NAG M  3  .   ? 51.585 -24.667 -20.519 1.00 62.85  ?  603 NAG B O6    1 
HETATM 10194 O  O7    . NAG M  3  .   ? 55.381 -27.043 -25.485 1.00 78.73  ?  603 NAG B O7    1 
HETATM 10195 C  C1    . NAG N  3  .   ? 82.084 -36.070 11.082  1.00 73.84  ?  604 NAG B C1    1 
HETATM 10196 C  C2    . NAG N  3  .   ? 83.272 -37.031 11.420  1.00 77.14  ?  604 NAG B C2    1 
HETATM 10197 C  C3    . NAG N  3  .   ? 84.589 -36.405 10.877  1.00 79.53  ?  604 NAG B C3    1 
HETATM 10198 C  C4    . NAG N  3  .   ? 84.496 -36.237 9.366   1.00 78.87  ?  604 NAG B C4    1 
HETATM 10199 C  C5    . NAG N  3  .   ? 83.358 -35.232 9.119   1.00 77.51  ?  604 NAG B C5    1 
HETATM 10200 C  C6    . NAG N  3  .   ? 83.048 -34.872 7.661   1.00 76.23  ?  604 NAG B C6    1 
HETATM 10201 C  C7    . NAG N  3  .   ? 82.697 -38.245 13.533  1.00 75.19  ?  604 NAG B C7    1 
HETATM 10202 C  C8    . NAG N  3  .   ? 82.917 -38.282 15.057  1.00 72.10  ?  604 NAG B C8    1 
HETATM 10203 N  N2    . NAG N  3  .   ? 83.357 -37.252 12.885  1.00 76.28  ?  604 NAG B N2    1 
HETATM 10204 O  O3    . NAG N  3  .   ? 85.736 -37.212 11.176  1.00 85.35  ?  604 NAG B O3    1 
HETATM 10205 O  O4    . NAG N  3  .   ? 85.777 -35.797 8.852   1.00 78.84  ?  604 NAG B O4    1 
HETATM 10206 O  O5    . NAG N  3  .   ? 82.134 -35.814 9.642   1.00 76.07  ?  604 NAG B O5    1 
HETATM 10207 O  O6    . NAG N  3  .   ? 83.900 -35.626 6.805   1.00 75.87  ?  604 NAG B O6    1 
HETATM 10208 O  O7    . NAG N  3  .   ? 81.979 -39.087 12.984  1.00 75.54  ?  604 NAG B O7    1 
HETATM 10209 C  C1    . NAG O  3  .   ? 45.323 -30.600 2.393   1.00 45.34  ?  605 NAG B C1    1 
HETATM 10210 C  C2    . NAG O  3  .   ? 45.295 -30.481 3.984   1.00 44.69  ?  605 NAG B C2    1 
HETATM 10211 C  C3    . NAG O  3  .   ? 45.008 -31.786 4.705   1.00 47.52  ?  605 NAG B C3    1 
HETATM 10212 C  C4    . NAG O  3  .   ? 43.646 -32.421 4.264   1.00 51.02  ?  605 NAG B C4    1 
HETATM 10213 C  C5    . NAG O  3  .   ? 43.668 -32.618 2.701   1.00 51.92  ?  605 NAG B C5    1 
HETATM 10214 C  C6    . NAG O  3  .   ? 42.323 -33.199 2.296   1.00 52.55  ?  605 NAG B C6    1 
HETATM 10215 C  C7    . NAG O  3  .   ? 46.610 -28.827 5.247   1.00 44.99  ?  605 NAG B C7    1 
HETATM 10216 C  C8    . NAG O  3  .   ? 47.997 -28.416 5.741   1.00 47.33  ?  605 NAG B C8    1 
HETATM 10217 N  N2    . NAG O  3  .   ? 46.560 -29.965 4.536   1.00 42.14  ?  605 NAG B N2    1 
HETATM 10218 O  O3    . NAG O  3  .   ? 44.975 -31.428 6.092   1.00 51.15  ?  605 NAG B O3    1 
HETATM 10219 O  O4    . NAG O  3  .   ? 43.277 -33.708 5.007   1.00 45.40  ?  605 NAG B O4    1 
HETATM 10220 O  O5    . NAG O  3  .   ? 44.039 -31.354 1.940   1.00 48.85  ?  605 NAG B O5    1 
HETATM 10221 O  O6    . NAG O  3  .   ? 42.347 -34.550 2.827   1.00 52.74  ?  605 NAG B O6    1 
HETATM 10222 O  O7    . NAG O  3  .   ? 45.642 -28.117 5.498   1.00 46.01  ?  605 NAG B O7    1 
HETATM 10223 ZN ZN    . ZN  P  4  .   ? 66.591 -28.266 -6.113  1.00 35.79  ?  606 ZN  B ZN    1 
HETATM 10224 ZN ZN    . ZN  Q  4  .   ? 70.098 -28.074 -5.801  1.00 40.09  ?  607 ZN  B ZN    1 
HETATM 10225 C  C1    . GOL R  6  .   ? 77.351 -43.571 17.245  1.00 43.77  ?  608 GOL B C1    1 
HETATM 10226 O  O1    . GOL R  6  .   ? 77.576 -44.937 16.896  1.00 41.66  ?  608 GOL B O1    1 
HETATM 10227 C  C2    . GOL R  6  .   ? 78.441 -43.090 18.218  1.00 44.70  ?  608 GOL B C2    1 
HETATM 10228 O  O2    . GOL R  6  .   ? 78.704 -41.701 17.912  1.00 42.76  ?  608 GOL B O2    1 
HETATM 10229 C  C3    . GOL R  6  .   ? 77.956 -43.344 19.663  1.00 44.56  ?  608 GOL B C3    1 
HETATM 10230 O  O3    . GOL R  6  .   ? 79.073 -43.113 20.560  1.00 41.81  ?  608 GOL B O3    1 
HETATM 10231 C  C1    . GOL S  6  .   ? 81.822 -9.047  -23.332 1.00 68.70  ?  609 GOL B C1    1 
HETATM 10232 O  O1    . GOL S  6  .   ? 82.191 -10.382 -23.708 1.00 67.93  ?  609 GOL B O1    1 
HETATM 10233 C  C2    . GOL S  6  .   ? 80.722 -8.437  -24.264 1.00 66.03  ?  609 GOL B C2    1 
HETATM 10234 O  O2    . GOL S  6  .   ? 79.802 -9.428  -24.767 1.00 63.32  ?  609 GOL B O2    1 
HETATM 10235 C  C3    . GOL S  6  .   ? 79.973 -7.302  -23.529 1.00 62.35  ?  609 GOL B C3    1 
HETATM 10236 O  O3    . GOL S  6  .   ? 78.998 -7.831  -22.591 1.00 52.29  ?  609 GOL B O3    1 
HETATM 10237 C  C1    . MLI T  7  .   ? 79.430 -20.391 -26.567 1.00 64.11  ?  610 MLI B C1    1 
HETATM 10238 C  C2    . MLI T  7  .   ? 78.230 -19.631 -27.281 1.00 65.44  ?  610 MLI B C2    1 
HETATM 10239 C  C3    . MLI T  7  .   ? 79.986 -19.804 -25.204 1.00 62.28  ?  610 MLI B C3    1 
HETATM 10240 O  O6    . MLI T  7  .   ? 77.232 -20.313 -27.627 1.00 67.74  ?  610 MLI B O6    1 
HETATM 10241 O  O7    . MLI T  7  .   ? 78.349 -18.414 -27.564 1.00 63.98  ?  610 MLI B O7    1 
HETATM 10242 O  O8    . MLI T  7  .   ? 79.739 -18.606 -24.923 1.00 65.24  ?  610 MLI B O8    1 
HETATM 10243 O  O9    . MLI T  7  .   ? 80.698 -20.558 -24.476 1.00 52.60  ?  610 MLI B O9    1 
HETATM 10244 C  "C1'" . RP5 U  8  .   ? 69.765 -33.350 -0.637  1.00 66.25  ?  611 RP5 B "C1'" 1 
HETATM 10245 O  "O1'" . RP5 U  8  .   ? 69.850 -32.824 -1.932  1.00 68.52  ?  611 RP5 B "O1'" 1 
HETATM 10246 C  "C2'" . RP5 U  8  .   ? 68.300 -33.672 -0.446  1.00 67.36  ?  611 RP5 B "C2'" 1 
HETATM 10247 O  "O2'" . RP5 U  8  .   ? 68.039 -35.007 -0.854  1.00 62.59  ?  611 RP5 B "O2'" 1 
HETATM 10248 C  "C3'" . RP5 U  8  .   ? 67.568 -32.719 -1.356  1.00 68.15  ?  611 RP5 B "C3'" 1 
HETATM 10249 O  "O3'" . RP5 U  8  .   ? 66.297 -33.207 -1.789  1.00 61.54  ?  611 RP5 B "O3'" 1 
HETATM 10250 C  "C4'" . RP5 U  8  .   ? 68.543 -32.664 -2.473  1.00 70.20  ?  611 RP5 B "C4'" 1 
HETATM 10251 C  "C5'" . RP5 U  8  .   ? 68.439 -31.381 -3.237  1.00 73.23  ?  611 RP5 B "C5'" 1 
HETATM 10252 O  "O5'" . RP5 U  8  .   ? 69.057 -31.738 -4.450  1.00 76.83  ?  611 RP5 B "O5'" 1 
HETATM 10253 P  "P'"  . RP5 U  8  .   ? 68.803 -30.948 -5.752  1.00 75.00  ?  611 RP5 B "P'"  1 
HETATM 10254 O  O1X   . RP5 U  8  .   ? 69.005 -31.939 -6.813  1.00 81.31  -1 611 RP5 B O1X   1 
HETATM 10255 O  O2X   . RP5 U  8  .   ? 69.755 -29.729 -5.732  1.00 78.19  ?  611 RP5 B O2X   1 
HETATM 10256 O  O3X   . RP5 U  8  .   ? 67.458 -30.319 -5.648  1.00 68.94  ?  611 RP5 B O3X   1 
HETATM 10257 O  O1    . RP5 U  8  .   ? 70.137 -32.288 0.212   1.00 62.71  ?  611 RP5 B O1    1 
HETATM 10258 C  C1    . NAG V  3  .   ? 90.230 26.139  -18.669 1.00 47.91  ?  601 NAG C C1    1 
HETATM 10259 C  C2    . NAG V  3  .   ? 91.078 27.516  -18.554 1.00 46.76  ?  601 NAG C C2    1 
HETATM 10260 C  C3    . NAG V  3  .   ? 92.476 27.478  -19.219 1.00 47.04  ?  601 NAG C C3    1 
HETATM 10261 C  C4    . NAG V  3  .   ? 93.319 26.269  -18.786 1.00 50.25  ?  601 NAG C C4    1 
HETATM 10262 C  C5    . NAG V  3  .   ? 92.573 24.966  -19.243 1.00 51.63  ?  601 NAG C C5    1 
HETATM 10263 C  C6    . NAG V  3  .   ? 93.378 23.730  -18.819 1.00 52.21  ?  601 NAG C C6    1 
HETATM 10264 C  C7    . NAG V  3  .   ? 89.446 29.433  -18.431 1.00 46.23  ?  601 NAG C C7    1 
HETATM 10265 C  C8    . NAG V  3  .   ? 88.837 30.589  -19.238 1.00 47.63  ?  601 NAG C C8    1 
HETATM 10266 N  N2    . NAG V  3  .   ? 90.340 28.676  -19.122 1.00 45.14  ?  601 NAG C N2    1 
HETATM 10267 O  O3    . NAG V  3  .   ? 93.149 28.656  -18.807 1.00 47.32  ?  601 NAG C O3    1 
HETATM 10268 O  O4    . NAG V  3  .   ? 94.732 26.345  -19.301 1.00 47.40  ?  601 NAG C O4    1 
HETATM 10269 O  O5    . NAG V  3  .   ? 91.155 24.904  -18.756 1.00 49.42  ?  601 NAG C O5    1 
HETATM 10270 O  O6    . NAG V  3  .   ? 93.452 23.768  -17.378 1.00 50.29  ?  601 NAG C O6    1 
HETATM 10271 O  O7    . NAG V  3  .   ? 89.102 29.257  -17.258 1.00 43.84  ?  601 NAG C O7    1 
HETATM 10272 C  C1    . NAG W  3  .   ? 64.246 18.654  -27.610 1.00 55.82  ?  602 NAG C C1    1 
HETATM 10273 C  C2    . NAG W  3  .   ? 64.038 17.519  -28.680 1.00 53.84  ?  602 NAG C C2    1 
HETATM 10274 C  C3    . NAG W  3  .   ? 65.138 16.428  -28.546 1.00 52.79  ?  602 NAG C C3    1 
HETATM 10275 C  C4    . NAG W  3  .   ? 66.549 17.002  -28.619 1.00 53.16  ?  602 NAG C C4    1 
HETATM 10276 C  C5    . NAG W  3  .   ? 66.729 18.112  -27.526 1.00 53.78  ?  602 NAG C C5    1 
HETATM 10277 C  C6    . NAG W  3  .   ? 68.121 18.752  -27.615 1.00 52.90  ?  602 NAG C C6    1 
HETATM 10278 C  C7    . NAG W  3  .   ? 61.534 17.504  -28.875 1.00 52.93  ?  602 NAG C C7    1 
HETATM 10279 C  C8    . NAG W  3  .   ? 60.268 16.665  -28.658 1.00 51.78  ?  602 NAG C C8    1 
HETATM 10280 N  N2    . NAG W  3  .   ? 62.698 16.890  -28.536 1.00 53.94  ?  602 NAG C N2    1 
HETATM 10281 O  O3    . NAG W  3  .   ? 65.033 15.480  -29.598 1.00 51.99  ?  602 NAG C O3    1 
HETATM 10282 O  O4    . NAG W  3  .   ? 67.512 15.888  -28.490 1.00 51.29  ?  602 NAG C O4    1 
HETATM 10283 O  O5    . NAG W  3  .   ? 65.670 19.119  -27.645 1.00 54.80  ?  602 NAG C O5    1 
HETATM 10284 O  O6    . NAG W  3  .   ? 67.938 20.134  -27.990 1.00 50.65  ?  602 NAG C O6    1 
HETATM 10285 O  O7    . NAG W  3  .   ? 61.446 18.655  -29.308 1.00 51.21  ?  602 NAG C O7    1 
HETATM 10286 C  C1    . NAG X  3  .   ? 63.618 46.567  4.680   1.00 63.06  ?  603 NAG C C1    1 
HETATM 10287 C  C2    . NAG X  3  .   ? 63.854 47.967  5.284   1.00 63.08  ?  603 NAG C C2    1 
HETATM 10288 C  C3    . NAG X  3  .   ? 62.840 48.979  4.665   1.00 64.15  ?  603 NAG C C3    1 
HETATM 10289 C  C4    . NAG X  3  .   ? 63.180 49.163  3.193   1.00 65.18  ?  603 NAG C C4    1 
HETATM 10290 C  C5    . NAG X  3  .   ? 62.898 47.834  2.473   1.00 68.02  ?  603 NAG C C5    1 
HETATM 10291 C  C6    . NAG X  3  .   ? 63.991 47.525  1.464   1.00 68.45  ?  603 NAG C C6    1 
HETATM 10292 C  C7    . NAG X  3  .   ? 64.845 47.744  7.571   1.00 57.28  ?  603 NAG C C7    1 
HETATM 10293 C  C8    . NAG X  3  .   ? 64.561 47.598  9.071   1.00 54.75  ?  603 NAG C C8    1 
HETATM 10294 N  N2    . NAG X  3  .   ? 63.750 47.836  6.762   1.00 61.39  ?  603 NAG C N2    1 
HETATM 10295 O  O3    . NAG X  3  .   ? 62.905 50.259  5.271   1.00 68.95  ?  603 NAG C O3    1 
HETATM 10296 O  O4    . NAG X  3  .   ? 62.408 50.246  2.610   1.00 56.91  ?  603 NAG C O4    1 
HETATM 10297 O  O5    . NAG X  3  .   ? 62.745 46.708  3.443   1.00 72.46  ?  603 NAG C O5    1 
HETATM 10298 O  O6    . NAG X  3  .   ? 63.548 48.213  0.294   1.00 67.70  ?  603 NAG C O6    1 
HETATM 10299 O  O7    . NAG X  3  .   ? 66.010 47.773  7.173   1.00 53.82  ?  603 NAG C O7    1 
HETATM 10300 C  C1    . NAG Y  3  .   ? 76.958 11.754  -3.513  1.00 49.76  ?  604 NAG C C1    1 
HETATM 10301 C  C2    . NAG Y  3  .   ? 77.005 11.398  -1.956  1.00 49.43  ?  604 NAG C C2    1 
HETATM 10302 C  C3    . NAG Y  3  .   ? 78.411 11.559  -1.319  1.00 49.92  ?  604 NAG C C3    1 
HETATM 10303 C  C4    . NAG Y  3  .   ? 79.463 10.931  -2.192  1.00 51.63  ?  604 NAG C C4    1 
HETATM 10304 C  C5    . NAG Y  3  .   ? 79.341 11.509  -3.634  1.00 50.47  ?  604 NAG C C5    1 
HETATM 10305 C  C6    . NAG Y  3  .   ? 80.373 10.924  -4.561  1.00 52.06  ?  604 NAG C C6    1 
HETATM 10306 C  C7    . NAG Y  3  .   ? 75.944 13.423  -0.775  1.00 54.33  ?  604 NAG C C7    1 
HETATM 10307 C  C8    . NAG Y  3  .   ? 76.936 14.447  -1.380  1.00 51.73  ?  604 NAG C C8    1 
HETATM 10308 N  N2    . NAG Y  3  .   ? 75.997 12.086  -1.102  1.00 49.27  ?  604 NAG C N2    1 
HETATM 10309 O  O3    . NAG Y  3  .   ? 78.417 10.860  -0.074  1.00 47.29  ?  604 NAG C O3    1 
HETATM 10310 O  O4    . NAG Y  3  .   ? 80.806 11.152  -1.603  1.00 53.49  ?  604 NAG C O4    1 
HETATM 10311 O  O5    . NAG Y  3  .   ? 78.102 11.150  -4.222  1.00 47.01  ?  604 NAG C O5    1 
HETATM 10312 O  O6    . NAG Y  3  .   ? 80.717 9.656   -3.992  1.00 52.49  ?  604 NAG C O6    1 
HETATM 10313 O  O7    . NAG Y  3  .   ? 75.080 13.872  -0.020  1.00 55.29  ?  604 NAG C O7    1 
HETATM 10314 ZN ZN    . ZN  Z  4  .   ? 62.861 32.616  -11.713 1.00 50.69  ?  605 ZN  C ZN    1 
HETATM 10315 ZN ZN    . ZN  AA 4  .   ? 64.835 29.315  -12.190 1.00 32.16  ?  606 ZN  C ZN    1 
HETATM 10316 O  O3P   . C5P BA 5  .   ? 66.027 30.520  -12.294 1.00 53.54  ?  607 C5P C O3P   1 
HETATM 10317 P  P     . C5P BA 5  .   ? 65.840 31.887  -11.683 1.00 56.80  ?  607 C5P C P     1 
HETATM 10318 O  O1P   . C5P BA 5  .   ? 65.986 33.061  -12.620 1.00 59.29  ?  607 C5P C O1P   1 
HETATM 10319 O  O2P   . C5P BA 5  .   ? 64.531 31.973  -10.960 1.00 61.89  -1 607 C5P C O2P   1 
HETATM 10320 O  "O5'" . C5P BA 5  .   ? 67.078 32.097  -10.595 1.00 68.26  ?  607 C5P C "O5'" 1 
HETATM 10321 C  "C5'" . C5P BA 5  .   ? 67.410 31.291  -9.419  1.00 72.72  ?  607 C5P C "C5'" 1 
HETATM 10322 C  "C4'" . C5P BA 5  .   ? 68.862 30.726  -9.194  1.00 75.70  ?  607 C5P C "C4'" 1 
HETATM 10323 O  "O4'" . C5P BA 5  .   ? 69.704 30.635  -10.376 1.00 76.84  ?  607 C5P C "O4'" 1 
HETATM 10324 C  "C3'" . C5P BA 5  .   ? 69.704 31.463  -8.125  1.00 77.10  ?  607 C5P C "C3'" 1 
HETATM 10325 O  "O3'" . C5P BA 5  .   ? 69.623 30.858  -6.819  1.00 67.22  ?  607 C5P C "O3'" 1 
HETATM 10326 C  "C2'" . C5P BA 5  .   ? 71.142 31.505  -8.672  1.00 79.94  ?  607 C5P C "C2'" 1 
HETATM 10327 O  "O2'" . C5P BA 5  .   ? 72.101 30.883  -7.809  1.00 72.85  ?  607 C5P C "O2'" 1 
HETATM 10328 C  "C1'" . C5P BA 5  .   ? 71.104 30.810  -10.043 1.00 81.66  ?  607 C5P C "C1'" 1 
HETATM 10329 N  N1    . C5P BA 5  .   ? 71.923 31.502  -11.108 1.00 86.76  ?  607 C5P C N1    1 
HETATM 10330 C  C2    . C5P BA 5  .   ? 71.774 32.854  -11.593 1.00 84.51  ?  607 C5P C C2    1 
HETATM 10331 N  N3    . C5P BA 5  .   ? 72.594 33.342  -12.564 1.00 80.76  ?  607 C5P C N3    1 
HETATM 10332 C  C4    . C5P BA 5  .   ? 73.566 32.579  -13.112 1.00 77.49  ?  607 C5P C C4    1 
HETATM 10333 C  C5    . C5P BA 5  .   ? 73.741 31.277  -12.680 1.00 83.53  ?  607 C5P C C5    1 
HETATM 10334 C  C6    . C5P BA 5  .   ? 72.908 30.771  -11.675 1.00 90.44  ?  607 C5P C C6    1 
HETATM 10335 O  O2    . C5P BA 5  .   ? 70.911 33.651  -11.169 1.00 86.15  ?  607 C5P C O2    1 
HETATM 10336 N  N4    . C5P BA 5  .   ? 74.371 33.065  -14.069 1.00 69.38  ?  607 C5P C N4    1 
HETATM 10337 S  S     . SCN CA 9  .   ? 50.170 21.181  17.672  1.00 48.96  ?  608 SCN C S     1 
HETATM 10338 C  C     . SCN CA 9  .   ? 50.591 20.226  16.610  1.00 44.45  ?  608 SCN C C     1 
HETATM 10339 N  N     . SCN CA 9  .   ? 50.919 19.469  15.784  1.00 36.47  ?  608 SCN C N     1 
HETATM 10340 S  S     . SCN DA 9  .   ? 70.722 39.187  -16.107 1.00 52.95  ?  609 SCN C S     1 
HETATM 10341 C  C     . SCN DA 9  .   ? 71.073 38.894  -17.511 1.00 43.88  ?  609 SCN C C     1 
HETATM 10342 N  N     . SCN DA 9  .   ? 71.349 38.642  -18.589 1.00 40.21  ?  609 SCN C N     1 
HETATM 10343 O  O     . HOH EA 10 .   ? 14.463 -7.596  2.544   1.00 15.18  ?  701 HOH A O     1 
HETATM 10344 O  O     . HOH EA 10 .   ? 24.508 5.096   2.211   1.00 12.86  ?  702 HOH A O     1 
HETATM 10345 O  O     . HOH EA 10 .   ? 4.678  -1.519  15.794  1.00 13.40  ?  703 HOH A O     1 
HETATM 10346 O  O     . HOH EA 10 .   ? 18.353 11.348  -12.682 1.00 13.16  ?  704 HOH A O     1 
HETATM 10347 O  O     . HOH EA 10 .   ? 12.115 -10.673 0.802   1.00 6.90   ?  705 HOH A O     1 
HETATM 10348 O  O     . HOH EA 10 .   ? 21.351 -5.479  -15.582 1.00 17.36  ?  706 HOH A O     1 
HETATM 10349 O  O     . HOH EA 10 .   ? 25.679 10.690  -26.579 1.00 16.20  ?  707 HOH A O     1 
HETATM 10350 O  O     . HOH EA 10 .   ? 19.265 -1.299  -4.597  1.00 21.26  ?  708 HOH A O     1 
HETATM 10351 O  O     . HOH EA 10 .   ? 21.133 -13.510 -11.830 1.00 19.37  ?  709 HOH A O     1 
HETATM 10352 O  O     . HOH EA 10 .   ? 8.016  -5.502  5.837   1.00 27.78  ?  710 HOH A O     1 
HETATM 10353 O  O     . HOH EA 10 .   ? 24.956 1.059   -6.837  1.00 26.88  ?  711 HOH A O     1 
HETATM 10354 O  O     . HOH EA 10 .   ? 25.943 -4.910  -0.464  1.00 8.65   ?  712 HOH A O     1 
HETATM 10355 O  O     . HOH EA 10 .   ? 9.181  6.505   -10.890 1.00 4.93   ?  713 HOH A O     1 
HETATM 10356 O  O     . HOH EA 10 .   ? 22.116 2.889   6.014   1.00 6.54   ?  714 HOH A O     1 
HETATM 10357 O  O     . HOH EA 10 .   ? 7.750  2.903   -14.997 1.00 13.49  ?  715 HOH A O     1 
HETATM 10358 O  O     . HOH EA 10 .   ? 9.048  -0.622  -10.283 1.00 8.59   ?  716 HOH A O     1 
HETATM 10359 O  O     . HOH EA 10 .   ? 17.262 -2.917  6.923   1.00 2.00   ?  717 HOH A O     1 
HETATM 10360 O  O     . HOH EA 10 .   ? 9.553  -24.448 -12.603 1.00 13.60  ?  718 HOH A O     1 
HETATM 10361 O  O     . HOH EA 10 .   ? -6.830 -0.546  17.950  1.00 16.06  ?  719 HOH A O     1 
HETATM 10362 O  O     . HOH FA 10 .   ? 62.707 -27.306 -7.485  1.00 21.15  ?  701 HOH B O     1 
HETATM 10363 O  O     . HOH FA 10 .   ? 62.105 -38.662 -22.051 1.00 41.75  ?  702 HOH B O     1 
HETATM 10364 O  O     . HOH FA 10 .   ? 59.051 -22.422 10.228  1.00 9.15   ?  703 HOH B O     1 
HETATM 10365 O  O     . HOH FA 10 .   ? 65.005 -25.169 -1.881  1.00 20.34  ?  704 HOH B O     1 
HETATM 10366 O  O     . HOH FA 10 .   ? 74.379 -26.200 10.523  1.00 29.77  ?  705 HOH B O     1 
HETATM 10367 O  O     . HOH FA 10 .   ? 76.784 -26.250 3.731   1.00 16.12  ?  706 HOH B O     1 
HETATM 10368 O  O     . HOH FA 10 .   ? 60.508 -21.231 -3.315  1.00 28.50  ?  707 HOH B O     1 
HETATM 10369 O  O     . HOH FA 10 .   ? 61.824 -7.558  -14.670 1.00 29.96  ?  708 HOH B O     1 
HETATM 10370 O  O     . HOH FA 10 .   ? 55.818 -28.674 -22.537 1.00 21.35  ?  709 HOH B O     1 
HETATM 10371 O  O     . HOH FA 10 .   ? 57.346 -24.059 4.885   1.00 45.43  ?  710 HOH B O     1 
HETATM 10372 O  O     . HOH FA 10 .   ? 67.578 -21.576 -12.692 1.00 28.69  ?  711 HOH B O     1 
HETATM 10373 O  O     . HOH FA 10 .   ? 59.719 -25.042 9.099   1.00 11.78  ?  712 HOH B O     1 
HETATM 10374 O  O     . HOH FA 10 .   ? 68.698 -30.793 -14.538 1.00 23.45  ?  713 HOH B O     1 
HETATM 10375 O  O     . HOH FA 10 .   ? 76.359 -4.237  -12.309 1.00 20.84  ?  714 HOH B O     1 
HETATM 10376 O  O     . HOH FA 10 .   ? 81.673 -27.973 8.394   1.00 12.41  ?  715 HOH B O     1 
HETATM 10377 O  O     . HOH FA 10 .   ? 74.589 -32.582 9.222   1.00 42.67  ?  716 HOH B O     1 
HETATM 10378 O  O     . HOH FA 10 .   ? 61.510 -20.242 8.653   1.00 11.99  ?  717 HOH B O     1 
HETATM 10379 O  O     . HOH FA 10 .   ? 60.542 -41.821 -8.919  1.00 8.26   ?  718 HOH B O     1 
HETATM 10380 O  O     . HOH FA 10 .   ? 56.014 -5.275  -12.357 1.00 17.28  ?  719 HOH B O     1 
HETATM 10381 O  O     . HOH FA 10 .   ? 86.235 -6.135  -6.431  1.00 11.19  ?  720 HOH B O     1 
HETATM 10382 O  O     . HOH FA 10 .   ? 77.876 -32.885 -0.372  1.00 25.77  ?  721 HOH B O     1 
HETATM 10383 O  O     . HOH FA 10 .   ? 64.516 -2.745  -6.880  1.00 17.14  ?  722 HOH B O     1 
HETATM 10384 O  O     . HOH FA 10 .   ? 85.738 -15.931 -11.784 1.00 15.54  ?  723 HOH B O     1 
HETATM 10385 O  O     . HOH FA 10 .   ? 77.276 -28.588 -7.995  1.00 24.36  ?  724 HOH B O     1 
HETATM 10386 O  O     . HOH FA 10 .   ? 69.396 -2.713  -14.244 1.00 4.35   ?  725 HOH B O     1 
HETATM 10387 O  O     . HOH FA 10 .   ? 50.636 -10.814 -17.133 1.00 32.49  ?  726 HOH B O     1 
HETATM 10388 O  O     . HOH FA 10 .   ? 67.662 -27.118 5.036   1.00 22.82  ?  727 HOH B O     1 
HETATM 10389 O  O     . HOH FA 10 .   ? 68.222 -32.006 4.980   1.00 13.18  ?  728 HOH B O     1 
HETATM 10390 O  O     . HOH FA 10 .   ? 63.529 -19.892 6.983   1.00 18.52  ?  729 HOH B O     1 
HETATM 10391 O  O     . HOH FA 10 .   ? 79.752 -4.614  -23.086 1.00 35.98  ?  730 HOH B O     1 
HETATM 10392 O  O     . HOH FA 10 .   ? 47.022 -19.926 -11.964 1.00 15.95  ?  731 HOH B O     1 
HETATM 10393 O  O     . HOH FA 10 .   ? 55.212 -10.343 -23.729 1.00 12.89  ?  732 HOH B O     1 
HETATM 10394 O  O     . HOH FA 10 .   ? 62.590 -41.049 23.905  1.00 15.46  ?  733 HOH B O     1 
HETATM 10395 O  O     . HOH FA 10 .   ? 73.770 -4.943  -18.758 1.00 7.09   ?  734 HOH B O     1 
HETATM 10396 O  O     . HOH FA 10 .   ? 69.673 -23.891 -30.722 1.00 21.23  ?  735 HOH B O     1 
HETATM 10397 O  O     . HOH FA 10 .   ? 69.934 -15.195 -23.970 1.00 24.05  ?  736 HOH B O     1 
HETATM 10398 O  O     . HOH FA 10 .   ? 55.047 -26.493 24.857  1.00 19.48  ?  737 HOH B O     1 
HETATM 10399 O  O     . HOH FA 10 .   ? 58.603 -0.415  -4.024  1.00 24.87  ?  738 HOH B O     1 
HETATM 10400 O  O     . HOH FA 10 .   ? 65.322 0.143   -13.217 1.00 20.62  ?  739 HOH B O     1 
HETATM 10401 O  O     . HOH FA 10 .   ? 82.581 -26.645 21.480  1.00 26.36  ?  740 HOH B O     1 
HETATM 10402 O  O     . HOH FA 10 .   ? 81.050 -25.274 -22.281 1.00 17.40  ?  741 HOH B O     1 
HETATM 10403 O  O     . HOH FA 10 .   ? 59.232 -12.204 -24.356 1.00 16.19  ?  742 HOH B O     1 
HETATM 10404 O  O     . HOH FA 10 .   ? 46.725 -31.484 -16.598 1.00 25.85  ?  743 HOH B O     1 
HETATM 10405 O  O     . HOH FA 10 .   ? 82.353 -36.355 3.059   1.00 17.37  ?  744 HOH B O     1 
HETATM 10406 O  O     . HOH FA 10 .   ? 80.330 -3.408  -8.362  1.00 16.74  ?  745 HOH B O     1 
HETATM 10407 O  O     . HOH FA 10 .   ? 88.169 -17.107 -16.023 1.00 18.84  ?  746 HOH B O     1 
HETATM 10408 O  O     . HOH FA 10 .   ? 73.862 -12.626 -28.718 1.00 16.60  ?  747 HOH B O     1 
HETATM 10409 O  O     . HOH FA 10 .   ? 50.881 -7.140  -12.051 1.00 28.80  ?  748 HOH B O     1 
HETATM 10410 O  O     . HOH FA 10 .   ? 56.765 -37.246 -23.044 1.00 18.63  ?  749 HOH B O     1 
HETATM 10411 O  O     . HOH FA 10 .   ? 72.961 -35.720 0.590   1.00 25.74  ?  750 HOH B O     1 
HETATM 10412 O  O     . HOH FA 10 .   ? 63.481 -16.346 -26.257 1.00 20.32  ?  751 HOH B O     1 
HETATM 10413 O  O     . HOH FA 10 .   ? 83.138 -41.936 16.679  1.00 15.92  ?  752 HOH B O     1 
HETATM 10414 O  O     . HOH FA 10 .   ? 66.121 -8.920  -23.305 1.00 10.92  ?  753 HOH B O     1 
HETATM 10415 O  O     . HOH FA 10 .   ? 88.107 -13.359 -11.717 1.00 17.82  ?  754 HOH B O     1 
HETATM 10416 O  O     . HOH FA 10 .   ? 57.082 -15.451 25.843  1.00 19.75  ?  755 HOH B O     1 
HETATM 10417 O  O     . HOH FA 10 .   ? 66.283 -23.632 -31.103 1.00 25.06  ?  756 HOH B O     1 
HETATM 10418 O  O     . HOH FA 10 .   ? 77.409 12.100  7.945   1.00 7.90   ?  757 HOH B O     1 
HETATM 10419 O  O     . HOH FA 10 .   ? 69.756 -12.374 -28.146 1.00 20.90  ?  758 HOH B O     1 
HETATM 10420 O  O     . HOH FA 10 .   ? 60.982 -15.393 -27.888 1.00 35.54  ?  759 HOH B O     1 
HETATM 10421 O  O     . HOH FA 10 .   ? 58.548 -6.251  -24.513 1.00 31.51  ?  760 HOH B O     1 
HETATM 10422 O  O     . HOH GA 10 .   ? 76.500 25.403  -11.263 1.00 32.49  ?  701 HOH C O     1 
HETATM 10423 O  O     . HOH GA 10 .   ? 62.516 32.662  -2.863  1.00 30.00  ?  702 HOH C O     1 
HETATM 10424 O  O     . HOH GA 10 .   ? 51.488 31.859  -15.197 1.00 18.32  ?  703 HOH C O     1 
HETATM 10425 O  O     . HOH GA 10 .   ? 58.589 5.957   -5.164  1.00 30.00  ?  704 HOH C O     1 
HETATM 10426 O  O     . HOH GA 10 .   ? 70.347 25.776  -8.962  1.00 17.94  ?  705 HOH C O     1 
HETATM 10427 O  O     . HOH GA 10 .   ? 66.100 19.104  -0.659  1.00 16.29  ?  706 HOH C O     1 
HETATM 10428 O  O     . HOH GA 10 .   ? 58.320 26.691  -18.809 1.00 22.62  ?  707 HOH C O     1 
HETATM 10429 O  O     . HOH GA 10 .   ? 66.147 11.497  8.743   1.00 25.26  ?  708 HOH C O     1 
HETATM 10430 O  O     . HOH GA 10 .   ? 76.056 16.135  -6.918  1.00 25.79  ?  709 HOH C O     1 
HETATM 10431 O  O     . HOH GA 10 .   ? 50.820 39.481  9.843   1.00 25.99  ?  710 HOH C O     1 
HETATM 10432 O  O     . HOH GA 10 .   ? 74.552 20.856  -15.838 1.00 24.23  ?  711 HOH C O     1 
HETATM 10433 O  O     . HOH GA 10 .   ? 84.599 25.358  -13.119 1.00 27.49  ?  712 HOH C O     1 
HETATM 10434 O  O     . HOH GA 10 .   ? 63.036 26.771  -7.580  1.00 17.63  ?  713 HOH C O     1 
HETATM 10435 O  O     . HOH GA 10 .   ? 42.208 25.487  4.532   1.00 15.16  ?  714 HOH C O     1 
HETATM 10436 O  O     . HOH GA 10 .   ? 64.153 28.885  4.005   1.00 18.63  ?  715 HOH C O     1 
HETATM 10437 O  O     . HOH GA 10 .   ? 86.463 21.264  -11.066 1.00 19.38  ?  716 HOH C O     1 
HETATM 10438 O  O     . HOH GA 10 .   ? 66.817 15.638  13.315  1.00 11.97  ?  717 HOH C O     1 
HETATM 10439 O  O     . HOH GA 10 .   ? 47.531 29.047  17.890  1.00 24.22  ?  718 HOH C O     1 
HETATM 10440 O  O     . HOH GA 10 .   ? 46.854 13.794  8.791   1.00 35.68  ?  719 HOH C O     1 
HETATM 10441 O  O     . HOH GA 10 .   ? 62.444 20.648  -9.990  1.00 29.22  ?  720 HOH C O     1 
HETATM 10442 O  O     . HOH GA 10 .   ? 72.942 17.400  3.317   1.00 14.17  ?  721 HOH C O     1 
HETATM 10443 O  O     . HOH GA 10 .   ? 56.544 22.574  -3.739  1.00 13.39  ?  722 HOH C O     1 
HETATM 10444 O  O     . HOH GA 10 .   ? 63.116 29.901  -0.201  1.00 21.73  ?  723 HOH C O     1 
HETATM 10445 O  O     . HOH GA 10 .   ? 59.625 28.353  1.734   1.00 87.38  ?  724 HOH C O     1 
HETATM 10446 O  O     . HOH GA 10 .   ? 73.641 36.122  -12.387 1.00 20.74  ?  725 HOH C O     1 
HETATM 10447 O  O     . HOH GA 10 .   ? 43.618 12.619  7.488   1.00 28.93  ?  726 HOH C O     1 
HETATM 10448 O  O     . HOH GA 10 .   ? 69.355 21.108  19.930  1.00 7.18   ?  727 HOH C O     1 
HETATM 10449 O  O     . HOH GA 10 .   ? 64.442 21.561  3.606   1.00 4.28   ?  728 HOH C O     1 
HETATM 10450 O  O     . HOH GA 10 .   ? 57.965 38.048  -2.072  1.00 22.45  ?  729 HOH C O     1 
HETATM 10451 O  O     . HOH GA 10 .   ? 66.782 31.840  -1.878  1.00 21.21  ?  730 HOH C O     1 
HETATM 10452 O  O     . HOH GA 10 .   ? 55.871 35.769  14.403  1.00 7.48   ?  731 HOH C O     1 
HETATM 10453 O  O     . HOH GA 10 .   ? 71.502 34.982  -17.733 1.00 12.08  ?  732 HOH C O     1 
HETATM 10454 O  O     . HOH GA 10 .   ? 49.568 41.544  7.922   1.00 12.13  ?  733 HOH C O     1 
HETATM 10455 O  O     . HOH GA 10 .   ? 70.233 13.075  5.542   1.00 2.00   ?  734 HOH C O     1 
HETATM 10456 O  O     . HOH GA 10 .   ? 53.700 17.850  13.858  1.00 30.00  ?  735 HOH C O     1 
HETATM 10457 O  O     . HOH GA 10 .   ? 44.026 27.179  9.170   1.00 14.16  ?  736 HOH C O     1 
HETATM 10458 O  O     . HOH GA 10 .   ? 66.363 31.384  17.199  1.00 8.48   ?  737 HOH C O     1 
HETATM 10459 O  O     . HOH GA 10 .   ? 69.626 7.883   -1.238  1.00 26.70  ?  738 HOH C O     1 
HETATM 10460 O  O     . HOH GA 10 .   ? 68.795 31.176  19.970  1.00 15.26  ?  739 HOH C O     1 
HETATM 10461 O  O     . HOH GA 10 .   ? 67.746 34.227  -7.570  1.00 10.78  ?  740 HOH C O     1 
HETATM 10462 O  O     . HOH GA 10 .   ? 69.059 43.483  12.947  1.00 16.02  ?  741 HOH C O     1 
HETATM 10463 O  O     . HOH GA 10 .   ? 60.458 32.488  15.520  1.00 7.64   ?  742 HOH C O     1 
HETATM 10464 O  O     . HOH GA 10 .   ? 60.159 40.988  -29.896 1.00 30.00  ?  743 HOH C O     1 
HETATM 10465 O  O     . HOH GA 10 .   ? 52.284 8.454   5.008   1.00 11.88  ?  744 HOH C O     1 
HETATM 10466 O  O     . HOH GA 10 .   ? 68.721 42.478  -27.037 1.00 22.34  ?  745 HOH C O     1 
HETATM 10467 O  O     . HOH GA 10 .   ? 38.798 8.780   0.251   1.00 13.75  ?  746 HOH C O     1 
HETATM 10468 O  O     . HOH GA 10 .   ? 39.056 34.612  8.233   1.00 9.15   ?  747 HOH C O     1 
HETATM 10469 O  O     . HOH GA 10 .   ? 62.551 14.241  19.241  1.00 20.05  ?  748 HOH C O     1 
HETATM 10470 O  O     . HOH GA 10 .   ? 58.453 4.519   -0.565  1.00 2.00   ?  749 HOH C O     1 
HETATM 10471 O  O     . HOH GA 10 .   ? 48.626 28.346  20.627  1.00 3.56   ?  750 HOH C O     1 
HETATM 10472 O  O     . HOH GA 10 .   ? 54.389 21.468  20.655  1.00 8.76   ?  751 HOH C O     1 
# 
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   PRO 1   33  33  PRO PRO A . n 
A 1 2   PRO 2   34  34  PRO PRO A . n 
A 1 3   PRO 3   35  35  PRO PRO A . n 
A 1 4   ALA 4   36  36  ALA ALA A . n 
A 1 5   ILE 5   37  37  ILE ILE A . n 
A 1 6   GLY 6   38  38  GLY GLY A . n 
A 1 7   GLN 7   39  39  GLN GLN A . n 
A 1 8   PHE 8   40  40  PHE PHE A . n 
A 1 9   TRP 9   41  41  TRP TRP A . n 
A 1 10  HIS 10  42  42  HIS HIS A . n 
A 1 11  VAL 11  43  43  VAL VAL A . n 
A 1 12  THR 12  44  44  THR THR A . n 
A 1 13  ASP 13  45  45  ASP ASP A . n 
A 1 14  LEU 14  46  46  LEU LEU A . n 
A 1 15  HIS 15  47  47  HIS HIS A . n 
A 1 16  LEU 16  48  48  LEU LEU A . n 
A 1 17  ASP 17  49  49  ASP ASP A . n 
A 1 18  PRO 18  50  50  PRO PRO A . n 
A 1 19  THR 19  51  51  THR THR A . n 
A 1 20  TYR 20  52  52  TYR TYR A . n 
A 1 21  HIS 21  53  53  HIS HIS A . n 
A 1 22  ILE 22  54  54  ILE ILE A . n 
A 1 23  THR 23  55  55  THR THR A . n 
A 1 24  ASP 24  56  56  ASP ASP A . n 
A 1 25  ASP 25  57  57  ASP ASP A . n 
A 1 26  HIS 26  58  58  HIS HIS A . n 
A 1 27  THR 27  59  59  THR THR A . n 
A 1 28  LYS 28  60  60  LYS LYS A . n 
A 1 29  VAL 29  61  61  VAL VAL A . n 
A 1 30  CYS 30  62  62  CYS CYS A . n 
A 1 31  ALA 31  63  63  ALA ALA A . n 
A 1 32  SER 32  64  64  SER SER A . n 
A 1 33  SER 33  65  65  SER SER A . n 
A 1 34  LYS 34  66  66  LYS LYS A . n 
A 1 35  GLY 35  67  67  GLY GLY A . n 
A 1 36  ALA 36  68  68  ALA ALA A . n 
A 1 37  ASN 37  69  69  ASN ASN A . n 
A 1 38  ALA 38  70  70  ALA ALA A . n 
A 1 39  SER 39  71  71  SER SER A . n 
A 1 40  ASN 40  72  72  ASN ASN A . n 
A 1 41  PRO 41  73  73  PRO PRO A . n 
A 1 42  GLY 42  74  74  GLY GLY A . n 
A 1 43  PRO 43  75  75  PRO PRO A . n 
A 1 44  PHE 44  76  76  PHE PHE A . n 
A 1 45  GLY 45  77  77  GLY GLY A . n 
A 1 46  ASP 46  78  78  ASP ASP A . n 
A 1 47  VAL 47  79  79  VAL VAL A . n 
A 1 48  LEU 48  80  80  LEU LEU A . n 
A 1 49  CYS 49  81  81  CYS CYS A . n 
A 1 50  ASP 50  82  82  ASP ASP A . n 
A 1 51  SER 51  83  83  SER SER A . n 
A 1 52  PRO 52  84  84  PRO PRO A . n 
A 1 53  TYR 53  85  85  TYR TYR A . n 
A 1 54  GLN 54  86  86  GLN GLN A . n 
A 1 55  LEU 55  87  87  LEU LEU A . n 
A 1 56  ILE 56  88  88  ILE ILE A . n 
A 1 57  LEU 57  89  89  LEU LEU A . n 
A 1 58  SER 58  90  90  SER SER A . n 
A 1 59  ALA 59  91  91  ALA ALA A . n 
A 1 60  PHE 60  92  92  PHE PHE A . n 
A 1 61  ASP 61  93  93  ASP ASP A . n 
A 1 62  PHE 62  94  94  PHE PHE A . n 
A 1 63  ILE 63  95  95  ILE ILE A . n 
A 1 64  LYS 64  96  96  LYS LYS A . n 
A 1 65  ASN 65  97  97  ASN ASN A . n 
A 1 66  SER 66  98  98  SER SER A . n 
A 1 67  GLY 67  99  99  GLY GLY A . n 
A 1 68  GLN 68  100 100 GLN GLN A . n 
A 1 69  GLU 69  101 101 GLU GLU A . n 
A 1 70  ALA 70  102 102 ALA ALA A . n 
A 1 71  SER 71  103 103 SER SER A . n 
A 1 72  PHE 72  104 104 PHE PHE A . n 
A 1 73  MET 73  105 105 MET MET A . n 
A 1 74  ILE 74  106 106 ILE ILE A . n 
A 1 75  TRP 75  107 107 TRP TRP A . n 
A 1 76  THR 76  108 108 THR THR A . n 
A 1 77  GLY 77  109 109 GLY GLY A . n 
A 1 78  ASP 78  110 110 ASP ASP A . n 
A 1 79  SER 79  111 111 SER SER A . n 
A 1 80  PRO 80  112 112 PRO PRO A . n 
A 1 81  PRO 81  113 113 PRO PRO A . n 
A 1 82  HIS 82  114 114 HIS HIS A . n 
A 1 83  VAL 83  115 115 VAL VAL A . n 
A 1 84  PRO 84  116 116 PRO PRO A . n 
A 1 85  VAL 85  117 117 VAL VAL A . n 
A 1 86  PRO 86  118 118 PRO PRO A . n 
A 1 87  GLU 87  119 119 GLU GLU A . n 
A 1 88  LEU 88  120 120 LEU LEU A . n 
A 1 89  SER 89  121 121 SER SER A . n 
A 1 90  THR 90  122 122 THR THR A . n 
A 1 91  ASP 91  123 123 ASP ASP A . n 
A 1 92  THR 92  124 124 THR THR A . n 
A 1 93  VAL 93  125 125 VAL VAL A . n 
A 1 94  ILE 94  126 126 ILE ILE A . n 
A 1 95  ASN 95  127 127 ASN ASN A . n 
A 1 96  VAL 96  128 128 VAL VAL A . n 
A 1 97  ILE 97  129 129 ILE ILE A . n 
A 1 98  THR 98  130 130 THR THR A . n 
A 1 99  ASN 99  131 131 ASN ASN A . n 
A 1 100 MET 100 132 132 MET MET A . n 
A 1 101 THR 101 133 133 THR THR A . n 
A 1 102 THR 102 134 134 THR THR A . n 
A 1 103 THR 103 135 135 THR THR A . n 
A 1 104 ILE 104 136 136 ILE ILE A . n 
A 1 105 GLN 105 137 137 GLN GLN A . n 
A 1 106 SER 106 138 138 SER SER A . n 
A 1 107 LEU 107 139 139 LEU LEU A . n 
A 1 108 PHE 108 140 140 PHE PHE A . n 
A 1 109 PRO 109 141 141 PRO PRO A . n 
A 1 110 ASN 110 142 142 ASN ASN A . n 
A 1 111 LEU 111 143 143 LEU LEU A . n 
A 1 112 GLN 112 144 144 GLN GLN A . n 
A 1 113 VAL 113 145 145 VAL VAL A . n 
A 1 114 PHE 114 146 146 PHE PHE A . n 
A 1 115 PRO 115 147 147 PRO PRO A . n 
A 1 116 ALA 116 148 148 ALA ALA A . n 
A 1 117 LEU 117 149 149 LEU LEU A . n 
A 1 118 GLY 118 150 150 GLY GLY A . n 
A 1 119 ASN 119 151 151 ASN ASN A . n 
A 1 120 HIS 120 152 152 HIS HIS A . n 
A 1 121 ASP 121 153 153 ASP ASP A . n 
A 1 122 TYR 122 154 154 TYR TYR A . n 
A 1 123 TRP 123 155 155 TRP TRP A . n 
A 1 124 PRO 124 156 156 PRO PRO A . n 
A 1 125 GLN 125 157 157 GLN GLN A . n 
A 1 126 ASP 126 158 158 ASP ASP A . n 
A 1 127 GLN 127 159 159 GLN GLN A . n 
A 1 128 LEU 128 160 160 LEU LEU A . n 
A 1 129 PRO 129 161 161 PRO PRO A . n 
A 1 130 VAL 130 162 162 VAL VAL A . n 
A 1 131 VAL 131 163 163 VAL VAL A . n 
A 1 132 THR 132 164 164 THR THR A . n 
A 1 133 SER 133 165 165 SER SER A . n 
A 1 134 LYS 134 166 166 LYS LYS A . n 
A 1 135 VAL 135 167 167 VAL VAL A . n 
A 1 136 TYR 136 168 168 TYR TYR A . n 
A 1 137 ASN 137 169 169 ASN ASN A . n 
A 1 138 ALA 138 170 170 ALA ALA A . n 
A 1 139 VAL 139 171 171 VAL VAL A . n 
A 1 140 ALA 140 172 172 ALA ALA A . n 
A 1 141 ASN 141 173 173 ASN ASN A . n 
A 1 142 LEU 142 174 174 LEU LEU A . n 
A 1 143 TRP 143 175 175 TRP TRP A . n 
A 1 144 LYS 144 176 176 LYS LYS A . n 
A 1 145 PRO 145 177 177 PRO PRO A . n 
A 1 146 TRP 146 178 178 TRP TRP A . n 
A 1 147 LEU 147 179 179 LEU LEU A . n 
A 1 148 ASP 148 180 180 ASP ASP A . n 
A 1 149 GLU 149 181 181 GLU GLU A . n 
A 1 150 GLU 150 182 182 GLU GLU A . n 
A 1 151 ALA 151 183 183 ALA ALA A . n 
A 1 152 ILE 152 184 184 ILE ILE A . n 
A 1 153 SER 153 185 185 SER SER A . n 
A 1 154 THR 154 186 186 THR THR A . n 
A 1 155 LEU 155 187 187 LEU LEU A . n 
A 1 156 ARG 156 188 188 ARG ARG A . n 
A 1 157 LYS 157 189 189 LYS LYS A . n 
A 1 158 GLY 158 190 190 GLY GLY A . n 
A 1 159 GLY 159 191 191 GLY GLY A . n 
A 1 160 PHE 160 192 192 PHE PHE A . n 
A 1 161 TYR 161 193 193 TYR TYR A . n 
A 1 162 SER 162 194 194 SER SER A . n 
A 1 163 GLN 163 195 195 GLN GLN A . n 
A 1 164 LYS 164 196 196 LYS LYS A . n 
A 1 165 VAL 165 197 197 VAL VAL A . n 
A 1 166 THR 166 198 198 THR THR A . n 
A 1 167 THR 167 199 199 THR THR A . n 
A 1 168 ASN 168 200 200 ASN ASN A . n 
A 1 169 PRO 169 201 201 PRO PRO A . n 
A 1 170 ASN 170 202 202 ASN ASN A . n 
A 1 171 LEU 171 203 203 LEU LEU A . n 
A 1 172 ARG 172 204 204 ARG ARG A . n 
A 1 173 ILE 173 205 205 ILE ILE A . n 
A 1 174 ILE 174 206 206 ILE ILE A . n 
A 1 175 SER 175 207 207 SER SER A . n 
A 1 176 LEU 176 208 208 LEU LEU A . n 
A 1 177 ASN 177 209 209 ASN ASN A . n 
A 1 178 THR 178 210 210 THR THR A . n 
A 1 179 ASN 179 211 211 ASN ASN A . n 
A 1 180 LEU 180 212 212 LEU LEU A . n 
A 1 181 TYR 181 213 213 TYR TYR A . n 
A 1 182 TYR 182 214 214 TYR TYR A . n 
A 1 183 GLY 183 215 215 GLY GLY A . n 
A 1 184 PRO 184 216 216 PRO PRO A . n 
A 1 185 ASN 185 217 217 ASN ASN A . n 
A 1 186 ILE 186 218 218 ILE ILE A . n 
A 1 187 MET 187 219 219 MET MET A . n 
A 1 188 THR 188 220 220 THR THR A . n 
A 1 189 LEU 189 221 221 LEU LEU A . n 
A 1 190 ASN 190 222 222 ASN ASN A . n 
A 1 191 LYS 191 223 223 LYS LYS A . n 
A 1 192 THR 192 224 224 THR THR A . n 
A 1 193 ASP 193 225 225 ASP ASP A . n 
A 1 194 PRO 194 226 226 PRO PRO A . n 
A 1 195 ALA 195 227 227 ALA ALA A . n 
A 1 196 ASN 196 228 228 ASN ASN A . n 
A 1 197 GLN 197 229 229 GLN GLN A . n 
A 1 198 PHE 198 230 230 PHE PHE A . n 
A 1 199 GLU 199 231 231 GLU GLU A . n 
A 1 200 TRP 200 232 232 TRP TRP A . n 
A 1 201 LEU 201 233 233 LEU LEU A . n 
A 1 202 GLU 202 234 234 GLU GLU A . n 
A 1 203 SER 203 235 235 SER SER A . n 
A 1 204 THR 204 236 236 THR THR A . n 
A 1 205 LEU 205 237 237 LEU LEU A . n 
A 1 206 ASN 206 238 238 ASN ASN A . n 
A 1 207 ASN 207 239 239 ASN ASN A . n 
A 1 208 SER 208 240 240 SER SER A . n 
A 1 209 GLN 209 241 241 GLN GLN A . n 
A 1 210 GLN 210 242 242 GLN GLN A . n 
A 1 211 ASN 211 243 243 ASN ASN A . n 
A 1 212 LYS 212 244 244 LYS LYS A . n 
A 1 213 GLU 213 245 245 GLU GLU A . n 
A 1 214 LYS 214 246 246 LYS LYS A . n 
A 1 215 VAL 215 247 247 VAL VAL A . n 
A 1 216 TYR 216 248 248 TYR TYR A . n 
A 1 217 ILE 217 249 249 ILE ILE A . n 
A 1 218 ILE 218 250 250 ILE ILE A . n 
A 1 219 ALA 219 251 251 ALA ALA A . n 
A 1 220 HIS 220 252 252 HIS HIS A . n 
A 1 221 VAL 221 253 253 VAL VAL A . n 
A 1 222 PRO 222 254 254 PRO PRO A . n 
A 1 223 VAL 223 255 255 VAL VAL A . n 
A 1 224 GLY 224 256 256 GLY GLY A . n 
A 1 225 TYR 225 257 257 TYR TYR A . n 
A 1 226 LEU 226 258 258 LEU LEU A . n 
A 1 227 PRO 227 259 259 PRO PRO A . n 
A 1 228 SER 228 260 260 SER SER A . n 
A 1 229 SER 229 261 261 SER SER A . n 
A 1 230 GLN 230 262 262 GLN GLN A . n 
A 1 231 ASN 231 263 263 ASN ASN A . n 
A 1 232 ILE 232 264 264 ILE ILE A . n 
A 1 233 THR 233 265 265 THR THR A . n 
A 1 234 ALA 234 266 266 ALA ALA A . n 
A 1 235 MET 235 267 267 MET MET A . n 
A 1 236 ARG 236 268 268 ARG ARG A . n 
A 1 237 GLU 237 269 269 GLU GLU A . n 
A 1 238 TYR 238 270 270 TYR TYR A . n 
A 1 239 TYR 239 271 271 TYR TYR A . n 
A 1 240 ASN 240 272 272 ASN ASN A . n 
A 1 241 GLU 241 273 273 GLU GLU A . n 
A 1 242 LYS 242 274 274 LYS LYS A . n 
A 1 243 LEU 243 275 275 LEU LEU A . n 
A 1 244 ILE 244 276 276 ILE ILE A . n 
A 1 245 ASP 245 277 277 ASP ASP A . n 
A 1 246 ILE 246 278 278 ILE ILE A . n 
A 1 247 PHE 247 279 279 PHE PHE A . n 
A 1 248 GLN 248 280 280 GLN GLN A . n 
A 1 249 LYS 249 281 281 LYS LYS A . n 
A 1 250 TYR 250 282 282 TYR TYR A . n 
A 1 251 SER 251 283 283 SER SER A . n 
A 1 252 ASP 252 284 284 ASP ASP A . n 
A 1 253 VAL 253 285 285 VAL VAL A . n 
A 1 254 ILE 254 286 286 ILE ILE A . n 
A 1 255 ALA 255 287 287 ALA ALA A . n 
A 1 256 GLY 256 288 288 GLY GLY A . n 
A 1 257 GLN 257 289 289 GLN GLN A . n 
A 1 258 PHE 258 290 290 PHE PHE A . n 
A 1 259 TYR 259 291 291 TYR TYR A . n 
A 1 260 GLY 260 292 292 GLY GLY A . n 
A 1 261 HIS 261 293 293 HIS HIS A . n 
A 1 262 THR 262 294 294 THR THR A . n 
A 1 263 HIS 263 295 295 HIS HIS A . n 
A 1 264 ARG 264 296 296 ARG ARG A . n 
A 1 265 ASP 265 297 297 ASP ASP A . n 
A 1 266 SER 266 298 298 SER SER A . n 
A 1 267 ILE 267 299 299 ILE ILE A . n 
A 1 268 MET 268 300 300 MET MET A . n 
A 1 269 VAL 269 301 301 VAL VAL A . n 
A 1 270 LEU 270 302 302 LEU LEU A . n 
A 1 271 SER 271 303 303 SER SER A . n 
A 1 272 ASP 272 304 304 ASP ASP A . n 
A 1 273 LYS 273 305 305 LYS LYS A . n 
A 1 274 LYS 274 306 306 LYS LYS A . n 
A 1 275 GLY 275 307 307 GLY GLY A . n 
A 1 276 SER 276 308 308 SER SER A . n 
A 1 277 PRO 277 309 309 PRO PRO A . n 
A 1 278 VAL 278 310 310 VAL VAL A . n 
A 1 279 ASN 279 311 311 ASN ASN A . n 
A 1 280 SER 280 312 312 SER SER A . n 
A 1 281 LEU 281 313 313 LEU LEU A . n 
A 1 282 PHE 282 314 314 PHE PHE A . n 
A 1 283 VAL 283 315 315 VAL VAL A . n 
A 1 284 ALA 284 316 316 ALA ALA A . n 
A 1 285 PRO 285 317 317 PRO PRO A . n 
A 1 286 ALA 286 318 318 ALA ALA A . n 
A 1 287 VAL 287 319 319 VAL VAL A . n 
A 1 288 THR 288 320 320 THR THR A . n 
A 1 289 PRO 289 321 321 PRO PRO A . n 
A 1 290 VAL 290 322 322 VAL VAL A . n 
A 1 291 LYS 291 323 323 LYS LYS A . n 
A 1 292 SER 292 324 324 SER SER A . n 
A 1 293 VAL 293 325 325 VAL VAL A . n 
A 1 294 LEU 294 326 326 LEU LEU A . n 
A 1 295 GLU 295 327 327 GLU GLU A . n 
A 1 296 LYS 296 328 328 LYS LYS A . n 
A 1 297 GLN 297 329 329 GLN GLN A . n 
A 1 298 THR 298 330 330 THR THR A . n 
A 1 299 ASN 299 331 331 ASN ASN A . n 
A 1 300 ASN 300 332 332 ASN ASN A . n 
A 1 301 PRO 301 333 333 PRO PRO A . n 
A 1 302 GLY 302 334 334 GLY GLY A . n 
A 1 303 ILE 303 335 335 ILE ILE A . n 
A 1 304 ARG 304 336 336 ARG ARG A . n 
A 1 305 LEU 305 337 337 LEU LEU A . n 
A 1 306 PHE 306 338 338 PHE PHE A . n 
A 1 307 GLN 307 339 339 GLN GLN A . n 
A 1 308 TYR 308 340 340 TYR TYR A . n 
A 1 309 ASP 309 341 341 ASP ASP A . n 
A 1 310 PRO 310 342 342 PRO PRO A . n 
A 1 311 ARG 311 343 343 ARG ARG A . n 
A 1 312 ASP 312 344 344 ASP ASP A . n 
A 1 313 TYR 313 345 345 TYR TYR A . n 
A 1 314 LYS 314 346 346 LYS LYS A . n 
A 1 315 LEU 315 347 347 LEU LEU A . n 
A 1 316 LEU 316 348 348 LEU LEU A . n 
A 1 317 ASP 317 349 349 ASP ASP A . n 
A 1 318 MET 318 350 350 MET MET A . n 
A 1 319 LEU 319 351 351 LEU LEU A . n 
A 1 320 GLN 320 352 352 GLN GLN A . n 
A 1 321 TYR 321 353 353 TYR TYR A . n 
A 1 322 TYR 322 354 354 TYR TYR A . n 
A 1 323 LEU 323 355 355 LEU LEU A . n 
A 1 324 ASN 324 356 356 ASN ASN A . n 
A 1 325 LEU 325 357 357 LEU LEU A . n 
A 1 326 THR 326 358 358 THR THR A . n 
A 1 327 GLU 327 359 359 GLU GLU A . n 
A 1 328 ALA 328 360 360 ALA ALA A . n 
A 1 329 ASN 329 361 361 ASN ASN A . n 
A 1 330 LEU 330 362 362 LEU LEU A . n 
A 1 331 LYS 331 363 363 LYS LYS A . n 
A 1 332 GLY 332 364 364 GLY GLY A . n 
A 1 333 GLU 333 365 365 GLU GLU A . n 
A 1 334 SER 334 366 366 SER SER A . n 
A 1 335 ILE 335 367 367 ILE ILE A . n 
A 1 336 TRP 336 368 368 TRP TRP A . n 
A 1 337 LYS 337 369 369 LYS LYS A . n 
A 1 338 LEU 338 370 370 LEU LEU A . n 
A 1 339 GLU 339 371 371 GLU GLU A . n 
A 1 340 TYR 340 372 372 TYR TYR A . n 
A 1 341 ILE 341 373 373 ILE ILE A . n 
A 1 342 LEU 342 374 374 LEU LEU A . n 
A 1 343 THR 343 375 375 THR THR A . n 
A 1 344 GLN 344 376 376 GLN GLN A . n 
A 1 345 THR 345 377 377 THR THR A . n 
A 1 346 TYR 346 378 378 TYR TYR A . n 
A 1 347 ASP 347 379 379 ASP ASP A . n 
A 1 348 ILE 348 380 380 ILE ILE A . n 
A 1 349 GLU 349 381 381 GLU GLU A . n 
A 1 350 ASP 350 382 382 ASP ASP A . n 
A 1 351 LEU 351 383 383 LEU LEU A . n 
A 1 352 GLN 352 384 384 GLN GLN A . n 
A 1 353 PRO 353 385 385 PRO PRO A . n 
A 1 354 GLU 354 386 386 GLU GLU A . n 
A 1 355 SER 355 387 387 SER SER A . n 
A 1 356 LEU 356 388 388 LEU LEU A . n 
A 1 357 TYR 357 389 389 TYR TYR A . n 
A 1 358 GLY 358 390 390 GLY GLY A . n 
A 1 359 LEU 359 391 391 LEU LEU A . n 
A 1 360 ALA 360 392 392 ALA ALA A . n 
A 1 361 LYS 361 393 393 LYS LYS A . n 
A 1 362 GLN 362 394 394 GLN GLN A . n 
A 1 363 PHE 363 395 395 PHE PHE A . n 
A 1 364 THR 364 396 396 THR THR A . n 
A 1 365 ILE 365 397 397 ILE ILE A . n 
A 1 366 LEU 366 398 398 LEU LEU A . n 
A 1 367 ASP 367 399 399 ASP ASP A . n 
A 1 368 SER 368 400 400 SER SER A . n 
A 1 369 LYS 369 401 401 LYS LYS A . n 
A 1 370 GLN 370 402 402 GLN GLN A . n 
A 1 371 PHE 371 403 403 PHE PHE A . n 
A 1 372 ILE 372 404 404 ILE ILE A . n 
A 1 373 LYS 373 405 405 LYS LYS A . n 
A 1 374 TYR 374 406 406 TYR TYR A . n 
A 1 375 TYR 375 407 407 TYR TYR A . n 
A 1 376 ASN 376 408 408 ASN ASN A . n 
A 1 377 TYR 377 409 409 TYR TYR A . n 
A 1 378 PHE 378 410 410 PHE PHE A . n 
A 1 379 PHE 379 411 411 PHE PHE A . n 
A 1 380 VAL 380 412 412 VAL VAL A . n 
A 1 381 SER 381 413 413 SER SER A . n 
A 1 382 TYR 382 414 414 TYR TYR A . n 
A 1 383 ASP 383 415 415 ASP ASP A . n 
A 1 384 SER 384 416 416 SER SER A . n 
A 1 385 SER 385 417 417 SER SER A . n 
A 1 386 VAL 386 418 418 VAL VAL A . n 
A 1 387 THR 387 419 419 THR THR A . n 
A 1 388 CYS 388 420 420 CYS CYS A . n 
A 1 389 ASP 389 421 421 ASP ASP A . n 
A 1 390 LYS 390 422 422 LYS LYS A . n 
A 1 391 THR 391 423 423 THR THR A . n 
A 1 392 CYS 392 424 424 CYS CYS A . n 
A 1 393 LYS 393 425 425 LYS LYS A . n 
A 1 394 ALA 394 426 426 ALA ALA A . n 
A 1 395 PHE 395 427 427 PHE PHE A . n 
A 1 396 GLN 396 428 428 GLN GLN A . n 
A 1 397 ILE 397 429 429 ILE ILE A . n 
A 1 398 CYS 398 430 430 CYS CYS A . n 
A 1 399 ALA 399 431 431 ALA ALA A . n 
A 1 400 ILE 400 432 432 ILE ILE A . n 
A 1 401 MET 401 433 433 MET MET A . n 
A 1 402 ASN 402 434 434 ASN ASN A . n 
A 1 403 LEU 403 435 435 LEU LEU A . n 
A 1 404 ASP 404 436 436 ASP ASP A . n 
A 1 405 ASN 405 437 437 ASN ASN A . n 
A 1 406 ILE 406 438 438 ILE ILE A . n 
A 1 407 SER 407 439 439 SER SER A . n 
A 1 408 TYR 408 440 440 TYR TYR A . n 
A 1 409 ALA 409 441 441 ALA ALA A . n 
A 1 410 ASP 410 442 442 ASP ASP A . n 
A 1 411 CYS 411 443 443 CYS CYS A . n 
A 1 412 LEU 412 444 444 LEU LEU A . n 
A 1 413 LYS 413 445 445 LYS LYS A . n 
A 1 414 GLN 414 446 446 GLN GLN A . n 
A 1 415 LEU 415 447 447 LEU LEU A . n 
A 1 416 TYR 416 448 448 TYR TYR A . n 
A 1 417 ILE 417 449 449 ILE ILE A . n 
A 1 418 LYS 418 450 450 LYS LYS A . n 
B 2 1   PRO 1   33  33  PRO PRO B . n 
B 2 2   PRO 2   34  34  PRO PRO B . n 
B 2 3   PRO 3   35  35  PRO PRO B . n 
B 2 4   ALA 4   36  36  ALA ALA B . n 
B 2 5   ILE 5   37  37  ILE ILE B . n 
B 2 6   GLY 6   38  38  GLY GLY B . n 
B 2 7   GLN 7   39  39  GLN GLN B . n 
B 2 8   PHE 8   40  40  PHE PHE B . n 
B 2 9   TRP 9   41  41  TRP TRP B . n 
B 2 10  HIS 10  42  42  HIS HIS B . n 
B 2 11  VAL 11  43  43  VAL VAL B . n 
B 2 12  THR 12  44  44  THR THR B . n 
B 2 13  ASP 13  45  45  ASP ASP B . n 
B 2 14  LEU 14  46  46  LEU LEU B . n 
B 2 15  HIS 15  47  47  HIS HIS B . n 
B 2 16  LEU 16  48  48  LEU LEU B . n 
B 2 17  ASP 17  49  49  ASP ASP B . n 
B 2 18  PRO 18  50  50  PRO PRO B . n 
B 2 19  THR 19  51  51  THR THR B . n 
B 2 20  TYR 20  52  52  TYR TYR B . n 
B 2 21  HIS 21  53  53  HIS HIS B . n 
B 2 22  ILE 22  54  54  ILE ILE B . n 
B 2 23  THR 23  55  55  THR THR B . n 
B 2 24  ASP 24  56  56  ASP ASP B . n 
B 2 25  ASP 25  57  57  ASP ASP B . n 
B 2 26  HIS 26  58  58  HIS HIS B . n 
B 2 27  THR 27  59  59  THR THR B . n 
B 2 28  LYS 28  60  60  LYS LYS B . n 
B 2 29  VAL 29  61  61  VAL VAL B . n 
B 2 30  CYS 30  62  62  CYS CYS B . n 
B 2 31  ALA 31  63  63  ALA ALA B . n 
B 2 32  SER 32  64  64  SER SER B . n 
B 2 33  SER 33  65  65  SER SER B . n 
B 2 34  LYS 34  66  66  LYS LYS B . n 
B 2 35  GLY 35  67  67  GLY GLY B . n 
B 2 36  ALA 36  68  68  ALA ALA B . n 
B 2 37  ASN 37  69  69  ASN ASN B . n 
B 2 38  ALA 38  70  70  ALA ALA B . n 
B 2 39  SER 39  71  71  SER SER B . n 
B 2 40  ASN 40  72  72  ASN ASN B . n 
B 2 41  PRO 41  73  73  PRO PRO B . n 
B 2 42  GLY 42  74  74  GLY GLY B . n 
B 2 43  PRO 43  75  75  PRO PRO B . n 
B 2 44  PHE 44  76  76  PHE PHE B . n 
B 2 45  GLY 45  77  77  GLY GLY B . n 
B 2 46  ASP 46  78  78  ASP ASP B . n 
B 2 47  VAL 47  79  79  VAL VAL B . n 
B 2 48  LEU 48  80  80  LEU LEU B . n 
B 2 49  CYS 49  81  81  CYS CYS B . n 
B 2 50  ASP 50  82  82  ASP ASP B . n 
B 2 51  SER 51  83  83  SER SER B . n 
B 2 52  PRO 52  84  84  PRO PRO B . n 
B 2 53  TYR 53  85  85  TYR TYR B . n 
B 2 54  GLN 54  86  86  GLN GLN B . n 
B 2 55  LEU 55  87  87  LEU LEU B . n 
B 2 56  ILE 56  88  88  ILE ILE B . n 
B 2 57  LEU 57  89  89  LEU LEU B . n 
B 2 58  SER 58  90  90  SER SER B . n 
B 2 59  ALA 59  91  91  ALA ALA B . n 
B 2 60  PHE 60  92  92  PHE PHE B . n 
B 2 61  ASP 61  93  93  ASP ASP B . n 
B 2 62  PHE 62  94  94  PHE PHE B . n 
B 2 63  ILE 63  95  95  ILE ILE B . n 
B 2 64  LYS 64  96  96  LYS LYS B . n 
B 2 65  ASN 65  97  97  ASN ASN B . n 
B 2 66  SER 66  98  98  SER SER B . n 
B 2 67  GLY 67  99  99  GLY GLY B . n 
B 2 68  GLN 68  100 100 GLN GLN B . n 
B 2 69  GLU 69  101 101 GLU GLU B . n 
B 2 70  ALA 70  102 102 ALA ALA B . n 
B 2 71  SER 71  103 103 SER SER B . n 
B 2 72  PHE 72  104 104 PHE PHE B . n 
B 2 73  MET 73  105 105 MET MET B . n 
B 2 74  ILE 74  106 106 ILE ILE B . n 
B 2 75  TRP 75  107 107 TRP TRP B . n 
B 2 76  THR 76  108 108 THR THR B . n 
B 2 77  GLY 77  109 109 GLY GLY B . n 
B 2 78  ASP 78  110 110 ASP ASP B . n 
B 2 79  SER 79  111 111 SER SER B . n 
B 2 80  PRO 80  112 112 PRO PRO B . n 
B 2 81  PRO 81  113 113 PRO PRO B . n 
B 2 82  HIS 82  114 114 HIS HIS B . n 
B 2 83  VAL 83  115 115 VAL VAL B . n 
B 2 84  PRO 84  116 116 PRO PRO B . n 
B 2 85  VAL 85  117 117 VAL VAL B . n 
B 2 86  PRO 86  118 118 PRO PRO B . n 
B 2 87  GLU 87  119 119 GLU GLU B . n 
B 2 88  LEU 88  120 120 LEU LEU B . n 
B 2 89  SER 89  121 121 SER SER B . n 
B 2 90  THR 90  122 122 THR THR B . n 
B 2 91  ASP 91  123 123 ASP ASP B . n 
B 2 92  THR 92  124 124 THR THR B . n 
B 2 93  VAL 93  125 125 VAL VAL B . n 
B 2 94  ILE 94  126 126 ILE ILE B . n 
B 2 95  ASN 95  127 127 ASN ASN B . n 
B 2 96  VAL 96  128 128 VAL VAL B . n 
B 2 97  ILE 97  129 129 ILE ILE B . n 
B 2 98  THR 98  130 130 THR THR B . n 
B 2 99  ASN 99  131 131 ASN ASN B . n 
B 2 100 MET 100 132 132 MET MET B . n 
B 2 101 THR 101 133 133 THR THR B . n 
B 2 102 THR 102 134 134 THR THR B . n 
B 2 103 THR 103 135 135 THR THR B . n 
B 2 104 ILE 104 136 136 ILE ILE B . n 
B 2 105 GLN 105 137 137 GLN GLN B . n 
B 2 106 SER 106 138 138 SER SER B . n 
B 2 107 LEU 107 139 139 LEU LEU B . n 
B 2 108 PHE 108 140 140 PHE PHE B . n 
B 2 109 PRO 109 141 141 PRO PRO B . n 
B 2 110 ASN 110 142 142 ASN ASN B . n 
B 2 111 LEU 111 143 143 LEU LEU B . n 
B 2 112 GLN 112 144 144 GLN GLN B . n 
B 2 113 VAL 113 145 145 VAL VAL B . n 
B 2 114 PHE 114 146 146 PHE PHE B . n 
B 2 115 PRO 115 147 147 PRO PRO B . n 
B 2 116 ALA 116 148 148 ALA ALA B . n 
B 2 117 LEU 117 149 149 LEU LEU B . n 
B 2 118 GLY 118 150 150 GLY GLY B . n 
B 2 119 ASN 119 151 151 ASN ASN B . n 
B 2 120 HIS 120 152 152 HIS HIS B . n 
B 2 121 ASP 121 153 153 ASP ASP B . n 
B 2 122 TYR 122 154 154 TYR TYR B . n 
B 2 123 TRP 123 155 155 TRP TRP B . n 
B 2 124 PRO 124 156 156 PRO PRO B . n 
B 2 125 GLN 125 157 157 GLN GLN B . n 
B 2 126 ASP 126 158 158 ASP ASP B . n 
B 2 127 GLN 127 159 159 GLN GLN B . n 
B 2 128 LEU 128 160 160 LEU LEU B . n 
B 2 129 PRO 129 161 161 PRO PRO B . n 
B 2 130 VAL 130 162 162 VAL VAL B . n 
B 2 131 VAL 131 163 163 VAL VAL B . n 
B 2 132 THR 132 164 164 THR THR B . n 
B 2 133 SER 133 165 165 SER SER B . n 
B 2 134 LYS 134 166 166 LYS LYS B . n 
B 2 135 VAL 135 167 167 VAL VAL B . n 
B 2 136 TYR 136 168 168 TYR TYR B . n 
B 2 137 ASN 137 169 169 ASN ASN B . n 
B 2 138 ALA 138 170 170 ALA ALA B . n 
B 2 139 VAL 139 171 171 VAL VAL B . n 
B 2 140 ALA 140 172 172 ALA ALA B . n 
B 2 141 ASN 141 173 173 ASN ASN B . n 
B 2 142 LEU 142 174 174 LEU LEU B . n 
B 2 143 TRP 143 175 175 TRP TRP B . n 
B 2 144 LYS 144 176 176 LYS LYS B . n 
B 2 145 PRO 145 177 177 PRO PRO B . n 
B 2 146 TRP 146 178 178 TRP TRP B . n 
B 2 147 LEU 147 179 179 LEU LEU B . n 
B 2 148 ASP 148 180 180 ASP ASP B . n 
B 2 149 GLU 149 181 181 GLU GLU B . n 
B 2 150 GLU 150 182 182 GLU GLU B . n 
B 2 151 ALA 151 183 183 ALA ALA B . n 
B 2 152 ILE 152 184 184 ILE ILE B . n 
B 2 153 SER 153 185 185 SER SER B . n 
B 2 154 THR 154 186 186 THR THR B . n 
B 2 155 LEU 155 187 187 LEU LEU B . n 
B 2 156 ARG 156 188 188 ARG ARG B . n 
B 2 157 LYS 157 189 189 LYS LYS B . n 
B 2 158 GLY 158 190 190 GLY GLY B . n 
B 2 159 GLY 159 191 191 GLY GLY B . n 
B 2 160 PHE 160 192 192 PHE PHE B . n 
B 2 161 TYR 161 193 193 TYR TYR B . n 
B 2 162 SER 162 194 194 SER SER B . n 
B 2 163 GLN 163 195 195 GLN GLN B . n 
B 2 164 LYS 164 196 196 LYS LYS B . n 
B 2 165 VAL 165 197 197 VAL VAL B . n 
B 2 166 THR 166 198 198 THR THR B . n 
B 2 167 THR 167 199 199 THR THR B . n 
B 2 168 ASN 168 200 200 ASN ASN B . n 
B 2 169 PRO 169 201 201 PRO PRO B . n 
B 2 170 ASN 170 202 202 ASN ASN B . n 
B 2 171 LEU 171 203 203 LEU LEU B . n 
B 2 172 ARG 172 204 204 ARG ARG B . n 
B 2 173 ILE 173 205 205 ILE ILE B . n 
B 2 174 ILE 174 206 206 ILE ILE B . n 
B 2 175 SER 175 207 207 SER SER B . n 
B 2 176 LEU 176 208 208 LEU LEU B . n 
B 2 177 ASN 177 209 209 ASN ASN B . n 
B 2 178 THR 178 210 210 THR THR B . n 
B 2 179 ASN 179 211 211 ASN ASN B . n 
B 2 180 LEU 180 212 212 LEU LEU B . n 
B 2 181 TYR 181 213 213 TYR TYR B . n 
B 2 182 TYR 182 214 214 TYR TYR B . n 
B 2 183 GLY 183 215 215 GLY GLY B . n 
B 2 184 PRO 184 216 216 PRO PRO B . n 
B 2 185 ASN 185 217 217 ASN ASN B . n 
B 2 186 ILE 186 218 218 ILE ILE B . n 
B 2 187 MET 187 219 219 MET MET B . n 
B 2 188 THR 188 220 220 THR THR B . n 
B 2 189 LEU 189 221 221 LEU LEU B . n 
B 2 190 ASN 190 222 222 ASN ASN B . n 
B 2 191 LYS 191 223 223 LYS LYS B . n 
B 2 192 THR 192 224 224 THR THR B . n 
B 2 193 ASP 193 225 225 ASP ASP B . n 
B 2 194 PRO 194 226 226 PRO PRO B . n 
B 2 195 ALA 195 227 227 ALA ALA B . n 
B 2 196 ASN 196 228 228 ASN ASN B . n 
B 2 197 GLN 197 229 229 GLN GLN B . n 
B 2 198 PHE 198 230 230 PHE PHE B . n 
B 2 199 GLU 199 231 231 GLU GLU B . n 
B 2 200 TRP 200 232 232 TRP TRP B . n 
B 2 201 LEU 201 233 233 LEU LEU B . n 
B 2 202 GLU 202 234 234 GLU GLU B . n 
B 2 203 SER 203 235 235 SER SER B . n 
B 2 204 THR 204 236 236 THR THR B . n 
B 2 205 LEU 205 237 237 LEU LEU B . n 
B 2 206 ASN 206 238 238 ASN ASN B . n 
B 2 207 ASN 207 239 239 ASN ASN B . n 
B 2 208 SER 208 240 240 SER SER B . n 
B 2 209 GLN 209 241 241 GLN GLN B . n 
B 2 210 GLN 210 242 242 GLN GLN B . n 
B 2 211 ASN 211 243 243 ASN ASN B . n 
B 2 212 LYS 212 244 244 LYS LYS B . n 
B 2 213 GLU 213 245 245 GLU GLU B . n 
B 2 214 LYS 214 246 246 LYS LYS B . n 
B 2 215 VAL 215 247 247 VAL VAL B . n 
B 2 216 TYR 216 248 248 TYR TYR B . n 
B 2 217 ILE 217 249 249 ILE ILE B . n 
B 2 218 ILE 218 250 250 ILE ILE B . n 
B 2 219 ALA 219 251 251 ALA ALA B . n 
B 2 220 HIS 220 252 252 HIS HIS B . n 
B 2 221 VAL 221 253 253 VAL VAL B . n 
B 2 222 PRO 222 254 254 PRO PRO B . n 
B 2 223 VAL 223 255 255 VAL VAL B . n 
B 2 224 GLY 224 256 256 GLY GLY B . n 
B 2 225 TYR 225 257 257 TYR TYR B . n 
B 2 226 LEU 226 258 258 LEU LEU B . n 
B 2 227 PRO 227 259 259 PRO PRO B . n 
B 2 228 SER 228 260 260 SER SER B . n 
B 2 229 SER 229 261 261 SER SER B . n 
B 2 230 GLN 230 262 262 GLN GLN B . n 
B 2 231 ASN 231 263 263 ASN ASN B . n 
B 2 232 ILE 232 264 264 ILE ILE B . n 
B 2 233 THR 233 265 265 THR THR B . n 
B 2 234 ALA 234 266 266 ALA ALA B . n 
B 2 235 MET 235 267 267 MET MET B . n 
B 2 236 ARG 236 268 268 ARG ARG B . n 
B 2 237 GLU 237 269 269 GLU GLU B . n 
B 2 238 TYR 238 270 270 TYR TYR B . n 
B 2 239 TYR 239 271 271 TYR TYR B . n 
B 2 240 ASN 240 272 272 ASN ASN B . n 
B 2 241 GLU 241 273 273 GLU GLU B . n 
B 2 242 LYS 242 274 274 LYS LYS B . n 
B 2 243 LEU 243 275 275 LEU LEU B . n 
B 2 244 ILE 244 276 276 ILE ILE B . n 
B 2 245 ASP 245 277 277 ASP ASP B . n 
B 2 246 ILE 246 278 278 ILE ILE B . n 
B 2 247 PHE 247 279 279 PHE PHE B . n 
B 2 248 GLN 248 280 280 GLN GLN B . n 
B 2 249 LYS 249 281 281 LYS LYS B . n 
B 2 250 TYR 250 282 282 TYR TYR B . n 
B 2 251 SER 251 283 283 SER SER B . n 
B 2 252 ASP 252 284 284 ASP ASP B . n 
B 2 253 VAL 253 285 285 VAL VAL B . n 
B 2 254 ILE 254 286 286 ILE ILE B . n 
B 2 255 ALA 255 287 287 ALA ALA B . n 
B 2 256 GLY 256 288 288 GLY GLY B . n 
B 2 257 GLN 257 289 289 GLN GLN B . n 
B 2 258 PHE 258 290 290 PHE PHE B . n 
B 2 259 TYR 259 291 291 TYR TYR B . n 
B 2 260 GLY 260 292 292 GLY GLY B . n 
B 2 261 HIS 261 293 293 HIS HIS B . n 
B 2 262 THR 262 294 294 THR THR B . n 
B 2 263 HIS 263 295 295 HIS HIS B . n 
B 2 264 ARG 264 296 296 ARG ARG B . n 
B 2 265 ASP 265 297 297 ASP ASP B . n 
B 2 266 SER 266 298 298 SER SER B . n 
B 2 267 ILE 267 299 299 ILE ILE B . n 
B 2 268 MET 268 300 300 MET MET B . n 
B 2 269 VAL 269 301 301 VAL VAL B . n 
B 2 270 LEU 270 302 302 LEU LEU B . n 
B 2 271 SER 271 303 303 SER SER B . n 
B 2 272 ASP 272 304 304 ASP ASP B . n 
B 2 273 LYS 273 305 305 LYS LYS B . n 
B 2 274 LYS 274 306 306 LYS LYS B . n 
B 2 275 GLY 275 307 307 GLY GLY B . n 
B 2 276 SER 276 308 308 SER SER B . n 
B 2 277 PRO 277 309 309 PRO PRO B . n 
B 2 278 VAL 278 310 310 VAL VAL B . n 
B 2 279 ASN 279 311 311 ASN ASN B . n 
B 2 280 SER 280 312 312 SER SER B . n 
B 2 281 LEU 281 313 313 LEU LEU B . n 
B 2 282 PHE 282 314 314 PHE PHE B . n 
B 2 283 VAL 283 315 315 VAL VAL B . n 
B 2 284 ALA 284 316 316 ALA ALA B . n 
B 2 285 PRO 285 317 317 PRO PRO B . n 
B 2 286 ALA 286 318 318 ALA ALA B . n 
B 2 287 VAL 287 319 319 VAL VAL B . n 
B 2 288 THR 288 320 320 THR THR B . n 
B 2 289 PRO 289 321 321 PRO PRO B . n 
B 2 290 VAL 290 322 322 VAL VAL B . n 
B 2 291 LYS 291 323 323 LYS LYS B . n 
B 2 292 SER 292 324 324 SER SER B . n 
B 2 293 VAL 293 325 325 VAL VAL B . n 
B 2 294 LEU 294 326 326 LEU LEU B . n 
B 2 295 GLU 295 327 327 GLU GLU B . n 
B 2 296 LYS 296 328 328 LYS LYS B . n 
B 2 297 GLN 297 329 329 GLN GLN B . n 
B 2 298 THR 298 330 330 THR THR B . n 
B 2 299 ASN 299 331 331 ASN ASN B . n 
B 2 300 ASN 300 332 332 ASN ASN B . n 
B 2 301 PRO 301 333 333 PRO PRO B . n 
B 2 302 GLY 302 334 334 GLY GLY B . n 
B 2 303 ILE 303 335 335 ILE ILE B . n 
B 2 304 ARG 304 336 336 ARG ARG B . n 
B 2 305 LEU 305 337 337 LEU LEU B . n 
B 2 306 PHE 306 338 338 PHE PHE B . n 
B 2 307 GLN 307 339 339 GLN GLN B . n 
B 2 308 TYR 308 340 340 TYR TYR B . n 
B 2 309 ASP 309 341 341 ASP ASP B . n 
B 2 310 PRO 310 342 342 PRO PRO B . n 
B 2 311 ARG 311 343 343 ARG ARG B . n 
B 2 312 ASP 312 344 344 ASP ASP B . n 
B 2 313 TYR 313 345 345 TYR TYR B . n 
B 2 314 LYS 314 346 346 LYS LYS B . n 
B 2 315 LEU 315 347 347 LEU LEU B . n 
B 2 316 LEU 316 348 348 LEU LEU B . n 
B 2 317 ASP 317 349 349 ASP ASP B . n 
B 2 318 MET 318 350 350 MET MET B . n 
B 2 319 LEU 319 351 351 LEU LEU B . n 
B 2 320 GLN 320 352 352 GLN GLN B . n 
B 2 321 TYR 321 353 353 TYR TYR B . n 
B 2 322 TYR 322 354 354 TYR TYR B . n 
B 2 323 LEU 323 355 355 LEU LEU B . n 
B 2 324 ASN 324 356 356 ASN ASN B . n 
B 2 325 LEU 325 357 357 LEU LEU B . n 
B 2 326 THR 326 358 358 THR THR B . n 
B 2 327 GLU 327 359 359 GLU GLU B . n 
B 2 328 ALA 328 360 360 ALA ALA B . n 
B 2 329 ASN 329 361 361 ASN ASN B . n 
B 2 330 LEU 330 362 362 LEU LEU B . n 
B 2 331 LYS 331 363 363 LYS LYS B . n 
B 2 332 GLY 332 364 364 GLY GLY B . n 
B 2 333 GLU 333 365 365 GLU GLU B . n 
B 2 334 SER 334 366 366 SER SER B . n 
B 2 335 ILE 335 367 367 ILE ILE B . n 
B 2 336 TRP 336 368 368 TRP TRP B . n 
B 2 337 LYS 337 369 369 LYS LYS B . n 
B 2 338 LEU 338 370 370 LEU LEU B . n 
B 2 339 GLU 339 371 371 GLU GLU B . n 
B 2 340 TYR 340 372 372 TYR TYR B . n 
B 2 341 ILE 341 373 373 ILE ILE B . n 
B 2 342 LEU 342 374 374 LEU LEU B . n 
B 2 343 THR 343 375 375 THR THR B . n 
B 2 344 GLN 344 376 376 GLN GLN B . n 
B 2 345 THR 345 377 377 THR THR B . n 
B 2 346 TYR 346 378 378 TYR TYR B . n 
B 2 347 ASP 347 379 379 ASP ASP B . n 
B 2 348 ILE 348 380 380 ILE ILE B . n 
B 2 349 GLU 349 381 381 GLU GLU B . n 
B 2 350 ASP 350 382 382 ASP ASP B . n 
B 2 351 LEU 351 383 383 LEU LEU B . n 
B 2 352 GLN 352 384 384 GLN GLN B . n 
B 2 353 PRO 353 385 385 PRO PRO B . n 
B 2 354 GLU 354 386 386 GLU GLU B . n 
B 2 355 SER 355 387 387 SER SER B . n 
B 2 356 LEU 356 388 388 LEU LEU B . n 
B 2 357 TYR 357 389 389 TYR TYR B . n 
B 2 358 GLY 358 390 390 GLY GLY B . n 
B 2 359 LEU 359 391 391 LEU LEU B . n 
B 2 360 ALA 360 392 392 ALA ALA B . n 
B 2 361 LYS 361 393 393 LYS LYS B . n 
B 2 362 GLN 362 394 394 GLN GLN B . n 
B 2 363 PHE 363 395 395 PHE PHE B . n 
B 2 364 THR 364 396 396 THR THR B . n 
B 2 365 ILE 365 397 397 ILE ILE B . n 
B 2 366 LEU 366 398 398 LEU LEU B . n 
B 2 367 ASP 367 399 399 ASP ASP B . n 
B 2 368 SER 368 400 400 SER SER B . n 
B 2 369 LYS 369 401 401 LYS LYS B . n 
B 2 370 GLN 370 402 402 GLN GLN B . n 
B 2 371 PHE 371 403 403 PHE PHE B . n 
B 2 372 ILE 372 404 404 ILE ILE B . n 
B 2 373 LYS 373 405 405 LYS LYS B . n 
B 2 374 TYR 374 406 406 TYR TYR B . n 
B 2 375 TYR 375 407 407 TYR TYR B . n 
B 2 376 ASN 376 408 408 ASN ASN B . n 
B 2 377 TYR 377 409 409 TYR TYR B . n 
B 2 378 PHE 378 410 410 PHE PHE B . n 
B 2 379 PHE 379 411 411 PHE PHE B . n 
B 2 380 VAL 380 412 412 VAL VAL B . n 
B 2 381 SER 381 413 413 SER SER B . n 
B 2 382 TYR 382 414 414 TYR TYR B . n 
B 2 383 ASP 383 415 415 ASP ASP B . n 
B 2 384 SER 384 416 416 SER SER B . n 
B 2 385 SER 385 417 417 SER SER B . n 
B 2 386 VAL 386 418 418 VAL VAL B . n 
B 2 387 THR 387 419 419 THR THR B . n 
B 2 388 CYS 388 420 420 CYS CYS B . n 
B 2 389 ASP 389 421 421 ASP ASP B . n 
B 2 390 LYS 390 422 422 LYS LYS B . n 
B 2 391 THR 391 423 423 THR THR B . n 
B 2 392 CYS 392 424 424 CYS CYS B . n 
B 2 393 LYS 393 425 425 LYS LYS B . n 
B 2 394 ALA 394 426 426 ALA ALA B . n 
B 2 395 PHE 395 427 427 PHE PHE B . n 
B 2 396 GLN 396 428 428 GLN GLN B . n 
B 2 397 ILE 397 429 429 ILE ILE B . n 
B 2 398 CYS 398 430 430 CYS CYS B . n 
B 2 399 ALA 399 431 431 ALA ALA B . n 
B 2 400 ILE 400 432 432 ILE ILE B . n 
B 2 401 MET 401 433 433 MET MET B . n 
B 2 402 ASN 402 434 434 ASN ASN B . n 
B 2 403 LEU 403 435 435 LEU LEU B . n 
B 2 404 ASP 404 436 436 ASP ASP B . n 
B 2 405 ASN 405 437 437 ASN ASN B . n 
B 2 406 ILE 406 438 438 ILE ILE B . n 
B 2 407 SER 407 439 439 SER SER B . n 
B 2 408 TYR 408 440 440 TYR TYR B . n 
B 2 409 ALA 409 441 441 ALA ALA B . n 
B 2 410 ASP 410 442 442 ASP ASP B . n 
B 2 411 CYS 411 443 443 CYS CYS B . n 
B 2 412 LEU 412 444 444 LEU LEU B . n 
B 2 413 LYS 413 445 445 LYS LYS B . n 
B 2 414 GLN 414 446 446 GLN GLN B . n 
B 2 415 LEU 415 447 447 LEU LEU B . n 
C 2 1   PRO 1   33  33  PRO PRO C . n 
C 2 2   PRO 2   34  34  PRO PRO C . n 
C 2 3   PRO 3   35  35  PRO PRO C . n 
C 2 4   ALA 4   36  36  ALA ALA C . n 
C 2 5   ILE 5   37  37  ILE ILE C . n 
C 2 6   GLY 6   38  38  GLY GLY C . n 
C 2 7   GLN 7   39  39  GLN GLN C . n 
C 2 8   PHE 8   40  40  PHE PHE C . n 
C 2 9   TRP 9   41  41  TRP TRP C . n 
C 2 10  HIS 10  42  42  HIS HIS C . n 
C 2 11  VAL 11  43  43  VAL VAL C . n 
C 2 12  THR 12  44  44  THR THR C . n 
C 2 13  ASP 13  45  45  ASP ASP C . n 
C 2 14  LEU 14  46  46  LEU LEU C . n 
C 2 15  HIS 15  47  47  HIS HIS C . n 
C 2 16  LEU 16  48  48  LEU LEU C . n 
C 2 17  ASP 17  49  49  ASP ASP C . n 
C 2 18  PRO 18  50  50  PRO PRO C . n 
C 2 19  THR 19  51  51  THR THR C . n 
C 2 20  TYR 20  52  52  TYR TYR C . n 
C 2 21  HIS 21  53  53  HIS HIS C . n 
C 2 22  ILE 22  54  54  ILE ILE C . n 
C 2 23  THR 23  55  55  THR THR C . n 
C 2 24  ASP 24  56  56  ASP ASP C . n 
C 2 25  ASP 25  57  57  ASP ASP C . n 
C 2 26  HIS 26  58  58  HIS HIS C . n 
C 2 27  THR 27  59  59  THR THR C . n 
C 2 28  LYS 28  60  60  LYS LYS C . n 
C 2 29  VAL 29  61  61  VAL VAL C . n 
C 2 30  CYS 30  62  62  CYS CYS C . n 
C 2 31  ALA 31  63  63  ALA ALA C . n 
C 2 32  SER 32  64  64  SER SER C . n 
C 2 33  SER 33  65  65  SER SER C . n 
C 2 34  LYS 34  66  66  LYS LYS C . n 
C 2 35  GLY 35  67  67  GLY GLY C . n 
C 2 36  ALA 36  68  68  ALA ALA C . n 
C 2 37  ASN 37  69  69  ASN ASN C . n 
C 2 38  ALA 38  70  70  ALA ALA C . n 
C 2 39  SER 39  71  71  SER SER C . n 
C 2 40  ASN 40  72  72  ASN ASN C . n 
C 2 41  PRO 41  73  73  PRO PRO C . n 
C 2 42  GLY 42  74  74  GLY GLY C . n 
C 2 43  PRO 43  75  75  PRO PRO C . n 
C 2 44  PHE 44  76  76  PHE PHE C . n 
C 2 45  GLY 45  77  77  GLY GLY C . n 
C 2 46  ASP 46  78  78  ASP ASP C . n 
C 2 47  VAL 47  79  79  VAL VAL C . n 
C 2 48  LEU 48  80  80  LEU LEU C . n 
C 2 49  CYS 49  81  81  CYS CYS C . n 
C 2 50  ASP 50  82  82  ASP ASP C . n 
C 2 51  SER 51  83  83  SER SER C . n 
C 2 52  PRO 52  84  84  PRO PRO C . n 
C 2 53  TYR 53  85  85  TYR TYR C . n 
C 2 54  GLN 54  86  86  GLN GLN C . n 
C 2 55  LEU 55  87  87  LEU LEU C . n 
C 2 56  ILE 56  88  88  ILE ILE C . n 
C 2 57  LEU 57  89  89  LEU LEU C . n 
C 2 58  SER 58  90  90  SER SER C . n 
C 2 59  ALA 59  91  91  ALA ALA C . n 
C 2 60  PHE 60  92  92  PHE PHE C . n 
C 2 61  ASP 61  93  93  ASP ASP C . n 
C 2 62  PHE 62  94  94  PHE PHE C . n 
C 2 63  ILE 63  95  95  ILE ILE C . n 
C 2 64  LYS 64  96  96  LYS LYS C . n 
C 2 65  ASN 65  97  97  ASN ASN C . n 
C 2 66  SER 66  98  98  SER SER C . n 
C 2 67  GLY 67  99  99  GLY GLY C . n 
C 2 68  GLN 68  100 100 GLN GLN C . n 
C 2 69  GLU 69  101 101 GLU GLU C . n 
C 2 70  ALA 70  102 102 ALA ALA C . n 
C 2 71  SER 71  103 103 SER SER C . n 
C 2 72  PHE 72  104 104 PHE PHE C . n 
C 2 73  MET 73  105 105 MET MET C . n 
C 2 74  ILE 74  106 106 ILE ILE C . n 
C 2 75  TRP 75  107 107 TRP TRP C . n 
C 2 76  THR 76  108 108 THR THR C . n 
C 2 77  GLY 77  109 109 GLY GLY C . n 
C 2 78  ASP 78  110 110 ASP ASP C . n 
C 2 79  SER 79  111 111 SER SER C . n 
C 2 80  PRO 80  112 112 PRO PRO C . n 
C 2 81  PRO 81  113 113 PRO PRO C . n 
C 2 82  HIS 82  114 114 HIS HIS C . n 
C 2 83  VAL 83  115 115 VAL VAL C . n 
C 2 84  PRO 84  116 116 PRO PRO C . n 
C 2 85  VAL 85  117 117 VAL VAL C . n 
C 2 86  PRO 86  118 118 PRO PRO C . n 
C 2 87  GLU 87  119 119 GLU GLU C . n 
C 2 88  LEU 88  120 120 LEU LEU C . n 
C 2 89  SER 89  121 121 SER SER C . n 
C 2 90  THR 90  122 122 THR THR C . n 
C 2 91  ASP 91  123 123 ASP ASP C . n 
C 2 92  THR 92  124 124 THR THR C . n 
C 2 93  VAL 93  125 125 VAL VAL C . n 
C 2 94  ILE 94  126 126 ILE ILE C . n 
C 2 95  ASN 95  127 127 ASN ASN C . n 
C 2 96  VAL 96  128 128 VAL VAL C . n 
C 2 97  ILE 97  129 129 ILE ILE C . n 
C 2 98  THR 98  130 130 THR THR C . n 
C 2 99  ASN 99  131 131 ASN ASN C . n 
C 2 100 MET 100 132 132 MET MET C . n 
C 2 101 THR 101 133 133 THR THR C . n 
C 2 102 THR 102 134 134 THR THR C . n 
C 2 103 THR 103 135 135 THR THR C . n 
C 2 104 ILE 104 136 136 ILE ILE C . n 
C 2 105 GLN 105 137 137 GLN GLN C . n 
C 2 106 SER 106 138 138 SER SER C . n 
C 2 107 LEU 107 139 139 LEU LEU C . n 
C 2 108 PHE 108 140 140 PHE PHE C . n 
C 2 109 PRO 109 141 141 PRO PRO C . n 
C 2 110 ASN 110 142 142 ASN ASN C . n 
C 2 111 LEU 111 143 143 LEU LEU C . n 
C 2 112 GLN 112 144 144 GLN GLN C . n 
C 2 113 VAL 113 145 145 VAL VAL C . n 
C 2 114 PHE 114 146 146 PHE PHE C . n 
C 2 115 PRO 115 147 147 PRO PRO C . n 
C 2 116 ALA 116 148 148 ALA ALA C . n 
C 2 117 LEU 117 149 149 LEU LEU C . n 
C 2 118 GLY 118 150 150 GLY GLY C . n 
C 2 119 ASN 119 151 151 ASN ASN C . n 
C 2 120 HIS 120 152 152 HIS HIS C . n 
C 2 121 ASP 121 153 153 ASP ASP C . n 
C 2 122 TYR 122 154 154 TYR TYR C . n 
C 2 123 TRP 123 155 155 TRP TRP C . n 
C 2 124 PRO 124 156 156 PRO PRO C . n 
C 2 125 GLN 125 157 157 GLN GLN C . n 
C 2 126 ASP 126 158 158 ASP ASP C . n 
C 2 127 GLN 127 159 159 GLN GLN C . n 
C 2 128 LEU 128 160 160 LEU LEU C . n 
C 2 129 PRO 129 161 161 PRO PRO C . n 
C 2 130 VAL 130 162 162 VAL VAL C . n 
C 2 131 VAL 131 163 163 VAL VAL C . n 
C 2 132 THR 132 164 164 THR THR C . n 
C 2 133 SER 133 165 165 SER SER C . n 
C 2 134 LYS 134 166 166 LYS LYS C . n 
C 2 135 VAL 135 167 167 VAL VAL C . n 
C 2 136 TYR 136 168 168 TYR TYR C . n 
C 2 137 ASN 137 169 169 ASN ASN C . n 
C 2 138 ALA 138 170 170 ALA ALA C . n 
C 2 139 VAL 139 171 171 VAL VAL C . n 
C 2 140 ALA 140 172 172 ALA ALA C . n 
C 2 141 ASN 141 173 173 ASN ASN C . n 
C 2 142 LEU 142 174 174 LEU LEU C . n 
C 2 143 TRP 143 175 175 TRP TRP C . n 
C 2 144 LYS 144 176 176 LYS LYS C . n 
C 2 145 PRO 145 177 177 PRO PRO C . n 
C 2 146 TRP 146 178 178 TRP TRP C . n 
C 2 147 LEU 147 179 179 LEU LEU C . n 
C 2 148 ASP 148 180 180 ASP ASP C . n 
C 2 149 GLU 149 181 181 GLU GLU C . n 
C 2 150 GLU 150 182 182 GLU GLU C . n 
C 2 151 ALA 151 183 183 ALA ALA C . n 
C 2 152 ILE 152 184 184 ILE ILE C . n 
C 2 153 SER 153 185 185 SER SER C . n 
C 2 154 THR 154 186 186 THR THR C . n 
C 2 155 LEU 155 187 187 LEU LEU C . n 
C 2 156 ARG 156 188 188 ARG ARG C . n 
C 2 157 LYS 157 189 189 LYS LYS C . n 
C 2 158 GLY 158 190 190 GLY GLY C . n 
C 2 159 GLY 159 191 191 GLY GLY C . n 
C 2 160 PHE 160 192 192 PHE PHE C . n 
C 2 161 TYR 161 193 193 TYR TYR C . n 
C 2 162 SER 162 194 194 SER SER C . n 
C 2 163 GLN 163 195 195 GLN GLN C . n 
C 2 164 LYS 164 196 196 LYS LYS C . n 
C 2 165 VAL 165 197 197 VAL VAL C . n 
C 2 166 THR 166 198 198 THR THR C . n 
C 2 167 THR 167 199 199 THR THR C . n 
C 2 168 ASN 168 200 200 ASN ASN C . n 
C 2 169 PRO 169 201 201 PRO PRO C . n 
C 2 170 ASN 170 202 202 ASN ASN C . n 
C 2 171 LEU 171 203 203 LEU LEU C . n 
C 2 172 ARG 172 204 204 ARG ARG C . n 
C 2 173 ILE 173 205 205 ILE ILE C . n 
C 2 174 ILE 174 206 206 ILE ILE C . n 
C 2 175 SER 175 207 207 SER SER C . n 
C 2 176 LEU 176 208 208 LEU LEU C . n 
C 2 177 ASN 177 209 209 ASN ASN C . n 
C 2 178 THR 178 210 210 THR THR C . n 
C 2 179 ASN 179 211 211 ASN ASN C . n 
C 2 180 LEU 180 212 212 LEU LEU C . n 
C 2 181 TYR 181 213 213 TYR TYR C . n 
C 2 182 TYR 182 214 214 TYR TYR C . n 
C 2 183 GLY 183 215 215 GLY GLY C . n 
C 2 184 PRO 184 216 216 PRO PRO C . n 
C 2 185 ASN 185 217 217 ASN ASN C . n 
C 2 186 ILE 186 218 218 ILE ILE C . n 
C 2 187 MET 187 219 219 MET MET C . n 
C 2 188 THR 188 220 220 THR THR C . n 
C 2 189 LEU 189 221 221 LEU LEU C . n 
C 2 190 ASN 190 222 222 ASN ASN C . n 
C 2 191 LYS 191 223 223 LYS LYS C . n 
C 2 192 THR 192 224 224 THR THR C . n 
C 2 193 ASP 193 225 225 ASP ASP C . n 
C 2 194 PRO 194 226 226 PRO PRO C . n 
C 2 195 ALA 195 227 227 ALA ALA C . n 
C 2 196 ASN 196 228 228 ASN ASN C . n 
C 2 197 GLN 197 229 229 GLN GLN C . n 
C 2 198 PHE 198 230 230 PHE PHE C . n 
C 2 199 GLU 199 231 231 GLU GLU C . n 
C 2 200 TRP 200 232 232 TRP TRP C . n 
C 2 201 LEU 201 233 233 LEU LEU C . n 
C 2 202 GLU 202 234 234 GLU GLU C . n 
C 2 203 SER 203 235 235 SER SER C . n 
C 2 204 THR 204 236 236 THR THR C . n 
C 2 205 LEU 205 237 237 LEU LEU C . n 
C 2 206 ASN 206 238 238 ASN ASN C . n 
C 2 207 ASN 207 239 239 ASN ASN C . n 
C 2 208 SER 208 240 240 SER SER C . n 
C 2 209 GLN 209 241 241 GLN GLN C . n 
C 2 210 GLN 210 242 242 GLN GLN C . n 
C 2 211 ASN 211 243 243 ASN ASN C . n 
C 2 212 LYS 212 244 244 LYS LYS C . n 
C 2 213 GLU 213 245 245 GLU GLU C . n 
C 2 214 LYS 214 246 246 LYS LYS C . n 
C 2 215 VAL 215 247 247 VAL VAL C . n 
C 2 216 TYR 216 248 248 TYR TYR C . n 
C 2 217 ILE 217 249 249 ILE ILE C . n 
C 2 218 ILE 218 250 250 ILE ILE C . n 
C 2 219 ALA 219 251 251 ALA ALA C . n 
C 2 220 HIS 220 252 252 HIS HIS C . n 
C 2 221 VAL 221 253 253 VAL VAL C . n 
C 2 222 PRO 222 254 254 PRO PRO C . n 
C 2 223 VAL 223 255 255 VAL VAL C . n 
C 2 224 GLY 224 256 256 GLY GLY C . n 
C 2 225 TYR 225 257 257 TYR TYR C . n 
C 2 226 LEU 226 258 258 LEU LEU C . n 
C 2 227 PRO 227 259 259 PRO PRO C . n 
C 2 228 SER 228 260 260 SER SER C . n 
C 2 229 SER 229 261 261 SER SER C . n 
C 2 230 GLN 230 262 262 GLN GLN C . n 
C 2 231 ASN 231 263 263 ASN ASN C . n 
C 2 232 ILE 232 264 264 ILE ILE C . n 
C 2 233 THR 233 265 265 THR THR C . n 
C 2 234 ALA 234 266 266 ALA ALA C . n 
C 2 235 MET 235 267 267 MET MET C . n 
C 2 236 ARG 236 268 268 ARG ARG C . n 
C 2 237 GLU 237 269 269 GLU GLU C . n 
C 2 238 TYR 238 270 270 TYR TYR C . n 
C 2 239 TYR 239 271 271 TYR TYR C . n 
C 2 240 ASN 240 272 272 ASN ASN C . n 
C 2 241 GLU 241 273 273 GLU GLU C . n 
C 2 242 LYS 242 274 274 LYS LYS C . n 
C 2 243 LEU 243 275 275 LEU LEU C . n 
C 2 244 ILE 244 276 276 ILE ILE C . n 
C 2 245 ASP 245 277 277 ASP ASP C . n 
C 2 246 ILE 246 278 278 ILE ILE C . n 
C 2 247 PHE 247 279 279 PHE PHE C . n 
C 2 248 GLN 248 280 280 GLN GLN C . n 
C 2 249 LYS 249 281 281 LYS LYS C . n 
C 2 250 TYR 250 282 282 TYR TYR C . n 
C 2 251 SER 251 283 283 SER SER C . n 
C 2 252 ASP 252 284 284 ASP ASP C . n 
C 2 253 VAL 253 285 285 VAL VAL C . n 
C 2 254 ILE 254 286 286 ILE ILE C . n 
C 2 255 ALA 255 287 287 ALA ALA C . n 
C 2 256 GLY 256 288 288 GLY GLY C . n 
C 2 257 GLN 257 289 289 GLN GLN C . n 
C 2 258 PHE 258 290 290 PHE PHE C . n 
C 2 259 TYR 259 291 291 TYR TYR C . n 
C 2 260 GLY 260 292 292 GLY GLY C . n 
C 2 261 HIS 261 293 293 HIS HIS C . n 
C 2 262 THR 262 294 294 THR THR C . n 
C 2 263 HIS 263 295 295 HIS HIS C . n 
C 2 264 ARG 264 296 296 ARG ARG C . n 
C 2 265 ASP 265 297 297 ASP ASP C . n 
C 2 266 SER 266 298 298 SER SER C . n 
C 2 267 ILE 267 299 299 ILE ILE C . n 
C 2 268 MET 268 300 300 MET MET C . n 
C 2 269 VAL 269 301 301 VAL VAL C . n 
C 2 270 LEU 270 302 302 LEU LEU C . n 
C 2 271 SER 271 303 303 SER SER C . n 
C 2 272 ASP 272 304 304 ASP ASP C . n 
C 2 273 LYS 273 305 305 LYS LYS C . n 
C 2 274 LYS 274 306 306 LYS LYS C . n 
C 2 275 GLY 275 307 307 GLY GLY C . n 
C 2 276 SER 276 308 308 SER SER C . n 
C 2 277 PRO 277 309 309 PRO PRO C . n 
C 2 278 VAL 278 310 310 VAL VAL C . n 
C 2 279 ASN 279 311 311 ASN ASN C . n 
C 2 280 SER 280 312 312 SER SER C . n 
C 2 281 LEU 281 313 313 LEU LEU C . n 
C 2 282 PHE 282 314 314 PHE PHE C . n 
C 2 283 VAL 283 315 315 VAL VAL C . n 
C 2 284 ALA 284 316 316 ALA ALA C . n 
C 2 285 PRO 285 317 317 PRO PRO C . n 
C 2 286 ALA 286 318 318 ALA ALA C . n 
C 2 287 VAL 287 319 319 VAL VAL C . n 
C 2 288 THR 288 320 320 THR THR C . n 
C 2 289 PRO 289 321 321 PRO PRO C . n 
C 2 290 VAL 290 322 322 VAL VAL C . n 
C 2 291 LYS 291 323 323 LYS LYS C . n 
C 2 292 SER 292 324 324 SER SER C . n 
C 2 293 VAL 293 325 325 VAL VAL C . n 
C 2 294 LEU 294 326 326 LEU LEU C . n 
C 2 295 GLU 295 327 327 GLU GLU C . n 
C 2 296 LYS 296 328 328 LYS LYS C . n 
C 2 297 GLN 297 329 329 GLN GLN C . n 
C 2 298 THR 298 330 330 THR THR C . n 
C 2 299 ASN 299 331 331 ASN ASN C . n 
C 2 300 ASN 300 332 332 ASN ASN C . n 
C 2 301 PRO 301 333 333 PRO PRO C . n 
C 2 302 GLY 302 334 334 GLY GLY C . n 
C 2 303 ILE 303 335 335 ILE ILE C . n 
C 2 304 ARG 304 336 336 ARG ARG C . n 
C 2 305 LEU 305 337 337 LEU LEU C . n 
C 2 306 PHE 306 338 338 PHE PHE C . n 
C 2 307 GLN 307 339 339 GLN GLN C . n 
C 2 308 TYR 308 340 340 TYR TYR C . n 
C 2 309 ASP 309 341 341 ASP ASP C . n 
C 2 310 PRO 310 342 342 PRO PRO C . n 
C 2 311 ARG 311 343 343 ARG ARG C . n 
C 2 312 ASP 312 344 344 ASP ASP C . n 
C 2 313 TYR 313 345 345 TYR TYR C . n 
C 2 314 LYS 314 346 346 LYS LYS C . n 
C 2 315 LEU 315 347 347 LEU LEU C . n 
C 2 316 LEU 316 348 348 LEU LEU C . n 
C 2 317 ASP 317 349 349 ASP ASP C . n 
C 2 318 MET 318 350 350 MET MET C . n 
C 2 319 LEU 319 351 351 LEU LEU C . n 
C 2 320 GLN 320 352 352 GLN GLN C . n 
C 2 321 TYR 321 353 353 TYR TYR C . n 
C 2 322 TYR 322 354 354 TYR TYR C . n 
C 2 323 LEU 323 355 355 LEU LEU C . n 
C 2 324 ASN 324 356 356 ASN ASN C . n 
C 2 325 LEU 325 357 357 LEU LEU C . n 
C 2 326 THR 326 358 358 THR THR C . n 
C 2 327 GLU 327 359 359 GLU GLU C . n 
C 2 328 ALA 328 360 360 ALA ALA C . n 
C 2 329 ASN 329 361 361 ASN ASN C . n 
C 2 330 LEU 330 362 362 LEU LEU C . n 
C 2 331 LYS 331 363 363 LYS LYS C . n 
C 2 332 GLY 332 364 364 GLY GLY C . n 
C 2 333 GLU 333 365 365 GLU GLU C . n 
C 2 334 SER 334 366 366 SER SER C . n 
C 2 335 ILE 335 367 367 ILE ILE C . n 
C 2 336 TRP 336 368 368 TRP TRP C . n 
C 2 337 LYS 337 369 369 LYS LYS C . n 
C 2 338 LEU 338 370 370 LEU LEU C . n 
C 2 339 GLU 339 371 371 GLU GLU C . n 
C 2 340 TYR 340 372 372 TYR TYR C . n 
C 2 341 ILE 341 373 373 ILE ILE C . n 
C 2 342 LEU 342 374 374 LEU LEU C . n 
C 2 343 THR 343 375 375 THR THR C . n 
C 2 344 GLN 344 376 376 GLN GLN C . n 
C 2 345 THR 345 377 377 THR THR C . n 
C 2 346 TYR 346 378 378 TYR TYR C . n 
C 2 347 ASP 347 379 379 ASP ASP C . n 
C 2 348 ILE 348 380 380 ILE ILE C . n 
C 2 349 GLU 349 381 381 GLU GLU C . n 
C 2 350 ASP 350 382 382 ASP ASP C . n 
C 2 351 LEU 351 383 383 LEU LEU C . n 
C 2 352 GLN 352 384 384 GLN GLN C . n 
C 2 353 PRO 353 385 385 PRO PRO C . n 
C 2 354 GLU 354 386 386 GLU GLU C . n 
C 2 355 SER 355 387 387 SER SER C . n 
C 2 356 LEU 356 388 388 LEU LEU C . n 
C 2 357 TYR 357 389 389 TYR TYR C . n 
C 2 358 GLY 358 390 390 GLY GLY C . n 
C 2 359 LEU 359 391 391 LEU LEU C . n 
C 2 360 ALA 360 392 392 ALA ALA C . n 
C 2 361 LYS 361 393 393 LYS LYS C . n 
C 2 362 GLN 362 394 394 GLN GLN C . n 
C 2 363 PHE 363 395 395 PHE PHE C . n 
C 2 364 THR 364 396 396 THR THR C . n 
C 2 365 ILE 365 397 397 ILE ILE C . n 
C 2 366 LEU 366 398 398 LEU LEU C . n 
C 2 367 ASP 367 399 399 ASP ASP C . n 
C 2 368 SER 368 400 400 SER SER C . n 
C 2 369 LYS 369 401 401 LYS LYS C . n 
C 2 370 GLN 370 402 402 GLN GLN C . n 
C 2 371 PHE 371 403 403 PHE PHE C . n 
C 2 372 ILE 372 404 404 ILE ILE C . n 
C 2 373 LYS 373 405 405 LYS LYS C . n 
C 2 374 TYR 374 406 406 TYR TYR C . n 
C 2 375 TYR 375 407 407 TYR TYR C . n 
C 2 376 ASN 376 408 408 ASN ASN C . n 
C 2 377 TYR 377 409 409 TYR TYR C . n 
C 2 378 PHE 378 410 410 PHE PHE C . n 
C 2 379 PHE 379 411 411 PHE PHE C . n 
C 2 380 VAL 380 412 412 VAL VAL C . n 
C 2 381 SER 381 413 413 SER SER C . n 
C 2 382 TYR 382 414 414 TYR TYR C . n 
C 2 383 ASP 383 415 415 ASP ASP C . n 
C 2 384 SER 384 416 416 SER SER C . n 
C 2 385 SER 385 417 417 SER SER C . n 
C 2 386 VAL 386 418 418 VAL VAL C . n 
C 2 387 THR 387 419 419 THR THR C . n 
C 2 388 CYS 388 420 420 CYS CYS C . n 
C 2 389 ASP 389 421 421 ASP ASP C . n 
C 2 390 LYS 390 422 422 LYS LYS C . n 
C 2 391 THR 391 423 423 THR THR C . n 
C 2 392 CYS 392 424 424 CYS CYS C . n 
C 2 393 LYS 393 425 425 LYS LYS C . n 
C 2 394 ALA 394 426 426 ALA ALA C . n 
C 2 395 PHE 395 427 427 PHE PHE C . n 
C 2 396 GLN 396 428 428 GLN GLN C . n 
C 2 397 ILE 397 429 429 ILE ILE C . n 
C 2 398 CYS 398 430 430 CYS CYS C . n 
C 2 399 ALA 399 431 431 ALA ALA C . n 
C 2 400 ILE 400 432 432 ILE ILE C . n 
C 2 401 MET 401 433 433 MET MET C . n 
C 2 402 ASN 402 434 434 ASN ASN C . n 
C 2 403 LEU 403 435 435 LEU LEU C . n 
C 2 404 ASP 404 436 436 ASP ASP C . n 
C 2 405 ASN 405 437 437 ASN ASN C . n 
C 2 406 ILE 406 438 438 ILE ILE C . n 
C 2 407 SER 407 439 439 SER SER C . n 
C 2 408 TYR 408 440 440 TYR TYR C . n 
C 2 409 ALA 409 441 441 ALA ALA C . n 
C 2 410 ASP 410 442 442 ASP ASP C . n 
C 2 411 CYS 411 443 443 CYS CYS C . n 
C 2 412 LEU 412 444 444 LEU LEU C . n 
C 2 413 LYS 413 445 445 LYS LYS C . n 
C 2 414 GLN 414 446 446 GLN GLN C . n 
C 2 415 LEU 415 447 447 LEU LEU C . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
D  3  NAG 1  601 601 NAG NAG A . 
E  3  NAG 1  602 602 NAG NAG A . 
F  3  NAG 1  603 603 NAG NAG A . 
G  3  NAG 1  604 604 NAG NAG A . 
H  4  ZN  1  605 1   ZN  ZN  A . 
I  4  ZN  1  606 2   ZN  ZN  A . 
J  5  C5P 1  607 1   C5P C5P A . 
K  3  NAG 1  601 601 NAG NAG B . 
L  3  NAG 1  602 602 NAG NAG B . 
M  3  NAG 2  603 603 NAG NAG B . 
N  3  NAG 1  604 604 NAG NAG B . 
O  3  NAG 1  605 605 NAG NAG B . 
P  4  ZN  1  606 5   ZN  ZN  B . 
Q  4  ZN  1  607 6   ZN  ZN  B . 
R  6  GOL 1  608 1   GOL GOL B . 
S  6  GOL 1  609 2   GOL GOL B . 
T  7  MLI 1  610 1   MLI MLI B . 
U  8  RP5 1  611 1   RP5 RP5 B . 
V  3  NAG 1  601 601 NAG NAG C . 
W  3  NAG 1  602 602 NAG NAG C . 
X  3  NAG 1  603 603 NAG NAG C . 
Y  3  NAG 1  604 604 NAG NAG C . 
Z  4  ZN  1  605 3   ZN  ZN  C . 
AA 4  ZN  1  606 4   ZN  ZN  C . 
BA 5  C5P 1  607 3   C5P C5P C . 
CA 9  SCN 1  608 1   SCN SCN C . 
DA 9  SCN 1  609 2   SCN SCN C . 
EA 10 HOH 1  701 58  HOH HOH A . 
EA 10 HOH 2  702 21  HOH HOH A . 
EA 10 HOH 3  703 61  HOH HOH A . 
EA 10 HOH 4  704 95  HOH HOH A . 
EA 10 HOH 5  705 24  HOH HOH A . 
EA 10 HOH 6  706 94  HOH HOH A . 
EA 10 HOH 7  707 25  HOH HOH A . 
EA 10 HOH 8  708 20  HOH HOH A . 
EA 10 HOH 9  709 2   HOH HOH A . 
EA 10 HOH 10 710 23  HOH HOH A . 
EA 10 HOH 11 711 3   HOH HOH A . 
EA 10 HOH 12 712 1   HOH HOH A . 
EA 10 HOH 13 713 87  HOH HOH A . 
EA 10 HOH 14 714 125 HOH HOH A . 
EA 10 HOH 15 715 18  HOH HOH A . 
EA 10 HOH 16 716 19  HOH HOH A . 
EA 10 HOH 17 717 22  HOH HOH A . 
EA 10 HOH 18 718 108 HOH HOH A . 
EA 10 HOH 19 719 60  HOH HOH A . 
FA 10 HOH 1  701 91  HOH HOH B . 
FA 10 HOH 2  702 122 HOH HOH B . 
FA 10 HOH 3  703 65  HOH HOH B . 
FA 10 HOH 4  704 68  HOH HOH B . 
FA 10 HOH 5  705 63  HOH HOH B . 
FA 10 HOH 6  706 62  HOH HOH B . 
FA 10 HOH 7  707 90  HOH HOH B . 
FA 10 HOH 8  708 117 HOH HOH B . 
FA 10 HOH 9  709 97  HOH HOH B . 
FA 10 HOH 10 710 93  HOH HOH B . 
FA 10 HOH 11 711 70  HOH HOH B . 
FA 10 HOH 12 712 92  HOH HOH B . 
FA 10 HOH 13 713 69  HOH HOH B . 
FA 10 HOH 14 714 74  HOH HOH B . 
FA 10 HOH 15 715 101 HOH HOH B . 
FA 10 HOH 16 716 100 HOH HOH B . 
FA 10 HOH 17 717 64  HOH HOH B . 
FA 10 HOH 18 718 96  HOH HOH B . 
FA 10 HOH 19 719 8   HOH HOH B . 
FA 10 HOH 20 720 72  HOH HOH B . 
FA 10 HOH 21 721 99  HOH HOH B . 
FA 10 HOH 22 722 78  HOH HOH B . 
FA 10 HOH 23 723 75  HOH HOH B . 
FA 10 HOH 24 724 5   HOH HOH B . 
FA 10 HOH 25 725 10  HOH HOH B . 
FA 10 HOH 26 726 104 HOH HOH B . 
FA 10 HOH 27 727 67  HOH HOH B . 
FA 10 HOH 28 728 66  HOH HOH B . 
FA 10 HOH 29 729 89  HOH HOH B . 
FA 10 HOH 30 730 102 HOH HOH B . 
FA 10 HOH 31 731 103 HOH HOH B . 
FA 10 HOH 32 732 110 HOH HOH B . 
FA 10 HOH 33 733 86  HOH HOH B . 
FA 10 HOH 34 734 9   HOH HOH B . 
FA 10 HOH 35 735 115 HOH HOH B . 
FA 10 HOH 36 736 109 HOH HOH B . 
FA 10 HOH 37 737 52  HOH HOH B . 
FA 10 HOH 38 738 7   HOH HOH B . 
FA 10 HOH 39 739 11  HOH HOH B . 
FA 10 HOH 40 740 124 HOH HOH B . 
FA 10 HOH 41 741 45  HOH HOH B . 
FA 10 HOH 42 742 119 HOH HOH B . 
FA 10 HOH 43 743 16  HOH HOH B . 
FA 10 HOH 44 744 98  HOH HOH B . 
FA 10 HOH 45 745 73  HOH HOH B . 
FA 10 HOH 46 746 76  HOH HOH B . 
FA 10 HOH 47 747 112 HOH HOH B . 
FA 10 HOH 48 748 118 HOH HOH B . 
FA 10 HOH 49 749 123 HOH HOH B . 
FA 10 HOH 50 750 88  HOH HOH B . 
FA 10 HOH 51 751 114 HOH HOH B . 
FA 10 HOH 52 752 36  HOH HOH B . 
FA 10 HOH 53 753 121 HOH HOH B . 
FA 10 HOH 54 754 71  HOH HOH B . 
FA 10 HOH 55 755 126 HOH HOH B . 
FA 10 HOH 56 756 116 HOH HOH B . 
FA 10 HOH 57 757 83  HOH HOH B . 
FA 10 HOH 58 758 111 HOH HOH B . 
FA 10 HOH 59 759 113 HOH HOH B . 
FA 10 HOH 60 760 120 HOH HOH B . 
GA 10 HOH 1  701 105 HOH HOH C . 
GA 10 HOH 2  702 129 HOH HOH C . 
GA 10 HOH 3  703 12  HOH HOH C . 
GA 10 HOH 4  704 132 HOH HOH C . 
GA 10 HOH 5  705 106 HOH HOH C . 
GA 10 HOH 6  706 41  HOH HOH C . 
GA 10 HOH 7  707 38  HOH HOH C . 
GA 10 HOH 8  708 80  HOH HOH C . 
GA 10 HOH 9  709 85  HOH HOH C . 
GA 10 HOH 10 710 28  HOH HOH C . 
GA 10 HOH 11 711 33  HOH HOH C . 
GA 10 HOH 12 712 34  HOH HOH C . 
GA 10 HOH 13 713 39  HOH HOH C . 
GA 10 HOH 14 714 50  HOH HOH C . 
GA 10 HOH 15 715 15  HOH HOH C . 
GA 10 HOH 16 716 35  HOH HOH C . 
GA 10 HOH 17 717 82  HOH HOH C . 
GA 10 HOH 18 718 48  HOH HOH C . 
GA 10 HOH 19 719 54  HOH HOH C . 
GA 10 HOH 20 720 40  HOH HOH C . 
GA 10 HOH 21 721 84  HOH HOH C . 
GA 10 HOH 22 722 4   HOH HOH C . 
GA 10 HOH 23 723 26  HOH HOH C . 
GA 10 HOH 24 724 42  HOH HOH C . 
GA 10 HOH 25 725 17  HOH HOH C . 
GA 10 HOH 26 726 55  HOH HOH C . 
GA 10 HOH 27 727 127 HOH HOH C . 
GA 10 HOH 28 728 14  HOH HOH C . 
GA 10 HOH 29 729 43  HOH HOH C . 
GA 10 HOH 30 730 27  HOH HOH C . 
GA 10 HOH 31 731 29  HOH HOH C . 
GA 10 HOH 32 732 37  HOH HOH C . 
GA 10 HOH 33 733 57  HOH HOH C . 
GA 10 HOH 34 734 81  HOH HOH C . 
GA 10 HOH 35 735 130 HOH HOH C . 
GA 10 HOH 36 736 49  HOH HOH C . 
GA 10 HOH 37 737 30  HOH HOH C . 
GA 10 HOH 38 738 79  HOH HOH C . 
GA 10 HOH 39 739 31  HOH HOH C . 
GA 10 HOH 40 740 13  HOH HOH C . 
GA 10 HOH 41 741 107 HOH HOH C . 
GA 10 HOH 42 742 32  HOH HOH C . 
GA 10 HOH 43 743 131 HOH HOH C . 
GA 10 HOH 44 744 46  HOH HOH C . 
GA 10 HOH 45 745 44  HOH HOH C . 
GA 10 HOH 46 746 56  HOH HOH C . 
GA 10 HOH 47 747 51  HOH HOH C . 
GA 10 HOH 48 748 128 HOH HOH C . 
GA 10 HOH 49 749 6   HOH HOH C . 
GA 10 HOH 50 750 47  HOH HOH C . 
GA 10 HOH 51 751 53  HOH HOH C . 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
3 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,D,E,F,G,H,I,J,EA         
2 1 B,K,L,M,N,O,P,Q,R,S,T,U,FA 
3 1 C,V,W,X,Y,Z,AA,BA,CA,DA,GA 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OD2 ? A ASP 13  ? A ASP 45  ? 1_555 ZN ? I  ZN . ? A ZN 606 ? 1_555 NE2 ? A  HIS 15  ? A HIS 47  ? 1_555 111.8 ? 
2  OD2 ? A ASP 13  ? A ASP 45  ? 1_555 ZN ? I  ZN . ? A ZN 606 ? 1_555 OD2 ? A  ASP 78  ? A ASP 110 ? 1_555 75.6  ? 
3  NE2 ? A HIS 15  ? A HIS 47  ? 1_555 ZN ? I  ZN . ? A ZN 606 ? 1_555 OD2 ? A  ASP 78  ? A ASP 110 ? 1_555 87.3  ? 
4  OD2 ? A ASP 13  ? A ASP 45  ? 1_555 ZN ? I  ZN . ? A ZN 606 ? 1_555 NE2 ? A  HIS 263 ? A HIS 295 ? 1_555 101.4 ? 
5  NE2 ? A HIS 15  ? A HIS 47  ? 1_555 ZN ? I  ZN . ? A ZN 606 ? 1_555 NE2 ? A  HIS 263 ? A HIS 295 ? 1_555 97.6  ? 
6  OD2 ? A ASP 78  ? A ASP 110 ? 1_555 ZN ? I  ZN . ? A ZN 606 ? 1_555 NE2 ? A  HIS 263 ? A HIS 295 ? 1_555 175.0 ? 
7  OD2 ? A ASP 13  ? A ASP 45  ? 1_555 ZN ? I  ZN . ? A ZN 606 ? 1_555 O2P ? J  C5P .   ? A C5P 607 ? 1_555 128.1 ? 
8  NE2 ? A HIS 15  ? A HIS 47  ? 1_555 ZN ? I  ZN . ? A ZN 606 ? 1_555 O2P ? J  C5P .   ? A C5P 607 ? 1_555 114.1 ? 
9  OD2 ? A ASP 78  ? A ASP 110 ? 1_555 ZN ? I  ZN . ? A ZN 606 ? 1_555 O2P ? J  C5P .   ? A C5P 607 ? 1_555 83.7  ? 
10 NE2 ? A HIS 263 ? A HIS 295 ? 1_555 ZN ? I  ZN . ? A ZN 606 ? 1_555 O2P ? J  C5P .   ? A C5P 607 ? 1_555 95.3  ? 
11 OD2 ? A ASP 78  ? A ASP 110 ? 1_555 ZN ? H  ZN . ? A ZN 605 ? 1_555 OD1 ? A  ASN 119 ? A ASN 151 ? 1_555 105.3 ? 
12 OD2 ? A ASP 78  ? A ASP 110 ? 1_555 ZN ? H  ZN . ? A ZN 605 ? 1_555 NE2 ? A  HIS 220 ? A HIS 252 ? 1_555 87.7  ? 
13 OD1 ? A ASN 119 ? A ASN 151 ? 1_555 ZN ? H  ZN . ? A ZN 605 ? 1_555 NE2 ? A  HIS 220 ? A HIS 252 ? 1_555 78.4  ? 
14 OD2 ? A ASP 78  ? A ASP 110 ? 1_555 ZN ? H  ZN . ? A ZN 605 ? 1_555 ND1 ? A  HIS 261 ? A HIS 293 ? 1_555 160.0 ? 
15 OD1 ? A ASN 119 ? A ASN 151 ? 1_555 ZN ? H  ZN . ? A ZN 605 ? 1_555 ND1 ? A  HIS 261 ? A HIS 293 ? 1_555 94.6  ? 
16 NE2 ? A HIS 220 ? A HIS 252 ? 1_555 ZN ? H  ZN . ? A ZN 605 ? 1_555 ND1 ? A  HIS 261 ? A HIS 293 ? 1_555 93.9  ? 
17 OD2 ? A ASP 78  ? A ASP 110 ? 1_555 ZN ? H  ZN . ? A ZN 605 ? 1_555 O1P ? J  C5P .   ? A C5P 607 ? 1_555 80.8  ? 
18 OD1 ? A ASN 119 ? A ASN 151 ? 1_555 ZN ? H  ZN . ? A ZN 605 ? 1_555 O1P ? J  C5P .   ? A C5P 607 ? 1_555 85.7  ? 
19 NE2 ? A HIS 220 ? A HIS 252 ? 1_555 ZN ? H  ZN . ? A ZN 605 ? 1_555 O1P ? J  C5P .   ? A C5P 607 ? 1_555 157.1 ? 
20 ND1 ? A HIS 261 ? A HIS 293 ? 1_555 ZN ? H  ZN . ? A ZN 605 ? 1_555 O1P ? J  C5P .   ? A C5P 607 ? 1_555 103.7 ? 
21 OD2 ? B ASP 13  ? B ASP 45  ? 1_555 ZN ? P  ZN . ? B ZN 606 ? 1_555 NE2 ? B  HIS 15  ? B HIS 47  ? 1_555 108.7 ? 
22 OD2 ? B ASP 13  ? B ASP 45  ? 1_555 ZN ? P  ZN . ? B ZN 606 ? 1_555 OD2 ? B  ASP 78  ? B ASP 110 ? 1_555 86.5  ? 
23 NE2 ? B HIS 15  ? B HIS 47  ? 1_555 ZN ? P  ZN . ? B ZN 606 ? 1_555 OD2 ? B  ASP 78  ? B ASP 110 ? 1_555 76.7  ? 
24 OD2 ? B ASP 13  ? B ASP 45  ? 1_555 ZN ? P  ZN . ? B ZN 606 ? 1_555 NE2 ? B  HIS 263 ? B HIS 295 ? 1_555 97.8  ? 
25 NE2 ? B HIS 15  ? B HIS 47  ? 1_555 ZN ? P  ZN . ? B ZN 606 ? 1_555 NE2 ? B  HIS 263 ? B HIS 295 ? 1_555 95.8  ? 
26 OD2 ? B ASP 78  ? B ASP 110 ? 1_555 ZN ? P  ZN . ? B ZN 606 ? 1_555 NE2 ? B  HIS 263 ? B HIS 295 ? 1_555 172.3 ? 
27 OD2 ? B ASP 13  ? B ASP 45  ? 1_555 ZN ? P  ZN . ? B ZN 606 ? 1_555 O3X ? U  RP5 .   ? B RP5 611 ? 1_555 152.5 ? 
28 NE2 ? B HIS 15  ? B HIS 47  ? 1_555 ZN ? P  ZN . ? B ZN 606 ? 1_555 O3X ? U  RP5 .   ? B RP5 611 ? 1_555 97.9  ? 
29 OD2 ? B ASP 78  ? B ASP 110 ? 1_555 ZN ? P  ZN . ? B ZN 606 ? 1_555 O3X ? U  RP5 .   ? B RP5 611 ? 1_555 92.9  ? 
30 NE2 ? B HIS 263 ? B HIS 295 ? 1_555 ZN ? P  ZN . ? B ZN 606 ? 1_555 O3X ? U  RP5 .   ? B RP5 611 ? 1_555 86.2  ? 
31 OD2 ? B ASP 78  ? B ASP 110 ? 1_555 ZN ? Q  ZN . ? B ZN 607 ? 1_555 OD1 ? B  ASN 119 ? B ASN 151 ? 1_555 105.3 ? 
32 OD2 ? B ASP 78  ? B ASP 110 ? 1_555 ZN ? Q  ZN . ? B ZN 607 ? 1_555 NE2 ? B  HIS 220 ? B HIS 252 ? 1_555 85.4  ? 
33 OD1 ? B ASN 119 ? B ASN 151 ? 1_555 ZN ? Q  ZN . ? B ZN 607 ? 1_555 NE2 ? B  HIS 220 ? B HIS 252 ? 1_555 83.3  ? 
34 OD2 ? B ASP 78  ? B ASP 110 ? 1_555 ZN ? Q  ZN . ? B ZN 607 ? 1_555 ND1 ? B  HIS 261 ? B HIS 293 ? 1_555 153.1 ? 
35 OD1 ? B ASN 119 ? B ASN 151 ? 1_555 ZN ? Q  ZN . ? B ZN 607 ? 1_555 ND1 ? B  HIS 261 ? B HIS 293 ? 1_555 101.0 ? 
36 NE2 ? B HIS 220 ? B HIS 252 ? 1_555 ZN ? Q  ZN . ? B ZN 607 ? 1_555 ND1 ? B  HIS 261 ? B HIS 293 ? 1_555 103.2 ? 
37 OD2 ? C ASP 13  ? C ASP 45  ? 1_555 ZN ? AA ZN . ? C ZN 606 ? 1_555 NE2 ? C  HIS 15  ? C HIS 47  ? 1_555 119.3 ? 
38 OD2 ? C ASP 13  ? C ASP 45  ? 1_555 ZN ? AA ZN . ? C ZN 606 ? 1_555 OD2 ? C  ASP 78  ? C ASP 110 ? 1_555 79.3  ? 
39 NE2 ? C HIS 15  ? C HIS 47  ? 1_555 ZN ? AA ZN . ? C ZN 606 ? 1_555 OD2 ? C  ASP 78  ? C ASP 110 ? 1_555 98.3  ? 
40 OD2 ? C ASP 13  ? C ASP 45  ? 1_555 ZN ? AA ZN . ? C ZN 606 ? 1_555 NE2 ? C  HIS 263 ? C HIS 295 ? 1_555 99.5  ? 
41 NE2 ? C HIS 15  ? C HIS 47  ? 1_555 ZN ? AA ZN . ? C ZN 606 ? 1_555 NE2 ? C  HIS 263 ? C HIS 295 ? 1_555 87.0  ? 
42 OD2 ? C ASP 78  ? C ASP 110 ? 1_555 ZN ? AA ZN . ? C ZN 606 ? 1_555 NE2 ? C  HIS 263 ? C HIS 295 ? 1_555 174.4 ? 
43 OD2 ? C ASP 78  ? C ASP 110 ? 1_555 ZN ? Z  ZN . ? C ZN 605 ? 1_555 OD1 ? C  ASN 119 ? C ASN 151 ? 1_555 99.1  ? 
44 OD2 ? C ASP 78  ? C ASP 110 ? 1_555 ZN ? Z  ZN . ? C ZN 605 ? 1_555 NE2 ? C  HIS 220 ? C HIS 252 ? 1_555 75.7  ? 
45 OD1 ? C ASN 119 ? C ASN 151 ? 1_555 ZN ? Z  ZN . ? C ZN 605 ? 1_555 NE2 ? C  HIS 220 ? C HIS 252 ? 1_555 79.8  ? 
46 OD2 ? C ASP 78  ? C ASP 110 ? 1_555 ZN ? Z  ZN . ? C ZN 605 ? 1_555 ND1 ? C  HIS 261 ? C HIS 293 ? 1_555 139.9 ? 
47 OD1 ? C ASN 119 ? C ASN 151 ? 1_555 ZN ? Z  ZN . ? C ZN 605 ? 1_555 ND1 ? C  HIS 261 ? C HIS 293 ? 1_555 119.1 ? 
48 NE2 ? C HIS 220 ? C HIS 252 ? 1_555 ZN ? Z  ZN . ? C ZN 605 ? 1_555 ND1 ? C  HIS 261 ? C HIS 293 ? 1_555 98.2  ? 
49 OD2 ? C ASP 78  ? C ASP 110 ? 1_555 ZN ? Z  ZN . ? C ZN 605 ? 1_555 O2P ? BA C5P .   ? C C5P 607 ? 1_555 87.1  ? 
50 OD1 ? C ASN 119 ? C ASN 151 ? 1_555 ZN ? Z  ZN . ? C ZN 605 ? 1_555 O2P ? BA C5P .   ? C C5P 607 ? 1_555 152.1 ? 
51 NE2 ? C HIS 220 ? C HIS 252 ? 1_555 ZN ? Z  ZN . ? C ZN 605 ? 1_555 O2P ? BA C5P .   ? C C5P 607 ? 1_555 128.0 ? 
52 ND1 ? C HIS 261 ? C HIS 293 ? 1_555 ZN ? Z  ZN . ? C ZN 605 ? 1_555 O2P ? BA C5P .   ? C C5P 607 ? 1_555 65.3  ? 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2016-01-20 
2 'Structure model' 1 1 2016-02-03 
3 'Structure model' 1 2 2016-03-30 
# 
_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         ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references' 
2 3 'Structure model' 'Database references' 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? 5.8.0073 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? 10.5.8   2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? 0.3.11   3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? 2.5.6    4 
? 'model building' ? ? ? ? ? ? ? ? ? ? ? Coot    ? ? ? 0.8      5 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 SG  B CYS 430 ? ? SG  B CYS 443 ? ? 0.50 
2  1 ND2 A ASN 356 ? ? C1  A NAG 604 ? ? 1.61 
3  1 ZN  B ZN  607 ? ? O2X B RP5 611 ? ? 1.69 
4  1 ZN  C ZN  606 ? ? O3P C C5P 607 ? ? 1.70 
5  1 N   C LEU 80  ? ? O   C HOH 701 ? ? 1.78 
6  1 ND2 C ASN 356 ? ? O5  C NAG 604 ? ? 1.88 
7  1 OG1 C THR 294 ? B O   C HOH 702 ? ? 1.89 
8  1 ND2 B ASN 263 ? ? O5  B NAG 604 ? ? 1.90 
9  1 CG2 C THR 294 ? A O   C HOH 702 ? ? 1.97 
10 1 O   C GLY 191 ? ? O   C HOH 703 ? ? 2.12 
11 1 O4  B NAG 602 ? ? O5  B NAG 603 ? ? 2.14 
12 1 OD2 B ASP 49  ? ? OG  B SER 64  ? ? 2.15 
13 1 SG  B CYS 430 ? ? CB  B CYS 443 ? ? 2.17 
14 1 ND2 B ASN 131 ? ? O5  B NAG 602 ? ? 2.19 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CB A HIS 53  ? ? CA A HIS 53  ? ? C  A HIS 53  ? ? 122.46 110.40 12.06  2.00 N 
2 1 CB A GLN 446 ? ? CA A GLN 446 ? ? C  A GLN 446 ? ? 122.89 110.40 12.49  2.00 N 
3 1 C  B PRO 34  ? ? N  B PRO 35  ? ? CD B PRO 35  ? ? 112.60 128.40 -15.80 2.10 Y 
4 1 CA B CYS 443 ? ? CB B CYS 443 ? ? SG B CYS 443 ? ? 124.22 114.20 10.02  1.10 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASP A 45  ? ? 39.86   67.81   
2  1 HIS A 53  ? ? 178.04  151.46  
3  1 ASN A 72  ? ? -162.48 75.05   
4  1 ASP A 110 ? ? 52.08   74.91   
5  1 ASP A 153 ? ? -87.38  49.66   
6  1 GLN A 157 ? ? -47.12  150.21  
7  1 ASP A 158 ? ? 73.21   -8.71   
8  1 GLN A 159 ? ? -98.84  47.96   
9  1 ASN A 200 ? ? -160.99 92.84   
10 1 PRO A 216 ? ? -54.16  0.17    
11 1 ASN A 222 ? ? 58.99   14.78   
12 1 ALA A 227 ? ? 48.23   25.21   
13 1 HIS A 252 ? ? -92.75  -63.93  
14 1 HIS A 293 ? ? 74.20   -53.08  
15 1 VAL A 310 ? ? -143.79 -7.31   
16 1 ASP A 382 ? ? -159.66 -158.06 
17 1 SER A 417 ? ? -93.86  32.83   
18 1 LEU A 447 ? ? -163.59 79.76   
19 1 ASP B 45  ? ? 51.88   74.54   
20 1 HIS B 53  ? ? -171.77 147.35  
21 1 ASN B 72  ? ? -164.40 73.20   
22 1 LEU B 80  ? ? 65.58   -6.50   
23 1 THR B 108 ? ? -100.64 57.92   
24 1 ASP B 110 ? ? 51.60   77.07   
25 1 TYR B 154 ? ? 177.95  154.07  
26 1 GLN B 157 ? ? -46.23  152.73  
27 1 ASP B 158 ? ? 73.19   -14.33  
28 1 GLN B 159 ? ? -90.77  30.29   
29 1 ASN B 200 ? ? -161.84 67.90   
30 1 ASN B 222 ? ? 55.37   13.82   
31 1 ALA B 227 ? ? 37.90   34.07   
32 1 ASN B 228 ? ? 32.95   63.35   
33 1 HIS B 252 ? ? -92.74  -76.80  
34 1 TYR B 282 ? ? -99.54  30.18   
35 1 HIS B 293 ? ? 74.26   -50.80  
36 1 ASN B 356 ? ? -68.59  89.29   
37 1 ASP B 382 ? ? -152.12 -156.94 
38 1 SER B 417 ? ? -119.85 58.11   
39 1 CYS B 443 ? ? -77.24  39.68   
40 1 LYS B 445 ? ? -51.74  -5.09   
41 1 ASN C 72  ? ? -156.44 76.29   
42 1 LEU C 80  ? ? 79.52   -15.87  
43 1 ASP C 110 ? ? 44.00   74.36   
44 1 ASP C 153 ? ? -79.52  32.94   
45 1 GLN C 159 ? ? -100.39 52.16   
46 1 ASN C 200 ? ? -160.53 62.06   
47 1 PRO C 201 ? ? -69.18  7.76    
48 1 PRO C 216 ? ? -62.78  2.55    
49 1 ASN C 222 ? ? 58.49   18.58   
50 1 LYS C 244 ? ? 38.97   58.36   
51 1 HIS C 293 ? ? 63.39   -58.79  
52 1 HIS C 293 ? ? 63.39   -58.58  
53 1 ARG C 343 ? ? -90.88  -61.68  
54 1 ASP C 379 ? ? 49.88   71.04   
55 1 ASP C 382 ? ? -153.00 -157.84 
56 1 ASP C 399 ? ? 32.01   53.46   
57 1 SER C 413 ? ? 58.99   17.35   
58 1 TYR C 414 ? ? -49.90  -73.08  
59 1 SER C 417 ? ? -88.05  36.01   
60 1 GLN C 446 ? ? -139.85 -60.38  
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? B HOH 759 ? 6.02 .    
2 1 O ? B HOH 760 ? 6.65 .    
3 1 O ? C HOH 751 ? .    6.31 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 N 1 A NAG 604 ? O1 ? G NAG 1 O1 
2 1 N 1 A NAG 604 ? O3 ? G NAG 1 O3 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3  N-ACETYL-D-GLUCOSAMINE            NAG 
4  'ZINC ION'                        ZN  
5  "CYTIDINE-5'-MONOPHOSPHATE"       C5P 
6  GLYCEROL                          GOL 
7  'MALONATE ION'                    MLI 
8  5-O-phosphono-beta-D-ribofuranose RP5 
9  'THIOCYANATE ION'                 SCN 
10 water                             HOH 
# 
